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+The protein's natural variant, known as in strain: 1, features a modification of the amino acid from A to V at position 223.
+The protein's natural variant, known as in strain: 1, features a modification of the amino acid from L to F at position 432.
+The protein's natural variant, known as in plasmid pMYSH6000 and plasmid pCP301, features a modification of the amino acid from T to I at position 11.
+The protein's natural variant, known as in plasmid pCP301, features a modification of the amino acid from L to R at position 84.
+The protein's natural variant, known as in plasmid pMYSH6000 and plasmid pCP301, features a modification of the amino acid from A to T at position 353.
+The protein's natural variant, known as in PFCRD; results in a complete loss of enzyme activity, features a modification of the amino acid from EVVYP to D at position 169.
+The protein's natural variant, known as in PFCRD; results in a complete loss of enzyme activity;, features a modification of the amino acid from D to G at position 365.
+The protein's natural variant, known as in CSPSD; increased ether lipid biosynthetic process in patient cells; increased FAR1 protein levels in patient cells due to impaired down-regulation by plasmalogen;, features a modification of the amino acid from R to C at position 480.
+The protein's natural variant, known as in CSPSD; increased ether lipid biosynthetic process in patient cells; increased FAR1 protein levels in patient cells due to impaired down-regulation by plasmalogen;, features a modification of the amino acid from R to H at position 480.
+The protein's natural variant, known as in CSPSD;, features a modification of the amino acid from R to L at position 480.
+The natural variant of this protein is characterized by an amino acid alteration from S to A at position 77.
+The natural variant of this protein is characterized by an amino acid alteration from S to F at position 77.
+The natural variant of this protein is characterized by an amino acid alteration from N to S at position 208.
+The natural variant of this protein is characterized by an amino acid alteration from F to L at position 209.
+The natural variant of this protein is characterized by an amino acid alteration from T to I at position 371.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 375.
+The natural variant of this protein is characterized by an amino acid alteration from L to H at position 442.
+The natural variant of this protein is characterized by an amino acid alteration from T to M at position 489.
+The natural variant of this protein is characterized by an amino acid alteration from I to M at position 495.
+The protein's natural variant, known as in PBD-CG8; impaired protein import into peroxisome; decreased interaction with PEX6; does not affect localization to peroxisomal membrane, features a modification of the amino acid from L to P at position 44.
+The protein's natural variant, known as in PBD7B; infantile Refsum disease;, features a modification of the amino acid from L to P at position 45.
+The protein's natural variant, known as in PBD7A;, features a modification of the amino acid from G to R at position 89.
+The protein's natural variant, known as in PBD7B and PBD-CG8; neonatal adrenoleukodystrophy; impaired protein import into peroxisome; affects the interaction with PEX6;, features a modification of the amino acid from R to W at position 98.
+The protein's natural variant, known as in PBD7A, features a modification of the amino acid from L to Q at position 116.
+The protein's natural variant, known as in PBD-CG8; impaired protein import into peroxisome; decreased interaction with PEX6; does not affect localization to peroxisomal membrane, features a modification of the amino acid from P to L at position 117.
+The protein's natural variant, known as in strain: Isolate ligus8, features a modification of the amino acid from F to L at position 108.
+The protein's natural variant, known as in strain: Isolate ligus8, features a modification of the amino acid from S to G at position 270.
+The protein's natural variant, known as in strain: Isolate ligus2, features a modification of the amino acid from M to I at position 271.
+The protein's natural variant, known as in strain: Isolate ligus7, features a modification of the amino acid from R to P at position 437.
+The protein's natural variant, known as in NEDMAB; unknown pathological significance; no effect on channel function, features a modification of the amino acid from E to Q at position 30.
+The protein's natural variant, known as in NEDMAB; requires 2 nucleotide substitutions, features a modification of the amino acid from I to S at position 288.
+The protein's natural variant, known as in NEDMAB; loss of function of homomeric channels, features a modification of the amino acid from I to M at position 359.
+The protein's natural variant, known as in NEDMAB, features a modification of the amino acid from Y to C at position 361.
+The protein's natural variant, known as in NEDMAB; loss of function of homomeric channels, features a modification of the amino acid from G to S at position 362.
+The protein's natural variant, known as in DYT34; unknown pathological significance, features a modification of the amino acid from G to E at position 371.
+The protein's natural variant, known as in NEDMAB; loss of function of homomeric channels, features a modification of the amino acid from L to V at position 388.
+The protein's natural variant, known as in NEDMAB; loss of function of homomeric channels, features a modification of the amino acid from L to P at position 432.
+The protein's natural variant, known as in GPIBD16; decreased function in GPI-anchor biosynthesis as indicated by reduced surface expression of various GPI-anchored proteins;, features a modification of the amino acid from L to W at position 189.
+The protein's natural variant, known as in GPIBD16; decreased function in GPI-anchor biosynthesis as indicated by reduced surface expression of various GPI-anchored proteins;, features a modification of the amino acid from L to P at position 212.
+The protein's natural variant, known as found in two patients with developmental delay/intellectual disability, neuromuscular and psychiatric symptoms; unknown pathological significance;, features a modification of the amino acid from T to M at position 137.
+The protein's natural variant, known as found in a patient with developmental delay/intellectual disability, neuromuscular and psychiatric symptoms; unknown pathological significance, features a modification of the amino acid from P to S at position 139.
+The protein's natural variant, known as found in a patient with developmental delay/intellectual disability, neuromuscular and psychiatric symptoms; unknown pathological significance;, features a modification of the amino acid from D to N at position 264.
+The protein's natural variant, known as in strain: cv. Ci-0, features a modification of the amino acid from S to T at position 22.
+The protein's natural variant, known as in strain: cv. Es-0, features a modification of the amino acid from E to A at position 42.
+The protein's natural variant, known as in strain: cv. Ci-0, features a modification of the amino acid from Q to R at position 69.
+The protein's natural variant, known as in strain: cv. Ci-0, features a modification of the amino acid from E to K at position 120.
+The protein's natural variant, known as in strain: cv. Ci-0, features a modification of the amino acid from I to V at position 125.
+The protein's natural variant, known as in strain: cv. Ci-0, cv. Ita-0 and cv. Pog-0, features a modification of the amino acid from T to S at position 169.
+The protein's natural variant, known as in strain: cv. Ci-0, features a modification of the amino acid from F to Y at position 173.
+The protein's natural variant, known as in strain: cv. Yo-0, features a modification of the amino acid from S to T at position 174.
+The protein's natural variant, known as in strain: cv. Ita-0 and cv. Pog-0, features a modification of the amino acid from I to V at position 180.
+The protein's natural variant, known as in strain: cv. Mt-0, features a modification of the amino acid from C to W at position 217.
+The protein's natural variant, known as in strain: cv. Ita-0 and cv. Pog-0, features a modification of the amino acid from S to T at position 220.
+The protein's natural variant, known as in strain: cv. Chi-0, features a modification of the amino acid from A to T at position 239.
+The protein's natural variant, known as in strain: cv. Ita-0, features a modification of the amino acid from F to I at position 243.
+The protein's natural variant, known as in strain: cv. Pog-0, features a modification of the amino acid from F to L at position 243.
+The protein's natural variant, known as in strain: cv. Yo-0, features a modification of the amino acid from G to V at position 257.
+The protein's natural variant, known as in strain: cv. Ci-0, features a modification of the amino acid from K to N at position 274.
+The protein's natural variant, known as in strain: cv. Bla-10, features a modification of the amino acid from L to S at position 299.
+The protein's natural variant, known as in strain: cv. Bs-1, features a modification of the amino acid from L to V at position 299.
+The protein's natural variant, known as found in a child with sporadic epilepsy; unknown pathological significance;, features a modification of the amino acid from R to H at position 131.
+The protein's natural variant, known as in strain: cv. Wassilewskija, features a modification of the amino acid from Q to L at position 174.
+The protein's natural variant, known as in HSD10MD; decreased dehydrogenase activity; decreased tRNA methylation; decreased mitochondrial tRNA 5'-end processing, features a modification of the amino acid from V to L at position 12.
+The protein's natural variant, known as in HSD10MD; unknown pathological significance;, features a modification of the amino acid from V to A at position 65.
+The protein's natural variant, known as in HSD10MD; decreased 3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity; no effect on NAD(+) binding; complete loss of phospholipase C-like activity toward cardiolipin;, features a modification of the amino acid from D to G at position 86.
+The protein's natural variant, known as in HSD10MD;, features a modification of the amino acid from L to V at position 122.
+The protein's natural variant, known as in HSD10MD; decreased stability; decreased 3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity; decreased mitochondrial tRNA 5'-end processing; decreased tRNA methylation; does not affect homotetramerization; complete loss of phospholipase C-like activity toward cardiolipin;, features a modification of the amino acid from R to C at position 130.
+The protein's natural variant, known as in HSD10MD; loss of 3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity; does not bind NAD(+); complete loss of phospholipase C-like activity toward cardiolipin, features a modification of the amino acid from Q to H at position 165.
+The protein's natural variant, known as in HSD10MD; decreased dehydrogenase activity; strongly decreased tRNA methylation; strongly decreased mitochondrial tRNA 5'-end processing, features a modification of the amino acid from V to M at position 176.
+The protein's natural variant, known as in HSD10MD; decreased 3-hydroxyacyl-CoA dehydrogenase activity; decreased mitochondrial tRNA 5'-end processing; decreased tRNA methylation; does not affect homotetramerization, features a modification of the amino acid from P to S at position 210.
+The protein's natural variant, known as in HSD10MD; 4-fold decrease of 3-hydroxyacyl-CoA dehydrogenase activity; decreased interaction with TRMT10C; decreased function in mitochondrial tRNA methylation; decreased function in mitochondrial tRNA processing;, features a modification of the amino acid from K to E at position 212.
+The protein's natural variant, known as in HSD10MD; strongly decreased 3-hydroxyacyl-CoA dehydrogenase activity; abolished mitochondrial tRNA 5'-end processing; abolished tRNA methylation; impaired homotetramerization;, features a modification of the amino acid from R to Q at position 226.
+The protein's natural variant, known as in HSD10MD; strongly decreased 3-hydroxyacyl-CoA dehydrogenase activity; abolished mitochondrial tRNA 5'-end processing; abolished tRNA methylation; impaired homotetramerization;, features a modification of the amino acid from N to S at position 247.
+The protein's natural variant, known as in HSD10MD; decreased 3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity;, features a modification of the amino acid from E to Q at position 249.
+The protein's natural variant, known as may be a risk factor for Parkinson disease; reduced protease activity;, features a modification of the amino acid from A to S at position 141.
+The protein's natural variant, known as in MGCA8; loss of protein expression;, features a modification of the amino acid from LP to PS at position 244.
+The protein's natural variant, known as may be a risk factor for Parkinson disease; reduced protease activity;, features a modification of the amino acid from G to S at position 399.
+The protein's natural variant, known as in MGCA8; may lead to skipping of exon 7 and the resultant protein may be truncated; loss of protein expression in patient cells homozygous for the mutation;, features a modification of the amino acid from R to Q at position 404.
+The protein's natural variant, known as in PARK13;, features a modification of the amino acid from R to W at position 404.
+The protein's natural variant, known as in ACCPN; loss of potassium-chloride cotransport activity; abnormal perinuclear localization; stabilization of homodimeric state;, features a modification of the amino acid from R to C at position 207.
+The protein's natural variant, known as in CMT2II, features a modification of the amino acid from R to H at position 207.
+The protein's natural variant, known as in CMT2II, features a modification of the amino acid from E to K at position 289.
+The protein's natural variant, known as in CMT2II, features a modification of the amino acid from Y to C at position 679.
+The protein's natural variant, known as in CMT2II; unknown pathological significance, features a modification of the amino acid from Y to S at position 679.
+The protein's natural variant, known as in CMT2II; abolished WNK kinase-dependent inhibitory phosphorylation; constitutively enhanced potassium-chloride cotransport activity; reduced acute swelling response to hypotonic stress, features a modification of the amino acid from T to A at position 991.
+The protein's natural variant, known as associated with coumarin resistance; increased warfarin maintenance dose in patients on warfarin anti-coagulant therapy due to decreased vitamin K catabolism; decreased phylloquinone omega-hydroxylase activity; decreased production of 20-hydroxyeicosatetraenoic acid (20-HETE);, features a modification of the amino acid from V to M at position 433.
+The natural variant of this protein is characterized by an amino acid alteration from P to R at position 367.
+The protein's natural variant, known as in MLDSAPB; reduces the intracellular activity of the protein significantly;, features a modification of the amino acid from N to H at position 215.
+The protein's natural variant, known as in MLDSAPB;, features a modification of the amino acid from N to K at position 215.
+The protein's natural variant, known as in MLDSAPB; juvenile; affects glycosylation at N-215;, features a modification of the amino acid from T to I at position 217.
+The protein's natural variant, known as in MLDSAPB; severe;, features a modification of the amino acid from C to S at position 241.
+The protein's natural variant, known as in GDSAPC;, features a modification of the amino acid from L to P at position 349.
+The protein's natural variant, known as in GDSAPC, features a modification of the amino acid from C to F at position 388.
+The protein's natural variant, known as in PARK24; associated with disease susceptibility; affects the intracellular trafficking, resulting in endoplasmic reticulum retention; affects the intracellular trafficking, resulting in endoplasmic reticulum retention; cells carrying this variant show accumulation of autophagic vacuoles, impaired autophagic flux and alpha-synuclein/SNCA aggregation, features a modification of the amino acid from C to Y at position 412.
+The protein's natural variant, known as in PARK24; associated with disease susceptibility; affects the intracellular trafficking, resulting in endoplasmic reticulum retention; cells carrying this variant show accumulation of autophagic vacuoles, impaired autophagic flux and alpha-synuclein/SNCA aggregation, features a modification of the amino acid from Q to P at position 453.
+The protein's natural variant, known as in strain: A450 and A461, features a modification of the amino acid from S to G at position 26.
+The protein's natural variant, known as in strain: A450, features a modification of the amino acid from T to N at position 35.
+The protein's natural variant, known as in strain: A400 and A450, features a modification of the amino acid from D to S at position 47.
+The protein's natural variant, known as in strain: A400, features a modification of the amino acid from F to D at position 48.
+The natural variant of this protein is characterized by an amino acid alteration from N to Y at position 104.
+The natural variant of this protein is characterized by an amino acid alteration from P to L at position 47.
+The protein's natural variant, known as in an ovarian mucinous carcinoma sample; somatic mutation;, features a modification of the amino acid from G to S at position 611.
+The protein's natural variant, known as in an ovarian serous carcinoma sample; somatic mutation, features a modification of the amino acid from P to L at position 748.
+The protein's natural variant, known as in a breast pleomorphic lobular carcinoma sample; somatic mutation, features a modification of the amino acid from I to M at position 765.
+The protein's natural variant, known as in CMS18; interfers with calcium-induced fusion; inhibits exocytosis of catecholamine-containing vesicles;, features a modification of the amino acid from I to N at position 67.
+The protein's natural variant, known as in an ovarian serous carcinoma sample; somatic mutation, features a modification of the amino acid from I to T at position 320.
+The protein's natural variant, known as in a lung squamous cell carcinoma sample; somatic mutation, features a modification of the amino acid from T to N at position 403.
+The natural variant of this protein is characterized by an amino acid alteration from S to N at position 762.
+The protein's natural variant, known as loss of IFNB induction, features a modification of the amino acid from F to S at position 24.
+The protein's natural variant, known as in FTDALS4; loss of kinase activity, features a modification of the amino acid from R to H at position 47.
+The protein's natural variant, known as in IIAE8; decreased expression levels;, features a modification of the amino acid from D to A at position 50.
+The protein's natural variant, known as in FTDALS4;, features a modification of the amino acid from Y to C at position 105.
+The protein's natural variant, known as no effect on IFNB induction, features a modification of the amino acid from V to L at position 152.
+The protein's natural variant, known as in IIAE8; loss of kinase activity; loss of autophosphorylation at S-172; loss of IFNB induction;, features a modification of the amino acid from G to A at position 159.
+The protein's natural variant, known as in IIAE8; unknown pathological significance;, features a modification of the amino acid from I to V at position 207.
+The protein's natural variant, known as in a breast pleomorphic lobular carcinoma sample; somatic mutation, features a modification of the amino acid from D to H at position 296.
+The protein's natural variant, known as in FTDALS4;, features a modification of the amino acid from I to T at position 305.
+The protein's natural variant, known as in FTDALS4; unknown pathological significance;, features a modification of the amino acid from L to I at position 306.
+The protein's natural variant, known as in FTDALS4; reduced kinase activity, features a modification of the amino acid from R to Q at position 308.
+The protein's natural variant, known as in FTDALS4; reduced kinase activity;, features a modification of the amino acid from R to Q at position 357.
+The protein's natural variant, known as no effect on IFNB induction, features a modification of the amino acid from R to Q at position 384.
+The protein's natural variant, known as no effect on IFNB induction, features a modification of the amino acid from N to S at position 388.
+The protein's natural variant, known as no effect on IFNB induction, features a modification of the amino acid from I to T at position 397.
+The protein's natural variant, known as in FTDALS4;, features a modification of the amino acid from K to E at position 401.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from G to R at position 410.
+The protein's natural variant, known as no effect on IFNB induction, features a modification of the amino acid from L to I at position 508.
+The protein's natural variant, known as no effect on IFNB induction, features a modification of the amino acid from I to M at position 522.
+The protein's natural variant, known as no effect on IFNB induction, features a modification of the amino acid from A to T at position 533.
+The protein's natural variant, known as in FTDALS4; loss of kinase activity, features a modification of the amino acid from M to R at position 559.
+The protein's natural variant, known as in FTDALS4;, features a modification of the amino acid from A to V at position 571.
+The protein's natural variant, known as in FTDALS4;, features a modification of the amino acid from M to V at position 598.
+The protein's natural variant, known as no effect on IFNB induction, features a modification of the amino acid from E to Q at position 653.
+The protein's natural variant, known as no effect on IFNB induction, features a modification of the amino acid from P to S at position 659.
+The protein's natural variant, known as in FTDALS4; loss of kinase activity; impairs binding to OPTN;, features a modification of the amino acid from E to K at position 696.
+The protein's natural variant, known as in type B, features a modification of the amino acid from S to G at position 5.
+The protein's natural variant, known as in type B, features a modification of the amino acid from L to K at position 10.
+The protein's natural variant, known as in type B, features a modification of the amino acid from I to K at position 18.
+The protein's natural variant, known as in HMN6;, features a modification of the amino acid from L to P at position 17.
+The protein's natural variant, known as in HMN6;, features a modification of the amino acid from L to P at position 192.
+The protein's natural variant, known as in HMN6; severe reduction of ATPase activity and loss of helicase activity on RNA duplices;, features a modification of the amino acid from Q to R at position 196.
+The protein's natural variant, known as in CMT2S;, features a modification of the amino acid from F to V at position 202.
+The protein's natural variant, known as in HMN6;, features a modification of the amino acid from H to R at position 213.
+The protein's natural variant, known as in HMN6;, features a modification of the amino acid from P to L at position 216.
+The protein's natural variant, known as in HMN6; severe reduction of ATPase activity and loss of helicase activity on RNA duplices;, features a modification of the amino acid from T to A at position 221.
+The protein's natural variant, known as in HMN6; severe reduction of ATPase activity and loss of helicase activity on RNA duplices;, features a modification of the amino acid from C to R at position 241.
+The protein's natural variant, known as in HMN6;, features a modification of the amino acid from L to P at position 251.
+The protein's natural variant, known as in HMN6;, features a modification of the amino acid from E to K at position 334.
+The protein's natural variant, known as in HMN6;, features a modification of the amino acid from L to P at position 361.
+The protein's natural variant, known as in HMN6;, features a modification of the amino acid from L to P at position 364.
+The protein's natural variant, known as in HMN6;, features a modification of the amino acid from F to L at position 369.
+The protein's natural variant, known as in CMT2S;, features a modification of the amino acid from V to G at position 373.
+The protein's natural variant, known as in HMN6; severe reduction of ATPase activity and loss of helicase activity on RNA duplices;, features a modification of the amino acid from E to K at position 382.
+The protein's natural variant, known as in HMN6;, features a modification of the amino acid from W to R at position 386.
+The protein's natural variant, known as in HMN6;, features a modification of the amino acid from L to P at position 426.
+The protein's natural variant, known as in HMN6; severe reduction of ATPase activity and loss of helicase activity on RNA duplices;, features a modification of the amino acid from H to P at position 445.
+The protein's natural variant, known as in HMN6;, features a modification of the amino acid from L to P at position 472.
+The protein's natural variant, known as in HMN6; does not affect activity; reduces protein steady-state levels;, features a modification of the amino acid from T to I at position 493.
+The protein's natural variant, known as in HMN6;, features a modification of the amino acid from E to K at position 514.
+The protein's natural variant, known as in CMT2S;, features a modification of the amino acid from A to T at position 528.
+The protein's natural variant, known as in HMN6; does not affect ATPase activity; loss of helicase activity on RNA duplices;, features a modification of the amino acid from D to N at position 565.
+The protein's natural variant, known as in HMN6;, features a modification of the amino acid from L to P at position 577.
+The protein's natural variant, known as in HMN6;, features a modification of the amino acid from V to I at position 580.
+The protein's natural variant, known as in HMN6;, features a modification of the amino acid from R to S at position 581.
+The protein's natural variant, known as in HMN6; severe reduction of ATPase activity and loss of helicase activity on RNA duplices;, features a modification of the amino acid from N to I at position 583.
+The protein's natural variant, known as in HMN6, features a modification of the amino acid from G to C at position 586.
+The protein's natural variant, known as in HMN6;, features a modification of the amino acid from R to C at position 603.
+The protein's natural variant, known as in HMN6; severe reduction of ATPase activity and loss of helicase activity on RNA duplices;, features a modification of the amino acid from R to H at position 603.
+The protein's natural variant, known as in HMN6;, features a modification of the amino acid from R to C at position 637.
+The protein's natural variant, known as in HMN6; unknown pathological significance;, features a modification of the amino acid from D to E at position 974.
+The protein's natural variant, known as in strain: Yak_5, features a modification of the amino acid from R to W at position 11.
+The protein's natural variant, known as in strain: Yak_23 and Yak_8, features a modification of the amino acid from D to N at position 39.
+The protein's natural variant, known as in strain: Yak_2, features a modification of the amino acid from G to E at position 49.
+The protein's natural variant, known as in strain: Yak_2, features a modification of the amino acid from H to Y at position 179.
+The protein's natural variant, known as in strain: Yak_5, features a modification of the amino acid from L to F at position 195.
+The protein's natural variant, known as in strain: Yak_23, features a modification of the amino acid from T to S at position 227.
+The protein's natural variant, known as in strain: Yak_23, features a modification of the amino acid from L to H at position 260.
+The protein's natural variant, known as in strain: Yak_2, features a modification of the amino acid from A to V at position 331.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from R to G at position 122.
+The protein's natural variant, known as in RNA edited version; does not alter GABA receptor activity; retains inhibition by picrotoxin; shows resistance to picrotoxinin; when associated with S-301, features a modification of the amino acid from I to V at position 283.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from N to D at position 294.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from M to V at position 360.
+The protein's natural variant, known as in clone PC4H-II, features a modification of the amino acid from V to I at position 40.
+The protein's natural variant, known as in allele NAT2*21; slow acetylator, features a modification of the amino acid from V to I at position 121.
+The protein's natural variant, known as in allele NAT2*21; slow acetylator, features a modification of the amino acid from V to I at position 266.
+The protein's natural variant, known as in CMS7A;, features a modification of the amino acid from D to A at position 307.
+The protein's natural variant, known as in CMS7A;, features a modification of the amino acid from P to L at position 308.
+The protein's natural variant, known as in CMS7A, features a modification of the amino acid from L to P at position 365.
+The protein's natural variant, known as in a Shy-Drager syndrome patient; unknown pathological significance;, features a modification of the amino acid from A to V at position 280.
+The protein's natural variant, known as in strain: LT2 / SGSC1412 and S4194; resistance to polymyxin B and neutrophil proteins, features a modification of the amino acid from H to R at position 81.
+The protein's natural variant, known as in JBTS1;, features a modification of the amino acid from G to R at position 286.
+The protein's natural variant, known as in JBTS1;, features a modification of the amino acid from V to M at position 303.
+The protein's natural variant, known as in JBTS1, features a modification of the amino acid from R to S at position 345.
+The protein's natural variant, known as in JBTS1; slightly reduced phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity;, features a modification of the amino acid from R to C at position 378.
+The protein's natural variant, known as in JBTS1, features a modification of the amino acid from T to N at position 426.
+The protein's natural variant, known as in JBTS1; severe reduction of phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity;, features a modification of the amino acid from R to Q at position 435.
+The protein's natural variant, known as in JBTS1; unknown pathological significance, features a modification of the amino acid from W to R at position 474.
+The protein's natural variant, known as in JBTS1; associated with W-515; severe reduction of phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity;, features a modification of the amino acid from R to W at position 512.
+The protein's natural variant, known as in JBTS1; associated with W-512; severe reduction of phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity;, features a modification of the amino acid from R to W at position 515.
+The protein's natural variant, known as in JBTS1; reduced levels of protein in patients' fibroblasts; significant number of cells from patients have shorter or no cilia;, features a modification of the amino acid from G to A at position 522.
+The protein's natural variant, known as in JBTS1, features a modification of the amino acid from Y to D at position 534.
+The protein's natural variant, known as in JBTS1; slightly reduced phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity;, features a modification of the amino acid from R to H at position 563.
+The protein's natural variant, known as in JBTS1; severe reduction of phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity, features a modification of the amino acid from K to E at position 580.
+The protein's natural variant, known as in JBTS1;, features a modification of the amino acid from R to C at position 585.
+The protein's natural variant, known as in JBTS1;, features a modification of the amino acid from R to Q at position 621.
+The protein's natural variant, known as in JBTS1, features a modification of the amino acid from C to R at position 641.
+The protein's natural variant, known as in MAHCC;, features a modification of the amino acid from Q to R at position 27.
+The protein's natural variant, known as in MAHCC;, features a modification of the amino acid from L to P at position 116.
+The protein's natural variant, known as in MAHCC, features a modification of the amino acid from H to R at position 122.
+The protein's natural variant, known as in MAHCC;, features a modification of the amino acid from Y to H at position 130.
+The protein's natural variant, known as in MAHCC;, features a modification of the amino acid from G to A at position 147.
+The protein's natural variant, known as in MAHCC; loss of cyanocobalamin binding;, features a modification of the amino acid from G to D at position 147.
+The protein's natural variant, known as in MAHCC;, features a modification of the amino acid from G to D at position 156.
+The protein's natural variant, known as in MAHCC;, features a modification of the amino acid from W to C at position 157.
+The protein's natural variant, known as in MAHCC; results in decreased stability and decreased methylcobalamin dealkylation activity;, features a modification of the amino acid from R to G at position 161.
+The protein's natural variant, known as in MAHCC; results in decreased stability and reduced stabilization induced by cobalamin binding; has reduced affinity for cyanocobalamin and reduced activity in dealkylation of methylcobalamin;, features a modification of the amino acid from R to Q at position 161.
+The protein's natural variant, known as in MAHCC;, features a modification of the amino acid from R to S at position 189.
+The protein's natural variant, known as in MAHCC;, features a modification of the amino acid from L to P at position 193.
+The protein's natural variant, known as in MAHCC;, features a modification of the amino acid from R to P at position 206.
+The protein's natural variant, known as in MAHCC;, features a modification of the amino acid from R to W at position 206.
+The protein's natural variant, known as in strain: SHR/OlaIpcv and Brown Norway/Crl, features a modification of the amino acid from S to G at position 226.
+The protein's natural variant, known as in strain: SHR/OlaIpcv and Brown Norway/Crl, features a modification of the amino acid from N to D at position 260.
+The protein's natural variant, known as in DIH4; decreased retinoic acid biosynthetic process, features a modification of the amino acid from Q to K at position 182.
+The protein's natural variant, known as in DIH4; decreased expression, features a modification of the amino acid from R to H at position 347.
+The protein's natural variant, known as in DIH4; unknown pathological significance, features a modification of the amino acid from A to T at position 383.
+The protein's natural variant, known as in DIH4; decreased retinoic acid biosynthetic process, features a modification of the amino acid from S to Y at position 461.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation, features a modification of the amino acid from G to E at position 52.
+The protein's natural variant, known as in a lung squamous cell carcinoma sample; somatic mutation, features a modification of the amino acid from E to Q at position 148.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation, features a modification of the amino acid from H to Q at position 244.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from D to H at position 166.
+The protein's natural variant, known as more effective in stimulating IP3 but not cAMP production;, features a modification of the amino acid from A to T at position 18.
+The protein's natural variant, known as in HH23; lack of receptor binding;, features a modification of the amino acid from Q to R at position 74.
+The protein's natural variant, known as may be implicated in female infertility;, features a modification of the amino acid from G to S at position 122.
+The natural variant of this protein is characterized by an amino acid alteration from F to S at position 4.
+The natural variant of this protein is characterized by an amino acid alteration from C to S at position 9.
+The natural variant of this protein is characterized by an amino acid alteration from A to S at position 17.
+The protein's natural variant, known as in GLC1A;, features a modification of the amino acid from C to R at position 25.
+The protein's natural variant, known as in GLC1A and GLC3A; the GLC3A patient also carries mutation H-368 in CYP1B1 suggesting digenic inheritance;, features a modification of the amino acid from Q to H at position 48.
+The protein's natural variant, known as in GLC1A;, features a modification of the amino acid from V to A at position 53.
+The natural variant of this protein is characterized by an amino acid alteration from N to D at position 57.
+The protein's natural variant, known as loss of higher molecular weight isoform;, features a modification of the amino acid from N to S at position 57.
+The natural variant of this protein is characterized by an amino acid alteration from N to S at position 73.
+The natural variant of this protein is characterized by an amino acid alteration from D to E at position 77.
+The protein's natural variant, known as in GLC1A;, features a modification of the amino acid from R to C at position 82.
+The natural variant of this protein is characterized by an amino acid alteration from L to P at position 95.
+The protein's natural variant, known as in GLC1A;, features a modification of the amino acid from R to W at position 126.
+The protein's natural variant, known as in GLC1A;, features a modification of the amino acid from R to Q at position 158.
+The natural variant of this protein is characterized by an amino acid alteration from S to F at position 203.
+The protein's natural variant, known as in GLC1A; unknown pathological significance;, features a modification of the amino acid from D to E at position 208.
+The protein's natural variant, known as in GLC1A; unknown pathological significance;, features a modification of the amino acid from G to V at position 244.
+The protein's natural variant, known as in GLC1A; forms homomultimeric complexes that migrate at molecular weights larger than their wild-type counterparts; these mutant complexes remain sequestered intracellularly;, features a modification of the amino acid from C to Y at position 245.
+The protein's natural variant, known as in GLC1A, features a modification of the amino acid from G to R at position 246.
+The protein's natural variant, known as in GLC1A, features a modification of the amino acid from V to A at position 251.
+The protein's natural variant, known as in GLC1A;, features a modification of the amino acid from G to R at position 252.
+The protein's natural variant, known as in GLC1A;, features a modification of the amino acid from E to K at position 261.
+The protein's natural variant, known as in GLC1A; unknown pathological significance, features a modification of the amino acid from R to G at position 272.
+The protein's natural variant, known as in GLC1A, features a modification of the amino acid from P to R at position 274.
+The protein's natural variant, known as in GLC1A;, features a modification of the amino acid from W to R at position 286.
+The protein's natural variant, known as in GLC1A; no effect on protein stability;, features a modification of the amino acid from T to K at position 293.
+The protein's natural variant, known as in GLC1A; unknown pathological significance;, features a modification of the amino acid from E to K at position 300.
+The protein's natural variant, known as in GLC1A; inhibits endoproteolytic processing; mainly accumulates as insoluble aggregates inside the endoplasmic reticulum, features a modification of the amino acid from E to K at position 323.
+The protein's natural variant, known as slightly decreased protein stability;, features a modification of the amino acid from V to M at position 329.
+The protein's natural variant, known as in GLC1A, features a modification of the amino acid from Q to E at position 337.
+The protein's natural variant, known as in GLC1A;, features a modification of the amino acid from Q to R at position 337.
+The protein's natural variant, known as in GLC1A;, features a modification of the amino acid from S to P at position 341.
+The protein's natural variant, known as in GLC1A, features a modification of the amino acid from R to K at position 342.
+The protein's natural variant, known as in GLC1A, features a modification of the amino acid from I to M at position 345.
+The protein's natural variant, known as in GLC1A; unknown pathological significance;, features a modification of the amino acid from E to K at position 352.
+The protein's natural variant, known as in GLC1A; unknown pathological significance; no significant effect on protein stability;, features a modification of the amino acid from T to I at position 353.
+The protein's natural variant, known as in GLC1A, features a modification of the amino acid from I to N at position 360.
+The protein's natural variant, known as in GLC1A;, features a modification of the amino acid from P to S at position 361.
+The protein's natural variant, known as in GLC1A, features a modification of the amino acid from A to T at position 363.
+The protein's natural variant, known as in GLC1A;, features a modification of the amino acid from G to V at position 364.
+The protein's natural variant, known as in GLC1A;, features a modification of the amino acid from G to R at position 367.
+The protein's natural variant, known as in GLC1A, features a modification of the amino acid from F to L at position 369.
+The protein's natural variant, known as in GLC1A; severe form; inhibits endoproteolytic processing; produced the highest inhibition of the endoproteolytic processing; mainly accumulates as insoluble aggregates inside the endoplasmic reticulum; inhibits neurite outgrowth;, features a modification of the amino acid from P to L at position 370.
+The protein's natural variant, known as in GLC1A, features a modification of the amino acid from T to K at position 377.
+The protein's natural variant, known as in GLC1A;, features a modification of the amino acid from T to M at position 377.
+The protein's natural variant, known as in GLC1A; incomplete penetrance; inhibits endoproteolytic processing; mainly accumulates as insoluble aggregates inside the endoplasmic reticulum, features a modification of the amino acid from D to A at position 380.
+The protein's natural variant, known as in GLC1A, features a modification of the amino acid from D to G at position 380.
+The protein's natural variant, known as in GLC1A;, features a modification of the amino acid from D to H at position 380.
+The protein's natural variant, known as in GLC1A, features a modification of the amino acid from D to N at position 380.
+The protein's natural variant, known as in GLC1A, features a modification of the amino acid from S to N at position 393.
+The protein's natural variant, known as in GLC1A;, features a modification of the amino acid from S to R at position 393.
+The protein's natural variant, known as in GLC1A;, features a modification of the amino acid from G to V at position 399.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 402.
+The protein's natural variant, known as no effect on protein stability;, features a modification of the amino acid from R to C at position 422.
+The protein's natural variant, known as in GLC1A;, features a modification of the amino acid from R to H at position 422.
+The protein's natural variant, known as in GLC1A; heterozygote specific phenotype;, features a modification of the amino acid from K to E at position 423.
+The protein's natural variant, known as decreases protein stability, features a modification of the amino acid from S to P at position 425.
+The protein's natural variant, known as in GLC1A, features a modification of the amino acid from V to F at position 426.
+The protein's natural variant, known as in GLC1A;, features a modification of the amino acid from A to T at position 427.
+The protein's natural variant, known as in GLC1A; severe form;, features a modification of the amino acid from C to R at position 433.
+The protein's natural variant, known as in GLC1A;, features a modification of the amino acid from G to S at position 434.
+The protein's natural variant, known as in GLC1A;, features a modification of the amino acid from Y to H at position 437.
+The protein's natural variant, known as in GLC1A, features a modification of the amino acid from T to I at position 438.
+The protein's natural variant, known as in GLC1A; no effect on protein stability;, features a modification of the amino acid from A to V at position 445.
+The protein's natural variant, known as in GLC1A, features a modification of the amino acid from T to P at position 448.
+The protein's natural variant, known as in GLC1A, features a modification of the amino acid from N to D at position 450.
+The protein's natural variant, known as in GLC1A, features a modification of the amino acid from I to M at position 465.
+The protein's natural variant, known as in GLC1A;, features a modification of the amino acid from R to C at position 470.
+The protein's natural variant, known as in GLC1A; unknown pathological significance;, features a modification of the amino acid from Y to C at position 471.
+The protein's natural variant, known as no effect on protein stability, features a modification of the amino acid from Y to C at position 473.
+The protein's natural variant, known as in GLC1A; induces stress fiber formation in only 5% of cells;, features a modification of the amino acid from I to N at position 477.
+The protein's natural variant, known as in GLC1A;, features a modification of the amino acid from I to S at position 477.
+The protein's natural variant, known as in GLC1A;, features a modification of the amino acid from N to K at position 480.
+The protein's natural variant, known as in GLC1A, features a modification of the amino acid from P to L at position 481.
+The protein's natural variant, known as in GLC1A, features a modification of the amino acid from P to T at position 481.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 495.
+The protein's natural variant, known as in GLC1A, features a modification of the amino acid from I to F at position 499.
+The protein's natural variant, known as in GLC1A, features a modification of the amino acid from I to S at position 499.
+The protein's natural variant, known as in GLC1A, features a modification of the amino acid from S to P at position 502.
+The protein's natural variant, known as in strain: MA7, features a modification of the amino acid from S to G at position 3.
+The protein's natural variant, known as in strain: LA116, MA18, MA45, MA48, MA50, MA7, MA8, MW25, MW29, MW3, MW32, MW37, MW44, MW46, MW56, MW6, MW7, MW9, NC21a, NC52a, NC62a, NC73a and NC79b, features a modification of the amino acid from Q to K at position 4.
+The protein's natural variant, known as in strain: LA116, MA13, MA18, MA43, MA45, MA48, MA50, MA7, MA74, MA8, MW25, MW27, MW29, MW3, MW32, MW37, MW44, MW46, MW56, MW6, MW7, MW9, NC21a, NC52a, NC62a, NC73a and NC79b, features a modification of the amino acid from V to I at position 25.
+The protein's natural variant, known as in strain: NC52a and NC73a, features a modification of the amino acid from V to L at position 30.
+The protein's natural variant, known as in strain: NC21a, NC52a, NC62a, NC73a and NC79b, features a modification of the amino acid from V to E at position 38.
+The protein's natural variant, known as in strain: LA116, MA45, MA50, MW37, MW6 and MW9, features a modification of the amino acid from D to I at position 45.
+The protein's natural variant, known as in strain: LA116, features a modification of the amino acid from H to P at position 47.
+The protein's natural variant, known as in strain: MA45, MA50, MW37, MW6 and MW9, features a modification of the amino acid from V to A at position 69.
+The protein's natural variant, known as in strain: LA116, features a modification of the amino acid from I to L at position 87.
+The protein's natural variant, known as in strain: LA116, features a modification of the amino acid from Q to E at position 88.
+The protein's natural variant, known as in strain: NC21a, NC52a, NC62a, NC73a and NC79b, features a modification of the amino acid from N to D at position 92.
+The protein's natural variant, known as in strain: LA116, features a modification of the amino acid from M to V at position 93.
+The protein's natural variant, known as in strain: MA45, MA50, MW37, MW6 and MW9, features a modification of the amino acid from Y to C at position 101.
+The protein's natural variant, known as in strain: MA45, MA50, MW37, MW6 and MW9, features a modification of the amino acid from L to F at position 102.
+The protein's natural variant, known as in strain: MA45, MA50, MW37, MW6 and MW9, features a modification of the amino acid from Q to E at position 111.
+The protein's natural variant, known as in strain: MA45, MA50, MW37, MW6 and MW9, features a modification of the amino acid from C to R at position 126.
+The protein's natural variant, known as in strain: LA9, features a modification of the amino acid from G to A at position 140.
+The protein's natural variant, known as in strain: MA45, MA50, MW37, MW6 and MW9, features a modification of the amino acid from A to L at position 150.
+The protein's natural variant, known as in strain: MA45, MA50, MW37, MW6 and MW9, features a modification of the amino acid from I to F at position 156.
+The protein's natural variant, known as in strain: MA45, MA50, MW37, MW6 and MW9, features a modification of the amino acid from S to T at position 157.
+The protein's natural variant, known as in strain: MA45, MA50, MW37, MW6 and MW9, features a modification of the amino acid from I to V at position 167.
+The protein's natural variant, known as in strain: LA116, MA13, MA18, MA43, MA45, MA48, MA50, MA7, MA74, MA8, MW25, MW27, MW29, MW3, MW32, MW37, MW44, MW46, MW56, MW6, MW7, MW9, NC21a, NC52a, NC62a, NC73a and NC79b, features a modification of the amino acid from R to M at position 194.
+The protein's natural variant, known as in strain: LA116, features a modification of the amino acid from W to L at position 196.
+The protein's natural variant, known as in strain: NC21a, NC52a, NC62a, NC73a and NC79b, features a modification of the amino acid from D to A at position 201.
+The protein's natural variant, known as in strain: LA116, MA45, MA50, MW37, MW6, MW9, NC52a and NC73a, features a modification of the amino acid from V to L at position 213.
+The protein's natural variant, known as in strain: LA116, MA45, MA50, MW37, MW6 and MW9, features a modification of the amino acid from I to M at position 214.
+The protein's natural variant, known as in strain: LA116, MA45, MA50, MW37, MW6 and MW9, features a modification of the amino acid from T to S at position 220.
+The protein's natural variant, known as in strain: MA45, MA50, MW37, MW6 and MW9, features a modification of the amino acid from R to M at position 235.
+The protein's natural variant, known as in strain: LA116, MA45, MA50, MW37, MW6 and MW9, features a modification of the amino acid from A to T at position 245.
+The protein's natural variant, known as in strain: MW44, features a modification of the amino acid from D to N at position 256.
+The protein's natural variant, known as in strain: MA45, MA50, MW37, MW6 and MW9, features a modification of the amino acid from G to R at position 267.
+The protein's natural variant, known as in strain: LA108 and LA120, features a modification of the amino acid from I to V at position 278.
+The protein's natural variant, known as in strain: LA116, LA25, LA4, MA24, MA45, MA50, MW37, MW6 and MW9, features a modification of the amino acid from Q to E at position 309.
+The protein's natural variant, known as in strain: NC16a, features a modification of the amino acid from F to S at position 313.
+The protein's natural variant, known as in strain: LA116, features a modification of the amino acid from R to S at position 341.
+The protein's natural variant, known as in strain: NC52a, NC73a and NC79b, features a modification of the amino acid from L to I at position 354.
+The protein's natural variant, known as in strain: LA9, features a modification of the amino acid from V to M at position 387.
+The protein's natural variant, known as in SLY1-20 mutant, features a modification of the amino acid from E to K at position 532.
+The protein's natural variant, known as in DD;, features a modification of the amino acid from G to E at position 23.
+The protein's natural variant, known as in DD, features a modification of the amino acid from N to T at position 39.
+The protein's natural variant, known as in DD, features a modification of the amino acid from K to KMFLTGK at position 47.
+The protein's natural variant, known as in DD; severe form, features a modification of the amino acid from L to S at position 65.
+The protein's natural variant, known as in DD, features a modification of the amino acid from N to S at position 101.
+The protein's natural variant, known as in DD;, features a modification of the amino acid from R to Q at position 131.
+The protein's natural variant, known as in DD, features a modification of the amino acid from P to L at position 160.
+The protein's natural variant, known as in DD, features a modification of the amino acid from S to P at position 186.
+The protein's natural variant, known as in DD; severe form, features a modification of the amino acid from G to D at position 211.
+The protein's natural variant, known as in DD, features a modification of the amino acid from V to M at position 223.
+The protein's natural variant, known as in DD; haemorrhagic lesions;, features a modification of the amino acid from C to F at position 268.
+The protein's natural variant, known as in DD, features a modification of the amino acid from G to V at position 310.
+The protein's natural variant, known as in DD; severe form, features a modification of the amino acid from C to R at position 318.
+The protein's natural variant, known as in DD, features a modification of the amino acid from I to T at position 348.
+The protein's natural variant, known as in DD, features a modification of the amino acid from T to K at position 357.
+The protein's natural variant, known as in DD, features a modification of the amino acid from E to G at position 412.
+The protein's natural variant, known as in DD, features a modification of the amino acid from S to F at position 495.
+The protein's natural variant, known as in DD; neuropsychiatric phenotype;, features a modification of the amino acid from C to R at position 560.
+The protein's natural variant, known as in DD, features a modification of the amino acid from L to P at position 590.
+The protein's natural variant, known as in AKV; no effect on protein abundance; loss of calcium ion transmembrane transport;, features a modification of the amino acid from P to L at position 602.
+The protein's natural variant, known as in DD, features a modification of the amino acid from G to A at position 625.
+The protein's natural variant, known as in DD, features a modification of the amino acid from D to E at position 626.
+The protein's natural variant, known as in DD, features a modification of the amino acid from A to P at position 672.
+The protein's natural variant, known as in DD; multiple neuropsychiatric features, features a modification of the amino acid from F to S at position 675.
+The protein's natural variant, known as in DD; depression, features a modification of the amino acid from K to E at position 683.
+The protein's natural variant, known as in DD, features a modification of the amino acid from Q to P at position 691.
+The protein's natural variant, known as in DD; moderate form, features a modification of the amino acid from D to N at position 702.
+The protein's natural variant, known as in DD; moderate form, features a modification of the amino acid from A to D at position 745.
+The protein's natural variant, known as in DD, features a modification of the amino acid from G to R at position 749.
+The protein's natural variant, known as in DD, features a modification of the amino acid from R to W at position 750.
+The protein's natural variant, known as in DD, features a modification of the amino acid from S to L at position 765.
+The protein's natural variant, known as in DD, features a modification of the amino acid from S to W at position 765.
+The protein's natural variant, known as in DD; haemorrhagic lesions and neuropsychiatric phenotype;, features a modification of the amino acid from N to S at position 767.
+The protein's natural variant, known as in DD;, features a modification of the amino acid from G to R at position 769.
+The protein's natural variant, known as in DD; mild/moderate form, features a modification of the amino acid from A to T at position 803.
+The protein's natural variant, known as in DD; severe form; petit mal epilepsy, features a modification of the amino acid from A to P at position 838.
+The protein's natural variant, known as in DD; depression, features a modification of the amino acid from V to F at position 843.
+The protein's natural variant, known as in DD, features a modification of the amino acid from G to GG at position 849.
+The protein's natural variant, known as in DD; retinitis pigmentosa, features a modification of the amino acid from C to G at position 875.
+The protein's natural variant, known as in DD, features a modification of the amino acid from L to P at position 900.
+The protein's natural variant, known as in DD; mild/moderate/severe form; one patient with epilepsy, features a modification of the amino acid from S to Y at position 920.
+The protein's natural variant, known as in DD; learning difficulties, features a modification of the amino acid from H to R at position 943.
+The protein's natural variant, known as in DD, features a modification of the amino acid from P to R at position 975.
+The protein's natural variant, known as in AFDCIN;, features a modification of the amino acid from E to Q at position 593.
+The protein's natural variant, known as in AFDCIN;, features a modification of the amino acid from V to F at position 1299.
+The protein's natural variant, known as in SPGF19; unknown pathological significance;, features a modification of the amino acid from R to W at position 85.
+The protein's natural variant, known as in SPGF19; unknown pathological significance;, features a modification of the amino acid from S to Y at position 129.
+The protein's natural variant, known as in SPGF19; unknown pathological significance;, features a modification of the amino acid from V to A at position 347.
+The protein's natural variant, known as in murE1, features a modification of the amino acid from E to K at position 344.
+The protein's natural variant, known as in murE1, features a modification of the amino acid from A to S at position 495.
+The natural variant of this protein is characterized by an amino acid alteration from L to I at position 170.
+The protein's natural variant, known as in strain: CM1-3, features a modification of the amino acid from I to T at position 127.
+The protein's natural variant, known as in strain: AM4 and CM1-3, features a modification of the amino acid from K to E at position 213.
+The protein's natural variant, known as in strain: AM4, features a modification of the amino acid from D to E at position 293.
+The natural variant of this protein is characterized by an amino acid alteration from A to T at position 25.
+The protein's natural variant, known as in GAMOS4;, features a modification of the amino acid from G to D at position 42.
+The protein's natural variant, known as in GAMOS4; abolished interaction with TPRKB;, features a modification of the amino acid from T to R at position 81.
+The protein's natural variant, known as in GAMOS4;, features a modification of the amino acid from R to L at position 243.
+The natural variant of this protein is characterized by an amino acid alteration from R to H at position 97.
+The natural variant of this protein is characterized by an amino acid alteration from D to G at position 164.
+The natural variant of this protein is characterized by an amino acid alteration from R to Q at position 456.
+The natural variant of this protein is characterized by an amino acid alteration from E to K at position 520.
+The natural variant of this protein is characterized by an amino acid alteration from E to Q at position 520.
+The natural variant of this protein is characterized by an amino acid alteration from M to I at position 525.
+The natural variant of this protein is characterized by an amino acid alteration from I to F at position 197.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to H at position 100.
+The protein's natural variant, known as in IVA;, features a modification of the amino acid from L to P at position 45.
+The protein's natural variant, known as in IVA;, features a modification of the amino acid from R to P at position 53.
+The protein's natural variant, known as in IVA;, features a modification of the amino acid from D to N at position 72.
+The protein's natural variant, known as in IVA, features a modification of the amino acid from A to G at position 97.
+The protein's natural variant, known as in IVA;, features a modification of the amino acid from G to R at position 123.
+The protein's natural variant, known as in IVA, features a modification of the amino acid from I to M at position 199.
+The protein's natural variant, known as in IVA;, features a modification of the amino acid from G to V at position 202.
+The protein's natural variant, known as in IVA; unknown pathological significance, features a modification of the amino acid from G to A at position 250.
+The protein's natural variant, known as in IVA, features a modification of the amino acid from L to P at position 279.
+The protein's natural variant, known as in IVA; unknown pathological significance;, features a modification of the amino acid from A to V at position 291.
+The protein's natural variant, known as in IVA;, features a modification of the amino acid from A to V at position 314.
+The protein's natural variant, known as in IVA;, features a modification of the amino acid from C to R at position 360.
+The protein's natural variant, known as in IVA;, features a modification of the amino acid from V to A at position 374.
+The protein's natural variant, known as in IVA; unknown pathological significance, features a modification of the amino acid from I to T at position 379.
+The protein's natural variant, known as in IVA;, features a modification of the amino acid from R to C at position 395.
+The protein's natural variant, known as in IVA; unknown pathological significance;, features a modification of the amino acid from R to Q at position 398.
+The protein's natural variant, known as in IVA;, features a modification of the amino acid from Y to C at position 403.
+The protein's natural variant, known as in IVA; unknown pathological significance, features a modification of the amino acid from Y to N at position 403.
+The protein's natural variant, known as in IVA, features a modification of the amino acid from R to L at position 414.
+The protein's natural variant, known as in strain: Guyane 11, features a modification of the amino acid from V to F at position 92.
+The protein's natural variant, known as in ALS22;, features a modification of the amino acid from T to P at position 145.
+The protein's natural variant, known as in ALS22; displays significantly different distribution in terms of incorporation into microtubules;, features a modification of the amino acid from R to C at position 215.
+The protein's natural variant, known as in ALS22; displays significantly lower levels of dimer assembly;, features a modification of the amino acid from R to C at position 320.
+The protein's natural variant, known as in ALS22; displays significantly lower levels of dimer assembly;, features a modification of the amino acid from R to H at position 320.
+The protein's natural variant, known as in ALS22; displays significantly different distribution in terms of incorporation into microtubules; destabilizes the microtubule network;, features a modification of the amino acid from A to T at position 383.
+The natural variant of this protein is characterized by an amino acid alteration from S to R at position 376.
+The protein's natural variant, known as in strain: Canton-S, features a modification of the amino acid from K to N at position 642.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from T to A at position 404.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from S to N at position 468.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from S to L at position 624.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from S to T at position 737.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from I to M at position 902.
+The protein's natural variant, known as in MRD23, features a modification of the amino acid from S to G at position 175.
+The protein's natural variant, known as in MRD23; unknown pathological significance, features a modification of the amino acid from Y to C at position 1071.
+The protein's natural variant, known as in IMGT allele IGHV3-23*02, features a modification of the amino acid from V to L at position 24.
+The protein's natural variant, known as in IMGT allele IGHV3-23*02, features a modification of the amino acid from A to G at position 80.
+The protein's natural variant, known as rare variant; unknown pathological significance; loss of NF-kappa-B complex activation; loss of interaction with IRAK4; reduces homooligomerization;, features a modification of the amino acid from S to Y at position 34.
+The protein's natural variant, known as found in hematological malignancies; somatic mutation; unknown pathological significance;, features a modification of the amino acid from V to M at position 39.
+The protein's natural variant, known as in IMD68; results in a loss of function; loss of NF-kappa-B complex activation;, features a modification of the amino acid from L to P at position 93.
+The protein's natural variant, known as found in hematological malignancies; somatic mutation; unknown pathological significance; loss of NF-kappa-B complex activation; loss of interaction with IRAK4; reduces homooligomerization;, features a modification of the amino acid from R to C at position 98.
+The protein's natural variant, known as found in hematological malignancies; somatic mutation; unknown pathological significance, features a modification of the amino acid from S to G at position 136.
+The protein's natural variant, known as found in hematological malignancies; somatic mutation; unknown pathological significance, features a modification of the amino acid from S to I at position 136.
+The protein's natural variant, known as found in hematological malignancies; somatic mutation; unknown pathological significance; no effect on NF-kappaB complex activation;, features a modification of the amino acid from M to I at position 178.
+The protein's natural variant, known as in IMD68; results in a loss of function; decreases NF-kappa-B complex activation;, features a modification of the amino acid from R to C at position 196.
+The protein's natural variant, known as found in hematological malignancies; somatic mutation; unknown pathological significance;, features a modification of the amino acid from V to F at position 204.
+The protein's natural variant, known as found in hematological malignancies; somatic mutation; unknown pathological significance, features a modification of the amino acid from W to R at position 205.
+The protein's natural variant, known as found in hematological malignancies; somatic mutation; unknown pathological significance, features a modification of the amino acid from S to C at position 206.
+The protein's natural variant, known as found in hematological malignancies; somatic mutation; unknown pathological significance, features a modification of the amino acid from I to T at position 207.
+The protein's natural variant, known as found in hematological malignancies; somatic mutation; unknown pathological significance; constitutively activates NF-kappaB complex activation, features a modification of the amino acid from S to R at position 209.
+The protein's natural variant, known as found in hematological malignancies; somatic mutation; unknown pathological significance; constitutively activates NF-kappaB complex activation, features a modification of the amino acid from M to T at position 219.
+The protein's natural variant, known as found in hematological malignancies; somatic mutation; unknown pathological significance; constitutively activates NF-kappaB complex activation;, features a modification of the amino acid from S to N at position 230.
+The protein's natural variant, known as in WM1; found in hematological malignancies; somatic mutation; unknown pathological significance; constitutively activates NF-kappaB complex activation; gain-of-function mutation; does not affect interaction with IRAK4;, features a modification of the amino acid from L to P at position 252.
+The protein's natural variant, known as found in hematological malignancies; somatic mutation; unknown pathological significance; no effect on NF-kappaB complex activation, features a modification of the amino acid from T to P at position 281.
+The natural variant of this protein is characterized by an amino acid alteration from A to T at position 164.
+The natural variant of this protein is characterized by an amino acid alteration from F to I at position 220.
+The protein's natural variant, known as in strain: cv. Lisse, features a modification of the amino acid from K to R at position 31.
+The protein's natural variant, known as in strain: cv. Bretagny, features a modification of the amino acid from M to T at position 47.
+The protein's natural variant, known as in strain: cv. Corsacalla-1, features a modification of the amino acid from N to D at position 61.
+The protein's natural variant, known as in strain: cv. Li-8, features a modification of the amino acid from T to S at position 73.
+The protein's natural variant, known as in strain: cv. Kas-1, features a modification of the amino acid from L to V at position 109.
+The protein's natural variant, known as in strain: cv. Chi-1 and cv. Gr-3, features a modification of the amino acid from E to K at position 115.
+The protein's natural variant, known as in strain: cv. Bla-1, features a modification of the amino acid from M to K at position 128.
+The protein's natural variant, known as in strain: cv. Lisse, features a modification of the amino acid from E to A at position 137.
+The protein's natural variant, known as in strain: cv. Lisse, features a modification of the amino acid from K to E at position 141.
+The protein's natural variant, known as in strain: cv. Lisse, features a modification of the amino acid from N to S at position 145.
+The protein's natural variant, known as in strain: cv. Kent, features a modification of the amino acid from K to M at position 151.
+The protein's natural variant, known as in strain: cv. Kas-1, features a modification of the amino acid from N to S at position 154.
+The protein's natural variant, known as in strain: cv. Kent, features a modification of the amino acid from D to G at position 159.
+The protein's natural variant, known as in strain: cv. Li-8, features a modification of the amino acid from D to N at position 159.
+The protein's natural variant, known as in strain: cv. Li-8, features a modification of the amino acid from N to D at position 163.
+The protein's natural variant, known as in strain: cv. Li-8, features a modification of the amino acid from Y to C at position 212.
+The protein's natural variant, known as in strain: cv. Bla-1, features a modification of the amino acid from A to T at position 219.
+The protein's natural variant, known as in CTRCT3; unknown pathological significance, features a modification of the amino acid from V to L at position 146.
+The protein's natural variant, known as in CTRCT3; unknown pathological significance, features a modification of the amino acid from G to V at position 149.
+The protein's natural variant, known as in CTRCT3; unknown pathological significance, features a modification of the amino acid from Q to K at position 155.
+The protein's natural variant, known as in CTRCT3; unknown pathological significance, features a modification of the amino acid from R to L at position 188.
+The protein's natural variant, known as in strain: W, features a modification of the amino acid from S to T at position 127.
+The protein's natural variant, known as changed DNA polymerase activity characterized by decreased fidelity and unchanged polymerization capacity; changed function in DNA double-strand break repair by non-homologous end joining and homologous recombination; no effect on 5'-deoxyribose-5-phosphate lyase activity;, features a modification of the amino acid from R to W at position 438.
+The protein's natural variant, known as probable disease-associated variant found in a sporadic case of centronulear myopathy; does not induce membrane tubulation in cultured cells, features a modification of the amino acid from R to C at position 24.
+The protein's natural variant, known as in CNM2;, features a modification of the amino acid from K to N at position 35.
+The protein's natural variant, known as in CNM2;, features a modification of the amino acid from R to C at position 145.
+The protein's natural variant, known as in CNM2; results in severely decreased membrane tubulation;, features a modification of the amino acid from D to N at position 151.
+The protein's natural variant, known as in CNM2; results in severely decreased membrane tubulation;, features a modification of the amino acid from R to Q at position 154.
+The protein's natural variant, known as in CNM2;, features a modification of the amino acid from R to C at position 234.
+The protein's natural variant, known as in strain: Isolate LSUMZM-3076, features a modification of the amino acid from V to I at position 3.
+The protein's natural variant, known as in strain: Isolate LSUMZM-3076, features a modification of the amino acid from T to A at position 514.
+The protein's natural variant, known as in DSS4-1; a dominant suppressor of SEC4-8, features a modification of the amino acid from D to G at position 108.
+The protein's natural variant, known as in allele HA-1H; induction of CTL recognition for epitope HA-1;, features a modification of the amino acid from R to H at position 139.
+The protein's natural variant, known as in PKD6;, features a modification of the amino acid from P to R at position 54.
+The protein's natural variant, known as in PKD6;, features a modification of the amino acid from L to P at position 77.
+The protein's natural variant, known as in IFN-tau1D, features a modification of the amino acid from D to N at position 29.
+The protein's natural variant, known as in IFN-tau1A, features a modification of the amino acid from F to L at position 88.
+The protein's natural variant, known as in IFN-tau1C and IFN-tau1D, features a modification of the amino acid from V to M at position 169.
+The protein's natural variant, known as in RNA edited version;, features a modification of the amino acid from Y to C at position 2.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from Q to R at position 5.
+The protein's natural variant, known as in RNA edited version;, features a modification of the amino acid from K to R at position 15.
+The protein's natural variant, known as in MRXSPF, features a modification of the amino acid from R to Q at position 117.
+The protein's natural variant, known as in MRXSPF, features a modification of the amino acid from Q to P at position 119.
+The protein's natural variant, known as in MRXSPF, features a modification of the amino acid from E to G at position 184.
+The protein's natural variant, known as in MRXSPF, features a modification of the amino acid from P to L at position 186.
+The protein's natural variant, known as in MRXSPF, features a modification of the amino acid from T to K at position 187.
+The protein's natural variant, known as in MRXSPF;, features a modification of the amino acid from T to M at position 187.
+The protein's natural variant, known as in MRXSPF, features a modification of the amino acid from T to P at position 187.
+The protein's natural variant, known as in MRXSPF, features a modification of the amino acid from T to R at position 187.
+The protein's natural variant, known as in MRXSPF;, features a modification of the amino acid from Y to C at position 189.
+The protein's natural variant, known as in MRXSPF, features a modification of the amino acid from H to Q at position 190.
+The protein's natural variant, known as in MRXSPF, features a modification of the amino acid from L to P at position 191.
+The protein's natural variant, known as in MRXSPF, features a modification of the amino acid from Q to P at position 201.
+The protein's natural variant, known as in PARK20; impairs the phosphatase activity of the enzyme toward phosphatidylinositol-3-phosphate and phosphatidylinositol-4-phosphate;, features a modification of the amino acid from R to Q at position 219.
+The protein's natural variant, known as in PARK20;, features a modification of the amino acid from R to P at position 420.
+The protein's natural variant, known as in DEE53; decreased inositol phosphate phosphatase activity;, features a modification of the amino acid from Y to C at position 849.
+The protein's natural variant, known as likely benign variant; no effect on inositol phosphate phosphatase activity;, features a modification of the amino acid from M to I at position 981.
+The protein's natural variant, known as likely benign variant; no effect on inositol phosphate phosphatase activity, features a modification of the amino acid from Y to S at position 1018.
+The protein's natural variant, known as in PARK20; unknown pathological significance; the patient also carries a heterozygous PINK1 truncating mutation;, features a modification of the amino acid from S to R at position 1383.
+The protein's natural variant, known as in MCOP8;, features a modification of the amino acid from V to M at position 71.
+The protein's natural variant, known as in MCOP8; does not affect ALDH1A3 expression; results in strongly reduced protein levels;, features a modification of the amino acid from R to C at position 89.
+The protein's natural variant, known as in MCOP8;, features a modification of the amino acid from A to V at position 145.
+The protein's natural variant, known as in MCOP8, features a modification of the amino acid from C to Y at position 174.
+The protein's natural variant, known as in MCOP8, features a modification of the amino acid from P to R at position 355.
+The protein's natural variant, known as in MCOP8, features a modification of the amino acid from I to F at position 369.
+The protein's natural variant, known as in MCOP8, features a modification of the amino acid from G to R at position 382.
+The protein's natural variant, known as in MCOP8, features a modification of the amino acid from E to K at position 411.
+The protein's natural variant, known as in MCOP8, features a modification of the amino acid from N to K at position 466.
+The protein's natural variant, known as in MCOP8; does not affect ALDH1A3 expression; results in strongly reduced protein levels;, features a modification of the amino acid from A to P at position 493.
+The protein's natural variant, known as in PLS;, features a modification of the amino acid from W to S at position 39.
+The protein's natural variant, known as in PLS;, features a modification of the amino acid from H to P at position 127.
+The protein's natural variant, known as in PLS;, features a modification of the amino acid from V to E at position 129.
+The protein's natural variant, known as in PLS;, features a modification of the amino acid from G to R at position 139.
+The protein's natural variant, known as in PLS;, features a modification of the amino acid from D to Y at position 236.
+The protein's natural variant, known as in PLS, features a modification of the amino acid from V to F at position 249.
+The protein's natural variant, known as in PLS;, features a modification of the amino acid from Q to L at position 252.
+The protein's natural variant, known as in PLS;, features a modification of the amino acid from R to H at position 272.
+The protein's natural variant, known as in PLS;, features a modification of the amino acid from R to P at position 272.
+The protein's natural variant, known as in HMS and PLS;, features a modification of the amino acid from Q to R at position 286.
+The protein's natural variant, known as in PLS;, features a modification of the amino acid from C to Y at position 291.
+The protein's natural variant, known as in PLS, features a modification of the amino acid from Y to H at position 294.
+The protein's natural variant, known as in PLS, features a modification of the amino acid from G to D at position 300.
+The protein's natural variant, known as in PLS, features a modification of the amino acid from G to S at position 300.
+The protein's natural variant, known as in PLS;, features a modification of the amino acid from G to S at position 301.
+The protein's natural variant, known as in PLS, features a modification of the amino acid from G to V at position 301.
+The protein's natural variant, known as in PLS, features a modification of the amino acid from Y to N at position 304.
+The protein's natural variant, known as in PLS;, features a modification of the amino acid from Q to R at position 312.
+The protein's natural variant, known as in PLS;, features a modification of the amino acid from E to G at position 319.
+The protein's natural variant, known as in PLS;, features a modification of the amino acid from R to C at position 339.
+The protein's natural variant, known as in PLS, features a modification of the amino acid from Y to C at position 340.
+The protein's natural variant, known as in PLS and AP1;, features a modification of the amino acid from Y to C at position 347.
+The protein's natural variant, known as in PLS, features a modification of the amino acid from H to N at position 405.
+The protein's natural variant, known as in PLS;, features a modification of the amino acid from H to R at position 405.
+The protein's natural variant, known as in AP1;, features a modification of the amino acid from Y to C at position 412.
+The protein's natural variant, known as in PLS;, features a modification of the amino acid from W to C at position 429.
+The protein's natural variant, known as in PLS, features a modification of the amino acid from E to G at position 447.
+The protein's natural variant, known as 60% decrease of 7-alpha hydroxylase activity;, features a modification of the amino acid from R to P at position 23.
+The protein's natural variant, known as associated with elevated serum (24S)-hydroxycholesterol levels; 30% decrease of 7-alpha hydroxylase activity;, features a modification of the amino acid from R to H at position 103.
+The protein's natural variant, known as 10% decrease of 7-alpha hydroxylase activity;, features a modification of the amino acid from Y to H at position 288.
+The protein's natural variant, known as associated with elevated serum (24S)-hydroxycholesterol levels; impairs 7-alpha hydroxylase activity;, features a modification of the amino acid from N to K at position 324.
+The protein's natural variant, known as impairs 7-alpha hydroxylase activity;, features a modification of the amino acid from K to Q at position 329.
+The protein's natural variant, known as in NEDRIHF, features a modification of the amino acid from IA to T at position 89.
+The protein's natural variant, known as in NEDRIHF;, features a modification of the amino acid from A to P at position 89.
+The protein's natural variant, known as in NEDRIHF;, features a modification of the amino acid from K to E at position 97.
+The protein's natural variant, known as in NEDRIHF;, features a modification of the amino acid from L to P at position 100.
+The protein's natural variant, known as in NEDRIHF;, features a modification of the amino acid from M to K at position 157.
+The protein's natural variant, known as in NEDRIHF;, features a modification of the amino acid from R to P at position 199.
+The protein's natural variant, known as in NEDRIHF;, features a modification of the amino acid from I to F at position 206.
+The protein's natural variant, known as in head and neck cancer, features a modification of the amino acid from S to L at position 184.
+The protein's natural variant, known as in lung carcinoma; somatic mutation, features a modification of the amino acid from A to P at position 187.
+The protein's natural variant, known as in SHFM4, features a modification of the amino acid from T to TP at position 193.
+The protein's natural variant, known as in cervical cancer, features a modification of the amino acid from Q to L at position 204.
+The protein's natural variant, known as in SHFM4;, features a modification of the amino acid from K to E at position 232.
+The protein's natural variant, known as in SHFM4;, features a modification of the amino acid from K to E at position 233.
+The protein's natural variant, known as in EEC3;, features a modification of the amino acid from R to Q at position 243.
+The protein's natural variant, known as in EEC3;, features a modification of the amino acid from R to W at position 243.
+The protein's natural variant, known as in EEC3;, features a modification of the amino acid from R to Q at position 266.
+The protein's natural variant, known as in colon cancer, features a modification of the amino acid from P to H at position 279.
+The protein's natural variant, known as in EEC3, features a modification of the amino acid from C to Y at position 308.
+The protein's natural variant, known as in EEC3, features a modification of the amino acid from S to N at position 311.
+The protein's natural variant, known as in EEC3;, features a modification of the amino acid from R to C at position 318.
+The protein's natural variant, known as in EEC3 and RHS; does not decrease the transcriptional activity of the isoform 5 on a TP53 reporter system but disrupts the dominant-negative activity of isoform 2 and isoform 5 on the transcriptional activity of TP53;, features a modification of the amino acid from R to H at position 318.
+The protein's natural variant, known as in EEC3, features a modification of the amino acid from R to Q at position 318.
+The protein's natural variant, known as in EEC3;, features a modification of the amino acid from R to C at position 319.
+The protein's natural variant, known as in EEC3 and SHFM4;, features a modification of the amino acid from R to H at position 319.
+The protein's natural variant, known as in EEC3, features a modification of the amino acid from R to S at position 319.
+The protein's natural variant, known as in ADULT syndrome; confers novel transcription activation capacity on isoform 6;, features a modification of the amino acid from R to Q at position 337.
+The protein's natural variant, known as in EEC3;, features a modification of the amino acid from R to Q at position 343.
+The protein's natural variant, known as in EEC3;, features a modification of the amino acid from R to W at position 343.
+The protein's natural variant, known as in EEC3; abolishes transcription activation;, features a modification of the amino acid from C to R at position 345.
+The protein's natural variant, known as in EEC3, features a modification of the amino acid from C to S at position 347.
+The protein's natural variant, known as in EEC3, features a modification of the amino acid from P to S at position 348.
+The protein's natural variant, known as in EEC3;, features a modification of the amino acid from D to G at position 351.
+The protein's natural variant, known as in EEC3, features a modification of the amino acid from D to H at position 351.
+The protein's natural variant, known as in OFC8;, features a modification of the amino acid from R to G at position 352.
+The protein's natural variant, known as in RHS;, features a modification of the amino acid from I to T at position 549.
+The protein's natural variant, known as in AEC;, features a modification of the amino acid from L to F at position 553.
+The protein's natural variant, known as in ovarian cancer, features a modification of the amino acid from S to A at position 560.
+The protein's natural variant, known as in AEC;, features a modification of the amino acid from C to G at position 561.
+The protein's natural variant, known as in RHS;, features a modification of the amino acid from S to P at position 580.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation, features a modification of the amino acid from G to E at position 144.
+The protein's natural variant, known as in an ovarian mucinous carcinoma sample; somatic mutation, features a modification of the amino acid from F to L at position 150.
+The protein's natural variant, known as in a renal clear cell carcinoma sample; somatic mutation, features a modification of the amino acid from I to V at position 301.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from E to D at position 562.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation, features a modification of the amino acid from R to I at position 567.
+The protein's natural variant, known as in DFNB108; impairs plasma membrane location; abolishes downstream NFkB activation;, features a modification of the amino acid from R to T at position 736.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation, features a modification of the amino acid from S to N at position 776.
+The protein's natural variant, known as in strain: Zhongzuo 06-06, features a modification of the amino acid from D to N at position 170.
+The protein's natural variant, known as in strain: Liao 04M05-3 and Zhongzuo J8035, features a modification of the amino acid from R to K at position 180.
+The protein's natural variant, known as in about 30% of the molecules, features a modification of the amino acid from Y to F at position 62.
+The protein's natural variant, known as in strain: C7258, features a modification of the amino acid from E to D at position 40.
+The protein's natural variant, known as in strain: AU1808, features a modification of the amino acid from L to LL at position 13.
+The protein's natural variant, known as found in a patient with cohesinopathy; unknown pathological significance;, features a modification of the amino acid from R to H at position 731.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to Q at position 74.
+The protein's natural variant, known as in OCA4;, features a modification of the amino acid from M to I at position 42.
+The protein's natural variant, known as in OCA4;, features a modification of the amino acid from P to A at position 58.
+The protein's natural variant, known as in OCA4, features a modification of the amino acid from P to S at position 58.
+The protein's natural variant, known as in OCA4;, features a modification of the amino acid from L to R at position 60.
+The protein's natural variant, known as in OCA4, features a modification of the amino acid from G to S at position 64.
+The protein's natural variant, known as in OCA4;, features a modification of the amino acid from G to R at position 110.
+The protein's natural variant, known as in OCA4, features a modification of the amino acid from L to P at position 151.
+The protein's natural variant, known as in OCA4;, features a modification of the amino acid from D to N at position 157.
+The protein's natural variant, known as in OCA4;, features a modification of the amino acid from D to H at position 160.
+The protein's natural variant, known as in OCA4, features a modification of the amino acid from G to V at position 188.
+The protein's natural variant, known as in OCA4;, features a modification of the amino acid from W to C at position 202.
+The protein's natural variant, known as in OCA4, features a modification of the amino acid from H to Q at position 233.
+The protein's natural variant, known as associated with variability of hair, eye and skin pigmentation; in Caucasians associated with dark hair, skin and eye color; strong protective effect for melanoma risk;, features a modification of the amino acid from E to K at position 272.
+The protein's natural variant, known as in OCA4;, features a modification of the amino acid from T to S at position 302.
+The protein's natural variant, known as in OCA4, features a modification of the amino acid from Y to C at position 317.
+The protein's natural variant, known as in OCA4;, features a modification of the amino acid from R to C at position 348.
+The protein's natural variant, known as in OCA4;, features a modification of the amino acid from G to R at position 349.
+The protein's natural variant, known as in OCA4;, features a modification of the amino acid from L to P at position 361.
+The protein's natural variant, known as in OCA4;, features a modification of the amino acid from E to K at position 368.
+The protein's natural variant, known as associated with variability of hair, eye and skin pigmentation; in Caucasians associated with dark hair, skin and eye color; strong protective effect for melanoma risk; decreased protein stability; no effect on subcellular location;, features a modification of the amino acid from L to F at position 374.
+The protein's natural variant, known as in OCA4;, features a modification of the amino acid from F to L at position 418.
+The protein's natural variant, known as in OCA4;, features a modification of the amino acid from A to T at position 477.
+The protein's natural variant, known as in OCA4;, features a modification of the amino acid from A to V at position 486.
+The protein's natural variant, known as in mutant RNA1-1, features a modification of the amino acid from S to F at position 17.
+The protein's natural variant, known as in mutant RNA1-1, features a modification of the amino acid from A to V at position 194.
+The protein's natural variant, known as in BBS3; abrogates the GTP-binding ability without affecting GDP-binding/dissociating properties; increased proteasomal degradation;, features a modification of the amino acid from T to M at position 31.
+The protein's natural variant, known as in BBS3; locked in a GDP-bound state that differs from its wild-type counterpart which is mainly GTP-bound; increased proteasomal degradation;, features a modification of the amino acid from T to R at position 31.
+The protein's natural variant, known as in RP55;, features a modification of the amino acid from A to V at position 89.
+The protein's natural variant, known as in BBS3;, features a modification of the amino acid from I to T at position 94.
+The protein's natural variant, known as in BBS3; abrogates the GTP-binding ability; increased proteasomal degradation;, features a modification of the amino acid from G to A at position 169.
+The protein's natural variant, known as in BBS3; abrogates the GTP-binding ability; increased proteasomal degradation;, features a modification of the amino acid from L to W at position 170.
+The protein's natural variant, known as in allele A, features a modification of the amino acid from N to NN at position 216.
+The protein's natural variant, known as in allele B, features a modification of the amino acid from S to SQS at position 251.
+The natural variant of this protein is characterized by an amino acid alteration from G to D at position 32.
+The natural variant of this protein is characterized by an amino acid alteration from P to L at position 994.
+The protein's natural variant, known as in SCKL7; does not disrupt protein expression or localization or affect mitotic functions in an obvious way;, features a modification of the amino acid from Q to R at position 1222.
+The protein's natural variant, known as in SCKL7; does not disrupt protein expression or localization or affect mitotic functions in an obvious way;, features a modification of the amino acid from N to S at position 1709.
+The protein's natural variant, known as in HFI; reduced enzymatic activity;, features a modification of the amino acid from R to W at position 46.
+The protein's natural variant, known as in HFI; affects proper folding;, features a modification of the amino acid from I to T at position 74.
+The protein's natural variant, known as in HFI; America; partial activity, features a modification of the amino acid from C to R at position 135.
+The protein's natural variant, known as in one subject with fructose intolerance; rare variant; America;, features a modification of the amino acid from W to R at position 148.
+The protein's natural variant, known as in HFI; frequent mutation;, features a modification of the amino acid from A to P at position 150.
+The protein's natural variant, known as in HFI; frequent mutation;, features a modification of the amino acid from A to D at position 175.
+The protein's natural variant, known as in HFI, features a modification of the amino acid from C to R at position 178.
+The protein's natural variant, known as in HFI, features a modification of the amino acid from P to R at position 185.
+The protein's natural variant, known as in HFI; affects proper folding;, features a modification of the amino acid from V to F at position 222.
+The protein's natural variant, known as in HFI; affects proper folding;, features a modification of the amino acid from L to P at position 229.
+The protein's natural variant, known as in HFI; Italy;, features a modification of the amino acid from L to P at position 257.
+The protein's natural variant, known as in HFI, features a modification of the amino acid from L to P at position 284.
+The protein's natural variant, known as in HFI; 100-fold decrease in catalytic efficiency for substrates FBP and F1P;, features a modification of the amino acid from R to Q at position 304.
+The protein's natural variant, known as in HFI; Turkey; 4800-fold decrease in catalytic efficiency for FBP and inactive with F1P;, features a modification of the amino acid from R to W at position 304.
+The protein's natural variant, known as in HFI; frequent mutation;, features a modification of the amino acid from N to K at position 335.
+The protein's natural variant, known as in HFI; Turkey and South Europe;, features a modification of the amino acid from A to V at position 338.
+The protein's natural variant, known as in HFI; almost no effect on enzymatic activity at 30 degrees Celsius, but reduced activity at higher temperatures;, features a modification of the amino acid from Y to H at position 343.
+The protein's natural variant, known as improve activity, features a modification of the amino acid from D to N at position 92.
+The protein's natural variant, known as improve activity, features a modification of the amino acid from E to K at position 93.
+The protein's natural variant, known as improve activity, features a modification of the amino acid from W to C at position 976.
+The protein's natural variant, known as improve activity, features a modification of the amino acid from S to G at position 978.
+The natural variant of this protein is characterized by an amino acid alteration from L to LQ at position 387.
+The protein's natural variant, known as in strain: Isolate Durban5, features a modification of the amino acid from T to I at position 2.
+The protein's natural variant, known as in strain: Isolate Durban5, features a modification of the amino acid from K to M at position 129.
+The protein's natural variant, known as in strain: Isolate Durban5, features a modification of the amino acid from K to M at position 138.
+The protein's natural variant, known as in strain: Isolate Durban5, features a modification of the amino acid from F to S at position 215.
+The protein's natural variant, known as in strain: Autumn Gold, Desert Storm, Salinas 88 and Vanguard 75, alleles mo1(2) and Ls-eIF4E(2), features a modification of the amino acid from A to P at position 75.
+The protein's natural variant, known as in strain: Alize, Classic, Floribibb, Malika, Mantilia, Oriana and Presidio, alleles mo1(1) and Ls-eIF4E(1), features a modification of the amino acid from QGA to H at position 115.
+The protein's natural variant, known as in strain: Alize, Classic, Floribibb, Malika, Mantilia, Oriana and Presidio, alleles mo1(1) and Ls-eIF4E(1), features a modification of the amino acid from A to S at position 191.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation;, features a modification of the amino acid from S to F at position 737.
+The protein's natural variant, known as in IDDPADS; unknown pathological significance;, features a modification of the amino acid from P to L at position 149.
+The protein's natural variant, known as in IDDPADS; unknown pathological significance; loss of 3',5'-cyclic-AMP phosphodiesterase activity; loss of 3',5'-cyclic-GMP phosphodiesterase activity, features a modification of the amino acid from D to G at position 480.
+The natural variant of this protein is characterized by an amino acid alteration from S to SSSS at position 319.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 70.
+The natural variant of this protein is characterized by an amino acid alteration from E to K at position 95.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from D to Y at position 191.
+The protein's natural variant, known as in HAFOUS;, features a modification of the amino acid from M to I at position 225.
+The protein's natural variant, known as in HAFOUS, features a modification of the amino acid from E to K at position 345.
+The protein's natural variant, known as in HAFOUS, features a modification of the amino acid from L to F at position 373.
+The protein's natural variant, known as in HAFOUS, features a modification of the amino acid from G to D at position 392.
+The protein's natural variant, known as in HAFOUS, features a modification of the amino acid from V to G at position 485.
+The protein's natural variant, known as in HAFOUS; unknown pathological significance; the patient also carries a de novo clinically relevant variant in SLC2A1, features a modification of the amino acid from L to P at position 757.
+The protein's natural variant, known as in HAFOUS, features a modification of the amino acid from I to T at position 766.
+The protein's natural variant, known as in HAFOUS, features a modification of the amino acid from D to N at position 1080.
+The natural variant of this protein is characterized by an amino acid alteration from A to S at position 149.
+The protein's natural variant, known as in MOTA; unknown pathological significance;, features a modification of the amino acid from D to G at position 102.
+The protein's natural variant, known as in TRIGNO2;, features a modification of the amino acid from R to Q at position 498.
+The protein's natural variant, known as in BNAR;, features a modification of the amino acid from R to W at position 649.
+The protein's natural variant, known as in MOTA;, features a modification of the amino acid from L to R at position 1324.
+The protein's natural variant, known as in BNAR;, features a modification of the amino acid from G to S at position 1440.
+The protein's natural variant, known as in TRIGNO2;, features a modification of the amino acid from E to V at position 1500.
+The protein's natural variant, known as in MOTA;, features a modification of the amino acid from V to I at position 2091.
+The protein's natural variant, known as reduced activity, features a modification of the amino acid from L to I at position 209.
+The protein's natural variant, known as found in a patient with isolated coloboma; decreased incorporation into F-actin; decreased interaction with cofilin; loss of interaction with TWF1, CAPZB and profilin, features a modification of the amino acid from P to L at position 70.
+The protein's natural variant, known as in DFNA20;, features a modification of the amino acid from T to I at position 89.
+The protein's natural variant, known as in DFNA20;, features a modification of the amino acid from K to M at position 118.
+The protein's natural variant, known as in DFNA20;, features a modification of the amino acid from K to N at position 118.
+The protein's natural variant, known as in BRWS2;, features a modification of the amino acid from T to I at position 120.
+The protein's natural variant, known as in DFNA20;, features a modification of the amino acid from I to V at position 122.
+The protein's natural variant, known as in BRWS2;, features a modification of the amino acid from A to V at position 135.
+The protein's natural variant, known as in BRWS2;, features a modification of the amino acid from S to F at position 155.
+The protein's natural variant, known as in DFNA20, features a modification of the amino acid from D to H at position 187.
+The protein's natural variant, known as in BRWS2;, features a modification of the amino acid from T to K at position 203.
+The protein's natural variant, known as in DFNA20;, features a modification of the amino acid from E to K at position 241.
+The protein's natural variant, known as in BRWS2;, features a modification of the amino acid from R to W at position 254.
+The protein's natural variant, known as in BRWS2;, features a modification of the amino acid from R to W at position 256.
+The protein's natural variant, known as in DFNA20;, features a modification of the amino acid from P to L at position 264.
+The protein's natural variant, known as in DFNA20;, features a modification of the amino acid from T to I at position 278.
+The protein's natural variant, known as in DFNA20; unknown pathological significance, features a modification of the amino acid from E to K at position 316.
+The protein's natural variant, known as in DFNA20;, features a modification of the amino acid from P to A at position 332.
+The protein's natural variant, known as in DFNA20;, features a modification of the amino acid from V to A at position 370.
+The protein's natural variant, known as in PMDS1;, features a modification of the amino acid from V to G at position 12.
+The protein's natural variant, known as in PMDS1, features a modification of the amino acid from L to P at position 70.
+The protein's natural variant, known as in PMDS1, features a modification of the amino acid from G to V at position 101.
+The protein's natural variant, known as in PMDS1;, features a modification of the amino acid from R to W at position 123.
+The protein's natural variant, known as in PMDS1;, features a modification of the amino acid from Y to C at position 167.
+The protein's natural variant, known as in PMDS1;, features a modification of the amino acid from R to C at position 194.
+The protein's natural variant, known as in PMDS1;, features a modification of the amino acid from V to A at position 477.
+The protein's natural variant, known as in PMDS1;, features a modification of the amino acid from H to Q at position 506.
+The protein's natural variant, known as in PMDS1, features a modification of the amino acid from C to Y at position 525.
+The protein's natural variant, known as found in a family with intellectual disability; unknown pathological significance;, features a modification of the amino acid from S to N at position 179.
+The protein's natural variant, known as in strain: C57BL/6 and Swiss Webster, features a modification of the amino acid from G to S at position 253.
+The protein's natural variant, known as in strain: C57BL/6 and Swiss Webster, features a modification of the amino acid from L to P at position 262.
+The protein's natural variant, known as in strain: Swiss Webster, features a modification of the amino acid from G to D at position 269.
+The protein's natural variant, known as in strain: Swiss Webster, features a modification of the amino acid from S to T at position 293.
+The protein's natural variant, known as in strain: C57BL/6 and Swiss Webster, features a modification of the amino acid from A to P at position 447.
+The protein's natural variant, known as in strain: C57BL/6 and Swiss Webster, features a modification of the amino acid from S to P at position 451.
+The protein's natural variant, known as in strain: C57BL/6 and Swiss Webster, features a modification of the amino acid from L to R at position 526.
+The protein's natural variant, known as in strain: C57BL/6, features a modification of the amino acid from N to S at position 552.
+The protein's natural variant, known as in strain: C57BL/6, features a modification of the amino acid from M to T at position 579.
+The protein's natural variant, known as in strain: C57BL/10, features a modification of the amino acid from T to A at position 656.
+The protein's natural variant, known as in strain: C57BL/10, features a modification of the amino acid from R to C at position 659.
+The protein's natural variant, known as in strain: C57BL/10, features a modification of the amino acid from D to N at position 685.
+The protein's natural variant, known as in strain: Swiss Webster, features a modification of the amino acid from E to G at position 706.
+The protein's natural variant, known as in strain: Swiss Webster, features a modification of the amino acid from E to G at position 711.
+The protein's natural variant, known as in strain: C57BL/10, features a modification of the amino acid from T to A at position 717.
+The protein's natural variant, known as in strain: 129/J, features a modification of the amino acid from S to C at position 778.
+The protein's natural variant, known as in strain: C57BL/6, features a modification of the amino acid from S to T at position 996.
+The protein's natural variant, known as in strain: C57BL/6, features a modification of the amino acid from P to S at position 1188.
+The protein's natural variant, known as in strain: C57BL/6, features a modification of the amino acid from MSTF to TCTL at position 1199.
+The protein's natural variant, known as in strain: FVB/N, features a modification of the amino acid from I to L at position 666.
+The protein's natural variant, known as found in a renal cell carcinoma sample; somatic mutation, features a modification of the amino acid from M to K at position 356.
+The protein's natural variant, known as in FMD2;, features a modification of the amino acid from E to Q at position 70.
+The protein's natural variant, known as in FMD2;, features a modification of the amino acid from V to E at position 100.
+The protein's natural variant, known as in CSCF;, features a modification of the amino acid from G to C at position 110.
+The protein's natural variant, known as in FMD2; increases autophosphorylation; no effect on MAPK signaling; no effect on NF-kappa-B signaling;, features a modification of the amino acid from G to R at position 168.
+The protein's natural variant, known as in CSCF;, features a modification of the amino acid from W to R at position 241.
+The protein's natural variant, known as found in a consanguineous family with intellectual disability; unknown pathological significance;, features a modification of the amino acid from R to Q at position 410.
+The protein's natural variant, known as in FMD2; does not affect interaction with TAB2; does not affect homodimerization; increases autophosphorylation; increases MAPK signaling; increases NF-kappa-B signaling;, features a modification of the amino acid from P to L at position 512.
+The protein's natural variant, known as in DEE4, features a modification of the amino acid from S to F at position 42.
+The protein's natural variant, known as probable disease-associated variant found in a patient with epileptic encephalopathy;, features a modification of the amino acid from S to P at position 80.
+The protein's natural variant, known as in DEE4; may alter protein structure;, features a modification of the amino acid from V to D at position 84.
+The protein's natural variant, known as no effect on subcellular location;, features a modification of the amino acid from V to I at position 84.
+The protein's natural variant, known as in DEE4; reduced thermostability; decreased binding to STX1A;, features a modification of the amino acid from C to Y at position 180.
+The protein's natural variant, known as in DEE4, features a modification of the amino acid from L to R at position 183.
+The protein's natural variant, known as in DEE4;, features a modification of the amino acid from R to W at position 190.
+The protein's natural variant, known as in DEE4, features a modification of the amino acid from A to T at position 251.
+The protein's natural variant, known as in DEE4, features a modification of the amino acid from L to P at position 281.
+The protein's natural variant, known as in DEE4;, features a modification of the amino acid from E to K at position 283.
+The protein's natural variant, known as in DEE4, features a modification of the amino acid from D to Y at position 285.
+The protein's natural variant, known as in DEE4;, features a modification of the amino acid from R to H at position 292.
+The protein's natural variant, known as in DEE4;, features a modification of the amino acid from C to R at position 354.
+The protein's natural variant, known as in DEE4;, features a modification of the amino acid from R to C at position 406.
+The protein's natural variant, known as in DEE4;, features a modification of the amino acid from R to H at position 406.
+The protein's natural variant, known as variant of uncertain significance; expressed at low levels compared with wild-type; no effect on subcellular location, features a modification of the amino acid from Q to L at position 431.
+The protein's natural variant, known as in DEE4; may alter protein structure;, features a modification of the amino acid from M to R at position 443.
+The protein's natural variant, known as in DEE4, features a modification of the amino acid from H to P at position 445.
+The protein's natural variant, known as in DEE4;, features a modification of the amino acid from P to L at position 480.
+The protein's natural variant, known as found in a patient with Lennox-Gastaut syndrome; unknown pathological significance;, features a modification of the amino acid from G to C at position 544.
+The protein's natural variant, known as in DEE4; may alter protein structure;, features a modification of the amino acid from G to D at position 544.
+The protein's natural variant, known as probable disease-associated variant found in a patient with epileptic encephalopathy, features a modification of the amino acid from T to A at position 570.
+The protein's natural variant, known as in DEE4, features a modification of the amino acid from T to P at position 574.
+The protein's natural variant, known as in a patient with Sezary syndrome, features a modification of the amino acid from E to K at position 2200.
+The protein's natural variant, known as associated with a pro-atherogenic phenotype;, features a modification of the amino acid from A to P at position 387.
+The protein's natural variant, known as in strain: 221, features a modification of the amino acid from V to I at position 40.
+The protein's natural variant, known as in strain: 221, features a modification of the amino acid from T to A at position 42.
+The protein's natural variant, known as in strain: 221, features a modification of the amino acid from M to L at position 44.
+The protein's natural variant, known as in strain: 221, features a modification of the amino acid from L to F at position 49.
+The protein's natural variant, known as in strain: 221, features a modification of the amino acid from N to Y at position 56.
+The protein's natural variant, known as in strain: 221, features a modification of the amino acid from VE to QD at position 60.
+The protein's natural variant, known as in strain: 221, features a modification of the amino acid from T to L at position 65.
+The protein's natural variant, known as in strain: 221, features a modification of the amino acid from L to G at position 68.
+The protein's natural variant, known as in strain: 221, features a modification of the amino acid from V to I at position 100.
+The protein's natural variant, known as in strain: 221, features a modification of the amino acid from L to Q at position 103.
+The natural variant of this protein is characterized by an amino acid alteration from D to G at position 203.
+The protein's natural variant, known as in DBA13; results in reduced protein expression; results in pre-rRNA processing defect;, features a modification of the amino acid from I to F at position 31.
+The protein's natural variant, known as in DBA13; results in reduced protein expression; results in pre-rRNA processing defect;, features a modification of the amino acid from I to T at position 50.
+The protein's natural variant, known as in ALS20; unknown pathological significance, features a modification of the amino acid from Q to K at position 277.
+The protein's natural variant, known as in ALS20;, features a modification of the amino acid from D to N at position 314.
+The protein's natural variant, known as in IBMPFD3; reduces binding to UBQLN2;, features a modification of the amino acid from D to V at position 314.
+The protein's natural variant, known as in ALS20;, features a modification of the amino acid from N to S at position 319.
+The protein's natural variant, known as in ALS20; increases subcellular localization of HNRNPA1 in cytoplasmic inclusions with stress granules, features a modification of the amino acid from P to S at position 340.
+The protein's natural variant, known as in Thionville; O(2) affinity down;, features a modification of the amino acid from V to E at position 2.
+The protein's natural variant, known as in ChongQing; O(2) affinity up;, features a modification of the amino acid from L to R at position 3.
+The protein's natural variant, known as in J-Toronto;, features a modification of the amino acid from A to D at position 6.
+The protein's natural variant, known as in Karachi;, features a modification of the amino acid from A to P at position 6.
+The protein's natural variant, known as in Sawara; O(2) affinity up;, features a modification of the amino acid from D to A at position 7.
+The protein's natural variant, known as in Swan River;, features a modification of the amino acid from D to G at position 7.
+The protein's natural variant, known as in Dunn; O(2) affinity up;, features a modification of the amino acid from D to N at position 7.
+The protein's natural variant, known as in Ferndown; O(2) affinity up;, features a modification of the amino acid from D to V at position 7.
+The protein's natural variant, known as in Woodville; O(2) affinity up;, features a modification of the amino acid from D to Y at position 7.
+The protein's natural variant, known as in Kurosaki;, features a modification of the amino acid from K to E at position 8.
+The protein's natural variant, known as in Broomfield;, features a modification of the amino acid from N to T at position 10.
+The protein's natural variant, known as in Anantharaj;, features a modification of the amino acid from K to E at position 12.
+The protein's natural variant, known as in J-Paris 1/J-Aljezur;, features a modification of the amino acid from A to D at position 13.
+The protein's natural variant, known as in Ravenscourt Park; causes alpha-thalassemia;, features a modification of the amino acid from A to P at position 14.
+The protein's natural variant, known as in Evanston; O(2) affinity up;, features a modification of the amino acid from W to R at position 15.
+The protein's natural variant, known as in Ottawa/Siam;, features a modification of the amino acid from G to R at position 16.
+The protein's natural variant, known as in Harbin; slightly unstable;, features a modification of the amino acid from K to M at position 17.
+The protein's natural variant, known as in Beijing;, features a modification of the amino acid from K to N at position 17.
+The protein's natural variant, known as in Al-Ain Abu Dhabi;, features a modification of the amino acid from G to D at position 19.
+The protein's natural variant, known as in Handsworth;, features a modification of the amino acid from G to R at position 19.
+The protein's natural variant, known as in J-Kurosh, features a modification of the amino acid from A to D at position 20.
+The protein's natural variant, known as in J-Tashikuergan;, features a modification of the amino acid from A to E at position 20.
+The protein's natural variant, known as in Le Lamentin;, features a modification of the amino acid from H to Q at position 21.
+The protein's natural variant, known as in Hobart;, features a modification of the amino acid from H to R at position 21.
+The protein's natural variant, known as in J-Nyanza;, features a modification of the amino acid from A to D at position 22.
+The protein's natural variant, known as in Fontainebleau;, features a modification of the amino acid from A to P at position 22.
+The protein's natural variant, known as in J-Medellin;, features a modification of the amino acid from G to D at position 23.
+The protein's natural variant, known as in Reims; slightly unstable;, features a modification of the amino acid from E to G at position 24.
+The protein's natural variant, known as in Chad;, features a modification of the amino acid from E to K at position 24.
+The protein's natural variant, known as in Luxembourg; unstable;, features a modification of the amino acid from Y to H at position 25.
+The protein's natural variant, known as in Shenyang; unstable;, features a modification of the amino acid from A to E at position 27.
+The protein's natural variant, known as in Campinas;, features a modification of the amino acid from A to V at position 27.
+The protein's natural variant, known as in Hekinan;, features a modification of the amino acid from E to D at position 28.
+The protein's natural variant, known as in Fort Worth;, features a modification of the amino acid from E to G at position 28.
+The protein's natural variant, known as in Spanish town;, features a modification of the amino acid from E to V at position 28.
+The protein's natural variant, known as in O-Padova;, features a modification of the amino acid from E to K at position 31.
+The protein's natural variant, known as causes alpha-thalassemia;, features a modification of the amino acid from R to K at position 32.
+The protein's natural variant, known as in Prato; unstable;, features a modification of the amino acid from R to S at position 32.
+The protein's natural variant, known as in Queens/Ogi;, features a modification of the amino acid from L to R at position 35.
+The protein's natural variant, known as in Catonsville, features a modification of the amino acid from P to PE at position 38.
+The protein's natural variant, known as in Bourmedes;, features a modification of the amino acid from P to R at position 38.
+The protein's natural variant, known as in Kanagawa; O(2) affinity up;, features a modification of the amino acid from K to M at position 41.
+The protein's natural variant, known as in Miyano; O(2) affinity up;, features a modification of the amino acid from T to S at position 42.
+The protein's natural variant, known as in Hirosaki; unstable;, features a modification of the amino acid from F to L at position 44.
+The protein's natural variant, known as in Milledgeville; O(2) affinity up;, features a modification of the amino acid from P to L at position 45.
+The protein's natural variant, known as in Kawachi; O(2) affinity up;, features a modification of the amino acid from P to R at position 45.
+The protein's natural variant, known as in Bari;, features a modification of the amino acid from H to Q at position 46.
+The protein's natural variant, known as in Fort de France; O(2) affinity up;, features a modification of the amino acid from H to R at position 46.
+The protein's natural variant, known as in Cordele; unstable;, features a modification of the amino acid from D to A at position 48.
+The protein's natural variant, known as in Kokura; also in Umi/Michigan; unstable;, features a modification of the amino acid from D to G at position 48.
+The protein's natural variant, known as in Hasharon/Sinai; unstable;, features a modification of the amino acid from D to H at position 48.
+The protein's natural variant, known as in Kurdistan;, features a modification of the amino acid from D to Y at position 48.
+The protein's natural variant, known as in Montgomery;, features a modification of the amino acid from L to R at position 49.
+The protein's natural variant, known as in Savaria;, features a modification of the amino acid from S to R at position 50.
+The protein's natural variant, known as in Aichi; slightly unstable;, features a modification of the amino acid from H to R at position 51.
+The protein's natural variant, known as in J-Abidjan;, features a modification of the amino acid from G to D at position 52.
+The protein's natural variant, known as in Russ;, features a modification of the amino acid from G to R at position 52.
+The protein's natural variant, known as in J-Rovigo; unstable;, features a modification of the amino acid from A to D at position 54.
+The protein's natural variant, known as in Hikoshima/Shimonoseki;, features a modification of the amino acid from Q to R at position 55.
+The protein's natural variant, known as in Port Huron;, features a modification of the amino acid from K to R at position 57.
+The protein's natural variant, known as in Thailand;, features a modification of the amino acid from K to T at position 57.
+The protein's natural variant, known as in L-Persian Gulf;, features a modification of the amino acid from G to R at position 58.
+The protein's natural variant, known as in Boghe;, features a modification of the amino acid from H to Q at position 59.
+The protein's natural variant, known as in M-Boston/M-Osaka; O(2) affinity down;, features a modification of the amino acid from H to Y at position 59.
+The protein's natural variant, known as in Adana; unstable; causes alpha-thalassemia;, features a modification of the amino acid from G to D at position 60.
+The protein's natural variant, known as in Tottori; unstable;, features a modification of the amino acid from G to V at position 60.
+The protein's natural variant, known as in Zambia;, features a modification of the amino acid from K to N at position 61.
+The protein's natural variant, known as in J-Buda;, features a modification of the amino acid from K to N at position 62.
+The protein's natural variant, known as in J-Anatolia;, features a modification of the amino acid from K to T at position 62.
+The protein's natural variant, known as in Evans; unstable;, features a modification of the amino acid from V to M at position 63.
+The protein's natural variant, known as in Pontoise; unstable;, features a modification of the amino acid from A to D at position 64.
+The protein's natural variant, known as in Persepolis;, features a modification of the amino acid from D to Y at position 65.
+The protein's natural variant, known as in G-Philadelphia;, features a modification of the amino acid from N to K at position 69.
+The protein's natural variant, known as in J-Habana;, features a modification of the amino acid from A to E at position 72.
+The protein's natural variant, known as in Ozieri;, features a modification of the amino acid from A to V at position 72.
+The protein's natural variant, known as in Daneskgah-Teheran;, features a modification of the amino acid from H to R at position 73.
+The protein's natural variant, known as in Lille;, features a modification of the amino acid from D to A at position 75.
+The protein's natural variant, known as in Chapel Hill;, features a modification of the amino acid from D to G at position 75.
+The protein's natural variant, known as in G-Pest;, features a modification of the amino acid from D to N at position 75.
+The protein's natural variant, known as in Duan;, features a modification of the amino acid from D to A at position 76.
+The protein's natural variant, known as in Q-Iran;, features a modification of the amino acid from D to H at position 76.
+The protein's natural variant, known as in Noko;, features a modification of the amino acid from M to K at position 77.
+The protein's natural variant, known as in Aztec;, features a modification of the amino acid from M to T at position 77.
+The protein's natural variant, known as in Guizhou;, features a modification of the amino acid from P to R at position 78.
+The protein's natural variant, known as in Davenport;, features a modification of the amino acid from N to H at position 79.
+The protein's natural variant, known as in Stanleyville-2;, features a modification of the amino acid from N to K at position 79.
+The protein's natural variant, known as in Singapore;, features a modification of the amino acid from A to G at position 80.
+The protein's natural variant, known as in Ann Arbor; unstable;, features a modification of the amino acid from L to R at position 81.
+The protein's natural variant, known as in Nigeria;, features a modification of the amino acid from S to C at position 82.
+The protein's natural variant, known as in Garden State;, features a modification of the amino acid from A to D at position 83.
+The protein's natural variant, known as in Etobicoke; O(2) affinity up;, features a modification of the amino acid from S to R at position 85.
+The protein's natural variant, known as in Inkster; O(2) affinity up;, features a modification of the amino acid from D to V at position 86.
+The protein's natural variant, known as in Atago; O(2) affinity up;, features a modification of the amino acid from D to Y at position 86.
+The protein's natural variant, known as in Moabit; unstable;, features a modification of the amino acid from L to R at position 87.
+The protein's natural variant, known as in Auckland; unstable;, features a modification of the amino acid from H to N at position 88.
+The protein's natural variant, known as in Iwata; unstable;, features a modification of the amino acid from H to R at position 88.
+The protein's natural variant, known as in Loire; O(2) affinity up;, features a modification of the amino acid from A to S at position 89.
+The protein's natural variant, known as in Handa; O(2) affinity up;, features a modification of the amino acid from K to M at position 91.
+The protein's natural variant, known as in Port Phillip; unstable;, features a modification of the amino acid from L to P at position 92.
+The protein's natural variant, known as in J-Cape Town; O(2) affinity up;, features a modification of the amino acid from R to Q at position 93.
+The protein's natural variant, known as in Cemenelum; O(2) affinity up;, features a modification of the amino acid from R to W at position 93.
+The protein's natural variant, known as in Bassett; markedly reduced oxygen affinity;, features a modification of the amino acid from D to A at position 95.
+The protein's natural variant, known as in Setif; unstable;, features a modification of the amino acid from D to Y at position 95.
+The protein's natural variant, known as in Denmark Hill; O(2) affinity up;, features a modification of the amino acid from P to A at position 96.
+The protein's natural variant, known as in Godavari; O(2) affinity up;, features a modification of the amino acid from P to T at position 96.
+The protein's natural variant, known as in Dallas; O(2) affinity up;, features a modification of the amino acid from N to K at position 98.
+The protein's natural variant, known as in Turriff;, features a modification of the amino acid from K to E at position 100.
+The protein's natural variant, known as in Manitoba; slightly unstable;, features a modification of the amino acid from S to R at position 103.
+The protein's natural variant, known as in Contaldo; unstable;, features a modification of the amino acid from H to R at position 104.
+The protein's natural variant, known as in Charolles;, features a modification of the amino acid from H to Y at position 104.
+The protein's natural variant, known as in Suan-Dok; unstable; causes alpha-thalassemia;, features a modification of the amino acid from L to R at position 110.
+The protein's natural variant, known as in Petah Tikva; unstable; causes alpha-thalassemia;, features a modification of the amino acid from A to D at position 111.
+The protein's natural variant, known as in Hopkins-II; unstable;, features a modification of the amino acid from H to D at position 113.
+The protein's natural variant, known as in Twin Peaks;, features a modification of the amino acid from L to H at position 114.
+The protein's natural variant, known as in Nouakchott;, features a modification of the amino acid from P to L at position 115.
+The protein's natural variant, known as in Chiapas;, features a modification of the amino acid from P to R at position 115.
+The protein's natural variant, known as in Melusine;, features a modification of the amino acid from P to S at position 115.
+The protein's natural variant, known as in J-Tongariki;, features a modification of the amino acid from A to D at position 116.
+The protein's natural variant, known as in Ube-4;, features a modification of the amino acid from E to A at position 117.
+The protein's natural variant, known as in Zaire, features a modification of the amino acid from E to EHLPAE at position 117.
+The protein's natural variant, known as in Phnom Penh, features a modification of the amino acid from F to FI at position 118.
+The protein's natural variant, known as in Grady, features a modification of the amino acid from T to TEFT at position 119.
+The protein's natural variant, known as in J-Meerut/J-Birmingham;, features a modification of the amino acid from A to E at position 121.
+The protein's natural variant, known as in Owari;, features a modification of the amino acid from V to M at position 122.
+The protein's natural variant, known as in Westmead;, features a modification of the amino acid from H to Q at position 123.
+The protein's natural variant, known as in Quong Sze; causes alpha-thalassemia;, features a modification of the amino acid from L to P at position 126.
+The protein's natural variant, known as in Plasencia; family with moderate microcytosis and hypochromia;, features a modification of the amino acid from L to R at position 126.
+The protein's natural variant, known as in West One;, features a modification of the amino acid from D to G at position 127.
+The protein's natural variant, known as in Fukutomi; O(2) affinity up;, features a modification of the amino acid from D to V at position 127.
+The protein's natural variant, known as in Montefiore; O(2) affinity up;, features a modification of the amino acid from D to Y at position 127.
+The protein's natural variant, known as in Jackson;, features a modification of the amino acid from K to N at position 128.
+The protein's natural variant, known as in Tunis-Bizerte; unstable; causes alpha-thalassemia;, features a modification of the amino acid from L to P at position 130.
+The protein's natural variant, known as in Yuda; O(2) affinity down;, features a modification of the amino acid from A to D at position 131.
+The protein's natural variant, known as in Sun Prairie; unstable;, features a modification of the amino acid from A to P at position 131.
+The protein's natural variant, known as in Questembert; highly unstable; causes alpha-thalassemia;, features a modification of the amino acid from S to P at position 132.
+The protein's natural variant, known as in Val de Marne; O(2) affinity up;, features a modification of the amino acid from S to R at position 134.
+The protein's natural variant, known as in Pavie;, features a modification of the amino acid from V to E at position 136.
+The protein's natural variant, known as in Chicago;, features a modification of the amino acid from L to M at position 137.
+The protein's natural variant, known as in Bibba; unstable; causes alpha-thalassemia;, features a modification of the amino acid from L to P at position 137.
+The protein's natural variant, known as in Toyama;, features a modification of the amino acid from L to R at position 137.
+The protein's natural variant, known as in Attleboro; O(2) affinity up;, features a modification of the amino acid from S to P at position 139.
+The protein's natural variant, known as in Hanamaki; O(2) affinity up;, features a modification of the amino acid from K to E at position 140.
+The protein's natural variant, known as in Tokoname; O(2) affinity up;, features a modification of the amino acid from K to T at position 140.
+The protein's natural variant, known as in Rouen/Ethiopia; O(2) affinity up;, features a modification of the amino acid from Y to H at position 141.
+The protein's natural variant, known as in Nunobiki; O(2) affinity up;, features a modification of the amino acid from R to C at position 142.
+The protein's natural variant, known as in Suresnes; O(2) affinity up;, features a modification of the amino acid from R to H at position 142.
+The protein's natural variant, known as in Legnano; O(2) affinity up;, features a modification of the amino acid from R to L at position 142.
+The protein's natural variant, known as in Singapore;, features a modification of the amino acid from R to P at position 142.
+The protein's natural variant, known as in RPA; loss of ability to bind 11-cis-retinaldehyde;, features a modification of the amino acid from R to Q at position 151.
+The protein's natural variant, known as in RPA;, features a modification of the amino acid from M to K at position 226.
+The protein's natural variant, known as in BRD;, features a modification of the amino acid from R to W at position 234.
+The protein's natural variant, known as in PMGEDSV; does not affect interaction with ADGRG1;, features a modification of the amino acid from P to A at position 49.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to C at position 183.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to D at position 183.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to S at position 183.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to V at position 192.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to R at position 201.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to D at position 204.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to S at position 204.
+The protein's natural variant, known as in EDSVASC, features a modification of the amino acid from G to D at position 210.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to C at position 219.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to V at position 225.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to E at position 228.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to R at position 240.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to V at position 243.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to D at position 249.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to V at position 249.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to D at position 252.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to R at position 252.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to V at position 252.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to V at position 255.
+The protein's natural variant, known as in EDSVASC, features a modification of the amino acid from G to R at position 264.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to V at position 267.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to R at position 297.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to R at position 303.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to V at position 321.
+The protein's natural variant, known as in EDSVASC, features a modification of the amino acid from G to D at position 327.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to R at position 345.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to R at position 417.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from G to S at position 420.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to R at position 444.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to E at position 489.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to R at position 501.
+The protein's natural variant, known as in EDSVASC, features a modification of the amino acid from G to V at position 519.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to R at position 540.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to E at position 549.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to E at position 552.
+The protein's natural variant, known as in EDSVASC, features a modification of the amino acid from G to E at position 567.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to S at position 582.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to D at position 588.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to R at position 636.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to E at position 657.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to D at position 660.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to D at position 666.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to R at position 699.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to R at position 726.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to S at position 738.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to V at position 738.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to V at position 744.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to E at position 756.
+The protein's natural variant, known as in EDSVASC, features a modification of the amino acid from G to C at position 762.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to R at position 786.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to S at position 804.
+The protein's natural variant, known as in EDSVASC, features a modification of the amino acid from G to R at position 828.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to W at position 828.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to C at position 852.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to V at position 879.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to D at position 882.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to D at position 900.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to E at position 903.
+The protein's natural variant, known as in EDSVASC, features a modification of the amino acid from G to D at position 909.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to V at position 909.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to E at position 918.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to C at position 924.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to R at position 936.
+The protein's natural variant, known as in EDSVASC, features a modification of the amino acid from G to S at position 936.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to D at position 939.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to E at position 942.
+The protein's natural variant, known as in EDSVASC; severe variant;, features a modification of the amino acid from G to S at position 957.
+The protein's natural variant, known as in EDSVASC; severe variant;, features a modification of the amino acid from G to V at position 960.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to V at position 966.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to A at position 972.
+The protein's natural variant, known as in EDSVASC; requires 2 nucleotide substitutions;, features a modification of the amino acid from G to T at position 984.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to E at position 996.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to R at position 999.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to E at position 1011.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to E at position 1014.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to V at position 1032.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to C at position 1035.
+The protein's natural variant, known as in EDSVASC, features a modification of the amino acid from G to D at position 1044.
+The protein's natural variant, known as in EDSVASC; mild variant;, features a modification of the amino acid from G to D at position 1050.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to V at position 1050.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to V at position 1071.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to V at position 1077.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to D at position 1089.
+The protein's natural variant, known as in EDSVASC, features a modification of the amino acid from G to D at position 1098.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to V at position 1098.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to E at position 1101.
+The protein's natural variant, known as in EDSVASC, features a modification of the amino acid from G to A at position 1104.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to V at position 1161.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to E at position 1164.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to R at position 1164.
+The protein's natural variant, known as in spondyloepiphyseal dysplasia, features a modification of the amino acid from G to S at position 1164.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to V at position 1167.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to D at position 1170.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to V at position 1170.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to E at position 1173.
+The protein's natural variant, known as in EDSVASC; Gottron type acrogeria;, features a modification of the amino acid from G to R at position 1173.
+The protein's natural variant, known as in EDSVASC; severe, features a modification of the amino acid from G to V at position 1176.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to R at position 1179.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to E at position 1182.
+The protein's natural variant, known as in EDSVASC; severe variant;, features a modification of the amino acid from G to D at position 1185.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to V at position 1185.
+The protein's natural variant, known as in EDSVASC; severe variant;, features a modification of the amino acid from G to E at position 1188.
+The protein's natural variant, known as in EDSVASC;, features a modification of the amino acid from G to R at position 1188.
+The protein's natural variant, known as in PMGEDSV;, features a modification of the amino acid from G to E at position 1284.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to C at position 1434.
+The protein's natural variant, known as found in patients with ulcerative colitis; loss of alpha-(1,3)-fucosyltransferase activity;, features a modification of the amino acid from R to Q at position 110.
+The protein's natural variant, known as in strain: CB4857, features a modification of the amino acid from E to D at position 47.
+The protein's natural variant, known as in strain: CB4855, features a modification of the amino acid from S to P at position 155.
+The protein's natural variant, known as in strain: CB4855, features a modification of the amino acid from T to P at position 165.
+The protein's natural variant, known as in strain: DBY939, features a modification of the amino acid from L to P at position 16.
+The protein's natural variant, known as in strain: DBY939 and SEY6210, features a modification of the amino acid from R to S at position 23.
+The protein's natural variant, known as in strain: DBY939, features a modification of the amino acid from T to S at position 321.
+The protein's natural variant, known as in strain: DBY939, features a modification of the amino acid from S to A at position 399.
+The protein's natural variant, known as in strain: DBY939, features a modification of the amino acid from PI to SL at position 434.
+The protein's natural variant, known as in strain: DBY939, features a modification of the amino acid from T to K at position 461.
+The protein's natural variant, known as in LDAMD; results in impaired regulation of actin polymerization;, features a modification of the amino acid from R to W at position 204.
+The natural variant of this protein is characterized by an amino acid alteration from L to P at position 425.
+The protein's natural variant, known as in OPTB1, features a modification of the amino acid from A to P at position 141.
+The protein's natural variant, known as in OPTB1;, features a modification of the amino acid from G to R at position 405.
+The protein's natural variant, known as in OPTB1;, features a modification of the amino acid from R to L at position 444.
+The protein's natural variant, known as in OPTB1;, features a modification of the amino acid from D to N at position 517.
+The protein's natural variant, known as in OPTB1, features a modification of the amino acid from P to R at position 775.
+The protein's natural variant, known as in DWOPNED; unknown pathological significance, features a modification of the amino acid from L to P at position 119.
+The protein's natural variant, known as in DWOPNED, features a modification of the amino acid from C to R at position 816.
+The protein's natural variant, known as in DWOPNED; unknown pathological significance, features a modification of the amino acid from R to W at position 881.
+The protein's natural variant, known as in DWOPNED; unknown pathological significance, features a modification of the amino acid from R to H at position 1077.
+The protein's natural variant, known as found in a patient with an autosomal dominant neurodevelopmental disorder; unknown pathological significance;, features a modification of the amino acid from R to Q at position 1185.
+The protein's natural variant, known as found in a patient with an autosomal dominant neurodevelopmental disorder; unknown pathological significance;, features a modification of the amino acid from R to W at position 1495.
+The protein's natural variant, known as probable disease-associated variant found in a patient with an autosomal dominant neurodevelopmental disorder;, features a modification of the amino acid from R to C at position 1748.
+The protein's natural variant, known as in strain: Isolate Y6, features a modification of the amino acid from H to R at position 313.
+The protein's natural variant, known as in strain: Isolate Y6, features a modification of the amino acid from R to W at position 318.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from D to H at position 195.
+The protein's natural variant, known as in strain: ATCC 6633, features a modification of the amino acid from S to I at position 4.
+The protein's natural variant, known as in strain: ATCC 6633, features a modification of the amino acid from Q to H at position 21.
+The protein's natural variant, known as in strain: ATCC 6633, features a modification of the amino acid from I to T at position 47.
+The protein's natural variant, known as in strain: ATCC 6633, features a modification of the amino acid from K to N at position 54.
+The protein's natural variant, known as in strain: ATCC 6633, features a modification of the amino acid from N to D at position 70.
+The protein's natural variant, known as in MTDPS6; unknown pathological significance;, features a modification of the amino acid from L to R at position 21.
+The protein's natural variant, known as in MTDPS6; results in altered ribonucleotide incorporation in mtDNA from patient fibroblasts, features a modification of the amino acid from A to P at position 23.
+The protein's natural variant, known as in MTDPS6; unknown pathological significance;, features a modification of the amino acid from G to W at position 24.
+The protein's natural variant, known as in MTDPS6; unknown pathological significance;, features a modification of the amino acid from Q to P at position 36.
+The protein's natural variant, known as in CMT2EE;, features a modification of the amino acid from R to Q at position 41.
+The protein's natural variant, known as in MTDPS6;, features a modification of the amino acid from R to W at position 41.
+The protein's natural variant, known as in MTDPS6; does not completely rescue iridophores loss in zebrafish 'tra' mutants; may cause protein instability and decay;, features a modification of the amino acid from R to Q at position 50.
+The protein's natural variant, known as in MTDPS6;, features a modification of the amino acid from R to W at position 50.
+The protein's natural variant, known as in MTDPS6;, features a modification of the amino acid from P to R at position 64.
+The protein's natural variant, known as in MTDPS6; unknown pathological significance, features a modification of the amino acid from V to E at position 66.
+The protein's natural variant, known as in MTDPS6;, features a modification of the amino acid from K to E at position 88.
+The protein's natural variant, known as in MTDPS6, features a modification of the amino acid from D to G at position 92.
+The protein's natural variant, known as in MTDPS6; results in altered ribonucleotide incorporation in mtDNA from patient fibroblasts, features a modification of the amino acid from Q to P at position 93.
+The protein's natural variant, known as in MTDPS6;, features a modification of the amino acid from G to R at position 94.
+The protein's natural variant, known as in MTDPS6; unknown pathological significance;, features a modification of the amino acid from G to D at position 95.
+The protein's natural variant, known as in MTDPS6 and CMT2EE; results in incomplete closing of the channel;, features a modification of the amino acid from P to L at position 98.
+The protein's natural variant, known as in MTDPS6;, features a modification of the amino acid from R to M at position 154.
+The protein's natural variant, known as in MTDPS6;, features a modification of the amino acid from A to D at position 162.
+The protein's natural variant, known as in MTDPS6;, features a modification of the amino acid from N to K at position 166.
+The protein's natural variant, known as in MTDPS6;, features a modification of the amino acid from S to F at position 170.
+The protein's natural variant, known as in MPMCD; less stable than the wild-type protein within the mitochondria, increased rate of dissociation of FAD by about 45-fold;, features a modification of the amino acid from R to H at position 194.
+The protein's natural variant, known as in HYPOC2;, features a modification of the amino acid from R to C at position 60.
+The protein's natural variant, known as in HHC2; induces a decrease in sensitivity to changes in extracellular calcium concentrations;, features a modification of the amino acid from L to Q at position 135.
+The protein's natural variant, known as in HYPOC2; induces an increase in sensitivity to changes in extracellular calcium concentrations;, features a modification of the amino acid from R to Q at position 181.
+The protein's natural variant, known as in HYPOC2;, features a modification of the amino acid from S to W at position 211.
+The protein's natural variant, known as in HYPOC2; induces an increase in sensitivity to changes in extracellular calcium concentrations;, features a modification of the amino acid from F to L at position 341.
+The protein's natural variant, known as in L10A/B, features a modification of the amino acid from I to V at position 148.
+The protein's natural variant, known as in L10A/B, features a modification of the amino acid from H to Y at position 232.
+The protein's natural variant, known as in HSAN1A; inactive in the heterodimeric SPT complex; largely reduced activity with serine as substrate, but nearly no effect on serine affinity in the heterotrimeric SPT complex; in contrast to wild-type is able to use alanine as substrate leading to the formation of 1-deoxysphinganine (1-deoxySa); does not interfere with SPT complex formation;, features a modification of the amino acid from C to W at position 133.
+The protein's natural variant, known as in HSAN1A; reduced activity; does not interfere with SPT complex formation;, features a modification of the amino acid from C to Y at position 133.
+The protein's natural variant, known as in HSAN1A; present with both painful and painles phenotypes; reduced activity; does not interfere with SPT complex formation;, features a modification of the amino acid from V to D at position 144.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from R to W at position 239.
+The protein's natural variant, known as found in a patient with HSAN1A; uncertain pathological significance;, features a modification of the amino acid from A to G at position 310.
+The protein's natural variant, known as in HSAN1A; severe form with early onset; reduced activity;, features a modification of the amino acid from S to F at position 331.
+The protein's natural variant, known as probable disease-associated variant found in severe HMSN; reduced activity;, features a modification of the amino acid from S to Y at position 331.
+The protein's natural variant, known as in HSAN1A; reduced activity;, features a modification of the amino acid from A to V at position 352.
+The protein's natural variant, known as does not affect activity; does not interfere with SPT complex formation;, features a modification of the amino acid from G to A at position 387.
+The protein's natural variant, known as in strain: Guyane 11, features a modification of the amino acid from T to A at position 394.
+The protein's natural variant, known as in strain: DSR 3 and DSR 4, features a modification of the amino acid from E to K at position 22.
+The protein's natural variant, known as in strain: DSR 4, features a modification of the amino acid from I to M at position 84.
+The protein's natural variant, known as in strain: DSR 4, features a modification of the amino acid from G to C at position 95.
+The protein's natural variant, known as in strain: DSR 4, features a modification of the amino acid from V to A at position 122.
+The protein's natural variant, known as in strain: DSR 4, features a modification of the amino acid from D to N at position 306.
+The protein's natural variant, known as in strain: DSR 4, features a modification of the amino acid from N to T at position 320.
+The protein's natural variant, known as in strain: DSR 4, features a modification of the amino acid from T to S at position 383.
+The protein's natural variant, known as in strain: DSR 4, features a modification of the amino acid from AVD to SVE at position 552.
+The protein's natural variant, known as in strain: DSR 4, features a modification of the amino acid from L to M at position 593.
+The natural variant of this protein is characterized by an amino acid alteration from C to S at position 430.
+The natural variant of this protein is characterized by an amino acid alteration from A to V at position 790.
+The protein's natural variant, known as in MYPBB; loss of interaction with CACNA1S;, features a modification of the amino acid from W to S at position 284.
+The protein's natural variant, known as may be associated with type 2 diabetes obese individuals;, features a modification of the amino acid from T to M at position 79.
+The protein's natural variant, known as in NTD; unknown pathological significance;, features a modification of the amino acid from R to H at position 349.
+The protein's natural variant, known as in NTD; reduces interaction with PRKCA, disrupts tight junction formation in epithelial cells;, features a modification of the amino acid from D to G at position 783.
+The protein's natural variant, known as in NTD; reduces interaction with PRKCA; increases phosphorylation; disrupts tight junction formation in epithelial cells;, features a modification of the amino acid from P to Q at position 913.
+The protein's natural variant, known as in strain: C57BL/6J, features a modification of the amino acid from Y to H at position 366.
+The protein's natural variant, known as seems to contribute to the development of type II diabetes; 50% reduction in activity;, features a modification of the amino acid from R to W at position 140.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from D to G at position 415.
+The natural variant of this protein is characterized by an amino acid alteration from F to S at position 704.
+The protein's natural variant, known as found as a heterozygous variant in a patient with non-syndromic hearing impairment; unknown pathological significance;, features a modification of the amino acid from R to W at position 90.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from I to V at position 240.
+The protein's natural variant, known as in BBS19; loss-of-function mutation; results in significantly reduced protein levels;, features a modification of the amino acid from C to Y at position 100.
+The protein's natural variant, known as in strain: Seychelles-1 and Seychelles-15, features a modification of the amino acid from P to T at position 143.
+The protein's natural variant, known as in strain: Seychelles-12, features a modification of the amino acid from F to S at position 152.
+The protein's natural variant, known as in strain: Seychelles-7 and Seychelles-8, features a modification of the amino acid from W to L at position 293.
+The protein's natural variant, known as in strain: Seychelles-8 and Seychelles-10, features a modification of the amino acid from F to S at position 423.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from E to V at position 681.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from N to T at position 685.
+The protein's natural variant, known as in strain: CWL029 and TW-183, features a modification of the amino acid from R to K at position 279.
+The protein's natural variant, known as associated with P haplotype, features a modification of the amino acid from P to L at position 112.
+The protein's natural variant, known as associated with P haplotype, features a modification of the amino acid from V to I at position 211.
+The protein's natural variant, known as in SYNS3; expressed and secreted as efficiently as wild-type; however it induces compromised chondrocyte proliferation and differentiation accompanied by enhanced osteogenic differentiation and matrix mineralization of bone marrow-derived mesenchymal stem cells;, features a modification of the amino acid from S to N at position 99.
+The protein's natural variant, known as associated with a markedly reduced risk of acute coronary artery disease; associated with higher risk of developing ARMD12; chemotaxis of monocytes of individuals with homozygous Ile-249 and Met-280 genotypes is impaired in the presence of bound CX3CR1 protein;, features a modification of the amino acid from V to I at position 249.
+The protein's natural variant, known as associated with higher risk of developing ARMD12; impaired antifungal innate immune response; chemotaxis of monocytes of individuals with homozygous Met-280 and Ile-249 genotypes is impaired in the presence of bound CX3CR1 protein;, features a modification of the amino acid from T to M at position 280.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from E to K at position 170.
+The protein's natural variant, known as found in a family with early-onset autosomal recessive parkinsonism and intellectual disability; unknown pathological significance; does not affect protein abundance; does not affect expression at the cell surface;, features a modification of the amino acid from G to S at position 279.
+The protein's natural variant, known as in neurotoxin-1', features a modification of the amino acid from V to I at position 36.
+The protein's natural variant, known as in MANDP1;, features a modification of the amino acid from F to S at position 74.
+The protein's natural variant, known as in SEMDM; abnormal intracellular autoactivation and autodegradation within the ER/Golgi resulting in the secretion of small and inactive fragments;, features a modification of the amino acid from F to S at position 75.
+The protein's natural variant, known as in MANDP1;, features a modification of the amino acid from M to T at position 91.
+The protein's natural variant, known as in MDST;, features a modification of the amino acid from W to G at position 207.
+The protein's natural variant, known as in MANDP1;, features a modification of the amino acid from H to N at position 232.
+The protein's natural variant, known as may be associated with siamese coat color, features a modification of the amino acid from G to W at position 227.
+The protein's natural variant, known as may be associated with burmese coat color, features a modification of the amino acid from G to R at position 302.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 99.
+The protein's natural variant, known as in NOCGUS, features a modification of the amino acid from T to I at position 115.
+The protein's natural variant, known as in NOCGUS; no effect on interaction with PACS1 and PACS2; does not affect homodimerization, features a modification of the amino acid from S to F at position 119.
+The protein's natural variant, known as in NOCGUS, features a modification of the amino acid from S to Y at position 119.
+The protein's natural variant, known as in NOCGUS; no effect on interaction with PACS1 and PACS2; does not affect homodimerization, features a modification of the amino acid from T to I at position 125.
+The protein's natural variant, known as in NOCGUS; no effect on interaction with PACS1 and PACS2; does not affect homodimerization, features a modification of the amino acid from S to C at position 129.
+The protein's natural variant, known as in NOCGUS; no effect on interaction with PACS1 and PACS2; does not affect homodimerization, features a modification of the amino acid from T to I at position 130.
+The protein's natural variant, known as in NOCGUS; loss of interaction with PACS1 and PACS2; does not affect homodimerization; does not affect subcellular location to cytoplasm, features a modification of the amino acid from D to G at position 220.
+The protein's natural variant, known as in NOCGUS; unknown pathological significance; no effect on interaction with PACS1 and PACS2; does not affect homodimerization; does not affect subcellular location to cytoplasm, features a modification of the amino acid from P to H at position 257.
+The protein's natural variant, known as in NOCGUS; no effect on interaction with PACS1 and PACS2; does not affect homodimerization; does not affect subcellular location to cytoplasm, features a modification of the amino acid from D to N at position 260.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from A to E at position 586.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from G to S at position 622.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from V to M at position 1264.
+The natural variant of this protein is characterized by an amino acid alteration from R to Q at position 85.
+The natural variant of this protein is characterized by an amino acid alteration from N to D at position 168.
+The protein's natural variant, known as in CMS24; unknown pathological significance;, features a modification of the amino acid from Y to C at position 203.
+The natural variant of this protein is characterized by an amino acid alteration from L to P at position 211.
+The protein's natural variant, known as in CMS24; unknown pathological significance;, features a modification of the amino acid from R to H at position 1517.
+The protein's natural variant, known as in CMS24; unknown pathological significance;, features a modification of the amino acid from D to G at position 1698.
+The protein's natural variant, known as in CMS24; unknown pathological significance, features a modification of the amino acid from G to E at position 2282.
+The protein's natural variant, known as in CMS24; unknown pathological significance;, features a modification of the amino acid from R to H at position 2283.
+The protein's natural variant, known as likely benign variant; no effect on localization at the plasma membrane; no change in calcium ion import across plasma membrane;, features a modification of the amino acid from A to S at position 18.
+The protein's natural variant, known as in HRPTTN; decreased localization at the plasma membrane; loss of calcium ion import across plasma membrane;, features a modification of the amino acid from C to Y at position 212.
+The protein's natural variant, known as in HRPTTN; decreased localization at the plasma membrane; no change in calcium ion import across plasma membrane;, features a modification of the amino acid from I to T at position 223.
+The protein's natural variant, known as in HRPTTN; decreased localization at the plasma membrane; loss of calcium ion import across plasma membrane;, features a modification of the amino acid from R to Q at position 425.
+The protein's natural variant, known as in HRPTTN; decreased localization at the plasma membrane; loss of calcium ion import across plasma membrane;, features a modification of the amino acid from G to R at position 428.
+The protein's natural variant, known as in HRPTTN; induces cell death most likely through intracellular calcium overload; increased calcium ion import across plasma membrane; may lack intracellular calcium-dependent inactivation, features a modification of the amino acid from G to E at position 451.
+The protein's natural variant, known as in HRPTTN; decreased localization at the plasma membrane; loss of calcium ion import across plasma membrane;, features a modification of the amino acid from R to W at position 483.
+The protein's natural variant, known as in DEE71;, features a modification of the amino acid from R to K at position 272.
+The protein's natural variant, known as in GDPAG; loss of enzyme activity;, features a modification of the amino acid from P to L at position 313.
+The protein's natural variant, known as in CASGID; increased enzyme activity;, features a modification of the amino acid from S to C at position 482.
+The protein's natural variant, known as in strain: cv. Conference and cv. Pyrodwarf, features a modification of the amino acid from R to K at position 93.
+The protein's natural variant, known as in strain: cv. Conference and cv. Pyrodwarf, features a modification of the amino acid from S to G at position 347.
+The protein's natural variant, known as in components B and C, features a modification of the amino acid from D to K at position 6.
+The natural variant of this protein is characterized by an amino acid alteration from Q to S at position 10.
+The protein's natural variant, known as in components B and C, features a modification of the amino acid from E to G at position 24.
+The natural variant of this protein is characterized by an amino acid alteration from S to T at position 34.
+The protein's natural variant, known as in component C, features a modification of the amino acid from H to Q at position 37.
+The natural variant of this protein is characterized by an amino acid alteration from M to L at position 47.
+The protein's natural variant, known as in components B and C, features a modification of the amino acid from F to Y at position 49.
+The protein's natural variant, known as in components B and C, features a modification of the amino acid from D to N at position 59.
+The protein's natural variant, known as in components B and C, features a modification of the amino acid from S to N at position 63.
+The protein's natural variant, known as in components B and C, features a modification of the amino acid from S to Y at position 63.
+The protein's natural variant, known as in strain: JR-341, features a modification of the amino acid from A to T at position 4.
+The protein's natural variant, known as in strain: JR-142 and JR-460, features a modification of the amino acid from L to W at position 10.
+The protein's natural variant, known as in strain: GB-8 and JR-50, features a modification of the amino acid from S to F at position 18.
+The protein's natural variant, known as in strain: GB-115, GB-336, JR-38, JR-106, JR-198 and JR-382, features a modification of the amino acid from A to V at position 23.
+The protein's natural variant, known as in strain: GB-336, features a modification of the amino acid from D to Y at position 24.
+The protein's natural variant, known as in strain: GB-4, JR-126 and JR-460, features a modification of the amino acid from L to M at position 26.
+The protein's natural variant, known as in strain: JR-198 and JR-460, features a modification of the amino acid from L to T at position 83.
+The protein's natural variant, known as in strain: JR-50, features a modification of the amino acid from G to E at position 93.
+The protein's natural variant, known as in strain: GB-115, JR-50, JR-106, JR-126, JR-142, JR-198, JR-341 and JR-382, features a modification of the amino acid from K to R at position 110.
+The protein's natural variant, known as in strain: JR-32, features a modification of the amino acid from IS to RG at position 155.
+The protein's natural variant, known as in strain: JR-126, features a modification of the amino acid from S to T at position 155.
+The protein's natural variant, known as in strain: GB-4, GB-139 and JR-38, features a modification of the amino acid from D to N at position 170.
+The protein's natural variant, known as in strain: JR-106, features a modification of the amino acid from L to F at position 171.
+The protein's natural variant, known as in strain: JR-126, features a modification of the amino acid from S to R at position 193.
+The protein's natural variant, known as in strain: JR-126, features a modification of the amino acid from G to A at position 211.
+The protein's natural variant, known as in strain: GB-4, GB-115 and JR-142, features a modification of the amino acid from L to V at position 225.
+The protein's natural variant, known as in strain: JR-38 and JR-382, features a modification of the amino acid from G to L at position 248.
+The protein's natural variant, known as in strain: GB-115, features a modification of the amino acid from R to G at position 285.
+The protein's natural variant, known as in strain: GB-4, features a modification of the amino acid from A to S at position 291.
+The protein's natural variant, known as in strain: GB-329, GB-336, JR-32 and JR-460, features a modification of the amino acid from S to T at position 313.
+The protein's natural variant, known as in strain: GB-329, GB-336, JR-32 and JR-460, features a modification of the amino acid from V to I at position 317.
+The protein's natural variant, known as in strain: GB-329 and JR-32, features a modification of the amino acid from A to S at position 326.
+The protein's natural variant, known as in strain: GB-336, JR-126 and JR-460, features a modification of the amino acid from Q to K at position 327.
+The protein's natural variant, known as in strain: JR-106, features a modification of the amino acid from Y to C at position 334.
+The protein's natural variant, known as in strain: JR-341, features a modification of the amino acid from D to Y at position 386.
+The protein's natural variant, known as in strain: GB-336, features a modification of the amino acid from D to E at position 444.
+The protein's natural variant, known as in strain: GB-336, JR-32, JR-50, JR-106 and JR-382, features a modification of the amino acid from I to M at position 474.
+The protein's natural variant, known as in strain: GB-329, features a modification of the amino acid from E to K at position 488.
+The protein's natural variant, known as in strain: GB-8, features a modification of the amino acid from I to V at position 491.
+The protein's natural variant, known as in strain: GB-336, JR-32, JR-50, JR-106 and JR-126, features a modification of the amino acid from T to A at position 514.
+The protein's natural variant, known as in strain: GB-139, GB-329, JR-142 and JR-460, features a modification of the amino acid from S to R at position 523.
+The protein's natural variant, known as in strain: JR-341, features a modification of the amino acid from T to S at position 532.
+The protein's natural variant, known as in strain: JR-50, features a modification of the amino acid from R to Q at position 533.
+The protein's natural variant, known as in CRSDA;, features a modification of the amino acid from P to R at position 221.
+The protein's natural variant, known as in CRSDA;, features a modification of the amino acid from S to C at position 245.
+The protein's natural variant, known as in CRSDA; renders the receptor unable to mediate the IL11 signal;, features a modification of the amino acid from R to W at position 296.
+The protein's natural variant, known as in CRSDA, features a modification of the amino acid from S to STWS at position 308.
+The protein's natural variant, known as modest increase in catalytic efficiency toward trimethylamine, methimazole, ethylenethiourea and sulindac, features a modification of the amino acid from E to D at position 24.
+The protein's natural variant, known as in TMAU;, features a modification of the amino acid from E to K at position 32.
+The protein's natural variant, known as in TMAU;, features a modification of the amino acid from A to T at position 52.
+The protein's natural variant, known as loss of activity, features a modification of the amino acid from N to K at position 61.
+The protein's natural variant, known as in TMAU; more than 90% reduction in catalytic efficiency toward trimethylamine, benzydamine and methyl p-tolyl sulfide;, features a modification of the amino acid from N to S at position 61.
+The protein's natural variant, known as in TMAU; loss of activity; affects FAD binding;, features a modification of the amino acid from M to I at position 66.
+The protein's natural variant, known as in TMAU; 90% reduction in catalytic efficiency toward trimethylamine and benzydamine; 34% reduction in catalytic efficiency toward methyl p-tolyl sulfide; nearly no effect on affinity for these substrates;, features a modification of the amino acid from P to L at position 153.
+The protein's natural variant, known as 35%, 45% and 71% increase in catalytic efficiency toward trimethylamine, benzydamine and methyl p-tolyl sulfide, respectively;, features a modification of the amino acid from E to K at position 158.
+The protein's natural variant, known as 65% increase in catalytic efficiency toward trimethylamine and 60% reduction toward benzydamine and methyl p-tolyl sulfide;, features a modification of the amino acid from V to M at position 257.
+The protein's natural variant, known as 16% reduction in catalytic efficiency toward trimethylamine and 40% increase toward benzydamine and methyl p-tolyl sulfide;, features a modification of the amino acid from E to G at position 308.
+The protein's natural variant, known as in TMAU;, features a modification of the amino acid from R to L at position 387.
+The protein's natural variant, known as 2-fold decrease in affinity for trimethylamine; 3-fold decrease in catalytic efficiency toward methimazole; 3-fold increase in catalytic efficiency toward sulindac; 30% increase in catalytic efficiency toward ethylenethiourea;, features a modification of the amino acid from K to N at position 416.
+The protein's natural variant, known as in TMAU; profoundly alters enzyme function;, features a modification of the amino acid from M to I at position 434.
+The protein's natural variant, known as in TMAU; loss of activity; affects FAD binding;, features a modification of the amino acid from R to W at position 492.
+The protein's natural variant, known as in ALS4; heterozygous; does not affect the interaction with EXOSC9 and UBE2I; does not decrease sumoylation;, features a modification of the amino acid from T to I at position 3.
+The protein's natural variant, known as in SCAN2;, features a modification of the amino acid from M to I at position 274.
+The protein's natural variant, known as in SCAN2;, features a modification of the amino acid from M to V at position 274.
+The protein's natural variant, known as in SCAN2; abolishes interaction with EXOSC9; does not abolish interaction with UBE2I; decreases sumoylation;, features a modification of the amino acid from W to C at position 305.
+The protein's natural variant, known as in SCAN2;, features a modification of the amino acid from I to K at position 331.
+The protein's natural variant, known as in SCAN2;, features a modification of the amino acid from R to W at position 332.
+The protein's natural variant, known as in ALS4; does not affect the interaction with EXOSC9 and UBE2I; does not decrease sumoylation and ubiquitination; does not inhibit homodimerization; unlike the wild-type protein the mutant induces interaction with C14orf178;, features a modification of the amino acid from L to S at position 389.
+The protein's natural variant, known as in SCAN2; abolishes interaction with EXOSC9; does not abolish interaction with UBE2I; decreases sumoylation;, features a modification of the amino acid from P to L at position 413.
+The protein's natural variant, known as in SCAN2;, features a modification of the amino acid from P to L at position 496.
+The protein's natural variant, known as in SCAN2; atypical; associated with K-653;, features a modification of the amino acid from N to D at position 603.
+The protein's natural variant, known as in SCAN2; atypical; associated with D-603;, features a modification of the amino acid from Q to K at position 653.
+The protein's natural variant, known as in SCAN2;, features a modification of the amino acid from R to C at position 1294.
+The protein's natural variant, known as in ALS4; likely benign variant;, features a modification of the amino acid from C to G at position 1554.
+The protein's natural variant, known as in SCAN2; heterozygous in a British family;, features a modification of the amino acid from F to S at position 1756.
+The protein's natural variant, known as in SCAN2;, features a modification of the amino acid from L to R at position 1976.
+The protein's natural variant, known as in ALS4;, features a modification of the amino acid from K to E at position 2029.
+The protein's natural variant, known as in ALS4;, features a modification of the amino acid from R to H at position 2136.
+The protein's natural variant, known as in SCAN2;, features a modification of the amino acid from P to L at position 2213.
+The protein's natural variant, known as in SCAN2;, features a modification of the amino acid from M to T at position 2229.
+The protein's natural variant, known as in SCAN2;, features a modification of the amino acid from P to R at position 2368.
+The protein's natural variant, known as in ALS4;, features a modification of the amino acid from I to T at position 2547.
+The protein's natural variant, known as in chylomicronemia syndrome; no lipase activity, features a modification of the amino acid from P to L at position 241.
+The protein's natural variant, known as found in a renal cell carcinoma case; somatic mutation, features a modification of the amino acid from N to T at position 141.
+The protein's natural variant, known as in strain: cv. C24, features a modification of the amino acid from D to N at position 95.
+The protein's natural variant, known as in strain: DSM 938, features a modification of the amino acid from H to D at position 62.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from A to T at position 464.
+The protein's natural variant, known as associated with resistance to anticancer indisulam; decreased interaction with the DCX(DCAF15) complex in presence of indisulam; abolished degradation by the DCX(DCAF15) complex in presence of indisulam, features a modification of the amino acid from M to L at position 265.
+The protein's natural variant, known as associated with resistance to anticancer indisulam, features a modification of the amino acid from G to E at position 268.
+The protein's natural variant, known as associated with resistance to anticancer indisulam; abolished degradation by the DCX(DCAF15) complex in presence of indisulam, features a modification of the amino acid from G to R at position 268.
+The protein's natural variant, known as associated with resistance to anticancer indisulam; decreased interaction with the DCX(DCAF15) complex in presence of indisulam; abolished degradation by the DCX(DCAF15) complex in presence of indisulam, features a modification of the amino acid from G to V at position 268.
+The protein's natural variant, known as associated with resistance to anticancer indisulam; decreased interaction with the DCX(DCAF15) complex in presence of indisulam; abolished degradation by the DCX(DCAF15) complex in presence of indisulam, features a modification of the amino acid from G to W at position 268.
+The protein's natural variant, known as associated with resistance to anticancer indisulam, features a modification of the amino acid from E to G at position 271.
+The protein's natural variant, known as associated with resistance to anticancer indisulam; abolished degradation by the DCX(DCAF15) complex in presence of indisulam, features a modification of the amino acid from E to Q at position 271.
+The protein's natural variant, known as associated with resistance to anticancer indisulam; abolished degradation by the DCX(DCAF15) complex in presence of indisulam, features a modification of the amino acid from P to S at position 272.
+The protein's natural variant, known as in VCTRL; unknown pathological significance, features a modification of the amino acid from M to V at position 57.
+The protein's natural variant, known as in BLS2;, features a modification of the amino acid from R to Q at position 149.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation; no effect on secretion;, features a modification of the amino acid from T to M at position 86.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from P to L at position 29.
+The protein's natural variant, known as in IMD73B; unknown pathological significance; increased interaction with PAK1 compared to wild-type; potential gain-of-function variant, features a modification of the amino acid from P to H at position 34.
+The protein's natural variant, known as in IMD73A; dominant-negative mutant; binds GDP, but not GTP; inhibits oxidase activation and superoxide anion production in vitro;, features a modification of the amino acid from D to N at position 57.
+The protein's natural variant, known as in IMD73B; gain-of-function variant; exhibits impaired GAP-mediated GTP hydrolysis, resulting in sustained GTP association and prolonged RAC2-driven activation of downstream effectors; when transfected into cells, shows increased basal reactive oxygen species production following stimulation by PMA compared to cells transfected with wild-type; increased interaction with PAK1, compared to wild-type;, features a modification of the amino acid from E to K at position 62.
+The protein's natural variant, known as in IMD73B; unknown pathological significance; cells transfected with this variant show higher production of reactive oxygen species compared to wild-type; potential gain-of-function variant, features a modification of the amino acid from N to T at position 92.
+The protein's natural variant, known as in ICP1;, features a modification of the amino acid from N to T at position 45.
+The protein's natural variant, known as in BRIC1; compound heterozygote with Q-600; uncertain pathological significance; may be associated with ICP; reduces interaction with TMEM30A; has no effect on PC flippase activity;, features a modification of the amino acid from D to N at position 70.
+The protein's natural variant, known as in PFIC1; loss of PC flippase activity, features a modification of the amino acid from L to P at position 127.
+The protein's natural variant, known as in ICP1; unknown pathological significance;, features a modification of the amino acid from K to E at position 203.
+The protein's natural variant, known as in PFIC1;, features a modification of the amino acid from P to T at position 209.
+The protein's natural variant, known as in PFIC1;, features a modification of the amino acid from L to S at position 288.
+The protein's natural variant, known as in BRIC1;, features a modification of the amino acid from G to D at position 308.
+The protein's natural variant, known as in PFIC1; greatly reduced expression due to proteosomal degradation; abolishes interaction with TMEM30A;, features a modification of the amino acid from G to V at position 308.
+The protein's natural variant, known as in BRIC1; loss of PC flippase activity;, features a modification of the amino acid from I to F at position 344.
+The protein's natural variant, known as in PFIC1, features a modification of the amino acid from S to Y at position 403.
+The protein's natural variant, known as in PFIC1, features a modification of the amino acid from R to P at position 412.
+The protein's natural variant, known as in BRIC1, features a modification of the amino acid from S to Y at position 453.
+The protein's natural variant, known as in BRIC1, features a modification of the amino acid from D to G at position 454.
+The protein's natural variant, known as in PFIC1;, features a modification of the amino acid from T to M at position 456.
+The protein's natural variant, known as in PFIC1;, features a modification of the amino acid from Y to H at position 500.
+The protein's natural variant, known as in PFIC1, features a modification of the amino acid from H to L at position 535.
+The protein's natural variant, known as in PFIC1; greatly reduced expression due to proteosomal degradation; abolishes interaction with TMEM30A;, features a modification of the amino acid from D to N at position 554.
+The protein's natural variant, known as in BRIC1; compound heterozygote with N-70;, features a modification of the amino acid from R to Q at position 600.
+The protein's natural variant, known as in BRIC1;, features a modification of the amino acid from R to W at position 600.
+The protein's natural variant, known as in BRIC1;, features a modification of the amino acid from R to W at position 628.
+The protein's natural variant, known as in BRIC1 and PFIC1; common mutation; reduces interaction with TMEM30A;, features a modification of the amino acid from I to T at position 661.
+The protein's natural variant, known as in PFIC1;, features a modification of the amino acid from D to G at position 688.
+The protein's natural variant, known as in BRIC1;, features a modification of the amino acid from I to T at position 694.
+The protein's natural variant, known as in PFIC1;, features a modification of the amino acid from G to R at position 733.
+The protein's natural variant, known as in PFIC1;, features a modification of the amino acid from F to S at position 853.
+The protein's natural variant, known as in ICP1; reduces interaction with TMEM30A;, features a modification of the amino acid from R to C at position 867.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from A to V at position 886.
+The protein's natural variant, known as in PFIC1 and BRIC1;, features a modification of the amino acid from G to R at position 892.
+The protein's natural variant, known as in PFIC1, features a modification of the amino acid from S to I at position 1012.
+The protein's natural variant, known as in PFIC1; greatly reduces interaction with TMEM30A;, features a modification of the amino acid from G to R at position 1040.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from I to M at position 1178.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from E to K at position 605.
+The protein's natural variant, known as in CDG1N;, features a modification of the amino acid from R to C at position 67.
+The protein's natural variant, known as in CDG1N;, features a modification of the amino acid from K to E at position 152.
+The protein's natural variant, known as in CDG1N;, features a modification of the amino acid from E to K at position 298.
+The protein's natural variant, known as in HLD7;, features a modification of the amino acid from P to L at position 91.
+The protein's natural variant, known as in HLD7;, features a modification of the amino acid from W to C at position 310.
+The protein's natural variant, known as in HLD7;, features a modification of the amino acid from D to N at position 372.
+The protein's natural variant, known as in HLD7;, features a modification of the amino acid from A to G at position 387.
+The protein's natural variant, known as in HLD7;, features a modification of the amino acid from F to L at position 558.
+The protein's natural variant, known as in HLD7;, features a modification of the amino acid from S to R at position 602.
+The protein's natural variant, known as in HLD7;, features a modification of the amino acid from S to Y at position 636.
+The protein's natural variant, known as in HLD7;, features a modification of the amino acid from G to E at position 672.
+The protein's natural variant, known as in HLD7;, features a modification of the amino acid from C to Y at position 724.
+The protein's natural variant, known as in HLD7;, features a modification of the amino acid from N to I at position 775.
+The protein's natural variant, known as in HLD7, features a modification of the amino acid from I to T at position 804.
+The protein's natural variant, known as in HLD7;, features a modification of the amino acid from M to V at position 852.
+The protein's natural variant, known as in HLD7;, features a modification of the amino acid from I to N at position 897.
+The protein's natural variant, known as in WDRTS; unknown pathological significance;, features a modification of the amino acid from G to R at position 903.
+The protein's natural variant, known as in HLD7;, features a modification of the amino acid from R to C at position 1005.
+The protein's natural variant, known as in WDRTS; unknown pathological significance;, features a modification of the amino acid from R to Q at position 1069.
+The protein's natural variant, known as in WDRTS; unknown pathological significance;, features a modification of the amino acid from K to R at position 1131.
+The protein's natural variant, known as in HLD7, features a modification of the amino acid from T to TT at position 1247.
+The protein's natural variant, known as in HLD7;, features a modification of the amino acid from E to K at position 1261.
+The protein's natural variant, known as in WDRTS; unknown pathological significance;, features a modification of the amino acid from D to N at position 1292.
+The protein's natural variant, known as in WDRTS; unknown pathological significance;, features a modification of the amino acid from G to R at position 1335.
+The protein's natural variant, known as in allele DOA*01:03;, features a modification of the amino acid from L to V at position 99.
+The protein's natural variant, known as in allele DOA*01:02;, features a modification of the amino acid from R to C at position 105.
+The protein's natural variant, known as in lineages GB01, GB02, GB03, GB04 and GB05, features a modification of the amino acid from P to S at position 57.
+The protein's natural variant, known as in lineages GB01, GB02, GB03, GB04 and GB05, features a modification of the amino acid from I to M at position 89.
+The protein's natural variant, known as in lineages GB01, GB02, GB03, GB04, GB05, GB08, GB09, GB10, GB12, GB14 and GB17, features a modification of the amino acid from P to S at position 110.
+The protein's natural variant, known as in lineages GB01, GB02, GB03, GB04 and GB05, features a modification of the amino acid from I to V at position 123.
+The protein's natural variant, known as in lineages GB01, GB02, GB03 and GB05, features a modification of the amino acid from I to V at position 153.
+The protein's natural variant, known as in lineages GB01, GB02, GB03, GB04 and GB05, features a modification of the amino acid from A to T at position 236.
+The protein's natural variant, known as in lineages GB01, GB02, GB03, GB04 and GB05, features a modification of the amino acid from T to A at position 238.
+The protein's natural variant, known as in lineages GB01, GB02, GB03, GB04 and GB05, features a modification of the amino acid from T to I at position 257.
+The protein's natural variant, known as in lineages GB01, GB02, GB03, GB04 and GB05, features a modification of the amino acid from I to L at position 303.
+The protein's natural variant, known as in lineage GB01, features a modification of the amino acid from I to T at position 368.
+The protein's natural variant, known as in lineages GB10 and GB12, features a modification of the amino acid from N to S at position 375.
+The protein's natural variant, known as in ARCI13; decreased protein abundance;, features a modification of the amino acid from R to W at position 72.
+The protein's natural variant, known as in ARCI13; decreased protein abundance;, features a modification of the amino acid from I to T at position 200.
+The protein's natural variant, known as may be associated with susceptibility to monomelic amyotrophy;, features a modification of the amino acid from G to S at position 668.
+The protein's natural variant, known as in strain: YJM269, YJM270, YJM326 and YJM1129, features a modification of the amino acid from P to A at position 378.
+The protein's natural variant, known as in strain: YJM627, features a modification of the amino acid from M to I at position 423.
+The protein's natural variant, known as in strain: YJM269, YJM270, YJM326 and YJM1129, features a modification of the amino acid from P to S at position 424.
+The protein's natural variant, known as in strain: SK1, V1-09, YJM269, YJM270, YJM280, YJM320, YJM326, YJM339, YJM627, YJM789 and YJM1129, features a modification of the amino acid from T to A at position 426.
+The protein's natural variant, known as in strain: V1-09 and YJM627, features a modification of the amino acid from H to N at position 480.
+The protein's natural variant, known as in APS1;, features a modification of the amino acid from R to C at position 15.
+The protein's natural variant, known as in APS1; prevents homooligomerization; slightly alters subcellular localization; no effect on the transcriptional transactivation activity;, features a modification of the amino acid from R to L at position 15.
+The protein's natural variant, known as in APS1; prevents homooligomerization; slightly alters subcellular localization; no effect on the transcriptional transactivation activity;, features a modification of the amino acid from T to M at position 16.
+The protein's natural variant, known as in APS1; no effect on homooligomerization; no effect on subcellular localization; no effect on the transcriptional transactivation activity;, features a modification of the amino acid from A to V at position 21.
+The protein's natural variant, known as in APS1; abolishes association with cytoplasmic tubular structures and homodimerization; loss of doted nuclear localization; nuclear smear; severe decrease of transcriptional transactivation activity;, features a modification of the amino acid from L to P at position 28.
+The protein's natural variant, known as in APS1;, features a modification of the amino acid from L to P at position 29.
+The protein's natural variant, known as in APS1; loss of homooligomerization;, features a modification of the amino acid from F to S at position 77.
+The protein's natural variant, known as in APS1; loss of homooligomerization;, features a modification of the amino acid from W to R at position 78.
+The protein's natural variant, known as in APS1;, features a modification of the amino acid from V to L at position 80.
+The protein's natural variant, known as in APS1;, features a modification of the amino acid from K to E at position 83.
+The protein's natural variant, known as in APS1; no significant effect on transcriptional transactivation activity;, features a modification of the amino acid from Y to C at position 85.
+The protein's natural variant, known as in APS1; decreases doted nuclear localization;, features a modification of the amino acid from Y to C at position 90.
+The protein's natural variant, known as in APS1;, features a modification of the amino acid from L to R at position 93.
+The protein's natural variant, known as in APS1; changes the subcellular localization and in addition disrupts the transactivating capacity of the wild-type AIRE; acts with a dominant negative effect by binding to the wild-type AIRE thus preventing the protein from forming the complexes needed for transactivation;, features a modification of the amino acid from G to W at position 228.
+The protein's natural variant, known as in APS1; benign variant; does not affect transcriptional transactivation activity;, features a modification of the amino acid from P to L at position 252.
+The protein's natural variant, known as in APS1; no effect on protein structure or on interaction with histone H3; no effect on doted nuclear localization; dominant-negative effect on regulation of target gene transcription;, features a modification of the amino acid from V to M at position 301.
+The protein's natural variant, known as found in patients with hypothyroidism and organ- and cytokine-specific autoantibodies; no effect on doted nuclear localization; dominant-negative effect on regulation of target gene transcription, features a modification of the amino acid from C to Y at position 302.
+The protein's natural variant, known as found in a patient with pernicious anemia and neuropathy; unknown pathological significance; no effect on doted nuclear localization; dominant-negative effect on regulation of target gene transcription, features a modification of the amino acid from G to S at position 305.
+The protein's natural variant, known as in APS1; impairs zinc binding and folding of the PHD-type 1 zinc finger; dominant-negative effect on the regulation of target gene transcription; no effect on doted nuclear localization; dominant-negative effect on regulation of target gene transcription;, features a modification of the amino acid from C to Y at position 311.
+The protein's natural variant, known as unknown pathological significance; found in a patient with pernicious anemia;, features a modification of the amino acid from R to W at position 316.
+The protein's natural variant, known as in APS1; no significant effect on structure, but may alter protein interactions; no effect on doted nuclear localization; dominant-negative effect on regulation of target gene transcription;, features a modification of the amino acid from P to L at position 326.
+The protein's natural variant, known as in APS1; alters folding of the PHD-type 1 zinc finger;, features a modification of the amino acid from P to Q at position 326.
+The protein's natural variant, known as found in a patient with acrofacial vitiligo and gastric parietal cell autoantibodies; no effect on doted nuclear localization; dominant-negative effect on regulation of target gene transcription;, features a modification of the amino acid from R to Q at position 328.
+The protein's natural variant, known as found in a patient with acrofacial vitiligo and gastric parietal cell autoantibodies; unknown pathological significance;, features a modification of the amino acid from V to A at position 484.
+The protein's natural variant, known as in APS1;, features a modification of the amino acid from P to L at position 539.
+The protein's natural variant, known as in RP43;, features a modification of the amino acid from R to H at position 102.
+The protein's natural variant, known as in RP43;, features a modification of the amino acid from R to S at position 102.
+The protein's natural variant, known as in RP43;, features a modification of the amino acid from S to R at position 344.
+The protein's natural variant, known as in RP43;, features a modification of the amino acid from Q to K at position 569.
+The protein's natural variant, known as in RP43;, features a modification of the amino acid from S to P at position 573.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from R to T at position 216.
+The protein's natural variant, known as in HEMB; severe; UK 22, features a modification of the amino acid from I to N at position 17.
+The protein's natural variant, known as in HEMB; unknown pathological significance; decreased protein abundance; decreased function in blood coagulation, features a modification of the amino acid from L to S at position 20.
+The protein's natural variant, known as in HEMB; moderate; HB130;, features a modification of the amino acid from C to R at position 28.
+The protein's natural variant, known as in HEMB; decreased protein abundance; decreased function in blood coagulation, features a modification of the amino acid from C to Y at position 28.
+The protein's natural variant, known as in HEMB, features a modification of the amino acid from V to I at position 30.
+The protein's natural variant, known as in WARFS; reduced affinity of the glutamate carboxylase for the factor IX precursor; 4.4-fold decreased in the EC(50) for warfarin;, features a modification of the amino acid from A to T at position 37.
+The protein's natural variant, known as in WARFS; 2.5-fold decreased in the EC(50) for warfarin;, features a modification of the amino acid from A to V at position 37.
+The protein's natural variant, known as in HEMB; severe; Bendorf, Beuten, Gleiwitz; impairs removal of propeptide;, features a modification of the amino acid from R to L at position 43.
+The protein's natural variant, known as in HEMB; severe; San Dimas, Oxford-3, Strasbourg-2; impairs removal of propeptide;, features a modification of the amino acid from R to Q at position 43.
+The protein's natural variant, known as in HEMB; severe; Boxtel, Heiden, Lienen; impairs removal of propeptide;, features a modification of the amino acid from R to W at position 43.
+The protein's natural variant, known as in HEMB; severe; Seattle E, features a modification of the amino acid from K to N at position 45.
+The protein's natural variant, known as in HEMB; severe; Cambridge; impaired processing of the propeptide; impaired gamma-carboxylation; decreased protein abundance; loss of function in blood coagulation, features a modification of the amino acid from R to S at position 46.
+The protein's natural variant, known as in HEMB; severe, features a modification of the amino acid from R to T at position 46.
+The protein's natural variant, known as in HEMB; severe; Calgary-16, features a modification of the amino acid from N to I at position 48.
+The protein's natural variant, known as in HEMB, features a modification of the amino acid from S to P at position 49.
+The protein's natural variant, known as in HEMB; severe; Gla mutant, features a modification of the amino acid from L to S at position 52.
+The protein's natural variant, known as in HEMB; severe; Oxford-B2; Gla mutant, features a modification of the amino acid from E to A at position 53.
+The protein's natural variant, known as in HEMB; unknown pathological significance; no effect on protein abundance; loss of function in blood coagulation, features a modification of the amino acid from E to D at position 54.
+The protein's natural variant, known as in HEMB; severe; HB151; Gla mutant, features a modification of the amino acid from E to G at position 54.
+The protein's natural variant, known as in HEMB, features a modification of the amino acid from F to C at position 55.
+The protein's natural variant, known as in HEMB; severe; Hong Kong-1, features a modification of the amino acid from G to A at position 58.
+The protein's natural variant, known as in HEMB; unknown pathological significance; no effect on protein abundance; loss of function in blood coagulation, features a modification of the amino acid from G to E at position 58.
+The protein's natural variant, known as in HEMB; severe; Los Angeles-4, features a modification of the amino acid from G to R at position 58.
+The protein's natural variant, known as in HEMB; moderate, features a modification of the amino acid from E to V at position 66.
+The protein's natural variant, known as in HEMB; severe; Nagoya-4; Gla mutant;, features a modification of the amino acid from E to K at position 67.
+The protein's natural variant, known as in HEMB; severe, features a modification of the amino acid from F to S at position 71.
+The protein's natural variant, known as in HEMB; severe; Seattle-3; Gla mutant;, features a modification of the amino acid from E to K at position 73.
+The protein's natural variant, known as in HEMB; severe; Chongqing; Gla mutant;, features a modification of the amino acid from E to V at position 73.
+The protein's natural variant, known as in HEMB; mild;, features a modification of the amino acid from R to Q at position 75.
+The protein's natural variant, known as in HEMB;, features a modification of the amino acid from E to D at position 79.
+The protein's natural variant, known as in HEMB; decreased protein abundance; loss of function in blood coagulation, features a modification of the amino acid from T to R at position 84.
+The protein's natural variant, known as in HEMB; moderate, features a modification of the amino acid from Y to C at position 91.
+The protein's natural variant, known as in HEMB; moderate; Alabama;, features a modification of the amino acid from D to G at position 93.
+The protein's natural variant, known as in HEMB; severe; New London;, features a modification of the amino acid from Q to P at position 96.
+The protein's natural variant, known as in HEMB, features a modification of the amino acid from C to S at position 97.
+The protein's natural variant, known as in HEMB, features a modification of the amino acid from P to R at position 101.
+The protein's natural variant, known as in HEMB; severe; Basel;, features a modification of the amino acid from C to R at position 102.
+The protein's natural variant, known as in HEMB, features a modification of the amino acid from G to D at position 106.
+The protein's natural variant, known as in HEMB; mild; Durham;, features a modification of the amino acid from G to S at position 106.
+The protein's natural variant, known as in HEMB, features a modification of the amino acid from C to S at position 108.
+The protein's natural variant, known as in HEMB; severe; Oxford-D1;, features a modification of the amino acid from D to N at position 110.
+The protein's natural variant, known as in HEMB, features a modification of the amino acid from I to S at position 112.
+The protein's natural variant, known as in HEMB; mild, features a modification of the amino acid from N to K at position 113.
+The protein's natural variant, known as in HEMB; severe;, features a modification of the amino acid from Y to C at position 115.
+The protein's natural variant, known as in HEMB; severe, features a modification of the amino acid from C to F at position 119.
+The protein's natural variant, known as in HEMB; Iran, features a modification of the amino acid from C to R at position 119.
+The protein's natural variant, known as in HEMB, features a modification of the amino acid from E to K at position 124.
+The protein's natural variant, known as in HEMB, features a modification of the amino acid from G to E at position 125.
+The protein's natural variant, known as in HEMB, features a modification of the amino acid from G to R at position 125.
+The protein's natural variant, known as in HEMB, features a modification of the amino acid from G to V at position 125.
+The protein's natural variant, known as in HEMB, features a modification of the amino acid from C to Y at position 134.
+The protein's natural variant, known as in HEMB; mild;, features a modification of the amino acid from I to T at position 136.
+The protein's natural variant, known as in HEMB; unknown pathological significance; decreased protein abundance; decreased function in blood coagulation, features a modification of the amino acid from N to H at position 138.
+The protein's natural variant, known as in HEMB; severe;, features a modification of the amino acid from G to D at position 139.
+The protein's natural variant, known as in HEMB, features a modification of the amino acid from G to S at position 139.
+The protein's natural variant, known as in HEMB; severe;, features a modification of the amino acid from C to F at position 155.
+The protein's natural variant, known as in HEMB; mild, features a modification of the amino acid from G to E at position 160.
+The protein's natural variant, known as in HEMB; mild, features a modification of the amino acid from Q to H at position 167.
+The protein's natural variant, known as in HEMB, features a modification of the amino acid from S to C at position 169.
+The protein's natural variant, known as in HEMB, features a modification of the amino acid from C to F at position 170.
+The protein's natural variant, known as in HEMB, features a modification of the amino acid from C to R at position 178.
+The protein's natural variant, known as in HEMB; severe, features a modification of the amino acid from C to W at position 178.
+The protein's natural variant, known as in HEMB; moderate; Albuquerque, Cardiff-1;, features a modification of the amino acid from R to C at position 191.
+The protein's natural variant, known as in HEMB; moderate; Chapel-Hill, Chicago-2;, features a modification of the amino acid from R to H at position 191.
+The protein's natural variant, known as in HEMB; severe; Madrid, features a modification of the amino acid from R to G at position 226.
+The protein's natural variant, known as in HEMB; severe; Hilo and Novara; no effect on protein abundance; loss of function in blood coagulation;, features a modification of the amino acid from R to Q at position 226.
+The protein's natural variant, known as in HEMB; severe; Nagoya-1, Dernbach, Deventer, Idaho;, features a modification of the amino acid from R to W at position 226.
+The protein's natural variant, known as in HEMB; mild, features a modification of the amino acid from V to D at position 227.
+The protein's natural variant, known as in HEMB; Milano;, features a modification of the amino acid from V to F at position 227.
+The protein's natural variant, known as in HEMB; severe; Kashihara;, features a modification of the amino acid from V to F at position 228.
+The protein's natural variant, known as in HEMB; mild; Cardiff-2;, features a modification of the amino acid from V to L at position 228.
+The protein's natural variant, known as in HEMB;, features a modification of the amino acid from Q to H at position 241.
+The protein's natural variant, known as in HEMB, features a modification of the amino acid from Q to K at position 241.
+The protein's natural variant, known as in HEMB; severe;, features a modification of the amino acid from C to S at position 252.
+The protein's natural variant, known as in HEMB, features a modification of the amino acid from C to Y at position 252.
+The protein's natural variant, known as in HEMB; severe, features a modification of the amino acid from G to E at position 253.
+The protein's natural variant, known as in HEMB; severe; Luanda;, features a modification of the amino acid from G to R at position 253.
+The protein's natural variant, known as in HEMB; mild, features a modification of the amino acid from A to T at position 265.
+The protein's natural variant, known as in HEMB; moderate;, features a modification of the amino acid from C to W at position 268.
+The protein's natural variant, known as in HEMB; mild;, features a modification of the amino acid from A to T at position 279.
+The protein's natural variant, known as in HEMB; severe, features a modification of the amino acid from N to D at position 283.
+The protein's natural variant, known as in HEMB; Monschau;, features a modification of the amino acid from E to V at position 291.
+The protein's natural variant, known as in HEMB; severe, features a modification of the amino acid from R to G at position 294.
+The protein's natural variant, known as in HEMB; mild to moderate; Dreihacken, Penafiel and Seattle-4;, features a modification of the amino acid from R to Q at position 294.
+The protein's natural variant, known as in HEMB; unknown pathological significance; decreased protein abundance; decreased function in blood coagulation, features a modification of the amino acid from V to M at position 296.
+The protein's natural variant, known as in HEMB, features a modification of the amino acid from H to R at position 302.
+The protein's natural variant, known as in HEMB; mild;, features a modification of the amino acid from N to S at position 306.
+The protein's natural variant, known as in HEMB, features a modification of the amino acid from I to F at position 316.
+The protein's natural variant, known as in HEMB;, features a modification of the amino acid from L to R at position 318.
+The protein's natural variant, known as in HEMB; severe, features a modification of the amino acid from L to Q at position 321.
+The protein's natural variant, known as in HEMB; unknown pathological significance; decreased protein abundance; decreased function in blood coagulation, features a modification of the amino acid from N to K at position 328.
+The protein's natural variant, known as in HEMB; moderate; decreased protein abundance; decreased function in blood coagulation, features a modification of the amino acid from N to Y at position 328.
+The protein's natural variant, known as in HEMB; severe, features a modification of the amino acid from P to H at position 333.
+The protein's natural variant, known as in HEMB, features a modification of the amino acid from P to T at position 333.
+The protein's natural variant, known as in HEMB; mild, features a modification of the amino acid from T to K at position 342.
+The protein's natural variant, known as in HEMB; moderate;, features a modification of the amino acid from T to M at position 342.
+The protein's natural variant, known as in HEMB, features a modification of the amino acid from I to L at position 344.
+The protein's natural variant, known as in HEMB, features a modification of the amino acid from G to D at position 351.
+The protein's natural variant, known as in HEMB; severe, features a modification of the amino acid from W to C at position 356.
+The protein's natural variant, known as in HEMB; severe; Amagasaki;, features a modification of the amino acid from G to E at position 357.
+The protein's natural variant, known as in HEMB;, features a modification of the amino acid from G to R at position 357.
+The protein's natural variant, known as in HEMB; moderate, features a modification of the amino acid from K to E at position 362.
+The protein's natural variant, known as in HEMB, features a modification of the amino acid from G to W at position 363.
+The protein's natural variant, known as in HEMB, features a modification of the amino acid from A to D at position 366.
+The protein's natural variant, known as in HEMB; moderate;, features a modification of the amino acid from R to G at position 379.
+The protein's natural variant, known as in HEMB; severe; Iceland-1, London and Sesimbra;, features a modification of the amino acid from R to Q at position 379.
+The protein's natural variant, known as in HEMB;, features a modification of the amino acid from C to Y at position 382.
+The protein's natural variant, known as in HEMB, features a modification of the amino acid from L to F at position 383.
+The protein's natural variant, known as in HEMB, features a modification of the amino acid from L to I at position 383.
+The protein's natural variant, known as in THPH8; factor IXPadua; higher specific activity than wild-type;, features a modification of the amino acid from R to L at position 384.
+The protein's natural variant, known as in HEMB; mild, features a modification of the amino acid from K to E at position 387.
+The protein's natural variant, known as in HEMB; severe, features a modification of the amino acid from I to F at position 390.
+The protein's natural variant, known as in HEMB, features a modification of the amino acid from M to K at position 394.
+The protein's natural variant, known as in HEMB;, features a modification of the amino acid from F to I at position 395.
+The protein's natural variant, known as in HEMB;, features a modification of the amino acid from F to L at position 395.
+The protein's natural variant, known as in HEMB, features a modification of the amino acid from C to F at position 396.
+The protein's natural variant, known as in HEMB; severe;, features a modification of the amino acid from C to S at position 396.
+The protein's natural variant, known as in HEMB; mild; Hong Kong-11;, features a modification of the amino acid from A to P at position 397.
+The protein's natural variant, known as in HEMB, features a modification of the amino acid from R to T at position 404.
+The protein's natural variant, known as in HEMB, features a modification of the amino acid from C to R at position 407.
+The protein's natural variant, known as in HEMB; severe, features a modification of the amino acid from C to S at position 407.
+The protein's natural variant, known as in HEMB; Mechtal;, features a modification of the amino acid from D to H at position 410.
+The protein's natural variant, known as in HEMB; Varel;, features a modification of the amino acid from S to G at position 411.
+The protein's natural variant, known as in HEMB; Schmallenberg;, features a modification of the amino acid from S to I at position 411.
+The protein's natural variant, known as in HEMB;, features a modification of the amino acid from G to E at position 412.
+The protein's natural variant, known as in HEMB; moderate to severe;, features a modification of the amino acid from G to R at position 413.
+The protein's natural variant, known as in HEMB; Bergamo; increased protein abundance; loss of function in blood coagulation;, features a modification of the amino acid from P to T at position 414.
+The protein's natural variant, known as in HEMB; moderately severe;, features a modification of the amino acid from V to E at position 419.
+The protein's natural variant, known as in HEMB, features a modification of the amino acid from F to V at position 424.
+The protein's natural variant, known as in HEMB; severe; Barcelos;, features a modification of the amino acid from T to P at position 426.
+The protein's natural variant, known as in HEMB, features a modification of the amino acid from S to T at position 430.
+The protein's natural variant, known as in HEMB, features a modification of the amino acid from W to G at position 431.
+The protein's natural variant, known as in HEMB; moderate, features a modification of the amino acid from W to R at position 431.
+The protein's natural variant, known as in HEMB; severe;, features a modification of the amino acid from G to S at position 432.
+The protein's natural variant, known as in HEMB; severe, features a modification of the amino acid from G to V at position 432.
+The protein's natural variant, known as in HEMB, features a modification of the amino acid from E to A at position 433.
+The protein's natural variant, known as in HEMB;, features a modification of the amino acid from E to K at position 433.
+The protein's natural variant, known as in HEMB;, features a modification of the amino acid from C to Y at position 435.
+The protein's natural variant, known as in HEMB; moderately severe; Niigata;, features a modification of the amino acid from A to V at position 436.
+The protein's natural variant, known as in HEMB;, features a modification of the amino acid from G to E at position 442.
+The protein's natural variant, known as in HEMB; severe; Angers;, features a modification of the amino acid from G to R at position 442.
+The protein's natural variant, known as in HEMB; moderately severe; Long Beach, Los Angeles and Vancouver;, features a modification of the amino acid from I to T at position 443.
+The protein's natural variant, known as in HEMB; severe; Lousada, features a modification of the amino acid from T to TIYT at position 445.
+The protein's natural variant, known as in HEMB; reduced protein abundance; loss of function in blood coagulation, features a modification of the amino acid from V to VYTKV at position 447.
+The protein's natural variant, known as in HEMB; mild;, features a modification of the amino acid from R to Q at position 449.
+The protein's natural variant, known as in HEMB; mild;, features a modification of the amino acid from R to W at position 449.
+The protein's natural variant, known as in HEMB; severe;, features a modification of the amino acid from Y to C at position 450.
+The protein's natural variant, known as in HEMB;, features a modification of the amino acid from W to R at position 453.
+The protein's natural variant, known as in HEMB; Italy;, features a modification of the amino acid from I to T at position 454.
+The protein's natural variant, known as in SCA21;, features a modification of the amino acid from T to M at position 80.
+The protein's natural variant, known as in SCA21;, features a modification of the amino acid from R to C at position 116.
+The protein's natural variant, known as in SCA21;, features a modification of the amino acid from E to K at position 149.
+The protein's natural variant, known as in SCA21;, features a modification of the amino acid from P to L at position 170.
+The protein's natural variant, known as in SCA21;, features a modification of the amino acid from R to W at position 171.
+The protein's natural variant, known as in 62% of the population;, features a modification of the amino acid from A to S at position 180.
+The protein's natural variant, known as in BCM;, features a modification of the amino acid from C to R at position 203.
+The protein's natural variant, known as in BCM;, features a modification of the amino acid from P to L at position 307.
+The protein's natural variant, known as in CBP;, features a modification of the amino acid from G to E at position 338.
+The protein's natural variant, known as in MPS4A;, features a modification of the amino acid from L to M at position 15.
+The protein's natural variant, known as in MPS4A; reduced enzymatic activity;, features a modification of the amino acid from V to E at position 16.
+The protein's natural variant, known as in MPS4A, features a modification of the amino acid from G to R at position 23.
+The protein's natural variant, known as in MPS4A, features a modification of the amino acid from L to P at position 36.
+The protein's natural variant, known as in MPS4A; reduced enzymatic activity;, features a modification of the amino acid from L to R at position 36.
+The protein's natural variant, known as in MPS4A, features a modification of the amino acid from D to N at position 40.
+The protein's natural variant, known as in MPS4A;, features a modification of the amino acid from M to L at position 41.
+The protein's natural variant, known as in MPS4A, features a modification of the amino acid from G to E at position 42.
+The protein's natural variant, known as in MPS4A; severe form;, features a modification of the amino acid from G to R at position 47.
+The protein's natural variant, known as in MPS4A;, features a modification of the amino acid from V to G at position 48.
+The protein's natural variant, known as in MPS4A; reduced enzymatic activity;, features a modification of the amino acid from E to K at position 51.
+The protein's natural variant, known as in MPS4A;, features a modification of the amino acid from S to F at position 53.
+The protein's natural variant, known as in MPS4A; mild form;, features a modification of the amino acid from D to N at position 60.
+The protein's natural variant, known as in MPS4A;, features a modification of the amino acid from R to W at position 61.
+The protein's natural variant, known as associated with S-409 in a MPS4A patient;, features a modification of the amino acid from L to M at position 67.
+The protein's natural variant, known as in MPS4A;, features a modification of the amino acid from F to V at position 69.
+The protein's natural variant, known as in MPS4A, features a modification of the amino acid from NFYS to T at position 74.
+The natural variant of this protein is characterized by an amino acid alteration from S to F at position 74.
+The protein's natural variant, known as in MPS4A; severe form, features a modification of the amino acid from P to R at position 77.
+The protein's natural variant, known as in MPS4A;, features a modification of the amino acid from C to Y at position 79.
+The protein's natural variant, known as in MPS4A; intermediate form;, features a modification of the amino acid from S to L at position 80.
+The protein's natural variant, known as in MPS4A; reduced enzymatic activity, features a modification of the amino acid from P to L at position 81.
+The protein's natural variant, known as in MPS4A; loss of enzymatic activity;, features a modification of the amino acid from A to E at position 84.
+The protein's natural variant, known as in MPS4A; severe form;, features a modification of the amino acid from R to W at position 90.
+The protein's natural variant, known as in MPS4A; loss of enzymatic activity, features a modification of the amino acid from L to P at position 91.
+The protein's natural variant, known as in MPS4A; mild/intermediate form;, features a modification of the amino acid from R to C at position 94.
+The protein's natural variant, known as in MPS4A; mild/intermediate form;, features a modification of the amino acid from R to G at position 94.
+The protein's natural variant, known as in MPS4A, features a modification of the amino acid from R to L at position 94.
+The protein's natural variant, known as in MPS4A, features a modification of the amino acid from G to C at position 96.
+The protein's natural variant, known as in MPS4A; severe form, features a modification of the amino acid from G to V at position 96.
+The protein's natural variant, known as in MPS4A; mild form, features a modification of the amino acid from F to V at position 97.
+The protein's natural variant, known as in MPS4A;, features a modification of the amino acid from A to T at position 107.
+The protein's natural variant, known as in MPS4A; intermediate form, features a modification of the amino acid from Q to R at position 111.
+The protein's natural variant, known as in MPS4A; severe form; common mutation; found in patients with Irish-British ancestry;, features a modification of the amino acid from I to F at position 113.
+The protein's natural variant, known as in MPS4A;, features a modification of the amino acid from G to S at position 116.
+The protein's natural variant, known as in MPS4A; reduced enzymatic activity, features a modification of the amino acid from G to V at position 116.
+The natural variant of this protein is characterized by an amino acid alteration from E to D at position 121.
+The protein's natural variant, known as in MPS4A; severe form;, features a modification of the amino acid from P to L at position 125.
+The protein's natural variant, known as in MPS4A; severe form, features a modification of the amino acid from S to R at position 135.
+The protein's natural variant, known as in MPS4A; mild/severe/intermediate form;, features a modification of the amino acid from V to A at position 138.
+The protein's natural variant, known as in MPS4A; severe form;, features a modification of the amino acid from G to S at position 139.
+The protein's natural variant, known as in MPS4A, features a modification of the amino acid from W to C at position 141.
+The protein's natural variant, known as in MPS4A; severe form;, features a modification of the amino acid from W to R at position 141.
+The protein's natural variant, known as in MPS4A; reduced enzymatic activity;, features a modification of the amino acid from H to Y at position 145.
+The protein's natural variant, known as in MPS4A;, features a modification of the amino acid from H to Y at position 150.
+The protein's natural variant, known as in MPS4A; severe form;, features a modification of the amino acid from P to L at position 151.
+The protein's natural variant, known as in MPS4A; severe form, features a modification of the amino acid from P to S at position 151.
+The protein's natural variant, known as in MPS4A, features a modification of the amino acid from G to E at position 155.
+The protein's natural variant, known as in MPS4A; severe form;, features a modification of the amino acid from G to R at position 155.
+The protein's natural variant, known as in MPS4A; severe form;, features a modification of the amino acid from F to C at position 156.
+The protein's natural variant, known as in MPS4A; reduced enzymatic activity;, features a modification of the amino acid from F to L at position 156.
+The protein's natural variant, known as in MPS4A; mild form, features a modification of the amino acid from F to S at position 156.
+The natural variant of this protein is characterized by an amino acid alteration from W to C at position 159.
+The protein's natural variant, known as in MPS4A;, features a modification of the amino acid from S to F at position 162.
+The protein's natural variant, known as in MPS4A;, features a modification of the amino acid from N to T at position 164.
+The protein's natural variant, known as in MPS4A; severe form;, features a modification of the amino acid from H to Q at position 166.
+The protein's natural variant, known as in MPS4A; reduced enzymatic activity, features a modification of the amino acid from H to R at position 166.
+The protein's natural variant, known as in MPS4A;, features a modification of the amino acid from F to V at position 167.
+The protein's natural variant, known as in MPS4A;, features a modification of the amino acid from G to R at position 168.
+The protein's natural variant, known as in MPS4A, features a modification of the amino acid from D to A at position 171.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 178.
+The protein's natural variant, known as in MPS4A; severe form, features a modification of the amino acid from P to H at position 179.
+The protein's natural variant, known as in MPS4A; severe form, features a modification of the amino acid from P to L at position 179.
+The protein's natural variant, known as in MPS4A, features a modification of the amino acid from P to S at position 179.
+The protein's natural variant, known as in MPS4A; severe form, features a modification of the amino acid from E to G at position 185.
+The protein's natural variant, known as in MPS4A; reduced enzymatic activity;, features a modification of the amino acid from G to E at position 201.
+The protein's natural variant, known as in MPS4A, features a modification of the amino acid from A to V at position 203.
+The protein's natural variant, known as in MPS4A; mild form;, features a modification of the amino acid from N to K at position 204.
+The protein's natural variant, known as in MPS4A; reduced enzymatic activity;, features a modification of the amino acid from L to P at position 214.
+The protein's natural variant, known as in MPS4A; reduced enzymatic activity;, features a modification of the amino acid from F to S at position 216.
+The protein's natural variant, known as in MPS4A; severe form, features a modification of the amino acid from W to G at position 230.
+The protein's natural variant, known as in MPS4A;, features a modification of the amino acid from D to N at position 233.
+The protein's natural variant, known as in MPS4A;, features a modification of the amino acid from T to K at position 235.
+The protein's natural variant, known as in MPS4A, features a modification of the amino acid from V to F at position 239.
+The protein's natural variant, known as in MPS4A;, features a modification of the amino acid from G to D at position 247.
+The protein's natural variant, known as in MPS4A;, features a modification of the amino acid from R to W at position 253.
+The natural variant of this protein is characterized by an amino acid alteration from Y to C at position 254.
+The protein's natural variant, known as in MPS4A; severe form;, features a modification of the amino acid from A to T at position 257.
+The protein's natural variant, known as in MPS4A; mild form;, features a modification of the amino acid from R to Q at position 259.
+The protein's natural variant, known as in MPS4A, features a modification of the amino acid from E to D at position 260.
+The natural variant of this protein is characterized by an amino acid alteration from E to K at position 260.
+The protein's natural variant, known as in MPS4A; reduced enzymatic activity, features a modification of the amino acid from S to T at position 264.
+The protein's natural variant, known as in MPS4A; severe form;, features a modification of the amino acid from F to V at position 284.
+The protein's natural variant, known as in MPS4A; severe form;, features a modification of the amino acid from S to L at position 287.
+The protein's natural variant, known as in MPS4A; severe form;, features a modification of the amino acid from G to S at position 290.
+The protein's natural variant, known as in MPS4A; mild form, features a modification of the amino acid from A to D at position 291.
+The protein's natural variant, known as in MPS4A; severe form;, features a modification of the amino acid from A to T at position 291.
+The protein's natural variant, known as in MPS4A; mild form;, features a modification of the amino acid from S to F at position 295.
+The protein's natural variant, known as in MPS4A; severe form;, features a modification of the amino acid from G to C at position 301.
+The protein's natural variant, known as in MPS4A, features a modification of the amino acid from L to P at position 307.
+The protein's natural variant, known as in MPS4A; severe form, features a modification of the amino acid from G to R at position 309.
+The protein's natural variant, known as in MPS4A;, features a modification of the amino acid from K to N at position 310.
+The protein's natural variant, known as in MPS4A; mild/intermediate/severe form;, features a modification of the amino acid from T to S at position 312.
+The protein's natural variant, known as in MPS4A; severe form;, features a modification of the amino acid from M to R at position 318.
+The protein's natural variant, known as in MPS4A;, features a modification of the amino acid from W to C at position 325.
+The protein's natural variant, known as in MPS4A;, features a modification of the amino acid from G to D at position 340.
+The protein's natural variant, known as in MPS4A, features a modification of the amino acid from S to R at position 341.
+The protein's natural variant, known as in MPS4A; severe form, features a modification of the amino acid from M to R at position 343.
+The protein's natural variant, known as in MPS4A, features a modification of the amino acid from D to E at position 344.
+The protein's natural variant, known as in MPS4A; severe form, features a modification of the amino acid from D to N at position 344.
+The protein's natural variant, known as in MPS4A, features a modification of the amino acid from L to P at position 345.
+The protein's natural variant, known as in MPS4A; severe form, features a modification of the amino acid from F to L at position 346.
+The protein's natural variant, known as in MPS4A; severe form;, features a modification of the amino acid from A to V at position 351.
+The protein's natural variant, known as in MPS4A, features a modification of the amino acid from L to P at position 352.
+The protein's natural variant, known as in MPS4A;, features a modification of the amino acid from P to L at position 357.
+The protein's natural variant, known as in MPS4A;, features a modification of the amino acid from R to G at position 361.
+The protein's natural variant, known as in MPS4A, features a modification of the amino acid from L to P at position 369.
+The protein's natural variant, known as in MPS4A; severe form;, features a modification of the amino acid from R to Q at position 376.
+The protein's natural variant, known as in MPS4A; loss of enzymatic activity;, features a modification of the amino acid from R to G at position 380.
+The protein's natural variant, known as in MPS4A;, features a modification of the amino acid from R to S at position 380.
+The protein's natural variant, known as in MPS4A, features a modification of the amino acid from R to T at position 380.
+The protein's natural variant, known as in MPS4A; severe form;, features a modification of the amino acid from R to C at position 386.
+The protein's natural variant, known as in MPS4A;, features a modification of the amino acid from R to H at position 386.
+The protein's natural variant, known as in MPS4A;, features a modification of the amino acid from D to N at position 388.
+The protein's natural variant, known as in MPS4A; severe form;, features a modification of the amino acid from M to V at position 391.
+The protein's natural variant, known as in MPS4A;, features a modification of the amino acid from A to V at position 392.
+The protein's natural variant, known as in MPS4A, features a modification of the amino acid from L to P at position 395.
+The protein's natural variant, known as in MPS4A; severe form, features a modification of the amino acid from L to V at position 395.
+The protein's natural variant, known as in MPS4A, features a modification of the amino acid from H to D at position 398.
+The protein's natural variant, known as in MPS4A, features a modification of the amino acid from H to Y at position 401.
+The protein's natural variant, known as in MPS4A;, features a modification of the amino acid from N to H at position 407.
+The protein's natural variant, known as in MPS4A; associated with M-67 in a patient, features a modification of the amino acid from W to S at position 409.
+The protein's natural variant, known as in MPS4A; loss of enzymatic activity, features a modification of the amino acid from G to V at position 415.
+The protein's natural variant, known as in MPS4A; reduced enzymatic activity;, features a modification of the amino acid from I to T at position 416.
+The protein's natural variant, known as in MPS4A; reduced enzymatic activity, features a modification of the amino acid from P to R at position 420.
+The protein's natural variant, known as in MPS4A; severe form, features a modification of the amino acid from E to V at position 450.
+The protein's natural variant, known as in MPS4A;, features a modification of the amino acid from F to I at position 452.
+The protein's natural variant, known as in MPS4A, features a modification of the amino acid from S to P at position 470.
+The protein's natural variant, known as in MPS4A;, features a modification of the amino acid from P to S at position 484.
+The protein's natural variant, known as in MPS4A;, features a modification of the amino acid from N to S at position 487.
+The protein's natural variant, known as in MPS4A; reduced enzymatic activity;, features a modification of the amino acid from A to T at position 492.
+The protein's natural variant, known as in MPS4A; severe form;, features a modification of the amino acid from M to V at position 494.
+The protein's natural variant, known as in MPS4A; reduced enzymatic activity;, features a modification of the amino acid from G to S at position 500.
+The protein's natural variant, known as in MPS4A;, features a modification of the amino acid from C to F at position 507.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from P to T at position 510.
+The protein's natural variant, known as in AIFEC; results in a gain of function mutation with constitutive activation of caspase-1;, features a modification of the amino acid from T to S at position 337.
+The protein's natural variant, known as in AIFEC; results in a gain of function mutation with constitutive activation of caspase-1;, features a modification of the amino acid from V to A at position 341.
+The protein's natural variant, known as in FCAS4; the mutation increases oligomerization of the NLRC4 protein; results in hyperactivation of caspase-1 with an increase in IL1B protein secretion;, features a modification of the amino acid from H to P at position 443.
+The protein's natural variant, known as in strain: H265, features a modification of the amino acid from E to V at position 4.
+The protein's natural variant, known as in strain: H518, features a modification of the amino acid from I to N at position 600.
+The protein's natural variant, known as in strain: H201, features a modification of the amino acid from I to T at position 1276.
+The natural variant of this protein is characterized by an amino acid alteration from G to A at position 76.
+The natural variant of this protein is characterized by an amino acid alteration from K to N at position 138.
+The protein's natural variant, known as in allele GSTM1B;, features a modification of the amino acid from K to N at position 173.
+The protein's natural variant, known as in SMVTD; reduced membrane localization; impaired biotin transport, features a modification of the amino acid from R to L at position 123.
+The protein's natural variant, known as in COMNB; no effect on membrane localization, features a modification of the amino acid from Y to C at position 162.
+The protein's natural variant, known as in SMVTD; impaired biotin transport;, features a modification of the amino acid from R to T at position 400.
+The protein's natural variant, known as in COMNB; no effect on membrane localization, features a modification of the amino acid from S to G at position 429.
+The protein's natural variant, known as in DIJOS, features a modification of the amino acid from W to R at position 117.
+The protein's natural variant, known as in DIJOS; unknown pathological significance;, features a modification of the amino acid from D to G at position 336.
+The protein's natural variant, known as in DIJOS;, features a modification of the amino acid from R to Q at position 943.
+The protein's natural variant, known as in DIJOS, features a modification of the amino acid from R to W at position 943.
+The protein's natural variant, known as in DIJOS, features a modification of the amino acid from R to Q at position 1028.
+The protein's natural variant, known as in DIJOS;, features a modification of the amino acid from D to V at position 1032.
+The protein's natural variant, known as in DIJOS, features a modification of the amino acid from L to P at position 1509.
+The protein's natural variant, known as in DIJOS; unknown pathological significance, features a modification of the amino acid from Y to C at position 1544.
+The protein's natural variant, known as in DIJOS; unknown pathological significance;, features a modification of the amino acid from E to K at position 1731.
+The protein's natural variant, known as in DIJOS, features a modification of the amino acid from L to R at position 1734.
+The protein's natural variant, known as in strain: cv. Chi-1, cv. Co-1, cv. Kon, cv. PHW-1 and cv. Sha, features a modification of the amino acid from I to V at position 83.
+The protein's natural variant, known as in strain: cv. Bu-0, cv. Da(1)-12, cv. Di-G, cv. Landsberg erecta, cv. Le-0, cv. Lip-0, cv. Mrk-0, cv. Stw-0 and cv. Ta-0, features a modification of the amino acid from Q to S at position 127.
+The protein's natural variant, known as in strain: cv. Chi-1, cv. Co-1, cv. Kon, cv. PHW-1 and cv. Sha, features a modification of the amino acid from D to E at position 326.
+The protein's natural variant, known as in strain: cv. Cvi-0, features a modification of the amino acid from V to M at position 367.
+The protein's natural variant, known as in strain: cv. Cvi-0, features a modification of the amino acid from T to I at position 476.
+The protein's natural variant, known as in strain: cv. Chi-1, cv. Co-1, cv. Kon, cv. PHW-1 and cv. Sha, features a modification of the amino acid from A to G at position 482.
+The protein's natural variant, known as in strain: cv. Chi-1, cv. Co-1, cv. Kon, cv. PHW-1 and cv. Sha, features a modification of the amino acid from A to S at position 498.
+The protein's natural variant, known as in strain: cv. Chi-1, cv. Co-1, cv. Kon, cv. PHW-1 and cv. Sha, features a modification of the amino acid from F to L at position 507.
+The protein's natural variant, known as in strain: cv. Chi-1, cv. Co-1, cv. Kon, cv. PHW-1 and cv. Sha, features a modification of the amino acid from G to E at position 511.
+The protein's natural variant, known as in strain: cv. Chi-1, cv. Co-1, cv. Kon, cv. PHW-1 and cv. Sha, features a modification of the amino acid from V to L at position 543.
+The protein's natural variant, known as in strain: cv. Chi-1, cv. Co-1, cv. Kon, cv. PHW-1 and cv. Sha, features a modification of the amino acid from C to Y at position 611.
+The protein's natural variant, known as in a patient with hypospadias, features a modification of the amino acid from A to T at position 131.
+The protein's natural variant, known as in WT1;, features a modification of the amino acid from P to S at position 181.
+The protein's natural variant, known as in WT1, features a modification of the amino acid from S to N at position 223.
+The protein's natural variant, known as in WT1, features a modification of the amino acid from G to A at position 253.
+The protein's natural variant, known as found in a mesothelioma sample; somatic mutation;, features a modification of the amino acid from S to G at position 273.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from L to P at position 281.
+The protein's natural variant, known as in NPHS4, features a modification of the amino acid from R to Q at position 312.
+The protein's natural variant, known as in DDS, features a modification of the amino acid from C to Y at position 330.
+The protein's natural variant, known as in DDS, features a modification of the amino acid from M to R at position 342.
+The protein's natural variant, known as in WT1, features a modification of the amino acid from C to G at position 355.
+The protein's natural variant, known as in DDS, features a modification of the amino acid from C to Y at position 355.
+The protein's natural variant, known as in DDS, features a modification of the amino acid from C to G at position 360.
+The protein's natural variant, known as in DDS, features a modification of the amino acid from C to Y at position 360.
+The protein's natural variant, known as in NPHS4, features a modification of the amino acid from F to L at position 364.
+The protein's natural variant, known as in WT1, DDS and MEACHS, features a modification of the amino acid from R to C at position 366.
+The protein's natural variant, known as in DDS and WT1, features a modification of the amino acid from R to H at position 366.
+The protein's natural variant, known as in DDS, features a modification of the amino acid from R to L at position 366.
+The protein's natural variant, known as in DDS, features a modification of the amino acid from Q to P at position 369.
+The protein's natural variant, known as in DDS and WT1, features a modification of the amino acid from H to Q at position 373.
+The protein's natural variant, known as in DDS, features a modification of the amino acid from H to Y at position 373.
+The protein's natural variant, known as in DDS, features a modification of the amino acid from H to R at position 377.
+The protein's natural variant, known as in NPHS4, features a modification of the amino acid from H to Y at position 377.
+The protein's natural variant, known as in NPHS4, features a modification of the amino acid from G to C at position 379.
+The protein's natural variant, known as in NPHS4, features a modification of the amino acid from F to L at position 383.
+The protein's natural variant, known as in DDS, features a modification of the amino acid from C to R at position 385.
+The protein's natural variant, known as in DDS, features a modification of the amino acid from C to F at position 388.
+The protein's natural variant, known as in NPHS4, features a modification of the amino acid from C to R at position 388.
+The protein's natural variant, known as in DDS, features a modification of the amino acid from C to Y at position 388.
+The protein's natural variant, known as in FS, features a modification of the amino acid from F to L at position 392.
+The protein's natural variant, known as in WT1, features a modification of the amino acid from R to L at position 394.
+The protein's natural variant, known as in DDS, features a modification of the amino acid from R to P at position 394.
+The protein's natural variant, known as in DDS and NPHS4, features a modification of the amino acid from R to Q at position 394.
+The protein's natural variant, known as in DDS, WT1, MEACHS and NPHS4, features a modification of the amino acid from R to W at position 394.
+The protein's natural variant, known as in DDS, features a modification of the amino acid from D to G at position 396.
+The protein's natural variant, known as in DDS and NPHS4, features a modification of the amino acid from D to N at position 396.
+The protein's natural variant, known as in DDS, features a modification of the amino acid from D to Y at position 396.
+The protein's natural variant, known as in NPHS4, features a modification of the amino acid from H to P at position 397.
+The protein's natural variant, known as in DDS, features a modification of the amino acid from L to P at position 398.
+The protein's natural variant, known as in DDS, features a modification of the amino acid from H to Y at position 401.
+The protein's natural variant, known as in DDS, features a modification of the amino acid from H to R at position 405.
+The protein's natural variant, known as in JLNS2; impairs glycosylation at N-5;, features a modification of the amino acid from T to I at position 7.
+The protein's natural variant, known as in LQT5; unknown pathological significance;, features a modification of the amino acid from A to V at position 8.
+The protein's natural variant, known as in LQT5; unknown pathological significance;, features a modification of the amino acid from T to M at position 10.
+The protein's natural variant, known as in LQT5; unknown pathological significance;, features a modification of the amino acid from S to L at position 28.
+The protein's natural variant, known as in LQT5; unknown pathological significance;, features a modification of the amino acid from R to H at position 32.
+The protein's natural variant, known as in LQT5; unknown pathological significance;, features a modification of the amino acid from R to H at position 36.
+The protein's natural variant, known as in JLNS2;, features a modification of the amino acid from V to F at position 47.
+The protein's natural variant, known as in JLNS2, features a modification of the amino acid from L to H at position 51.
+The protein's natural variant, known as in LQT5; unknown pathological significance;, features a modification of the amino acid from F to S at position 53.
+The protein's natural variant, known as in LQT5; unknown pathological significance;, features a modification of the amino acid from G to S at position 55.
+The protein's natural variant, known as in JLNS2;, features a modification of the amino acid from TL to PP at position 59.
+The protein's natural variant, known as in LQT5; unknown pathological significance;, features a modification of the amino acid from T to P at position 58.
+The protein's natural variant, known as in LQT5; unknown pathological significance;, features a modification of the amino acid from L to P at position 59.
+The protein's natural variant, known as in LQT5; unknown pathological significance;, features a modification of the amino acid from R to C at position 67.
+The protein's natural variant, known as in LQT5; unknown pathological significance;, features a modification of the amino acid from R to H at position 67.
+The protein's natural variant, known as in LQT5; unknown pathological significance;, features a modification of the amino acid from K to M at position 70.
+The protein's natural variant, known as in LQT5;, features a modification of the amino acid from S to L at position 74.
+The protein's natural variant, known as in LQT5 and JLNS2; suppresses KCNQ1 currents markedly;, features a modification of the amino acid from D to N at position 76.
+The protein's natural variant, known as in LQT5; unknown pathological significance;, features a modification of the amino acid from E to K at position 83.
+The protein's natural variant, known as predisposes to acquired LQT5 susceptibility; shows a significant difference in current density and midpoint potential compared to the wild-type channel;, features a modification of the amino acid from D to N at position 85.
+The protein's natural variant, known as in LQT5;, features a modification of the amino acid from W to R at position 87.
+The protein's natural variant, known as in LQT5;, features a modification of the amino acid from R to W at position 98.
+The protein's natural variant, known as in LQT5; mild phenotype; unknown pathological significance; no effect on KCNQ1 C-terminus interaction; increases cAMP-mediated up-regulation of the I(KS) current; no effect on phosphorylation at S27;, features a modification of the amino acid from V to I at position 109.
+The protein's natural variant, known as in LQT5; unknown pathological significance;, features a modification of the amino acid from T to M at position 125.
+The protein's natural variant, known as in LQT5; moderately reduces I(KS) current density; no change of the voltage dependence of channel activation; markedly reduces interaction with KCNQ1 C-terminus; no effect on plasma membrane localization; loss of cAMP-mediated up-regulation of the I(KS) current; no effect on interaction with AKAP9; impairs phosphorylation at S-27 during cAMP-dependent stimulation;, features a modification of the amino acid from P to T at position 127.
+The natural variant of this protein is characterized by an amino acid alteration from F to L at position 668.
+The protein's natural variant, known as in POIKTMP;, features a modification of the amino acid from Y to D at position 621.
+The protein's natural variant, known as in POIKTMP;, features a modification of the amino acid from R to G at position 627.
+The protein's natural variant, known as in POIKTMP;, features a modification of the amino acid from S to N at position 628.
+The protein's natural variant, known as in MRX108; probable gain-of-function variant; affects the regulation of trans-Golgi network/post-Golgi pH homeostasis, causing alkalinization of these compartments compared to wild-type, hence affecting its own glycosylation and that of exported cargo proteins; no effect on subcellular location in the Golgi apparatus and plasma membrane, features a modification of the amino acid from L to F at position 515.
+The protein's natural variant, known as in strain: Miranda, PBOL and DM28C, features a modification of the amino acid from K to N at position 23.
+The protein's natural variant, known as in strain: DM28C, features a modification of the amino acid from R to P at position 33.
+The protein's natural variant, known as in strain: Miranda, PBOL and DM28C, features a modification of the amino acid from H to Y at position 71.
+The protein's natural variant, known as in strain: DM28C, features a modification of the amino acid from K to R at position 79.
+The protein's natural variant, known as in strain: PBOL and DM28C, features a modification of the amino acid from P to S at position 85.
+The protein's natural variant, known as in strain: DM28C, features a modification of the amino acid from R to G at position 86.
+The protein's natural variant, known as in strain: PBOL, features a modification of the amino acid from A to S at position 98.
+The protein's natural variant, known as in strain: PBOL, features a modification of the amino acid from A to T at position 100.
+The protein's natural variant, known as in strain: Miranda, features a modification of the amino acid from A to V at position 100.
+The protein's natural variant, known as in strain: Miranda, DM28C and PBOL, features a modification of the amino acid from L to F at position 152.
+The protein's natural variant, known as in strain: Miranda, features a modification of the amino acid from S to K at position 210.
+The protein's natural variant, known as in strain: cv. Shokei, features a modification of the amino acid from N to S at position 151.
+The protein's natural variant, known as in strain: cv. Shokei, features a modification of the amino acid from N to D at position 161.
+The natural variant of this protein is characterized by an amino acid alteration from M to I at position 49.
+The natural variant of this protein is characterized by an amino acid alteration from M to T at position 49.
+The protein's natural variant, known as in plasmid pCHL1, features a modification of the amino acid from S to R at position 5.
+The protein's natural variant, known as may be associated with NTD;, features a modification of the amino acid from I to T at position 69.
+The protein's natural variant, known as may be associated with NTD;, features a modification of the amino acid from N to H at position 81.
+The protein's natural variant, known as in EPM1B; affects interaction with REST;, features a modification of the amino acid from R to Q at position 104.
+The protein's natural variant, known as may be associated with NTD;, features a modification of the amino acid from V to I at position 121.
+The protein's natural variant, known as in EPM1B;, features a modification of the amino acid from R to H at position 144.
+The protein's natural variant, known as may be associated with NTD;, features a modification of the amino acid from T to M at position 275.
+The protein's natural variant, known as in EPM1B;, features a modification of the amino acid from Y to H at position 472.
+The protein's natural variant, known as may be associated with NTD;, features a modification of the amino acid from R to C at position 682.
+The protein's natural variant, known as may be associated with NTD;, features a modification of the amino acid from S to F at position 739.
+The protein's natural variant, known as may be associated with NTD;, features a modification of the amino acid from D to N at position 771.
+The protein's natural variant, known as may be associated with NTD, features a modification of the amino acid from S to C at position 799.
+The natural variant of this protein is characterized by an amino acid alteration from S to Y at position 254.
+The protein's natural variant, known as in ECYT5; unknown pathological significance;, features a modification of the amino acid from D to N at position 70.
+The protein's natural variant, known as in ECYT5; unknown pathological significance;, features a modification of the amino acid from G to R at position 84.
+The protein's natural variant, known as found in a patient thought to have erythrocytosis, but had normal red cell mass; unknown pathological significance, features a modification of the amino acid from E to G at position 99.
+The protein's natural variant, known as in ECYT5; unknown pathological significance;, features a modification of the amino acid from P to L at position 114.
+The protein's natural variant, known as in a hepatocellular carcinoma, features a modification of the amino acid from SL to NF at position 132.
+The protein's natural variant, known as in ECYT5; unknown pathological significance;, features a modification of the amino acid from S to C at position 147.
+The protein's natural variant, known as in a hepatocellular carcinoma, features a modification of the amino acid from P to Q at position 149.
+The protein's natural variant, known as in DBAL; loss of support of normal erythroid expansion or differentiation; reduced ability to promote EPOR dimer formation upon binding, resulting in reduced JAK2 activation and decreased STAT1 and STAT3 phosphorylation; mild decrease in affinity for EPOR; no effect on STAT5A phosphorylation;, features a modification of the amino acid from R to Q at position 177.
+The protein's natural variant, known as in RP78; decreased function in positive regulation of Rho protein signal transduction; loss of function in regulation of actomyosin structure organization;, features a modification of the amino acid from T to A at position 458.
+The protein's natural variant, known as no quinolone resistance, features a modification of the amino acid from D to A at position 352.
+The protein's natural variant, known as in strain: PB303, features a modification of the amino acid from G to S at position 41.
+The protein's natural variant, known as in strain: CB4855, features a modification of the amino acid from F to L at position 70.
+The protein's natural variant, known as in strain: RDEC-1, 83/39, 413/89-1 and CK379, features a modification of the amino acid from Y to H at position 151.
+The protein's natural variant, known as in NEDBSS;, features a modification of the amino acid from I to K at position 70.
+The protein's natural variant, known as in NEDBSS;, features a modification of the amino acid from N to K at position 383.
+The natural variant of this protein is characterized by an amino acid alteration from Q to E at position 1568.
+The protein's natural variant, known as in MLC1;, features a modification of the amino acid from G to E at position 59.
+The protein's natural variant, known as in MLC1;, features a modification of the amino acid from S to L at position 69.
+The protein's natural variant, known as in MLC1;, features a modification of the amino acid from M to I at position 80.
+The protein's natural variant, known as in MLC1;, features a modification of the amino acid from R to C at position 84.
+The protein's natural variant, known as in MLC1;, features a modification of the amino acid from P to S at position 92.
+The protein's natural variant, known as in MLC1;, features a modification of the amino acid from S to L at position 93.
+The protein's natural variant, known as in MLC1;, features a modification of the amino acid from T to R at position 118.
+The protein's natural variant, known as in MLC1; accumulates in the cytoplasmic perinuclear region and endoplasmic reticulum; affects interaction with ATP1B1;, features a modification of the amino acid from C to R at position 125.
+The protein's natural variant, known as in MLC1;, features a modification of the amino acid from N to K at position 141.
+The protein's natural variant, known as in MLC1;, features a modification of the amino acid from N to S at position 141.
+The protein's natural variant, known as in MLC1;, features a modification of the amino acid from G to R at position 212.
+The protein's natural variant, known as in MLC1;, features a modification of the amino acid from A to P at position 245.
+The protein's natural variant, known as in MLC1; does not affect subcellular location;, features a modification of the amino acid from S to R at position 246.
+The protein's natural variant, known as in MLC1; accumulates in the cytoplasmic perinuclear region and endoplasmic reticulum; affects the interaction with ATP1B1, TRPV4, AQP4 and HEPACAM;, features a modification of the amino acid from S to L at position 280.
+The protein's natural variant, known as in a pedigree affected by schizophrenia;, features a modification of the amino acid from L to M at position 309.
+The protein's natural variant, known as in MLC1;, features a modification of the amino acid from T to K at position 320.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from Q to H at position 123.
+The protein's natural variant, known as in EDSKSCL1; loss of enzyme activity, features a modification of the amino acid from W to G at position 446.
+The protein's natural variant, known as in EDSKSCL1;, features a modification of the amino acid from W to C at position 612.
+The protein's natural variant, known as in EDSKSCL1;, features a modification of the amino acid from A to T at position 667.
+The protein's natural variant, known as in EDSKSCL1;, features a modification of the amino acid from G to R at position 678.
+The protein's natural variant, known as in EDSKSCL1, features a modification of the amino acid from H to R at position 706.
+The protein's natural variant, known as does not affect fatty acid beta-oxidation;, features a modification of the amino acid from N to T at position 13.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from E to K at position 90.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from A to D at position 95.
+The protein's natural variant, known as in ALD; CALD type;, features a modification of the amino acid from S to L at position 98.
+The protein's natural variant, known as in ALD; AMN-type, features a modification of the amino acid from A to D at position 99.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from S to R at position 103.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from R to C at position 104.
+The protein's natural variant, known as in ALD; ADO-type;, features a modification of the amino acid from R to H at position 104.
+The protein's natural variant, known as in ALD; ADO-type, features a modification of the amino acid from T to I at position 105.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from T to P at position 105.
+The protein's natural variant, known as in ALD; ALD/AMN/ADO-types and asymptomatic;, features a modification of the amino acid from L to P at position 107.
+The protein's natural variant, known as in ALD;, features a modification of the amino acid from S to L at position 108.
+The protein's natural variant, known as in ALD; CALD and AMN-types, features a modification of the amino acid from S to W at position 108.
+The protein's natural variant, known as in ALD;, features a modification of the amino acid from R to C at position 113.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from R to P at position 113.
+The protein's natural variant, known as in ALD; CALD-type;, features a modification of the amino acid from G to R at position 116.
+The protein's natural variant, known as in ALD;, features a modification of the amino acid from A to T at position 141.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from P to S at position 143.
+The protein's natural variant, known as in ALD; ADO-type;, features a modification of the amino acid from N to S at position 148.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from S to N at position 149.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from R to L at position 152.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from R to P at position 152.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from R to S at position 152.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from S to P at position 161.
+The protein's natural variant, known as in ALD;, features a modification of the amino acid from R to H at position 163.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from R to P at position 163.
+The protein's natural variant, known as in ALD;, features a modification of the amino acid from Y to C at position 174.
+The protein's natural variant, known as in ALD; ALD-type;, features a modification of the amino acid from Y to D at position 174.
+The protein's natural variant, known as in ALD; CALD-type;, features a modification of the amino acid from Y to S at position 174.
+The protein's natural variant, known as in ALD; AMN-type, features a modification of the amino acid from Q to E at position 178.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from R to P at position 182.
+The protein's natural variant, known as in ALD;, features a modification of the amino acid from R to W at position 189.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from L to P at position 190.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from D to H at position 194.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from T to K at position 198.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from T to R at position 198.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from D to N at position 200.
+The protein's natural variant, known as in ALD; CALD-type, features a modification of the amino acid from D to V at position 200.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from S to SAAS at position 207.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from L to P at position 211.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from S to C at position 213.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from N to D at position 214.
+The protein's natural variant, known as in ALD; not able to restore defective beta-oxidation in fibroblast from patients with ALD, features a modification of the amino acid from K to E at position 217.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from P to T at position 218.
+The protein's natural variant, known as in ALD;, features a modification of the amino acid from L to P at position 220.
+The protein's natural variant, known as in ALD; CALD and AMN-types, features a modification of the amino acid from D to G at position 221.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from V to E at position 224.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from L to P at position 229.
+The protein's natural variant, known as in ALD; AMN-type;, features a modification of the amino acid from T to M at position 254.
+The protein's natural variant, known as in ALD; AMN-type, features a modification of the amino acid from T to P at position 254.
+The protein's natural variant, known as in ALD; CALD, AMN and AD-types, features a modification of the amino acid from P to L at position 263.
+The protein's natural variant, known as in ALD;, features a modification of the amino acid from G to E at position 266.
+The protein's natural variant, known as in ALD;, features a modification of the amino acid from G to R at position 266.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from E to K at position 271.
+The protein's natural variant, known as in ALD;, features a modification of the amino acid from R to W at position 274.
+The protein's natural variant, known as in ALD; CALD-type, features a modification of the amino acid from K to E at position 276.
+The protein's natural variant, known as in ALD; ADO-type, features a modification of the amino acid from G to GN at position 277.
+The protein's natural variant, known as in ALD; AMN-type;, features a modification of the amino acid from G to R at position 277.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from G to W at position 277.
+The protein's natural variant, known as in ALD;, features a modification of the amino acid from R to C at position 280.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from R to P at position 285.
+The protein's natural variant, known as in ALD; ACALD and CALD-types, features a modification of the amino acid from E to D at position 291.
+The protein's natural variant, known as in ALD;, features a modification of the amino acid from E to K at position 291.
+The protein's natural variant, known as in ALD; AMN-type;, features a modification of the amino acid from A to T at position 294.
+The protein's natural variant, known as in ALD;, features a modification of the amino acid from Y to C at position 296.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from G to D at position 298.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from E to EVGQ at position 300.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from E to K at position 302.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from Q to P at position 316.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from L to P at position 322.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from K to M at position 336.
+The protein's natural variant, known as in ALD;, features a modification of the amino acid from W to R at position 339.
+The protein's natural variant, known as in ALD; AMN-type, features a modification of the amino acid from S to P at position 342.
+The protein's natural variant, known as in ALD;, features a modification of the amino acid from G to D at position 343.
+The protein's natural variant, known as in ALD; AMN-type;, features a modification of the amino acid from R to G at position 389.
+The protein's natural variant, known as in ALD; does not affect protein stability, homo- and heterodimerization with ABCD2 and ABCD3;, features a modification of the amino acid from R to H at position 389.
+The protein's natural variant, known as in ALD; ALD and AMN-types; does not affect protein stability, homo- and heterodimerization with ABCD2 and ABCD3;, features a modification of the amino acid from R to Q at position 401.
+The protein's natural variant, known as in ALD;, features a modification of the amino acid from R to W at position 401.
+The protein's natural variant, known as in ALD; AMN-type;, features a modification of the amino acid from R to W at position 418.
+The protein's natural variant, known as in ALD; CALD, AMN and ADO-types; significantly decreases homodimerization and abolishes heterodimerization with ABCD2 and ABCD3;, features a modification of the amino acid from P to R at position 484.
+The protein's natural variant, known as in ALD; CALD-types, features a modification of the amino acid from G to V at position 507.
+The protein's natural variant, known as in ALD; CALD and AS-types; reduced ATPase activity;, features a modification of the amino acid from G to S at position 512.
+The protein's natural variant, known as in ALD;, features a modification of the amino acid from S to F at position 515.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from L to P at position 516.
+The protein's natural variant, known as in ALD; CALD-type;, features a modification of the amino acid from R to Q at position 518.
+The protein's natural variant, known as in ALD; CALD-type;, features a modification of the amino acid from R to W at position 518.
+The protein's natural variant, known as in ALD; AD-type, features a modification of the amino acid from G to W at position 522.
+The protein's natural variant, known as in ALD;, features a modification of the amino acid from L to F at position 523.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from G to S at position 529.
+The protein's natural variant, known as in ALD; CALD-type, features a modification of the amino acid from P to L at position 534.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from F to C at position 540.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from F to S at position 540.
+The protein's natural variant, known as in ALD;, features a modification of the amino acid from P to L at position 543.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from Q to R at position 544.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from S to P at position 552.
+The protein's natural variant, known as in ALD;, features a modification of the amino acid from R to H at position 554.
+The protein's natural variant, known as in ALD; ACALD type, features a modification of the amino acid from Q to R at position 556.
+The protein's natural variant, known as in ALD; CALD-type;, features a modification of the amino acid from P to L at position 560.
+The protein's natural variant, known as in ALD; AMN and ALMD-types, features a modification of the amino acid from P to R at position 560.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from P to S at position 560.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from M to K at position 566.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from R to P at position 591.
+The protein's natural variant, known as in ALD; AMN-type; significantly decreases homodimerization and abolishes heterodimerization with ABCD2 and ABCD3;, features a modification of the amino acid from R to Q at position 591.
+The protein's natural variant, known as in ALD;, features a modification of the amino acid from R to W at position 591.
+The protein's natural variant, known as in ALD; decreased ATP-binding affinity;, features a modification of the amino acid from S to L at position 606.
+The protein's natural variant, known as in ALD; CALD, AMN and ALMD-types;, features a modification of the amino acid from S to P at position 606.
+The protein's natural variant, known as in ALD; CALD-type;, features a modification of the amino acid from G to D at position 608.
+The protein's natural variant, known as in ALD;, features a modification of the amino acid from E to G at position 609.
+The protein's natural variant, known as in ALD; AMN-type;, features a modification of the amino acid from E to K at position 609.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from A to V at position 616.
+The protein's natural variant, known as in ALD; ALD-type and asymptomatic;, features a modification of the amino acid from R to C at position 617.
+The protein's natural variant, known as in ALD; ADO and AMN-types with cerebral involvement, features a modification of the amino acid from R to G at position 617.
+The protein's natural variant, known as in ALD;, features a modification of the amino acid from R to H at position 617.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from A to D at position 626.
+The protein's natural variant, known as in ALD; CALD and AMN-types;, features a modification of the amino acid from A to T at position 626.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from D to H at position 629.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from E to G at position 630.
+The protein's natural variant, known as in ALD;, features a modification of the amino acid from C to Y at position 631.
+The protein's natural variant, known as in ALD;, features a modification of the amino acid from T to I at position 632.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from T to P at position 632.
+The protein's natural variant, known as in ALD; asymptomatic, features a modification of the amino acid from S to I at position 633.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from S to R at position 633.
+The protein's natural variant, known as in ALD;, features a modification of the amino acid from V to M at position 635.
+The protein's natural variant, known as in ALD;, features a modification of the amino acid from S to I at position 636.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from D to Y at position 638.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from E to K at position 640.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from A to P at position 646.
+The protein's natural variant, known as in ALD;, features a modification of the amino acid from L to P at position 654.
+The protein's natural variant, known as in ALD; CALD-type, features a modification of the amino acid from R to P at position 660.
+The protein's natural variant, known as in ALD;, features a modification of the amino acid from R to Q at position 660.
+The protein's natural variant, known as in ALD; CALD, ALMD and AS-types;, features a modification of the amino acid from R to W at position 660.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from H to D at position 667.
+The protein's natural variant, known as in ALD;, features a modification of the amino acid from T to I at position 668.
+The protein's natural variant, known as in ALD, features a modification of the amino acid from G to D at position 677.
+The protein's natural variant, known as in ALD; AMN-type;, features a modification of the amino acid from W to R at position 679.
+The protein's natural variant, known as in ALD;, features a modification of the amino acid from T to M at position 693.
+The protein's natural variant, known as in SHR, features a modification of the amino acid from I to M at position 412.
+The protein's natural variant, known as in SHR, features a modification of the amino acid from T to S at position 423.
+The protein's natural variant, known as in SHR, features a modification of the amino acid from V to D at position 463.
+The protein's natural variant, known as in SHR, features a modification of the amino acid from G to A at position 668.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from V to A at position 88.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from R to H at position 105.
+The protein's natural variant, known as in HSAN8; no effect on nuclear localization; not able to induce histone H3-K9 dimethylation;, features a modification of the amino acid from D to Y at position 31.
+The protein's natural variant, known as in HSAN8; no effect on nuclear localization; not able to induce histone H3-K9 dimethylation;, features a modification of the amino acid from I to N at position 102.
+The protein's natural variant, known as in HSAN8; no effect on nuclear localization; not able to induce histone H3-K9 dimethylation, features a modification of the amino acid from W to C at position 160.
+The protein's natural variant, known as in HSAN8; no effect on nuclear localization; not able to induce histone H3-K9 dimethylation;, features a modification of the amino acid from R to C at position 168.
+The protein's natural variant, known as in HSAN8; no effect on nuclear localization; not able to induce histone H3-K9 dimethylation;, features a modification of the amino acid from E to D at position 172.
+The protein's natural variant, known as in HSAN8; no effect on nuclear localization; not able to induce histone H3-K9 dimethylation;, features a modification of the amino acid from H to L at position 289.
+The protein's natural variant, known as in HSAN8; reduced protein amount; results in protein aggregation, features a modification of the amino acid from A to AAAAAAAA at position 352.
+The protein's natural variant, known as in MRT58; unknown pathological significance;, features a modification of the amino acid from H to R at position 206.
+The protein's natural variant, known as in MRT58; unknown pathological significance;, features a modification of the amino acid from R to W at position 462.
+The protein's natural variant, known as in allele S and allele W1, features a modification of the amino acid from C to G at position 14.
+The protein's natural variant, known as in allele S, features a modification of the amino acid from S to A at position 21.
+The protein's natural variant, known as in allele W1, features a modification of the amino acid from D to E at position 74.
+The protein's natural variant, known as in allele W1, features a modification of the amino acid from V to M at position 135.
+The protein's natural variant, known as in allele S, features a modification of the amino acid from T to A at position 140.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from C to S at position 272.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from K to T at position 204.
+The protein's natural variant, known as in lpr, features a modification of the amino acid from I to N at position 246.
+The protein's natural variant, known as in MC1DN26; loss of function in complex I assembly; accumulation of several low and high molecular weight assembly intermediates is observed in patient fibroblasts;, features a modification of the amino acid from R to P at position 321.
+The protein's natural variant, known as in MC1DN26; loss of function in complex I assembly; accumulation of several low and high molecular weight assembly intermediates is observed in patient fibroblasts;, features a modification of the amino acid from R to C at position 360.
+The protein's natural variant, known as in AGS8; impaired histone 3'-end pre-mRNA processing, leading to defects in chromatin structure; promoting CGAS-dependent activation of the type I interferon pathway, features a modification of the amino acid from G to S at position 211.
+The protein's natural variant, known as in strain: Showa, features a modification of the amino acid from M to I at position 17.
+The protein's natural variant, known as in strain: Showa, features a modification of the amino acid from G to S at position 49.
+The protein's natural variant, known as in strain: Showa, features a modification of the amino acid from Y to H at position 62.
+The protein's natural variant, known as in strain: Showa, features a modification of the amino acid from S to N at position 65.
+The protein's natural variant, known as resistance to EMB, features a modification of the amino acid from S to A at position 297.
+The protein's natural variant, known as resistance to EMB, features a modification of the amino acid from M to I at position 306.
+The protein's natural variant, known as resistance to EMB, features a modification of the amino acid from M to L at position 306.
+The protein's natural variant, known as resistance to EMB, features a modification of the amino acid from M to V at position 306.
+The protein's natural variant, known as resistance to EMB, features a modification of the amino acid from D to G at position 328.
+The protein's natural variant, known as resistance to EMB, features a modification of the amino acid from D to Y at position 328.
+The protein's natural variant, known as resistance to EMB, features a modification of the amino acid from F to V at position 330.
+The protein's natural variant, known as resistance to EMB, features a modification of the amino acid from Y to H at position 334.
+The protein's natural variant, known as resistance to EMB, features a modification of the amino acid from G to A at position 406.
+The protein's natural variant, known as resistance to EMB, features a modification of the amino acid from G to C at position 406.
+The protein's natural variant, known as resistance to EMB, features a modification of the amino acid from G to D at position 406.
+The protein's natural variant, known as resistance to EMB, features a modification of the amino acid from Q to K at position 497.
+The protein's natural variant, known as resistance to EMB, features a modification of the amino acid from Q to R at position 497.
+The protein's natural variant, known as resistance to EMB, features a modification of the amino acid from G to D at position 745.
+The protein's natural variant, known as resistance to EMB, features a modification of the amino acid from D to A at position 959.
+The protein's natural variant, known as resistance to EMB, features a modification of the amino acid from M to R at position 1000.
+The protein's natural variant, known as resistance to EMB, features a modification of the amino acid from D to N at position 1024.
+The natural variant of this protein is characterized by an amino acid alteration from L to LPP at position 23.
+The protein's natural variant, known as may be associated with increased susceptibility to arrhythmogenic right ventricular cardiomyopathy;, features a modification of the amino acid from D to N at position 26.
+The protein's natural variant, known as in ARVD9; unknown pathological significance; decreased interaction with DSP;, features a modification of the amino acid from Q to L at position 59.
+The protein's natural variant, known as in ARVD9; unknown pathological significance; decreased protein stability; decreased interaction with DSP; does not affect subcellular location to the desmosomes;, features a modification of the amino acid from Q to K at position 62.
+The natural variant of this protein is characterized by an amino acid alteration from K to N at position 112.
+The protein's natural variant, known as in ARVD9;, features a modification of the amino acid from E to K at position 137.
+The protein's natural variant, known as in ARVD9;, features a modification of the amino acid from S to G at position 169.
+The protein's natural variant, known as in ARVD9;, features a modification of the amino acid from F to S at position 424.
+The protein's natural variant, known as in ARVD9; unknown pathological significance;, features a modification of the amino acid from G to R at position 489.
+The protein's natural variant, known as may be associated with increased susceptibility to arrhythmogenic right ventricular cardiomyopathy;, features a modification of the amino acid from V to I at position 587.
+The protein's natural variant, known as in ARVD9; impairs protein stability;, features a modification of the amino acid from S to F at position 615.
+The protein's natural variant, known as in ARVD9;, features a modification of the amino acid from Y to C at position 631.
+The protein's natural variant, known as in ARVD9; impairs protein stability;, features a modification of the amino acid from K to Q at position 654.
+The protein's natural variant, known as in ARVD9; unknown pathological significance;, features a modification of the amino acid from G to V at position 673.
+The protein's natural variant, known as in ARVD9;, features a modification of the amino acid from L to F at position 787.
+The protein's natural variant, known as in ARVD9; impairs protein stability;, features a modification of the amino acid from C to R at position 796.
+The protein's natural variant, known as in CSA;, features a modification of the amino acid from A to T at position 160.
+The protein's natural variant, known as in CSA;, features a modification of the amino acid from A to V at position 160.
+The protein's natural variant, known as in CSA;, features a modification of the amino acid from W to C at position 194.
+The protein's natural variant, known as in CSA;, features a modification of the amino acid from L to S at position 202.
+The protein's natural variant, known as in CSA;, features a modification of the amino acid from A to P at position 205.
+The protein's natural variant, known as in CSA;, features a modification of the amino acid from D to G at position 266.
+The protein's natural variant, known as in UVSS2;, features a modification of the amino acid from W to C at position 361.
+The protein's natural variant, known as in MRT41; loss of localization to F-actin-rich regions; cytoplasmic accumulation at irregular perinuclear sites, features a modification of the amino acid from M to MWSVLQ at position 241.
+The protein's natural variant, known as found in a patient diagnosed with multiple sclerosis; unknown pathological significance; decreased protein abundance; not changed aminopeptidase activity;, features a modification of the amino acid from C to G at position 28.
+The protein's natural variant, known as in IMD78; decreased protein abundance; decreased aminopeptidase activity;, features a modification of the amino acid from G to D at position 500.
+The protein's natural variant, known as found in a patient diagnosed with multiple sclerosis; unknown pathological significance;, features a modification of the amino acid from T to I at position 676.
+The protein's natural variant, known as in strain: Okinawa, features a modification of the amino acid from K to N at position 121.
+The protein's natural variant, known as in strain: PI 269818, alleles resistant-2, sbm1, eIF4E(R) and A-6. In strain: JI 1405, allele resistant-1. In strain: JI 2009, alleles susceptible and SBM1, features a modification of the amino acid from D to E at position 5.
+The protein's natural variant, known as in strain: VIR 1589, allele C-2, features a modification of the amino acid from N to I at position 19.
+The protein's natural variant, known as in strain: PI 378158, allele A-4. In strain: JI 1370, allele B-2, features a modification of the amino acid from V to A at position 23.
+The protein's natural variant, known as in strain: JI 1090, alleles B-3, features a modification of the amino acid from V to D at position 23.
+The protein's natural variant, known as in strain: JI 1845, allele S-1, features a modification of the amino acid from IEDDN to FEDDD at position 28.
+The protein's natural variant, known as in strain: PI 347492. In strain: PI 347422, ATC-6931 and PI 347484, allele S-3, features a modification of the amino acid from E to A at position 34.
+The protein's natural variant, known as in strain: JI 1010, allele S-6. In strain: JI 1007, allele S-5. In strain: JI 1090, allele B-3. In strain: JI 1370, allele B-2, features a modification of the amino acid from V to A at position 49.
+The protein's natural variant, known as in strain: Brutus, features a modification of the amino acid from N to S at position 57.
+The protein's natural variant, known as in strain: Bonneville, features a modification of the amino acid from SWTFL to PWTFW at position 62.
+The protein's natural variant, known as in strain: PI 269818, alleles resistant-2, sbm1, eIF4E(R) and A-6. In strain: JI 2009, alleles SBM1 and susceptible. In strain: Dark skinned Perfection. In strain: Brutus. In strain: JI 2643, Fjord, JI 261, JI 194, JI 205, JI 1109, JI 267, PI 505122, PI 639981, JI 1104, JI 1108, ATC-6927, ATC-7173, JI 1758, JI 1030, JI 190, PI 357290, JI 193, JI 2607, JI 2571, JI 1107, JI 1085, JI 2065, JI 1121, JI 1756, JI 182 and JI 3157, alleles S-1, eIF4E(S) and C-1. In strain: VIR 1589, allele C-2. In strain: JI 2630, allele S-1. In strain: JI 1632, allele S-4. In strain: JI 1091 and JI 3001, allele S-1. In strain: JI 1010, allele S-6. In strain: JI 1007, allele S-5. In strain: JI 2646, allele S-7. In strain: JI 1845, allele S-1. In strain: PI 347328, allele S-2. In strain: PI 347422, ATC-6931 and PI 347484, allele S-3. In strain: PI 269774, allele A-7. In strain: CGN-3302, allele A-1. In strain: JI 1194, CGN-3311, ATC-7140, ATC-3275, ATC-7134, IPK-477 and CGN-3319, allele B-1. In strain: JI 1090, allele B-3. In strain: JI 1370, allele B-2, features a modification of the amino acid from L to W at position 62.
+The protein's natural variant, known as in strain: PI 347328, allele S-2, features a modification of the amino acid from DDWGS to AAWGR at position 77.
+The protein's natural variant, known as in strain: PI 269818, alleles resistant-2, sbm1, eIF4E(R) and A-6. In strain: PI 269774, allele A-7, features a modification of the amino acid from DDWGS to PDWG at position 77.
+The protein's natural variant, known as in strain: JI 2009, alleles susceptible and SBM1. In strain: Dark skinned Perfection. In strain: Bonneville. In strain: Brutus. In strain: JI 2643, Fjord, JI 261, JI 194, JI 205, JI 1109, JI 267, PI 505122, PI 639981, JI 1104, JI 1108, ATC-6927, ATC-7173, JI 1758, JI 1030, JI 190, PI 357290, JI 193, JI 2607, JI 2571, JI 1107, JI 1085, JI 2065, JI 1121, JI 1756, JI 182 and JI 3157, alleles S-1, eIF4E(S) and C-1. In strain: VIR 1589, allele C-2. In strain: JI 2630, allele S-1. In strain: JI 1632, allele S-4. In strain: JI 1091 and JI 3001, allele S-1. In strain: JI 1010, allele S-6. In strain: JI 1007, allele S-5. In strain: JI 2646, allele S-7. In strain: JI 1845, allele S-1. In strain: PI 347422, ATC-6931 and PI 347484, allele S-3. In strain: JI 1194, CGN-3311, ATC-7140, ATC-3275, ATC-7134, IPK-477 and CGN-3319, allele B-1. In strain: JI 1090, allele B-3. In strain: JI 1370, allele B-2, features a modification of the amino acid from DD to AA at position 74.
+The protein's natural variant, known as in strain: CGN-3302, allele A-1, features a modification of the amino acid from D to V at position 73.
+The protein's natural variant, known as in strain: JI 1787, allele 1, features a modification of the amino acid from D to A at position 74.
+The protein's natural variant, known as in strain: JI 2646, allele S-7, features a modification of the amino acid from S to C at position 86.
+The protein's natural variant, known as in strain: Dark skinned Perfection, features a modification of the amino acid from VR to AG at position 107.
+The protein's natural variant, known as in strain: PI 269818, alleles resistant-2, sbm1, eIF4E(R) and A-6. In strain: JI 2009, alleles susceptible and SBM1. In strain: Bonneville. In strain: Brutus. In strain: JI 2643, Fjord, JI 261, JI 194, JI 205, JI 1109, JI 267, PI 505122, PI 639981, JI 1104, JI 1108, ATC-6927, ATC-7173, JI 1758, JI 1030, JI 190, PI 357290, JI 193, JI 2607, JI 2571, JI 1107, JI 1085, JI 2065, JI 1121, JI 1756, JI 182 and JI 3157, alleles S-1, eIF4E(S) and C-1. In strain: VIR 1589, allele C-2. In strain: JI 2630, allele S-1. In strain: JI 1632, allele S-4. In strain: JI 1091 and JI 3001, allele S-1. In strain: JI 1010, allele S-6. In strain: JI 1007, allele S-5. In strain: JI 2646, allele S-7. In strain: JI 1845, allele S-1. In strain: PI 347328, allele S-2. In strain: PI 347422, ATC-6931 and PI 347484, allele S-3. In strain: PI 269774, allele A-7. In strain: JI 1194, CGN-3311, ATC-7140, ATC-3275, ATC-7134, IPK-477 and CGN-3319, allele B-1. In strain: JI 1090, allele B-3. In strain: JI 1370, allele B-2, features a modification of the amino acid from R to G at position 107.
+The protein's natural variant, known as in strain: PI 347464, allele A-5, features a modification of the amino acid from A to P at position 108.
+The protein's natural variant, known as in strain: PI 347464, allele A-5, features a modification of the amino acid from H to R at position 115.
+The protein's natural variant, known as in strain: Dark skinned Perfection, features a modification of the amino acid from L to S at position 149.
+The protein's natural variant, known as in strain: JI 1007, allele S-5, features a modification of the amino acid from L to W at position 149.
+The protein's natural variant, known as in strain: PI 347328, allele S-2, features a modification of the amino acid from I to T at position 163.
+The protein's natural variant, known as in strain: Brutus, features a modification of the amino acid from KVR to NVG at position 171.
+The protein's natural variant, known as in strain: CGN-3302, allele A-1, features a modification of the amino acid from KV to NA at position 170.
+The protein's natural variant, known as in strain: PI 269818, alleles resistant-2, sbm1, eIF4E(R) and A-6. In strain: JI 2009, alleles susceptible and SBM1. In strain: Dark skinned Perfection. In strain: Bonneville. In strain: JI 2643, Fjord, JI 261, JI 194, JI 205, JI 1109, JI 267, PI 505122, PI 639981, JI 1104, JI 1108, ATC-6927, ATC-7173, JI 1758, JI 1030, JI 190, PI 357290, JI 193, JI 2607, JI 2571, JI 1107, JI 1085, JI 2065, JI 1121, JI 1756, JI 182 and JI 3157, alleles S-1, eIF4E(S) and C-1. In strain: VIR 1589, allele C-2. In strain: JI 2630, allele S-1. In strain: JI 1632, allele S-4. In strain: JI 1091 and JI 3001, allele S-1. In strain: JI 1010, allele S-6. In strain: JI 1007, allele S-5. In strain: JI 2646, allele S-7. In strain: JI 1845, allele S-1. In strain: PI 347328, allele S-2. In strain: PI 347422, ATC-6931 and PI 347484, allele S-3. In strain: JI 1194, CGN-3311, ATC-7140, ATC-3275, ATC-7134, IPK-477 and CGN-3319, allele B-1. In strain: JI 1090, allele B-3. In strain: JI 1370, allele B-2, features a modification of the amino acid from K to N at position 169.
+The protein's natural variant, known as in strain: JI 1546, allele A-2, features a modification of the amino acid from N to H at position 186.
+The protein's natural variant, known as in strain: Dark skinned Perfection, features a modification of the amino acid from L to P at position 201.
+The protein's natural variant, known as in strain: Dark skinned Perfection, features a modification of the amino acid from T to A at position 206.
+The protein's natural variant, known as in strain: JI 1632, allele S-4. In strain: JI 1194, CGN-3311, ATC-7140, ATC-3275, ATC-7134, IPK-477 and CGN-3319, allele B-1, features a modification of the amino acid from M to I at position 207.
+The protein's natural variant, known as in strain: JI 1532. In strain: VIR 1589, allele C-2. In strain: JI 2630, allele S-1. In strain: JI 1787, allele A-1. In strain: JI 1546, allele A-2, features a modification of the amino acid from A to S at position 215.
+The protein's natural variant, known as in strain: JI 1194, CGN-3311, ATC-7140, ATC-3275, ATC-7134, IPK-477 and CGN-3319, allele B-1, features a modification of the amino acid from LD to QE at position 219.
+The natural variant of this protein is characterized by an amino acid alteration from L to S at position 18.
+The protein's natural variant, known as in HPE12;, features a modification of the amino acid from R to C at position 535.
+The protein's natural variant, known as in VIBOS; uncertain pathological significance, features a modification of the amino acid from Q to E at position 642.
+The protein's natural variant, known as in VIBOS, features a modification of the amino acid from E to K at position 897.
+The protein's natural variant, known as in VIBOS, features a modification of the amino acid from R to C at position 900.
+The protein's natural variant, known as in VIBOS; uncertain pathological significance, features a modification of the amino acid from T to I at position 1038.
+The protein's natural variant, known as in VIBOS; uncertain pathological significance;, features a modification of the amino acid from V to L at position 1089.
+The protein's natural variant, known as in VIBOS, features a modification of the amino acid from L to P at position 1148.
+The protein's natural variant, known as in VIBOS, features a modification of the amino acid from D to G at position 1188.
+The protein's natural variant, known as in VIBOS, features a modification of the amino acid from K to R at position 1241.
+The protein's natural variant, known as in VIBOS;, features a modification of the amino acid from T to A at position 1419.
+The protein's natural variant, known as in VIBOS, features a modification of the amino acid from F to S at position 1428.
+The protein's natural variant, known as in VIBOS;, features a modification of the amino acid from R to C at position 1478.
+The protein's natural variant, known as in VIBOS, features a modification of the amino acid from Q to H at position 1494.
+The protein's natural variant, known as in VIBOS, features a modification of the amino acid from Y to D at position 1572.
+The protein's natural variant, known as in VIBOS;, features a modification of the amino acid from N to S at position 2216.
+The protein's natural variant, known as in strain: cv. Ag-0, cv. Bay-0, cv. Br-0, cv. C24, cv. Ct-1, cv. CVi-0, cv. Edi-0, cv. Ei-2, cv. Ga-0, cv. Gy-0, cv. Kas-2, cv. Ll-0, cv. Mrk-0, cv. Ms-0, cv. Mt-0, cv. Nd-1, cv. Nok-3, cv. Oy-0, cv. Sorbo, cv. Wassilewskija, cv. Wei-0 and cv. Wt-5, features a modification of the amino acid from H to D at position 411.
+The protein's natural variant, known as in strain: cv. Nd-1, features a modification of the amino acid from G to S at position 473.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from M to I at position 9.
+The protein's natural variant, known as in CMS13; strongly reduced enzyme activity;, features a modification of the amino acid from M to I at position 108.
+The protein's natural variant, known as in CMS13; mildly reduced enzyme activity;, features a modification of the amino acid from V to I at position 117.
+The protein's natural variant, known as in CMS13; strongly reduced enzyme activity;, features a modification of the amino acid from L to M at position 120.
+The protein's natural variant, known as in CMS13; increased enzyme activity;, features a modification of the amino acid from G to S at position 160.
+The protein's natural variant, known as in CDG1J; strongly reduced enzyme activity;, features a modification of the amino acid from Y to C at position 170.
+The protein's natural variant, known as in CMS13; strongly reduced enzyme activity;, features a modification of the amino acid from G to S at position 192.
+The protein's natural variant, known as in CMS13; increased enzyme activity;, features a modification of the amino acid from V to G at position 264.
+The protein's natural variant, known as in JBTS39; unknown pathological significance, features a modification of the amino acid from G to V at position 9.
+The protein's natural variant, known as in JBTS39; fails to rescue the ciliopathy phenotype in a zebrafish disease model, features a modification of the amino acid from R to S at position 37.
+The protein's natural variant, known as in JBTS39, features a modification of the amino acid from R to C at position 80.
+The protein's natural variant, known as in JBTS39, features a modification of the amino acid from R to H at position 80.
+The protein's natural variant, known as in strain: 85-736, features a modification of the amino acid from G to A at position 51.
+The protein's natural variant, known as in strain: 85-736, features a modification of the amino acid from I to V at position 63.
+The protein's natural variant, known as in allele Gov(b);, features a modification of the amino acid from Y to S at position 703.
+The natural variant of this protein is characterized by an amino acid alteration from D to G at position 791.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from Q to E at position 1007.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from N to K at position 1065.
+The protein's natural variant, known as in strain: C3H/HeJ and CBA/J, features a modification of the amino acid from P to L at position 263.
+The protein's natural variant, known as in strain: C3H/HeJ and CBA/J, features a modification of the amino acid from V to M at position 312.
+The protein's natural variant, known as in strain: C3H/HeJ and CBA/J, features a modification of the amino acid from P to S at position 330.
+The protein's natural variant, known as in strain: 240-3 / ETEC, features a modification of the amino acid from T to A at position 96.
+The protein's natural variant, known as in PILBOS;, features a modification of the amino acid from R to G at position 141.
+The protein's natural variant, known as in PILBOS;, features a modification of the amino acid from R to K at position 460.
+The protein's natural variant, known as in PILBOS; patient cells show a global increase of methylated histone binding;, features a modification of the amino acid from R to Q at position 618.
+The protein's natural variant, known as in PILBOS;, features a modification of the amino acid from R to Q at position 1708.
+The protein's natural variant, known as in strain: 4M-147, features a modification of the amino acid from E to K at position 32.
+The protein's natural variant, known as in strain: 4M-147, features a modification of the amino acid from D to S at position 39.
+The protein's natural variant, known as in strain: 4M-147, features a modification of the amino acid from V to T at position 121.
+The protein's natural variant, known as in strain: 4M-147, features a modification of the amino acid from G to A at position 233.
+The protein's natural variant, known as in strain: 4M-147, features a modification of the amino acid from C to A at position 268.
+The protein's natural variant, known as in strain: 4M-147, features a modification of the amino acid from F to W at position 273.
+The protein's natural variant, known as in strain: 4M-147, features a modification of the amino acid from A to E at position 309.
+The protein's natural variant, known as in strain: 4M-147, features a modification of the amino acid from T to S at position 316.
+The protein's natural variant, known as in strain: 4M-147, features a modification of the amino acid from C to S at position 337.
+The protein's natural variant, known as in strain: Isolate LMS_Z102, features a modification of the amino acid from V to I at position 184.
+The protein's natural variant, known as in strain: Isolate LMS_Z102, features a modification of the amino acid from P to S at position 261.
+The natural variant of this protein is characterized by an amino acid alteration from K to N at position 51.
+The protein's natural variant, known as in 33% of the molecules, features a modification of the amino acid from T to V at position 34.
+The protein's natural variant, known as in two patients with hawkinsinuria;, features a modification of the amino acid from A to T at position 33.
+The protein's natural variant, known as in TYRSN3;, features a modification of the amino acid from Y to C at position 160.
+The natural variant of this protein is characterized by an amino acid alteration from I to F at position 267.
+The protein's natural variant, known as in TYRSN3, features a modification of the amino acid from A to V at position 268.
+The protein's natural variant, known as in TYRSN3, features a modification of the amino acid from I to M at position 335.
+The protein's natural variant, known as in strain: Breinl, features a modification of the amino acid from GS to VQ at position 10.
+The protein's natural variant, known as in strain: Breinl, features a modification of the amino acid from E to Q at position 432.
+The natural variant of this protein is characterized by an amino acid alteration from Q to R at position 128.
+The natural variant of this protein is characterized by an amino acid alteration from G to S at position 302.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 354.
+The protein's natural variant, known as in PD;, features a modification of the amino acid from R to Q at position 184.
+The protein's natural variant, known as in PD;, features a modification of the amino acid from D to N at position 276.
+The protein's natural variant, known as in PD;, features a modification of the amino acid from G to D at position 278.
+The protein's natural variant, known as in PD;, features a modification of the amino acid from G to R at position 448.
+The protein's natural variant, known as associated with coronary artery disease; no effect on ligand-specificity; may increase levels of rolling and adhesion of neutrophils and peripheral blood mononuclear cells to the endothelium; may induce constitutive stimulation of the MAPK signaling pathway, in the absence of leukocyte adhesion;, features a modification of the amino acid from S to R at position 149.
+The natural variant of this protein is characterized by an amino acid alteration from P to L at position 545.
+The protein's natural variant, known as in SPG64;, features a modification of the amino acid from G to R at position 210.
+The protein's natural variant, known as in strain: 97-337, features a modification of the amino acid from V to A at position 106.
+The protein's natural variant, known as in MSSP;, features a modification of the amino acid from C to Y at position 27.
+The protein's natural variant, known as in MSSP;, features a modification of the amino acid from L to F at position 932.
+The protein's natural variant, known as found in a consanguineous family with intellectual disability; unknown pathological significance;, features a modification of the amino acid from Y to C at position 228.
+The protein's natural variant, known as in strain: Isolate SNP-2, features a modification of the amino acid from I to V at position 14.
+The protein's natural variant, known as in strain: Isolate SNP-2, features a modification of the amino acid from M to T at position 60.
+The protein's natural variant, known as in strain: Isolate SNP-2, features a modification of the amino acid from T to A at position 67.
+The protein's natural variant, known as in strain: Isolate SNP-2, features a modification of the amino acid from M to L at position 102.
+The protein's natural variant, known as in strain: Isolate SNP-2, features a modification of the amino acid from MI to LV at position 238.
+The protein's natural variant, known as found in a patient with autosomal recessive microcytic hypochromic anemia and increased fetal hemoglobin; unknown pathological significance; no effect on protein abundance; no effect on protein localization; decreased transcriptional activity;, features a modification of the amino acid from A to P at position 298.
+The protein's natural variant, known as in blood group-In(Lu);, features a modification of the amino acid from H to Y at position 299.
+The natural variant of this protein is characterized by an amino acid alteration from C to W at position 316.
+The protein's natural variant, known as in CDAN4; has a dominant-negative effect on the transcriptional activation of CD44 and AQP1 promoters;, features a modification of the amino acid from E to K at position 325.
+The protein's natural variant, known as in blood group-In(Lu);, features a modification of the amino acid from R to H at position 328.
+The protein's natural variant, known as in blood group-In(Lu), features a modification of the amino acid from R to L at position 328.
+The protein's natural variant, known as in blood group-In(Lu), features a modification of the amino acid from R to G at position 331.
+The protein's natural variant, known as found in a patient with autosomal recessive microcytic hypochromic anemia and increased fetal hemoglobin; with microcytic hypochromic anemia; no effect on protein abundance; no effect on protein localization; decreased transcriptional activity;, features a modification of the amino acid from P to S at position 338.
+The protein's natural variant, known as in strain: B, features a modification of the amino acid from V to L at position 103.
+The protein's natural variant, known as in mycophenolic acid resistant cells, features a modification of the amino acid from T to I at position 333.
+The protein's natural variant, known as in mycophenolic acid resistant cells, features a modification of the amino acid from S to Y at position 351.
+The protein's natural variant, known as may contribute to insulin resistance by impairing metabolic signaling through PI3K-dependent pathways;, features a modification of the amino acid from T to R at position 608.
+The protein's natural variant, known as in T2D, features a modification of the amino acid from S to Y at position 1043.
+The protein's natural variant, known as in T2D, features a modification of the amino acid from C to Y at position 1095.
+The protein's natural variant, known as in strain: NBD and Qingdao, features a modification of the amino acid from G to D at position 33.
+The protein's natural variant, known as in strain: Isolate Emyo384, features a modification of the amino acid from T to A at position 334.
+The protein's natural variant, known as in NPHLOP2; impairs the interaction with SLC34A1; causes a reduction of SLC34A1 amount on cell membrane and affects SLC34A1-dependent phosphate uptake;, features a modification of the amino acid from E to A at position 68.
+The protein's natural variant, known as in NPHLOP2; the mutant expressed in cultured renal cells increases the generation of cyclic AMP (cAMP) by parathyroid hormone (PTH) and inhibits phosphate transport;, features a modification of the amino acid from L to V at position 110.
+The protein's natural variant, known as in NPHLOP2; the mutant expressed in cultured renal cells increases the generation of cAMP by PTH and inhibits phosphate transport;, features a modification of the amino acid from R to Q at position 153.
+The protein's natural variant, known as in NPHLOP2; the mutant expressed in cultured renal cells increases the generation of cAMP by PTH and inhibits phosphate transport;, features a modification of the amino acid from E to K at position 225.
+The protein's natural variant, known as in KEFH; does not affect ability to homooligomerize into ordered polymers;, features a modification of the amino acid from D to H at position 21.
+The protein's natural variant, known as in CINCA;, features a modification of the amino acid from I to T at position 174.
+The protein's natural variant, known as in FCAS1 and MWS;, features a modification of the amino acid from V to M at position 200.
+The protein's natural variant, known as in CINCA;, features a modification of the amino acid from R to L at position 262.
+The protein's natural variant, known as in CINCA;, features a modification of the amino acid from R to P at position 262.
+The protein's natural variant, known as in FCAS1 and MWS; spontaneous polymerization into inflammasome speck;, features a modification of the amino acid from R to W at position 262.
+The protein's natural variant, known as in CINCA;, features a modification of the amino acid from L to H at position 266.
+The protein's natural variant, known as in CINCA;, features a modification of the amino acid from D to G at position 305.
+The protein's natural variant, known as in CINCA and MWS; spontaneous polymerization into inflammasome speck;, features a modification of the amino acid from D to N at position 305.
+The protein's natural variant, known as in FCAS1 and MWS;, features a modification of the amino acid from L to P at position 307.
+The protein's natural variant, known as in CINCA;, features a modification of the amino acid from Q to K at position 308.
+The protein's natural variant, known as in CINCA;, features a modification of the amino acid from F to S at position 311.
+The protein's natural variant, known as in MWS and CINCA; spontaneous polymerization into inflammasome speck;, features a modification of the amino acid from T to M at position 350.
+The protein's natural variant, known as in MWS;, features a modification of the amino acid from A to V at position 354.
+The protein's natural variant, known as in FCAS1;, features a modification of the amino acid from L to P at position 355.
+The protein's natural variant, known as in CINCA;, features a modification of the amino acid from E to D at position 356.
+The protein's natural variant, known as in CINCA;, features a modification of the amino acid from H to R at position 360.
+The protein's natural variant, known as in CINCA;, features a modification of the amino acid from T to P at position 407.
+The protein's natural variant, known as in CINCA;, features a modification of the amino acid from T to I at position 438.
+The protein's natural variant, known as in CINCA;, features a modification of the amino acid from T to N at position 438.
+The protein's natural variant, known as in MWS;, features a modification of the amino acid from A to T at position 441.
+The protein's natural variant, known as in FCAS1;, features a modification of the amino acid from A to V at position 441.
+The protein's natural variant, known as in FCAS1;, features a modification of the amino acid from R to K at position 490.
+The protein's natural variant, known as in FCAS1;, features a modification of the amino acid from F to C at position 525.
+The protein's natural variant, known as in CINCA;, features a modification of the amino acid from F to L at position 525.
+The protein's natural variant, known as in MWS;, features a modification of the amino acid from G to R at position 571.
+The protein's natural variant, known as in CINCA;, features a modification of the amino acid from Y to C at position 572.
+The protein's natural variant, known as in CINCA;, features a modification of the amino acid from F to S at position 575.
+The protein's natural variant, known as in FCAS1;, features a modification of the amino acid from E to G at position 629.
+The protein's natural variant, known as in CINCA;, features a modification of the amino acid from L to F at position 634.
+The protein's natural variant, known as in CINCA;, features a modification of the amino acid from M to T at position 664.
+The protein's natural variant, known as in CINCA;, features a modification of the amino acid from Y to C at position 861.
+The protein's natural variant, known as in DFNA34; unknown pathological significance; increases inflammatory response;, features a modification of the amino acid from R to Q at position 920.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from G to S at position 214.
+The protein's natural variant, known as moderate reduction of enzymatic activity;, features a modification of the amino acid from Q to P at position 19.
+The protein's natural variant, known as may be a risk factor for schizophrenia; moderate reduction of enzymatic activity;, features a modification of the amino acid from A to V at position 167.
+The protein's natural variant, known as mild decrease of enzymatic activity;, features a modification of the amino acid from R to Q at position 185.
+The protein's natural variant, known as moderate reduction of enzymatic activity;, features a modification of the amino acid from R to W at position 185.
+The protein's natural variant, known as in HYRPRO1; mild decrease of enzymatic activity;, features a modification of the amino acid from L to M at position 289.
+The protein's natural variant, known as in SCZD4; may be associated with disease susceptibility; strongly reduced enzymatic activity;, features a modification of the amino acid from P to L at position 406.
+The protein's natural variant, known as in HYRPRO1; moderate reduction of enzymatic activity, features a modification of the amino acid from D to N at position 426.
+The protein's natural variant, known as in HYRPRO1 and SCZD4; may be associated with disease susceptibility; moderate reduction of enzymatic activity;, features a modification of the amino acid from V to M at position 427.
+The protein's natural variant, known as in HYRPRO1; moderate reduction of enzymatic activity;, features a modification of the amino acid from R to H at position 431.
+The protein's natural variant, known as in HYRPRO1 and SCZD4; may be associated with disease susceptibility; strongly reduced enzymatic activity;, features a modification of the amino acid from L to P at position 441.
+The protein's natural variant, known as in HYRPRO1 and SCZD4; may be associated with disease susceptibility; strongly reduced enzymatic activity;, features a modification of the amino acid from R to C at position 453.
+The protein's natural variant, known as in HYRPRO1; mild decrease of enzymatic activity;, features a modification of the amino acid from A to S at position 455.
+The protein's natural variant, known as in SCZD4; may be associated with disease susceptibility; strongly reduced affinity for FAD; strongly reduced enzymatic activity;, features a modification of the amino acid from T to M at position 466.
+The protein's natural variant, known as in HYRPRO1 and SCZD4; associated with disease susceptibility; mild decrease of enzymatic activity;, features a modification of the amino acid from A to T at position 472.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from N to S at position 488.
+The protein's natural variant, known as strongly reduced enzymatic activity;, features a modification of the amino acid from Q to E at position 521.
+The protein's natural variant, known as in HYRPRO1 and SCZD4; may be associated with disease susceptibility; enhanced enzymatic activity;, features a modification of the amino acid from Q to R at position 521.
+The protein's natural variant, known as in strain: C57BL/6J; could be associated with tumor susceptibility; does not affect binding with tubulin; more unstable, features a modification of the amino acid from N to S at position 60.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from A to V at position 272.
+The protein's natural variant, known as in MNLIX;, features a modification of the amino acid from N to D at position 114.
+The protein's natural variant, known as in MNLIX;, features a modification of the amino acid from N to H at position 114.
+The protein's natural variant, known as in MNLIX;, features a modification of the amino acid from E to K at position 402.
+The protein's natural variant, known as in MNLIX;, features a modification of the amino acid from E to Q at position 402.
+The protein's natural variant, known as in MNLIX, features a modification of the amino acid from L to P at position 409.
+The protein's natural variant, known as in MNLIX, features a modification of the amino acid from L to P at position 410.
+The protein's natural variant, known as in MNLIX;, features a modification of the amino acid from E to D at position 413.
+The protein's natural variant, known as in MNLIX;, features a modification of the amino acid from E to K at position 413.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from P to L at position 68.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from E to Q at position 143.
+The natural variant of this protein is characterized by an amino acid alteration from Q to E at position 479.
+The protein's natural variant, known as in strain: O22, features a modification of the amino acid from V to M at position 133.
+The protein's natural variant, known as in strain: O22 and MO45, features a modification of the amino acid from G to D at position 242.
+The protein's natural variant, known as in RJALS; impaired metalloprotease activity and ability to cleave covalent DNA-protein cross-links (DPCs); cells are completely unable to restore DNA replication fork progression;, features a modification of the amino acid from Y to C at position 117.
+The protein's natural variant, known as in IMD87; affects function in vesicle-mediated protein transport as shown by impaired CTLA4 trafficking to cell surface in homozygous patient T cells; severely decreased protein levels in patient T cells; increased protein degradation, features a modification of the amino acid from Y to D at position 210.
+The protein's natural variant, known as in IMD87; affects function in vesicle-mediated protein transport as shown by impaired CTLA4 trafficking to cell surface in homozygous patient T cells; decreased interaction with RAB11A;, features a modification of the amino acid from E to K at position 331.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 191.
+The protein's natural variant, known as in CFC3;, features a modification of the amino acid from F to S at position 53.
+The protein's natural variant, known as in MEL; somatic mutation;, features a modification of the amino acid from Q to P at position 56.
+The protein's natural variant, known as in MEL; somatic mutation;, features a modification of the amino acid from K to E at position 57.
+The protein's natural variant, known as in MEL; somatic mutation; results in increased MAPK signal transduction;, features a modification of the amino acid from K to N at position 57.
+The protein's natural variant, known as in CFC3;, features a modification of the amino acid from G to V at position 128.
+The protein's natural variant, known as in CFC3;, features a modification of the amino acid from Y to C at position 130.
+The protein's natural variant, known as in strain: PAC174, features a modification of the amino acid from D to E at position 46.
+The protein's natural variant, known as in strain: PAC174, features a modification of the amino acid from K to R at position 55.
+The protein's natural variant, known as in strain: PAC174, features a modification of the amino acid from Q to R at position 115.
+The protein's natural variant, known as in strain: PAC174, features a modification of the amino acid from P to S at position 163.
+The protein's natural variant, known as in strain: PAC174, features a modification of the amino acid from V to L at position 170.
+The protein's natural variant, known as in strain: PAC174, features a modification of the amino acid from A to S at position 181.
+The protein's natural variant, known as in strain: PAC174, features a modification of the amino acid from WA to S at position 207.
+The protein's natural variant, known as in NEDBAS; unknown pathological significance, features a modification of the amino acid from Q to QIGGQ at position 18.
+The protein's natural variant, known as in NEDBAS, features a modification of the amino acid from C to F at position 179.
+The protein's natural variant, known as in an ovarian clear cell carcinoma sample; somatic mutation, features a modification of the amino acid from V to L at position 60.
+The natural variant of this protein is characterized by an amino acid alteration from H to R at position 20.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from R to H at position 269.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from G to R at position 271.
+The protein's natural variant, known as in IFN-tau6A and IFN-tau6B, features a modification of the amino acid from K to E at position 130.
+The protein's natural variant, known as in IFN-tau6A, IFN-tau6B and IFN-tau6C, features a modification of the amino acid from K to N at position 136.
+The protein's natural variant, known as in IFN-tau6A, features a modification of the amino acid from T to M at position 188.
+The natural variant of this protein is characterized by an amino acid alteration from P to L at position 218.
+The protein's natural variant, known as homozygous in a thrombopathic calf; heterozygous in other calves, features a modification of the amino acid from L to P at position 234.
+The protein's natural variant, known as in strain: DI7, KY038 and Loua, features a modification of the amino acid from F to L at position 9.
+The protein's natural variant, known as in strain: DI7, Loua and S30, features a modification of the amino acid from V to A at position 36.
+The protein's natural variant, known as in strain: DI7, Loua, Monty5, Tahiti and ZW141, features a modification of the amino acid from S to A at position 113.
+The protein's natural variant, known as in SMDP2; targeted abnormally to early endosomes and likely to result in a toxic gain of function;, features a modification of the amino acid from E to K at position 66.
+The protein's natural variant, known as in SMDP2; abnormal trafficking and accumulation of aberrantly processed proSPC within alveoli;, features a modification of the amino acid from I to T at position 73.
+The protein's natural variant, known as in SMDP2;, features a modification of the amino acid from A to D at position 116.
+The protein's natural variant, known as influences susceptibility to RDS in premature infants;, features a modification of the amino acid from N to T at position 138.
+The protein's natural variant, known as in SMDP2;, features a modification of the amino acid from R to Q at position 167.
+The protein's natural variant, known as influences susceptibility to RDS in premature infants;, features a modification of the amino acid from N to S at position 186.
+The protein's natural variant, known as in SMDP2;, features a modification of the amino acid from L to Q at position 188.
+The protein's natural variant, known as in RRS1, features a modification of the amino acid from C to Y at position 182.
+The protein's natural variant, known as in RRS1;, features a modification of the amino acid from R to C at position 184.
+The protein's natural variant, known as in RRS1;, features a modification of the amino acid from R to W at position 189.
+The protein's natural variant, known as in RRS1, features a modification of the amino acid from R to W at position 366.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from V to M at position 542.
+The protein's natural variant, known as in RRS1, features a modification of the amino acid from N to K at position 620.
+The protein's natural variant, known as loss of acetylation; localization primarily within the cytoplasm; increased likelihood of existing as monomer; stronger binding to XPO1/CRM1;, features a modification of the amino acid from K to E at position 129.
+The protein's natural variant, known as in allele MC1R*2 and strain Jeju native black, features a modification of the amino acid from V to M at position 95.
+The protein's natural variant, known as in allele MC1R*2 and strain Jeju native black; may form a constitutively active receptor, features a modification of the amino acid from L to P at position 102.
+The protein's natural variant, known as in allele MC1R*3, features a modification of the amino acid from D to N at position 124.
+The protein's natural variant, known as in allele MC1R*4, features a modification of the amino acid from A to V at position 164.
+The protein's natural variant, known as in strain: Jeju native black, features a modification of the amino acid from L to M at position 192.
+The protein's natural variant, known as in strain: Jeju native black, features a modification of the amino acid from M to V at position 213.
+The protein's natural variant, known as in allele MC1R*4, features a modification of the amino acid from A to T at position 243.
+The protein's natural variant, known as in CTRCT22; unknown pathological significance;, features a modification of the amino acid from R to H at position 75.
+The protein's natural variant, known as in CTRCT22;, features a modification of the amino acid from G to R at position 165.
+The protein's natural variant, known as in CTRCT22;, features a modification of the amino acid from V to E at position 194.
+The protein's natural variant, known as in scnA", features a modification of the amino acid from T to E at position 2.
+The protein's natural variant, known as in scnA", features a modification of the amino acid from EH to NN at position 5.
+The protein's natural variant, known as in scnA", features a modification of the amino acid from I to V at position 7.
+The protein's natural variant, known as found in a patient with childhood-onset nephrotic syndrome, focal segmental glomerulosclerosis and end-stage renal disease; unknown pathological significance;, features a modification of the amino acid from A to D at position 44.
+The protein's natural variant, known as found in a patient with childhood-onset steroid-resistant nephrotic syndrome; unknown pathological significance, features a modification of the amino acid from A to T at position 156.
+The protein's natural variant, known as found in a patient with nephrotic syndrome also carrying mutation P-159 in MYO1E;, features a modification of the amino acid from E to K at position 181.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from K to R at position 242.
+The protein's natural variant, known as in IDDSSBA; loss of function;, features a modification of the amino acid from R to Q at position 335.
+The protein's natural variant, known as in IDDSSBA; loss of function;, features a modification of the amino acid from T to M at position 357.
+The protein's natural variant, known as in strain: 129/J, features a modification of the amino acid from N to D at position 244.
+The protein's natural variant, known as in strain: 129/J, features a modification of the amino acid from D to A at position 281.
+The protein's natural variant, known as in strain: 129/J, features a modification of the amino acid from NIPNVS to YITNVP at position 314.
+The protein's natural variant, known as in strain: 129/J, features a modification of the amino acid from M to T at position 347.
+The protein's natural variant, known as in strain: 129/J, features a modification of the amino acid from H to Y at position 418.
+The protein's natural variant, known as in strain: 129/J, features a modification of the amino acid from K to N at position 443.
+The protein's natural variant, known as in strain: 129/J, features a modification of the amino acid from K to E at position 626.
+The natural variant of this protein is characterized by an amino acid alteration from V to M at position 221.
+The natural variant of this protein is characterized by an amino acid alteration from TT to NE at position 224.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from S to C at position 687.
+The protein's natural variant, known as in lrp-1 mutant, features a modification of the amino acid from D to E at position 114.
+The protein's natural variant, known as in MYP25;, features a modification of the amino acid from Q to R at position 140.
+The protein's natural variant, known as in MYP25; unknown pathological significance;, features a modification of the amino acid from I to V at position 150.
+The protein's natural variant, known as in MYP25; decreases protein abundance;, features a modification of the amino acid from E to K at position 291.
+The protein's natural variant, known as in strain: ATCC 33430, features a modification of the amino acid from G to V at position 33.
+The protein's natural variant, known as in strain: ATCC 33430, features a modification of the amino acid from W to M at position 56.
+The protein's natural variant, known as found in 15 autistic individuals, decreased expression at the cell surface; increased affinity for serotonin; increased serotonin transport capacity; loss of regulation through cGMP and MAP kinases pathways; hypoplasia of the enteric nervous system and decreased gastrointestinal peristaltic reflexes shown by a mouse knockin model of the mutation;, features a modification of the amino acid from G to A at position 56.
+The protein's natural variant, known as found in 2 autistic individuals; increased affinity for serotonin; increased serotonin transport rate;, features a modification of the amino acid from I to L at position 425.
+The protein's natural variant, known as linked with susceptibility to obsessive-compulsive disorder; increased serotonin transport capacity;, features a modification of the amino acid from I to V at position 425.
+The protein's natural variant, known as found in 2 autistic individuals; increased expression at the cell surface; increased affinity for serotonin;, features a modification of the amino acid from F to L at position 465.
+The protein's natural variant, known as found in 2 autistic individuals; increased expression at the cell surface; increased affinity for serotonin;, features a modification of the amino acid from L to V at position 550.
+The protein's natural variant, known as in BROVCA3;, features a modification of the amino acid from G to V at position 125.
+The protein's natural variant, known as in BROVCA3; reduces interaction with BRCA2 and to a lesser extent with PALB2 and RAD51;, features a modification of the amino acid from L to F at position 138.
+The protein's natural variant, known as reduces interaction with BRCA2 and to a lesser extent with PALB2 and RAD51, features a modification of the amino acid from D to N at position 159.
+The protein's natural variant, known as in BROVCA3;, features a modification of the amino acid from G to E at position 162.
+The protein's natural variant, known as in BROVCA3, features a modification of the amino acid from Q to P at position 178.
+The protein's natural variant, known as in FANCO; possibly hypomorphic allele; reduces interaction with BRCA2 and to a lesser extent with PALB2 and RAD51;, features a modification of the amino acid from R to H at position 258.
+The protein's natural variant, known as in BROVCA3;, features a modification of the amino acid from T to A at position 287.
+The protein's natural variant, known as abolishes TEA transport activity. Decreases plasma membrane localization, features a modification of the amino acid from K to N at position 64.
+The protein's natural variant, known as abolishes plasma membrane localization, features a modification of the amino acid from G to V at position 247.
+The natural variant of this protein is characterized by an amino acid alteration from P to A at position 40.
+The natural variant of this protein is characterized by an amino acid alteration from I to T at position 252.
+The protein's natural variant, known as in Sprague-Dawley males; could be unrelated to gender, features a modification of the amino acid from GM to AR at position 120.
+The protein's natural variant, known as in Sprague-Dawley males; could be unrelated to gender, features a modification of the amino acid from A to T at position 649.
+The protein's natural variant, known as in Sprague-Dawley males; could be unrelated to gender, features a modification of the amino acid from F to L at position 1276.
+The protein's natural variant, known as in Sprague-Dawley males; could be unrelated to gender, features a modification of the amino acid from T to R at position 1315.
+The natural variant of this protein is characterized by an amino acid alteration from S to W at position 97.
+The protein's natural variant, known as in DMJDS1; unknown pathological significance;, features a modification of the amino acid from S to I at position 147.
+The protein's natural variant, known as in DMJDS1; unknown pathological significance;, features a modification of the amino acid from I to N at position 332.
+The protein's natural variant, known as in DMJDS1; unknown pathological significance;, features a modification of the amino acid from G to S at position 1091.
+The protein's natural variant, known as in NEDHYBA, features a modification of the amino acid from Y to C at position 85.
+The protein's natural variant, known as in NEDHYBA;, features a modification of the amino acid from I to T at position 252.
+The protein's natural variant, known as in NEDHYBA, features a modification of the amino acid from V to A at position 324.
+The protein's natural variant, known as in NEDHYBA; unknown pathological significance;, features a modification of the amino acid from A to V at position 413.
+The protein's natural variant, known as in NEDHYBA, features a modification of the amino acid from S to R at position 453.
+The protein's natural variant, known as in NEDHYBA;, features a modification of the amino acid from T to I at position 570.
+The protein's natural variant, known as in NEDHYBA, features a modification of the amino acid from I to T at position 607.
+The protein's natural variant, known as in NEDHYBA, features a modification of the amino acid from V to A at position 772.
+The protein's natural variant, known as in strain: Horst 97, features a modification of the amino acid from I to L at position 9.
+The protein's natural variant, known as in strain: Horst 97, features a modification of the amino acid from T to I at position 11.
+The protein's natural variant, known as in strain: Horst 97, features a modification of the amino acid from V to L at position 49.
+The protein's natural variant, known as in strain: Horst 97, features a modification of the amino acid from D to E at position 51.
+The protein's natural variant, known as in strain: Horst 97, features a modification of the amino acid from V to I at position 84.
+The natural variant of this protein is characterized by an amino acid alteration from G to R at position 666.
+The protein's natural variant, known as in strain: F98, features a modification of the amino acid from Q to H at position 125.
+The protein's natural variant, known as in strain: Canton-S, features a modification of the amino acid from FE to VQ at position 177.
+The protein's natural variant, known as or in position 7, in a common allele, features a modification of the amino acid from E to G at position 7.
+The protein's natural variant, known as in Nv1-9, features a modification of the amino acid from V to A at position 9.
+The protein's natural variant, known as in ILFS3;, features a modification of the amino acid from A to T at position 368.
+The protein's natural variant, known as in ILFS3;, features a modification of the amino acid from L to P at position 370.
+The protein's natural variant, known as in MC1DN22;, features a modification of the amino acid from Q to R at position 142.
+The protein's natural variant, known as in MC1DN22; unknown pathological significance;, features a modification of the amino acid from L to P at position 294.
+The protein's natural variant, known as in strain: CLIB 410, features a modification of the amino acid from IADSEEFGL to LPIPKNSAW at position 27.
+The protein's natural variant, known as in SEMDAG; creates a functional N-glycosylation site; does not adversely affect protein trafficking and secretion;, features a modification of the amino acid from D to N at position 2381.
+The protein's natural variant, known as in SSOAOD;, features a modification of the amino acid from V to M at position 2418.
+The protein's natural variant, known as in HDR;, features a modification of the amino acid from W to R at position 274.
+The protein's natural variant, known as in HDR; loss of enhancer activity on PTH gene promoter and on GATA responsive element, features a modification of the amino acid from R to Q at position 298.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from R to L at position 366.
+The protein's natural variant, known as in strain: NRRL 35600, features a modification of the amino acid from R to S at position 7.
+The protein's natural variant, known as in strain: NRRL 35600, features a modification of the amino acid from D to G at position 435.
+The protein's natural variant, known as in Nv1-15, features a modification of the amino acid from S to L at position 3.
+The protein's natural variant, known as in Nv1-17 and in Nv1-18, features a modification of the amino acid from K to N at position 5.
+The protein's natural variant, known as in Nv1-5, Nv8/Nv19 and Nv1-15, features a modification of the amino acid from V to A at position 9.
+The protein's natural variant, known as in Nv1-15, features a modification of the amino acid from L to V at position 13.
+The protein's natural variant, known as in Nv1-2, Nv1-13, features a modification of the amino acid from C to S at position 19.
+The protein's natural variant, known as in Nv1-13, features a modification of the amino acid from D to T at position 29.
+The protein's natural variant, known as in Nv1-4, Nv8/Nv19, features a modification of the amino acid from F to Y at position 33.
+The protein's natural variant, known as in Nv1-18, features a modification of the amino acid from A to V at position 43.
+The protein's natural variant, known as in Nv1-4, features a modification of the amino acid from M to V at position 62.
+The protein's natural variant, known as in Nv1-13, features a modification of the amino acid from I to V at position 78.
+The protein's natural variant, known as decreases double-stranded DNA break-initiated homologous recombination;, features a modification of the amino acid from K to R at position 18.
+The protein's natural variant, known as abrogates the interaction with BRCA1; decreases double-stranded DNA break-initiated homologous recombination; reduces PALB2 and RAD51 localization to ionizing radiation-induced foci; may weaken homooligomerization;, features a modification of the amino acid from Y to C at position 28.
+The protein's natural variant, known as in BC; abrogates the interaction with BRCA1; abrogates double-stranded DNA break-initiated homologous recombination; abrogates PALB2 and RAD51 localization to ionizing radiation-induced foci; may weaken homooligomerization;, features a modification of the amino acid from L to P at position 35.
+The protein's natural variant, known as decreases double-stranded DNA break-initiated homologous recombination;, features a modification of the amino acid from R to H at position 37.
+The natural variant of this protein is characterized by an amino acid alteration from H to Y at position 46.
+The natural variant of this protein is characterized by an amino acid alteration from F to L at position 728.
+The protein's natural variant, known as may be associated with breast cancer susceptibility; reduces interaction with BRCA2, RAD51 and XRCC3; decreases double-stranded DNA break-initiated homologous recombination; increases sensitivity to IR;, features a modification of the amino acid from L to W at position 939.
+The protein's natural variant, known as may be associated with breast cancer susceptibility;, features a modification of the amino acid from G to E at position 998.
+The protein's natural variant, known as may be associated with breast cancer susceptibility; reduces interaction with BRCA2, RAD51C, RAD51 and XRCC3; decreases double-stranded DNA break-initiated homologous recombination; increases sensitivity to IR;, features a modification of the amino acid from G to A at position 1043.
+The natural variant of this protein is characterized by an amino acid alteration from S to G at position 1075.
+The natural variant of this protein is characterized by an amino acid alteration from V to A at position 1105.
+The protein's natural variant, known as may be associated with breast cancer susceptibility;, features a modification of the amino acid from L to P at position 1143.
+The protein's natural variant, known as in IDDILF, features a modification of the amino acid from H to R at position 372.
+The protein's natural variant, known as in IDDILF; decreased P-body assembly; decreased interaction with LSM14A; decreased interaction with LSM14B; decreased interaction with EIF4ENIF1/4E-T; decreased interaction with PATL1, features a modification of the amino acid from R to Q at position 373.
+The protein's natural variant, known as in IDDILF; decreased P-body assembly; decreased interaction with LSM14A; decreased interaction with LSM14B; decreased interaction with EIF4ENIF1/4E-T, features a modification of the amino acid from C to R at position 390.
+The protein's natural variant, known as in IDDILF; decreased P-body assembly, features a modification of the amino acid from T to I at position 391.
+The protein's natural variant, known as in IDDILF; decreased P-body assembly, features a modification of the amino acid from T to P at position 391.
+The protein's natural variant, known as in CAKUT1; unknown pathological significance;, features a modification of the amino acid from R to Q at position 29.
+The protein's natural variant, known as in CAKUT1, features a modification of the amino acid from D to G at position 200.
+The protein's natural variant, known as in CAKUT1;, features a modification of the amino acid from S to L at position 843.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from M to T at position 265.
+The protein's natural variant, known as in PGK1D; with congenital non-spherocytic anemia; variant Matsue;, features a modification of the amino acid from L to P at position 88.
+The protein's natural variant, known as in PGK1D; with chronic hemolytic anemia; variant Shizuoka;, features a modification of the amino acid from G to V at position 158.
+The protein's natural variant, known as in PGK1D; with chronic hemolytic anemia and intellectual disability; variant Amiens;, features a modification of the amino acid from D to V at position 164.
+The protein's natural variant, known as in PGK1D; with chronic hemolytic anemia; variant Uppsala;, features a modification of the amino acid from R to P at position 206.
+The protein's natural variant, known as in PGK1D; with chronic hemolytic anemia; variant Antwerp, features a modification of the amino acid from E to A at position 252.
+The protein's natural variant, known as in PGK1D; with chronic non-spherocytic hemolytic anemia; variant Tokyo;, features a modification of the amino acid from V to M at position 266.
+The protein's natural variant, known as in Munchen; 21% of activity;, features a modification of the amino acid from D to N at position 268.
+The protein's natural variant, known as in PGK1D; with chronic hemolytic anemia; variant Herlev; 50% of activity;, features a modification of the amino acid from D to V at position 285.
+The protein's natural variant, known as in PGK1D; with rhabdomyolysis; variant Creteil, features a modification of the amino acid from D to N at position 315.
+The protein's natural variant, known as in PGK1D; with chronic hemolytic anemia; variant Michigan;, features a modification of the amino acid from C to R at position 316.
+The protein's natural variant, known as in DKCA3;, features a modification of the amino acid from K to E at position 280.
+The protein's natural variant, known as in DKCA3 and DKCA5;, features a modification of the amino acid from R to H at position 282.
+The protein's natural variant, known as in DKCA3;, features a modification of the amino acid from R to S at position 282.
+The protein's natural variant, known as in NBIA4;, features a modification of the amino acid from T to M at position 11.
+The protein's natural variant, known as in NBIA4;, features a modification of the amino acid from S to F at position 39.
+The protein's natural variant, known as in NBIA4, features a modification of the amino acid from A to P at position 48.
+The protein's natural variant, known as in NBIA4;, features a modification of the amino acid from G to R at position 53.
+The protein's natural variant, known as in NBIA4; predominantly cytosolic distribution with a localization also seen in the mitochondrial matrix; no cytosolic redistribution seen in response to oxidative stress; patient fibroblasts accumulate high levels of mitochondrial calcium and are more prone to oxidative stress-induced apoptosis;, features a modification of the amino acid from G to S at position 58.
+The protein's natural variant, known as in NBIA4;, features a modification of the amino acid from P to L at position 60.
+The protein's natural variant, known as in NBIA4 and SPG43; impairs subcellular localization to the endoplasmic reticulum or mitochondrion;, features a modification of the amino acid from A to P at position 63.
+The protein's natural variant, known as in NBIA4;, features a modification of the amino acid from G to E at position 65.
+The protein's natural variant, known as in NBIA4;, features a modification of the amino acid from G to V at position 65.
+The protein's natural variant, known as in NBIA4; impairs subcellular localization to the endoplasmic reticulum or mitochondrion;, features a modification of the amino acid from G to R at position 69.
+The protein's natural variant, known as in NBIA4;, features a modification of the amino acid from P to L at position 83.
+The protein's natural variant, known as in NBIA4; no effect on its subcellular localization; no cytosolic redistribution seen in response to oxidative stress, features a modification of the amino acid from Q to P at position 96.
+The protein's natural variant, known as in NBIA4;, features a modification of the amino acid from R to S at position 98.
+The protein's natural variant, known as in NBIA4, features a modification of the amino acid from L to Q at position 121.
+The protein's natural variant, known as in NBIA4; unknown pathological significance;, features a modification of the amino acid from A to P at position 134.
+The protein's natural variant, known as found in families with neurodegeneration with brain iron accumulation; uncertain pathological significance;, features a modification of the amino acid from K to E at position 142.
+The protein's natural variant, known as in strain: NEM318, features a modification of the amino acid from R to A at position 68.
+The protein's natural variant, known as in strain: ATCC 12403, features a modification of the amino acid from N to D at position 104.
+The protein's natural variant, known as in allele KIR2DS5*001; not expressed at the cell surface when associated with P-132, S-185 and A-195 in allele KIR2DS5*001; no effect cell surface expression, features a modification of the amino acid from S to L at position 2.
+The protein's natural variant, known as in allele KIR2DS5*008; increases binding to C2 epitopes of HLA-C alleles when associated with G-179 in allele KIR2DS5*008, features a modification of the amino acid from H to R at position 22.
+The protein's natural variant, known as in allele KIR2DS5*001; not expressed at the cell surface when associated with R-22, S-185 and A-195 in allele KIR2DS5*001; abolishes cell surface expression, features a modification of the amino acid from S to P at position 132.
+The protein's natural variant, known as in allele KIR2DS5*003; increases cell surface expression, glycosylation levels and binding to C2 epitopes of HLA-C alleles when associated with G-179 in allele KIR2DS5*003, features a modification of the amino acid from S to N at position 144.
+The protein's natural variant, known as in allele KIR2DS5*010; decreases binding to C2 epitopes of HLA-C alleles when associated with G-179 and H-203 in allele KIR2DS5*010, features a modification of the amino acid from S to F at position 148.
+The protein's natural variant, known as in alleles KIR2DS5*006 and KIR2DS5*011; increases binding to C2 epitopes of HLA-C alleles when associated with G-179 in allele KIR2DS5*006; decreases binding to C2 epitopes of HLA-C alleles when associated with T-197 in allele KIR2DS5*011, features a modification of the amino acid from P to T at position 175.
+The protein's natural variant, known as in alleles KIR2DS5*003, KIR2DS5*004, KIR2DS5*005, KIR2DS5*006, KIR2DS5*007, KIR2DS5*008 and KIR2DS5*010; increases binding to C2 epitopes of HLA-C alleles in allele KIR2DS5*005; increases binding to C2 epitopes of HLA-C alleles but no effect on cell surface expression when associated with R-22 in allele KIR2DS5*008; increases cell surface expression, glycosylation levels and binding to C2 epitopes of HLA-C alleles when associated with N-144 in allele KIR2DS5*003; decreases binding to C2 epitopes of HLA-C alleles when associated with F-148 and H-203 in allele KIR2DS5*010; increases binding to C2 epitopes of HLA-C alleles when associated with T-175 in allele KIR2DS5*006; increases binding to C2 epitopes of HLA-C alleles when associated with H-203 in allele KIR2DS5*004; increases binding to C2 epitopes of HLA-C alleles when associated with K-237 in allele KIR2DS5*007, features a modification of the amino acid from R to G at position 179.
+The protein's natural variant, known as in allele KIR2DS5*001; not expressed at the cell surface when associated with R-22, P-132 and A-195 in allele KIR2DS5*001; abolishes cell surface expression, features a modification of the amino acid from F to S at position 185.
+The protein's natural variant, known as in allele KIR2DS5*001; not expressed at the cell surface when associated with R-22, P-132 and S-185 in allele KIR2DS5*001; decreases cell surface expression, features a modification of the amino acid from T to A at position 195.
+The protein's natural variant, known as in alleles KIR2DS5*009 and KIR2DS5*011; decreases binding to C2 epitopes of HLA-C alleles but no effect on cell surface expression in allele KIR2DS5*009; decreases binding to C2 epitopes of HLA-C alleles when associated with T-175 in allele KIR2DS5*011, features a modification of the amino acid from R to T at position 197.
+The protein's natural variant, known as in alleles KIR2DS5*004 and KIR2DS5*010; increases binding to C2 epitopes of HLA-C alleles when associated with G-179 in allele KIR2DS5*004; decreases binding to C2 epitopes of HLA-C alleles when associated with F-148 and G-179 in allele KIR2DS5*010, features a modification of the amino acid from R to H at position 203.
+The protein's natural variant, known as in allele KIR2DS5*007; increases binding to C2 epitopes of HLA-C alleles when associated with G-179 in allele KIR2DS5*007, features a modification of the amino acid from E to K at position 237.
+The protein's natural variant, known as in CDG2A; strongly reduced protein levels; loss of enzyme activity;, features a modification of the amino acid from H to R at position 262.
+The protein's natural variant, known as in CDG2A; strongly reduced protein levels; loss of enzyme activity;, features a modification of the amino acid from S to F at position 290.
+The protein's natural variant, known as in CDG2A;, features a modification of the amino acid from N to D at position 318.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from G to V at position 19.
+The protein's natural variant, known as improved maturation and increased expression at the cell surface;, features a modification of the amino acid from C to F at position 27.
+The protein's natural variant, known as in CMAMMA;, features a modification of the amino acid from M to R at position 198.
+The protein's natural variant, known as in CMAMMA;, features a modification of the amino acid from P to L at position 243.
+The protein's natural variant, known as in CMAMMA;, features a modification of the amino acid from T to I at position 358.
+The protein's natural variant, known as in CMAMMA;, features a modification of the amino acid from E to K at position 359.
+The protein's natural variant, known as in CMAMMA;, features a modification of the amino acid from K to T at position 462.
+The protein's natural variant, known as in CMAMMA;, features a modification of the amino acid from R to Q at position 471.
+The protein's natural variant, known as in CMAMMA;, features a modification of the amino acid from R to W at position 471.
+The protein's natural variant, known as in CMAMMA, features a modification of the amino acid from G to S at position 480.
+The protein's natural variant, known as in CMAMMA;, features a modification of the amino acid from R to W at position 558.
+The protein's natural variant, known as in Ly9-1, features a modification of the amino acid from D to G at position 10.
+The protein's natural variant, known as in Ly9-1, features a modification of the amino acid from G to S at position 14.
+The protein's natural variant, known as in Ly9-1, features a modification of the amino acid from I to T at position 79.
+The protein's natural variant, known as in Ly9-1, features a modification of the amino acid from F to S at position 91.
+The protein's natural variant, known as in Ly9-1, features a modification of the amino acid from H to Y at position 130.
+The protein's natural variant, known as in Ly9-1, features a modification of the amino acid from I to T at position 139.
+The natural variant of this protein is characterized by an amino acid alteration from P to S at position 362.
+The protein's natural variant, known as in Ly9-1, features a modification of the amino acid from K to N at position 366.
+The protein's natural variant, known as in Ly9-1, features a modification of the amino acid from E to K at position 377.
+The protein's natural variant, known as in Ly9-1, features a modification of the amino acid from M to I at position 550.
+The protein's natural variant, known as in Ly9-1, features a modification of the amino acid from G to E at position 592.
+The natural variant of this protein is characterized by an amino acid alteration from G to S at position 103.
+The natural variant of this protein is characterized by an amino acid alteration from E to G at position 256.
+The protein's natural variant, known as found in a patient with combined respiratory complex deficiencies, muscle weakness and hearing loss; unknown pathological significance;, features a modification of the amino acid from P to S at position 33.
+The protein's natural variant, known as in MTDPS8A;, features a modification of the amino acid from W to R at position 64.
+The protein's natural variant, known as in MTDPS8B;, features a modification of the amino acid from R to H at position 110.
+The protein's natural variant, known as in colorectal adenocarcinomas cell line; loss of ribonucleotide reductase activity, features a modification of the amino acid from V to L at position 115.
+The protein's natural variant, known as in MTDPS8B;, features a modification of the amino acid from R to H at position 121.
+The protein's natural variant, known as in MTDPS8A;, features a modification of the amino acid from E to G at position 194.
+The protein's natural variant, known as in MTDPS8A;, features a modification of the amino acid from E to K at position 194.
+The protein's natural variant, known as in MTDPS8A; without tubulopathy;, features a modification of the amino acid from I to S at position 224.
+The protein's natural variant, known as in MTDPS8A;, features a modification of the amino acid from C to F at position 236.
+The protein's natural variant, known as in RCDFRD, features a modification of the amino acid from E to D at position 262.
+The protein's natural variant, known as in MTDPS8A; without tubulopathy;, features a modification of the amino acid from M to I at position 282.
+The protein's natural variant, known as in MTDPS8A; without tubulopathy;, features a modification of the amino acid from L to V at position 317.
+The protein's natural variant, known as in HMGCLD; activity lower than 5% respect to the wild-type, features a modification of the amino acid from E to K at position 37.
+The protein's natural variant, known as in HMGCLD; loss of activity and of proton exchange;, features a modification of the amino acid from R to Q at position 41.
+The protein's natural variant, known as in HMGCLD; reduced activity, features a modification of the amino acid from D to E at position 42.
+The protein's natural variant, known as in HMGCLD; loss of activity;, features a modification of the amino acid from D to G at position 42.
+The protein's natural variant, known as in HMGCLD; loss of activity, features a modification of the amino acid from D to H at position 42.
+The protein's natural variant, known as in HMGCLD; abolishes almost all enzymatic activity, features a modification of the amino acid from K to N at position 48.
+The protein's natural variant, known as in HMGCLD;, features a modification of the amino acid from V to L at position 70.
+The protein's natural variant, known as in HMGCLD;, features a modification of the amino acid from S to R at position 75.
+The protein's natural variant, known as in HMGCLD; activity lower than 5% respect to the wild-type, features a modification of the amino acid from S to F at position 142.
+The protein's natural variant, known as in HMGCLD;, features a modification of the amino acid from R to Q at position 165.
+The protein's natural variant, known as in HMGCLD; activity lower than 5% respect to the wild-type;, features a modification of the amino acid from C to Y at position 174.
+The protein's natural variant, known as in HMGCLD; activity lower than 5% respect to the wild-type, features a modification of the amino acid from F to S at position 192.
+The protein's natural variant, known as in HMGCLD; activity lower than 5% respect to the wild-type, features a modification of the amino acid from I to F at position 200.
+The protein's natural variant, known as in HMGCLD;, features a modification of the amino acid from S to Y at position 201.
+The protein's natural variant, known as in HMGCLD; complete loss of activity;, features a modification of the amino acid from G to E at position 203.
+The protein's natural variant, known as in HMGCLD, features a modification of the amino acid from D to N at position 204.
+The protein's natural variant, known as in HMGCLD; loss of activity;, features a modification of the amino acid from H to R at position 233.
+The protein's natural variant, known as in HMGCLD, features a modification of the amino acid from L to P at position 263.
+The protein's natural variant, known as in HMGCLD;, features a modification of the amino acid from E to K at position 279.
+The protein's natural variant, known as in a lung squamous cell carcinoma sample; somatic mutation, features a modification of the amino acid from Q to L at position 142.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from R to W at position 154.
+The protein's natural variant, known as in an ovarian serous carcinoma sample; somatic mutation, features a modification of the amino acid from N to I at position 234.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation, features a modification of the amino acid from S to N at position 251.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from A to T at position 279.
+The protein's natural variant, known as found in a renal cell carcinoma case; somatic mutation, features a modification of the amino acid from I to T at position 282.
+The protein's natural variant, known as in IMD8; the mutation causes a decrease in protein stability; patient T-cell blasts show delayed activation of signaling molecules MAPK3 and MAPK1;, features a modification of the amino acid from V to M at position 134.
+The protein's natural variant, known as in DBA18; unknown pathological significance;, features a modification of the amino acid from L to S at position 51.
+The protein's natural variant, known as in IPS;, features a modification of the amino acid from A to T at position 92.
+The protein's natural variant, known as correlates with lower body mass index, triglyceride concentrations, systolic blood pressure, insulin concentrations and homeostasis model assessment index;, features a modification of the amino acid from G to S at position 209.
+The protein's natural variant, known as in IPS;, features a modification of the amino acid from S to P at position 247.
+The protein's natural variant, known as in IPS;, features a modification of the amino acid from Q to R at position 300.
+The protein's natural variant, known as in IPS;, features a modification of the amino acid from R to C at position 374.
+The protein's natural variant, known as in IPS;, features a modification of the amino acid from R to H at position 583.
+The protein's natural variant, known as in Lgj, features a modification of the amino acid from H to N at position 168.
+The protein's natural variant, known as in DEE39; decreased antiporter activity; significant loss in ability to transport aspartate or glutamate; no effect on localization to mitochondrial inner membrane; no effect on protein abundance;, features a modification of the amino acid from R to Q at position 353.
+The protein's natural variant, known as in DEE39; loss of antiporter activity; unable to transport aspartate or glutamate; no effect on localization to mitochondrial inner membrane; no effect on protein abundance;, features a modification of the amino acid from Q to R at position 590.
+The protein's natural variant, known as in CCM1, features a modification of the amino acid from F to S at position 97.
+The protein's natural variant, known as in CCM1, features a modification of the amino acid from K to E at position 569.
+The protein's natural variant, known as found in patients with an intermediate form of Charcot-Marie-Tooth disease; does not affect subcellular location; reduced protein expression; increased intracellular Ca(2+);, features a modification of the amino acid from K to I at position 28.
+The protein's natural variant, known as probable disease-associated variant found in patients with a form of Charcot-Marie-Tooth disease leading to demyelinating form; does not affect subcellular location; increased protein expression; increased aggregation in vesicles; increased intracellular Ca(2+); decreased mitochondrial Ca(2+);, features a modification of the amino acid from I to N at position 122.
+The protein's natural variant, known as in mutants SL1102 and SL1027; heptoseless LPS, features a modification of the amino acid from K to R at position 2.
+The protein's natural variant, known as in mutant SL1102; heptoseless LPS, features a modification of the amino acid from G to E at position 236.
+The protein's natural variant, known as in mutant SL1027; heptoseless LPS, features a modification of the amino acid from RA to PP at position 316.
+The protein's natural variant, known as in C7D;, features a modification of the amino acid from R to Q at position 220.
+The protein's natural variant, known as in C7D;, features a modification of the amino acid from G to R at position 379.
+The protein's natural variant, known as confirmed at protein level;, features a modification of the amino acid from S to T at position 389.
+The protein's natural variant, known as in C7D;, features a modification of the amino acid from R to S at position 521.
+The protein's natural variant, known as confirmed at protein level;, features a modification of the amino acid from T to P at position 587.
+The protein's natural variant, known as in C7D;, features a modification of the amino acid from E to Q at position 682.
+The protein's natural variant, known as in C7D;, features a modification of the amino acid from R to H at position 687.
+The protein's natural variant, known as in MRD65, features a modification of the amino acid from L to P at position 220.
+The protein's natural variant, known as in MRD65, features a modification of the amino acid from R to W at position 222.
+The protein's natural variant, known as in MRD65, features a modification of the amino acid from H to R at position 768.
+The protein's natural variant, known as in MRD65; unknown pathological significance, features a modification of the amino acid from P to L at position 1095.
+The protein's natural variant, known as in strain: sonoma_017, features a modification of the amino acid from K to R at position 398.
+The protein's natural variant, known as in strain: sonoma_009, sonoma_051, sonoma_053 and sonoma_054, features a modification of the amino acid from A to T at position 443.
+The protein's natural variant, known as in strain: sonoma_010, sonoma_013, sonoma_019 and sonoma_117, features a modification of the amino acid from Q to K at position 461.
+The protein's natural variant, known as in strain: NapaValley5, NapaValley12, sonoma_015, sonoma_016, sonoma_023, sonoma_032, sonoma_034, sonoma_038, sonoma_040, sonoma_045, sonoma_048, sonoma_050, sonoma_061, sonoma_073, sonoma_081, sonoma_085, sonoma_094, sonoma_097 and sonoma_119, features a modification of the amino acid from G to A at position 652.
+The protein's natural variant, known as in strain: sonoma_008, sonoma_015, sonoma_016, sonoma_032, sonoma_034, sonoma_038, sonoma_040, sonoma_045, sonoma_048, sonoma_050, sonoma_061, sonoma_073, sonoma_081, sonoma_085, sonoma_094 and sonoma_097, features a modification of the amino acid from L to M at position 662.
+The protein's natural variant, known as in strain: sonoma_006, sonoma_022 and sonoma_040, features a modification of the amino acid from A to T at position 761.
+The protein's natural variant, known as in strain: nps_6, nps_18, nps_34, sonoma_048 and sonoma_050, features a modification of the amino acid from S to G at position 787.
+The protein's natural variant, known as in strain: sonoma_002, features a modification of the amino acid from G to R at position 800.
+The protein's natural variant, known as in strain: nps_19, nps_21, nps_25, nps_26, nps_27, nps_30, nps_31, nps_33, nps_35, nps_42, nps_43, nps_45, nps_47, sonoma_002, sonoma_003, sonoma_004, sonoma_005, sonoma_006, sonoma_007, sonoma_008, sonoma_009, sonoma_014, sonoma_016, sonoma_017, sonoma_022, sonoma_024, sonoma_032, sonoma_033, sonoma_036, sonoma_038, sonoma_045, sonoma_051, sonoma_053, sonoma_054, sonoma_055, sonoma_059, sonoma_061, sonoma_064, sonoma_081, sonoma_086, sonoma_087, sonoma_094, sonoma_095, sonoma_097, sonoma_106, sonoma_107 and sonoma_119, features a modification of the amino acid from V to A at position 812.
+The protein's natural variant, known as in strain: 10, features a modification of the amino acid from E to Q at position 3.
+The protein's natural variant, known as in strain: 10, features a modification of the amino acid from S to G at position 16.
+The protein's natural variant, known as in SPGF55; unknown pathological significance; decreased protein expression in homozygous patient sperm;, features a modification of the amino acid from R to Q at position 1448.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from D to E at position 1707.
+The protein's natural variant, known as in strain: BC9405/90 / Serotype 18, features a modification of the amino acid from H to S at position 28.
+The protein's natural variant, known as in strain: ATCC 35847 / Serotype 7, features a modification of the amino acid from S to T at position 30.
+The protein's natural variant, known as in strain: BC9405/90 / Serotype 18, features a modification of the amino acid from A to T at position 98.
+The protein's natural variant, known as in strain: ATCC 35847 / Serotype 7, features a modification of the amino acid from N to S at position 135.
+The protein's natural variant, known as in strain: O29, features a modification of the amino acid from K to E at position 102.
+The protein's natural variant, known as in MGCA1; decreased methylglutaconyl-CoA hydratase activity;, features a modification of the amino acid from A to V at position 240.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to Q at position 133.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from A to T at position 298.
+The protein's natural variant, known as in a pancreatic ductal adenocarcinoma sample; somatic mutation, features a modification of the amino acid from H to Q at position 609.
+The protein's natural variant, known as in plastocyanin B", features a modification of the amino acid from G to A at position 65.
+The protein's natural variant, known as in plastocyanin B", features a modification of the amino acid from T to S at position 81.
+The protein's natural variant, known as in plastocyanin B", features a modification of the amino acid from A to S at position 85.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from K to R at position 121.
+The natural variant of this protein is characterized by an amino acid alteration from T to V at position 193.
+The natural variant of this protein is characterized by an amino acid alteration from N to Y at position 296.
+The natural variant of this protein is characterized by an amino acid alteration from Q to P at position 299.
+The natural variant of this protein is characterized by an amino acid alteration from I to L at position 346.
+The protein's natural variant, known as in PKHYP;, features a modification of the amino acid from G to E at position 37.
+The protein's natural variant, known as in PKRD;, features a modification of the amino acid from R to W at position 40.
+The protein's natural variant, known as in PKRD, features a modification of the amino acid from L to P at position 73.
+The protein's natural variant, known as in PKRD, features a modification of the amino acid from S to P at position 80.
+The protein's natural variant, known as in PKRD, features a modification of the amino acid from R to P at position 86.
+The protein's natural variant, known as in PKRD, features a modification of the amino acid from I to N at position 90.
+The protein's natural variant, known as in PKRD;, features a modification of the amino acid from G to R at position 95.
+The protein's natural variant, known as in PKRD, features a modification of the amino acid from M to T at position 107.
+The protein's natural variant, known as in PKRD;, features a modification of the amino acid from G to R at position 111.
+The protein's natural variant, known as in PKRD; Val de Marne, features a modification of the amino acid from A to P at position 115.
+The protein's natural variant, known as in PKRD; Beaujon, features a modification of the amino acid from S to F at position 120.
+The protein's natural variant, known as in PKRD; Conakry;, features a modification of the amino acid from S to Y at position 130.
+The protein's natural variant, known as in PKRD;, features a modification of the amino acid from V to D at position 134.
+The protein's natural variant, known as in PKRD, features a modification of the amino acid from I to T at position 153.
+The protein's natural variant, known as in PKRD;, features a modification of the amino acid from A to T at position 154.
+The protein's natural variant, known as in PKRD, features a modification of the amino acid from L to P at position 155.
+The protein's natural variant, known as in PKRD;, features a modification of the amino acid from G to V at position 159.
+The protein's natural variant, known as in PKRD; Linz;, features a modification of the amino acid from R to C at position 163.
+The protein's natural variant, known as in PKRD, features a modification of the amino acid from R to L at position 163.
+The protein's natural variant, known as in PKRD, features a modification of the amino acid from G to V at position 165.
+The protein's natural variant, known as in PKRD; Sassari;, features a modification of the amino acid from E to Q at position 172.
+The protein's natural variant, known as in PKRD;, features a modification of the amino acid from I to T at position 219.
+The protein's natural variant, known as in PKRD, features a modification of the amino acid from D to DD at position 221.
+The protein's natural variant, known as in PKRD; Katsushika, features a modification of the amino acid from G to A at position 222.
+The protein's natural variant, known as in PKRD;, features a modification of the amino acid from G to R at position 263.
+The protein's natural variant, known as in PKRD, features a modification of the amino acid from G to W at position 263.
+The protein's natural variant, known as in PKRD;, features a modification of the amino acid from L to V at position 272.
+The protein's natural variant, known as in PKRD;, features a modification of the amino acid from G to R at position 275.
+The protein's natural variant, known as in PKRD, features a modification of the amino acid from D to N at position 281.
+The protein's natural variant, known as in PKRD, features a modification of the amino acid from F to V at position 287.
+The protein's natural variant, known as in PKRD; Moriguchi, features a modification of the amino acid from V to L at position 288.
+The protein's natural variant, known as in PKRD;, features a modification of the amino acid from D to N at position 293.
+The protein's natural variant, known as in PKRD;, features a modification of the amino acid from A to V at position 295.
+The protein's natural variant, known as in PKRD; Dordrecht, features a modification of the amino acid from I to N at position 310.
+The protein's natural variant, known as in PKRD; Hong Kong;, features a modification of the amino acid from I to T at position 314.
+The protein's natural variant, known as in PKRD, features a modification of the amino acid from E to K at position 315.
+The protein's natural variant, known as in PKRD;, features a modification of the amino acid from V to L at position 320.
+The protein's natural variant, known as in PKRD; Parma;, features a modification of the amino acid from D to E at position 331.
+The protein's natural variant, known as in PKRD;, features a modification of the amino acid from D to N at position 331.
+The protein's natural variant, known as in PKRD; loss of catalytical activity;, features a modification of the amino acid from G to S at position 332.
+The protein's natural variant, known as in PKRD, features a modification of the amino acid from V to M at position 335.
+The protein's natural variant, known as in PKRD, features a modification of the amino acid from A to S at position 336.
+The protein's natural variant, known as in PKRD, features a modification of the amino acid from R to P at position 337.
+The protein's natural variant, known as in PKRD;, features a modification of the amino acid from R to Q at position 337.
+The protein's natural variant, known as in PKRD;, features a modification of the amino acid from D to H at position 339.
+The protein's natural variant, known as in PKRD;, features a modification of the amino acid from G to A at position 341.
+The protein's natural variant, known as in PKRD, features a modification of the amino acid from G to D at position 341.
+The protein's natural variant, known as in PKRD, features a modification of the amino acid from I to F at position 342.
+The protein's natural variant, known as in PKRD; Kamata, features a modification of the amino acid from K to N at position 348.
+The protein's natural variant, known as in PKRD;, features a modification of the amino acid from A to D at position 352.
+The protein's natural variant, known as in PKRD;, features a modification of the amino acid from I to T at position 357.
+The protein's natural variant, known as in PKRD, features a modification of the amino acid from G to E at position 358.
+The protein's natural variant, known as in PKRD; Aomori;, features a modification of the amino acid from R to C at position 359.
+The protein's natural variant, known as in PKRD;, features a modification of the amino acid from R to H at position 359.
+The protein's natural variant, known as in PKRD;, features a modification of the amino acid from N to D at position 361.
+The protein's natural variant, known as in PKRD; Tjaereborg; unstability of the protein and decrease in catalytic activity;, features a modification of the amino acid from G to D at position 364.
+The protein's natural variant, known as in PKRD; Osaka, features a modification of the amino acid from V to F at position 368.
+The protein's natural variant, known as in PKRD, features a modification of the amino acid from L to P at position 374.
+The protein's natural variant, known as in PKRD, features a modification of the amino acid from S to I at position 376.
+The protein's natural variant, known as in PKRD; Tokyo/Beirut; no conformational change;, features a modification of the amino acid from T to M at position 384.
+The protein's natural variant, known as in PKRD, features a modification of the amino acid from R to W at position 385.
+The protein's natural variant, known as in PKRD, features a modification of the amino acid from E to G at position 387.
+The protein's natural variant, known as in PKRD; Mantova; almost complete inactivation;, features a modification of the amino acid from D to N at position 390.
+The protein's natural variant, known as in PKRD;, features a modification of the amino acid from A to T at position 392.
+The protein's natural variant, known as in PKRD;, features a modification of the amino acid from N to K at position 393.
+The protein's natural variant, known as in PKRD; Paris;, features a modification of the amino acid from N to S at position 393.
+The protein's natural variant, known as in PKRD;, features a modification of the amino acid from A to D at position 394.
+The protein's natural variant, known as in PKRD, features a modification of the amino acid from A to V at position 394.
+The protein's natural variant, known as in PKRD, features a modification of the amino acid from C to CS at position 401.
+The protein's natural variant, known as in PKRD; Hirosaki, features a modification of the amino acid from T to A at position 408.
+The protein's natural variant, known as in PKRD, features a modification of the amino acid from T to I at position 408.
+The protein's natural variant, known as in PKRD; Fukushima/Maebashi/Sendai;, features a modification of the amino acid from Q to K at position 421.
+The protein's natural variant, known as in PKRD; Sapporo;, features a modification of the amino acid from R to Q at position 426.
+The protein's natural variant, known as in PKRD; Naniwa;, features a modification of the amino acid from R to W at position 426.
+The protein's natural variant, known as in PKRD, features a modification of the amino acid from E to A at position 427.
+The protein's natural variant, known as in PKRD, features a modification of the amino acid from E to D at position 427.
+The protein's natural variant, known as in PKRD;, features a modification of the amino acid from A to T at position 431.
+The protein's natural variant, known as in PKRD;, features a modification of the amino acid from G to D at position 458.
+The protein's natural variant, known as in PKRD, features a modification of the amino acid from A to V at position 459.
+The protein's natural variant, known as in PKRD;, features a modification of the amino acid from V to M at position 460.
+The protein's natural variant, known as in PKRD;, features a modification of the amino acid from A to G at position 468.
+The protein's natural variant, known as in PKRD; Hadano, features a modification of the amino acid from A to V at position 468.
+The protein's natural variant, known as in PKRD;, features a modification of the amino acid from T to A at position 477.
+The protein's natural variant, known as in PKRD; Amish; no conformational change;, features a modification of the amino acid from R to H at position 479.
+The protein's natural variant, known as in PKRD, features a modification of the amino acid from S to F at position 485.
+The protein's natural variant, known as in PKRD; no conformational change;, features a modification of the amino acid from R to W at position 486.
+The protein's natural variant, known as in PKRD;, features a modification of the amino acid from R to Q at position 488.
+The protein's natural variant, known as in PKRD;, features a modification of the amino acid from R to W at position 490.
+The protein's natural variant, known as in PKRD, features a modification of the amino acid from A to T at position 495.
+The protein's natural variant, known as in PKRD;, features a modification of the amino acid from A to V at position 495.
+The protein's natural variant, known as in PKRD;, features a modification of the amino acid from R to C at position 498.
+The protein's natural variant, known as in PKRD;, features a modification of the amino acid from R to H at position 498.
+The protein's natural variant, known as in PKRD; instability of the protein;, features a modification of the amino acid from R to L at position 504.
+The protein's natural variant, known as in PKRD;, features a modification of the amino acid from R to Q at position 510.
+The protein's natural variant, known as in PKRD, features a modification of the amino acid from G to R at position 511.
+The protein's natural variant, known as in PKRD, features a modification of the amino acid from R to C at position 531.
+The protein's natural variant, known as in PKRD;, features a modification of the amino acid from R to Q at position 532.
+The protein's natural variant, known as in PKRD; Complete loss in the responsiveness to fructose 1,6-bisphosphate, FBP;, features a modification of the amino acid from R to W at position 532.
+The protein's natural variant, known as in PKRD;, features a modification of the amino acid from V to M at position 552.
+The protein's natural variant, known as in PKRD, features a modification of the amino acid from G to A at position 557.
+The protein's natural variant, known as in PKRD, features a modification of the amino acid from R to G at position 559.
+The protein's natural variant, known as in PKRD, features a modification of the amino acid from N to K at position 566.
+The protein's natural variant, known as in PKRD;, features a modification of the amino acid from R to Q at position 569.
+The protein's natural variant, known as in CRYPTO; functionally inactive;, features a modification of the amino acid from T to P at position 222.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 10.
+The natural variant of this protein is characterized by an amino acid alteration from N to S at position 19.
+The protein's natural variant, known as in MPS7;, features a modification of the amino acid from P to S at position 30.
+The protein's natural variant, known as in MPS7; very mild phenotype;, features a modification of the amino acid from C to G at position 38.
+The protein's natural variant, known as in MPS7; loss of activity;, features a modification of the amino acid from S to F at position 52.
+The protein's natural variant, known as in MPS7;, features a modification of the amino acid from G to R at position 136.
+The protein's natural variant, known as in MPS7;, features a modification of the amino acid from P to S at position 148.
+The protein's natural variant, known as in MPS7, features a modification of the amino acid from E to K at position 150.
+The protein's natural variant, known as in MPS7, features a modification of the amino acid from D to G at position 152.
+The protein's natural variant, known as likely benign variant; associated with beta-glucuronidase pseudodeficiency with no clinical consequences; reduced activity levels;, features a modification of the amino acid from D to N at position 152.
+The protein's natural variant, known as in MPS7;, features a modification of the amino acid from L to F at position 176.
+The protein's natural variant, known as in MPS7;, features a modification of the amino acid from R to W at position 216.
+The protein's natural variant, known as in MPS7, features a modification of the amino acid from L to P at position 243.
+The protein's natural variant, known as in MPS7, features a modification of the amino acid from Y to C at position 320.
+The protein's natural variant, known as in MPS7;, features a modification of the amino acid from Y to S at position 320.
+The protein's natural variant, known as in MPS7, features a modification of the amino acid from N to S at position 339.
+The protein's natural variant, known as in MPS7;, features a modification of the amino acid from K to N at position 350.
+The protein's natural variant, known as in MPS7;, features a modification of the amino acid from H to Y at position 351.
+The protein's natural variant, known as in MPS7;, features a modification of the amino acid from A to V at position 354.
+The protein's natural variant, known as in MPS7;, features a modification of the amino acid from D to N at position 362.
+The protein's natural variant, known as in MPS7;, features a modification of the amino acid from P to L at position 364.
+The protein's natural variant, known as in MPS7;, features a modification of the amino acid from R to C at position 374.
+The protein's natural variant, known as in MPS7;, features a modification of the amino acid from R to C at position 382.
+The protein's natural variant, known as in MPS7;, features a modification of the amino acid from R to H at position 382.
+The protein's natural variant, known as in MPS7;, features a modification of the amino acid from P to S at position 408.
+The protein's natural variant, known as in MPS7;, features a modification of the amino acid from P to L at position 415.
+The protein's natural variant, known as in MPS7, features a modification of the amino acid from R to P at position 435.
+The protein's natural variant, known as in MPS7;, features a modification of the amino acid from R to W at position 477.
+The protein's natural variant, known as in MPS7;, features a modification of the amino acid from Y to C at position 495.
+The protein's natural variant, known as in MPS7, features a modification of the amino acid from Y to C at position 508.
+The protein's natural variant, known as in MPS7, features a modification of the amino acid from E to K at position 540.
+The protein's natural variant, known as in MPS7, features a modification of the amino acid from G to D at position 572.
+The protein's natural variant, known as in MPS7; loss of activity;, features a modification of the amino acid from R to L at position 577.
+The protein's natural variant, known as in MPS7, features a modification of the amino acid from K to N at position 606.
+The protein's natural variant, known as in MPS7;, features a modification of the amino acid from G to A at position 607.
+The protein's natural variant, known as in MPS7;, features a modification of the amino acid from R to W at position 611.
+The protein's natural variant, known as in MPS7;, features a modification of the amino acid from A to V at position 619.
+The protein's natural variant, known as in MPS7; very mild phenotype;, features a modification of the amino acid from Y to H at position 626.
+The protein's natural variant, known as in MPS7;, features a modification of the amino acid from W to C at position 627.
+The protein's natural variant, known as in strain: 297, features a modification of the amino acid from V to L at position 179.
+The natural variant of this protein is characterized by an amino acid alteration from P to A at position 45.
+The protein's natural variant, known as in NEM7; unknown pathological significance;, features a modification of the amino acid from V to M at position 7.
+The protein's natural variant, known as in NEM7; protein is less soluble when expressed in Escherichia coli;, features a modification of the amino acid from A to T at position 35.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from I to M at position 47.
+The protein's natural variant, known as found in a renal cell carcinoma sample; somatic mutation, features a modification of the amino acid from L to I at position 48.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from R to H at position 674.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from A to T at position 233.
+The protein's natural variant, known as in strain: cv. Bla-10, cv. Chi-1, cv. Cvi-0, cv. Di-G, cv. Gr-3, cv. Landsberg erecta, cv. Li-3, cv. Mt-0, cv. PHW-1 and cv. Sha, features a modification of the amino acid from E to D at position 98.
+The protein's natural variant, known as in strain: cv. Bla-10, features a modification of the amino acid from K to T at position 150.
+The protein's natural variant, known as in strain: cv. Bla-10, cv. Chi-1, cv. Co-1, cv. Cvi-0, cv. Di-G, cv. Gr-3, cv. Landsberg erecta, cv. Li-3, cv. Mt-0, cv. PHW-32 and cv. Sha, features a modification of the amino acid from H to R at position 193.
+The protein's natural variant, known as in EDSPD1; requires 2 nucleotide substitutions; the mutant is not secreted but retained intracellularly, features a modification of the amino acid from V to D at position 50.
+The protein's natural variant, known as confirmed at protein level;, features a modification of the amino acid from E to K at position 184.
+The protein's natural variant, known as confirmed at protein level;, features a modification of the amino acid from G to R at position 261.
+The protein's natural variant, known as in EDSPD1; unknown pathological significance;, features a modification of the amino acid from D to G at position 290.
+The protein's natural variant, known as in EDSPD1; unknown pathological significance;, features a modification of the amino acid from G to D at position 297.
+The protein's natural variant, known as in EDSPD1; unknown pathological significance;, features a modification of the amino acid from L to P at position 300.
+The protein's natural variant, known as in EDSPD1; unknown pathological significance;, features a modification of the amino acid from R to P at position 301.
+The protein's natural variant, known as in EDSPD1;, features a modification of the amino acid from Y to C at position 302.
+The protein's natural variant, known as in EDSPD1, features a modification of the amino acid from IIKC to RR at position 309.
+The protein's natural variant, known as in EDSPD1; the mutant is not secreted but retained intracellularly;, features a modification of the amino acid from C to W at position 309.
+The protein's natural variant, known as in EDSPD1;, features a modification of the amino acid from C to R at position 338.
+The protein's natural variant, known as in EDSPD1;, features a modification of the amino acid from C to F at position 358.
+The protein's natural variant, known as in EDSPD1; unknown pathological significance;, features a modification of the amino acid from W to C at position 364.
+The protein's natural variant, known as in EDSPD1; the mutant is not secreted but retained intracellularly;, features a modification of the amino acid from C to W at position 371.
+The protein's natural variant, known as in EDSPD1; unknown pathological significance, features a modification of the amino acid from RIQYY to HVI at position 405.
+The protein's natural variant, known as in EDSPD1; unknown pathological significance;, features a modification of the amino acid from W to R at position 435.
+The protein's natural variant, known as in NEDSGA;, features a modification of the amino acid from T to S at position 639.
+The protein's natural variant, known as in NEDSGA;, features a modification of the amino acid from N to D at position 641.
+The protein's natural variant, known as in NEDSGA;, features a modification of the amino acid from A to G at position 643.
+The protein's natural variant, known as in NEDSGA;, features a modification of the amino acid from A to V at position 644.
+The protein's natural variant, known as in NEDSGA; unknown pathological significance, features a modification of the amino acid from R to P at position 697.
+The protein's natural variant, known as in a glioblastoma multiforme sample; somatic mutation, features a modification of the amino acid from G to S at position 211.
+The protein's natural variant, known as in DEE30; no change in subcellular location;, features a modification of the amino acid from P to T at position 287.
+The protein's natural variant, known as in DEE30; no change in subcellular location, features a modification of the amino acid from S to C at position 411.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation, features a modification of the amino acid from G to D at position 469.
+The protein's natural variant, known as in DEE30; no change in subcellular location;, features a modification of the amino acid from G to S at position 636.
+The protein's natural variant, known as in strain: cv. Taichung 65; strong reduction of DNA-binding activity, features a modification of the amino acid from G to R at position 219.
+The protein's natural variant, known as in NC; increased autophosphorylation at T-210;, features a modification of the amino acid from I to T at position 167.
+The protein's natural variant, known as in NC; increased autophosphorylation at T-210;, features a modification of the amino acid from I to T at position 573.
+The protein's natural variant, known as in APUG;, features a modification of the amino acid from R to H at position 681.
+The protein's natural variant, known as in a lung neuroendocrine carcinoma sample; somatic mutation, features a modification of the amino acid from P to S at position 870.
+The protein's natural variant, known as in PDB2, features a modification of the amino acid from L to LALLLLCALL at position 21.
+The protein's natural variant, known as in FEO, features a modification of the amino acid from L to LLLCALL at position 21.
+The protein's natural variant, known as in OPTB7; two patients with osteoclast-poor osteopetrosis;, features a modification of the amino acid from G to R at position 53.
+The protein's natural variant, known as in OPTB7; a patient with osteoclast-poor osteopetrosis;, features a modification of the amino acid from R to C at position 129.
+The protein's natural variant, known as in OPTB7; two siblings with osteoclast-poor osteopetrosis;, features a modification of the amino acid from R to G at position 170.
+The protein's natural variant, known as in OPTB7; two patients with osteoclast-poor osteopetrosis;, features a modification of the amino acid from C to R at position 175.
+The protein's natural variant, known as in OPTB7; one patient with osteoclast-poor osteopetrosis;, features a modification of the amino acid from A to S at position 244.
+The natural variant of this protein is characterized by an amino acid alteration from G to A at position 81.
+The protein's natural variant, known as in strain: NCTC 8798, features a modification of the amino acid from V to I at position 211.
+The protein's natural variant, known as in strain: NCTC 8798, features a modification of the amino acid from A to E at position 278.
+The protein's natural variant, known as in strain: cv. Chipper and cv. Baekmibaekdadagi, features a modification of the amino acid from T to R at position 86.
+The protein's natural variant, known as in HIGM1;, features a modification of the amino acid from M to R at position 36.
+The protein's natural variant, known as in HIGM1, features a modification of the amino acid from G to R at position 38.
+The protein's natural variant, known as in HIGM1, features a modification of the amino acid from G to R at position 116.
+The protein's natural variant, known as in HIGM1, features a modification of the amino acid from G to S at position 116.
+The protein's natural variant, known as in HIGM1;, features a modification of the amino acid from A to E at position 123.
+The protein's natural variant, known as in HIGM1, features a modification of the amino acid from H to R at position 125.
+The protein's natural variant, known as in HIGM1, features a modification of the amino acid from V to A at position 126.
+The protein's natural variant, known as in HIGM1, features a modification of the amino acid from V to D at position 126.
+The protein's natural variant, known as in HIGM1, features a modification of the amino acid from SE to RG at position 129.
+The protein's natural variant, known as in HIGM1, features a modification of the amino acid from W to C at position 140.
+The protein's natural variant, known as in HIGM1;, features a modification of the amino acid from W to G at position 140.
+The protein's natural variant, known as in HIGM1, features a modification of the amino acid from W to R at position 140.
+The protein's natural variant, known as in HIGM1, features a modification of the amino acid from K to T at position 143.
+The protein's natural variant, known as in HIGM1;, features a modification of the amino acid from G to E at position 144.
+The protein's natural variant, known as in HIGM1;, features a modification of the amino acid from T to N at position 147.
+The protein's natural variant, known as in HIGM1;, features a modification of the amino acid from L to P at position 155.
+The protein's natural variant, known as in HIGM1; decreases ITGA5:ITGB1 and ITGAV:ITGB3 binding of the soluble form; decreases activation of NF-kappa-B signaling; slightly decreases CD40 binding of the soluble form;, features a modification of the amino acid from Y to C at position 170.
+The protein's natural variant, known as in HIGM1, features a modification of the amino acid from A to D at position 173.
+The protein's natural variant, known as in HIGM1; decreases ITGA5:ITGB1 and ITGAV:ITGB3 binding of the soluble form; decreases activation of NF-kappa-B signaling, features a modification of the amino acid from Q to R at position 174.
+The protein's natural variant, known as in HIGM1; decreases ITGA5:ITGB1 and ITGAV:ITGB3 binding of the soluble form; decreases activation of NF-kappa-B signaling, features a modification of the amino acid from T to I at position 176.
+The protein's natural variant, known as in HIGM1, features a modification of the amino acid from L to P at position 195.
+The protein's natural variant, known as in HIGM1; decreases ITGA5:ITGB1 and ITGAV:ITGB3 binding of the soluble form; decreases activation of NF-kappa-B signaling, features a modification of the amino acid from A to D at position 208.
+The protein's natural variant, known as in HIGM1;, features a modification of the amino acid from T to N at position 211.
+The protein's natural variant, known as in HIGM1; no effect on ITGA5:ITGB1 and ITGAV:ITGB3 binding of the soluble form; increases NF-kappa-B signaling, features a modification of the amino acid from H to Y at position 224.
+The protein's natural variant, known as in HIGM1; no effect on ITGA5:ITGB1 and ITGAV:ITGB3 binding of the soluble form; slightly increases NF-kappa-B signaling, features a modification of the amino acid from G to A at position 226.
+The protein's natural variant, known as in HIGM1; decreases ITGA5:ITGB1 and ITGAV:ITGB3 binding of the soluble form; decreases activation of NF-kappa-B signaling;, features a modification of the amino acid from G to V at position 227.
+The protein's natural variant, known as in HIGM1, features a modification of the amino acid from L to S at position 231.
+The protein's natural variant, known as in HIGM1;, features a modification of the amino acid from A to P at position 235.
+The protein's natural variant, known as in HIGM1, features a modification of the amino acid from V to E at position 237.
+The protein's natural variant, known as in HIGM1;, features a modification of the amino acid from T to M at position 254.
+The protein's natural variant, known as in HIGM1;, features a modification of the amino acid from G to D at position 257.
+The protein's natural variant, known as in HIGM1, features a modification of the amino acid from G to S at position 257.
+The protein's natural variant, known as in HIGM1; decreases ITGA5:ITGB1 and ITGAV:ITGB3 binding of the soluble form; decreases activation of NF-kappa-B signaling;, features a modification of the amino acid from L to S at position 258.
+The protein's natural variant, known as in ARCI11;, features a modification of the amino acid from G to R at position 827.
+The protein's natural variant, known as in MC1DN8; unknown pathological significance; decrease in enzyme activity; impaired assembly of complex I;, features a modification of the amino acid from R to W at position 140.
+The protein's natural variant, known as in MC1DN8; decrease in enzyme activity; increased protein instability and aggregation; compound heterozygous with W-199;, features a modification of the amino acid from T to I at position 145.
+The protein's natural variant, known as in MC1DN8; decrease in enzyme activity; impaired assembly of complex I; increased protein instability and aggregation; compound heterozygous with I-145;, features a modification of the amino acid from R to W at position 199.
+The protein's natural variant, known as found in a patient with obesity; unknown pathological significance;, features a modification of the amino acid from N to Y at position 88.
+The protein's natural variant, known as found in a patient with obesity; unknown pathological significance;, features a modification of the amino acid from L to V at position 115.
+The protein's natural variant, known as found in a patient with obesity; unknown pathological significance;, features a modification of the amino acid from R to C at position 125.
+The protein's natural variant, known as in 45% of the population;, features a modification of the amino acid from C to R at position 46.
+The protein's natural variant, known as in DIAR8; unknown pathological significance; does not affect cell membrane localization; reduces weakly Na(+)/H(+) exchange activity;, features a modification of the amino acid from A to T at position 127.
+The protein's natural variant, known as in DIAR8; decreases cell membrane expression; reduces Na(+)/H(+) exchange activity;, features a modification of the amino acid from A to T at position 269.
+The protein's natural variant, known as in DIAR8; decreases cell membrane expression; strongly reduces Na(+)/H(+) exchange activity;, features a modification of the amino acid from A to V at position 311.
+The protein's natural variant, known as in DIAR8; unknown pathological significance, features a modification of the amino acid from E to K at position 347.
+The protein's natural variant, known as in DIAR8; decreases cell membrane localization; strongly reduces Na(+)/H(+) exchange activity;, features a modification of the amino acid from R to Q at position 382.
+The protein's natural variant, known as in a lung large cell carcinoma sample; somatic mutation, features a modification of the amino acid from Y to C at position 140.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation, features a modification of the amino acid from S to T at position 258.
+The protein's natural variant, known as in strain: Isolate Australia, features a modification of the amino acid from P to S at position 249.
+The protein's natural variant, known as in DMAN; lower protein expression. Fails to rescue the lysosomal trafficking defect in LYSET-deficient cells. Severe reduction of interaction with GNPTAB, features a modification of the amino acid from R to W at position 39.
+The protein's natural variant, known as in streptolydigan resistant alleles stl6/stl445, features a modification of the amino acid from D to G at position 796.
+The protein's natural variant, known as found in patients with pathologic myopia; unknown pathological significance;, features a modification of the amino acid from V to I at position 1067.
+The protein's natural variant, known as in BBS6, features a modification of the amino acid from I to M at position 32.
+The protein's natural variant, known as in MKKS and BBS6; causes both increased MKKS protein degradation and reduced solubility relative to wild-type and Tyr-84 mutant; the mutant is immobilized at the centrosome even in the absence of proteasome inhibition; the mutant is also highly polyubiquitinated; no effect on import to the nucleus;, features a modification of the amino acid from Y to C at position 37.
+The protein's natural variant, known as in BBS6;, features a modification of the amino acid from G to R at position 41.
+The protein's natural variant, known as in BBS6; fails to associate with centrosome;, features a modification of the amino acid from G to D at position 52.
+The protein's natural variant, known as in BBS6; found in a patient also carrying A-155 in TMEM237; causes both increased MKKS protein degradation and reduced solubility relative to wild-type and Y-84 mutant; greatly reduces the ability to interact with BBS12;, features a modification of the amino acid from T to A at position 57.
+The protein's natural variant, known as in MKKS; associated with S-242; decreased interaction with BBS12; no effect on ciliogenesis; disrupts import to the nucleus; no effect on interaction with SMARCC1; may affect modulation of SMARCC1 subcellular location;, features a modification of the amino acid from H to Y at position 84.
+The protein's natural variant, known as in BBS6;, features a modification of the amino acid from C to R at position 99.
+The protein's natural variant, known as in BBS6; increases MKKS protein degradation; localizes properly to the centrosome;, features a modification of the amino acid from R to L at position 155.
+The protein's natural variant, known as in BBS6, features a modification of the amino acid from A to P at position 181.
+The protein's natural variant, known as in BBS6, features a modification of the amino acid from S to P at position 236.
+The protein's natural variant, known as in BBS6;, features a modification of the amino acid from T to A at position 237.
+The protein's natural variant, known as in BBS6, features a modification of the amino acid from T to P at position 237.
+The protein's natural variant, known as in MKKS and BBS6; associated with Y-84 in MKKS; unknown pathological significance; increases MKKS protein degradation; no effect on ciliogenesis; disrupts import to the nucleus; no effect on interaction with SMARCC1; may affect modulation of SMARCC1 subcellular location;, features a modification of the amino acid from A to S at position 242.
+The protein's natural variant, known as in BBS6; moderately affects interaction with BBS2; greatly reduces the ability to interact with BBS12;, features a modification of the amino acid from L to P at position 277.
+The protein's natural variant, known as in BBS6; fails to associate with centrosome, features a modification of the amino acid from D to A at position 286.
+The protein's natural variant, known as in BBS6;, features a modification of the amino acid from P to L at position 299.
+The protein's natural variant, known as has a modifier effect on BBS; causes a mislocalization of the protein; fails to associate with centrosome;, features a modification of the amino acid from T to P at position 325.
+The protein's natural variant, known as in BBS6; increases MKKS protein degradation; fails to associate with centrosome; the mutant is highly polyubiquitinated and rapidly degraded by the ubiquitin-proteasome protein degradation pathway;, features a modification of the amino acid from G to E at position 345.
+The protein's natural variant, known as in BBS6; atypical mild phenotype consisting of retinitis pigmentosa and polydactyly without other signs of Bardet-Biedl syndrome; results in decreased interaction with BBS12;, features a modification of the amino acid from H to R at position 395.
+The protein's natural variant, known as in BBS6, features a modification of the amino acid from S to P at position 460.
+The protein's natural variant, known as in a patient with Bardet-Biedl syndrome compound heterozygote for mutations in BBS12; uncertain pathological role;, features a modification of the amino acid from A to T at position 488.
+The protein's natural variant, known as in BBS6; unknown pathological significance;, features a modification of the amino acid from D to N at position 492.
+The protein's natural variant, known as in BBS6; causes both increased MKKS protein degradation and reduced solubility relative to wild-type and Tyr-84 mutant; localizes properly to the centrosome;, features a modification of the amino acid from C to S at position 499.
+The protein's natural variant, known as in BBS6, features a modification of the amino acid from S to A at position 511.
+The protein's natural variant, known as in BBS6;, features a modification of the amino acid from R to H at position 518.
+The protein's natural variant, known as found in infertile men; unknown pathological significance; decreased induction of target genes expression;, features a modification of the amino acid from G to R at position 68.
+The protein's natural variant, known as found in infertile men; unknown pathological significance;, features a modification of the amino acid from L to F at position 176.
+The protein's natural variant, known as found in infertile men; unknown pathological significance; decreased induction of target genes expression, features a modification of the amino acid from G to R at position 227.
+The protein's natural variant, known as found in infertile men; unknown pathological significance;, features a modification of the amino acid from D to G at position 235.
+The protein's natural variant, known as in strain: NC335, NC362 and NC390, features a modification of the amino acid from E to D at position 208.
+The protein's natural variant, known as in strain: NC335, NC362 and NC390, features a modification of the amino acid from H to V at position 219.
+The protein's natural variant, known as in strain: NC335, NC362 and NC390, features a modification of the amino acid from V to E at position 220.
+The protein's natural variant, known as in strain: MW25, features a modification of the amino acid from A to E at position 246.
+The protein's natural variant, known as in strain: MW25, features a modification of the amino acid from S to M at position 249.
+The protein's natural variant, known as in strain: NC306, features a modification of the amino acid from E to Q at position 281.
+The protein's natural variant, known as in strain: MW9, features a modification of the amino acid from K to T at position 349.
+The protein's natural variant, known as in strain: NC361 and NC375, features a modification of the amino acid from V to E at position 422.
+The protein's natural variant, known as in strain: MW6, features a modification of the amino acid from V to I at position 450.
+The protein's natural variant, known as in strain: MW6, features a modification of the amino acid from D to N at position 480.
+The protein's natural variant, known as in strain: MW25, MW27, MW56, MW9, NC303, NC306, NC335, NC336, NC390 and NC399, features a modification of the amino acid from E to Q at position 490.
+The protein's natural variant, known as in strain: NC303, NC306 and NC335, features a modification of the amino acid from V to I at position 491.
+The protein's natural variant, known as in strain: MW25, features a modification of the amino acid from C to S at position 580.
+The protein's natural variant, known as in strain: MW25, features a modification of the amino acid from M to I at position 586.
+The protein's natural variant, known as in strain: NC336, NC358, NC361, NC362 and NC375, features a modification of the amino acid from S to N at position 623.
+The protein's natural variant, known as in strain: NC357 and NC397, features a modification of the amino acid from T to S at position 646.
+The protein's natural variant, known as in strain: MW6, NC357, NC358, NC361, NC362, NC375 and NC397, features a modification of the amino acid from T to A at position 657.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation, features a modification of the amino acid from E to K at position 199.
+The protein's natural variant, known as likely benign variant; does not affect nuclear localization; no loss of transcriptional repression activity; no loss of ability to self-associate; no loss of interaction with FOXP2, features a modification of the amino acid from I to T at position 107.
+The protein's natural variant, known as does not affect nuclear localization; no loss of transcriptional repression activity; no loss of ability to self-associate; no loss of interaction with FOXP2;, features a modification of the amino acid from P to A at position 215.
+The natural variant of this protein is characterized by an amino acid alteration from S to P at position 261.
+The protein's natural variant, known as in MRLIAF; nuclear and cytoplasmic aggregation; loss of transcriptional repression activity; loss of ability to self-associate; loss of interaction with FOXP2;, features a modification of the amino acid from R to G at position 465.
+The protein's natural variant, known as in MRLIAF; nuclear and cytoplasmic aggregation; loss of transcriptional repression activity; loss of ability to self-associate; loss of interaction with FOXP2;, features a modification of the amino acid from R to C at position 514.
+The protein's natural variant, known as in MRLIAF; nuclear and cytoplasmic aggregation; loss of transcriptional repression activity; loss of ability to self-associate; loss of interaction with FOXP2;, features a modification of the amino acid from W to R at position 534.
+The protein's natural variant, known as does not affect nuclear localization; no loss of transcriptional repression activity; no loss of ability to self-associate; no loss of interaction with FOXP2;, features a modification of the amino acid from N to S at position 570.
+The protein's natural variant, known as in MRLIAF; unknown pathological significance; does not affect nuclear localization; no loss of transcriptional repression activity; no loss of ability to self-associate; no loss of interaction with FOXP2, features a modification of the amino acid from N to T at position 597.
+The protein's natural variant, known as in strain: Canetti and SO93, features a modification of the amino acid from R to Q at position 305.
+The protein's natural variant, known as in strain: Canetti and SO93, features a modification of the amino acid from A to L at position 430.
+The protein's natural variant, known as in strain: Canetti and SO93, features a modification of the amino acid from QQ to RR at position 435.
+The protein's natural variant, known as in strain: Canetti and SO93, features a modification of the amino acid from IY to VH at position 439.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from S to N at position 64.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from S to F at position 159.
+The natural variant of this protein is characterized by an amino acid alteration from W to R at position 60.
+The natural variant of this protein is characterized by an amino acid alteration from Q to R at position 94.
+The natural variant of this protein is characterized by an amino acid alteration from G to GGWGQPHGG at position 98.
+The natural variant of this protein is characterized by an amino acid alteration from S to N at position 154.
+The natural variant of this protein is characterized by an amino acid alteration from E to K at position 211.
+The natural variant of this protein is characterized by an amino acid alteration from Q to R at position 234.
+The protein's natural variant, known as in DA5D;, features a modification of the amino acid from R to C at position 404.
+The protein's natural variant, known as in DA5D;, features a modification of the amino acid from R to S at position 418.
+The protein's natural variant, known as in DA5D; patients have ophthalmoplegia, features a modification of the amino acid from G to S at position 607.
+The protein's natural variant, known as in DA5D;, features a modification of the amino acid from C to R at position 760.
+The protein's natural variant, known as in NEDMHS; unknown pathological significance;, features a modification of the amino acid from I to T at position 354.
+The protein's natural variant, known as in NEDMHS;, features a modification of the amino acid from G to E at position 468.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from D to N at position 578.
+The protein's natural variant, known as in strain: isolate Gabon 25, features a modification of the amino acid from I to V at position 19.
+The protein's natural variant, known as in strain: isolate Gabon 24, features a modification of the amino acid from S to G at position 20.
+The protein's natural variant, known as in strain: isolate Gabon 23, features a modification of the amino acid from L to I at position 24.
+The protein's natural variant, known as in strain: isolate Gabon 20, features a modification of the amino acid from D to G at position 84.
+The protein's natural variant, known as in strain: isolate Gabon 21, features a modification of the amino acid from K to E at position 108.
+The protein's natural variant, known as in strain: isolate Gabon 21, features a modification of the amino acid from V to A at position 135.
+The protein's natural variant, known as in strain: isolate Gabon 20, features a modification of the amino acid from G to S at position 151.
+The protein's natural variant, known as in strain: isolate Gabon 26, features a modification of the amino acid from I to T at position 166.
+The protein's natural variant, known as in strain: isolate Gabon 22, features a modification of the amino acid from D to N at position 167.
+The protein's natural variant, known as in strain: P1, features a modification of the amino acid from M to L at position 16.
+The protein's natural variant, known as in strain: P1, features a modification of the amino acid from N to S at position 23.
+The protein's natural variant, known as in strain: P1, features a modification of the amino acid from S to P at position 28.
+The protein's natural variant, known as in strain: P1, features a modification of the amino acid from A to R at position 74.
+The protein's natural variant, known as in strain: P1, features a modification of the amino acid from S to Q at position 79.
+The protein's natural variant, known as associated with susceptibility to ischemic stroke; increases autophosphorylation and kinase activity;, features a modification of the amino acid from V to I at position 374.
+The protein's natural variant, known as in a aLLTEL/AML1+ sample; somatic mutation;, features a modification of the amino acid from T to A at position 575.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation, features a modification of the amino acid from T to I at position 594.
+The protein's natural variant, known as in HGGI-I, HGGI-II and HGGI-III, features a modification of the amino acid from T to A at position 21.
+The protein's natural variant, known as in strain: Isolate Emaj614, features a modification of the amino acid from I to V at position 39.
+The protein's natural variant, known as in strain: Isolate Emaj556 and Isolate Emaj614, features a modification of the amino acid from I to V at position 42.
+The protein's natural variant, known as in strain: Isolate Emaj614, features a modification of the amino acid from I to M at position 240.
+The protein's natural variant, known as in strain: Isolate Emaj614, features a modification of the amino acid from I to V at position 327.
+The protein's natural variant, known as in strain: Isolate Emaj614, features a modification of the amino acid from I to T at position 334.
+The protein's natural variant, known as in strain: Isolate Emaj614, features a modification of the amino acid from I to A at position 349.
+The protein's natural variant, known as in strain: Isolate Emaj614, features a modification of the amino acid from V to I at position 356.
+The protein's natural variant, known as in FFEVF2;, features a modification of the amino acid from L to P at position 105.
+The protein's natural variant, known as in FFEVF2; unknown pathological significance, features a modification of the amino acid from T to S at position 110.
+The protein's natural variant, known as in FFEVF2; unknown pathological significance;, features a modification of the amino acid from P to H at position 198.
+The protein's natural variant, known as in FFEVF2; unknown pathological significance;, features a modification of the amino acid from D to H at position 214.
+The protein's natural variant, known as in FTDALS7; cells expressing the mutant protein have large cytoplasmic vacuoles with an accumulation of the mutant protein on the outer membrane termed halos; cells with the mutant protein also have aberrant localization of CD63 and an increase in MAP1LC3A1 overall indicating a defect in the autophagic pathway;, features a modification of the amino acid from I to V at position 29.
+The protein's natural variant, known as in FTDALS7; cells expressing the mutant protein have large cytoplasmic vacuoles with an accumulation of the mutant protein on the outer membrane termed halos; cells with the mutant protein also have aberrant localization of CD63 and an increase in MAP1LC3A overall indicating a defect in the autophagic pathway;, features a modification of the amino acid from T to N at position 104.
+The protein's natural variant, known as in FTDALS7;, features a modification of the amino acid from D to Y at position 148.
+The protein's natural variant, known as in FTDALS7; cells expressing the mutant protein have large cytoplasmic vacuoles with an accumulation of the mutant protein on the outer membrane termed halos; cells with the mutant protein also have aberrant localization of CD63 and an increase in MAP1LC3A overall indicating a defect in the autophagic pathway;, features a modification of the amino acid from Q to H at position 206.
+The protein's natural variant, known as in strain: 41, features a modification of the amino acid from A to S at position 39.
+The protein's natural variant, known as in strain: 41, features a modification of the amino acid from M to V at position 166.
+The protein's natural variant, known as in P.miliaris clone H22, features a modification of the amino acid from T to S at position 16.
+The protein's natural variant, known as in P.miliaris clone H22, features a modification of the amino acid from A to G at position 121.
+The protein's natural variant, known as in strain: cv. Ri-0, cv. Tul-0 and cv. Yo-1, features a modification of the amino acid from V to L at position 77.
+The protein's natural variant, known as in strain: cv. Cha-0, cv. Con, cv. Cvi-0, cv. Gr-5, cv. Ita-0, cv. Kas-1, cv. La-0, cv. Ler, cv. Me-0, cv. Mh-0, cv. Nc-1, cv. Per-1, cv. Ri-0, cv. Rsch-0, cv. Rub-1, cv. Tul-0, cv. Ws-0 and cv. Yo-1, features a modification of the amino acid from D to N at position 148.
+The protein's natural variant, known as in strain: cv. Me-0, cv. Mh-0, cv. Per-1 and cv. Ws-0, features a modification of the amino acid from E to K at position 158.
+The protein's natural variant, known as in strain: cv. Cha-0, cv. Con, cv. Cvi-0, cv. Gr-5, cv. Ita-0, cv. Kas-1, cv. La-0, cv. Ler, cv. Me-0, cv. Mh-0, cv. Nc-1, cv. Per-1, cv. Ri-0, cv. Rsch-0, cv. Rub-1, cv. Tul-0, cv. Ws-0 and cv. Yo-1, features a modification of the amino acid from D to A at position 350.
+The protein's natural variant, known as in strain: cv. Me-0, features a modification of the amino acid from D to N at position 354.
+The protein's natural variant, known as in tufA, features a modification of the amino acid from S to G at position 394.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 9.
+The natural variant of this protein is characterized by an amino acid alteration from D to E at position 19.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from G to A at position 76.
+The protein's natural variant, known as in strain: MT78, features a modification of the amino acid from I to V at position 52.
+The protein's natural variant, known as in strain: Wistar, features a modification of the amino acid from T to A at position 207.
+The protein's natural variant, known as in strain: Wistar, features a modification of the amino acid from F to I at position 213.
+The protein's natural variant, known as in strain: Wistar, features a modification of the amino acid from I to V at position 232.
+The protein's natural variant, known as in allele NKG2-D*02, features a modification of the amino acid from V to I at position 61.
+The protein's natural variant, known as in strain: cv. Ge-1, features a modification of the amino acid from S to N at position 45.
+The protein's natural variant, known as in strain: cv. Ge-1, features a modification of the amino acid from N to Y at position 269.
+The protein's natural variant, known as in strain: cv. Old-1, cv. Uk-3 and cv. Wassilewskija, features a modification of the amino acid from M to T at position 278.
+The protein's natural variant, known as in strain: cv. Nok-0, features a modification of the amino acid from I to T at position 373.
+The protein's natural variant, known as in strain: cv. Ca-0 and cv. Co, features a modification of the amino acid from N to K at position 415.
+The protein's natural variant, known as in strain: cv. Fi-1, features a modification of the amino acid from G to A at position 420.
+The protein's natural variant, known as in strain: cv. Old-1, cv. Uk-3 and cv. Wassilewskija, features a modification of the amino acid from I to S at position 438.
+The protein's natural variant, known as in strain: cv. Ca-0, features a modification of the amino acid from T to I at position 562.
+The protein's natural variant, known as in strain: cv. Di-1, cv. Fi-1, cv. Gie, cv. Old-1, cv. Uk-3 and cv. Wassilewskija, features a modification of the amino acid from T to R at position 612.
+The protein's natural variant, known as in strain: cv. Ca-0, features a modification of the amino acid from G to D at position 630.
+The protein's natural variant, known as in strain: cv. Di-1, cv. Fi-1, cv. Gie, cv. Old-1, cv. Uk-3 and cv. Wassilewskija, features a modification of the amino acid from E to Q at position 676.
+The protein's natural variant, known as in strain: cv. Tc, features a modification of the amino acid from K to E at position 167.
+The protein's natural variant, known as in strain: cv. Tc, features a modification of the amino acid from I to V at position 175.
+The protein's natural variant, known as in AGM10; very low protein expression, if any, in peripheral blood mononuclear cells; when tested in transfected cells, decreased transcription activation; in vitro, fails to bind PU motif-containing DNA probes; does not affect interaction with IRF4 and IRF8, nor nuclear localization;, features a modification of the amino acid from H to P at position 211.
+The protein's natural variant, known as in AGM10; very low protein expression, if any, in peripheral blood mononuclear cells; when tested in transfected cells, decreased transcription activation; in vitro, fails to bind PU motif-containing DNA probes; does not affect interaction with IRF4 and IRF8, nor nuclear localization, features a modification of the amino acid from V to G at position 241.
+The protein's natural variant, known as in ACLSD, features a modification of the amino acid from C to S at position 60.
+The protein's natural variant, known as in ACLSD;, features a modification of the amino acid from P to L at position 73.
+The protein's natural variant, known as in ACLSD, features a modification of the amino acid from L to P at position 127.
+The protein's natural variant, known as in ACLSD, features a modification of the amino acid from L to Q at position 134.
+The protein's natural variant, known as in ACLSD, features a modification of the amino acid from R to RSLR at position 197.
+The protein's natural variant, known as in ACLSD;, features a modification of the amino acid from L to F at position 244.
+The protein's natural variant, known as in ACLSD;, features a modification of the amino acid from N to S at position 276.
+The protein's natural variant, known as in ACLSD, features a modification of the amino acid from L to LLEL at position 439.
+The protein's natural variant, known as in ACLSD;, features a modification of the amino acid from D to N at position 440.
+The protein's natural variant, known as in ACLSD;, features a modification of the amino acid from C to R at position 540.
+The protein's natural variant, known as in DRTA3, features a modification of the amino acid from G to D at position 175.
+The protein's natural variant, known as in DRTA3;, features a modification of the amino acid from R to H at position 449.
+The protein's natural variant, known as in DRTA3;, features a modification of the amino acid from P to L at position 524.
+The protein's natural variant, known as in DRTA3;, features a modification of the amino acid from M to T at position 580.
+The protein's natural variant, known as in DRTA3;, features a modification of the amino acid from R to Q at position 807.
+The protein's natural variant, known as in DRTA3;, features a modification of the amino acid from G to R at position 820.
+The protein's natural variant, known as in strain: Norwegian Landrace, features a modification of the amino acid from Q to H at position 129.
+The protein's natural variant, known as in strain: Large white and Norwegian Landrace, features a modification of the amino acid from I to V at position 148.
+The protein's natural variant, known as in strain: Large white, features a modification of the amino acid from H to R at position 160.
+The protein's natural variant, known as in strain: Norwegian Landrace, features a modification of the amino acid from G to A at position 296.
+The protein's natural variant, known as in strain: Norwegian Landrace, features a modification of the amino acid from G to S at position 329.
+The protein's natural variant, known as in strain: Large white and Norwegian Landrace, features a modification of the amino acid from D to E at position 623.
+The protein's natural variant, known as in strain: Large white, features a modification of the amino acid from P to S at position 644.
+The protein's natural variant, known as in strain: Norwegian Landrace, features a modification of the amino acid from RS to Q at position 706.
+The protein's natural variant, known as in strain: Norwegian Landrace, features a modification of the amino acid from G to R at position 722.
+The protein's natural variant, known as in FBR mutant, features a modification of the amino acid from G to E at position 378.
+The protein's natural variant, known as in strain: W303-1a, features a modification of the amino acid from I to L at position 7.
+The protein's natural variant, known as in strain: W303-1a, features a modification of the amino acid from F to V at position 328.
+The protein's natural variant, known as in strain: W303-1a, features a modification of the amino acid from K to E at position 343.
+The protein's natural variant, known as in strain: W303-1a, features a modification of the amino acid from N to D at position 570.
+The protein's natural variant, known as in PHA2D; impaired interaction with CUL3;, features a modification of the amino acid from A to E at position 77.
+The protein's natural variant, known as in PHA2D; impaired interaction with CUL3;, features a modification of the amino acid from M to V at position 78.
+The protein's natural variant, known as in PHA2D; impaired interaction with CUL3;, features a modification of the amino acid from E to A at position 85.
+The protein's natural variant, known as in PHA2D; impaired interaction with CUL3; de novo mutation;, features a modification of the amino acid from C to F at position 164.
+The protein's natural variant, known as in PHA2D, features a modification of the amino acid from R to G at position 228.
+The protein's natural variant, known as in PHA2D; impaired interaction with WNK1;, features a modification of the amino acid from Q to R at position 309.
+The protein's natural variant, known as in PHA2D;, features a modification of the amino acid from F to C at position 322.
+The protein's natural variant, known as in PHA2D;, features a modification of the amino acid from R to I at position 336.
+The protein's natural variant, known as in PHA2D; does not affect interaction with WNK1 or CUL3;, features a modification of the amino acid from A to V at position 340.
+The protein's natural variant, known as in PHA2D, features a modification of the amino acid from V to M at position 361.
+The protein's natural variant, known as in PHA2D;, features a modification of the amino acid from R to W at position 362.
+The protein's natural variant, known as in PHA2D; impaired interaction with WNK1;, features a modification of the amino acid from R to Q at position 384.
+The protein's natural variant, known as in PHA2D;, features a modification of the amino acid from R to W at position 384.
+The protein's natural variant, known as in PHA2D; abolished interaction with WNK1;, features a modification of the amino acid from L to P at position 387.
+The protein's natural variant, known as in PHA2D;, features a modification of the amino acid from A to V at position 398.
+The protein's natural variant, known as in PHA2D; impaired interaction with WNK1;, features a modification of the amino acid from S to L at position 410.
+The protein's natural variant, known as in PHA2D;, features a modification of the amino acid from P to L at position 426.
+The protein's natural variant, known as in PHA2D;, features a modification of the amino acid from M to T at position 427.
+The protein's natural variant, known as in PHA2D;, features a modification of the amino acid from R to Q at position 431.
+The protein's natural variant, known as in PHA2D; impaired interaction with WNK1;, features a modification of the amino acid from S to N at position 432.
+The protein's natural variant, known as in PHA2D; decreased interaction with WNK4, features a modification of the amino acid from S to G at position 433.
+The protein's natural variant, known as in PHA2D;, features a modification of the amino acid from S to N at position 433.
+The protein's natural variant, known as found in a patient with hypertension; unknown pathological significance;, features a modification of the amino acid from V to I at position 438.
+The protein's natural variant, known as in PHA2D; does not affect interaction with WNK1 or CUL3;, features a modification of the amino acid from A to T at position 494.
+The protein's natural variant, known as in PHA2D, features a modification of the amino acid from H to Y at position 498.
+The protein's natural variant, known as in PHA2D;, features a modification of the amino acid from G to V at position 500.
+The protein's natural variant, known as in PHA2D;, features a modification of the amino acid from P to T at position 501.
+The protein's natural variant, known as in PHA2D; impaired interaction with WNK1;, features a modification of the amino acid from R to C at position 528.
+The protein's natural variant, known as in PHA2D; dominant negative effect due to homodimer formation; impaired interaction with WNK1 and WNK4 and impaired ubiquitination of WNK4;, features a modification of the amino acid from R to H at position 528.
+The protein's natural variant, known as in PHA2D; impaired interaction with WNK1;, features a modification of the amino acid from N to K at position 529.
+The protein's natural variant, known as in PHA2D;, features a modification of the amino acid from S to L at position 553.
+The protein's natural variant, known as in PHA2D;, features a modification of the amino acid from Y to C at position 557.
+The protein's natural variant, known as in PHA2D;, features a modification of the amino acid from R to W at position 575.
+The protein's natural variant, known as in HYPT11; does not affect subcellular localization;, features a modification of the amino acid from G to S at position 45.
+The protein's natural variant, known as in OSTEOP; associated with disease susceptibility, features a modification of the amino acid from A to AN at position 253.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from D to A at position 488.
+The protein's natural variant, known as in strain: Z17561, features a modification of the amino acid from N to K at position 27.
+The protein's natural variant, known as in strain: Z17561, features a modification of the amino acid from V to I at position 55.
+The protein's natural variant, known as in strain: Z17561, features a modification of the amino acid from Q to E at position 59.
+The protein's natural variant, known as in strain: Z17561, features a modification of the amino acid from T to P at position 66.
+The protein's natural variant, known as in strain: Z17561, features a modification of the amino acid from E to D at position 69.
+The protein's natural variant, known as in MTS; disrupts the assembly of the heterohexamer with TIMM13;, features a modification of the amino acid from C to W at position 66.
+The protein's natural variant, known as in HYC2; unknown pathological significance;, features a modification of the amino acid from A to T at position 1760.
+The protein's natural variant, known as in strain: 297, features a modification of the amino acid from F to S at position 278.
+The protein's natural variant, known as in MRD34;, features a modification of the amino acid from S to L at position 132.
+The protein's natural variant, known as found in a patient with intellectual disability, features a modification of the amino acid from S to C at position 138.
+The protein's natural variant, known as in MRD34; associated with authism and epilepsy, features a modification of the amino acid from G to R at position 243.
+The protein's natural variant, known as in Macedonia-I;, features a modification of the amino acid from H to Q at position 3.
+The protein's natural variant, known as in Texas-1;, features a modification of the amino acid from E to K at position 6.
+The protein's natural variant, known as in Izumi/Kotobuki;, features a modification of the amino acid from E to G at position 7.
+The protein's natural variant, known as in Pordenone;, features a modification of the amino acid from E to Q at position 7.
+The protein's natural variant, known as in Calluna;, features a modification of the amino acid from T to R at position 13.
+The protein's natural variant, known as in Kuala Lumpur;, features a modification of the amino acid from D to G at position 23.
+The protein's natural variant, known as in Xinjiang; unstable;, features a modification of the amino acid from G to R at position 26.
+The protein's natural variant, known as in Pendergrass;, features a modification of the amino acid from P to R at position 37.
+The protein's natural variant, known as in Cobb;, features a modification of the amino acid from W to G at position 38.
+The protein's natural variant, known as in Bonaire;, features a modification of the amino acid from Q to R at position 40.
+The protein's natural variant, known as in Woodstock;, features a modification of the amino acid from R to K at position 41.
+The protein's natural variant, known as in Fukuyama;, features a modification of the amino acid from D to N at position 44.
+The protein's natural variant, known as in Beech island;, features a modification of the amino acid from A to D at position 54.
+The protein's natural variant, known as in Jamaica;, features a modification of the amino acid from K to E at position 62.
+The protein's natural variant, known as in Iwata;, features a modification of the amino acid from G to R at position 73.
+The protein's natural variant, known as in Xin-su;, features a modification of the amino acid from D to H at position 74.
+The protein's natural variant, known as in Forest Park; associated with T-76;, features a modification of the amino acid from D to N at position 74.
+The protein's natural variant, known as in Sardinia/Forest Park; associated with N-74;, features a modification of the amino acid from I to T at position 76.
+The protein's natural variant, known as in Dammam;, features a modification of the amino acid from D to N at position 80.
+The protein's natural variant, known as in Yamaguchi;, features a modification of the amino acid from D to N at position 81.
+The protein's natural variant, known as in Victoria jubilee;, features a modification of the amino acid from D to Y at position 81.
+The protein's natural variant, known as in Dickinson;, features a modification of the amino acid from H to R at position 98.
+The protein's natural variant, known as in Siena/Hull;, features a modification of the amino acid from E to K at position 122.
+The protein's natural variant, known as in Baskent;, features a modification of the amino acid from A to T at position 129.
+The protein's natural variant, known as in Jiangsu;, features a modification of the amino acid from V to M at position 135.
+The protein's natural variant, known as in PARK15; unknown pathological significance, features a modification of the amino acid from L to R at position 34.
+The protein's natural variant, known as in PARK15; no effect on interaction with PRKN;, features a modification of the amino acid from R to G at position 378.
+The protein's natural variant, known as found in two patients with Kufor-Rakeb syndrome also carrying R-877 in ATP13A2;, features a modification of the amino acid from R to C at position 481.
+The protein's natural variant, known as in strain: RM220-3, features a modification of the amino acid from ANED to EDEA at position 32.
+The protein's natural variant, known as in strain: RM220-3, features a modification of the amino acid from E to D at position 54.
+The protein's natural variant, known as in strain: RM220-3, features a modification of the amino acid from F to S at position 67.
+The protein's natural variant, known as in strain: RM220-3, features a modification of the amino acid from A to P at position 74.
+The protein's natural variant, known as in strain: RM220-3, features a modification of the amino acid from D to N at position 92.
+The natural variant of this protein is characterized by an amino acid alteration from I to T at position 598.
+The natural variant of this protein is characterized by an amino acid alteration from V to M at position 930.
+The protein's natural variant, known as in strain: IFO 16449, features a modification of the amino acid from TGT to NGS at position 114.
+The protein's natural variant, known as in strain: IFO 16449, features a modification of the amino acid from V to I at position 224.
+The protein's natural variant, known as in strain: IFO 16449, features a modification of the amino acid from E to K at position 354.
+The protein's natural variant, known as in AGS3;, features a modification of the amino acid from R to H at position 13.
+The protein's natural variant, known as in AGS3;, features a modification of the amino acid from D to Y at position 39.
+The protein's natural variant, known as in AGS3;, features a modification of the amino acid from R to W at position 69.
+The protein's natural variant, known as in AGS3;, features a modification of the amino acid from P to L at position 76.
+The protein's natural variant, known as in AGS3, features a modification of the amino acid from P to L at position 138.
+The protein's natural variant, known as in AGS3;, features a modification of the amino acid from K to I at position 143.
+The protein's natural variant, known as in AGS3;, features a modification of the amino acid from P to S at position 151.
+The protein's natural variant, known as in MC4DN20; decreased protein abundance in patient fibroblasts; decreased proteins abundance of mitochondrial respiratory chain complex IV in patient fibroblasts; no effect on respiratory chain complex IV assembly in patient fibroblasts; increased protein abundance of S1 complex IV intermediate in patient fibroblasts, features a modification of the amino acid from R to C at position 107.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from T to S at position 215.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from KT to QP at position 239.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from L to P at position 259.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from P to A at position 384.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from S to T at position 904.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from N to T at position 88.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from S to I at position 193.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to Q at position 765.
+The protein's natural variant, known as in strain: CEN.PK 113-7D, features a modification of the amino acid from Q to H at position 7.
+The protein's natural variant, known as in strain: CEN.PK 113-7D, features a modification of the amino acid from V to A at position 40.
+The protein's natural variant, known as in strain: CEN.PK 113-7D, features a modification of the amino acid from V to L at position 49.
+The protein's natural variant, known as in strain: CEN.PK 113-7D, features a modification of the amino acid from IL to VF at position 71.
+The protein's natural variant, known as in strain: FVB/N, features a modification of the amino acid from S to P at position 1420.
+The protein's natural variant, known as found in a patient with hypothalamic hamartoma; unknown pathological significance;, features a modification of the amino acid from R to W at position 646.
+The natural variant of this protein is characterized by an amino acid alteration from G to A at position 287.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from A to V at position 96.
+The natural variant of this protein is characterized by an amino acid alteration from D to Y at position 40.
+The natural variant of this protein is characterized by an amino acid alteration from D to L at position 376.
+The protein's natural variant, known as in cv. Borszczagowski, features a modification of the amino acid from S to K at position 222.
+The protein's natural variant, known as in cv. Borszczagowski, features a modification of the amino acid from F to S at position 285.
+The protein's natural variant, known as in HH10; phenotype consistent with normosmic idiopathic hypogonadotropic hypogonadism; the patient also carries a mutation in HS6ST1;, features a modification of the amino acid from R to S at position 80.
+The protein's natural variant, known as in HH10; has markedly reduced activity;, features a modification of the amino acid from M to T at position 90.
+The protein's natural variant, known as in GSD9A, features a modification of the amino acid from T to TYNTAT at position 120.
+The protein's natural variant, known as in GSD9A; type 2;, features a modification of the amino acid from H to P at position 132.
+The protein's natural variant, known as in GSD9A; type 2;, features a modification of the amino acid from H to Y at position 132.
+The protein's natural variant, known as in GSD9A; type 2;, features a modification of the amino acid from R to C at position 186.
+The protein's natural variant, known as in GSD9A; type 2;, features a modification of the amino acid from R to H at position 186.
+The protein's natural variant, known as in GSD9A; type 2;, features a modification of the amino acid from K to E at position 189.
+The protein's natural variant, known as in GSD9A; type 2, features a modification of the amino acid from G to V at position 193.
+The protein's natural variant, known as in GSD9A; type 1 and type 2;, features a modification of the amino acid from R to H at position 295.
+The protein's natural variant, known as in GSD9A; type 2;, features a modification of the amino acid from D to G at position 299.
+The protein's natural variant, known as in GSD9A; type 1, features a modification of the amino acid from P to S at position 399.
+The protein's natural variant, known as in GSD9A;, features a modification of the amino acid from P to L at position 498.
+The protein's natural variant, known as in GSD9A;, features a modification of the amino acid from P to R at position 869.
+The protein's natural variant, known as in GSD9A;, features a modification of the amino acid from R to W at position 916.
+The protein's natural variant, known as in GSD9A; type 1, features a modification of the amino acid from NL to I at position 954.
+The protein's natural variant, known as in GSD9A; type 2, features a modification of the amino acid from R to RTR at position 1111.
+The protein's natural variant, known as in GSD9A, features a modification of the amino acid from M to I at position 1113.
+The protein's natural variant, known as in GSD9A; type 2;, features a modification of the amino acid from T to I at position 1114.
+The protein's natural variant, known as in GSD9A; type 1;, features a modification of the amino acid from E to K at position 1125.
+The protein's natural variant, known as in GSD9A; type 1;, features a modification of the amino acid from P to L at position 1205.
+The protein's natural variant, known as in GSD9A; type 1, features a modification of the amino acid from G to W at position 1207.
+The protein's natural variant, known as in strain: 129/1224, features a modification of the amino acid from D to A at position 24.
+The protein's natural variant, known as in MC3DN8; results in impaired incorporation of the Rieske Fe-S protein into the CIII complex;, features a modification of the amino acid from D to N at position 25.
+The protein's natural variant, known as in clone M6, features a modification of the amino acid from I to T at position 66.
+The protein's natural variant, known as in clone M6, features a modification of the amino acid from K to N at position 414.
+The protein's natural variant, known as in strain: Isolate CN 97682, features a modification of the amino acid from I to V at position 211.
+The protein's natural variant, known as in strain: Isolate TK 18513, features a modification of the amino acid from D to N at position 214.
+The protein's natural variant, known as in strain: Isolate TK 15708 and Isolate TK 18513, features a modification of the amino acid from T to I at position 215.
+The natural variant of this protein is characterized by an amino acid alteration from S to T at position 171.
+The protein's natural variant, known as de novo variant found in a patient with childhood apraxia of speech; unknown pathological significance, features a modification of the amino acid from S to C at position 307.
+The protein's natural variant, known as no effect on creatine transporter activity;, features a modification of the amino acid from K to R at position 4.
+The protein's natural variant, known as no effect on creatine transporter activity;, features a modification of the amino acid from G to R at position 26.
+The protein's natural variant, known as in CCDS1, features a modification of the amino acid from Y to H at position 80.
+The protein's natural variant, known as in CCDS1; decreased creatine transporter activity;, features a modification of the amino acid from G to R at position 87.
+The protein's natural variant, known as in CCDS1;, features a modification of the amino acid from G to V at position 132.
+The protein's natural variant, known as in CCDS1; unknown pathological significance; loss of creatine transporter activity; no effect on cell membrane localization, features a modification of the amino acid from C to R at position 181.
+The protein's natural variant, known as 82.0% of wild type creatine transporter activity;, features a modification of the amino acid from R to H at position 186.
+The protein's natural variant, known as no effect on creatine transporter activity;, features a modification of the amino acid from V to M at position 270.
+The protein's natural variant, known as no effect on creatine transporter activity;, features a modification of the amino acid from K to Q at position 294.
+The protein's natural variant, known as 65.0% of wild type creatine transporter activity;, features a modification of the amino acid from F to L at position 314.
+The protein's natural variant, known as 78.0% of wild type creatine transporter activity;, features a modification of the amino acid from A to T at position 318.
+The protein's natural variant, known as in CCDS1; decreased creatine transporter activity;, features a modification of the amino acid from C to W at position 337.
+The protein's natural variant, known as in CCDS1;, features a modification of the amino acid from G to R at position 381.
+The protein's natural variant, known as in CCDS1, features a modification of the amino acid from G to C at position 383.
+The protein's natural variant, known as in CCDS1; decreased creatine transporter activity, features a modification of the amino acid from P to L at position 390.
+The protein's natural variant, known as in CCDS1; decreased creatine transporter activity;, features a modification of the amino acid from R to W at position 391.
+The protein's natural variant, known as in CCDS1, features a modification of the amino acid from A to D at position 448.
+The protein's natural variant, known as in CCDS1;, features a modification of the amino acid from C to W at position 491.
+The protein's natural variant, known as in CCDS1;, features a modification of the amino acid from V to I at position 539.
+The protein's natural variant, known as in CCDS1; unknown pathological significance; 35.0% of wild type creatine transporter activity;, features a modification of the amino acid from V to L at position 552.
+The protein's natural variant, known as in CCDS1; decreased creatine transporter activity;, features a modification of the amino acid from P to L at position 554.
+The protein's natural variant, known as no effect on creatine transporter activity;, features a modification of the amino acid from M to V at position 560.
+The protein's natural variant, known as no effect on creatine transporter activity;, features a modification of the amino acid from F to L at position 564.
+The protein's natural variant, known as no effect on creatine transporter activity;, features a modification of the amino acid from A to T at position 611.
+The protein's natural variant, known as no effect on creatine transporter activity;, features a modification of the amino acid from E to K at position 624.
+The protein's natural variant, known as no effect on creatine transporter activity;, features a modification of the amino acid from V to I at position 629.
+The protein's natural variant, known as in ND;, features a modification of the amino acid from L to R at position 13.
+The protein's natural variant, known as in ND, features a modification of the amino acid from L to P at position 16.
+The protein's natural variant, known as in EVR2; the patient presented significant phenotypic heterogeneity between the two eyes, features a modification of the amino acid from I to K at position 18.
+The protein's natural variant, known as in ND and EVR2;, features a modification of the amino acid from R to C at position 38.
+The protein's natural variant, known as in ND, features a modification of the amino acid from C to R at position 39.
+The protein's natural variant, known as in EVR2, features a modification of the amino acid from R to K at position 41.
+The protein's natural variant, known as in persistent fetal vasculature syndrome, features a modification of the amino acid from R to S at position 41.
+The protein's natural variant, known as in EVR2;, features a modification of the amino acid from H to R at position 42.
+The protein's natural variant, known as in ND, features a modification of the amino acid from H to Q at position 43.
+The protein's natural variant, known as in ND, features a modification of the amino acid from H to R at position 43.
+The protein's natural variant, known as in ND;, features a modification of the amino acid from Y to C at position 44.
+The protein's natural variant, known as in ND;, features a modification of the amino acid from V to E at position 45.
+The protein's natural variant, known as in ND, features a modification of the amino acid from V to M at position 45.
+The protein's natural variant, known as in EVR2, features a modification of the amino acid from K to N at position 54.
+The protein's natural variant, known as in ND, features a modification of the amino acid from C to R at position 55.
+The protein's natural variant, known as in ND and EVR2, features a modification of the amino acid from K to N at position 58.
+The protein's natural variant, known as in ND; reduction of protein amount in the extracellular matrix;, features a modification of the amino acid from V to E at position 60.
+The protein's natural variant, known as in ND;, features a modification of the amino acid from L to F at position 61.
+The protein's natural variant, known as in EVR2, features a modification of the amino acid from L to I at position 61.
+The protein's natural variant, known as in ND, features a modification of the amino acid from L to P at position 61.
+The protein's natural variant, known as in ND, features a modification of the amino acid from A to D at position 63.
+The protein's natural variant, known as in ND, features a modification of the amino acid from C to W at position 65.
+The protein's natural variant, known as in ND;, features a modification of the amino acid from C to Y at position 65.
+The protein's natural variant, known as in ND;, features a modification of the amino acid from G to E at position 67.
+The protein's natural variant, known as in ND, features a modification of the amino acid from G to R at position 67.
+The protein's natural variant, known as in ND; unknown pathological significance, features a modification of the amino acid from C to G at position 69.
+The protein's natural variant, known as in ND; unknown pathological significance;, features a modification of the amino acid from C to S at position 69.
+The protein's natural variant, known as in ND;, features a modification of the amino acid from R to C at position 74.
+The protein's natural variant, known as in ND;, features a modification of the amino acid from S to C at position 75.
+The protein's natural variant, known as in ND, features a modification of the amino acid from S to P at position 75.
+The protein's natural variant, known as in ND;, features a modification of the amino acid from F to L at position 89.
+The protein's natural variant, known as in ND;, features a modification of the amino acid from R to C at position 90.
+The protein's natural variant, known as in ND;, features a modification of the amino acid from R to P at position 90.
+The protein's natural variant, known as in ND, features a modification of the amino acid from S to P at position 92.
+The protein's natural variant, known as in ND, features a modification of the amino acid from HCC to QCGL at position 96.
+The protein's natural variant, known as in ND, features a modification of the amino acid from C to F at position 95.
+The protein's natural variant, known as in ND, features a modification of the amino acid from C to R at position 95.
+The protein's natural variant, known as in ND;, features a modification of the amino acid from C to W at position 96.
+The protein's natural variant, known as in ND;, features a modification of the amino acid from C to Y at position 96.
+The protein's natural variant, known as in ND, features a modification of the amino acid from R to P at position 97.
+The protein's natural variant, known as in ND, features a modification of the amino acid from P to L at position 98.
+The protein's natural variant, known as in ND;, features a modification of the amino acid from S to F at position 101.
+The protein's natural variant, known as in EVR2, features a modification of the amino acid from L to V at position 103.
+The protein's natural variant, known as in ND, features a modification of the amino acid from K to N at position 104.
+The protein's natural variant, known as in ND, features a modification of the amino acid from K to Q at position 104.
+The protein's natural variant, known as in ND;, features a modification of the amino acid from A to T at position 105.
+The protein's natural variant, known as in retinopathy of prematurity, features a modification of the amino acid from L to P at position 108.
+The protein's natural variant, known as in ND;, features a modification of the amino acid from C to G at position 110.
+The protein's natural variant, known as in ND, features a modification of the amino acid from C to R at position 110.
+The protein's natural variant, known as in ND, features a modification of the amino acid from G to E at position 112.
+The protein's natural variant, known as in EVR2, features a modification of the amino acid from R to L at position 115.
+The protein's natural variant, known as in ND, features a modification of the amino acid from A to D at position 118.
+The protein's natural variant, known as in EVR2, features a modification of the amino acid from Y to C at position 120.
+The protein's natural variant, known as in EVR2, features a modification of the amino acid from R to G at position 121.
+The protein's natural variant, known as in EVR2;, features a modification of the amino acid from R to L at position 121.
+The protein's natural variant, known as in EVR2 and ND; reduced amount of protein in the extracellular matrix, features a modification of the amino acid from R to Q at position 121.
+The protein's natural variant, known as in ND and EVR2;, features a modification of the amino acid from R to W at position 121.
+The protein's natural variant, known as in ND, features a modification of the amino acid from I to N at position 123.
+The protein's natural variant, known as in EVR2;, features a modification of the amino acid from L to F at position 124.
+The protein's natural variant, known as in ND, features a modification of the amino acid from C to S at position 126.
+The protein's natural variant, known as in ND, features a modification of the amino acid from C to R at position 128.
+The protein's natural variant, known as in a neuroblastoma sample; increased motility of carcinoma cells;, features a modification of the amino acid from S to G at position 120.
+The protein's natural variant, known as phosphorylated;, features a modification of the amino acid from N to S at position 159.
+The protein's natural variant, known as in strain: NRRLY-553, features a modification of the amino acid from E to G at position 37.
+The protein's natural variant, known as in strain: NRRLY-553, features a modification of the amino acid from L to W at position 91.
+The protein's natural variant, known as in strain: NRCC 205002 and NRRLY-553, features a modification of the amino acid from I to L at position 102.
+The protein's natural variant, known as in strain: NRCC 205002, features a modification of the amino acid from N to S at position 201.
+The protein's natural variant, known as in strain: NRRLY-553, features a modification of the amino acid from Q to K at position 259.
+The protein's natural variant, known as in strain: NRCC 205002, features a modification of the amino acid from A to T at position 297.
+The protein's natural variant, known as in strain: NRCC 205002 and NRRLY-553, features a modification of the amino acid from G to S at position 300.
+The protein's natural variant, known as in strain: NRCC 205002, features a modification of the amino acid from E to D at position 303.
+The protein's natural variant, known as in strain: NRCC 205002, features a modification of the amino acid from E to Q at position 400.
+The protein's natural variant, known as in strain: NRRLY-552, features a modification of the amino acid from S to P at position 405.
+The protein's natural variant, known as in strain: NRCC 205002, features a modification of the amino acid from A to S at position 421.
+The protein's natural variant, known as in strain: NRCC 205002, features a modification of the amino acid from K to Q at position 520.
+The protein's natural variant, known as in strain: NRCC 205002, NRRLY-552 and NRRLY-553, features a modification of the amino acid from S to A at position 528.
+The protein's natural variant, known as in strain: NRRLY-553, features a modification of the amino acid from I to V at position 538.
+The protein's natural variant, known as in OPA1; unknown pathological significance;, features a modification of the amino acid from A to S at position 8.
+The protein's natural variant, known as in OPA1;, features a modification of the amino acid from Y to C at position 80.
+The protein's natural variant, known as in OPA1;, features a modification of the amino acid from T to M at position 95.
+The protein's natural variant, known as in OPA1;, features a modification of the amino acid from Y to C at position 102.
+The protein's natural variant, known as in OPA1, features a modification of the amino acid from E to K at position 270.
+The protein's natural variant, known as in OPA1, features a modification of the amino acid from L to P at position 272.
+The protein's natural variant, known as in OPA1, features a modification of the amino acid from D to A at position 273.
+The protein's natural variant, known as in OPA1;, features a modification of the amino acid from R to Q at position 290.
+The protein's natural variant, known as in OPA1;, features a modification of the amino acid from R to W at position 290.
+The protein's natural variant, known as in OPA1; loss of GTPase activity; loss of function in promoting mitochondrial fusion;, features a modification of the amino acid from G to E at position 300.
+The protein's natural variant, known as in OPA1;, features a modification of the amino acid from Q to R at position 310.
+The protein's natural variant, known as in OPA1, features a modification of the amino acid from T to S at position 330.
+The protein's natural variant, known as in DOA+ and OPA1;, features a modification of the amino acid from A to T at position 357.
+The protein's natural variant, known as in OPA1;, features a modification of the amino acid from V to I at position 377.
+The protein's natural variant, known as in OPA1 and BEHRS;, features a modification of the amino acid from I to M at position 382.
+The protein's natural variant, known as in OPA1, features a modification of the amino acid from L to F at position 384.
+The protein's natural variant, known as in OPA1;, features a modification of the amino acid from L to P at position 396.
+The protein's natural variant, known as in OPA1;, features a modification of the amino acid from L to R at position 396.
+The protein's natural variant, known as in OPA1, features a modification of the amino acid from P to A at position 400.
+The protein's natural variant, known as in BEHRS;, features a modification of the amino acid from V to M at position 402.
+The protein's natural variant, known as in OPA1, features a modification of the amino acid from N to D at position 430.
+The protein's natural variant, known as in OPA1, features a modification of the amino acid from D to V at position 438.
+The protein's natural variant, known as in DOA+ and OPA1; decreased GTPase activity; loss of function in promoting mitochondrial fusion;, features a modification of the amino acid from G to V at position 439.
+The protein's natural variant, known as in DOA+ and OPA1; decreased GTPase activity; loss of function in promoting mitochondrial fusion;, features a modification of the amino acid from R to H at position 445.
+The protein's natural variant, known as in DOA+, features a modification of the amino acid from T to P at position 449.
+The protein's natural variant, known as in OPA1;, features a modification of the amino acid from T to R at position 449.
+The protein's natural variant, known as in OPA1, features a modification of the amino acid from G to E at position 459.
+The protein's natural variant, known as in OPA1, features a modification of the amino acid from I to IFIF at position 463.
+The protein's natural variant, known as in OPA1, features a modification of the amino acid from K to E at position 468.
+The protein's natural variant, known as in OPA1, features a modification of the amino acid from D to G at position 470.
+The protein's natural variant, known as in OPA1 and BEHRS, features a modification of the amino acid from E to K at position 487.
+The natural variant of this protein is characterized by an amino acid alteration from V to G at position 502.
+The protein's natural variant, known as in OPA1, features a modification of the amino acid from T to K at position 503.
+The protein's natural variant, known as in OPA1, features a modification of the amino acid from K to N at position 505.
+The protein's natural variant, known as in MTDPS14;, features a modification of the amino acid from L to R at position 534.
+The protein's natural variant, known as in DOA+ and OPA1; decreased GTPase activity; loss of function in promoting mitochondrial fusion;, features a modification of the amino acid from S to R at position 545.
+The natural variant of this protein is characterized by an amino acid alteration from D to N at position 550.
+The protein's natural variant, known as in OPA1 and DOA+;, features a modification of the amino acid from C to Y at position 551.
+The protein's natural variant, known as in OPA1;, features a modification of the amino acid from R to H at position 571.
+The protein's natural variant, known as in OPA1;, features a modification of the amino acid from L to P at position 574.
+The protein's natural variant, known as in DOA+;, features a modification of the amino acid from Y to C at position 582.
+The protein's natural variant, known as in OPA1;, features a modification of the amino acid from R to Q at position 590.
+The protein's natural variant, known as in OPA1;, features a modification of the amino acid from R to W at position 590.
+The protein's natural variant, known as in OPA1, features a modification of the amino acid from L to P at position 593.
+The protein's natural variant, known as in OPA1, features a modification of the amino acid from S to L at position 646.
+The protein's natural variant, known as in OPA1; loss of function in promoting mitochondrial fusion;, features a modification of the amino acid from N to K at position 728.
+The protein's natural variant, known as in OPA1, features a modification of the amino acid from G to D at position 768.
+The protein's natural variant, known as in OPA1;, features a modification of the amino acid from R to W at position 781.
+The protein's natural variant, known as in OPA1; loss of lipid binding and partial loss of function in promoting mitochondrial fusion;, features a modification of the amino acid from Q to R at position 785.
+The protein's natural variant, known as in OPA1, features a modification of the amino acid from S to Y at position 823.
+The protein's natural variant, known as in OPA1, features a modification of the amino acid from Y to C at position 841.
+The protein's natural variant, known as in OPA1, features a modification of the amino acid from R to L at position 882.
+The protein's natural variant, known as in OPA1, features a modification of the amino acid from L to P at position 887.
+The protein's natural variant, known as in DOA+; impairs protein folding; loss of function in promoting mitochondrial fusion;, features a modification of the amino acid from V to D at position 910.
+The protein's natural variant, known as in OPA1;, features a modification of the amino acid from R to C at position 932.
+The protein's natural variant, known as in OPA1; impairs protein folding; loss of function in promoting mitochondrial fusion, features a modification of the amino acid from L to P at position 939.
+The protein's natural variant, known as in OPA1, features a modification of the amino acid from L to P at position 949.
+The natural variant of this protein is characterized by an amino acid alteration from K to R at position 81.
+The protein's natural variant, known as in IDDABS; unknown pathological significance; mild phenotype; decreased pseudouridylate synthase activity, features a modification of the amino acid from G to R at position 128.
+The protein's natural variant, known as in IDDABS; unknown pathological significance, features a modification of the amino acid from T to M at position 387.
+The protein's natural variant, known as in IDDABS; decreased pseudouridylate synthase activity, features a modification of the amino acid from D to Y at position 503.
+The protein's natural variant, known as in clinical isolates: GKK-1 and GKK-3; colistin-resistant, features a modification of the amino acid from A to T at position 259.
+The protein's natural variant, known as in clone 2, features a modification of the amino acid from V to M at position 215.
+The natural variant of this protein is characterized by an amino acid alteration from K to R at position 308.
+The protein's natural variant, known as in strain: ATCC 90240 / AF-10, features a modification of the amino acid from S to N at position 498.
+The protein's natural variant, known as in strain: ATCC 90240 / AF-10, features a modification of the amino acid from DGSL to NGTV at position 593.
+The protein's natural variant, known as defines the adult i phenotype;, features a modification of the amino acid from A to T at position 169.
+The protein's natural variant, known as defines the adult i phenotype;, features a modification of the amino acid from R to Q at position 228.
+The protein's natural variant, known as in CTRCT13; unknown pathological significance;, features a modification of the amino acid from G to E at position 350.
+The protein's natural variant, known as in CTRCT13; unknown pathological significance, features a modification of the amino acid from F to S at position 364.
+The protein's natural variant, known as in CTRCT13; unknown pathological significance;, features a modification of the amino acid from R to H at position 385.
+The natural variant of this protein is characterized by an amino acid alteration from S to T at position 52.
+The natural variant of this protein is characterized by an amino acid alteration from H to R at position 80.
+The protein's natural variant, known as in SPGF48; unknown pathological significance, features a modification of the amino acid from S to P at position 50.
+The protein's natural variant, known as in SPGF48; unknown pathological significance, features a modification of the amino acid from R to Q at position 266.
+The protein's natural variant, known as in SPGF48; unknown pathological significance, features a modification of the amino acid from G to R at position 317.
+The protein's natural variant, known as in SPGF48; unknown pathological significance, features a modification of the amino acid from P to L at position 389.
+The protein's natural variant, known as in SPGF48; unknown pathological significance, features a modification of the amino acid from L to P at position 430.
+The protein's natural variant, known as in EDSSPD3; unknown pathological significance;, features a modification of the amino acid from G to D at position 74.
+The protein's natural variant, known as in strain: C57BL, features a modification of the amino acid from N to S at position 374.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from L to I at position 92.
+The protein's natural variant, known as specific to the Northeast Asian population; associated with increased susceptibility of sedentary males to type 2 diabetes; increased plasma levels of MOTS-c peptide, features a modification of the amino acid from K to Q at position 14.
+The protein's natural variant, known as in a form with an abnormally low affinity for methotrexate, features a modification of the amino acid from L to R at position 23.
+The protein's natural variant, known as in L-5178-Y cell line; methotrexate-resistant, requires 2 nucleotide substitutions, features a modification of the amino acid from F to W at position 32.
+The protein's natural variant, known as in the samba murine model of hearing loss, features a modification of the amino acid from I to N at position 1342.
+The protein's natural variant, known as probable disease-associated variant found in patients with global developmental delay and autism spectrum disorder;, features a modification of the amino acid from H to Y at position 63.
+The protein's natural variant, known as in BILU; loss-of-function variant in a yeast complementation assay, features a modification of the amino acid from S to L at position 488.
+The protein's natural variant, known as in BILU; decreased protein abundance; severely decreased DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity, features a modification of the amino acid from A to P at position 490.
+The protein's natural variant, known as in BILU; loss-of-function variant in a yeast complementation assay, features a modification of the amino acid from G to S at position 638.
+The protein's natural variant, known as in WS1, features a modification of the amino acid from F to L at position 45.
+The protein's natural variant, known as in WS3;, features a modification of the amino acid from N to H at position 47.
+The protein's natural variant, known as in CDHS;, features a modification of the amino acid from N to K at position 47.
+The protein's natural variant, known as in WS1;, features a modification of the amino acid from G to R at position 48.
+The protein's natural variant, known as in WS1; important hearing loss;, features a modification of the amino acid from P to L at position 50.
+The protein's natural variant, known as in WS1; associated with meningomyelocele;, features a modification of the amino acid from R to L at position 56.
+The protein's natural variant, known as in WS1, features a modification of the amino acid from I to F at position 59.
+The protein's natural variant, known as in WS1, features a modification of the amino acid from I to N at position 59.
+The protein's natural variant, known as in WS1, features a modification of the amino acid from V to M at position 60.
+The protein's natural variant, known as in WS1, features a modification of the amino acid from M to V at position 62.
+The protein's natural variant, known as in WS1;, features a modification of the amino acid from S to L at position 73.
+The protein's natural variant, known as in WS1, features a modification of the amino acid from V to M at position 78.
+The protein's natural variant, known as in WS1; results in decreased transcriptional activation of MITF; no effect on localization to nucleus; no effect on interaction with SOX10;, features a modification of the amino acid from H to D at position 80.
+The protein's natural variant, known as in WS1; originally classified as Waardenburg syndrome type 2;, features a modification of the amino acid from G to A at position 81.
+The protein's natural variant, known as in WS3;, features a modification of the amino acid from S to F at position 84.
+The protein's natural variant, known as in WS1, features a modification of the amino acid from K to E at position 85.
+The protein's natural variant, known as in WS3;, features a modification of the amino acid from Y to H at position 90.
+The protein's natural variant, known as in WS1;, features a modification of the amino acid from G to D at position 99.
+The protein's natural variant, known as in WS1, features a modification of the amino acid from L to P at position 234.
+The protein's natural variant, known as in WS1, features a modification of the amino acid from F to S at position 238.
+The protein's natural variant, known as in WS1, features a modification of the amino acid from V to F at position 265.
+The protein's natural variant, known as in WS1, features a modification of the amino acid from W to C at position 266.
+The protein's natural variant, known as in WS1 and WS3;, features a modification of the amino acid from R to C at position 270.
+The protein's natural variant, known as in WS1;, features a modification of the amino acid from R to C at position 271.
+The protein's natural variant, known as in WS1, features a modification of the amino acid from R to G at position 271.
+The protein's natural variant, known as in WS1; associated with K-273 in one family;, features a modification of the amino acid from R to H at position 271.
+The protein's natural variant, known as in WS1; associated with H-271 in one family; unknown pathological significance;, features a modification of the amino acid from R to K at position 273.
+The protein's natural variant, known as in WS1, features a modification of the amino acid from Q to H at position 391.
+The protein's natural variant, known as in BMFS3; loss of HSPA8-binding; no effect on PA2G4-, nor on ZNF622-binding;, features a modification of the amino acid from P to A at position 32.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from D to N at position 214.
+The protein's natural variant, known as in strain: SYNTEXCA755, features a modification of the amino acid from S to L at position 2.
+The protein's natural variant, known as in strain: SYNTEXCA755, features a modification of the amino acid from K to E at position 84.
+The protein's natural variant, known as in CAMRQ3; affects protein stability owing to accelerated proteasomal degradation;, features a modification of the amino acid from S to P at position 100.
+The natural variant of this protein is characterized by an amino acid alteration from Q to K at position 47.
+The natural variant of this protein is characterized by an amino acid alteration from P to A at position 52.
+The natural variant of this protein is characterized by an amino acid alteration from A to S at position 109.
+The protein's natural variant, known as in CAKUT2; results in decreased transcriptional repression through a dominant negative effect; does not affect nuclear localization; does not bind DNA; no effect on interaction with SIX1; no effect on interaction with TLE3;, features a modification of the amino acid from K to E at position 163.
+The protein's natural variant, known as in CAKUT2; results in decreased transcriptional repression through a dominant negative effect; does not affect nuclear localization; no effect on DNA binding; no effect on interaction with SIX1; no effect on interaction with TLE3;, features a modification of the amino acid from H to Y at position 524.
+The natural variant of this protein is characterized by an amino acid alteration from P to S at position 526.
+The protein's natural variant, known as in CHNG7; loss of thyrotropin-releasing hormone receptor activity; no effect on localization to plasma membrane, features a modification of the amino acid from P to R at position 81.
+The protein's natural variant, known as in CHNG7; loss of thyrotropin-releasing hormone receptor activity, features a modification of the amino acid from SITA to T at position 118.
+The protein's natural variant, known as in CHNG7; decreased affinity for TRH, features a modification of the amino acid from I to T at position 131.
+The protein's natural variant, known as in MRT43; reduced expression of the protein; alters the WASH complex;, features a modification of the amino acid from P to R at position 1019.
+The protein's natural variant, known as in strain: cv. Cvi-1; enhanced stability and better tolerance to photo-oxidative stress conditions; when associated with S-39, A-101 and K-164, features a modification of the amino acid from N to Y at position 23.
+The protein's natural variant, known as in strain: cv. Cvi-1; enhanced stability and better tolerance to photo-oxidative stress conditions; when associated with Y-23, A-101 and K-164, features a modification of the amino acid from N to S at position 39.
+The protein's natural variant, known as in strain: cv. Cvi-1; enhanced stability and better tolerance to photo-oxidative stress conditions; when associated with Y-23, S-39 and K-164, features a modification of the amino acid from T to A at position 101.
+The protein's natural variant, known as in strain: cv. Cvi-1; enhanced stability and better tolerance to photo-oxidative stress conditions; when associated with Y-23, S-39 and A-101, features a modification of the amino acid from N to K at position 164.
+The protein's natural variant, known as in VWM;, features a modification of the amino acid from L to Q at position 27.
+The protein's natural variant, known as in VWM, features a modification of the amino acid from G to E at position 47.
+The protein's natural variant, known as in VWM;, features a modification of the amino acid from A to V at position 87.
+The protein's natural variant, known as in VWM;, features a modification of the amino acid from R to Q at position 225.
+The protein's natural variant, known as in VWM;, features a modification of the amino acid from I to T at position 346.
+The protein's natural variant, known as in SCOTD;, features a modification of the amino acid from V to E at position 133.
+The protein's natural variant, known as in SCOTD; partial loss of activity;, features a modification of the amino acid from A to V at position 215.
+The protein's natural variant, known as in SCOTD;, features a modification of the amino acid from G to E at position 219.
+The protein's natural variant, known as in SCOTD;, features a modification of the amino acid from V to M at position 221.
+The protein's natural variant, known as in SCOTD; loss of activity;, features a modification of the amino acid from S to N at position 226.
+The protein's natural variant, known as in SCOTD; unknown pathological significance;, features a modification of the amino acid from V to F at position 245.
+The protein's natural variant, known as in SCOTD; unknown pathological significance;, features a modification of the amino acid from I to K at position 270.
+The protein's natural variant, known as in SCOTD; unknown pathological significance, features a modification of the amino acid from E to A at position 280.
+The protein's natural variant, known as in SCOTD;, features a modification of the amino acid from G to E at position 324.
+The protein's natural variant, known as in SCOTD; partial loss of activity, features a modification of the amino acid from L to P at position 327.
+The protein's natural variant, known as in SCOTD; loss of activity, features a modification of the amino acid from V to F at position 404.
+The protein's natural variant, known as in SCOTD; loss of activity, features a modification of the amino acid from S to P at position 405.
+The protein's natural variant, known as in SCOTD; unknown pathological significance, features a modification of the amino acid from V to M at position 437.
+The protein's natural variant, known as in SCOTD;, features a modification of the amino acid from C to F at position 456.
+The protein's natural variant, known as in SCOTD; partial loss of activity; the mutant retains half of the activity of the wild-type at 30 degrees;, features a modification of the amino acid from R to C at position 468.
+The protein's natural variant, known as in strain: DSM 149, features a modification of the amino acid from Y to F at position 38.
+The protein's natural variant, known as in strain: DSM 151, features a modification of the amino acid from L to M at position 41.
+The protein's natural variant, known as in strain: DSM 149, features a modification of the amino acid from A to V at position 49.
+The protein's natural variant, known as in strain: DSM 149, features a modification of the amino acid from T to S at position 51.
+The protein's natural variant, known as in strain: Isolate 1B and Isolate Timor sea, features a modification of the amino acid from T to S at position 60.
+The protein's natural variant, known as in strain: Isolate 1B and Isolate Timor sea, features a modification of the amino acid from M to I at position 98.
+The protein's natural variant, known as in strain: Isolate Timor sea, features a modification of the amino acid from S to N at position 263.
+The protein's natural variant, known as in strain: Isolate 1B and Isolate Timor sea, features a modification of the amino acid from P to A at position 266.
+The protein's natural variant, known as in strain: Isolate 1B and Isolate Timor sea, features a modification of the amino acid from I to V at position 300.
+The protein's natural variant, known as in strain: Isolate 1B and Isolate Timor sea, features a modification of the amino acid from V to T at position 327.
+The protein's natural variant, known as in strain: CC705 / UW505, features a modification of the amino acid from D to N at position 25.
+The protein's natural variant, known as in strain: CC705 / UW505, features a modification of the amino acid from G to E at position 27.
+The protein's natural variant, known as in strain: CC705 / UW505, features a modification of the amino acid from AV to TQ at position 49.
+The protein's natural variant, known as in strain: CC705 / UW505, features a modification of the amino acid from V to F at position 60.
+The protein's natural variant, known as in strain: CC705 / UW505, features a modification of the amino acid from S to P at position 68.
+The protein's natural variant, known as in strain: CC705 / UW505, features a modification of the amino acid from S to N at position 84.
+The protein's natural variant, known as in strain: CC705 / UW505, features a modification of the amino acid from G to A at position 100.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 80.
+The protein's natural variant, known as in HFE1; unknown pathological significance;, features a modification of the amino acid from R to S at position 6.
+The protein's natural variant, known as in HFE1; associated with D-63 in one patient, features a modification of the amino acid from G to D at position 43.
+The protein's natural variant, known as associated with hemochromatosis and variegate porphyria; increased frequency among patients with diabetic nephropathy;, features a modification of the amino acid from H to D at position 63.
+The protein's natural variant, known as in HFE1; mild form;, features a modification of the amino acid from S to C at position 65.
+The protein's natural variant, known as in HFE1;, features a modification of the amino acid from R to C at position 66.
+The protein's natural variant, known as in HFE1;, features a modification of the amino acid from G to R at position 93.
+The protein's natural variant, known as in HFE1;, features a modification of the amino acid from I to T at position 105.
+The protein's natural variant, known as in HFE1;, features a modification of the amino acid from Q to H at position 127.
+The protein's natural variant, known as in HFE1; uncertain pathological significance, features a modification of the amino acid from A to V at position 176.
+The protein's natural variant, known as in HFE1, features a modification of the amino acid from R to G at position 224.
+The protein's natural variant, known as in HFE1; associated with susceptibility to porphyria cutanea tarda; associated with increased serum transferrin levels; higher frequency in patients with type 2 diabetes than in controls;, features a modification of the amino acid from C to Y at position 282.
+The protein's natural variant, known as in HFE1; destabilizing effect on the tertiary structure of the protein; prevents the normal interaction between HFE and B2M and between HFE and TFRC; decreases the capacity of HFE to reduce transferrin-mediated iron uptake;, features a modification of the amino acid from Q to P at position 283.
+The protein's natural variant, known as in HFE1;, features a modification of the amino acid from V to A at position 295.
+The protein's natural variant, known as in HFE1;, features a modification of the amino acid from R to M at position 330.
+The protein's natural variant, known as in DKCB5; severe form consistent with Hoyeraal-Hreidarsson syndrome;, features a modification of the amino acid from E to K at position 251.
+The protein's natural variant, known as in PFBMFT3;, features a modification of the amino acid from P to L at position 484.
+The protein's natural variant, known as in DKCB5; severe form consistent with Hoyeraal-Hreidarsson syndrome;, features a modification of the amino acid from M to I at position 492.
+The protein's natural variant, known as in DKCB5; severe form consistent with Hoyeraal-Hreidarsson syndrome;, features a modification of the amino acid from E to D at position 591.
+The protein's natural variant, known as in DKCA4;, features a modification of the amino acid from A to T at position 621.
+The protein's natural variant, known as in PFBMFT3;, features a modification of the amino acid from P to L at position 647.
+The protein's natural variant, known as in DKCB5; severe form consistent with Hoyeraal-Hreidarsson syndrome;, features a modification of the amino acid from I to M at position 699.
+The protein's natural variant, known as in DKCB5; severe form consistent with Hoyeraal-Hreidarsson syndrome, features a modification of the amino acid from L to R at position 710.
+The protein's natural variant, known as in DKCB5; severe form consistent with Hoyeraal-Hreidarsson syndrome;, features a modification of the amino acid from G to V at position 739.
+The protein's natural variant, known as in DKCB5; severe form consistent with Hoyeraal-Hreidarsson syndrome;, features a modification of the amino acid from V to M at position 745.
+The natural variant of this protein is characterized by an amino acid alteration from Q to P at position 829.
+The protein's natural variant, known as in DKCB5; severe form consistent with Hoyeraal-Hreidarsson syndrome, features a modification of the amino acid from K to E at position 897.
+The protein's natural variant, known as in DKCB5; severe form consistent with Hoyeraal-Hreidarsson syndrome;, features a modification of the amino acid from R to W at position 957.
+The protein's natural variant, known as in DKCB5; severe form consistent with Hoyeraal-Hreidarsson syndrome;, features a modification of the amino acid from F to L at position 964.
+The protein's natural variant, known as in PFBMFT3;, features a modification of the amino acid from H to P at position 1124.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from G to E at position 221.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from S to L at position 393.
+The protein's natural variant, known as in MC1DN5; loss of catalytic activity, features a modification of the amino acid from V to A at position 228.
+The protein's natural variant, known as in MC1DN5; unknown pathological significance;, features a modification of the amino acid from R to W at position 241.
+The protein's natural variant, known as in MC1DN5; also found in a patient with muscular hypotonia; loss of catalytic activity;, features a modification of the amino acid from D to G at position 252.
+The protein's natural variant, known as in plasmid pWR100, plasmid pWR501 and plasmid pSF5, features a modification of the amino acid from R to K at position 19.
+The protein's natural variant, known as in plasmid pWR100, plasmid pWR501, plasmid pSF5, plasmid pINV_F6_M1382, plasmid pSf6_579, plasmid pSf3_575, plasmid pSf4a_576, plasmid pSf4b_577 and plasmid pSf5_246, features a modification of the amino acid from S to F at position 66.
+The natural variant of this protein is characterized by an amino acid alteration from P to A at position 514.
+The natural variant of this protein is characterized by an amino acid alteration from L to P at position 639.
+The natural variant of this protein is characterized by an amino acid alteration from H to P at position 711.
+The protein's natural variant, known as in RP9;, features a modification of the amino acid from H to L at position 137.
+The protein's natural variant, known as in RP9;, features a modification of the amino acid from D to G at position 170.
+The protein's natural variant, known as in DEE83; the nucleotide substitution also alters the translation of other alternatively spliced products of the gene globally reducing functional enzyme levels and causing reduced synthesis of UDP-glucose and decreased glycogen biosynthetic process; no effect on protein localization; no effect on UTP:glucose-1-phosphate uridylyltransferase activity;, features a modification of the amino acid from M to V at position 12.
+The protein's natural variant, known as in NEDCASB; unknown pathological significance;, features a modification of the amino acid from P to S at position 157.
+The protein's natural variant, known as in NEDCASB; unknown pathological significance, features a modification of the amino acid from T to R at position 186.
+The protein's natural variant, known as in NEDCASB; unknown pathological significance;, features a modification of the amino acid from N to D at position 379.
+The protein's natural variant, known as in NEDCASB; unknown pathological significance;, features a modification of the amino acid from G to S at position 423.
+The protein's natural variant, known as in NEDCASB; unknown pathological significance;, features a modification of the amino acid from Q to P at position 435.
+The protein's natural variant, known as in NEDCASB; no effect on protein abundance; decreased glycine hydroxymethyltransferase activity; associated with altered mitochondrial redox metabolism, features a modification of the amino acid from P to A at position 499.
+The protein's natural variant, known as in PSORS14; expression of the protein is severely impaired compared to wild-type; the mutant protein is substantially less able to inhibit IL1RL2 signaling than wild-type;, features a modification of the amino acid from L to P at position 27.
+The protein's natural variant, known as in PSORS14;, features a modification of the amino acid from R to W at position 48.
+The protein's natural variant, known as in PSORS14;, features a modification of the amino acid from S to L at position 113.
+The protein's natural variant, known as in PSORS14; shows impaired expression of the mutant protein which fails to antagonize the IL-36 signaling pathway;, features a modification of the amino acid from T to R at position 123.
+The protein's natural variant, known as rare variant; may act as a phenotype modifier in EIEE13 patients carrying SCN8A mutations;, features a modification of the amino acid from D to E at position 304.
+The protein's natural variant, known as rare variant; may act as a phenotype modifier in EIEE13 patients carrying SCN8A mutations;, features a modification of the amino acid from V to A at position 2196.
+The protein's natural variant, known as in CASP8D;, features a modification of the amino acid from R to W at position 248.
+The protein's natural variant, known as associated with protection against breast cancer; also associated with a lower risk of cutaneous melanoma;, features a modification of the amino acid from D to H at position 285.
+The natural variant of this protein is characterized by an amino acid alteration from V to A at position 302.
+The natural variant of this protein is characterized by an amino acid alteration from Y to H at position 85.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from P to L at position 169.
+The natural variant of this protein is characterized by an amino acid alteration from D to E at position 440.
+The protein's natural variant, known as in GCPS, features a modification of the amino acid from C to G at position 515.
+The protein's natural variant, known as in GCPS, features a modification of the amino acid from C to Y at position 520.
+The protein's natural variant, known as in GCPS;, features a modification of the amino acid from R to W at position 625.
+The protein's natural variant, known as in GCPS;, features a modification of the amino acid from P to S at position 707.
+The protein's natural variant, known as in PAPA1 and PAPB;, features a modification of the amino acid from G to R at position 727.
+The protein's natural variant, known as in GCPS; the patient was originally classifed as being affected by acrocallosal syndrome due to the absence of corpus callosum;, features a modification of the amino acid from A to P at position 934.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from S to P at position 1304.
+The protein's natural variant, known as in HLD24; results in altered lipid distribution at the cell membrane characterized by decreased phosphatidylcholine and increased sphingomyelin concentrations in the outer leaflet; affects substrate specificity resulting in novel flippase activity toward phosphatidylcholine; does not affect flippase activity toward phosphatidylserine and phosphatidylethanolamine; does not affect location to the cell membrane, features a modification of the amino acid from Q to E at position 84.
+The protein's natural variant, known as in strain: EFB1, features a modification of the amino acid from I to M at position 9.
+The protein's natural variant, known as in strain: EFB1, features a modification of the amino acid from AI to SV at position 22.
+The protein's natural variant, known as in strain: EFB1, features a modification of the amino acid from Q to M at position 29.
+The protein's natural variant, known as in strain: EFB1, features a modification of the amino acid from DTPVDDR to ETLAADQ at position 40.
+The protein's natural variant, known as in strain: EFB1, features a modification of the amino acid from D to N at position 44.
+The protein's natural variant, known as in strain: EFB1, features a modification of the amino acid from L to Q at position 52.
+The protein's natural variant, known as in strain: EFB1, features a modification of the amino acid from E to D at position 77.
+The protein's natural variant, known as in strain: EFB1, features a modification of the amino acid from E to D at position 92.
+The protein's natural variant, known as in strain: EFB1, features a modification of the amino acid from E to V at position 142.
+The protein's natural variant, known as in strain: EFB1, features a modification of the amino acid from L to V at position 147.
+The protein's natural variant, known as in strain: EFB1, features a modification of the amino acid from Q to E at position 153.
+The protein's natural variant, known as in strain: EFB1, features a modification of the amino acid from D to E at position 166.
+The protein's natural variant, known as in minor component, features a modification of the amino acid from G to FKG at position 2.
+The protein's natural variant, known as in AGM6;, features a modification of the amino acid from G to S at position 137.
+The natural variant of this protein is characterized by an amino acid alteration from D to E at position 8.
+The protein's natural variant, known as in FRUCT; loss of ketohexokinase function; insoluble;, features a modification of the amino acid from G to R at position 40.
+The protein's natural variant, known as in FRUCT; no effect on ketohexokinase function; decreases enzyme activity but no effect in substrate affinity; decreases thermal stability;, features a modification of the amino acid from A to T at position 43.
+The protein's natural variant, known as in strain: DS400/A3 and KL14-4A, features a modification of the amino acid from T to L at position 46.
+The protein's natural variant, known as in strain: DS400/A3, DS401 and oligomycin-resistant mutant, features a modification of the amino acid from L to F at position 53.
+The protein's natural variant, known as in oligomycin-resistant mutant and cross-resistance to venturicidin, features a modification of the amino acid from L to V at position 57.
+The protein's natural variant, known as in oligomycin-resistant mutant, features a modification of the amino acid from C to S at position 65.
+The natural variant of this protein is characterized by an amino acid alteration from V to L at position 23.
+The natural variant of this protein is characterized by an amino acid alteration from D to N at position 58.
+The protein's natural variant, known as in CMS8; results in decreased AChR clustering, features a modification of the amino acid from G to S at position 76.
+The protein's natural variant, known as in CMS8; results in decreased AChR clustering, features a modification of the amino acid from N to I at position 105.
+The natural variant of this protein is characterized by an amino acid alteration from T to M at position 267.
+The natural variant of this protein is characterized by an amino acid alteration from A to V at position 745.
+The natural variant of this protein is characterized by an amino acid alteration from V to M at position 984.
+The natural variant of this protein is characterized by an amino acid alteration from G to R at position 1341.
+The natural variant of this protein is characterized by an amino acid alteration from P to L at position 1451.
+The natural variant of this protein is characterized by an amino acid alteration from R to Q at position 1671.
+The natural variant of this protein is characterized by an amino acid alteration from R to P at position 1698.
+The protein's natural variant, known as in CMS8; results in disruption of the neuromuscular junction architecture; does not affect phosphorylation of MUSK; does not affect AChR clustering, features a modification of the amino acid from G to R at position 1709.
+The protein's natural variant, known as in CMS8; decreased AGRN-induced clustering of AChR by >100-fold and decreased phosphorylation of the MUSK receptor and AChR beta subunit by about 10-fold. Increased binding to alpha-dystroglycan, features a modification of the amino acid from V to F at position 1727.
+The natural variant of this protein is characterized by an amino acid alteration from D to N at position 1789.
+The protein's natural variant, known as in CMS8, features a modification of the amino acid from G to R at position 1875.
+The natural variant of this protein is characterized by an amino acid alteration from G to V at position 2046.
+The protein's natural variant, known as in DEE31;, features a modification of the amino acid from A to P at position 177.
+The protein's natural variant, known as in DEE31;, features a modification of the amino acid from K to N at position 206.
+The protein's natural variant, known as in DEE31;, features a modification of the amino acid from R to W at position 237.
+The protein's natural variant, known as in DEE31;, features a modification of the amino acid from G to A at position 359.
+The protein's natural variant, known as in strain: IFM 45815, IFM 45816, IFM 46868, IFM 50992, IFM 50995 and RMSCC 2267 / CA1, features a modification of the amino acid from A to G at position 196.
+The protein's natural variant, known as in NEDITPO; unknown pathological significance, features a modification of the amino acid from V to A at position 184.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from D to V at position 242.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from R to G at position 795.
+The protein's natural variant, known as in HOS;, features a modification of the amino acid from Q to K at position 49.
+The protein's natural variant, known as in HOS;, features a modification of the amino acid from I to T at position 54.
+The protein's natural variant, known as in HOS; significant cardiac malformations but only minor skeletal abnormalities; reduced protein stability and strongly reduced affinity for DNA;, features a modification of the amino acid from G to R at position 80.
+The protein's natural variant, known as probable disease-associated variant found in a patient with atrial fibrillation; reduces transcriptional activity; affects transcriptional regulation of NKX2-5, features a modification of the amino acid from P to S at position 132.
+The protein's natural variant, known as probable disease-associated variant found in a patient with sporadic dilated cardiomyopathy; associated with disease susceptibility; associated with significantly decreased transcriptional activity;, features a modification of the amino acid from A to T at position 143.
+The protein's natural variant, known as probable disease-associated variant found in patients with familial dilated cardiomyopathy; associated with disease susceptibility; associated with significantly decreased transcriptional activity, features a modification of the amino acid from S to A at position 154.
+The protein's natural variant, known as probable disease-associated variant found in a patient with atrial fibrillation; reduces transcriptional activity; affects transcriptional regulation of NKX2-5 or GATA4, features a modification of the amino acid from H to D at position 170.
+The protein's natural variant, known as in HOS; extensive upper limb malformations; affects transcriptional regulation of MYH6;, features a modification of the amino acid from R to Q at position 237.
+The protein's natural variant, known as in HOS; extensive upper limb malformations; strongly reduced affinity for DNA;, features a modification of the amino acid from R to W at position 237.
+The protein's natural variant, known as in LBSL;, features a modification of the amino acid from S to G at position 45.
+The protein's natural variant, known as in LBSL;, features a modification of the amino acid from C to F at position 152.
+The protein's natural variant, known as in LBSL;, features a modification of the amino acid from R to H at position 179.
+The protein's natural variant, known as in LBSL;, features a modification of the amino acid from Q to K at position 184.
+The protein's natural variant, known as in LBSL;, features a modification of the amino acid from Q to K at position 248.
+The protein's natural variant, known as in LBSL;, features a modification of the amino acid from R to Q at position 263.
+The protein's natural variant, known as in LBSL;, features a modification of the amino acid from D to V at position 560.
+The protein's natural variant, known as in LBSL;, features a modification of the amino acid from L to F at position 613.
+The protein's natural variant, known as in LBSL;, features a modification of the amino acid from L to Q at position 626.
+The protein's natural variant, known as in LBSL;, features a modification of the amino acid from L to V at position 626.
+The protein's natural variant, known as in LBSL;, features a modification of the amino acid from Y to C at position 629.
+The protein's natural variant, known as in MGORS4;, features a modification of the amino acid from A to T at position 66.
+The protein's natural variant, known as in MGORS4;, features a modification of the amino acid from Q to H at position 117.
+The protein's natural variant, known as in MGORS4;, features a modification of the amino acid from R to W at position 453.
+The protein's natural variant, known as in MGORS4;, features a modification of the amino acid from R to Q at position 462.
+The protein's natural variant, known as in MGORS4;, features a modification of the amino acid from E to K at position 468.
+The protein's natural variant, known as in PCH9;, features a modification of the amino acid from R to H at position 674.
+The protein's natural variant, known as in PCH9;, features a modification of the amino acid from E to D at position 778.
+The protein's natural variant, known as in PCH9;, features a modification of the amino acid from D to Y at position 793.
+The protein's natural variant, known as in MYPOP;, features a modification of the amino acid from E to K at position 706.
+The protein's natural variant, known as in one patient with familial myopathy; unknown pathological significance;, features a modification of the amino acid from V to I at position 970.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from K to R at position 129.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from K to E at position 137.
+The protein's natural variant, known as in strain: MmRL 1635, features a modification of the amino acid from D to A at position 401.
+The protein's natural variant, known as in strain: MmRL 1759, features a modification of the amino acid from A to V at position 519.
+The protein's natural variant, known as in strain: MmRL 1635 and MmRL 1759, features a modification of the amino acid from S to T at position 722.
+The protein's natural variant, known as in strain: MmRL 1636, features a modification of the amino acid from E to K at position 727.
+The natural variant of this protein is characterized by an amino acid alteration from T to A at position 208.
+The natural variant of this protein is characterized by an amino acid alteration from E to D at position 557.
+The natural variant of this protein is characterized by an amino acid alteration from P to L at position 573.
+The natural variant of this protein is characterized by an amino acid alteration from N to T at position 597.
+The protein's natural variant, known as in pcy, features a modification of the amino acid from I to S at position 614.
+The protein's natural variant, known as in MRXS99F, features a modification of the amino acid from L to W at position 1693.
+The protein's natural variant, known as in XLID99; unknown pathological significance; does not affect interaction with DCX; reduced subcellular localization in the axonal growth cones;, features a modification of the amino acid from L to H at position 2093.
+The protein's natural variant, known as in XLID99; unknown pathological significance; does not affect interaction with DCX; reduced subcellular localization in the axonal growth cones;, features a modification of the amino acid from L to I at position 2157.
+The natural variant of this protein is characterized by an amino acid alteration from A to E at position 239.
+The natural variant of this protein is characterized by an amino acid alteration from H to Y at position 258.
+The natural variant of this protein is characterized by an amino acid alteration from T to I at position 259.
+The natural variant of this protein is characterized by an amino acid alteration from S to R at position 284.
+The protein's natural variant, known as impaired ability to inhibit SCNN;, features a modification of the amino acid from P to L at position 355.
+The natural variant of this protein is characterized by an amino acid alteration from S to R at position 497.
+The protein's natural variant, known as in PVNH7;, features a modification of the amino acid from Y to C at position 679.
+The protein's natural variant, known as in PVNH7; increased degradation; changed function in regulation of TOR signaling;, features a modification of the amino acid from Q to H at position 694.
+The protein's natural variant, known as in PVNH7; increased degradation; changed function in regulation of TOR signaling;, features a modification of the amino acid from E to K at position 893.
+The protein's natural variant, known as in PVNH7; increased degradation; changed function in regulation of TOR signaling;, features a modification of the amino acid from R to Q at position 897.
+The protein's natural variant, known as in M(v) antigen;, features a modification of the amino acid from T to S at position 22.
+The protein's natural variant, known as in S antigen and Mit antigen;, features a modification of the amino acid from T to M at position 48.
+The protein's natural variant, known as in Mit antigen;, features a modification of the amino acid from R to H at position 54.
+The protein's natural variant, known as in s(D) antigen;, features a modification of the amino acid from P to R at position 58.
+The natural variant of this protein is characterized by an amino acid alteration from K to R at position 48.
+The natural variant of this protein is characterized by an amino acid alteration from M to V at position 404.
+The natural variant of this protein is characterized by an amino acid alteration from R to G at position 447.
+The natural variant of this protein is characterized by an amino acid alteration from L to P at position 708.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from M to V at position 165.
+The protein's natural variant, known as in SPGF32; unknown pathological significance; does not have any significant effect on its transactivation;, features a modification of the amino acid from C to R at position 31.
+The protein's natural variant, known as in SPGF32; unknown pathological significance; does not have any significant effect on its transactivation;, features a modification of the amino acid from P to T at position 177.
+The protein's natural variant, known as in strain: 2CPA1, 2CPA12, 2CPA51, 2CPA105, 2CPA118, 2CPA122, 8B, 8D, 8E, 8F, 8G, 9A, 9B, 9C, 9D, 9E, 9F, 9G, 9H, 10B, 10F, 10G, 10H and Oregon-R, features a modification of the amino acid from T to A at position 52.
+The protein's natural variant, known as in strain: 2CPA51, features a modification of the amino acid from A to V at position 64.
+The protein's natural variant, known as in STHAG8; reduced activation of Wnt signaling; reduced endothelial differentiation;, features a modification of the amino acid from R to Q at position 211.
+The protein's natural variant, known as associated with obesity; abrogates the ability of WNT10B to activate canonical Wnt signaling and blocks adipogenesis, features a modification of the amino acid from C to Y at position 256.
+The protein's natural variant, known as in SHFM6;, features a modification of the amino acid from R to W at position 332.
+The protein's natural variant, known as in strain: Milan hypertensive, features a modification of the amino acid from R to Q at position 529.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from H to Q at position 264.
+The protein's natural variant, known as in LCCS1; allele Fin(Major); does not affect subcellular localization, features a modification of the amino acid from T to TPFQ at position 144.
+The protein's natural variant, known as in LCCS1;, features a modification of the amino acid from R to H at position 569.
+The protein's natural variant, known as in CAAHD;, features a modification of the amino acid from V to M at position 617.
+The protein's natural variant, known as in CAAHD;, features a modification of the amino acid from I to T at position 684.
+The protein's natural variant, known as in OLE-1; enhanced accumulation of oleic acid but low ricinoleic acid levels in seeds, high-oleic castor mutant 1; when associated with A-242 and Q-319, features a modification of the amino acid from F to S at position 49.
+The protein's natural variant, known as in OLE-1; enhanced accumulation of oleic acid but low ricinoleic acid levels in seeds, high-oleic castor mutant 1; when associated with S-49 and Q-319, features a modification of the amino acid from V to A at position 242.
+The protein's natural variant, known as in OLE-1; enhanced accumulation of oleic acid but low ricinoleic acid levels in seeds, high-oleic castor mutant 1; when associated with S-49 and A-242, features a modification of the amino acid from H to Q at position 319.
+The protein's natural variant, known as in a melanoma sample; somatic mutation, features a modification of the amino acid from P to S at position 115.
+The protein's natural variant, known as in FOP; variant phenotype, features a modification of the amino acid from PF to L at position 198.
+The protein's natural variant, known as in FOP; with some atypical features;, features a modification of the amino acid from R to I at position 202.
+The protein's natural variant, known as in FOP;, features a modification of the amino acid from R to H at position 206.
+The protein's natural variant, known as in FOP; with some atypical features, features a modification of the amino acid from Q to E at position 207.
+The protein's natural variant, known as in FOP; variant phenotype;, features a modification of the amino acid from G to E at position 328.
+The protein's natural variant, known as in FOP; variant phenotype;, features a modification of the amino acid from G to R at position 328.
+The protein's natural variant, known as in FOP; variant phenotype;, features a modification of the amino acid from G to W at position 328.
+The protein's natural variant, known as in FOP; variant phenotype;, features a modification of the amino acid from G to D at position 356.
+The protein's natural variant, known as in FOP; variant phenotype;, features a modification of the amino acid from R to P at position 375.
+The protein's natural variant, known as in strain: B10.S/J and SJL/J, features a modification of the amino acid from M to T at position 169.
+The protein's natural variant, known as in strain: B10.S/J and SJL/J, features a modification of the amino acid from F to L at position 294.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from Y to CD at position 34.
+The natural variant of this protein is characterized by an amino acid alteration from G to S at position 56.
+The natural variant of this protein is characterized by an amino acid alteration from G to E at position 94.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from L to V at position 30.
+The protein's natural variant, known as in PKD5;, features a modification of the amino acid from A to V at position 90.
+The protein's natural variant, known as in PKD5;, features a modification of the amino acid from Q to H at position 91.
+The protein's natural variant, known as associated with SHEP4; greatly reduced exchange activity;, features a modification of the amino acid from T to A at position 111.
+The protein's natural variant, known as found in patients with North American Indian childhood cirrhosis; unknown pathological significance; does not affect nucleolar protein location; decreased interaction with HIVEP1 measured in yeast two-hybrid screening;, features a modification of the amino acid from R to W at position 565.
+The protein's natural variant, known as in SCA47; results in reduced PUM1 protein levels and decreased post-transcriptional repression of E2F3 and ATXN1;, features a modification of the amino acid from T to S at position 1033.
+The protein's natural variant, known as in SCA47; decreased post-transcriptional repression of E2F3 and ATXN1;, features a modification of the amino acid from R to W at position 1137.
+The protein's natural variant, known as in SCA47; results in reduced PUM1 protein levels and decreased post-transcriptional repression of E2F3 and ATXN1;, features a modification of the amino acid from R to W at position 1145.
+The protein's natural variant, known as in susceptible haplotype, features a modification of the amino acid from V to A at position 22.
+The protein's natural variant, known as in strain: NCTC 8468, features a modification of the amino acid from A to T at position 13.
+The protein's natural variant, known as in strain: NCTC 8468, features a modification of the amino acid from L to V at position 16.
+The protein's natural variant, known as in strain: NCTC 8468, features a modification of the amino acid from N to S at position 25.
+The protein's natural variant, known as in strain: 6-7626, features a modification of the amino acid from N to K at position 28.
+The protein's natural variant, known as in strain: NCTC 8468, features a modification of the amino acid from D to H at position 34.
+The protein's natural variant, known as in strain: Eagan, 3639, 3640, 6-7626, HK695 and Minna, features a modification of the amino acid from H to Q at position 62.
+The protein's natural variant, known as in strain: Eagan, 3639, 3640, NCTC 8468, 6-7626, HK695 and Minna, features a modification of the amino acid from S to A at position 63.
+The protein's natural variant, known as in strain: Eagan, 3639, 3640, NCTC 8468, 6-7626, HK695 and Minna, features a modification of the amino acid from Y to H at position 98.
+The protein's natural variant, known as in strain: NCTC 8468, features a modification of the amino acid from R to H at position 99.
+The protein's natural variant, known as in strain: 6-7626, features a modification of the amino acid from K to Q at position 144.
+The protein's natural variant, known as in strain: 6-7626, features a modification of the amino acid from K to R at position 168.
+The protein's natural variant, known as in strain: Eagan, 3639, 3640, NCTC 8468, 6-7626, HK695 and Minna, features a modification of the amino acid from T to A at position 191.
+The protein's natural variant, known as in strain: 6-7626, features a modification of the amino acid from P to S at position 253.
+The protein's natural variant, known as in strain: 6-7626, features a modification of the amino acid from Q to K at position 310.
+The protein's natural variant, known as in strain: Eagan, 3639, NCTC 8468, 6-7626, HK695 and Minna, features a modification of the amino acid from E to A at position 327.
+The protein's natural variant, known as in strain: Eagan, 3640, HK695 and Minna, features a modification of the amino acid from A to V at position 338.
+The protein's natural variant, known as in strain: 6-7626, features a modification of the amino acid from K to E at position 364.
+The protein's natural variant, known as in CLN4A;, features a modification of the amino acid from R to T at position 6.
+The protein's natural variant, known as in CLN6; unknown pathological significance;, features a modification of the amino acid from G to S at position 17.
+The protein's natural variant, known as in CLN4A;, features a modification of the amino acid from L to F at position 47.
+The protein's natural variant, known as in CLN6;, features a modification of the amino acid from R to H at position 62.
+The protein's natural variant, known as in CLN4A;, features a modification of the amino acid from L to P at position 67.
+The protein's natural variant, known as in CLN4A;, features a modification of the amino acid from N to K at position 77.
+The protein's natural variant, known as in CLN6, features a modification of the amino acid from N to K at position 90.
+The protein's natural variant, known as in CLN4A;, features a modification of the amino acid from R to Q at position 103.
+The protein's natural variant, known as in CLN6, features a modification of the amino acid from S to F at position 104.
+The protein's natural variant, known as in CLN6;, features a modification of the amino acid from G to D at position 123.
+The protein's natural variant, known as in CLN6;, features a modification of the amino acid from R to C at position 149.
+The protein's natural variant, known as in CLN4A;, features a modification of the amino acid from R to H at position 149.
+The protein's natural variant, known as in CLN6;, features a modification of the amino acid from P to L at position 159.
+The protein's natural variant, known as in CLN6;, features a modification of the amino acid from L to P at position 169.
+The protein's natural variant, known as in CLN6, features a modification of the amino acid from F to S at position 186.
+The protein's natural variant, known as in CLN6;, features a modification of the amino acid from Y to C at position 221.
+The protein's natural variant, known as in CLN6;, features a modification of the amino acid from Y to S at position 221.
+The protein's natural variant, known as in CLN6;, features a modification of the amino acid from F to L at position 234.
+The protein's natural variant, known as in CLN4A; requires 2 nucleotide substitutions, features a modification of the amino acid from F to T at position 238.
+The protein's natural variant, known as in CLN6; decreased protein level, resulting from ER membrane-to-cytosol dislocation of the protein followed by proteasome degradation.;, features a modification of the amino acid from M to T at position 241.
+The protein's natural variant, known as in CLN6;, features a modification of the amino acid from R to H at position 252.
+The protein's natural variant, known as in CLN6;, features a modification of the amino acid from G to S at position 259.
+The protein's natural variant, known as in CLN6;, features a modification of the amino acid from P to T at position 297.
+The protein's natural variant, known as in CLN6;, features a modification of the amino acid from P to L at position 299.
+The protein's natural variant, known as in CLN6;, features a modification of the amino acid from W to R at position 300.
+The protein's natural variant, known as associated with hypertension; significantly reduced arachidonic acid and lauric acid metabolizing activity;, features a modification of the amino acid from F to S at position 434.
+The protein's natural variant, known as in CYP4A11V, features a modification of the amino acid from NGIHLRLRRLPNPCEDKDQL to MESTCVSGGSLTLVKTRTSFEGLHLPSCLPDPRFCPLPVCPYPVFCLPTFPSSHLPAVPQSACPSLSHLSPGLPTCLSTCLLPTCISCWEKS at position 519.
+The protein's natural variant, known as in BAGOS, features a modification of the amino acid from M to K at position 303.
+The protein's natural variant, known as in BAGOS, features a modification of the amino acid from D to G at position 304.
+The protein's natural variant, known as in BAGOS, features a modification of the amino acid from D to E at position 366.
+The protein's natural variant, known as in BAGOS;, features a modification of the amino acid from I to T at position 368.
+The protein's natural variant, known as in BAGOS, features a modification of the amino acid from N to K at position 371.
+The protein's natural variant, known as found in a renal cell carcinoma sample; somatic mutation, features a modification of the amino acid from A to T at position 267.
+The protein's natural variant, known as in strain: F719, features a modification of the amino acid from Q to L at position 5.
+The protein's natural variant, known as in strain: F719, features a modification of the amino acid from L to I at position 46.
+The protein's natural variant, known as in strain: F719, features a modification of the amino acid from H to N at position 164.
+The protein's natural variant, known as in strain: F719, features a modification of the amino acid from TT to GE at position 193.
+The protein's natural variant, known as in strain: F719, features a modification of the amino acid from E to D at position 196.
+The protein's natural variant, known as in strain: F719, features a modification of the amino acid from RK to KN at position 200.
+The protein's natural variant, known as in strain: cv. Borszczagowski, features a modification of the amino acid from L to W at position 15.
+The protein's natural variant, known as in MT1353, features a modification of the amino acid from L to R at position 433.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from S to L at position 475.
+The natural variant of this protein is characterized by an amino acid alteration from H to R at position 45.
+The natural variant of this protein is characterized by an amino acid alteration from A to T at position 47.
+The protein's natural variant, known as in XLID1;, features a modification of the amino acid from R to C at position 359.
+The protein's natural variant, known as in XLID1;, features a modification of the amino acid from R to Q at position 758.
+The protein's natural variant, known as in XLID1; decreased guanine nucleotide exchange factor activity;, features a modification of the amino acid from A to V at position 789.
+The protein's natural variant, known as in XLID1;, features a modification of the amino acid from Q to P at position 801.
+The protein's natural variant, known as in XLID1;, features a modification of the amino acid from R to W at position 863.
+The protein's natural variant, known as in strain: Isolate TK 17633, features a modification of the amino acid from L to R at position 150.
+The protein's natural variant, known as in SLSN4;, features a modification of the amino acid from D to Y at position 3.
+The protein's natural variant, known as in SLSN4; also found in a patient with cardiac laterality defects; impairs localization to the ciliary transition zone;, features a modification of the amino acid from F to L at position 91.
+The protein's natural variant, known as in a patient with nephronophthisis with extra-renal features; the patient also carries W-735 in the same gene and L-209 in TTC21B, features a modification of the amino acid from R to L at position 160.
+The protein's natural variant, known as found in a patient with cardiac laterality defects; unknown pathological significance;, features a modification of the amino acid from H to Y at position 164.
+The protein's natural variant, known as in NPHP4;, features a modification of the amino acid from R to C at position 342.
+The protein's natural variant, known as in NPHP4;, features a modification of the amino acid from R to W at position 469.
+The protein's natural variant, known as found in a patient with cardiac laterality defects; unknown pathological significance;, features a modification of the amino acid from P to L at position 541.
+The protein's natural variant, known as in SLSN4;, features a modification of the amino acid from T to M at position 627.
+The protein's natural variant, known as in NPHP4, features a modification of the amino acid from A to G at position 654.
+The protein's natural variant, known as in NPHP4;, features a modification of the amino acid from R to W at position 735.
+The protein's natural variant, known as does not affect interaction with RPGRIP1L; does not affect interaction with RPGRIP1;, features a modification of the amino acid from R to H at position 740.
+The protein's natural variant, known as in NPHP4; affects interaction with RPGRIP1L; disrupts interaction with RPGRIP1;, features a modification of the amino acid from G to R at position 754.
+The protein's natural variant, known as in NPHP4; with color blindness, features a modification of the amino acid from Q to R at position 766.
+The protein's natural variant, known as in NPHP4;, features a modification of the amino acid from P to R at position 776.
+The protein's natural variant, known as in NPHP4;, features a modification of the amino acid from H to Q at position 782.
+The protein's natural variant, known as does not affect interaction with RPGRIP1L; does not affect interaction with RPGRIP1;, features a modification of the amino acid from R to W at position 848.
+The protein's natural variant, known as found in a patient with cardiac laterality defects; unknown pathological significance;, features a modification of the amino acid from V to M at position 883.
+The protein's natural variant, known as found in a patient with cardiac laterality defects; unknown pathological significance;, features a modification of the amino acid from R to C at position 906.
+The protein's natural variant, known as in SLSN4, features a modification of the amino acid from T to A at position 946.
+The protein's natural variant, known as in NPHP4; benign variant;, features a modification of the amino acid from R to H at position 961.
+The protein's natural variant, known as in NPHP4;, features a modification of the amino acid from F to S at position 991.
+The protein's natural variant, known as found in a patient with cardiac laterality defects; fails to rescue heart looping defects in zebrafish knockout;, features a modification of the amino acid from R to H at position 1044.
+The protein's natural variant, known as in NPHP4;, features a modification of the amino acid from A to T at position 1098.
+The protein's natural variant, known as found in a patient with cardiac laterality defects; unknown pathological significance;, features a modification of the amino acid from A to V at position 1110.
+The protein's natural variant, known as in NPHP4; also found in a patient with cardiac laterality defects;, features a modification of the amino acid from R to W at position 1192.
+The protein's natural variant, known as in SLSN4; benign variant;, features a modification of the amino acid from T to M at position 1225.
+The protein's natural variant, known as found in a patient with cardiac laterality defects; fails to rescue heart looping defects in zebrafish knockout;, features a modification of the amino acid from V to M at position 1236.
+The protein's natural variant, known as in NPHP4;, features a modification of the amino acid from R to C at position 1284.
+The protein's natural variant, known as in NPHP4; with hearing loss;, features a modification of the amino acid from Q to E at position 1287.
+The protein's natural variant, known as in LDHBD; slightly decreased activity;, features a modification of the amino acid from K to E at position 7.
+The protein's natural variant, known as in LDHBD, features a modification of the amino acid from A to E at position 35.
+The protein's natural variant, known as in LDHBD, features a modification of the amino acid from G to E at position 69.
+The protein's natural variant, known as in LDHBD; inactive;, features a modification of the amino acid from R to W at position 107.
+The protein's natural variant, known as in LDHBD;, features a modification of the amino acid from S to R at position 129.
+The protein's natural variant, known as in LDHBD, features a modification of the amino acid from F to V at position 171.
+The protein's natural variant, known as in LDHBD;, features a modification of the amino acid from R to H at position 172.
+The protein's natural variant, known as in LDHBD, features a modification of the amino acid from R to P at position 172.
+The protein's natural variant, known as in LDHBD, features a modification of the amino acid from M to L at position 175.
+The protein's natural variant, known as in LDHBD, features a modification of the amino acid from D to V at position 322.
+The protein's natural variant, known as in LDHBD;, features a modification of the amino acid from W to R at position 325.
+The protein's natural variant, known as in a clone, features a modification of the amino acid from H to Y at position 26.
+The protein's natural variant, known as in NEDFIH; unknown pathological significance, features a modification of the amino acid from L to F at position 49.
+The protein's natural variant, known as in NEDFIH; unknown pathological significance; decreased protein abundance in homozygous patient cells; patient cells show a decreased amount of neddylated proteins, features a modification of the amino acid from R to Q at position 85.
+The protein's natural variant, known as in NEDFIH; unknown pathological significance, features a modification of the amino acid from C to W at position 294.
+The protein's natural variant, known as in NEDFIH; unknown pathological significance, features a modification of the amino acid from R to Q at position 430.
+The protein's natural variant, known as no effect on IFNL1 induction, features a modification of the amino acid from S to P at position 134.
+The protein's natural variant, known as no effect on IFNL1 induction;, features a modification of the amino acid from R to G at position 251.
+The protein's natural variant, known as in IMD83; causes TLR3 deficiency and predisposition to herpes simplex encephalitis; inhibition of IFNL1 induction;, features a modification of the amino acid from P to S at position 554.
+The protein's natural variant, known as no effect on IFNL1 induction;, features a modification of the amino acid from F to L at position 732.
+The protein's natural variant, known as inhibition of IFNL1 induction;, features a modification of the amino acid from R to Q at position 867.
+The protein's natural variant, known as inhibition of IFNL1 induction, features a modification of the amino acid from M to V at position 870.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from P to L at position 82.
+The protein's natural variant, known as in RAFQS; results in about 1300-fold decrease in activity;, features a modification of the amino acid from R to C at position 334.
+The protein's natural variant, known as in RAFQS; disrupts stable protein expression;, features a modification of the amino acid from E to K at position 397.
+The protein's natural variant, known as in FHEIG; gain-of-function variant resulting in highly increased basal potassium currents; impaired sensitivity to arachidonic acid, features a modification of the amino acid from A to E at position 172.
+The protein's natural variant, known as in FHEIG; gain-of-function variant resulting in highly increased basal potassium currents; impaired sensitivity to arachidonic acid, features a modification of the amino acid from A to P at position 244.
+The protein's natural variant, known as in CRCS1; germline mutation; partial loss of activity;, features a modification of the amino acid from R to W at position 297.
+The protein's natural variant, known as in CRCS1; germline mutation; reduction of activity;, features a modification of the amino acid from D to N at position 303.
+The protein's natural variant, known as in CRCS1; somatic mutation; loss of activity, features a modification of the amino acid from E to D at position 341.
+The protein's natural variant, known as in CRCS1; germline mutation; partial loss of activity;, features a modification of the amino acid from R to H at position 373.
+The protein's natural variant, known as in CRCS1; germline mutation; loss of activity;, features a modification of the amino acid from R to H at position 382.
+The protein's natural variant, known as in CRCS1;, features a modification of the amino acid from Y to C at position 396.
+The protein's natural variant, known as in CRCS1; somatic mutation; loss of activity, features a modification of the amino acid from C to F at position 479.
+The protein's natural variant, known as in CRCS1; germline mutation; loss of activity;, features a modification of the amino acid from T to M at position 491.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from G to S at position 87.
+The protein's natural variant, known as in ECA5; the mutant protein is hyperglycosylated and has reduced mean current densities compared to wild-type;, features a modification of the amino acid from G to R at position 32.
+The protein's natural variant, known as in DEE43; no effect on localization to the plasma membrane; decreased GABA-gated chloride ion channel activity; decreased single channel open probability;, features a modification of the amino acid from D to N at position 120.
+The protein's natural variant, known as in DEE43;, features a modification of the amino acid from L to F at position 124.
+The protein's natural variant, known as in DEE43, features a modification of the amino acid from N to NH at position 138.
+The protein's natural variant, known as in DEE43; unknown pathological significance, features a modification of the amino acid from T to M at position 157.
+The protein's natural variant, known as in DEE43;, features a modification of the amino acid from Y to F at position 182.
+The protein's natural variant, known as found in a subject suffering from insomnia; functional analysis reveals a slower rate of the fast phase of desensitization compared with alpha1beta3gamma2SGABA(A) receptors; current deactivation is faster in the mutated receptors;, features a modification of the amino acid from R to H at position 217.
+The protein's natural variant, known as found in patients with Dravet syndrome; unknown pathological significance;, features a modification of the amino acid from R to Q at position 232.
+The protein's natural variant, known as in DEE43;, features a modification of the amino acid from Q to K at position 249.
+The protein's natural variant, known as in DEE43;, features a modification of the amino acid from S to F at position 254.
+The protein's natural variant, known as in DEE43, features a modification of the amino acid from L to Q at position 256.
+The protein's natural variant, known as in DEE43, features a modification of the amino acid from T to I at position 287.
+The protein's natural variant, known as in DEE43; unknown pathological significance, features a modification of the amino acid from L to H at position 293.
+The protein's natural variant, known as in DEE43;, features a modification of the amino acid from A to T at position 305.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from R to H at position 97.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from R to Q at position 399.
+The natural variant of this protein is characterized by an amino acid alteration from E to Q at position 204.
+The protein's natural variant, known as found in a consanguineous family with intellectual disability; unknown pathological significance;, features a modification of the amino acid from R to H at position 1183.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 2.
+The natural variant of this protein is characterized by an amino acid alteration from C to CPSCCA at position 81.
+The protein's natural variant, known as less common genetic variant;, features a modification of the amino acid from S to T at position 79.
+The protein's natural variant, known as no or minor deleterious effect observed;, features a modification of the amino acid from S to R at position 5.
+The protein's natural variant, known as in POF4, features a modification of the amino acid from R to Q at position 61.
+The protein's natural variant, known as in POF4;, features a modification of the amino acid from R to W at position 61.
+The protein's natural variant, known as in POF4; leads to marked reduction of mature protein production; does not generate a complete recovery of wild-type activity in granulosa cell line transfected with defective mutant and with equal amount of wild-type protein;, features a modification of the amino acid from R to W at position 68.
+The protein's natural variant, known as in POF4;, features a modification of the amino acid from R to C at position 76.
+The protein's natural variant, known as in POF4;, features a modification of the amino acid from R to H at position 76.
+The protein's natural variant, known as in POF4; leads to marked reduction of mature protein production; does not generate a complete recovery of wild-type activity in granulosa cell line transfected with defective mutant and with equal amount of wild-type protein;, features a modification of the amino acid from R to H at position 138.
+The protein's natural variant, known as in POF4; leads to marked reduction of mature protein production; does not generate a complete recovery of wild-type activity in granulosa cell line transfected with defective mutant and with equal amount of wild-type protein;, features a modification of the amino acid from L to P at position 148.
+The protein's natural variant, known as requires 2 nucleotide substitutions, features a modification of the amino acid from A to F at position 180.
+The protein's natural variant, known as in POF4; unknown pathological significance; no or minor deleterious effect detected;, features a modification of the amino acid from A to T at position 180.
+The protein's natural variant, known as in POF4, features a modification of the amino acid from N to K at position 196.
+The protein's natural variant, known as in POF4;, features a modification of the amino acid from R to H at position 206.
+The protein's natural variant, known as in POF4;, features a modification of the amino acid from W to R at position 221.
+The protein's natural variant, known as in ODG2; dominant-negative effect; may cause relevant modifications in the conformation of the precursor protein possibly leading to altered processing and impaired activation of latent forms or to abnormal dimerization;, features a modification of the amino acid from Y to C at position 235.
+The protein's natural variant, known as in POF4;, features a modification of the amino acid from I to V at position 243.
+The protein's natural variant, known as no or minor deleterious effect detected, features a modification of the amino acid from L to LL at position 263.
+The protein's natural variant, known as in POF4;, features a modification of the amino acid from R to C at position 329.
+The protein's natural variant, known as in strain: PSBZ, features a modification of the amino acid from Y to H at position 31.
+The protein's natural variant, known as in strain: Blue1, features a modification of the amino acid from ER to QH at position 71.
+The protein's natural variant, known as in strain: PSBZ, features a modification of the amino acid from FN to IP at position 106.
+The protein's natural variant, known as in strain: Blue1, features a modification of the amino acid from V to I at position 167.
+The protein's natural variant, known as in strain: Blue1, features a modification of the amino acid from D to E at position 253.
+The protein's natural variant, known as in strain: PSBZ and Blue1, features a modification of the amino acid from L to P at position 347.
+The protein's natural variant, known as in strain: Blue1, features a modification of the amino acid from I to L at position 349.
+The protein's natural variant, known as in SIDBA3; deficiency in Fe-S cluster synthesis; does not impair ISCU binding;, features a modification of the amino acid from K to Q at position 101.
+The protein's natural variant, known as in SIDBA3; deficiency in Fe-S cluster synthesis; does not impair ISCU binding;, features a modification of the amino acid from L to S at position 148.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from V to M at position 52.
+The protein's natural variant, known as in MYOSCO;, features a modification of the amino acid from R to C at position 56.
+The protein's natural variant, known as in IMD60; impairs protein stability; the mutant is unsoluble and forms multiple aggregates, features a modification of the amino acid from L to P at position 24.
+The protein's natural variant, known as in IMD60; unknown pathological significance; severely decreased localization in the nucleus; the mutant aggregates in the cytoplasm;, features a modification of the amino acid from E to K at position 788.
+The protein's natural variant, known as in CTRCT9; delays HSP70 expression increase in response to heat shock;, features a modification of the amino acid from R to C at position 12.
+The protein's natural variant, known as in CTRCT9; reduces protein solubility, features a modification of the amino acid from R to L at position 12.
+The protein's natural variant, known as in CTRCT9; associated with macular hypoplasia and a generally hypopigmented fundus, features a modification of the amino acid from R to L at position 21.
+The protein's natural variant, known as in CTRCT9; decreases oligomer formation;, features a modification of the amino acid from R to Q at position 21.
+The protein's natural variant, known as in CTRCT9;, features a modification of the amino acid from R to W at position 21.
+The protein's natural variant, known as in CTRCT9;, features a modification of the amino acid from R to C at position 49.
+The protein's natural variant, known as in CTRCT9; unknown pathological significance;, features a modification of the amino acid from R to C at position 54.
+The protein's natural variant, known as in CTRCT9; unknown pathological significance, features a modification of the amino acid from R to L at position 54.
+The protein's natural variant, known as in CTRCT9; unknown pathological significance, features a modification of the amino acid from R to P at position 54.
+The protein's natural variant, known as in CTRCT9; unknown pathological significance;, features a modification of the amino acid from R to Q at position 65.
+The protein's natural variant, known as in CTRCT9; unknown pathological significance; reduced chaperone-like activity in vitro, features a modification of the amino acid from F to L at position 71.
+The protein's natural variant, known as in CTRCT9; forms inclusion bodies, decreases chaperone activity, decreases protein stability at 45 degrees Celsius and increases protein aggregate formation in response to DTT in vitro;, features a modification of the amino acid from G to R at position 98.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from D to H at position 105.
+The protein's natural variant, known as in CTRCT9; zonular central nuclear cataract; reduced chaperone-like activity and increased membrane-binding capacity;, features a modification of the amino acid from R to C at position 116.
+The protein's natural variant, known as in CTRCT9; reverse phase-high-performance liquid chromatography suggests an increased hydrophobicity of the mutant protein; loss of chaperone activity of the mutant is seen in DL-dithiothreitol-induced insulin aggregation assay; fast protein liquid chromatography purification shows that the mutant protein has increased binding affinity to lysozyme;, features a modification of the amino acid from R to H at position 116.
+The protein's natural variant, known as in CTRCT9; unknown pathological significance;, features a modification of the amino acid from RY to H at position 118.
+The protein's natural variant, known as in CTRCT9; unknown pathological significance;, features a modification of the amino acid from R to H at position 119.
+The protein's natural variant, known as in CTRCT9; results in protein aggregation in the cytoplasm, features a modification of the amino acid from L to P at position 139.
+The protein's natural variant, known as in MRXSC; unknown pathological significance;, features a modification of the amino acid from T to I at position 213.
+The protein's natural variant, known as in MRXSC;, features a modification of the amino acid from R to C at position 572.
+The protein's natural variant, known as in MRXSC, features a modification of the amino acid from V to A at position 745.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from E to Q at position 160.
+The protein's natural variant, known as in allele B3;, features a modification of the amino acid from I to V at position 654.
+The protein's natural variant, known as in allele B2 and allele B3;, features a modification of the amino acid from I to V at position 655.
+The protein's natural variant, known as in VSCN2; almost complete loss of ERBB2 and ERBB3 phosphorylation in the presence or in the absence of NRG1 stimulation, suggesting alteration of downstream signaling; does not affect the subcellular localization at the cell membrane, features a modification of the amino acid from A to V at position 710.
+The protein's natural variant, known as in LNCR; somatic mutation; unknown pathological significance;, features a modification of the amino acid from L to P at position 755.
+The protein's natural variant, known as in LNCR; somatic mutation; unknown pathological significance, features a modification of the amino acid from M to MAYVM at position 774.
+The protein's natural variant, known as in GASC; somatic mutation; unknown pathological significance;, features a modification of the amino acid from G to S at position 776.
+The protein's natural variant, known as in LNCR; somatic mutation; unknown pathological significance, features a modification of the amino acid from S to SVGS at position 779.
+The protein's natural variant, known as in OC; somatic mutation; unknown pathological significance;, features a modification of the amino acid from N to S at position 857.
+The protein's natural variant, known as in GLM; somatic mutation; unknown pathological significance;, features a modification of the amino acid from E to K at position 914.
+The protein's natural variant, known as in strain: Isolate RMR 24, features a modification of the amino acid from T to A at position 2.
+The protein's natural variant, known as in strain: Isolate Jorg 37, features a modification of the amino acid from V to A at position 42.
+The protein's natural variant, known as in strain: Isolate Jorg 64, features a modification of the amino acid from I to V at position 78.
+The protein's natural variant, known as in strain: Isolate YLE357, features a modification of the amino acid from T to N at position 158.
+The protein's natural variant, known as in strain: Isolate Jorg 33, features a modification of the amino acid from F to Y at position 183.
+The protein's natural variant, known as in strain: Isolate RMR 24, features a modification of the amino acid from L to M at position 185.
+The protein's natural variant, known as in strain: Isolate YLE74, features a modification of the amino acid from P to T at position 186.
+The protein's natural variant, known as in strain: Isolate RMR 44, features a modification of the amino acid from V to I at position 195.
+The protein's natural variant, known as in strain: Isolate Jorg 64, features a modification of the amino acid from F to L at position 234.
+The protein's natural variant, known as in strain: Isolate Jorg 64, features a modification of the amino acid from G to D at position 251.
+The protein's natural variant, known as in strain: Isolate Jorg 37, features a modification of the amino acid from T to A at position 316.
+The protein's natural variant, known as in strain: Isolate 00-016A-8EBC and Isolate RMR 24, features a modification of the amino acid from M to I at position 324.
+The protein's natural variant, known as in strain: Isolate YLE199, features a modification of the amino acid from M to T at position 324.
+The protein's natural variant, known as in strain: Isolate 00-016A-8EBC, Isolate RMR 24 and Isolate YLE199, features a modification of the amino acid from H to Y at position 345.
+The natural variant of this protein is characterized by an amino acid alteration from A to V at position 34.
+The natural variant of this protein is characterized by an amino acid alteration from S to N at position 141.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from P to Q at position 146.
+The protein's natural variant, known as in CRC; somatic mutation;, features a modification of the amino acid from H to Y at position 23.
+The protein's natural variant, known as in PGL2; abolishes interaction with SDHA and flavination of SDHA;, features a modification of the amino acid from G to R at position 78.
+The protein's natural variant, known as confers glyphosate inhibition, features a modification of the amino acid from P to S at position 101.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from R to W at position 671.
+The protein's natural variant, known as no effect on the stabilization of microtubules;, features a modification of the amino acid from T to M at position 190.
+The protein's natural variant, known as in TBHS1; has an abnormal punctate expression pattern; has a drastically reduced ability to stabilize microtubules;, features a modification of the amino acid from T to P at position 397.
+The protein's natural variant, known as in OBLFC1; severely impairs the stabilization of microtubules;, features a modification of the amino acid from Q to P at position 415.
+The protein's natural variant, known as in TBHS1; unknown pathological significance, features a modification of the amino acid from E to D at position 420.
+The protein's natural variant, known as in TBHS1; has an abnormal punctate expression pattern; has a drastically reduced ability to stabilize microtubules;, features a modification of the amino acid from G to S at position 1083.
+The natural variant of this protein is characterized by an amino acid alteration from D to E at position 290.
+The natural variant of this protein is characterized by an amino acid alteration from R to K at position 783.
+The protein's natural variant, known as in PD, features a modification of the amino acid from R to G at position 82.
+The protein's natural variant, known as found in a large family with early-onset recessive retinal degeneration; abolishes autocleavage resulting in loss of enzymatic activity; increased protein aggregation; changes protein localization that becomes perinuclear, does not change ligand affinity for L-aspartic acid beta-hydroxamate, features a modification of the amino acid from G to R at position 178.
+The protein's natural variant, known as in dyl; negative regulation of lens epithelial cell proliferation; positive regulation of lens fiber cell differentiation; positive regulation of epithelial cell apoptotic process; loss of sequence-specific DNA binding, features a modification of the amino acid from F to L at position 93.
+The protein's natural variant, known as in dyl; negative regulation of lens epithelial cell proliferation; positive regulation of lens fiber cell differentiation; positive regulation of epithelial cell apoptotic process; loss of sequence-specific DNA binding, features a modification of the amino acid from F to S at position 98.
+The protein's natural variant, known as in FEPS2; increases the excitability of small DRG neurons;, features a modification of the amino acid from L to P at position 554.
+The protein's natural variant, known as found in a renal cell carcinoma sample; somatic mutation;, features a modification of the amino acid from R to W at position 916.
+The natural variant of this protein is characterized by an amino acid alteration from Q to L at position 940.
+The protein's natural variant, known as in FEPS2; increases the excitability of small DRG neurons;, features a modification of the amino acid from A to T at position 1304.
+The protein's natural variant, known as no gain in function in response to depolarization;, features a modification of the amino acid from C to Y at position 1523.
+The protein's natural variant, known as in strain: HFL97_3e2, features a modification of the amino acid from S to A at position 388.
+The protein's natural variant, known as in strain: HL-25, features a modification of the amino acid from A to S at position 24.
+The protein's natural variant, known as in strain: HL-25, features a modification of the amino acid from A to S at position 83.
+The protein's natural variant, known as in strain: C120, features a modification of the amino acid from P to L at position 204.
+The protein's natural variant, known as in a breast pleomorphic lobular carcinoma sample; somatic mutation, features a modification of the amino acid from E to K at position 703.
+The protein's natural variant, known as probable disease-associated variant found in a patient with opsoclonus-myoclonus ataxia-like syndrome;, features a modification of the amino acid from R to W at position 84.
+The protein's natural variant, known as in EPM3;, features a modification of the amino acid from R to W at position 94.
+The protein's natural variant, known as in EPM3;, features a modification of the amino acid from L to M at position 108.
+The protein's natural variant, known as in EPM3; uncertain pathological significance;, features a modification of the amino acid from D to Y at position 115.
+The protein's natural variant, known as in EPM3; results in markedly diminished localization at the cell membrane and appearance of prominent cytoplasmic aggregates;, features a modification of the amino acid from R to C at position 184.
+The protein's natural variant, known as in EPM3;, features a modification of the amino acid from N to I at position 273.
+The protein's natural variant, known as in SLSN9; results in altered folding of the N-terminus; does not affect interaction with IFT20; loss of interaction with MAP4, features a modification of the amino acid from I to S at position 17.
+The protein's natural variant, known as in SLSN9; results in altered folding of the N-terminus; does not affect interaction with IFT20; loss of interaction with MAP4;, features a modification of the amino acid from V to A at position 125.
+The protein's natural variant, known as in SLSN9; results in altered folding of the N-terminus; does not localize to the ciliary tip and transition zone; does not affect interaction with IFT20; loss of interaction with MAP4;, features a modification of the amino acid from V to M at position 125.
+The protein's natural variant, known as in SLSN9; does not localize to the ciliary tip;, features a modification of the amino acid from M to R at position 520.
+The protein's natural variant, known as in strain: STRA1; streptomycin resistant mutant which does not increase antibiotic production, features a modification of the amino acid from K to N at position 43.
+The protein's natural variant, known as in strain: KO-150 and KO-151; low level streptomycin resistant mutants which increase antibiotic production, features a modification of the amino acid from R to H at position 86.
+The protein's natural variant, known as streptomycin resistant mutant. Increases antibiotic production, features a modification of the amino acid from K to E at position 88.
+The natural variant of this protein is characterized by an amino acid alteration from Y to F at position 63.
+The protein's natural variant, known as in proline hyperproducing mutant; 700-X less sensitive to proline inhibition, features a modification of the amino acid from A to V at position 117.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from S to F at position 358.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 7.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 19.
+The natural variant of this protein is characterized by an amino acid alteration from A to V at position 82.
+The natural variant of this protein is characterized by an amino acid alteration from A to T at position 138.
+The protein's natural variant, known as confers relative resistance to infection by HIV-1; delay in disease progression in African Americans but not in Caucasians;, features a modification of the amino acid from V to I at position 64.
+The protein's natural variant, known as does not affect protein secretion;, features a modification of the amino acid from R to W at position 7.
+The protein's natural variant, known as in TTP;, features a modification of the amino acid from I to M at position 79.
+The protein's natural variant, known as in TTP; reduces protein secretion and proteolytic activity;, features a modification of the amino acid from V to M at position 88.
+The protein's natural variant, known as in TTP;, features a modification of the amino acid from H to D at position 96.
+The protein's natural variant, known as in TTP;, features a modification of the amino acid from R to C at position 102.
+The protein's natural variant, known as in TTP;, features a modification of the amino acid from S to F at position 119.
+The protein's natural variant, known as in TTP;, features a modification of the amino acid from I to T at position 178.
+The protein's natural variant, known as in TTP; low activity;, features a modification of the amino acid from R to W at position 193.
+The protein's natural variant, known as in TTP;, features a modification of the amino acid from T to I at position 196.
+The protein's natural variant, known as in TTP;, features a modification of the amino acid from S to P at position 203.
+The protein's natural variant, known as in TTP;, features a modification of the amino acid from L to Q at position 232.
+The protein's natural variant, known as in TTP;, features a modification of the amino acid from H to Q at position 234.
+The protein's natural variant, known as in TTP;, features a modification of the amino acid from D to H at position 235.
+The protein's natural variant, known as in TTP; mild effect on protein secretion; strong reduction of proteolytic activity;, features a modification of the amino acid from A to V at position 250.
+The protein's natural variant, known as in TTP;, features a modification of the amino acid from S to C at position 263.
+The protein's natural variant, known as in TTP; affects protein secretion;, features a modification of the amino acid from R to P at position 268.
+The protein's natural variant, known as in TTP;, features a modification of the amino acid from Y to C at position 304.
+The protein's natural variant, known as in TTP;, features a modification of the amino acid from C to Y at position 311.
+The protein's natural variant, known as in TTP;, features a modification of the amino acid from C to S at position 347.
+The protein's natural variant, known as in TTP;, features a modification of the amino acid from R to C at position 349.
+The protein's natural variant, known as in TTP;, features a modification of the amino acid from P to L at position 353.
+The protein's natural variant, known as in TTP;, features a modification of the amino acid from W to C at position 390.
+The protein's natural variant, known as in TTP;, features a modification of the amino acid from R to H at position 398.
+The protein's natural variant, known as does not affect protein secretion; normal proteolytic activity;, features a modification of the amino acid from Q to E at position 448.
+The protein's natural variant, known as in TTP;, features a modification of the amino acid from R to Q at position 507.
+The protein's natural variant, known as in TTP; impairs protein secretion;, features a modification of the amino acid from C to Y at position 508.
+The protein's natural variant, known as in TTP;, features a modification of the amino acid from G to D at position 525.
+The protein's natural variant, known as in TTP;, features a modification of the amino acid from R to G at position 528.
+The protein's natural variant, known as in TTP;, features a modification of the amino acid from A to V at position 596.
+The protein's natural variant, known as in TTP;, features a modification of the amino acid from A to P at position 606.
+The protein's natural variant, known as in TTP;, features a modification of the amino acid from Y to C at position 658.
+The protein's natural variant, known as in TTP;, features a modification of the amino acid from P to L at position 671.
+The protein's natural variant, known as in TTP; impairs protein secretion;, features a modification of the amino acid from I to F at position 673.
+The protein's natural variant, known as in TTP;, features a modification of the amino acid from R to C at position 692.
+The protein's natural variant, known as in TTP;, features a modification of the amino acid from C to R at position 758.
+The protein's natural variant, known as in TTP;, features a modification of the amino acid from C to S at position 908.
+The protein's natural variant, known as in TTP; impairs protein secretion;, features a modification of the amino acid from C to Y at position 908.
+The protein's natural variant, known as in TTP;, features a modification of the amino acid from C to G at position 951.
+The protein's natural variant, known as in TTP, features a modification of the amino acid from CAR to W at position 979.
+The protein's natural variant, known as in TTP;, features a modification of the amino acid from C to G at position 1024.
+The protein's natural variant, known as in TTP; affects protein secretion; the mutant protein has reduced protease activity;, features a modification of the amino acid from R to W at position 1060.
+The protein's natural variant, known as in a patient with thrombotic thrombocytopenic purpura;, features a modification of the amino acid from R to W at position 1095.
+The protein's natural variant, known as in TTP; impairs protein secretion; the mutant protein has reduced protease activity;, features a modification of the amino acid from R to C at position 1123.
+The protein's natural variant, known as in TTP;, features a modification of the amino acid from C to Y at position 1213.
+The protein's natural variant, known as in TTP; affects protein secretion; the mutant protein has reduced protease activity;, features a modification of the amino acid from R to W at position 1219.
+The protein's natural variant, known as in TTP; impairs protein secretion;, features a modification of the amino acid from G to V at position 1239.
+The protein's natural variant, known as found in a patient with hemolytic uremic syndrome;, features a modification of the amino acid from S to L at position 1314.
+The protein's natural variant, known as in TTP; impairs protein secretion and proteolytic activity;, features a modification of the amino acid from R to W at position 1336.
+The natural variant of this protein is characterized by an amino acid alteration from R to P at position 4.
+The natural variant of this protein is characterized by an amino acid alteration from S to N at position 45.
+The natural variant of this protein is characterized by an amino acid alteration from D to H at position 77.
+The protein's natural variant, known as in strain: Isolate S98, features a modification of the amino acid from L to F at position 239.
+The protein's natural variant, known as in strain: Isolate S98, features a modification of the amino acid from M to T at position 324.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from A to S at position 214.
+The protein's natural variant, known as in embryonal carcinoma cell line RAC65, features a modification of the amino acid from G to A at position 391.
+The protein's natural variant, known as in ovarian cancer and renal cell carcinoma cell lines, features a modification of the amino acid from L to M at position 15.
+The protein's natural variant, known as in renal cell carcinoma cell line, features a modification of the amino acid from P to L at position 19.
+The protein's natural variant, known as in strain: LA79, features a modification of the amino acid from V to I at position 6.
+The protein's natural variant, known as in COXPD31;, features a modification of the amino acid from L to Q at position 71.
+The protein's natural variant, known as in COXPD31;, features a modification of the amino acid from L to F at position 306.
+The protein's natural variant, known as in COXPD31;, features a modification of the amino acid from K to E at position 343.
+The protein's natural variant, known as in COXPD31; unknown pathological significance;, features a modification of the amino acid from H to D at position 512.
+The protein's natural variant, known as in COXPD31; unknown pathological significance;, features a modification of the amino acid from L to R at position 582.
+The protein's natural variant, known as in strain: PID 2, features a modification of the amino acid from A to Y at position 106.
+The protein's natural variant, known as in strain: PID 2, features a modification of the amino acid from A to G at position 298.
+The protein's natural variant, known as in strain: PID 2, features a modification of the amino acid from D to E at position 437.
+The protein's natural variant, known as in strain: PID 2, features a modification of the amino acid from L to V at position 451.
+The protein's natural variant, known as in strain: PID 2, features a modification of the amino acid from L to H at position 494.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from A to V at position 22.
+The natural variant of this protein is characterized by an amino acid alteration from S to F at position 57.
+The protein's natural variant, known as in IFN-tau3B, features a modification of the amino acid from T to S at position 87.
+The protein's natural variant, known as in IFN-tau3B, features a modification of the amino acid from FE to SQ at position 125.
+The protein's natural variant, known as in IFN-tau3B, features a modification of the amino acid from L to Y at position 130.
+The protein's natural variant, known as rare variant; found in a patient with pulmonary hypertension; unknown pathological significance;, features a modification of the amino acid from N to S at position 13.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from P to S at position 130.
+The protein's natural variant, known as in JPS;, features a modification of the amino acid from E to G at position 330.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from D to N at position 351.
+The protein's natural variant, known as in JP/HHT and JPS;, features a modification of the amino acid from G to R at position 352.
+The protein's natural variant, known as in JPS;, features a modification of the amino acid from R to C at position 361.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to H at position 361.
+The protein's natural variant, known as in JP/HHT;, features a modification of the amino acid from G to D at position 386.
+The protein's natural variant, known as in pancreatic carcinoma;, features a modification of the amino acid from D to H at position 493.
+The protein's natural variant, known as in MYHRS;, features a modification of the amino acid from I to M at position 500.
+The protein's natural variant, known as in MYHRS; there is an enhanced levels of SMAD4 protein with lower levels of ubiquitinated SMAD4 fibroblasts compared to controls suggesting stabilization of the mutant protein; 8-fold increase in phosphorylated SMAD2 and SMAD3; 11-fold increase in phosphorylated SMAD1, SMAD5 and SMAD8 in cell nuclei compared to controls;, features a modification of the amino acid from I to T at position 500.
+The protein's natural variant, known as in MYHRS;, features a modification of the amino acid from I to V at position 500.
+The protein's natural variant, known as in RP81; results in cilia shortening;, features a modification of the amino acid from E to K at position 34.
+The protein's natural variant, known as in SRTD18; patient cells show reduced amount of IFT43 protein and do not have cilia;, features a modification of the amino acid from W to R at position 174.
+The protein's natural variant, known as in CTRCT1; nuclear progressive cataract;, features a modification of the amino acid from R to T at position 23.
+The protein's natural variant, known as in CTRCT1; unknown pathological significance;, features a modification of the amino acid from W to R at position 25.
+The protein's natural variant, known as in CTRCT1; unknown pathological significance, features a modification of the amino acid from T to R at position 39.
+The protein's natural variant, known as in CTRCT1; cataract with microcornea;, features a modification of the amino acid from V to E at position 44.
+The protein's natural variant, known as in CTRCT1; unknown pathological significance;, features a modification of the amino acid from W to S at position 45.
+The protein's natural variant, known as in CTRCT1; unknown pathological significance;, features a modification of the amino acid from G to R at position 46.
+The protein's natural variant, known as in CTRCT1; unknown pathological significance; abolishes localization to the plasma membrane and function;, features a modification of the amino acid from D to N at position 47.
+The protein's natural variant, known as in CTRCT1; zonular pulverulent;, features a modification of the amino acid from E to K at position 48.
+The protein's natural variant, known as in CTRCT1; zonular pulverulent and nuclear progressive cataract, features a modification of the amino acid from V to G at position 64.
+The protein's natural variant, known as in CTRCT1, features a modification of the amino acid from D to G at position 67.
+The protein's natural variant, known as in CTRCT1, features a modification of the amino acid from S to F at position 73.
+The protein's natural variant, known as in CTRCT1, features a modification of the amino acid from R to C at position 76.
+The protein's natural variant, known as in CTRCT1; decreased gap junction channel activity, features a modification of the amino acid from P to L at position 88.
+The protein's natural variant, known as in CTRCT1; severely decreased gap junction channel activity; does not localize to the cell membrane, features a modification of the amino acid from P to Q at position 88.
+The protein's natural variant, known as in CTRCT1; zonular pulverulent;, features a modification of the amino acid from P to S at position 88.
+The protein's natural variant, known as in CTRCT1; unknown pathological significance;, features a modification of the amino acid from A to E at position 118.
+The protein's natural variant, known as in CTRCT1; unknown pathological significance;, features a modification of the amino acid from E to K at position 162.
+The protein's natural variant, known as in CTRCT1; cataract with microcornea;, features a modification of the amino acid from R to Q at position 198.
+The protein's natural variant, known as likely benign variant; does not affect gap junctions formation and gap junctional currents;, features a modification of the amino acid from I to M at position 247.
+The protein's natural variant, known as in strain: DBA/2J, features a modification of the amino acid from A to T at position 49.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation; greatly reduces kinase activity, increases cell proliferation and cell survival, features a modification of the amino acid from T to M at position 112.
+The protein's natural variant, known as in an ovarian mucinous carcinoma sample; somatic mutation; greatly reduces kinase activity, increases cell proliferation and cell survival, features a modification of the amino acid from D to N at position 161.
+The protein's natural variant, known as in a lung neuroendocrine carcinoma sample; somatic mutation; greatly reduces kinase activity, increases cell proliferation, cell adhesion and cell survival, features a modification of the amino acid from P to S at position 216.
+The protein's natural variant, known as in DYT25; loss of function mutation;, features a modification of the amino acid from V to M at position 137.
+The protein's natural variant, known as in DYT25; loss of function mutation;, features a modification of the amino acid from E to K at position 155.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from V to I at position 475.
+The protein's natural variant, known as in a gastric adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from R to Q at position 31.
+The protein's natural variant, known as in a breast infiltrating ductal carcinoma sample; somatic mutation, features a modification of the amino acid from I to M at position 275.
+The protein's natural variant, known as in MMYAT; autosomal dominant; patient cells show decreased mitochondrial fusion and mitochondrial network formation; patient cells show increased mitochondria aggregation and fragmentation;, features a modification of the amino acid from V to M at position 8.
+The protein's natural variant, known as in MMYAT; unknown pathological significance;, features a modification of the amino acid from T to I at position 324.
+The protein's natural variant, known as in MMYAT; unknown pathological significance;, features a modification of the amino acid from R to C at position 345.
+The protein's natural variant, known as in MMYAT; unknown pathological significance;, features a modification of the amino acid from F to L at position 376.
+The protein's natural variant, known as in strain: Oregon-R, features a modification of the amino acid from P to T at position 136.
+The protein's natural variant, known as in strain: Oregon-R, features a modification of the amino acid from A to V at position 209.
+The protein's natural variant, known as in strain: Oregon-R, features a modification of the amino acid from Y to C at position 358.
+The protein's natural variant, known as in strain: 2b, features a modification of the amino acid from V to I at position 411.
+The protein's natural variant, known as in strain: 2b, features a modification of the amino acid from H to Y at position 418.
+The protein's natural variant, known as in strain: 2b and Oregon-R, features a modification of the amino acid from S to L at position 425.
+The protein's natural variant, known as in strain: Oregon-R, features a modification of the amino acid from P to T at position 734.
+The protein's natural variant, known as in strain: Oregon-R, features a modification of the amino acid from S to A at position 958.
+The protein's natural variant, known as in strain: Oregon-R, features a modification of the amino acid from K to R at position 1069.
+The protein's natural variant, known as in strain: Oregon-R, features a modification of the amino acid from A to G at position 1146.
+The protein's natural variant, known as in strain: Oregon-R, features a modification of the amino acid from A to T at position 1167.
+The protein's natural variant, known as in strain: 2b, features a modification of the amino acid from A to D at position 1209.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to W at position 25.
+The natural variant of this protein is characterized by an amino acid alteration from A to S at position 136.
+The protein's natural variant, known as in strain: ECOR 37, features a modification of the amino acid from G to D at position 63.
+The natural variant of this protein is characterized by an amino acid alteration from GV to CA at position 44.
+The natural variant of this protein is characterized by an amino acid alteration from G to A at position 58.
+The natural variant of this protein is characterized by an amino acid alteration from I to M at position 60.
+The protein's natural variant, known as in DFNB15;, features a modification of the amino acid from G to R at position 46.
+The protein's natural variant, known as in DFNB15;, features a modification of the amino acid from M to I at position 88.
+The protein's natural variant, known as in DFNB15;, features a modification of the amino acid from G to D at position 94.
+The protein's natural variant, known as in DFNB15;, features a modification of the amino acid from R to C at position 189.
+The protein's natural variant, known as in DFNB15;, features a modification of the amino acid from T to I at position 221.
+The protein's natural variant, known as in DFNB15;, features a modification of the amino acid from G to D at position 256.
+The protein's natural variant, known as in DFNB15;, features a modification of the amino acid from L to R at position 262.
+The protein's natural variant, known as in PFMO-2 and PFMO-4, features a modification of the amino acid from A to S at position 120.
+The protein's natural variant, known as in PFMO-2 and PFMO-4, features a modification of the amino acid from Q to E at position 136.
+The protein's natural variant, known as in NPHS13; abrogates interaction with NUP93;, features a modification of the amino acid from F to S at position 1995.
+The protein's natural variant, known as in MTDPS12A; decreased function in ADP transport;, features a modification of the amino acid from R to H at position 80.
+The protein's natural variant, known as in PEOA2; decreased function in ADP transport, features a modification of the amino acid from A to D at position 90.
+The protein's natural variant, known as in PEOA2; decreased function in ADP transport;, features a modification of the amino acid from L to P at position 98.
+The protein's natural variant, known as in PEOA2; decreased function in ADP transport;, features a modification of the amino acid from D to G at position 104.
+The protein's natural variant, known as in PEOA2; decreased function in ADP transport; inverted direction of ADP:ATP transport, with ATP entering the mitochondrial matrix;, features a modification of the amino acid from A to P at position 114.
+The protein's natural variant, known as in MTDPS12B; loss of function in ADP transport;, features a modification of the amino acid from A to D at position 123.
+The protein's natural variant, known as in MTDPS12A; severely decreased function in ADP transport;, features a modification of the amino acid from R to G at position 235.
+The protein's natural variant, known as in MTDPS12B; loss of function in ADP transport;, features a modification of the amino acid from R to P at position 236.
+The protein's natural variant, known as in PEOA2; inverted direction of ADP:ATP transport, with ATP entering the mitochondrial matrix;, features a modification of the amino acid from V to M at position 289.
+The protein's natural variant, known as in HLPP1B; variant Wakayama;, features a modification of the amino acid from W to R at position 48.
+The protein's natural variant, known as in San Francisco; found in hyperlipidemic patients;, features a modification of the amino acid from E to K at position 60.
+The protein's natural variant, known as in Africa;, features a modification of the amino acid from K to Q at position 77.
+The protein's natural variant, known as in SPG45; unknown pathological significance, features a modification of the amino acid from L to P at position 460.
+The protein's natural variant, known as in MCSZ;, features a modification of the amino acid from L to F at position 176.
+The protein's natural variant, known as in MCSZ; impaired recruitment to DNA damage sites;, features a modification of the amino acid from E to K at position 326.
+The protein's natural variant, known as in AOA4;, features a modification of the amino acid from G to W at position 375.
+The protein's natural variant, known as in MCSZ; atypical phenotype;, features a modification of the amino acid from R to P at position 462.
+The protein's natural variant, known as in NPHS2, features a modification of the amino acid from R to G at position 3.
+The protein's natural variant, known as in NPHS2, features a modification of the amino acid from R to T at position 18.
+The protein's natural variant, known as in NPHS2, features a modification of the amino acid from R to M at position 26.
+The protein's natural variant, known as in NPHS2;, features a modification of the amino acid from K to M at position 28.
+The protein's natural variant, known as in NPHS2;, features a modification of the amino acid from A to T at position 29.
+The protein's natural variant, known as in NPHS2;, features a modification of the amino acid from E to K at position 30.
+The protein's natural variant, known as in NPHS2, features a modification of the amino acid from E to Q at position 30.
+The natural variant of this protein is characterized by an amino acid alteration from G to E at position 34.
+The protein's natural variant, known as in NPHS2, features a modification of the amino acid from Q to L at position 39.
+The natural variant of this protein is characterized by an amino acid alteration from E to A at position 44.
+The protein's natural variant, known as in NPHS2, features a modification of the amino acid from P to T at position 89.
+The protein's natural variant, known as in NPHS2;, features a modification of the amino acid from G to C at position 92.
+The protein's natural variant, known as in NPHS2; unknown pathological significance;, features a modification of the amino acid from G to S at position 97.
+The protein's natural variant, known as in NPHS2, features a modification of the amino acid from L to P at position 107.
+The protein's natural variant, known as in NPHS2, features a modification of the amino acid from M to T at position 115.
+The protein's natural variant, known as in NPHS2, features a modification of the amino acid from T to P at position 116.
+The protein's natural variant, known as in NPHS2;, features a modification of the amino acid from P to L at position 118.
+The protein's natural variant, known as in NPHS2;, features a modification of the amino acid from W to L at position 122.
+The protein's natural variant, known as in NPHS2;, features a modification of the amino acid from W to S at position 122.
+The protein's natural variant, known as in NPHS2;, features a modification of the amino acid from C to W at position 124.
+The protein's natural variant, known as in NPHS2, features a modification of the amino acid from K to N at position 126.
+The protein's natural variant, known as in NPHS2, features a modification of the amino acid from R to P at position 138.
+The protein's natural variant, known as in NPHS2;, features a modification of the amino acid from R to Q at position 138.
+The protein's natural variant, known as in NPHS2;, features a modification of the amino acid from L to R at position 139.
+The protein's natural variant, known as in NPHS2;, features a modification of the amino acid from L to P at position 142.
+The protein's natural variant, known as in NPHS2;, features a modification of the amino acid from D to G at position 160.
+The protein's natural variant, known as in NPHS2;, features a modification of the amino acid from R to C at position 168.
+The protein's natural variant, known as in NPHS2;, features a modification of the amino acid from R to H at position 168.
+The protein's natural variant, known as in NPHS2, features a modification of the amino acid from R to S at position 168.
+The protein's natural variant, known as in NPHS2; unknown pathological significance, features a modification of the amino acid from L to V at position 172.
+The protein's natural variant, known as in NPHS2; requires 2 nucleotide substitutions, features a modification of the amino acid from P to V at position 175.
+The protein's natural variant, known as in NPHS2;, features a modification of the amino acid from V to M at position 180.
+The protein's natural variant, known as in NPHS2, features a modification of the amino acid from D to Y at position 183.
+The protein's natural variant, known as in NPHS2; unknown pathological significance, features a modification of the amino acid from M to I at position 187.
+The protein's natural variant, known as in NPHS2, features a modification of the amino acid from I to V at position 192.
+The protein's natural variant, known as in NPHS2;, features a modification of the amino acid from A to T at position 208.
+The protein's natural variant, known as in NPHS2, features a modification of the amino acid from S to A at position 211.
+The protein's natural variant, known as in NPHS2, features a modification of the amino acid from A to T at position 213.
+The protein's natural variant, known as in NPHS2, features a modification of the amino acid from V to G at position 218.
+The protein's natural variant, known as in NPHS2, features a modification of the amino acid from T to I at position 221.
+The protein's natural variant, known as in NPHS2, features a modification of the amino acid from H to D at position 228.
+The protein's natural variant, known as in NPHS2, features a modification of the amino acid from R to L at position 229.
+The protein's natural variant, known as in NPHS2; unknown pathological significance;, features a modification of the amino acid from R to Q at position 229.
+The protein's natural variant, known as in NPHS2;, features a modification of the amino acid from R to S at position 238.
+The protein's natural variant, known as in NPHS2; unknown pathological significance, features a modification of the amino acid from C to F at position 254.
+The protein's natural variant, known as in NPHS2;, features a modification of the amino acid from V to E at position 260.
+The protein's natural variant, known as in NPHS2, features a modification of the amino acid from D to N at position 267.
+The protein's natural variant, known as in NPHS2, features a modification of the amino acid from V to L at position 268.
+The protein's natural variant, known as in NPHS2, features a modification of the amino acid from H to L at position 276.
+The protein's natural variant, known as in NPHS2, features a modification of the amino acid from E to A at position 281.
+The protein's natural variant, known as in NPHS2, features a modification of the amino acid from E to K at position 281.
+The protein's natural variant, known as in NPHS2; unknown pathological significance;, features a modification of the amino acid from A to V at position 284.
+The protein's natural variant, known as in NPHS2;, features a modification of the amino acid from V to M at position 290.
+The protein's natural variant, known as in NPHS2;, features a modification of the amino acid from R to W at position 291.
+The protein's natural variant, known as in NPHS2, features a modification of the amino acid from E to K at position 296.
+The protein's natural variant, known as in NPHS2, features a modification of the amino acid from A to V at position 309.
+The protein's natural variant, known as in NPHS2; unknown pathological significance, features a modification of the amino acid from E to K at position 310.
+The protein's natural variant, known as in NPHS2; unknown pathological significance;, features a modification of the amino acid from E to V at position 310.
+The protein's natural variant, known as in NPHS2; unknown pathological significance, features a modification of the amino acid from T to I at position 315.
+The protein's natural variant, known as in NPHS2;, features a modification of the amino acid from R to Q at position 322.
+The protein's natural variant, known as in NPHS2; unknown pathological significance, features a modification of the amino acid from Q to R at position 328.
+The protein's natural variant, known as in NPHS2; unknown pathological significance;, features a modification of the amino acid from E to G at position 333.
+The protein's natural variant, known as in NPHS2;, features a modification of the amino acid from P to S at position 341.
+The protein's natural variant, known as in NPHS2, features a modification of the amino acid from V to G at position 370.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from V to L at position 371.
+The protein's natural variant, known as in DIAR3; has a significantly reduced ability to inhibit trypsin compared to wild-type;, features a modification of the amino acid from Y to C at position 163.
+The protein's natural variant, known as in strain: B, features a modification of the amino acid from E to K at position 128.
+The protein's natural variant, known as in CAGS;, features a modification of the amino acid from G to V at position 278.
+The protein's natural variant, known as in CAGS, features a modification of the amino acid from A to T at position 377.
+The protein's natural variant, known as in CAGS, features a modification of the amino acid from L to P at position 519.
+The protein's natural variant, known as in CAGS, features a modification of the amino acid from L to R at position 716.
+The protein's natural variant, known as in CAGS, features a modification of the amino acid from L to R at position 1120.
+The protein's natural variant, known as in CAGS, features a modification of the amino acid from P to R at position 1186.
+The protein's natural variant, known as in CAGS, features a modification of the amino acid from G to A at position 1364.
+The protein's natural variant, known as in CAGS, features a modification of the amino acid from S to P at position 1880.
+The protein's natural variant, known as in CAGS, features a modification of the amino acid from R to G at position 2434.
+The protein's natural variant, known as variant of uncertain significance; may be a genetic risk for patients with azoospermia caused by meiotic arrest, features a modification of the amino acid from Y to H at position 335.
+The protein's natural variant, known as in allele A;, features a modification of the amino acid from T to S at position 681.
+The protein's natural variant, known as in allele L9/24; significantly reduces affinity for the DNA-binding motif 5'-GCCTCCCTAGCCACG-3';, features a modification of the amino acid from K to E at position 788.
+The protein's natural variant, known as in allele L20; reduces affinity for the DNA-binding motif 5?-GCCTCCCTAGCCACG-3';, features a modification of the amino acid from N to H at position 790.
+The protein's natural variant, known as in allele L13; Increases affinity for the DNA-binding motif 5'-GCCTCCCTAGCCACG-3';, features a modification of the amino acid from S to R at position 814.
+The natural variant of this protein is characterized by an amino acid alteration from E to D at position 141.
+The natural variant of this protein is characterized by an amino acid alteration from H to D at position 179.
+The natural variant of this protein is characterized by an amino acid alteration from L to V at position 195.
+The protein's natural variant, known as in CMD1AA;, features a modification of the amino acid from Q to R at position 9.
+The protein's natural variant, known as in CMH23 and CMD1AA;, features a modification of the amino acid from A to T at position 119.
+The protein's natural variant, known as in MPD6; unknown pathological significance;, features a modification of the amino acid from L to P at position 131.
+The protein's natural variant, known as in CMH23;, features a modification of the amino acid from M to T at position 228.
+The protein's natural variant, known as in MPD6;, features a modification of the amino acid from C to R at position 487.
+The protein's natural variant, known as in CMH23;, features a modification of the amino acid from T to M at position 495.
+The protein's natural variant, known as in CMH23;, features a modification of the amino acid from E to A at position 583.
+The protein's natural variant, known as in CMH23;, features a modification of the amino acid from E to G at position 628.
+The protein's natural variant, known as in MYOCOZ;, features a modification of the amino acid from L to R at position 727.
+The protein's natural variant, known as in LGMDD1; the mutation results in inefficient inhibition of protein aggregation by isoform B;, features a modification of the amino acid from F to I at position 89.
+The protein's natural variant, known as in LGMDD1; the mutation results in inefficient inhibition of protein aggregation by isoform B;, features a modification of the amino acid from F to L at position 93.
+The protein's natural variant, known as found in a family with autosomal-dominantly inherited distal-onset myopathy; significant loss of its ability to suppress aggregation of polyglutamine-containing proteins, features a modification of the amino acid from P to L at position 96.
+The protein's natural variant, known as in LGMDD1;, features a modification of the amino acid from P to R at position 96.
+The protein's natural variant, known as in strain: ATCCVR-358 / Fuller / CIP 107027, features a modification of the amino acid from QVREGDVSAGNDT to KFVKATFHRRY at position 133.
+The protein's natural variant, known as in strain: ATCCVR-358 /Fuller / CIP 107027, features a modification of the amino acid from KFRYPEDEALRK to SFVIQKNFAQ at position 149.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from G to D at position 425.
+The protein's natural variant, known as in BBS12;, features a modification of the amino acid from L to R at position 88.
+The protein's natural variant, known as associated with H-263 in a patient with Bardet-Biedl syndrome compound heterozygote for mutations in BBS10;, features a modification of the amino acid from G to S at position 119.
+The protein's natural variant, known as in BBS12; unknown pathological significance; significantly reduces the interaction with MKKS; the interaction with BBS10 is not affected by this mutation;, features a modification of the amino acid from P to L at position 159.
+The protein's natural variant, known as associated with S-119 in a patient with Bardet-Biedl syndrome compound heterozygote for mutations in BBS10;, features a modification of the amino acid from Y to H at position 263.
+The protein's natural variant, known as in BBS12; significantly reduces the interaction with MKKS; shows significantly decreased interaction with BBS7; the interaction with BBS10 is not affected by this mutation;, features a modification of the amino acid from A to P at position 289.
+The protein's natural variant, known as in BBS12, features a modification of the amino acid from Q to E at position 293.
+The protein's natural variant, known as in BBS12; significantly reduces the interaction with MKKS; shows significantly decreased interaction with BBS7; the interaction with BBS10 is not affected by this mutation;, features a modification of the amino acid from I to T at position 346.
+The protein's natural variant, known as in BBS12;, features a modification of the amino acid from R to Q at position 355.
+The protein's natural variant, known as in BBS12;, features a modification of the amino acid from V to M at position 400.
+The protein's natural variant, known as in a patient with Bardet-Biedl syndrome compound heterozygote for BBS2 mutations; unknown pathological significance, features a modification of the amino acid from K to R at position 408.
+The protein's natural variant, known as in BBS12; significantly reduces the interaction with MKKS; shows significantly decreased interaction with BBS7; the interaction with BBS10 is not affected by this mutation;, features a modification of the amino acid from T to M at position 501.
+The protein's natural variant, known as in a patient with Bardet-Biedl syndrome homozygous for a mutation in BBS2; unknown pathological significance;, features a modification of the amino acid from Y to C at position 524.
+The protein's natural variant, known as in BBS12; unknown pathological significance;, features a modification of the amino acid from R to H at position 525.
+The protein's natural variant, known as in BBS12, features a modification of the amino acid from G to D at position 539.
+The protein's natural variant, known as in BBS12; significantly reduces the interaction with MKKS; shows significantly decreased interaction with BBS7; the interaction with BBS10 is not affected by this mutation;, features a modification of the amino acid from G to V at position 540.
+The protein's natural variant, known as in BBS12;, features a modification of the amino acid from R to C at position 674.
+The protein's natural variant, known as in an individual with an atypical late-onset form of retinitis pigmentosa; does not affect ability to suppress GUCY2D activity induced by GCAPA;, features a modification of the amino acid from W to R at position 6.
+The protein's natural variant, known as in an individual with an atypical late-onset form of retinitis pigmentosa;, features a modification of the amino acid from E to D at position 23.
+The protein's natural variant, known as does not affect ability to suppress GUCY2D activity induced by GCAPA;, features a modification of the amino acid from G to R at position 35.
+The protein's natural variant, known as in an individual with cone-rod degeneration; abolishes protein expression; less effective in suppressing GUCY2D activity by GCAPA;, features a modification of the amino acid from G to V at position 57.
+The protein's natural variant, known as less effective in suppressing GUCY2D activity induced by GCAPA;, features a modification of the amino acid from R to W at position 68.
+The protein's natural variant, known as in an individual with cone-rod dystrophy features; less effective in suppressing GUCY2D activity by GCAPA;, features a modification of the amino acid from K to M at position 130.
+The protein's natural variant, known as in strain: B, features a modification of the amino acid from V to A at position 60.
+The protein's natural variant, known as in strain: B, features a modification of the amino acid from H to N at position 87.
+The protein's natural variant, known as in strain: B, features a modification of the amino acid from G to R at position 127.
+The protein's natural variant, known as in strain: B, features a modification of the amino acid from V to I at position 255.
+The protein's natural variant, known as in a breast pleomorphic lobular carcinoma sample; somatic mutation, features a modification of the amino acid from I to M at position 500.
+The protein's natural variant, known as in strain: NZB, features a modification of the amino acid from N to S at position 79.
+The protein's natural variant, known as in PRLTS2; unknown pathological significance, features a modification of the amino acid from L to Q at position 46.
+The protein's natural variant, known as in PRLTS2; unknown pathological significance, features a modification of the amino acid from K to E at position 58.
+The protein's natural variant, known as in PRLTS2; unknown pathological significance, features a modification of the amino acid from R to K at position 87.
+The protein's natural variant, known as in PRLTS2; unknown pathological significance, features a modification of the amino acid from R to C at position 150.
+The protein's natural variant, known as in PRLTS2; the mutant protein is expressed, can dimerize and localizes to the mitochondria; has significantly decreased enzymatic activity compared to wild-type;, features a modification of the amino acid from L to V at position 200.
+The protein's natural variant, known as in PRLTS2; unknown pathological significance, features a modification of the amino acid from R to Q at position 327.
+The protein's natural variant, known as in PRLTS2; the mutant protein is expressed, can dimerize and localizes to the mitochondria; has significantly decreased enzymatic activity compared to wild-type;, features a modification of the amino acid from V to L at position 368.
+The protein's natural variant, known as in MCLMR, features a modification of the amino acid from F to L at position 144.
+The protein's natural variant, known as in MCLMR, features a modification of the amino acid from R to C at position 234.
+The protein's natural variant, known as in MCLMR;, features a modification of the amino acid from S to C at position 235.
+The protein's natural variant, known as in MCLMR;, features a modification of the amino acid from R to C at position 944.
+The protein's natural variant, known as reduces transactivation activity; does not affect transrepression activity;, features a modification of the amino acid from R to K at position 23.
+The protein's natural variant, known as variant of uncertain significance; associated in cis with A-321 and S-766 in one individual; doubles transactivation potential, features a modification of the amino acid from N to D at position 72.
+The protein's natural variant, known as variant of uncertain significance; associated in cis with D-72 and S-766 in one individual; doubles transactivation potential, features a modification of the amino acid from V to A at position 321.
+The protein's natural variant, known as enhances transactivation activity; does not affect transrepression activity; may increase sensitivity to exogenously administered glucocorticoids; may contribute to central obesity in men and show lack of association with other risk factors for coronary heart disease and diabetes mellitus;, features a modification of the amino acid from N to S at position 363.
+The natural variant of this protein is characterized by an amino acid alteration from C to Y at position 421.
+The protein's natural variant, known as in GCCR; unknown pathological significance; reduces transactivation activity; delays nuclear translocation; does not exert a dominant negative effect; impairs DNA binding, features a modification of the amino acid from V to A at position 423.
+The protein's natural variant, known as in GCCR;, features a modification of the amino acid from R to H at position 477.
+The protein's natural variant, known as in GCCR; loss of DNA-binding and of transactivation activity; incomplete dexamethasone-induced translocation to the nucleus; no effect on dexamethasone-binding affinity compared with wild-type, features a modification of the amino acid from R to S at position 477.
+The protein's natural variant, known as in GCCR; decreased DNA-binding and transactivation activity; incomplete dexamethasone-induced translocation to the nucleus; no effect on dexamethasone-binding affinity compared with wild-type, features a modification of the amino acid from Y to C at position 478.
+The protein's natural variant, known as in GCCR; reduces transactivation activity; enhances transrepression activity; reduces affinity for ligand; delays nuclear translocation; does not exert a dominant negative effect; does not impair DNA binding, features a modification of the amino acid from T to I at position 556.
+The protein's natural variant, known as in GCCR; interferes with translocation to the nucleus and thereby strongly reduces transcription activation; is equally impaired in nuclear export; acts as dominant negative mutant;, features a modification of the amino acid from I to N at position 559.
+The protein's natural variant, known as in pseudohermaphroditism; female with hypokalemia due to glucocorticoid resistance; 6-fold reduction in binding affinity compared with the wild-type receptor;, features a modification of the amino acid from V to A at position 571.
+The protein's natural variant, known as in GCCR; unknown pathological significance; reduces transactivation activity; enhances transrepression activity; reduces affinity for ligand; delays nuclear translocation; does not exert a dominant negative effect; does not impair DNA binding, features a modification of the amino acid from V to G at position 575.
+The protein's natural variant, known as in GCCR;, features a modification of the amino acid from D to V at position 641.
+The protein's natural variant, known as in GCCR; loss of dexamethasone-binding, dexamethasone-induced translocation to the nucleus and of transactivation activity, features a modification of the amino acid from L to P at position 672.
+The protein's natural variant, known as in GCCR; has 50% binding affinity;, features a modification of the amino acid from G to S at position 679.
+The protein's natural variant, known as in GCCR; unknown pathological significance; reduces transactivation; reduces affinity for ligand; exerts a dominant negative effect; does not impair DNA binding, features a modification of the amino acid from R to Q at position 714.
+The protein's natural variant, known as in GCCR; unknown pathological significance; reduces transactivation and transrepression activity; reduces affinity for ligand; delays nuclear translocation; does not impair DNA binding, features a modification of the amino acid from H to R at position 726.
+The protein's natural variant, known as in GCCR;, features a modification of the amino acid from V to I at position 729.
+The protein's natural variant, known as in GCCR; reduces transactivation of the glucocorticoid-inducible tumor virus promoter; reduces affinity for ligand; delays its nuclear translocation; acts as dominant negative mutant;, features a modification of the amino acid from F to L at position 737.
+The protein's natural variant, known as in GCCR; alters interaction with NCOA2 and strongly reduces transcription activation; acts as dominant negative mutant;, features a modification of the amino acid from I to M at position 747.
+The protein's natural variant, known as variant of uncertain significance; associated in cis with D-72 and A-321 in one individual; doubles transactivation potential, features a modification of the amino acid from N to S at position 766.
+The protein's natural variant, known as in GCCR; reduces transactivation of the glucocorticoid-inducible tumor virus promoter; reduces affinity for ligand; delays its nuclear translocation; acts as dominant negative mutant;, features a modification of the amino acid from L to P at position 773.
+The protein's natural variant, known as found in a patient with a neurodevelopmental disorder; unknown pathological significance;, features a modification of the amino acid from D to Y at position 8.
+The protein's natural variant, known as found in a patient with a neurodevelopmental disorder; unknown pathological significance, features a modification of the amino acid from Q to E at position 107.
+The protein's natural variant, known as in strain: M110, features a modification of the amino acid from C to R at position 39.
+The protein's natural variant, known as in strain: M110, features a modification of the amino acid from I to P at position 80.
+The protein's natural variant, known as in strain: M110, features a modification of the amino acid from E to G at position 85.
+The protein's natural variant, known as in strain: M110, features a modification of the amino acid from C to V at position 228.
+The protein's natural variant, known as in strain: cv. Landsberg erecta and cv. Sha, features a modification of the amino acid from A to T at position 22.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from Y to N at position 48.
+The protein's natural variant, known as in CHTD2;, features a modification of the amino acid from P to S at position 208.
+The protein's natural variant, known as in CHTD2;, features a modification of the amino acid from Q to K at position 230.
+The protein's natural variant, known as found in an patient with a form of frontometaphyseal dysplasia; unknown pathological significance;, features a modification of the amino acid from E to K at position 569.
+The protein's natural variant, known as in strain: MN47; BTZ043-resistant, features a modification of the amino acid from C to G at position 386.
+The protein's natural variant, known as in strain: MN84; BTZ043-resistant, features a modification of the amino acid from C to S at position 386.
+The protein's natural variant, known as in strain: PH496, features a modification of the amino acid from G to S at position 126.
+The protein's natural variant, known as in strain: PH290, features a modification of the amino acid from V to I at position 550.
+The protein's natural variant, known as in strain: PH240, features a modification of the amino acid from Q to R at position 656.
+The protein's natural variant, known as in strain: PH240, features a modification of the amino acid from V to I at position 711.
+The protein's natural variant, known as in strain: PH496, features a modification of the amino acid from R to K at position 831.
+The protein's natural variant, known as in strain: PH240, features a modification of the amino acid from D to E at position 879.
+The protein's natural variant, known as in strain: PH240, features a modification of the amino acid from A to E at position 882.
+The protein's natural variant, known as in strain: PH240, features a modification of the amino acid from N to K at position 885.
+The protein's natural variant, known as in strain: PH240, features a modification of the amino acid from TQDELSK to DKSDLSQ at position 895.
+The protein's natural variant, known as in SCA13; unknown pathological significance; changes channel activity; shifts the voltage dependence of activation, features a modification of the amino acid from D to N at position 129.
+The protein's natural variant, known as variant of uncertain significance; changes channel activity; activates more quickly and deactivates more slowly, features a modification of the amino acid from G to D at position 263.
+The protein's natural variant, known as in SCA13; unknown pathological significance; dominant negative that decreases channel activity; decreases protein abundance; decreases protein stability; decreases localization to the plasma membrane; no effect on tetramerization;, features a modification of the amino acid from R to H at position 366.
+The protein's natural variant, known as in SCA13; dominant negative that induces loss of channel activity; decreases protein abundance; decreases protein stability; decreases localization to the plasma membrane and alters the localization of the wild-type protein; impairs N-glycosylation; no effect on tetramerization;, features a modification of the amino acid from R to H at position 420.
+The protein's natural variant, known as in SCA13; dominant negative that reduces channel activity; alters gating; decreases protein abundance; decreases localization to the plasma membrane; no effect on tetramerization;, features a modification of the amino acid from R to H at position 423.
+The protein's natural variant, known as in SCA13; alters gating; slows channel closing; decreases protein abundance; no effect on localization to the plasma membrane; no effect on N-glycosylation; no effect on tetramerization;, features a modification of the amino acid from F to L at position 448.
+The protein's natural variant, known as in SCA13; unknown pathological significance; no effect on channel activity;, features a modification of the amino acid from D to N at position 477.
+The protein's natural variant, known as in SCA13; changes channel activity; shifts the voltage dependence of activation, features a modification of the amino acid from V to M at position 535.
+The protein's natural variant, known as in SCA13; unknown pathological significance; reduces channel activity; shifts the voltage dependence of activation;, features a modification of the amino acid from S to G at position 591.
+The protein's natural variant, known as in SCA13; unknown pathological significance; no effect on channel activity;, features a modification of the amino acid from G to S at position 643.
+The protein's natural variant, known as in SCA13; unknown pathological significance; no effect on channel activity;, features a modification of the amino acid from P to R at position 645.
+The protein's natural variant, known as in SCA13; unknown pathological significance; no effect on channel activity;, features a modification of the amino acid from D to N at position 746.
+The protein's natural variant, known as in MCAND; reduced cleavage activity towards 'K-63'- and 'K-48'-chains; no effect on phosphorylation, features a modification of the amino acid from D to N at position 256.
+The protein's natural variant, known as in MCAND; partial mislocation at the cytoplasm; reduced cleavage activity towards 'K-63'- and 'K-48'-chains; no effect on phosphorylation;, features a modification of the amino acid from R to W at position 274.
+The protein's natural variant, known as in MCAND; in mice embryo the mutation is lethal; reduced cleavage activity towards 'K-48'-chains but not 'K-63'-chains; no effect on nuclear location; no effect on phosphorylation;, features a modification of the amino acid from L to P at position 352.
+The protein's natural variant, known as in MCAND; unknown pathological significance;, features a modification of the amino acid from R to W at position 404.
+The protein's natural variant, known as in MCAND; decreased mRNA and protein levels; no effect on cleavage activity towards 'K-48'-chains but not 'K-63'-chains; in mice embryo the mutation is lethal; no effect on phosphorylation, features a modification of the amino acid from G to S at position 494.
+The protein's natural variant, known as in MCAND; unknown pathological significance, features a modification of the amino acid from R to W at position 520.
+The protein's natural variant, known as in HHRH;, features a modification of the amino acid from S to F at position 138.
+The protein's natural variant, known as in HHRH;, features a modification of the amino acid from S to L at position 192.
+The protein's natural variant, known as in HHRH;, features a modification of the amino acid from G to R at position 196.
+The protein's natural variant, known as in HHRH;, features a modification of the amino acid from R to L at position 353.
+The protein's natural variant, known as in HHRH;, features a modification of the amino acid from A to E at position 413.
+The protein's natural variant, known as in HHRH;, features a modification of the amino acid from R to W at position 468.
+The protein's natural variant, known as in strain: cv. Ei-2 and cv. Tac-0, features a modification of the amino acid from G to E at position 13.
+The protein's natural variant, known as in strain: cv. Ei-2 and cv. Tac-0, features a modification of the amino acid from T to S at position 18.
+The protein's natural variant, known as in strain: cv. Ag-0, cv. Br-0, cv. CIBC-5, cv. Ei-2, cv. Gy-0, cv. HR-10, cv. HR-5, cv. Kin-0, cv. KNO-10, cv. KNO-18, cv. Lz-0, cv. NFA-8, cv. NFA-10, cv. Pna-10, cv. Ra-0, cv. Rmx-A180, cv. RRS-10, cv. Se-0, cv. Sq-1, cv. Tac-0, cv. Van-0, cv. Var2-6 and cv. Yo-0, features a modification of the amino acid from A to P at position 308.
+The natural variant of this protein is characterized by an amino acid alteration from S to N at position 697.
+The natural variant of this protein is characterized by an amino acid alteration from D to N at position 712.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from T to N at position 190.
+The protein's natural variant, known as in Mac-B, features a modification of the amino acid from R to K at position 71.
+The protein's natural variant, known as in Mac-B, features a modification of the amino acid from A to V at position 107.
+The protein's natural variant, known as in Mac-B, features a modification of the amino acid from P to L at position 192.
+The protein's natural variant, known as in Mac-B, features a modification of the amino acid from G to R at position 262.
+The protein's natural variant, known as in Mac-B, features a modification of the amino acid from Y to C at position 343.
+The protein's natural variant, known as does not affect enzymatic activity;, features a modification of the amino acid from K to R at position 40.
+The protein's natural variant, known as in BCHED;, features a modification of the amino acid from T to M at position 52.
+The protein's natural variant, known as in BCHED;, features a modification of the amino acid from F to I at position 56.
+The protein's natural variant, known as in BCHED; enzymatically inactive in the plasma;, features a modification of the amino acid from Y to C at position 61.
+The protein's natural variant, known as in BCHED; reduced enzyme activity with butyrylthiocholine as substrate; inactive with butyrylthiocholine as substrate in the presence of G-98; 2-fold lower affinity for butyrylthiocholine; 10-fold lower affinity for butyrylthiocholine in the presence of G-98;, features a modification of the amino acid from A to V at position 62.
+The protein's natural variant, known as in BCHED; seems to cause reduced expression of the protein;, features a modification of the amino acid from P to S at position 65.
+The protein's natural variant, known as in BCHED; atypical form; reduced enzyme activity with butyrylthiocholine as substrate; inactive with butyrylthiocholine as substrate in the presence of V-62; 2-fold lower affinity for butyrylthiocholine; 10-fold lower affinity for butyrylthiocholine in the presence of V-62 or at homozygosity;, features a modification of the amino acid from D to G at position 98.
+The protein's natural variant, known as in BCHED, features a modification of the amino acid from D to H at position 98.
+The protein's natural variant, known as in BCHED; reduced enzyme activity;, features a modification of the amino acid from G to R at position 103.
+The protein's natural variant, known as in BCHED; the mutant undergoes rapid degradation, features a modification of the amino acid from E to D at position 118.
+The protein's natural variant, known as in BCHED;, features a modification of the amino acid from N to Y at position 124.
+The protein's natural variant, known as does not affect enzyme activity;, features a modification of the amino acid from I to M at position 127.
+The protein's natural variant, known as in BCHED;, features a modification of the amino acid from P to S at position 128.
+The protein's natural variant, known as in BCHED;, features a modification of the amino acid from G to D at position 143.
+The protein's natural variant, known as in BCHED; seems to cause reduced expression of the protein;, features a modification of the amino acid from L to F at position 153.
+The protein's natural variant, known as in BCHED;, features a modification of the amino acid from Y to C at position 156.
+The protein's natural variant, known as in BCHED; allele H variant;, features a modification of the amino acid from V to M at position 170.
+The protein's natural variant, known as in BCHED; seems to cause reduced expression of the protein;, features a modification of the amino acid from D to E at position 198.
+The protein's natural variant, known as in BCHED; enzymatically inactive in the plasma;, features a modification of the amino acid from S to G at position 226.
+The protein's natural variant, known as in BCHED, features a modification of the amino acid from A to V at position 227.
+The protein's natural variant, known as in BCHED; enzymatically inactive in the plasma, features a modification of the amino acid from A to T at position 229.
+The protein's natural variant, known as in BCHED, features a modification of the amino acid from V to D at position 232.
+The protein's natural variant, known as in BCHED; allele fluoride-1;, features a modification of the amino acid from T to M at position 271.
+The protein's natural variant, known as in BCHED;, features a modification of the amino acid from T to P at position 278.
+The protein's natural variant, known as in BCHED;, features a modification of the amino acid from K to R at position 295.
+The protein's natural variant, known as does not affect enzymatic activity;, features a modification of the amino acid from V to M at position 322.
+The protein's natural variant, known as in BCHED; expressed at very low level;, features a modification of the amino acid from L to P at position 335.
+The protein's natural variant, known as in BCHED;, features a modification of the amino acid from A to D at position 356.
+The protein's natural variant, known as in BCHED; BChE variant form; fluoride-resistant;, features a modification of the amino acid from L to I at position 358.
+The protein's natural variant, known as in BCHED; results in 20% of activity compared to wild-type, features a modification of the amino acid from G to C at position 361.
+The protein's natural variant, known as in BCHED;, features a modification of the amino acid from G to R at position 393.
+The protein's natural variant, known as in BCHED;, features a modification of the amino acid from R to C at position 414.
+The protein's natural variant, known as in BCHED; allele fluoride-2;, features a modification of the amino acid from G to V at position 418.
+The protein's natural variant, known as in BCHED, features a modification of the amino acid from F to S at position 446.
+The protein's natural variant, known as in BCHED;, features a modification of the amino acid from E to K at position 488.
+The protein's natural variant, known as does not affect enzymatic activity;, features a modification of the amino acid from R to W at position 498.
+The protein's natural variant, known as in BCHED; seems to cause reduced expression of the protein, features a modification of the amino acid from W to R at position 499.
+The protein's natural variant, known as in BCHED;, features a modification of the amino acid from F to L at position 502.
+The protein's natural variant, known as in BCHED; allele J variant;, features a modification of the amino acid from E to V at position 525.
+The protein's natural variant, known as in BCHED;, features a modification of the amino acid from R to C at position 543.
+The protein's natural variant, known as in BCHED; seems to cause reduced expression of the protein, features a modification of the amino acid from Q to L at position 546.
+The protein's natural variant, known as in BCHED; allele K variant; with reduced enzyme activity;, features a modification of the amino acid from A to T at position 567.
+The protein's natural variant, known as in UROCD;, features a modification of the amino acid from L to P at position 70.
+The protein's natural variant, known as in UROCD; loss of activity;, features a modification of the amino acid from R to C at position 450.
+The protein's natural variant, known as in strain: B, features a modification of the amino acid from Q to L at position 85.
+The protein's natural variant, known as in BDB2;, features a modification of the amino acid from P to A at position 35.
+The protein's natural variant, known as in SYM1A and TCC;, features a modification of the amino acid from P to R at position 35.
+The protein's natural variant, known as in SYM1A and BDB2;, features a modification of the amino acid from P to S at position 35.
+The protein's natural variant, known as in BDB2, features a modification of the amino acid from A to P at position 36.
+The protein's natural variant, known as in BDB2, features a modification of the amino acid from E to K at position 48.
+The protein's natural variant, known as found in a family with radioulnar synostosis; unknown pathological significance, features a modification of the amino acid from P to L at position 83.
+The protein's natural variant, known as found in a case of radioulnar synostosis; unknown pathological significance, features a modification of the amino acid from L to M at position 104.
+The protein's natural variant, known as in BDB2;, features a modification of the amino acid from R to G at position 167.
+The protein's natural variant, known as in SYM1A; sporadic; de novo mutation;, features a modification of the amino acid from C to Y at position 184.
+The protein's natural variant, known as in BDB2, features a modification of the amino acid from P to S at position 187.
+The protein's natural variant, known as in SYM1A;, features a modification of the amino acid from G to C at position 189.
+The protein's natural variant, known as in TCC;, features a modification of the amino acid from R to L at position 204.
+The protein's natural variant, known as in SYM1A;, features a modification of the amino acid from W to C at position 205.
+The protein's natural variant, known as in SYNS1;, features a modification of the amino acid from W to G at position 217.
+The protein's natural variant, known as in SYM1A, features a modification of the amino acid from I to N at position 220.
+The protein's natural variant, known as in SYM1A and TCC;, features a modification of the amino acid from Y to C at position 222.
+The protein's natural variant, known as in SYM1A;, features a modification of the amino acid from Y to D at position 222.
+The protein's natural variant, known as in SYM1A;, features a modification of the amino acid from P to L at position 223.
+The protein's natural variant, known as in SYNS1;, features a modification of the amino acid from C to W at position 232.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation, features a modification of the amino acid from R to K at position 777.
+The protein's natural variant, known as in strain: ORS1096, features a modification of the amino acid from R to K at position 8.
+The protein's natural variant, known as in strain: ORS1096, features a modification of the amino acid from Q to E at position 16.
+The protein's natural variant, known as in strain: ORS1096, features a modification of the amino acid from I to V at position 21.
+The protein's natural variant, known as in strain: ORS1096, features a modification of the amino acid from M to I at position 69.
+The protein's natural variant, known as in strain: ORS1096, features a modification of the amino acid from K to R at position 77.
+The protein's natural variant, known as in strain: ORS1096, features a modification of the amino acid from I to L at position 102.
+The protein's natural variant, known as in strain: ORS1096, features a modification of the amino acid from L to F at position 106.
+The protein's natural variant, known as in strain: ORS1096, features a modification of the amino acid from VR to LL at position 110.
+The protein's natural variant, known as in strain: ORS1096, features a modification of the amino acid from Q to R at position 114.
+The protein's natural variant, known as in strain: ORS1096, features a modification of the amino acid from RD to HF at position 156.
+The protein's natural variant, known as in strain: ORS1096, features a modification of the amino acid from L to V at position 174.
+The protein's natural variant, known as in MTDPS2;, features a modification of the amino acid from I to M at position 53.
+The protein's natural variant, known as in MTDPS2;, features a modification of the amino acid from T to M at position 64.
+The protein's natural variant, known as in MTDPS2; reduction of activity;, features a modification of the amino acid from T to M at position 108.
+The protein's natural variant, known as in MTDPS2; severe form of combined brain and muscular atrophy; depletion of mtDNA in skeletal muscle; normal residual mtDNA in blood and fibroblasts, features a modification of the amino acid from M to V at position 117.
+The protein's natural variant, known as in MTDPS2; reduction of activity in muscles;, features a modification of the amino acid from H to N at position 121.
+The protein's natural variant, known as in MTDPS2; severe form of combined brain and muscular atrophy; depletion of mtDNA in skeletal muscle; normal residual mtDNA in blood and fibroblasts;, features a modification of the amino acid from A to V at position 139.
+The protein's natural variant, known as in MTDPS2 and PEOB3; reduction of activity; reduced affinity for ATP;, features a modification of the amino acid from R to W at position 183.
+The protein's natural variant, known as in PEOB3; reduction of activity; reduced affinity for ATP;, features a modification of the amino acid from T to A at position 188.
+The protein's natural variant, known as in MTDPS2; reduction of activity;, features a modification of the amino acid from R to K at position 192.
+The protein's natural variant, known as in MTDPS2; reduction of activity in muscles;, features a modification of the amino acid from I to N at position 212.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from E to V at position 488.
+The protein's natural variant, known as in bs, features a modification of the amino acid from FRHVV to M at position 235.
+The protein's natural variant, known as in DBA14;, features a modification of the amino acid from E to G at position 64.
+The protein's natural variant, known as in MF4, features a modification of the amino acid from R to L at position 68.
+The protein's natural variant, known as in DHS2;, features a modification of the amino acid from V to E at position 282.
+The protein's natural variant, known as in DHS2;, features a modification of the amino acid from V to M at position 282.
+The protein's natural variant, known as in DHS2; no effect on plasma membrane localization; increases calcium-activated potassium channel activity;, features a modification of the amino acid from R to H at position 352.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from E to K at position 138.
+The protein's natural variant, known as found in a patient with a severe neurological disorder; unknown pathological significance; reduced protein expression due to protein instability; protein misfolding; formation of nuclear puncta in some cells; loss of activation of HSPA1A, HSPA6 and DHRS2, features a modification of the amino acid from M to L at position 280.
+The protein's natural variant, known as found in individuals with plasma alpha(1,3)-fucosyltransferase deficiency and no clinically relevant phenotype; results in partial enzyme inactivation; complete enzyme inactivation when associated with V-244 and G-303;, features a modification of the amino acid from P to S at position 124.
+The protein's natural variant, known as found in individuals with plasma alpha(1,3)-fucosyltransferase deficiency and no clinically relevant phenotype; complete enzyme inactivation when associated with S-124 and G-303, features a modification of the amino acid from L to V at position 244.
+The protein's natural variant, known as found in individuals with plasma alpha(1,3)-fucosyltransferase deficiency and no clinically relevant phenotype; complete enzyme inactivation;, features a modification of the amino acid from E to K at position 247.
+The protein's natural variant, known as found in individuals with plasma alpha(1,3)-fucosyltransferase deficiency and no clinically relevant phenotype; complete enzyme inactivation when associated with S-124 and V-244;, features a modification of the amino acid from R to G at position 303.
+The protein's natural variant, known as in WT6; inhibits transcriptional repression activity, features a modification of the amino acid from R to P at position 160.
+The protein's natural variant, known as in WT6; inhibits transcriptional repression activity, features a modification of the amino acid from N to Y at position 290.
+The protein's natural variant, known as in WT6; inhibits transcriptional repression activity;, features a modification of the amino acid from H to R at position 322.
+The protein's natural variant, known as in WT6, features a modification of the amino acid from H to Q at position 412.
+The protein's natural variant, known as in SWNTS2; unknown pathological significance, features a modification of the amino acid from H to R at position 71.
+The protein's natural variant, known as in GLM; increased Ras signaling, features a modification of the amino acid from W to R at position 105.
+The protein's natural variant, known as in NS10; increased Ras signaling, features a modification of the amino acid from Y to C at position 119.
+The protein's natural variant, known as in NS2; unknown pathological significance; no effect on RAS-MAPK signaling; no effect on stability;, features a modification of the amino acid from H to D at position 121.
+The protein's natural variant, known as in SWNTS2; increased Ras signaling; decreased binding to Ras;, features a modification of the amino acid from S to L at position 122.
+The protein's natural variant, known as in NS10; unknown pathological significance, features a modification of the amino acid from N to S at position 143.
+The protein's natural variant, known as in SWNTS2; increased RAS-MAPK signaling;, features a modification of the amino acid from R to Q at position 170.
+The protein's natural variant, known as in NS2; when associated with T-205;, features a modification of the amino acid from R to W at position 170.
+The protein's natural variant, known as in SWNTS2; decreased binding to Ras, features a modification of the amino acid from L to R at position 187.
+The protein's natural variant, known as in GLM; increased Ras signaling; decreased ubiquitination of Ras, features a modification of the amino acid from R to G at position 198.
+The protein's natural variant, known as in SWNTS2; decreased binding to Ras, features a modification of the amino acid from M to R at position 202.
+The protein's natural variant, known as in NS2; unknown pathological significance; when associated with W-170;, features a modification of the amino acid from I to T at position 205.
+The protein's natural variant, known as in NS2; unknown pathological significance; no effect on RAS-MAPK signaling; decreased stability, features a modification of the amino acid from E to A at position 217.
+The protein's natural variant, known as in NS10; increased RAS-MAPK signaling; decreased stability; no effect on localization to Golgi apparatus;, features a modification of the amino acid from S to N at position 247.
+The protein's natural variant, known as in NS10 and GLM; increased RAS-MAPK signaling; decreased ubiquitination of Ras; decreased stability; no effect on localization to Golgi apparatus;, features a modification of the amino acid from G to R at position 248.
+The protein's natural variant, known as in NS10;, features a modification of the amino acid from R to Q at position 283.
+The protein's natural variant, known as in NS10 and SWNTS2; increased RAS-MAPK signaling; decreased stability; no effect on localization to Golgi apparatus;, features a modification of the amino acid from R to C at position 284.
+The protein's natural variant, known as in SWNTS2; unknown pathological significance; no effect on stability;, features a modification of the amino acid from G to R at position 286.
+The protein's natural variant, known as in NS10; increased Ras signaling, features a modification of the amino acid from H to Y at position 287.
+The protein's natural variant, known as in GLM; increased Ras signaling, features a modification of the amino acid from T to I at position 288.
+The protein's natural variant, known as in NS10; unknown pathological significance, features a modification of the amino acid from R to L at position 294.
+The protein's natural variant, known as in SWNTS2; unknown pathological significance;, features a modification of the amino acid from A to V at position 392.
+The protein's natural variant, known as in SWNTS2; unknown pathological significance; no effect on stability; no effect on localization to Golgi apparatus, features a modification of the amino acid from M to R at position 400.
+The protein's natural variant, known as in SWNTS2; increased Ras signaling; decreased binding to Ras;, features a modification of the amino acid from G to R at position 404.
+The protein's natural variant, known as in SWNTS2; increased Ras signaling; impaired subcellular location, features a modification of the amino acid from V to G at position 456.
+The protein's natural variant, known as in SWNTS2; unknown pathological significance;, features a modification of the amino acid from A to E at position 465.
+The protein's natural variant, known as in SWNTS2; increased Ras signaling; decreased interaction with CUL3; impaired subcellular location; impaired subcellular location;, features a modification of the amino acid from R to Q at position 466.
+The protein's natural variant, known as in SWNTS2; increased Ras signaling; impaired subcellular location;, features a modification of the amino acid from P to L at position 520.
+The protein's natural variant, known as in SWNTS2; unknown pathological significance, features a modification of the amino acid from L to R at position 528.
+The protein's natural variant, known as in SWNTS2; unknown pathological significance; somatic mutation, features a modification of the amino acid from G to C at position 539.
+The protein's natural variant, known as in NS10; unknown pathological significance, features a modification of the amino acid from A to P at position 554.
+The protein's natural variant, known as in NS2; unknown pathological significance; no effect on RAS-MAPK signaling; strongly decreased stability;, features a modification of the amino acid from E to Q at position 563.
+The protein's natural variant, known as has not effect on protein abundance; does not affect localization to Golgi apparatus; does not affect function in regulation of RAS-MAPK signaling, features a modification of the amino acid from R to H at position 619.
+The protein's natural variant, known as in SWNTS2; unknown pathological significance, features a modification of the amino acid from D to G at position 654.
+The protein's natural variant, known as in SWNTS2; unknown pathological significance;, features a modification of the amino acid from D to Y at position 668.
+The protein's natural variant, known as in SWNTS2; increased Ras signaling; decreased interaction with CUL3; impaired subcellular location;, features a modification of the amino acid from R to C at position 688.
+The protein's natural variant, known as in NS2; unknown pathological significance, features a modification of the amino acid from R to G at position 688.
+The protein's natural variant, known as in NS2;, features a modification of the amino acid from R to Q at position 697.
+The protein's natural variant, known as in SWNTS2; unknown pathological significance;, features a modification of the amino acid from R to W at position 697.
+The protein's natural variant, known as in NS2;, features a modification of the amino acid from P to H at position 701.
+The protein's natural variant, known as in NS2; unknown pathological significance;, features a modification of the amino acid from R to Q at position 755.
+The protein's natural variant, known as in SWNTS2; unknown pathological significance;, features a modification of the amino acid from C to R at position 760.
+The protein's natural variant, known as in GLM; increased Ras signaling;, features a modification of the amino acid from R to W at position 810.
+The protein's natural variant, known as in SWNTS2; decreased interaction with CUL3; impaired subcellular location; decreased ubiquitination of Ras;, features a modification of the amino acid from L to P at position 812.
+The protein's natural variant, known as in SWNTS2; increased Ras signaling, features a modification of the amino acid from S to I at position 813.
+The protein's natural variant, known as in NS2; unknown pathological significance; no effect on RAS-MAPK signaling; decreased localization to Golgi apparatus; no effect on stability;, features a modification of the amino acid from I to T at position 821.
+The natural variant of this protein is characterized by an amino acid alteration from P to L at position 84.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from I to V at position 567.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from Y to C at position 571.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from Q to R at position 621.
+The protein's natural variant, known as may decrease risk for coronary artery disease;, features a modification of the amino acid from R to Q at position 239.
+The natural variant of this protein is characterized by an amino acid alteration from R to G at position 607.
+The protein's natural variant, known as in AAT7; unknown pathological significance;, features a modification of the amino acid from V to M at position 1213.
+The protein's natural variant, known as in AAT7; decreases kinase activity;, features a modification of the amino acid from A to S at position 1491.
+The protein's natural variant, known as in an ovarian mucinous carcinoma sample; somatic mutation;, features a modification of the amino acid from P to L at position 1588.
+The protein's natural variant, known as in AAT7; 4-fold reduced affinity for calmodulin; decreased kinase activity compared to wild-type protein, features a modification of the amino acid from A to T at position 1754.
+The protein's natural variant, known as in AAT7; 7-fold reduced affinity for calmodulin; 6-fold decreased Vmax;, features a modification of the amino acid from S to P at position 1759.
+The protein's natural variant, known as in a breast pleomorphic lobular carcinoma sample; somatic mutation, features a modification of the amino acid from D to Y at position 385.
+The protein's natural variant, known as in MRXSHD;, features a modification of the amino acid from R to C at position 330.
+The protein's natural variant, known as in MRXSHD;, features a modification of the amino acid from R to H at position 330.
+The protein's natural variant, known as in MRXSHD; unknown pathological significance;, features a modification of the amino acid from R to Q at position 333.
+The protein's natural variant, known as in MRXSHD;, features a modification of the amino acid from I to T at position 337.
+The protein's natural variant, known as in MRXSHD; unknown pathological significance;, features a modification of the amino acid from R to Q at position 361.
+The protein's natural variant, known as in strain: ATCC 6633, features a modification of the amino acid from F to L at position 6.
+The protein's natural variant, known as in strain: ATCC 6633, features a modification of the amino acid from I to V at position 89.
+The protein's natural variant, known as in strain: ATCC 6633, features a modification of the amino acid from L to V at position 91.
+The protein's natural variant, known as in strain: ATCC 6633, features a modification of the amino acid from M to I at position 125.
+The protein's natural variant, known as in HPABH4D; increased proteolytic degradation; reduced interaction with HNF1B; loss of HNF1B-coactivator activity;, features a modification of the amino acid from T to I at position 79.
+The protein's natural variant, known as in HPABH4D; increased proteolytic degradation; reduced dehydratase activity; no impact on hydroxytetrahydrobiopterin-binding; reduced interaction with HNF1B; partial impact on HNF1B-coactivator activity;, features a modification of the amino acid from C to R at position 82.
+The protein's natural variant, known as in HPABH4D; when associated in cis with 27-E--T-104 del; unknown pathological significance; no impact on HNF1B interaction; no impact on HNF1B-coactivator activity;, features a modification of the amino acid from R to Q at position 88.
+The protein's natural variant, known as in HPABH4D; increased proteolytic degradation; loss of HNF1B interaction; loss of HNF1B-coactivator activity;, features a modification of the amino acid from E to K at position 97.
+The protein's natural variant, known as in acatalasemia; heat-labile, features a modification of the amino acid from A to T at position 327.
+The protein's natural variant, known as in a patient with spondylocostal dysostosis; inactive;, features a modification of the amino acid from L to V at position 125.
+The protein's natural variant, known as in strain: biovar 1, features a modification of the amino acid from P to T at position 301.
+The protein's natural variant, known as in strain: biovar 1, features a modification of the amino acid from R to P at position 362.
+The protein's natural variant, known as in strain: FVB/N, features a modification of the amino acid from V to G at position 145.
+The natural variant of this protein is characterized by an amino acid alteration from E to I at position 24.
+The natural variant of this protein is characterized by an amino acid alteration from N to T at position 31.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 33.
+The natural variant of this protein is characterized by an amino acid alteration from T to V at position 39.
+The protein's natural variant, known as in strain: D(s)/2923, D/IC-CAL8, D', F9334, D-9291, J9336, J9346, J(s)/5942, E/DK-20, F/MRC-301, E/4a, E/12a and E/7a, features a modification of the amino acid from I to T at position 47.
+The protein's natural variant, known as in strain: H/UW-4, features a modification of the amino acid from A to T at position 62.
+The protein's natural variant, known as in strain: C/UW-1, features a modification of the amino acid from L to P at position 90.
+The protein's natural variant, known as in strain: D(s)2923, D/IC-CAL8, D', F9334, D-9291, J9336 and J9346, features a modification of the amino acid from E to K at position 116.
+The protein's natural variant, known as in strain: Da/MT-566, features a modification of the amino acid from H to L at position 119.
+The protein's natural variant, known as in strain: Da/MT-566, features a modification of the amino acid from G to D at position 180.
+The protein's natural variant, known as in strain: J9329 and Ia/9309, features a modification of the amino acid from T to I at position 218.
+The protein's natural variant, known as in strain: B9227, features a modification of the amino acid from S to N at position 222.
+The protein's natural variant, known as in strain: C/UW-1, features a modification of the amino acid from C to R at position 252.
+The protein's natural variant, known as in strain: K/UW-31, features a modification of the amino acid from S to P at position 260.
+The protein's natural variant, known as in strain: I/UW-12, features a modification of the amino acid from S to F at position 261.
+The natural variant of this protein is characterized by an amino acid alteration from A to G at position 31.
+The natural variant of this protein is characterized by an amino acid alteration from A to S at position 31.
+The protein's natural variant, known as in CORD12, STGD4 and MCDR2; affects the interaction with actin;, features a modification of the amino acid from R to C at position 373.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to H at position 114.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from D to N at position 538.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from D to E at position 1216.
+The protein's natural variant, known as in PEBEL2; decreased reaction kinetics for ATP-dependent NAD(P)H-hydrate dehydratase activity; decreased affinity for (6S)-NADHX; changed ATP-dependent NAD(P)H-hydrate dehydratase activity; thermostability assays show that activity is lost at temperatures above 30 degrees Celsius;, features a modification of the amino acid from G to S at position 81.
+The protein's natural variant, known as in PEBEL2; decreased reaction kinetics for ATP-dependent NAD(P)H-hydrate dehydratase activity; decreased affinity for (6S)-NADHX; changed ATP-dependent NAD(P)H-hydrate dehydratase activity; thermostability assays show that activity is lost at temperatures above 30 degrees Celsius;, features a modification of the amino acid from R to C at position 326.
+The protein's natural variant, known as in strain: IFM 50993, features a modification of the amino acid from T to I at position 13.
+The protein's natural variant, known as in strain: IFM 45811, IFM 45812, IFM 45813, IFM 45817, IFM 4935, IFM 4945, IFM 50993, IFM 50994, IFM 51112, IFM 54194, IFM 54195, IFM 54196, RMSCC 1036 / AZ1 and RMSCC 2128 / TX1, features a modification of the amino acid from Y to S at position 26.
+The protein's natural variant, known as in strain: IFM 45811, IFM 45817, IFM 4945 and IFM 50994, features a modification of the amino acid from N to K at position 103.
+The protein's natural variant, known as in strain: IFM 45811, IFM 45817, IFM 4945 and IFM 50994, features a modification of the amino acid from I to T at position 109.
+The natural variant of this protein is characterized by an amino acid alteration from C to G at position 359.
+The protein's natural variant, known as in CTRCT33;, features a modification of the amino acid from D to N at position 348.
+The protein's natural variant, known as in NEDCAM; unknown pathological significance, features a modification of the amino acid from S to P at position 73.
+The protein's natural variant, known as in NEDCAM; unknown pathological significance, features a modification of the amino acid from H to R at position 105.
+The protein's natural variant, known as in NEDCAM; unknown pathological significance;, features a modification of the amino acid from H to R at position 162.
+The protein's natural variant, known as in NEDCAM; unknown pathological significance, features a modification of the amino acid from D to Y at position 210.
+The protein's natural variant, known as in NEDCAM; unknown pathological significance;, features a modification of the amino acid from V to M at position 611.
+The protein's natural variant, known as in NEDCAM; unknown pathological significance, features a modification of the amino acid from D to E at position 704.
+The protein's natural variant, known as in NEDCAM; impaired function in spliceosomal snRNP assembly; decreased protein abundance; decreased protein stability; decreased interaction with DDX20; decreased interaction with GEMIN4, features a modification of the amino acid from H to R at position 913.
+The protein's natural variant, known as in NEDCAM; unknown pathological significance, features a modification of the amino acid from H to P at position 923.
+The protein's natural variant, known as in NEDCAM; unknown pathological significance, features a modification of the amino acid from L to F at position 925.
+The protein's natural variant, known as in NEDCAM; unknown pathological significance, features a modification of the amino acid from Y to H at position 958.
+The protein's natural variant, known as in NEDCAM;, features a modification of the amino acid from I to F at position 988.
+The protein's natural variant, known as in NEDCAM; unknown pathological significance, features a modification of the amino acid from S to P at position 1000.
+The protein's natural variant, known as in NEDCAM; unknown pathological significance, features a modification of the amino acid from A to T at position 1007.
+The protein's natural variant, known as in NEDCAM; unknown pathological significance, features a modification of the amino acid from D to E at position 1019.
+The protein's natural variant, known as in NEDCAM; impaired function in spliceosomal snRNP assembly; decreased protein abundance; decreased protein stability; decreased interaction with DDX20; decreased interaction with GEMIN4, features a modification of the amino acid from L to P at position 1068.
+The protein's natural variant, known as in NEDCAM; unknown pathological significance, features a modification of the amino acid from L to S at position 1119.
+The protein's natural variant, known as in NEDCAM; unknown pathological significance;, features a modification of the amino acid from Y to H at position 1282.
+The protein's natural variant, known as in NEDCAM, features a modification of the amino acid from Y to C at position 1286.
+The protein's natural variant, known as in NEDCAM, features a modification of the amino acid from Y to N at position 1286.
+The protein's natural variant, known as in NEDCAM; unknown pathological significance, features a modification of the amino acid from H to P at position 1364.
+The protein's natural variant, known as in NEDCAM; unknown pathological significance;, features a modification of the amino acid from L to P at position 1367.
+The natural variant of this protein is characterized by an amino acid alteration from N to T at position 687.
+The natural variant of this protein is characterized by an amino acid alteration from K to N at position 695.
+The natural variant of this protein is characterized by an amino acid alteration from R to K at position 794.
+The natural variant of this protein is characterized by an amino acid alteration from P to T at position 839.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from D to H at position 437.
+The natural variant of this protein is characterized by an amino acid alteration from K to E at position 124.
+The natural variant of this protein is characterized by an amino acid alteration from M to V at position 201.
+The natural variant of this protein is characterized by an amino acid alteration from SG to NR at position 597.
+The protein's natural variant, known as in SSMED; impairs the protein function in DNA double-strand break repair;, features a modification of the amino acid from W to R at position 43.
+The protein's natural variant, known as in SSMED; impaired ability to repair DNA double-strand breaks, features a modification of the amino acid from D to E at position 82.
+The protein's natural variant, known as in SSMED; no expression of the protein is observed; complete loss of function in DNA double-strand break repair;, features a modification of the amino acid from R to Q at position 161.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from T to S at position 634.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from E to K at position 889.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from S to C at position 997.
+The protein's natural variant, known as in ATS1; adult type;, features a modification of the amino acid from G to D at position 54.
+The protein's natural variant, known as in ATS1, features a modification of the amino acid from G to S at position 114.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to E at position 123.
+The protein's natural variant, known as in ATS1; juvenile type;, features a modification of the amino acid from G to E at position 129.
+The protein's natural variant, known as in ATS1; juvenile type;, features a modification of the amino acid from G to V at position 129.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to R at position 174.
+The protein's natural variant, known as in ATS1; presenting with dot-and-fleck retinopathy;, features a modification of the amino acid from G to C at position 177.
+The protein's natural variant, known as in ATS1; adult type;, features a modification of the amino acid from G to R at position 177.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to R at position 192.
+The protein's natural variant, known as in ATS1; juvenile type;, features a modification of the amino acid from G to V at position 204.
+The protein's natural variant, known as in ATS1; juvenile type;, features a modification of the amino acid from G to R at position 216.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to S at position 219.
+The protein's natural variant, known as in ATS1; juvenile type;, features a modification of the amino acid from G to R at position 230.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to E at position 239.
+The protein's natural variant, known as in ATS1; adult type;, features a modification of the amino acid from G to R at position 264.
+The protein's natural variant, known as in ATS1; juvenile type;, features a modification of the amino acid from G to V at position 289.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to R at position 292.
+The protein's natural variant, known as in ATS1; juvenile type;, features a modification of the amino acid from G to V at position 292.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to D at position 295.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to S at position 298.
+The protein's natural variant, known as in ATS1; juvenile type;, features a modification of the amino acid from G to R at position 319.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to E at position 325.
+The protein's natural variant, known as in ATS1; juvenile and adult types;, features a modification of the amino acid from G to R at position 325.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to V at position 331.
+The protein's natural variant, known as in ATS1; juvenile type;, features a modification of the amino acid from G to E at position 365.
+The protein's natural variant, known as in ATS1; juvenile type;, features a modification of the amino acid from G to E at position 371.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to A at position 374.
+The protein's natural variant, known as in ATS1; juvenile type;, features a modification of the amino acid from G to D at position 383.
+The protein's natural variant, known as in ATS1; adult type;, features a modification of the amino acid from G to E at position 400.
+The protein's natural variant, known as in ATS1; adult type;, features a modification of the amino acid from G to V at position 406.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to D at position 409.
+The protein's natural variant, known as in ATS1; adult type;, features a modification of the amino acid from G to V at position 412.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to R at position 415.
+The protein's natural variant, known as in ATS1; juvenile type;, features a modification of the amino acid from G to E at position 420.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to V at position 420.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to E at position 423.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to E at position 466.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to R at position 472.
+The protein's natural variant, known as in ATS1; juvenile type;, features a modification of the amino acid from G to E at position 491.
+The protein's natural variant, known as in ATS1; adult type;, features a modification of the amino acid from G to D at position 494.
+The protein's natural variant, known as in ATS1; adult type;, features a modification of the amino acid from G to C at position 497.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to C at position 521.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to S at position 521.
+The protein's natural variant, known as in ATS1; adult type;, features a modification of the amino acid from G to D at position 524.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to R at position 545.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to V at position 545.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to R at position 558.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to R at position 561.
+The protein's natural variant, known as in ATS1; juvenile type;, features a modification of the amino acid from G to A at position 567.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to D at position 573.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to E at position 579.
+The protein's natural variant, known as in ATS1; adult type;, features a modification of the amino acid from G to R at position 579.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to V at position 603.
+The protein's natural variant, known as in ATS1; juvenile type;, features a modification of the amino acid from G to R at position 609.
+The protein's natural variant, known as in ATS1; juvenile type;, features a modification of the amino acid from G to V at position 609.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to C at position 621.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to D at position 624.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to D at position 629.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to D at position 632.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from E to K at position 633.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to D at position 635.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to A at position 638.
+The protein's natural variant, known as in ATS1; juvenile type;, features a modification of the amino acid from G to S at position 638.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to V at position 638.
+The protein's natural variant, known as in ATS1; juvenile type;, features a modification of the amino acid from G to R at position 653.
+The protein's natural variant, known as in ATS1; juvenile type;, features a modification of the amino acid from G to A at position 669.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to D at position 681.
+The protein's natural variant, known as in ATS1; adult type;, features a modification of the amino acid from G to V at position 684.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to E at position 687.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to E at position 722.
+The protein's natural variant, known as in ATS1; juvenile type;, features a modification of the amino acid from P to S at position 739.
+The protein's natural variant, known as in ATS1; juvenile type;, features a modification of the amino acid from G to E at position 740.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to D at position 743.
+The protein's natural variant, known as in ATS1; juvenile type;, features a modification of the amino acid from G to D at position 772.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to R at position 796.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to R at position 802.
+The protein's natural variant, known as in ATS1; adult type;, features a modification of the amino acid from G to E at position 808.
+The protein's natural variant, known as in ATS1; juvenile type;, features a modification of the amino acid from G to V at position 811.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to R at position 822.
+The protein's natural variant, known as in ATS1; juvenile type;, features a modification of the amino acid from G to E at position 852.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to R at position 852.
+The protein's natural variant, known as in ATS1; adult type;, features a modification of the amino acid from G to E at position 866.
+The protein's natural variant, known as in ATS1; juvenile type;, features a modification of the amino acid from G to R at position 869.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to R at position 872.
+The protein's natural variant, known as in ATS1, features a modification of the amino acid from G to R at position 878.
+The protein's natural variant, known as in ATS1; mild phenotype;, features a modification of the amino acid from M to V at position 898.
+The protein's natural variant, known as in ATS1; juvenile type;, features a modification of the amino acid from G to V at position 902.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to E at position 911.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to C at position 941.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to D at position 947.
+The protein's natural variant, known as in ATS1; found on the same allele as variant Glu-1211;, features a modification of the amino acid from G to V at position 953.
+The protein's natural variant, known as in ATS1, features a modification of the amino acid from G to A at position 1006.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to V at position 1006.
+The protein's natural variant, known as in ATS1, features a modification of the amino acid from G to E at position 1015.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to V at position 1015.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to S at position 1030.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to V at position 1036.
+The protein's natural variant, known as in ATS1; juvenile type;, features a modification of the amino acid from G to S at position 1039.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to E at position 1045.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to R at position 1066.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to S at position 1066.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to D at position 1086.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to V at position 1104.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to R at position 1107.
+The protein's natural variant, known as in ATS1; juvenile type;, features a modification of the amino acid from G to D at position 1143.
+The protein's natural variant, known as in ATS1; adult type;, features a modification of the amino acid from G to S at position 1143.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to R at position 1158.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to R at position 1161.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to S at position 1167.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to S at position 1170.
+The protein's natural variant, known as in ATS1; juvenile type;, features a modification of the amino acid from G to R at position 1182.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to R at position 1196.
+The protein's natural variant, known as in ATS1; juvenile type;, features a modification of the amino acid from G to C at position 1205.
+The protein's natural variant, known as in ATS1; found on the same allele as variant Val-953;, features a modification of the amino acid from G to E at position 1211.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to R at position 1211.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to D at position 1220.
+The protein's natural variant, known as in ATS1; adult type;, features a modification of the amino acid from G to D at position 1229.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to C at position 1241.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to D at position 1244.
+The protein's natural variant, known as in ATS1; adult type;, features a modification of the amino acid from G to S at position 1252.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to E at position 1261.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to S at position 1270.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to S at position 1333.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to S at position 1357.
+The protein's natural variant, known as in ATS1; adult type;, features a modification of the amino acid from G to V at position 1379.
+The protein's natural variant, known as in ATS1; adult and juvenile types;, features a modification of the amino acid from R to C at position 1410.
+The protein's natural variant, known as in ATS1; adult type;, features a modification of the amino acid from G to W at position 1421.
+The protein's natural variant, known as in ATS1; juvenile type;, features a modification of the amino acid from R to C at position 1422.
+The protein's natural variant, known as in ATS1; adult type;, features a modification of the amino acid from G to V at position 1427.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to D at position 1442.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to S at position 1451.
+The protein's natural variant, known as in ATS1; adult type;, features a modification of the amino acid from G to A at position 1486.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from S to F at position 1488.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from A to D at position 1498.
+The protein's natural variant, known as in ATS1; juvenile type; unknown pathological significance;, features a modification of the amino acid from R to H at position 1511.
+The protein's natural variant, known as in ATS1; juvenile type;, features a modification of the amino acid from P to T at position 1517.
+The protein's natural variant, known as in ATS1; adult type;, features a modification of the amino acid from W to S at position 1538.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from R to Q at position 1563.
+The protein's natural variant, known as in ATS1; adult type;, features a modification of the amino acid from C to S at position 1564.
+The protein's natural variant, known as in ATS1; juvenile type;, features a modification of the amino acid from C to R at position 1567.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from G to D at position 1596.
+The protein's natural variant, known as in ATS1; adult type;, features a modification of the amino acid from L to R at position 1649.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from R to P at position 1677.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from R to Q at position 1677.
+The protein's natural variant, known as in ATS1;, features a modification of the amino acid from C to W at position 1678.
+The protein's natural variant, known as in IMMAS; unknown pathological significance, features a modification of the amino acid from R to Q at position 535.
+The protein's natural variant, known as in IMMAS;, features a modification of the amino acid from Q to H at position 599.
+The protein's natural variant, known as in IMMAS;, features a modification of the amino acid from F to L at position 603.
+The protein's natural variant, known as in IMMAS; decreased trimethylation of 'Lys-27' of histone H3; no effect on interaction with EZH2;, features a modification of the amino acid from E to V at position 610.
+The protein's natural variant, known as in SRTD7;, features a modification of the amino acid from W to R at position 261.
+The protein's natural variant, known as in SRTD7 and SRTD7/20; the SRTD7/20 patient also carries variant INTU 276-Q--L-942 del; chondrocyte cell lines from a patient show a reduction of cilia indicating a defect in ciliogenesis;, features a modification of the amino acid from W to L at position 311.
+The protein's natural variant, known as in SRTD7; chondrocyte cell lines from the patient show a reduction of cilia indicating a defect in ciliogenesis;, features a modification of the amino acid from R to K at position 478.
+The protein's natural variant, known as in CED2;, features a modification of the amino acid from E to G at position 626.
+The protein's natural variant, known as in CED2;, features a modification of the amino acid from A to T at position 875.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 333.
+The protein's natural variant, known as found in a patient with neural tube defects; unknown pathological significance, features a modification of the amino acid from Q to H at position 139.
+The protein's natural variant, known as in OTFCS2; significantly reduced transactivation of the regulatory sequence of NKX3-2 in cells over-expressing the mutant sequence compared to cells over-expressing wild-type sequence;, features a modification of the amino acid from G to V at position 166.
+The protein's natural variant, known as in strain: CU741, features a modification of the amino acid from H to Q at position 3.
+The protein's natural variant, known as in GM2G1; late infantile, features a modification of the amino acid from P to S at position 25.
+The protein's natural variant, known as in GM2G1; infantile;, features a modification of the amino acid from L to R at position 39.
+The protein's natural variant, known as in GM2G1; unknown pathological significance;, features a modification of the amino acid from E to K at position 114.
+The protein's natural variant, known as in GM2G1, features a modification of the amino acid from L to F at position 127.
+The protein's natural variant, known as in GM2G1; infantile;, features a modification of the amino acid from L to R at position 127.
+The protein's natural variant, known as in GM2G1; late infantile, features a modification of the amino acid from R to G at position 166.
+The protein's natural variant, known as in GM2G1; infantile; inactive or unstable protein;, features a modification of the amino acid from R to Q at position 170.
+The protein's natural variant, known as in GM2G1; infantile;, features a modification of the amino acid from R to W at position 170.
+The protein's natural variant, known as in GM2G1; infantile; inactive protein;, features a modification of the amino acid from R to C at position 178.
+The protein's natural variant, known as in GM2G1; infantile; inactive protein;, features a modification of the amino acid from R to H at position 178.
+The protein's natural variant, known as in GM2G1; infantile;, features a modification of the amino acid from R to L at position 178.
+The protein's natural variant, known as in GM2G1;, features a modification of the amino acid from Y to H at position 180.
+The protein's natural variant, known as in GM2G1; infantile;, features a modification of the amino acid from V to L at position 192.
+The protein's natural variant, known as in GM2G1;, features a modification of the amino acid from N to S at position 196.
+The protein's natural variant, known as in GM2G1;, features a modification of the amino acid from K to T at position 197.
+The protein's natural variant, known as in GM2G1;, features a modification of the amino acid from V to M at position 200.
+The protein's natural variant, known as in GM2G1; infantile;, features a modification of the amino acid from H to R at position 204.
+The protein's natural variant, known as in GM2G1; infantile;, features a modification of the amino acid from S to F at position 210.
+The protein's natural variant, known as in GM2G1; infantile;, features a modification of the amino acid from F to S at position 211.
+The protein's natural variant, known as in GM2G1;, features a modification of the amino acid from S to F at position 226.
+The protein's natural variant, known as in HEXA pseudodeficiency;, features a modification of the amino acid from R to W at position 247.
+The protein's natural variant, known as in HEXA pseudodeficiency;, features a modification of the amino acid from R to W at position 249.
+The protein's natural variant, known as in GM2G1; juvenile;, features a modification of the amino acid from G to D at position 250.
+The protein's natural variant, known as in GM2G1;, features a modification of the amino acid from G to S at position 250.
+The protein's natural variant, known as in GM2G1;, features a modification of the amino acid from R to H at position 252.
+The protein's natural variant, known as in GM2G1, features a modification of the amino acid from R to L at position 252.
+The protein's natural variant, known as in GM2G1; infantile;, features a modification of the amino acid from D to H at position 258.
+The protein's natural variant, known as in GM2G1;, features a modification of the amino acid from G to D at position 269.
+The protein's natural variant, known as in GM2G1; late onset; inhibited subunit dissociation; loss of processing to a mature form; increased degradation;, features a modification of the amino acid from G to S at position 269.
+The protein's natural variant, known as in GM2G1; late infantile, features a modification of the amino acid from S to P at position 279.
+The protein's natural variant, known as in GM2G1;, features a modification of the amino acid from N to S at position 295.
+The protein's natural variant, known as in GM2G1; infantile;, features a modification of the amino acid from M to R at position 301.
+The protein's natural variant, known as in GM2G1;, features a modification of the amino acid from D to V at position 314.
+The protein's natural variant, known as in GM2G1;, features a modification of the amino acid from D to N at position 322.
+The protein's natural variant, known as in GM2G1;, features a modification of the amino acid from D to Y at position 322.
+The protein's natural variant, known as in GM2G1;, features a modification of the amino acid from I to F at position 335.
+The protein's natural variant, known as in GM2G1; mild; associated with spinal muscular atrophy, features a modification of the amino acid from V to M at position 391.
+The protein's natural variant, known as in GM2G1;, features a modification of the amino acid from R to P at position 393.
+The protein's natural variant, known as in GM2G1; infantile; inactive protein;, features a modification of the amino acid from W to C at position 420.
+The protein's natural variant, known as in GM2G1; infantile;, features a modification of the amino acid from G to S at position 454.
+The protein's natural variant, known as in GM2G1; late infantile, features a modification of the amino acid from G to R at position 455.
+The protein's natural variant, known as in GM2G1; infantile, features a modification of the amino acid from C to Y at position 458.
+The protein's natural variant, known as in GM2G1;, features a modification of the amino acid from E to V at position 462.
+The protein's natural variant, known as in GM2G1; subacute;, features a modification of the amino acid from W to C at position 474.
+The protein's natural variant, known as in GM2G1;, features a modification of the amino acid from G to R at position 478.
+The protein's natural variant, known as in GM2G1; infantile; loss of processing to a mature form; increased degradation;, features a modification of the amino acid from E to K at position 482.
+The protein's natural variant, known as in GM2G1; infantile, features a modification of the amino acid from L to Q at position 484.
+The protein's natural variant, known as in GM2G1; infantile;, features a modification of the amino acid from W to R at position 485.
+The protein's natural variant, known as in GM2G1; infantile;, features a modification of the amino acid from R to C at position 499.
+The protein's natural variant, known as in GM2G1; juvenile;, features a modification of the amino acid from R to H at position 499.
+The protein's natural variant, known as in GM2G1; infantile;, features a modification of the amino acid from R to C at position 504.
+The protein's natural variant, known as in GM2G1; juvenile; fails to associate with the beta-subunit to form the enzymatically active heterodimer;, features a modification of the amino acid from R to H at position 504.
+The protein's natural variant, known as found in a patient with Leber congenital amaurosis;, features a modification of the amino acid from F to V at position 214.
+The protein's natural variant, known as in a renal clear cell carcinoma sample; somatic mutation, features a modification of the amino acid from A to G at position 446.
+The protein's natural variant, known as in RP38;, features a modification of the amino acid from E to K at position 540.
+The protein's natural variant, known as in RP38, features a modification of the amino acid from S to C at position 661.
+The protein's natural variant, known as in a head & Neck squamous cell carcinoma sample; somatic mutation, features a modification of the amino acid from A to S at position 708.
+The protein's natural variant, known as in RP38;, features a modification of the amino acid from I to T at position 871.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 871.
+The protein's natural variant, known as found in a patient with Leber congenital amaurosis;, features a modification of the amino acid from P to L at position 958.
+The protein's natural variant, known as confers resistance to cycloheximide, an inhibitor of polypeptide elongation, features a modification of the amino acid from P to L at position 54.
+The protein's natural variant, known as confers resistance to cycloheximide, an inhibitor of polypeptide elongation, features a modification of the amino acid from P to S at position 54.
+The protein's natural variant, known as in CMT2P; abolishes interaction with FUS;, features a modification of the amino acid from C to R at position 694.
+The protein's natural variant, known as in CMT2P; unknown pathological significance;, features a modification of the amino acid from C to Y at position 694.
+The protein's natural variant, known as in PEOA3;, features a modification of the amino acid from R to Q at position 303.
+The protein's natural variant, known as in PEOA3; also detected in a case showing digenic inheritance;, features a modification of the amino acid from R to W at position 303.
+The protein's natural variant, known as in PEOA3; reduced single-strand DNA binding; increased heptamer oligomerization;, features a modification of the amino acid from W to L at position 315.
+The protein's natural variant, known as in PEOA3; reduces helicase activity; reduced single-strand DNA binding, features a modification of the amino acid from W to S at position 315.
+The protein's natural variant, known as in MTDPS7;, features a modification of the amino acid from A to T at position 318.
+The protein's natural variant, known as in PEOA3; the phenotype highly overlaps with sensory ataxic neuropathy dysarthria and ophthalmoparesis; reduces helicase activity and single-strand DNA binding;, features a modification of the amino acid from K to E at position 319.
+The protein's natural variant, known as in PEOA3, features a modification of the amino acid from K to T at position 319.
+The protein's natural variant, known as in PEOA3, features a modification of the amino acid from R to P at position 334.
+The protein's natural variant, known as in PEO; sporadic case; the patient also carries the S-848 mutation in the POLG gene suggesting digenic inheritance; retains hexamer and heptamer formation;, features a modification of the amino acid from R to Q at position 334.
+The protein's natural variant, known as in PEOA3; displays unusual oligomeric forms, features a modification of the amino acid from P to L at position 335.
+The protein's natural variant, known as in PEOA3;, features a modification of the amino acid from R to P at position 354.
+The protein's natural variant, known as in PEOA3;, features a modification of the amino acid from R to P at position 357.
+The protein's natural variant, known as in PEOA3; reduces helicase activity;, features a modification of the amino acid from A to T at position 359.
+The protein's natural variant, known as in MTDPS7; patients manifest multi-organ failure; requires 2 nucleotide substitutions, features a modification of the amino acid from L to G at position 360.
+The protein's natural variant, known as in PEOA3;, features a modification of the amino acid from A to P at position 362.
+The protein's natural variant, known as in PEOA3, features a modification of the amino acid from W to L at position 363.
+The protein's natural variant, known as in PEOA3, features a modification of the amino acid from I to T at position 367.
+The protein's natural variant, known as in PEOA3; reduces helicase activity; increases single strand DNA affinity; reduces closed-ring quaternary structure formation, features a modification of the amino acid from S to P at position 369.
+The protein's natural variant, known as in PEOA3;, features a modification of the amino acid from S to Y at position 369.
+The protein's natural variant, known as in PEOA3, features a modification of the amino acid from F to C at position 370.
+The protein's natural variant, known as in PEOA3;, features a modification of the amino acid from F to L at position 370.
+The protein's natural variant, known as in PEOA3; reduces helicase activity and alters nucleoid structure;, features a modification of the amino acid from R to Q at position 374.
+The protein's natural variant, known as in PEOA3; reduces closed-ring quaternary structure formation;, features a modification of the amino acid from L to P at position 381.
+The protein's natural variant, known as in PRLTS5;, features a modification of the amino acid from R to H at position 391.
+The protein's natural variant, known as in PEOA3, features a modification of the amino acid from S to N at position 426.
+The protein's natural variant, known as in PRLTS5;, features a modification of the amino acid from W to G at position 441.
+The protein's natural variant, known as in MTDPS7; infantile spinocerebellar ataxia phenotype;, features a modification of the amino acid from L to V at position 456.
+The protein's natural variant, known as in MTDPS7; affects helicase activity;, features a modification of the amino acid from T to I at position 457.
+The protein's natural variant, known as in PEOA3;, features a modification of the amino acid from Q to H at position 458.
+The protein's natural variant, known as in PEOA3, features a modification of the amino acid from A to P at position 460.
+The protein's natural variant, known as in PEOA3; reduces helicase activity and alters nucleoid structure;, features a modification of the amino acid from W to C at position 474.
+The protein's natural variant, known as in PEOA3;, features a modification of the amino acid from W to S at position 474.
+The protein's natural variant, known as in PEOA3, features a modification of the amino acid from A to D at position 475.
+The protein's natural variant, known as in PEOA3;, features a modification of the amino acid from A to P at position 475.
+The protein's natural variant, known as in PEOA3, features a modification of the amino acid from F to I at position 478.
+The protein's natural variant, known as in PEOA3;, features a modification of the amino acid from E to K at position 479.
+The protein's natural variant, known as in PRLTS5;, features a modification of the amino acid from V to I at position 507.
+The protein's natural variant, known as in MTDPS7;, features a modification of the amino acid from Y to C at position 508.
+The protein's natural variant, known as in PRLTS5;, features a modification of the amino acid from N to S at position 585.
+The protein's natural variant, known as found in a patient with LCA3;, features a modification of the amino acid from I to T at position 332.
+The protein's natural variant, known as in 30% of the molecules, features a modification of the amino acid from V to I at position 120.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from S to I at position 62.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from N to I at position 283.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from L to V at position 385.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from D to G at position 655.
+The protein's natural variant, known as in 5-1, features a modification of the amino acid from E to D at position 76.
+The protein's natural variant, known as in 5-1, features a modification of the amino acid from F to S at position 103.
+The protein's natural variant, known as in 5-1, features a modification of the amino acid from A to S at position 195.
+The protein's natural variant, known as in strain: Berkeley and Oregon-R, features a modification of the amino acid from S to T at position 392.
+The protein's natural variant, known as in strain: Berkeley and Oregon-R, features a modification of the amino acid from R to K at position 427.
+The protein's natural variant, known as in strain: Berkeley and Oregon-R, features a modification of the amino acid from A to T at position 428.
+The protein's natural variant, known as in strain: Canton-S, features a modification of the amino acid from L to P at position 927.
+The natural variant of this protein is characterized by an amino acid alteration from L to S at position 108.
+The protein's natural variant, known as in INSDM; may prevent phosphorylation at S-65; may enhance protein stability;, features a modification of the amino acid from S to F at position 64.
+The protein's natural variant, known as in CILD16; reduced tethering interaction between DNAH5 and tubulin;, features a modification of the amino acid from N to S at position 150.
+The protein's natural variant, known as in HYPT12; autosomal dominant;, features a modification of the amino acid from R to Q at position 32.
+The protein's natural variant, known as found in a patient with isolated erythrocytosis; unknown pathological significance, features a modification of the amino acid from A to V at position 215.
+The protein's natural variant, known as associated with susceptibility to CELIAC13 and T1D;, features a modification of the amino acid from W to R at position 262.
+The protein's natural variant, known as in strain: CB4854, features a modification of the amino acid from F to L at position 94.
+The protein's natural variant, known as in strain: AP1, features a modification of the amino acid from V to A at position 77.
+The protein's natural variant, known as in CTRCT4; progressive punctate cataract with early onset; causes disulfide-linked oligomers formation with consequent protein aggregation and precipitation;, features a modification of the amino acid from R to C at position 15.
+The protein's natural variant, known as in CTRCT4; reduces solubility;, features a modification of the amino acid from P to S at position 24.
+The protein's natural variant, known as in CTRCT4; unknown pathological significance; reduces solubility;, features a modification of the amino acid from P to T at position 24.
+The protein's natural variant, known as in CTRCT4; unknown pathological significance, features a modification of the amino acid from A to P at position 36.
+The protein's natural variant, known as in CTRCT4; very low solubility; crystallizes spontaneously;, features a modification of the amino acid from R to S at position 37.
+The protein's natural variant, known as in CTRCT4; much less stable than the wild-type protein; more prone to aggregate when subjected to environmental stresses such as heat and UV irradiation, features a modification of the amino acid from W to R at position 43.
+The protein's natural variant, known as in CTRCT4; unknown pathological significance;, features a modification of the amino acid from L to P at position 45.
+The protein's natural variant, known as in CTRCT4; lowered solubility; crystallizes easily;, features a modification of the amino acid from R to H at position 59.
+The natural variant of this protein is characterized by an amino acid alteration from M to V at position 102.
+The protein's natural variant, known as in CTRCT4, features a modification of the amino acid from E to A at position 107.
+The protein's natural variant, known as in strain: C57BL/6 XSJL, features a modification of the amino acid from A to V at position 9.
+The protein's natural variant, known as in strain: C57BL/6 XSJL, features a modification of the amino acid from M to V at position 351.
+The protein's natural variant, known as in strain: C57BL/6 XSJL, features a modification of the amino acid from T to I at position 361.
+The protein's natural variant, known as in strain: cv. Ka-0, cv. Lip-0, cv. No-0, cv. Sei-0, cv. Tsu-0 and cv. Wl-0, features a modification of the amino acid from A to V at position 67.
+The protein's natural variant, known as in strain: cv. Ka-0, cv. Lip-0, cv. No-0, cv. Sei-0, cv. Tsu-0 and cv. Wl-0, features a modification of the amino acid from L to I at position 75.
+The protein's natural variant, known as in strain: cv. Ka-0, cv. Lip-0, cv. No-0, cv. Sei-0, cv. Tsu-0 and cv. Wl-0, features a modification of the amino acid from R to H at position 86.
+The protein's natural variant, known as in strain: cv. Sorbo, features a modification of the amino acid from L to Q at position 109.
+The protein's natural variant, known as in strain: cv. Bl-0, cv. Ka-0, cv. Lip-0, cv. No-0, cv. Sei-0, cv. Sorbo, cv. Tsu-0 and cv. Wl-0, features a modification of the amino acid from D to G at position 252.
+The protein's natural variant, known as in strain: cv. Ka-0, cv. Lip-0, cv. No-0, cv. Sei-0, cv. Tsu-0 and cv. Wl-0, features a modification of the amino acid from A to V at position 450.
+The protein's natural variant, known as in strain: cv. Ka-0, cv. Lip-0, cv. No-0, cv. Sei-0, cv. Tsu-0 and cv. Wl-0, features a modification of the amino acid from M to L at position 470.
+The protein's natural variant, known as in strain: cv. Ka-0, cv. Lip-0, cv. No-0, cv. Sei-0, cv. Tsu-0 and cv. Wl-0, features a modification of the amino acid from G to E at position 479.
+The protein's natural variant, known as in strain: cv. Ka-0, cv. Lip-0, cv. No-0, cv. Sei-0, cv. Tsu-0 and cv. Wl-0, features a modification of the amino acid from S to L at position 485.
+The natural variant of this protein is characterized by an amino acid alteration from V to A at position 145.
+The natural variant of this protein is characterized by an amino acid alteration from A to T at position 172.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from E to D at position 507.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from L to F at position 692.
+The protein's natural variant, known as in NPHS22; loss of promotion of filipodia and podosome formation and migration, features a modification of the amino acid from C to Y at position 143.
+The protein's natural variant, known as in hypothyroidism, features a modification of the amino acid from P to L at position 556.
+The protein's natural variant, known as in OTCD;, features a modification of the amino acid from R to Q at position 26.
+The protein's natural variant, known as in OTCD; late onset;, features a modification of the amino acid from G to C at position 39.
+The protein's natural variant, known as in OTCD; late onset;, features a modification of the amino acid from R to C at position 40.
+The protein's natural variant, known as in OTCD; late onset;, features a modification of the amino acid from R to H at position 40.
+The protein's natural variant, known as in OTCD;, features a modification of the amino acid from T to I at position 44.
+The protein's natural variant, known as in OTCD;, features a modification of the amino acid from L to P at position 45.
+The protein's natural variant, known as in OTCD;, features a modification of the amino acid from L to V at position 45.
+The protein's natural variant, known as in OTCD; neonatal;, features a modification of the amino acid from N to I at position 47.
+The protein's natural variant, known as in OTCD; late onset;, features a modification of the amino acid from G to R at position 50.
+The protein's natural variant, known as in OTCD; late onset;, features a modification of the amino acid from Y to D at position 55.
+The protein's natural variant, known as in OTCD; late onset;, features a modification of the amino acid from M to T at position 56.
+The protein's natural variant, known as in OTCD;, features a modification of the amino acid from S to L at position 60.
+The protein's natural variant, known as in OTCD; late onset;, features a modification of the amino acid from L to P at position 63.
+The protein's natural variant, known as in OTCD;, features a modification of the amino acid from G to E at position 79.
+The protein's natural variant, known as in OTCD;, features a modification of the amino acid from G to D at position 83.
+The protein's natural variant, known as in OTCD; neonatal;, features a modification of the amino acid from G to R at position 83.
+The protein's natural variant, known as in OTCD;, features a modification of the amino acid from E to K at position 87.
+The protein's natural variant, known as in OTCD; late onset;, features a modification of the amino acid from K to N at position 88.
+The protein's natural variant, known as in OTCD;, features a modification of the amino acid from S to R at position 90.
+The protein's natural variant, known as in OTCD;, features a modification of the amino acid from R to Q at position 92.
+The protein's natural variant, known as in OTCD; late onset;, features a modification of the amino acid from T to A at position 93.
+The protein's natural variant, known as in OTCD;, features a modification of the amino acid from R to T at position 94.
+The protein's natural variant, known as in OTCD; late onset;, features a modification of the amino acid from G to D at position 100.
+The protein's natural variant, known as in OTCD;, features a modification of the amino acid from A to E at position 102.
+The protein's natural variant, known as in OTCD;, features a modification of the amino acid from H to L at position 117.
+The protein's natural variant, known as in OTCD; late onset;, features a modification of the amino acid from H to R at position 117.
+The protein's natural variant, known as in OTCD; neonatal;, features a modification of the amino acid from T to M at position 125.
+The protein's natural variant, known as in OTCD; early onset; loss of ornithine carbamoyltransferase activity; 0.9% of wild-type activity;, features a modification of the amino acid from D to G at position 126.
+The protein's natural variant, known as in OTCD; early onset; decreased ornithine carbamoyltransferase activity; 2.1% of wild-type activity;, features a modification of the amino acid from R to H at position 129.
+The protein's natural variant, known as in OTCD;, features a modification of the amino acid from L to S at position 139.
+The protein's natural variant, known as in OTCD; late onset;, features a modification of the amino acid from A to P at position 140.
+The protein's natural variant, known as in OTCD;, features a modification of the amino acid from R to P at position 141.
+The protein's natural variant, known as in OTCD; most common variant; loss of ornithine carbamoyltransferase activity; activity is 100-fold lower;, features a modification of the amino acid from R to Q at position 141.
+The protein's natural variant, known as in OTCD;, features a modification of the amino acid from L to F at position 148.
+The protein's natural variant, known as in OTCD;, features a modification of the amino acid from I to T at position 159.
+The protein's natural variant, known as in OTCD;, features a modification of the amino acid from I to S at position 160.
+The protein's natural variant, known as in OTCD;, features a modification of the amino acid from N to S at position 161.
+The protein's natural variant, known as in OTCD;, features a modification of the amino acid from G to R at position 162.
+The protein's natural variant, known as in OTCD; late onset;, features a modification of the amino acid from H to Q at position 168.
+The protein's natural variant, known as in OTCD; late onset;, features a modification of the amino acid from H to R at position 168.
+The protein's natural variant, known as in OTCD;, features a modification of the amino acid from I to F at position 172.
+The protein's natural variant, known as in OTCD; early onset; loss of ornithine carbamoyltransferase activity;, features a modification of the amino acid from I to M at position 172.
+The protein's natural variant, known as in OTCD;, features a modification of the amino acid from A to P at position 174.
+The protein's natural variant, known as in OTCD;, features a modification of the amino acid from D to V at position 175.
+The protein's natural variant, known as in OTCD; late onset;, features a modification of the amino acid from Y to C at position 176.
+The protein's natural variant, known as in OTCD; neonatal;, features a modification of the amino acid from T to M at position 178.
+The protein's natural variant, known as in OTCD;, features a modification of the amino acid from Q to H at position 180.
+The protein's natural variant, known as in OTCD; neonatal;, features a modification of the amino acid from E to G at position 181.
+The protein's natural variant, known as in OTCD;, features a modification of the amino acid from H to L at position 182.
+The protein's natural variant, known as in OTCD;, features a modification of the amino acid from Y to C at position 183.
+The protein's natural variant, known as in OTCD; late onset;, features a modification of the amino acid from Y to D at position 183.
+The protein's natural variant, known as in OTCD; neonatal;, features a modification of the amino acid from G to R at position 188.
+The protein's natural variant, known as in OTCD;, features a modification of the amino acid from G to V at position 188.
+The protein's natural variant, known as in OTCD;, features a modification of the amino acid from L to F at position 191.
+The protein's natural variant, known as in OTCD; neonatal;, features a modification of the amino acid from S to R at position 192.
+The protein's natural variant, known as in OTCD; loss of ornithine carbamoyltransferase activity;, features a modification of the amino acid from G to R at position 195.
+The protein's natural variant, known as in OTCD; neonatal; decreased ornithine carbamoyltransferase activity; 3.7% activity;, features a modification of the amino acid from D to V at position 196.
+The protein's natural variant, known as in OTCD; neonatal;, features a modification of the amino acid from D to Y at position 196.
+The protein's natural variant, known as in OTCD;, features a modification of the amino acid from G to E at position 197.
+The protein's natural variant, known as in OTCD;, features a modification of the amino acid from G to R at position 197.
+The protein's natural variant, known as in OTCD;, features a modification of the amino acid from N to K at position 198.
+The protein's natural variant, known as in OTCD; neonatal;, features a modification of the amino acid from L to P at position 201.
+The protein's natural variant, known as in OTCD;, features a modification of the amino acid from H to Y at position 202.
+The protein's natural variant, known as in OTCD;, features a modification of the amino acid from S to C at position 203.
+The protein's natural variant, known as in OTCD;, features a modification of the amino acid from M to I at position 206.
+The protein's natural variant, known as in OTCD; neonatal;, features a modification of the amino acid from M to R at position 206.
+The protein's natural variant, known as in OTCD; neonatal;, features a modification of the amino acid from S to R at position 207.
+The protein's natural variant, known as in OTCD; late onset;, features a modification of the amino acid from A to T at position 208.
+The protein's natural variant, known as in OTCD; neonatal;, features a modification of the amino acid from A to V at position 209.
+The protein's natural variant, known as in OTCD; late onset, features a modification of the amino acid from M to K at position 213.
+The protein's natural variant, known as in OTCD; neonatal;, features a modification of the amino acid from H to Y at position 214.
+The protein's natural variant, known as in OTCD;, features a modification of the amino acid from Q to E at position 216.
+The protein's natural variant, known as in OTCD; late onset;, features a modification of the amino acid from P to A at position 220.
+The protein's natural variant, known as in OTCD;, features a modification of the amino acid from P to L at position 225.
+The protein's natural variant, known as in OTCD; neonatal;, features a modification of the amino acid from P to R at position 225.
+The protein's natural variant, known as in OTCD; late onset;, features a modification of the amino acid from P to T at position 225.
+The protein's natural variant, known as in OTCD; late onset;, features a modification of the amino acid from T to I at position 242.
+The protein's natural variant, known as in OTCD; late onset;, features a modification of the amino acid from L to Q at position 244.
+The protein's natural variant, known as in OTCD; neonatal/late onset;, features a modification of the amino acid from T to K at position 247.
+The protein's natural variant, known as in OTCD;, features a modification of the amino acid from H to P at position 255.
+The protein's natural variant, known as in OTCD; mild;, features a modification of the amino acid from T to K at position 262.
+The protein's natural variant, known as in OTCD;, features a modification of the amino acid from D to G at position 263.
+The protein's natural variant, known as in OTCD;, features a modification of the amino acid from D to N at position 263.
+The protein's natural variant, known as in OTCD; late onset; decreased ornithine carbamoyltransferase activity; 8.9% activity;, features a modification of the amino acid from T to A at position 264.
+The protein's natural variant, known as in OTCD; late onset;, features a modification of the amino acid from T to I at position 264.
+The protein's natural variant, known as in OTCD; mild;, features a modification of the amino acid from W to L at position 265.
+The protein's natural variant, known as in OTCD;, features a modification of the amino acid from S to R at position 267.
+The protein's natural variant, known as in OTCD; late onset;, features a modification of the amino acid from M to T at position 268.
+The protein's natural variant, known as in OTCD; neonatal;, features a modification of the amino acid from G to E at position 269.
+The protein's natural variant, known as in OTCD; late onset;, features a modification of the amino acid from R to Q at position 277.
+The protein's natural variant, known as in OTCD; late onset;, features a modification of the amino acid from R to W at position 277.
+The protein's natural variant, known as in OTCD;, features a modification of the amino acid from L to F at position 301.
+The protein's natural variant, known as in OTCD; female; late onset;, features a modification of the amino acid from H to L at position 302.
+The protein's natural variant, known as in OTCD; late onset;, features a modification of the amino acid from H to Q at position 302.
+The protein's natural variant, known as in OTCD; neonatal;, features a modification of the amino acid from H to Y at position 302.
+The protein's natural variant, known as in OTCD; neonatal;, features a modification of the amino acid from C to R at position 303.
+The protein's natural variant, known as in OTCD;, features a modification of the amino acid from C to Y at position 303.
+The protein's natural variant, known as in OTCD;, features a modification of the amino acid from L to F at position 304.
+The protein's natural variant, known as in OTCD;, features a modification of the amino acid from P to H at position 305.
+The protein's natural variant, known as in OTCD;, features a modification of the amino acid from R to L at position 320.
+The protein's natural variant, known as in OTCD;, features a modification of the amino acid from E to K at position 326.
+The protein's natural variant, known as in OTCD;, features a modification of the amino acid from R to G at position 330.
+The natural variant of this protein is characterized by an amino acid alteration from T to A at position 333.
+The protein's natural variant, known as in OTCD; late onset;, features a modification of the amino acid from A to S at position 336.
+The protein's natural variant, known as in OTCD; late onset;, features a modification of the amino acid from V to L at position 337.
+The protein's natural variant, known as in OTCD; neonatal;, features a modification of the amino acid from V to L at position 339.
+The protein's natural variant, known as in OTCD; late onset;, features a modification of the amino acid from S to P at position 340.
+The protein's natural variant, known as in OTCD;, features a modification of the amino acid from L to P at position 341.
+The protein's natural variant, known as in OTCD; late onset;, features a modification of the amino acid from T to K at position 343.
+The protein's natural variant, known as in OTCD; neonatal;, features a modification of the amino acid from Y to C at position 345.
+The protein's natural variant, known as in OTCD;, features a modification of the amino acid from Y to D at position 345.
+The protein's natural variant, known as in OTCD; late onset;, features a modification of the amino acid from F to C at position 354.
+The protein's natural variant, known as in allele C1-B73, features a modification of the amino acid from L to LM at position 77.
+The protein's natural variant, known as in allele C1-I and allele C1-I-2K1, features a modification of the amino acid from D to E at position 101.
+The protein's natural variant, known as in allele C1-B73, allele C1-I and allele C1-I-2K1, features a modification of the amino acid from W to R at position 126.
+The protein's natural variant, known as in allele C1-B73, features a modification of the amino acid from V to I at position 129.
+The protein's natural variant, known as in allele C1-B73 and allele C1-I, features a modification of the amino acid from AC to SG at position 146.
+The protein's natural variant, known as in allele C1-I-2K1, features a modification of the amino acid from AC to SS at position 146.
+The protein's natural variant, known as in allele C1-B73, allele C1-I and allele C1-I-2K1, features a modification of the amino acid from NS to KG at position 152.
+The protein's natural variant, known as in allele C1-B73, allele C1-I and allele C1-I-2K1, features a modification of the amino acid from H to P at position 155.
+The protein's natural variant, known as in allele C1-I and C1-I-2K1, features a modification of the amino acid from G to S at position 182.
+The protein's natural variant, known as in allele C1-I and allele C1-I-2K1, features a modification of the amino acid from G to GVG at position 208.
+The protein's natural variant, known as in allele C1-B73, features a modification of the amino acid from G to L at position 210.
+The protein's natural variant, known as in allele C1-B73, features a modification of the amino acid from D to E at position 218.
+The protein's natural variant, known as in allele C1-B73, allele C1-I and allele C1-I-2K1, features a modification of the amino acid from L to P at position 228.
+The protein's natural variant, known as in allele C1-B73, features a modification of the amino acid from R to L at position 229.
+The protein's natural variant, known as in allele C1-B73, features a modification of the amino acid from H to Q at position 233.
+The protein's natural variant, known as in allele C1-B73, features a modification of the amino acid from G to C at position 244.
+The protein's natural variant, known as in allele C1-I-2K1, features a modification of the amino acid from WMDD to SWTT at position 249.
+The protein's natural variant, known as in allele C1-I, features a modification of the amino acid from DVRA to SWTT at position 252.
+The protein's natural variant, known as in NDI, features a modification of the amino acid from S to F at position 17.
+The protein's natural variant, known as in NDI; probably causes insufficient processing of precursor;, features a modification of the amino acid from A to T at position 19.
+The protein's natural variant, known as in NDI;, features a modification of the amino acid from A to V at position 19.
+The protein's natural variant, known as in NDI;, features a modification of the amino acid from Y to H at position 21.
+The protein's natural variant, known as in NDI; weakly active;, features a modification of the amino acid from P to L at position 26.
+The protein's natural variant, known as in NDI, features a modification of the amino acid from G to R at position 45.
+The protein's natural variant, known as in NDI;, features a modification of the amino acid from G to V at position 48.
+The protein's natural variant, known as in NDI, features a modification of the amino acid from R to C at position 51.
+The protein's natural variant, known as in NDI, features a modification of the amino acid from C to R at position 52.
+The protein's natural variant, known as in NDI;, features a modification of the amino acid from G to R at position 54.
+The protein's natural variant, known as in NDI;, features a modification of the amino acid from G to V at position 54.
+The protein's natural variant, known as in NDI, features a modification of the amino acid from P to L at position 55.
+The protein's natural variant, known as in NDI, features a modification of the amino acid from C to F at position 58.
+The protein's natural variant, known as in NDI, features a modification of the amino acid from C to R at position 59.
+The protein's natural variant, known as in NDI, features a modification of the amino acid from C to Y at position 59.
+The protein's natural variant, known as in NDI;, features a modification of the amino acid from V to A at position 67.
+The protein's natural variant, known as in NDI, features a modification of the amino acid from E to G at position 78.
+The protein's natural variant, known as in NDI, features a modification of the amino acid from L to P at position 81.
+The protein's natural variant, known as in NDI;, features a modification of the amino acid from S to F at position 87.
+The protein's natural variant, known as in NDI, features a modification of the amino acid from G to R at position 88.
+The protein's natural variant, known as in NDI;, features a modification of the amino acid from G to S at position 88.
+The protein's natural variant, known as in NDI, features a modification of the amino acid from C to S at position 92.
+The protein's natural variant, known as in NDI;, features a modification of the amino acid from C to Y at position 92.
+The protein's natural variant, known as in NDI;, features a modification of the amino acid from G to W at position 93.
+The protein's natural variant, known as in NDI, features a modification of the amino acid from G to C at position 96.
+The protein's natural variant, known as in NDI, features a modification of the amino acid from G to D at position 96.
+The protein's natural variant, known as in NDI;, features a modification of the amino acid from G to V at position 96.
+The protein's natural variant, known as in NDI, features a modification of the amino acid from R to C at position 97.
+The protein's natural variant, known as in NDI, features a modification of the amino acid from R to P at position 97.
+The protein's natural variant, known as in NDI, features a modification of the amino acid from C to G at position 98.
+The protein's natural variant, known as in NDI, features a modification of the amino acid from C to S at position 98.
+The protein's natural variant, known as in NDI, features a modification of the amino acid from A to P at position 99.
+The protein's natural variant, known as in NDI, features a modification of the amino acid from C to F at position 104.
+The protein's natural variant, known as in NDI, features a modification of the amino acid from C to G at position 104.
+The protein's natural variant, known as in NDI, features a modification of the amino acid from C to R at position 105.
+The protein's natural variant, known as in NDI, features a modification of the amino acid from C to Y at position 105.
+The protein's natural variant, known as in NDI; strong accumulation in the endoplasmic reticulum and an altered morphology of this organelle;, features a modification of the amino acid from C to G at position 116.
+The protein's natural variant, known as in NDI, features a modification of the amino acid from C to R at position 116.
+The protein's natural variant, known as in NDI, features a modification of the amino acid from C to W at position 116.
+The protein's natural variant, known as found in a patient with cohesinopathy; unknown pathological significance;, features a modification of the amino acid from V to I at position 85.
+The protein's natural variant, known as in MRD47;, features a modification of the amino acid from Q to R at position 214.
+The protein's natural variant, known as in MRD47;, features a modification of the amino acid from R to G at position 216.
+The protein's natural variant, known as in MRD47;, features a modification of the amino acid from H to R at position 220.
+The protein's natural variant, known as in MRD47;, features a modification of the amino acid from K to Q at position 333.
+The protein's natural variant, known as in MRD47;, features a modification of the amino acid from L to W at position 351.
+The protein's natural variant, known as in MRD47;, features a modification of the amino acid from R to Q at position 373.
+The protein's natural variant, known as found in a patient with cohesinopathy;, features a modification of the amino acid from R to C at position 377.
+The protein's natural variant, known as in MRD47;, features a modification of the amino acid from H to P at position 478.
+The protein's natural variant, known as in MRD47;, features a modification of the amino acid from K to R at position 979.
+The protein's natural variant, known as in alpha-2, features a modification of the amino acid from D to G at position 15.
+The protein's natural variant, known as in strain: Fr7, features a modification of the amino acid from VH to IS at position 60.
+The protein's natural variant, known as in strain: 686, De12, Fr7, Pt1 and Thomsen, features a modification of the amino acid from SGT to TGS at position 77.
+The protein's natural variant, known as in strain: Fr11 and Wf21, features a modification of the amino acid from K to N at position 80.
+The protein's natural variant, known as in strain: De12, Fr7, Pt1 and Thomsen, features a modification of the amino acid from S to G at position 85.
+The protein's natural variant, known as in strain: De12, Fr7, Pt1 and Thomsen, features a modification of the amino acid from RVSTG to MFNTN at position 95.
+The protein's natural variant, known as in strain: 686, De12, Fr7, Fr11, Pt1, Thomsen and Wf21, features a modification of the amino acid from SASNSREDGYYGTNSD to AANNSGVDGKYGNETSS at position 129.
+The protein's natural variant, known as in strain: 686, De12, Fr7, Fr11, Pt1, Thomsen and Wf21, features a modification of the amino acid from Q to E at position 134.
+The protein's natural variant, known as in strain: 686, De12, Fr7, Fr11, Pt1, Thomsen and Wf21, features a modification of the amino acid from Q to H at position 153.
+The protein's natural variant, known as in strain: 686, De12, Fr7, Fr11, Pt1, Thomsen and Wf21, features a modification of the amino acid from T to S at position 172.
+The protein's natural variant, known as in strain: 686, De12, Fr7, Fr11, Pt1, Thomsen and Wf21, features a modification of the amino acid from PVFKDSQGREINGRGYQ to GTTNYH at position 222.
+The protein's natural variant, known as in strain: 686, De12, Fr7, Fr11, Pt1, Thomsen and Wf21, features a modification of the amino acid from T to A at position 258.
+The protein's natural variant, known as in strain: 686, De12, Fr7, Fr11, Pt1, Thomsen and Wf21, features a modification of the amino acid from I to V at position 339.
+The protein's natural variant, known as in strain: 686, De12, Fr7, Fr11, Pt1, Thomsen and Wf21, features a modification of the amino acid from SN to GG at position 350.
+The protein's natural variant, known as in strain: 686, De12, Fr7, Fr11, Pt1, Thomsen and Wf21, features a modification of the amino acid from RELGNDTLDD to NTVAEDN at position 363.
+The protein's natural variant, known as in MEN1; no effect on histone methylation; almost no effect on JUND-binding;, features a modification of the amino acid from P to L at position 12.
+The protein's natural variant, known as in MEN1; no effect on histone methylation; almost no effect on JUND-binding; no repression of JUND transactivation;, features a modification of the amino acid from L to R at position 22.
+The protein's natural variant, known as in parathyroid adenoma and MEN1;, features a modification of the amino acid from E to K at position 26.
+The protein's natural variant, known as in MEN1, features a modification of the amino acid from L to W at position 39.
+The protein's natural variant, known as in MEN1, features a modification of the amino acid from G to D at position 42.
+The protein's natural variant, known as in MEN1;, features a modification of the amino acid from E to G at position 45.
+The protein's natural variant, known as in MEN1;, features a modification of the amino acid from E to K at position 45.
+The protein's natural variant, known as in MEN1, features a modification of the amino acid from R to L at position 98.
+The protein's natural variant, known as in MEN1;, features a modification of the amino acid from G to E at position 110.
+The protein's natural variant, known as in MEN1, features a modification of the amino acid from K to I at position 135.
+The protein's natural variant, known as in MEN1; almost complete loss of histone methylation; strong decrease in JUND-binding; no repression of JUND transactivation; reduced interaction with KMT2A;, features a modification of the amino acid from H to D at position 139.
+The protein's natural variant, known as in MEN1, features a modification of the amino acid from H to P at position 139.
+The protein's natural variant, known as in MEN1;, features a modification of the amino acid from H to R at position 139.
+The protein's natural variant, known as in MEN1; familial and sporadic cases; almost no effect on JUND-binding; no repression of JUND transactivation, features a modification of the amino acid from H to Y at position 139.
+The protein's natural variant, known as in MEN1;, features a modification of the amino acid from F to V at position 144.
+The protein's natural variant, known as in MEN1, features a modification of the amino acid from I to F at position 147.
+The protein's natural variant, known as in parathyroid tumors; somatic, features a modification of the amino acid from L to W at position 157.
+The protein's natural variant, known as in MEN1; also found in isolated hyperparathyroidism;, features a modification of the amino acid from D to V at position 158.
+The protein's natural variant, known as in MEN1;, features a modification of the amino acid from S to I at position 159.
+The protein's natural variant, known as in MEN1, features a modification of the amino acid from S to F at position 160.
+The protein's natural variant, known as in MEN1 and parathyroid tumor;, features a modification of the amino acid from G to D at position 161.
+The protein's natural variant, known as in MEN1; strong decrease in JUND-binding;, features a modification of the amino acid from A to P at position 165.
+The protein's natural variant, known as in MEN1, features a modification of the amino acid from A to T at position 165.
+The protein's natural variant, known as in MEN1, features a modification of the amino acid from V to F at position 167.
+The protein's natural variant, known as in MEN1, features a modification of the amino acid from A to D at position 169.
+The protein's natural variant, known as in MEN1, features a modification of the amino acid from C to R at position 170.
+The protein's natural variant, known as in MEN1;, features a modification of the amino acid from L to P at position 173.
+The protein's natural variant, known as in MEN1;, features a modification of the amino acid from D to Y at position 177.
+The protein's natural variant, known as in MEN1; loss of JUND-binding;, features a modification of the amino acid from A to P at position 181.
+The protein's natural variant, known as in MEN1;, features a modification of the amino acid from E to D at position 184.
+The protein's natural variant, known as in MEN1;, features a modification of the amino acid from E to K at position 184.
+The protein's natural variant, known as in MEN1, features a modification of the amino acid from E to Q at position 184.
+The protein's natural variant, known as in MEN1;, features a modification of the amino acid from H to R at position 186.
+The protein's natural variant, known as in MEN1 and parathyroid tumor;, features a modification of the amino acid from W to R at position 188.
+The protein's natural variant, known as in MEN1, features a modification of the amino acid from W to S at position 188.
+The protein's natural variant, known as probable disease-associated variant found in isolated hyperparathyroidism;, features a modification of the amino acid from V to E at position 189.
+The protein's natural variant, known as found in a parathyroid carcinoma sample; somatic mutation, features a modification of the amino acid from V to F at position 220.
+The protein's natural variant, known as in MEN1;, features a modification of the amino acid from V to M at position 220.
+The protein's natural variant, known as in MEN1;, features a modification of the amino acid from L to P at position 228.
+The protein's natural variant, known as in MEN1;, features a modification of the amino acid from G to R at position 230.
+The protein's natural variant, known as in MEN1, features a modification of the amino acid from R to L at position 234.
+The protein's natural variant, known as in MEN1, features a modification of the amino acid from V to F at position 245.
+The protein's natural variant, known as in MEN1; loss of interaction with KMT2A and JUND, features a modification of the amino acid from C to F at position 246.
+The protein's natural variant, known as in MEN1;, features a modification of the amino acid from C to R at position 246.
+The protein's natural variant, known as in MEN1;, features a modification of the amino acid from C to Y at position 246.
+The protein's natural variant, known as in MEN1; almost complete loss of histone methylation; loss of JUND-binding; no repression of JUND transactivation; reduced interaction with KMT2A, features a modification of the amino acid from A to V at position 247.
+The protein's natural variant, known as in MEN1, features a modification of the amino acid from S to P at position 258.
+The protein's natural variant, known as in parathyroid tumor;, features a modification of the amino acid from S to W at position 258.
+The protein's natural variant, known as probable disease-associated variant found in isolated hyperparathyroidism;, features a modification of the amino acid from E to K at position 260.
+The protein's natural variant, known as in MEN1, features a modification of the amino acid from L to R at position 264.
+The protein's natural variant, known as probable disease-associated variant found in isolated hyperparathyroidism, features a modification of the amino acid from Q to P at position 265.
+The protein's natural variant, known as in MEN1, features a modification of the amino acid from Q to QLQ at position 266.
+The protein's natural variant, known as in MEN1;, features a modification of the amino acid from L to P at position 269.
+The protein's natural variant, known as probable disease-associated variant found in isolated hyperparathyroidism, features a modification of the amino acid from L to P at position 272.
+The protein's natural variant, known as in parathyroid tumor, features a modification of the amino acid from E to A at position 279.
+The protein's natural variant, known as probable disease-associated variant found in isolated hyperparathyroidism;, features a modification of the amino acid from P to H at position 282.
+The protein's natural variant, known as in MEN1; loss of interaction with KMT2A and JUND;, features a modification of the amino acid from G to R at position 286.
+The protein's natural variant, known as in MEN1;, features a modification of the amino acid from A to E at position 289.
+The protein's natural variant, known as in parathyroid tumor, features a modification of the amino acid from A to P at position 289.
+The protein's natural variant, known as requires 2 nucleotide substitutions; yields insoluble protein, features a modification of the amino acid from A to Q at position 289.
+The protein's natural variant, known as in MEN1; almost no effect on JUND-binding, features a modification of the amino acid from L to P at position 291.
+The protein's natural variant, known as probable disease-associated variant found in isolated hyperparathyroidism, features a modification of the amino acid from G to D at position 310.
+The protein's natural variant, known as in MEN1; no effect on histone methylation; almost no effect on JUND-binding, features a modification of the amino acid from A to P at position 314.
+The protein's natural variant, known as in MEN1, features a modification of the amino acid from T to P at position 316.
+The protein's natural variant, known as in MEN1, features a modification of the amino acid from R to P at position 319.
+The protein's natural variant, known as in MEN1;, features a modification of the amino acid from H to R at position 322.
+The protein's natural variant, known as in MEN1, features a modification of the amino acid from H to Y at position 322.
+The protein's natural variant, known as in MEN1;, features a modification of the amino acid from P to L at position 325.
+The protein's natural variant, known as in MEN1, features a modification of the amino acid from P to R at position 325.
+The protein's natural variant, known as in MEN1, features a modification of the amino acid from A to P at position 330.
+The protein's natural variant, known as in MEN1;, features a modification of the amino acid from A to D at position 342.
+The protein's natural variant, known as in MEN1;, features a modification of the amino acid from A to P at position 342.
+The protein's natural variant, known as in MEN1, features a modification of the amino acid from W to R at position 346.
+The protein's natural variant, known as in MEN1;, features a modification of the amino acid from A to P at position 347.
+The protein's natural variant, known as in MEN1; almost complete loss of histone methylation; almost no effect on JUND-binding; yields insoluble protein, features a modification of the amino acid from T to R at position 349.
+The protein's natural variant, known as in MEN1, features a modification of the amino acid from I to N at position 353.
+The protein's natural variant, known as in MEN1, features a modification of the amino acid from Y to D at position 358.
+The protein's natural variant, known as in MEN1;, features a modification of the amino acid from R to W at position 360.
+The protein's natural variant, known as in MEN1, features a modification of the amino acid from D to H at position 362.
+The protein's natural variant, known as in MEN1;, features a modification of the amino acid from E to K at position 364.
+The protein's natural variant, known as in MEN1;, features a modification of the amino acid from A to D at position 373.
+The protein's natural variant, known as in MEN1, features a modification of the amino acid from I to M at position 377.
+The protein's natural variant, known as in MEN1;, features a modification of the amino acid from P to S at position 378.
+The protein's natural variant, known as in MEN1;, features a modification of the amino acid from A to V at position 390.
+The protein's natural variant, known as in MEN1; also found in isolated hyperparathyroidism, features a modification of the amino acid from A to P at position 416.
+The protein's natural variant, known as in MEN1, features a modification of the amino acid from L to R at position 418.
+The protein's natural variant, known as in MEN1, features a modification of the amino acid from L to P at position 419.
+The protein's natural variant, known as in MEN1;, features a modification of the amino acid from R to P at position 420.
+The protein's natural variant, known as in MEN1;, features a modification of the amino acid from D to H at position 423.
+The protein's natural variant, known as in MEN1;, features a modification of the amino acid from D to N at position 423.
+The protein's natural variant, known as in MEN1;, features a modification of the amino acid from C to Y at position 426.
+The protein's natural variant, known as in MEN1, features a modification of the amino acid from W to S at position 428.
+The protein's natural variant, known as in MEN1;, features a modification of the amino acid from S to R at position 432.
+The protein's natural variant, known as in MEN1;, features a modification of the amino acid from W to C at position 441.
+The protein's natural variant, known as in MEN1; no effect on histone methylation; almost no effect on JUND-binding; modest repression of JUND transactivation;, features a modification of the amino acid from W to R at position 441.
+The protein's natural variant, known as in MEN1, features a modification of the amino acid from L to P at position 449.
+The protein's natural variant, known as in MEN1; sporadic; with Zollinger-Ellison syndrome;, features a modification of the amino acid from F to S at position 452.
+The protein's natural variant, known as in MEN1, features a modification of the amino acid from W to C at position 476.
+The protein's natural variant, known as in MEN1, features a modification of the amino acid from R to C at position 532.
+The protein's natural variant, known as in MEN1;, features a modification of the amino acid from P to S at position 545.
+The protein's natural variant, known as in MEN1;, features a modification of the amino acid from P to S at position 549.
+The protein's natural variant, known as in adrenal adenoma; somatic;, features a modification of the amino acid from T to S at position 557.
+The protein's natural variant, known as in MEN1;, features a modification of the amino acid from S to N at position 560.
+The protein's natural variant, known as in MEN1, features a modification of the amino acid from S to R at position 560.
+The protein's natural variant, known as in ARMD11; alters processing and glycosylation;, features a modification of the amino acid from A to T at position 25.
+The protein's natural variant, known as in AMYL6;, features a modification of the amino acid from L to Q at position 94.
+The protein's natural variant, known as in strain: cv. Zhongshu 5, features a modification of the amino acid from K to R at position 87.
+The protein's natural variant, known as in FFEVF1; does not inhibit DEPDC5 signaling; does not change kinase activity of mTORC1; does not change association with the GATOR complex; inhibits slightly RRAGA/RRAGC and RRAGB/RRAGC heterodimer formation;, features a modification of the amino acid from V to I at position 90.
+The protein's natural variant, known as in FFEVF1; unknown pathological significance;, features a modification of the amino acid from H to D at position 214.
+The protein's natural variant, known as in FFEVF1; does not inhibit DEPDC5 signaling; does not change kinase activity of mTORC1; does not change association with the GATOR complex; does not change RRAGA/RRAGC and RRAGB/RRAGC heterodimer formation;, features a modification of the amino acid from V to L at position 272.
+The protein's natural variant, known as in FFEVF1; inhibits slightly DEPDC5 signaling; stimulates slightly kinase activity of mTORC1; does not change association with the GATOR complex; does not change RRAGA/RRAGC and RRAGB/RRAGC heterodimer formation;, features a modification of the amino acid from A to V at position 452.
+The protein's natural variant, known as in FFEVF1; does not inhibit DEPDC5 signaling; stimulates slightly kinase activity of mTORC1; does not change association with the GATOR complex; does not change RRAGA/RRAGC and RRAGB/RRAGC heterodimer formation;, features a modification of the amino acid from R to Q at position 485.
+The protein's natural variant, known as in FFEVF1; unknown pathological significance;, features a modification of the amino acid from Q to P at position 542.
+The protein's natural variant, known as in FFEVF1; inhibits slightly DEPDC5 signaling; does not change kinase activity of mTORC1; does not change association with the GATOR complex; does not change RRAGA/RRAGC and RRAGB/RRAGC heterodimer formation;, features a modification of the amino acid from T to M at position 864.
+The protein's natural variant, known as in FFEVF1; unknown pathological significance;, features a modification of the amino acid from K to R at position 1065.
+The protein's natural variant, known as in FFEVF1; inhibits slightly DEPDC5 signaling; does not change kinase activity of mTORC1; does not change association with the GATOR complex; does not change RRAGA/RRAGC and RRAGB/RRAGC heterodimer formation;, features a modification of the amino acid from S to R at position 1073.
+The protein's natural variant, known as in FFEVF1; unknown pathological significance;, features a modification of the amino acid from T to P at position 1081.
+The protein's natural variant, known as in FFEVF1; unknown pathological significance;, features a modification of the amino acid from S to L at position 1104.
+The protein's natural variant, known as in FFEVF1; unknown pathological significance;, features a modification of the amino acid from S to F at position 1154.
+The protein's natural variant, known as in FFEVF1; does not inhibit DEPDC5 signaling; does not change kinase activity of mTORC1; does not change association with the GATOR complex; does not change RRAGA/RRAGC and RRAGB/RRAGC heterodimer formation;, features a modification of the amino acid from S to G at position 1162.
+The protein's natural variant, known as in FFEVF1; unknown pathological significance;, features a modification of the amino acid from R to Q at position 1268.
+The protein's natural variant, known as in RAK;, features a modification of the amino acid from P to S at position 139.
+The protein's natural variant, known as in AD18; associated with disease susceptibility; significantly attenuates alpha-secretase activity of the enzyme; shifts APP processing toward beta-secretase-mediated cleavage resulting in enhanced amyloid-beta plaque load and reactive gliosis;, features a modification of the amino acid from Q to H at position 170.
+The protein's natural variant, known as in a cutaneous metastatic melanoma sample; somatic mutation;, features a modification of the amino acid from H to Y at position 176.
+The protein's natural variant, known as in AD18; associated with disease susceptibility; significantly attenuates alpha-secretase activity of the enzyme; shifts APP processing toward beta-secretase-mediated cleavage resulting in enhanced amyloid-beta plaque load and reactive gliosis;, features a modification of the amino acid from R to G at position 181.
+The protein's natural variant, known as in RAK;, features a modification of the amino acid from C to Y at position 524.
+The protein's natural variant, known as in ANOA, features a modification of the amino acid from L to V at position 215.
+The protein's natural variant, known as in ANOA, features a modification of the amino acid from R to W at position 242.
+The protein's natural variant, known as in ANOA, features a modification of the amino acid from R to C at position 306.
+The protein's natural variant, known as in ANOA, features a modification of the amino acid from R to S at position 327.
+The natural variant of this protein is characterized by an amino acid alteration from V to G at position 474.
+The protein's natural variant, known as in LPFS2;, features a modification of the amino acid from C to Y at position 53.
+The protein's natural variant, known as in DBQD1;, features a modification of the amino acid from D to E at position 112.
+The protein's natural variant, known as in DBQD1; severely affects activity;, features a modification of the amino acid from W to C at position 125.
+The protein's natural variant, known as in DBQD1; severely affects activity, features a modification of the amino acid from M to T at position 165.
+The protein's natural variant, known as in EDM7; unknown pathological significance;, features a modification of the amino acid from I to F at position 171.
+The protein's natural variant, known as in DBQD1; affects protein stability and secretion;, features a modification of the amino acid from L to P at position 224.
+The protein's natural variant, known as in DBQD1 and EDM7; severely affects activity;, features a modification of the amino acid from V to M at position 226.
+The protein's natural variant, known as in DBQD1;, features a modification of the amino acid from P to L at position 299.
+The protein's natural variant, known as in DBQD1; severely affects activity;, features a modification of the amino acid from R to C at position 300.
+The protein's natural variant, known as in DBQD1;, features a modification of the amino acid from R to H at position 300.
+The protein's natural variant, known as in DBQD1, features a modification of the amino acid from S to R at position 303.
+The protein's natural variant, known as does not affect activity;, features a modification of the amino acid from A to T at position 323.
+The protein's natural variant, known as in DBQD1; affects protein secretion;, features a modification of the amino acid from A to D at position 360.
+The protein's natural variant, known as in DBQD1, features a modification of the amino acid from I to N at position 374.
+The protein's natural variant, known as does not affect activity;, features a modification of the amino acid from G to E at position 391.
+The protein's natural variant, known as in haplotype NPD, features a modification of the amino acid from E to K at position 22.
+The protein's natural variant, known as in haplotype NPD, features a modification of the amino acid from T to A at position 39.
+The protein's natural variant, known as in haplotype NPD, features a modification of the amino acid from D to E at position 152.
+The protein's natural variant, known as in haplotype NPB, features a modification of the amino acid from T to S at position 176.
+The protein's natural variant, known as in haplotype NPC, features a modification of the amino acid from M to K at position 258.
+The protein's natural variant, known as in PFIC9; several lines of evidence suggest that M-76 may be the main initiator, a variant at this location would therefore disrupt translation initiation;, features a modification of the amino acid from M to V at position 76.
+The protein's natural variant, known as in NEDMCMS; increased homodimerization; even in absence of oxidative stress;, features a modification of the amino acid from R to C at position 53.
+The protein's natural variant, known as in NEDMCMS; unknown pathological significance;, features a modification of the amino acid from D to A at position 55.
+The protein's natural variant, known as in NEDMCMS; unknown pathological significance;, features a modification of the amino acid from G to R at position 56.
+The protein's natural variant, known as in NEDMCMS; unknown pathological significance, features a modification of the amino acid from D to H at position 62.
+The protein's natural variant, known as in NEDMCMS; unknown pathological significance;, features a modification of the amino acid from D to G at position 109.
+The protein's natural variant, known as in NEDMCMS; unknown pathological significance;, features a modification of the amino acid from I to V at position 117.
+The protein's natural variant, known as in NEDMCMS; unknown pathological significance, features a modification of the amino acid from A to T at position 178.
+The protein's natural variant, known as in NEDMCMS; changed alternative splicing; decreased protein abundance; homozygous patient cells show decreased mitochondrial respiratory reserve capacity and compensatory increased glycolytic activity;, features a modification of the amino acid from R to Q at position 205.
+The protein's natural variant, known as in NEDMCMS; increased homodimerization; even in absence of oxidative stress;, features a modification of the amino acid from R to W at position 231.
+The protein's natural variant, known as in haplotype 3, features a modification of the amino acid from R to C at position 95.
+The protein's natural variant, known as in DFNA1;, features a modification of the amino acid from P to S at position 678.
+The protein's natural variant, known as in transposon Tn3411, features a modification of the amino acid from L to M at position 134.
+The protein's natural variant, known as in transposon Tn3411, features a modification of the amino acid from P to H at position 184.
+The protein's natural variant, known as in transposon Tn3411, features a modification of the amino acid from S to P at position 291.
+The protein's natural variant, known as in transposon Tn3411, features a modification of the amino acid from A to S at position 377.
+The protein's natural variant, known as in strain: MT-4, features a modification of the amino acid from V to S at position 2.
+The protein's natural variant, known as in strain: MT-4, features a modification of the amino acid from P to S at position 7.
+The protein's natural variant, known as in strain: MT-4, features a modification of the amino acid from A to S at position 12.
+The protein's natural variant, known as in strain: MT-4, features a modification of the amino acid from D to N at position 42.
+The protein's natural variant, known as in strain: MT-4, features a modification of the amino acid from MV to NG at position 129.
+The natural variant of this protein is characterized by an amino acid alteration from F to I at position 6.
+The natural variant of this protein is characterized by an amino acid alteration from R to K at position 20.
+The protein's natural variant, known as in AHUS7;, features a modification of the amino acid from R to P at position 63.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from L to R at position 99.
+The protein's natural variant, known as in AHUS7;, features a modification of the amino acid from R to P at position 273.
+The protein's natural variant, known as in DL3, features a modification of the amino acid from L to I at position 43.
+The protein's natural variant, known as in DL1 and lysozyme II, features a modification of the amino acid from G to S at position 55.
+The protein's natural variant, known as in lysozyme II, features a modification of the amino acid from Q to E at position 75.
+The protein's natural variant, known as in DL1 and lysozyme II, features a modification of the amino acid from R to G at position 89.
+The protein's natural variant, known as in DL3, features a modification of the amino acid from P to R at position 97.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from T to A at position 207.
+The protein's natural variant, known as in MRCS1; decreased interaction with UNC119; decreased interaction with ARL2BP; changed cellular respiration; decreased ATP production, features a modification of the amino acid from R to L at position 15.
+The protein's natural variant, known as in LKENP; deleterious only under stress conditions;, features a modification of the amino acid from F to C at position 50.
+The protein's natural variant, known as found in patient with leukoencephalopathy; unknown pathological significance;, features a modification of the amino acid from A to V at position 77.
+The protein's natural variant, known as in COXPD8;, features a modification of the amino acid from L to R at position 155.
+The protein's natural variant, known as found in patient with leukoencephalopathy; unknown pathological significance;, features a modification of the amino acid from R to C at position 199.
+The protein's natural variant, known as in LKENP;, features a modification of the amino acid from E to K at position 405.
+The protein's natural variant, known as in COXPD8;, features a modification of the amino acid from R to W at position 592.
+The protein's natural variant, known as in LKENP;, features a modification of the amino acid from G to R at position 965.
+The protein's natural variant, known as in COXPD15; loss of methionyl-tRNA formyltransferase activity;, features a modification of the amino acid from S to L at position 125.
+The protein's natural variant, known as in COXPD15 and MC1DN27; decreased methionyl-tRNA formyltransferase activity;, features a modification of the amino acid from S to L at position 209.
+The protein's natural variant, known as in OPA12; unknown pathological significance, features a modification of the amino acid from E to A at position 74.
+The protein's natural variant, known as in SPAX5; unknown pathological significance, features a modification of the amino acid from K to E at position 306.
+The protein's natural variant, known as in OPA12; loss-of-function variant resulting in aberrant OPA1 processing and mitochondrial fragmentation;, features a modification of the amino acid from G to E at position 337.
+The protein's natural variant, known as in OPA12, features a modification of the amino acid from G to R at position 337.
+The protein's natural variant, known as in OPA12; unknown pathological significance;, features a modification of the amino acid from L to F at position 346.
+The protein's natural variant, known as in OPA12; unknown pathological significance, features a modification of the amino acid from E to K at position 376.
+The protein's natural variant, known as in OPA12; unknown pathological significance;, features a modification of the amino acid from F to S at position 377.
+The protein's natural variant, known as in OPA12; unknown pathological significance; decreased proteolytic function;, features a modification of the amino acid from D to G at position 407.
+The protein's natural variant, known as in OPA12; unknown pathological significance, features a modification of the amino acid from R to S at position 416.
+The protein's natural variant, known as in OPA12; unknown pathological significance;, features a modification of the amino acid from T to I at position 430.
+The protein's natural variant, known as in SCA28;, features a modification of the amino acid from N to T at position 432.
+The protein's natural variant, known as in OPA12 and SPAX5; decreased proteolytic function;, features a modification of the amino acid from A to V at position 462.
+The protein's natural variant, known as in OPA12; decreased proteolytic function;, features a modification of the amino acid from R to K at position 465.
+The protein's natural variant, known as in OPA12; decreased proteolytic function resulting in impaired autocatalytic processing and impaired proteolytic maturation of SPG7; does not affect the interaction with SPG7;, features a modification of the amino acid from R to C at position 468.
+The protein's natural variant, known as in OPA12; decreased proteolytic function;, features a modification of the amino acid from P to L at position 514.
+The protein's natural variant, known as in OPA12; unknown pathological significance;, features a modification of the amino acid from Y to C at position 605.
+The protein's natural variant, known as in SPAX5; hypomorphic mutation; results in impaired oligomerization with itself and SPG7; retains ATPase and proteolytic activities;, features a modification of the amino acid from Y to C at position 616.
+The protein's natural variant, known as in SPAX5; impaired function shown in a yeast complementation assay;, features a modification of the amino acid from Q to K at position 620.
+The protein's natural variant, known as in SCA28; unknown pathological significance, features a modification of the amino acid from L to V at position 621.
+The protein's natural variant, known as in OPA12; unknown pathological significance;, features a modification of the amino acid from T to S at position 644.
+The protein's natural variant, known as in SCA28;, features a modification of the amino acid from T to I at position 654.
+The protein's natural variant, known as in SCA28;, features a modification of the amino acid from M to R at position 666.
+The protein's natural variant, known as in SCA28;, features a modification of the amino acid from M to T at position 666.
+The protein's natural variant, known as in SCA28;, features a modification of the amino acid from M to V at position 666.
+The protein's natural variant, known as in SCA28;, features a modification of the amino acid from G to E at position 671.
+The protein's natural variant, known as in SCA28;, features a modification of the amino acid from G to R at position 671.
+The protein's natural variant, known as in SCA28;, features a modification of the amino acid from Y to H at position 689.
+The protein's natural variant, known as in SCA28, features a modification of the amino acid from Y to N at position 689.
+The protein's natural variant, known as in SCA28; impaired function shown in a yeast complementation assay;, features a modification of the amino acid from E to K at position 691.
+The protein's natural variant, known as in SCA28;, features a modification of the amino acid from A to E at position 694.
+The protein's natural variant, known as in SCA28;, features a modification of the amino acid from E to K at position 700.
+The protein's natural variant, known as in SCA28;, features a modification of the amino acid from R to Q at position 702.
+The protein's natural variant, known as in SNP-A; possible loss of CK2 phosphorylation site, features a modification of the amino acid from S to P at position 102.
+The protein's natural variant, known as in SNP-B; increased semen volume in ejaculate, features a modification of the amino acid from T to K at position 264.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 129.
+The protein's natural variant, known as in SCHZC and HPE2;, features a modification of the amino acid from G to C at position 37.
+The protein's natural variant, known as in HPE2;, features a modification of the amino acid from G to D at position 69.
+The protein's natural variant, known as in HPE2, features a modification of the amino acid from M to V at position 79.
+The protein's natural variant, known as in HPE2, features a modification of the amino acid from V to G at position 92.
+The protein's natural variant, known as in HPE2, features a modification of the amino acid from A to D at position 93.
+The protein's natural variant, known as in HPE2, features a modification of the amino acid from I to V at position 105.
+The protein's natural variant, known as in HPE2;, features a modification of the amino acid from W to C at position 113.
+The protein's natural variant, known as in HPE2, features a modification of the amino acid from S to L at position 114.
+The protein's natural variant, known as in HPE2, features a modification of the amino acid from V to D at position 138.
+The protein's natural variant, known as in HPE2, features a modification of the amino acid from F to I at position 157.
+The protein's natural variant, known as in SCHZC;, features a modification of the amino acid from A to S at position 167.
+The protein's natural variant, known as in HPE2, features a modification of the amino acid from A to V at position 172.
+The protein's natural variant, known as in HPE2, features a modification of the amino acid from H to P at position 173.
+The protein's natural variant, known as in HPE2, features a modification of the amino acid from Y to H at position 174.
+The protein's natural variant, known as in HPE2, features a modification of the amino acid from T to I at position 202.
+The protein's natural variant, known as in HPE2, features a modification of the amino acid from F to V at position 213.
+The protein's natural variant, known as in HPE2, features a modification of the amino acid from R to P at position 218.
+The protein's natural variant, known as in HPE2, features a modification of the amino acid from R to W at position 218.
+The protein's natural variant, known as in HPE2;, features a modification of the amino acid from L to V at position 226.
+The protein's natural variant, known as in HPE2, features a modification of the amino acid from Q to P at position 227.
+The protein's natural variant, known as in HPE2, features a modification of the amino acid from P to R at position 231.
+The protein's natural variant, known as in HPE2;, features a modification of the amino acid from G to C at position 244.
+The protein's natural variant, known as in HPE2; Significantly decreased its ability to activate NR4A3;, features a modification of the amino acid from V to A at position 250.
+The protein's natural variant, known as in HPE2, features a modification of the amino acid from F to L at position 254.
+The protein's natural variant, known as in HPE2, features a modification of the amino acid from R to G at position 257.
+The protein's natural variant, known as in HPE2; Significantly decreased interaction with NR4A3; Significantly decreased its ability to activate NR4A3;, features a modification of the amino acid from R to P at position 257.
+The protein's natural variant, known as in HPE2, features a modification of the amino acid from R to W at position 257.
+The protein's natural variant, known as in HPE2, features a modification of the amino acid from R to L at position 258.
+The protein's natural variant, known as in HPE2, features a modification of the amino acid from R to H at position 262.
+The protein's natural variant, known as in HPE2, features a modification of the amino acid from R to M at position 269.
+The protein's natural variant, known as in HPE2, features a modification of the amino acid from R to S at position 269.
+The protein's natural variant, known as in HPE2, features a modification of the amino acid from R to T at position 269.
+The protein's natural variant, known as in HPE2;, features a modification of the amino acid from P to L at position 297.
+The protein's natural variant, known as in MOT-1, features a modification of the amino acid from M to V at position 618.
+The protein's natural variant, known as in MOT-1, features a modification of the amino acid from G to R at position 624.
+The protein's natural variant, known as in ARCI1; skin phenotype consistent with lamellar ichthyosis;, features a modification of the amino acid from S to Y at position 42.
+The protein's natural variant, known as in ARCI1, features a modification of the amino acid from C to S at position 53.
+The protein's natural variant, known as in ARCI1;, features a modification of the amino acid from G to D at position 94.
+The protein's natural variant, known as in ARCI1; skin phenotype consistent with lamellar ichthyosis;, features a modification of the amino acid from D to V at position 102.
+The protein's natural variant, known as in ARCI1;, features a modification of the amino acid from R to C at position 126.
+The protein's natural variant, known as in ARCI1;, features a modification of the amino acid from R to H at position 126.
+The protein's natural variant, known as in ARCI1;, features a modification of the amino acid from Y to C at position 134.
+The protein's natural variant, known as in ARCI1;, features a modification of the amino acid from R to C at position 142.
+The protein's natural variant, known as in ARCI1; skin phenotype consistent with lamellar ichthyosis;, features a modification of the amino acid from R to H at position 142.
+The protein's natural variant, known as in ARCI1, features a modification of the amino acid from R to P at position 142.
+The protein's natural variant, known as in ARCI1; inhibits cell proliferation;, features a modification of the amino acid from R to C at position 143.
+The protein's natural variant, known as in ARCI1; skin phenotype consistent with lamellar ichthyosis;, features a modification of the amino acid from R to H at position 143.
+The protein's natural variant, known as in ARCI1;, features a modification of the amino acid from G to E at position 144.
+The protein's natural variant, known as in ARCI1;, features a modification of the amino acid from G to R at position 144.
+The protein's natural variant, known as in ARCI1;, features a modification of the amino acid from S to C at position 160.
+The protein's natural variant, known as in ARCI1;, features a modification of the amino acid from L to Q at position 205.
+The protein's natural variant, known as in ARCI1, features a modification of the amino acid from V to F at position 209.
+The protein's natural variant, known as in ARCI1; inhibits cell proliferation;, features a modification of the amino acid from S to F at position 212.
+The protein's natural variant, known as in ARCI1; skin phenotype consistent with lamellar ichthyosis;, features a modification of the amino acid from G to S at position 218.
+The protein's natural variant, known as in ARCI1;, features a modification of the amino acid from R to H at position 225.
+The protein's natural variant, known as in ARCI1;, features a modification of the amino acid from R to P at position 225.
+The protein's natural variant, known as in ARCI1, features a modification of the amino acid from I to S at position 243.
+The protein's natural variant, known as in ARCI1, features a modification of the amino acid from P to L at position 249.
+The protein's natural variant, known as in ARCI1;, features a modification of the amino acid from R to Q at position 264.
+The protein's natural variant, known as in ARCI1;, features a modification of the amino acid from R to W at position 264.
+The protein's natural variant, known as in ARCI1;, features a modification of the amino acid from S to P at position 272.
+The protein's natural variant, known as in ARCI1;, features a modification of the amino acid from Y to N at position 276.
+The protein's natural variant, known as in ARCI1;, features a modification of the amino acid from G to R at position 278.
+The protein's natural variant, known as in ARCI1;, features a modification of the amino acid from E to K at position 285.
+The protein's natural variant, known as in ARCI1;, features a modification of the amino acid from R to Q at position 286.
+The protein's natural variant, known as in ARCI1; skin phenotype consistent with lamellar ichthyosis;, features a modification of the amino acid from N to T at position 289.
+The protein's natural variant, known as in ARCI1, features a modification of the amino acid from F to V at position 293.
+The protein's natural variant, known as in ARCI1;, features a modification of the amino acid from I to F at position 304.
+The protein's natural variant, known as in ARCI1;, features a modification of the amino acid from R to G at position 307.
+The protein's natural variant, known as in ARCI1; skin phenotype consistent with lamellar ichthyosis;, features a modification of the amino acid from R to W at position 307.
+The protein's natural variant, known as in ARCI1;, features a modification of the amino acid from R to C at position 315.
+The protein's natural variant, known as in ARCI1;, features a modification of the amino acid from R to H at position 315.
+The protein's natural variant, known as in ARCI1;, features a modification of the amino acid from R to L at position 315.
+The protein's natural variant, known as in ARCI1; skin phenotype consistent with lamellar ichthyosis;, features a modification of the amino acid from R to Q at position 323.
+The protein's natural variant, known as in ARCI1;, features a modification of the amino acid from R to W at position 323.
+The protein's natural variant, known as in ARCI1, features a modification of the amino acid from N to H at position 330.
+The protein's natural variant, known as in ARCI1, features a modification of the amino acid from S to P at position 331.
+The protein's natural variant, known as in ARCI1, features a modification of the amino acid from W to R at position 342.
+The protein's natural variant, known as in ARCI1;, features a modification of the amino acid from S to R at position 358.
+The protein's natural variant, known as in ARCI1;, features a modification of the amino acid from V to M at position 359.
+The protein's natural variant, known as in ARCI1, features a modification of the amino acid from Y to D at position 365.
+The protein's natural variant, known as in ARCI1, features a modification of the amino acid from L to P at position 366.
+The protein's natural variant, known as in ARCI1;, features a modification of the amino acid from V to L at position 379.
+The protein's natural variant, known as in ARCI1, features a modification of the amino acid from G to R at position 382.
+The protein's natural variant, known as in ARCI1;, features a modification of the amino acid from V to M at position 383.
+The protein's natural variant, known as in ARCI1; skin phenotype consistent with non-bullous congenital ichthyosiform erythroderma;, features a modification of the amino acid from R to H at position 389.
+The protein's natural variant, known as in ARCI1;, features a modification of the amino acid from R to P at position 389.
+The protein's natural variant, known as in ARCI1;, features a modification of the amino acid from G to D at position 392.
+The protein's natural variant, known as in ARCI1;, features a modification of the amino acid from R to H at position 396.
+The protein's natural variant, known as in ARCI1; skin phenotype consistent with non-bullous congenital ichthyosiform erythroderma;, features a modification of the amino acid from R to L at position 396.
+The protein's natural variant, known as in ARCI1, features a modification of the amino acid from R to S at position 396.
+The protein's natural variant, known as in ARCI1;, features a modification of the amino acid from F to V at position 401.
+The protein's natural variant, known as in ARCI1;, features a modification of the amino acid from D to V at position 430.
+The protein's natural variant, known as in ARCI1;, features a modification of the amino acid from G to S at position 473.
+The protein's natural variant, known as in ARCI1;, features a modification of the amino acid from D to G at position 490.
+The protein's natural variant, known as in ARCI1;, features a modification of the amino acid from E to G at position 520.
+The protein's natural variant, known as in ARCI1;, features a modification of the amino acid from Y to C at position 544.
+The protein's natural variant, known as in ARCI1;, features a modification of the amino acid from R to C at position 687.
+The protein's natural variant, known as in ARCI1, features a modification of the amino acid from R to H at position 687.
+The protein's natural variant, known as in ARCI1;, features a modification of the amino acid from R to C at position 764.
+The protein's natural variant, known as normal DNA mismatch repair activity;, features a modification of the amino acid from I to V at position 18.
+The protein's natural variant, known as no effect on protein abundance; no effect on subcellular localization; normal DNA mismatch repair activity;, features a modification of the amino acid from R to Q at position 20.
+The protein's natural variant, known as no effect on protein levels;, features a modification of the amino acid from S to R at position 36.
+The protein's natural variant, known as in MMRCS4 and LYNCH4; strongly decreased DNA mismatch repair activity; no effect on protein abundance; no effect on subcellular localization;, features a modification of the amino acid from S to I at position 46.
+The protein's natural variant, known as in LYNCH4; strongly decreased DNA mismatch repair activity;, features a modification of the amino acid from S to N at position 46.
+The protein's natural variant, known as normal DNA mismatch repair activity;, features a modification of the amino acid from D to E at position 60.
+The protein's natural variant, known as in MMRCS4; unknown pathological significance; normal DNA mismatch repair activity;, features a modification of the amino acid from I to T at position 66.
+The protein's natural variant, known as in MMRCS4; decreased DNA mismatch repair activity;, features a modification of the amino acid from R to W at position 107.
+The protein's natural variant, known as in MMRCS4; decreased DNA mismatch repair activity, features a modification of the amino acid from C to G at position 115.
+The protein's natural variant, known as in LYNCH4; unknown pathological significance;, features a modification of the amino acid from A to T at position 182.
+The protein's natural variant, known as in MMRCS4 and LYNCH4; unknown pathological significance; normal DNA mismatch repair activity;, features a modification of the amino acid from Q to P at position 205.
+The protein's natural variant, known as in LYNCH4; unknown pathological significance; normal DNA mismatch repair activity; no effect on protein stability compared to wild-type; no effect on ATPase activity; does not appear to induce a significant structural rearrangement;, features a modification of the amino acid from G to E at position 207.
+The protein's natural variant, known as no effect on DNA mismatch repair activity in an in vitro assay, compared to wild-type; no effect on ATPase activity; no effect on protein stability;, features a modification of the amino acid from G to E at position 232.
+The protein's natural variant, known as no effect on DNA mismatch repair activity in an in vitro assay, compared to wild-type; no effect on ATPase activity; no effect on protein stability;, features a modification of the amino acid from S to R at position 238.
+The protein's natural variant, known as in MMRCS4 and LYNCH4; unknown pathological significance; normal DNA mismatch repair activity;, features a modification of the amino acid from L to V at position 263.
+The protein's natural variant, known as in MMRCS4; unknown pathological significance; decreased DNA mismatch repair activity;, features a modification of the amino acid from N to K at position 307.
+The protein's natural variant, known as no effect on DNA mismatch repair activity in an in vitro assay, compared to wild-type; loss of ATPase activity; retained ability to bind ATP; no effect on protein stability;, features a modification of the amino acid from N to S at position 335.
+The protein's natural variant, known as normal DNA mismatch repair activity;, features a modification of the amino acid from A to T at position 423.
+The protein's natural variant, known as in MMRCS4; unknown pathological significance; normal DNA mismatch repair activity;, features a modification of the amino acid from P to S at position 437.
+The protein's natural variant, known as no effect on protein abundance; no effect on subcellular localization; normal DNA mismatch repair activity;, features a modification of the amino acid from P to S at position 470.
+The protein's natural variant, known as no effect on protein levels;, features a modification of the amino acid from V to E at position 475.
+The protein's natural variant, known as in MMRCS4 and LYNCH4; unknown pathological significance; normal DNA mismatch repair activity;, features a modification of the amino acid from H to Q at position 479.
+The protein's natural variant, known as normal DNA mismatch repair activity;, features a modification of the amino acid from T to K at position 485.
+The protein's natural variant, known as in MMRCS4; unknown pathological significance; normal DNA mismatch repair activity;, features a modification of the amino acid from A to V at position 488.
+The protein's natural variant, known as in MMRCS4; unknown pathological significance; normal DNA mismatch repair activity;, features a modification of the amino acid from E to Q at position 504.
+The protein's natural variant, known as normal DNA mismatch repair activity;, features a modification of the amino acid from T to A at position 511.
+The protein's natural variant, known as normal DNA mismatch repair activity;, features a modification of the amino acid from T to M at position 511.
+The protein's natural variant, known as normal DNA mismatch repair activity;, features a modification of the amino acid from K to E at position 541.
+The protein's natural variant, known as normal DNA mismatch repair activity;, features a modification of the amino acid from R to L at position 563.
+The protein's natural variant, known as normal DNA mismatch repair activity;, features a modification of the amino acid from L to I at position 571.
+The protein's natural variant, known as in MMRCS4 and LYNCH4; unknown pathological significance; normal DNA mismatch repair activity;, features a modification of the amino acid from L to I at position 585.
+The protein's natural variant, known as normal DNA mismatch repair activity; significantly reduced interaction with MLH1;, features a modification of the amino acid from T to S at position 597.
+The protein's natural variant, known as in LYNCH4; unknown pathological significance; significantly reduced interaction with MLH1; normal DNA mismatch repair activity;, features a modification of the amino acid from M to I at position 622.
+The protein's natural variant, known as in LYNCH4; unknown pathological significance; normal DNA mismatch repair activity;, features a modification of the amino acid from E to A at position 663.
+The protein's natural variant, known as no effect on protein levels; decreased DNA mismatch repair activity in an in vitro assay;, features a modification of the amino acid from D to H at position 699.
+The protein's natural variant, known as in MMRCS4 and LYNCH4; decreased DNA mismatch repair activity; decreased protein stability;, features a modification of the amino acid from E to K at position 705.
+The protein's natural variant, known as in LYNCH4; unknown pathological significance; decreased DNA mismatch repair activity;, features a modification of the amino acid from G to D at position 750.
+The protein's natural variant, known as normal DNA mismatch repair activity;, features a modification of the amino acid from N to S at position 775.
+The protein's natural variant, known as increased DNA mismatch repair activity in an in vitro assay; no effect on protein stability;, features a modification of the amino acid from G to R at position 779.
+The protein's natural variant, known as no effect on protein levels;, features a modification of the amino acid from D to N at position 792.
+The protein's natural variant, known as in LYNCH4; unknown pathological significance; normal DNA mismatch repair activity;, features a modification of the amino acid from M to R at position 797.
+The protein's natural variant, known as increased DNA mismatch repair activity in an in vitro assay; no effect on protein stability;, features a modification of the amino acid from R to Q at position 799.
+The protein's natural variant, known as in MMRCS4; decreased DNA mismatch repair activity;, features a modification of the amino acid from S to L at position 815.
+The protein's natural variant, known as may affect protein stability, no effect on DNA mismatch repair activity in an in vitro assay, compared to wild-type;, features a modification of the amino acid from V to E at position 816.
+The protein's natural variant, known as in LYNCH4; decreased DNA mismatch repair activity;, features a modification of the amino acid from C to Y at position 843.
+The protein's natural variant, known as no effect on protein levels;, features a modification of the amino acid from I to M at position 853.
+The protein's natural variant, known as normal DNA mismatch repair activity;, features a modification of the amino acid from G to A at position 857.
+The protein's natural variant, known as in BDPLT15; the mutation dominantly affects the actin filament assembly likely resulting in abnormal cytoskeletal organization;, features a modification of the amino acid from Q to K at position 32.
+The protein's natural variant, known as in BDPLT15; disorganization of the actin and alpha-actinin 1 filaments;, features a modification of the amino acid from R to Q at position 46.
+The protein's natural variant, known as in BDPLT15; the mutation dominantly affects the actin filament assembly likely resulting in abnormal cytoskeletal organization;, features a modification of the amino acid from V to I at position 105.
+The protein's natural variant, known as in BDPLT15;, features a modification of the amino acid from E to K at position 225.
+The protein's natural variant, known as in BDPLT15;, features a modification of the amino acid from R to W at position 738.
+The protein's natural variant, known as in BDPLT15;, features a modification of the amino acid from R to Q at position 752.
+The protein's natural variant, known as found in a renal cell carcinoma sample; somatic mutation, features a modification of the amino acid from D to G at position 390.
+The protein's natural variant, known as in EDSSPD2; no effect on Golgi apparatus subcellular localization;, features a modification of the amino acid from R to W at position 6.
+The protein's natural variant, known as in SEMDJL1; decreased galactosylxylosylprotein 3-beta-galactosyltransferase activity; decreased localization to the Golgi apparatus;, features a modification of the amino acid from S to G at position 65.
+The protein's natural variant, known as in SEMDJL1; loss of galactosylxylosylprotein 3-beta-galactosyltransferase activity; decreased localization to the Golgi apparatus;, features a modification of the amino acid from P to L at position 67.
+The protein's natural variant, known as in SEMDJL1; decreased localization to the Golgi apparatus, features a modification of the amino acid from T to A at position 79.
+The protein's natural variant, known as in SEMDJL1; loss of galactosylxylosylprotein 3-beta-galactosyltransferase activity; normal Golgi apparatus subcellular localization;, features a modification of the amino acid from D to N at position 156.
+The protein's natural variant, known as in ALGAZ; unknown pathological significance; normal Golgi apparatus subcellular localization, features a modification of the amino acid from S to Y at position 159.
+The protein's natural variant, known as in EDSSPD2; unknown pathological significance;, features a modification of the amino acid from Y to C at position 182.
+The protein's natural variant, known as in SEMDJL1; also found in patients with EDSSPD2; decreased localization to the Golgi apparatus;, features a modification of the amino acid from F to L at position 186.
+The protein's natural variant, known as in ALGAZ; normal Golgi apparatus subcellular localization; proteoglycans maturation altered;, features a modification of the amino acid from C to W at position 206.
+The protein's natural variant, known as in SEMDJL1; normal Golgi apparatus subcellular localization;, features a modification of the amino acid from D to H at position 207.
+The protein's natural variant, known as in SEMDJL1; normal Golgi apparatus subcellular localization;, features a modification of the amino acid from G to S at position 217.
+The protein's natural variant, known as in SEMDJL1; the activity of the enzyme is significantly decreased; decreased localization to the Golgi apparatus;, features a modification of the amino acid from R to C at position 232.
+The protein's natural variant, known as in SEMDJL1; decreased localization to the Golgi apparatus;, features a modification of the amino acid from R to W at position 256.
+The protein's natural variant, known as in ALGAZ; unknown pathological significance; normal Golgi apparatus subcellular localization;, features a modification of the amino acid from E to D at position 265.
+The protein's natural variant, known as in SEMDJL1; loss of galactosylxylosylprotein 3-beta-galactosyltransferase activity; normal Golgi apparatus subcellular localization;, features a modification of the amino acid from C to S at position 300.
+The protein's natural variant, known as in EDSSPD2; normal Golgi apparatus subcellular localization;, features a modification of the amino acid from S to T at position 309.
+The protein's natural variant, known as in NEDBAF;, features a modification of the amino acid from P to L at position 29.
+The protein's natural variant, known as in NEDBAF;, features a modification of the amino acid from A to G at position 59.
+The protein's natural variant, known as in NEDBAF;, features a modification of the amino acid from Q to L at position 61.
+The protein's natural variant, known as in NEDBAF;, features a modification of the amino acid from E to K at position 62.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to C at position 642.
+The protein's natural variant, known as in KEL24 antigen;, features a modification of the amino acid from R to P at position 180.
+The protein's natural variant, known as in KEL1/K antigen;, features a modification of the amino acid from T to M at position 193.
+The protein's natural variant, known as in KEL25 antigen;, features a modification of the amino acid from R to Q at position 248.
+The protein's natural variant, known as in KEL27 antigen;, features a modification of the amino acid from E to K at position 249.
+The protein's natural variant, known as in KEL21/Kp(c) antigen;, features a modification of the amino acid from R to Q at position 281.
+The protein's natural variant, known as in KEL3/Kp(a) antigen;, features a modification of the amino acid from R to W at position 281.
+The protein's natural variant, known as in KEL17 antigen;, features a modification of the amino acid from V to A at position 302.
+The protein's natural variant, known as in KEL22 antigen;, features a modification of the amino acid from A to V at position 322.
+The protein's natural variant, known as in KEL23 antigen;, features a modification of the amino acid from Q to R at position 382.
+The protein's natural variant, known as in KEL26 antigen;, features a modification of the amino acid from R to Q at position 406.
+The protein's natural variant, known as in KEL19 antigen;, features a modification of the amino acid from R to Q at position 492.
+The protein's natural variant, known as in KEL10/Ul(a) antigen;, features a modification of the amino acid from E to V at position 494.
+The protein's natural variant, known as in KEL12 antigen;, features a modification of the amino acid from H to R at position 548.
+The protein's natural variant, known as in KEL6/Js(a) antigen;, features a modification of the amino acid from L to P at position 597.
+The protein's natural variant, known as in strain: Isolate G30, features a modification of the amino acid from P to S at position 266.
+The protein's natural variant, known as in CDAN3B; decreased function in erythropoiesis as shown by partial rescue of multinucleation defects in RACGAP1-deficient erythroid cells; decreased GAP activity towards RHOA, RAC1 and CDC42, features a modification of the amino acid from L to Q at position 396.
+The protein's natural variant, known as in CDAN3B; loss of function in erythropoiesis as it does not rescue multinucleation and cytokinesis defects in RACGAP1-deficient erythroid and Hela cells; increased GAP activity towards RHOA; no effect on GAP activity towards RAC1 and CDC42, features a modification of the amino acid from P to S at position 432.
+The protein's natural variant, known as in strain: CT45, features a modification of the amino acid from V to G at position 31.
+The protein's natural variant, known as in strain: CT42, features a modification of the amino acid from E to D at position 206.
+The protein's natural variant, known as in strain: CT27, features a modification of the amino acid from A to E at position 300.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation, features a modification of the amino acid from S to P at position 1194.
+The protein's natural variant, known as in strain: PAK, features a modification of the amino acid from V to A at position 116.
+The protein's natural variant, known as in strain: PAK and 170018, features a modification of the amino acid from T to A at position 280.
+The protein's natural variant, known as in strain: 5939, features a modification of the amino acid from F to I at position 332.
+The protein's natural variant, known as in Z-Wrexham, features a modification of the amino acid from S to L at position 4.
+The protein's natural variant, known as in V-Munich;, features a modification of the amino acid from D to A at position 26.
+The protein's natural variant, known as in M5-Karlsruhe;, features a modification of the amino acid from A to T at position 58.
+The protein's natural variant, known as in I;, features a modification of the amino acid from R to C at position 63.
+The protein's natural variant, known as in M-Procida;, features a modification of the amino acid from L to P at position 65.
+The protein's natural variant, known as in M6-Bonn;, features a modification of the amino acid from S to F at position 69.
+The protein's natural variant, known as in S-Iiyama;, features a modification of the amino acid from S to F at position 77.
+The protein's natural variant, known as in M6-Passau;, features a modification of the amino acid from A to T at position 84.
+The protein's natural variant, known as in M-Mineral springs; causes reduced AAT secretion;, features a modification of the amino acid from G to E at position 91.
+The protein's natural variant, known as in QO-Lisbon; deficient AAT with very low serum levels;, features a modification of the amino acid from T to I at position 92.
+The protein's natural variant, known as in Z-Bristol; deficient AA; disrupts the N-glycosylation site N-107;, features a modification of the amino acid from T to M at position 109.
+The protein's natural variant, known as in M5-Berlin;, features a modification of the amino acid from P to T at position 112.
+The protein's natural variant, known as in QO-Ludwigshafen;, features a modification of the amino acid from I to N at position 116.
+The protein's natural variant, known as in M2; associated with D-400;, features a modification of the amino acid from R to H at position 125.
+The protein's natural variant, known as in QO-Newport;, features a modification of the amino acid from G to S at position 139.
+The protein's natural variant, known as in V and M-Nichinan;, features a modification of the amino acid from G to R at position 172.
+The protein's natural variant, known as in M2-Obernburg;, features a modification of the amino acid from G to W at position 172.
+The protein's natural variant, known as in L-Frankfurt;, features a modification of the amino acid from Q to E at position 180.
+The protein's natural variant, known as in Aberrant form, features a modification of the amino acid from QGKIVDLVK to GFQNAILVR at position 198.
+The protein's natural variant, known as in X;, features a modification of the amino acid from E to K at position 228.
+The protein's natural variant, known as in M1A and Z; associated with K-366 in Z;, features a modification of the amino acid from V to A at position 237.
+The protein's natural variant, known as in F;, features a modification of the amino acid from R to C at position 247.
+The protein's natural variant, known as in P-Duarte/P-Cardiff/P-Lowell; associated with H-415 in Y-Barcelona;, features a modification of the amino acid from D to V at position 280.
+The protein's natural variant, known as in S and T;, features a modification of the amino acid from E to V at position 288.
+The protein's natural variant, known as in S-Munich;, features a modification of the amino acid from S to F at position 354.
+The protein's natural variant, known as in W-Bethesda;, features a modification of the amino acid from A to T at position 360.
+The protein's natural variant, known as in P-St.Albans/P-Donauwoerth;, features a modification of the amino acid from D to N at position 365.
+The protein's natural variant, known as in Z/Z-Augsburg/Z-Tun; associated with A-237 in Z;, features a modification of the amino acid from E to K at position 366.
+The protein's natural variant, known as in Pittsburgh; has antithrombin activity; inhibits factor VIIa activity; causes fatal bleeding diathesis;, features a modification of the amino acid from M to R at position 382.
+The protein's natural variant, known as in Sao Tome;, features a modification of the amino acid from P to H at position 386.
+The protein's natural variant, known as in L-Offenbach;, features a modification of the amino acid from P to T at position 386.
+The protein's natural variant, known as in Christchurch;, features a modification of the amino acid from E to K at position 387.
+The protein's natural variant, known as in M-Heerlen;, features a modification of the amino acid from P to L at position 393.
+The protein's natural variant, known as in M2 and M3; associated with H-125 in M2;, features a modification of the amino acid from E to D at position 400.
+The protein's natural variant, known as in Y-Barcelona; associated with V-280, features a modification of the amino acid from P to H at position 415.
+The protein's natural variant, known as probable disease-associated variant found in a patient with moderate intellectual disability and epilepsy, features a modification of the amino acid from G to S at position 199.
+The natural variant of this protein is characterized by an amino acid alteration from S to V at position 6.
+The natural variant of this protein is characterized by an amino acid alteration from Y to C at position 39.
+The natural variant of this protein is characterized by an amino acid alteration from I to F at position 60.
+The natural variant of this protein is characterized by an amino acid alteration from F to C at position 76.
+The natural variant of this protein is characterized by an amino acid alteration from F to S at position 78.
+The natural variant of this protein is characterized by an amino acid alteration from C to G at position 79.
+The protein's natural variant, known as in one of the major forms, features a modification of the amino acid from K to T at position 36.
+The natural variant of this protein is characterized by an amino acid alteration from T to A at position 2.
+The protein's natural variant, known as in strain: Isolate specimen 1580, features a modification of the amino acid from R to L at position 3.
+The protein's natural variant, known as in strain: Isolate specimen 1580, features a modification of the amino acid from A to S at position 8.
+The protein's natural variant, known as in strain: F428; produces a 2 to 3 times higher enzyme activity, features a modification of the amino acid from T to I at position 190.
+The protein's natural variant, known as in CIMDAG; unknown pathological significance;, features a modification of the amino acid from A to V at position 28.
+The protein's natural variant, known as in CIMDAG; patient peripheral red blood cells show abnormal CD71 expression indicating defective endosomal trafficking;, features a modification of the amino acid from G to E at position 203.
+The protein's natural variant, known as in CIMDAG, features a modification of the amino acid from E to K at position 206.
+The protein's natural variant, known as in CIMDAG; has a dominant negative effect on the regulation of endosomal size resulting in enlarged endosomal vacuoles; patient cells also have abnormal nuclear envelope morphology and primary cilium defects; no effect on protein abundance in patient cells, features a modification of the amino acid from R to G at position 284.
+The protein's natural variant, known as in CIMDAG; has a dominant negative effect on the regulation of endosomal size resulting in enlarged endosomal vacuoles; patient cells also have abnormal nuclear envelope morphology and primary cilium defects; no effect on protein abundance in patient cells; patient-derived induced erythroblasts show defective cytokinesis, features a modification of the amino acid from R to W at position 284.
+The protein's natural variant, known as found in a patient with non-specific intellectual disability; unknown pathological significance, features a modification of the amino acid from I to V at position 337.
+The protein's natural variant, known as in MOCODB;, features a modification of the amino acid from E to K at position 168.
+The protein's natural variant, known as in FPS;, features a modification of the amino acid from R to C at position 217.
+The protein's natural variant, known as in FPS; no effect on protein abundance; no effect on localization to the mitochondrion; altered mitochondrial ATP transport; increased sensitivity to oxidative stress that leads to mitochondrial swelling;, features a modification of the amino acid from R to H at position 217.
+The protein's natural variant, known as in CDG2O;, features a modification of the amino acid from D to Y at position 11.
+The protein's natural variant, known as in CDG2O;, features a modification of the amino acid from L to S at position 31.
+The protein's natural variant, known as in MCPH27; increased aggregation; changed nuclear envelope organization, features a modification of the amino acid from N to H at position 54.
+The protein's natural variant, known as in EPM9; disrupts fibrillar formation;, features a modification of the amino acid from H to Y at position 157.
+The protein's natural variant, known as may be a risk factor for partial acquired lipodystrophy;, features a modification of the amino acid from R to Q at position 235.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to W at position 236.
+The protein's natural variant, known as in APLD, features a modification of the amino acid from Y to H at position 252.
+The protein's natural variant, known as in MCPH27; increased aggregation; changed nuclear envelope organization;, features a modification of the amino acid from E to K at position 398.
+The protein's natural variant, known as in APLD;, features a modification of the amino acid from A to T at position 427.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from P to L at position 77.
+The protein's natural variant, known as in KNO2; loss of protein serine/threonine kinase activity, features a modification of the amino acid from E to K at position 435.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to H at position 144.
+The protein's natural variant, known as in allele GPDH-ACYG22, features a modification of the amino acid from N to Y at position 14.
+The protein's natural variant, known as in allele GPDH-ACB62, features a modification of the amino acid from C to G at position 266.
+The protein's natural variant, known as in allele GPDH-ACYG22, features a modification of the amino acid from R to C at position 273.
+The protein's natural variant, known as in allele GPDH-AT198, allele GPDH-ACB62 and allele GPDH-S, features a modification of the amino acid from N to K at position 337.
+The protein's natural variant, known as in LCWM; the loss of a disulfide bond may affect protein folding and stability; the protein is retained in the endoplasmic reticulum and the mitochondria while lysosomal localization is disrupted;, features a modification of the amino acid from C to R at position 184.
+The protein's natural variant, known as in alpha-1B;, features a modification of the amino acid from A to V at position 137.
+The protein's natural variant, known as in strain: CLIB 556 and CLIB 630, features a modification of the amino acid from N to K at position 76.
+The protein's natural variant, known as in strain: CLIB 556 and CLIB 630, features a modification of the amino acid from D to N at position 93.
+The protein's natural variant, known as in strain: CLIB 413 haplotype Ha2, features a modification of the amino acid from G to S at position 120.
+The protein's natural variant, known as in strain: R13 haplotype Ha2, features a modification of the amino acid from V to I at position 134.
+The protein's natural variant, known as in strain: YIIc12 haplotype Ha2 and YIIc17, features a modification of the amino acid from R to K at position 318.
+The protein's natural variant, known as in strain: Erdman, features a modification of the amino acid from AAA to PSG at position 114.
+The protein's natural variant, known as in strain: Erdman, features a modification of the amino acid from Q to A at position 116.
+The protein's natural variant, known as in strain: Erdman, features a modification of the amino acid from QH to HD at position 254.
+The protein's natural variant, known as in some molecules, features a modification of the amino acid from V to I at position 228.
+The protein's natural variant, known as in strain: DPF; induces a high-diapause phenotype, features a modification of the amino acid from A to V at position 347.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to W at position 471.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from I to M at position 1085.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from T to P at position 1428.
+The protein's natural variant, known as in ATCAY, features a modification of the amino acid from S to R at position 301.
+The protein's natural variant, known as in CISS2; heterozygous compound with a nonsense mutation; unable to bind CNTFR alpha;, features a modification of the amino acid from R to L at position 197.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from K to N at position 223.
+The protein's natural variant, known as in strain: Barriol, Espro, Padova and Praias, features a modification of the amino acid from G to S at position 97.
+The protein's natural variant, known as in strain: F-744 / L25; beta-carotene overproducing strain, features a modification of the amino acid from P to S at position 143.
+The protein's natural variant, known as in allele TGFBR1*10A, features a modification of the amino acid from A to AA at position 26.
+The protein's natural variant, known as in MSSE; hypomorphic variant, features a modification of the amino acid from C to Y at position 41.
+The protein's natural variant, known as in MSSE; hypomorphic variant;, features a modification of the amino acid from N to S at position 45.
+The protein's natural variant, known as in MSSE; hypomorphic variant;, features a modification of the amino acid from G to R at position 52.
+The protein's natural variant, known as in MSSE; hypomorphic variant;, features a modification of the amino acid from P to L at position 83.
+The protein's natural variant, known as in LDS1;, features a modification of the amino acid from T to I at position 200.
+The protein's natural variant, known as in LDS1, features a modification of the amino acid from K to E at position 232.
+The protein's natural variant, known as in LDS1;, features a modification of the amino acid from S to L at position 241.
+The protein's natural variant, known as in LDS1, features a modification of the amino acid from D to Y at position 266.
+The protein's natural variant, known as in a patient with Marfan syndrome, features a modification of the amino acid from N to H at position 267.
+The protein's natural variant, known as in LDS1;, features a modification of the amino acid from M to R at position 318.
+The protein's natural variant, known as in LDS1, features a modification of the amino acid from D to G at position 351.
+The protein's natural variant, known as in LDS1;, features a modification of the amino acid from T to R at position 375.
+The protein's natural variant, known as in LDS1;, features a modification of the amino acid from D to G at position 400.
+The protein's natural variant, known as in LDS1;, features a modification of the amino acid from R to P at position 487.
+The protein's natural variant, known as in LDS1;, features a modification of the amino acid from R to Q at position 487.
+The protein's natural variant, known as in LDS1;, features a modification of the amino acid from R to W at position 487.
+The protein's natural variant, known as in strain: ECOR 60, features a modification of the amino acid from I to S at position 113.
+The protein's natural variant, known as in strain: ECOR 50, features a modification of the amino acid from E to G at position 283.
+The protein's natural variant, known as in strain: ECOR 16, features a modification of the amino acid from G to S at position 378.
+The protein's natural variant, known as in strain: ECOR 46, features a modification of the amino acid from S to R at position 426.
+The protein's natural variant, known as in clones TR12, TR28 and TR45, features a modification of the amino acid from I to L at position 26.
+The protein's natural variant, known as in clones TR28 and TR45, features a modification of the amino acid from G to D at position 50.
+The protein's natural variant, known as in clone TR45, features a modification of the amino acid from VDNKNG to ADKKND at position 95.
+The protein's natural variant, known as in clones TR12 and TR28, features a modification of the amino acid from G to D at position 95.
+The protein's natural variant, known as in clones TR12, TR28 and TR45, features a modification of the amino acid from S to G at position 104.
+The protein's natural variant, known as in clones TR12 and TR28, features a modification of the amino acid from T to I at position 132.
+The protein's natural variant, known as in clones TR12, TR28 and TR45, features a modification of the amino acid from L to F at position 145.
+The protein's natural variant, known as in clones TR12, TR28 and TR45, features a modification of the amino acid from K to N at position 157.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from A to V at position 719.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from G to V at position 758.
+The natural variant of this protein is characterized by an amino acid alteration from L to S at position 7.
+The natural variant of this protein is characterized by an amino acid alteration from T to I at position 8.
+The protein's natural variant, known as reduced activity, features a modification of the amino acid from D to N at position 15.
+The natural variant of this protein is characterized by an amino acid alteration from M to L at position 113.
+The protein's natural variant, known as reduced activity, features a modification of the amino acid from D to V at position 233.
+The protein's natural variant, known as associated with MODY11; reduces the enhancing effect of BLK on insulin secretion; reduces the inducing effect of BLK on the expression of PDX1 and NKX6-1; found as somatic mutation in a colorectal adenocarcinoma sample;, features a modification of the amino acid from A to T at position 71.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from L to V at position 429.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from R to S at position 97.
+The protein's natural variant, known as in MCPH4; may inactivate an exonic splicing enhancer and result in abnormal splicing;, features a modification of the amino acid from M to I at position 2041.
+The protein's natural variant, known as found in a patient with endometrial cancer; slightly decreased PCNA-binding, features a modification of the amino acid from A to V at position 9.
+The protein's natural variant, known as increased PCNA-binding;, features a modification of the amino acid from Q to K at position 10.
+The protein's natural variant, known as in strain: Isolate FMNH 134296, features a modification of the amino acid from V to I at position 295.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation;, features a modification of the amino acid from P to S at position 217.
+The protein's natural variant, known as in MPYCD;, features a modification of the amino acid from L to H at position 79.
+The protein's natural variant, known as in MPYCD; inactive;, features a modification of the amino acid from R to W at position 97.
+The natural variant of this protein is characterized by an amino acid alteration from R to H at position 290.
+The natural variant of this protein is characterized by an amino acid alteration from C to R at position 531.
+The protein's natural variant, known as in POF10; inhibits protein recruitment to sites of DNA damage; shows significant reduction in DNA-binding affinity for single-strand DNA;, features a modification of the amino acid from P to R at position 149.
+The protein's natural variant, known as decreases the formation of MRE11 and RPA1 foci in response to cisplatin-induced DNA damage;, features a modification of the amino acid from E to K at position 341.
+The protein's natural variant, known as associated significantly with GBD4;, features a modification of the amino acid from D to H at position 19.
+The protein's natural variant, known as in STSL1; strongly decreased maturation of glycan chains;, features a modification of the amino acid from R to H at position 184.
+The protein's natural variant, known as in STSL1; strongly decreased maturation of glycan chains;, features a modification of the amino acid from P to T at position 231.
+The protein's natural variant, known as in STSL1; unknown pathological significance;, features a modification of the amino acid from E to K at position 238.
+The protein's natural variant, known as in STSL1; strongly decreased maturation of glycan chains;, features a modification of the amino acid from R to Q at position 263.
+The protein's natural variant, known as in STSL1;, features a modification of the amino acid from R to H at position 405.
+The protein's natural variant, known as in STSL1; strongly decreased maturation of glycan chains;, features a modification of the amino acid from L to P at position 501.
+The protein's natural variant, known as in STSL1; decreased maturation of glycan chains;, features a modification of the amino acid from R to S at position 543.
+The protein's natural variant, known as in STSL1;, features a modification of the amino acid from L to P at position 572.
+The protein's natural variant, known as in STSL1; strongly decreased maturation of glycan chains;, features a modification of the amino acid from G to E at position 574.
+The protein's natural variant, known as in STSL1; decreased maturation of glycan chains;, features a modification of the amino acid from G to R at position 574.
+The natural variant of this protein is characterized by an amino acid alteration from G to R at position 575.
+The protein's natural variant, known as in STSL1; strongly decreased maturation of glycan chains;, features a modification of the amino acid from L to R at position 596.
+The protein's natural variant, known as in ABL; no loss on localization to the endoplasmic reticulum; does not reduce interaction with APOB; inhibits interaction with P4HB/PDI; inhibits phospholipid or triglyceride transfer activity; inhibits apolipoprotein B secretion, features a modification of the amino acid from D to V at position 169.
+The protein's natural variant, known as in ABL; unknown pathological significance; does not reduce interaction with P4HB/PDI and APOB; does not reduce triglyceride transfer activity;, features a modification of the amino acid from G to R at position 264.
+The protein's natural variant, known as does not inhibit apolipoprotein B secretion;, features a modification of the amino acid from H to Q at position 297.
+The protein's natural variant, known as no loss on localization to the endoplasmic reticulum; does not reduce interaction with P4HB/PDI; reduces phospholipid or triglyceride transfer activity; does not inhibit apolipoprotein B secretion;, features a modification of the amino acid from D to A at position 384.
+The protein's natural variant, known as in ABL; no loss on localization to the endoplasmic reticulum; inhibits triglyceride transfer activity, features a modification of the amino acid from L to H at position 435.
+The protein's natural variant, known as in ABL; does not reduce interaction with P4HB/PDI and APOB; inhibits triglyceride transfer activity;, features a modification of the amino acid from Y to H at position 528.
+The protein's natural variant, known as in ABL; does not reduce interaction with P4HB/PDI and APOB; inhibits triglyceride transfer activity;, features a modification of the amino acid from R to C at position 540.
+The protein's natural variant, known as in ABL; no loss on localization to the endoplasmic reticulum; reduces interaction with P4HB/PDI; inhibits phospholipid or triglyceride transfer activity; inhibits apolipoprotein B secretion;, features a modification of the amino acid from R to H at position 540.
+The protein's natural variant, known as in ABL; no loss on localization to the endoplasmic reticulum; does not reduce interaction with P4HB/PDI; inhibits phospholipid or triglyceride transfer activity; inhibits apolipoprotein B secretion;, features a modification of the amino acid from S to I at position 590.
+The protein's natural variant, known as in ABL; unknown pathological significance; does not reduce interaction with P4HB/PDI and APOB; reduces triglyceride transfer activity, features a modification of the amino acid from N to S at position 649.
+The protein's natural variant, known as in ABL; no loss on localization to the endoplasmic reticulum; does not reduce interaction with P4HB/PDI; inhibits phospholipid or triglyceride transfer activity; inhibits apolipoprotein B secretion;, features a modification of the amino acid from G to E at position 746.
+The protein's natural variant, known as in ABL; no loss on localization to the endoplasmic reticulum; does not reduce interaction with P4HB/PDI; inhibits phospholipid or triglyceride transfer activity; inhibits apolipoprotein B secretion;, features a modification of the amino acid from N to Y at position 780.
+The natural variant of this protein is characterized by an amino acid alteration from V to F at position 99.
+The protein's natural variant, known as in variant C, features a modification of the amino acid from G to E at position 79.
+The protein's natural variant, known as in hsca1, features a modification of the amino acid from S to F at position 216.
+The natural variant of this protein is characterized by an amino acid alteration from G to D at position 835.
+The protein's natural variant, known as decreased sulfate assimilation;, features a modification of the amino acid from E to K at position 10.
+The protein's natural variant, known as in BCYM4; reduced 3'-phosphoadenosine 5'-phosphosulfate biosynthetic process, features a modification of the amino acid from C to Y at position 43.
+The protein's natural variant, known as in BCYM4; patient with premature pubarche and hyperandrogenism; decreased sulfate assimilation; increases ubiquitin-dependent protein instability;, features a modification of the amino acid from T to R at position 48.
+The protein's natural variant, known as in BCYM4; reduced 3'-phosphoadenosine 5'-phosphosulfate biosynthetic process, features a modification of the amino acid from L to Q at position 76.
+The protein's natural variant, known as no effect on 3'-phosphoadenosine 5'-phosphosulfate biosynthetic process;, features a modification of the amino acid from E to K at position 183.
+The protein's natural variant, known as in BCYM4; increases ubiquitin-dependent protein instability;, features a modification of the amino acid from G to D at position 270.
+The protein's natural variant, known as decreased sulfate assimilation;, features a modification of the amino acid from V to M at position 291.
+The protein's natural variant, known as in strain: ATCC 6633, features a modification of the amino acid from F to L at position 7.
+The protein's natural variant, known as in strain: ATCC 6633, features a modification of the amino acid from N to H at position 37.
+The protein's natural variant, known as in strain: ATCC 6633, features a modification of the amino acid from R to Q at position 39.
+The protein's natural variant, known as in strain: ATCC 6633, features a modification of the amino acid from I to M at position 187.
+The protein's natural variant, known as in strain: ATCC 6633, features a modification of the amino acid from E to T at position 221.
+The protein's natural variant, known as in strain: ATCC 6633, features a modification of the amino acid from V to L at position 224.
+The protein's natural variant, known as in strain: ATCC 6633, features a modification of the amino acid from Q to K at position 229.
+The protein's natural variant, known as in strain: ATCC 6633, features a modification of the amino acid from KV to EI at position 236.
+The natural variant of this protein is characterized by an amino acid alteration from G to V at position 1276.
+The natural variant of this protein is characterized by an amino acid alteration from P to S at position 519.
+The protein's natural variant, known as in strain: Oregon-R, features a modification of the amino acid from M to T at position 4.
+The protein's natural variant, known as in strain: Berkeley and Oregon-R, features a modification of the amino acid from H to Q at position 131.
+The protein's natural variant, known as in strain: Oregon-R, features a modification of the amino acid from SG to TR at position 159.
+The protein's natural variant, known as in strain: Oregon-R, features a modification of the amino acid from EL to DV at position 305.
+The protein's natural variant, known as in WS4B;, features a modification of the amino acid from Y to C at position 127.
+The protein's natural variant, known as in WS4B;, features a modification of the amino acid from C to F at position 159.
+The protein's natural variant, known as in HSCR4; risk factor associated with disease susceptibility;, features a modification of the amino acid from A to T at position 224.
+The natural variant of this protein is characterized by an amino acid alteration from A to V at position 438.
+The protein's natural variant, known as in ISDNA; changed glycosaminoglycan synthesis;, features a modification of the amino acid from R to W at position 339.
+The protein's natural variant, known as in ISDNA; changed glycosaminoglycan synthesis;, features a modification of the amino acid from P to L at position 461.
+The protein's natural variant, known as in ISDNA; changed glycosaminoglycan synthesis; no localization to Golgi apparatus in patient fibroblasts;, features a modification of the amino acid from R to C at position 513.
+The protein's natural variant, known as found in a small consanguineous family with intellectual disability; unknown pathological significance, features a modification of the amino acid from S to C at position 646.
+The protein's natural variant, known as in ISDNA; changed glycosaminoglycan synthesis;, features a modification of the amino acid from N to S at position 657.
+The protein's natural variant, known as in ISDNA; changed glycosaminoglycan synthesis, features a modification of the amino acid from Y to D at position 670.
+The protein's natural variant, known as in a lung large cell carcinoma sample; somatic mutation;, features a modification of the amino acid from R to W at position 670.
+The protein's natural variant, known as in strain: UVM 9-4, features a modification of the amino acid from E to G at position 572.
+The protein's natural variant, known as in strain: UVM 9-1 and CBS 340.81 / UVM 4-40, features a modification of the amino acid from Q to E at position 651.
+The protein's natural variant, known as in strain: UVM 9-1 and CBS 340.81 / UVM 4-40, features a modification of the amino acid from K to E at position 659.
+The protein's natural variant, known as in strain: UVM 9-1, features a modification of the amino acid from R to Q at position 729.
+The protein's natural variant, known as in strain: SFS 3.4, features a modification of the amino acid from N to S at position 39.
+The protein's natural variant, known as in strain: Canton-S, NFS 5.1, NFS 5.2, NFS 5.3, NFS 5.4, NFS 6.1, NFS 6.2, NFS 6.3, NFS 6.4, NFS 7.8, SFS 1.1, SFS 1.2, SFS 1.3, SFS 1.4, SFS 2.2, SFS 2.3, SFS 2.4, SFS 3.1, SFS 3.2, SFS 3.3, SFS 3.4, Zim63H-12C, Zim63H-16C, Zim63H-28C, Zim63H-34C, Zim63I-10C, Zim63I-18C, Zim63I-53C and Zim63I-7C, features a modification of the amino acid from K to N at position 49.
+The protein's natural variant, known as in strain: Zim63H-16C, Zim63H-34C and Zim63I-7C, features a modification of the amino acid from L to V at position 72.
+The protein's natural variant, known as in strain: Zim63H-30C, features a modification of the amino acid from HG to MA at position 74.
+The protein's natural variant, known as in strain: Zim63H-16C and Zim63H-34C, features a modification of the amino acid from H to Q at position 73.
+The protein's natural variant, known as in strain: Zim63H-16C, features a modification of the amino acid from K to E at position 75.
+The protein's natural variant, known as in strain: Zim63I-7C, features a modification of the amino acid from P to T at position 76.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from A to T at position 315.
+The protein's natural variant, known as in A and A', features a modification of the amino acid from I to T at position 72.
+The protein's natural variant, known as in A, features a modification of the amino acid from EA to DG at position 93.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from G to D at position 37.
+The protein's natural variant, known as in strain: ECOR 46, ECOR 48, ECOR 49 and O2:HN / ECOR 50 / P97 / UPEC, features a modification of the amino acid from N to D at position 11.
+The protein's natural variant, known as in strain: ECOR 53, ECOR 59 and ECOR 60, features a modification of the amino acid from D to N at position 14.
+The protein's natural variant, known as in strain: ECOR 23, ECOR 32, ECOR 38, ECOR 39, ECOR 40, ECOR 41, ECOR 51, ECOR 52, ECOR 54, ECOR 55, ECOR 56, ECOR 57, ECOR 61, ECOR 62, ECOR 63, ECOR 64, ECOR 65 and ECOR 66, features a modification of the amino acid from L to I at position 19.
+The protein's natural variant, known as in strain: ECOR 46, ECOR 49 and O2:HN / ECOR 50 / P97 / UPEC, features a modification of the amino acid from M to K at position 20.
+The protein's natural variant, known as in strain: ECOR 46, ECOR 48, ECOR 49 and O2:HN / ECOR 50 / P97 / UPEC, features a modification of the amino acid from A to T at position 27.
+The protein's natural variant, known as in strain: ECOR 38, ECOR 39, ECOR 41, ECOR 51, ECOR 52, ECOR 53, ECOR 54, ECOR 55, ECOR 56, ECOR 61, ECOR 63, ECOR 64, ECOR 65 and ECOR 66, features a modification of the amino acid from S to C at position 71.
+The protein's natural variant, known as in strain: ECOR 53, ECOR 59 and ECOR 60, features a modification of the amino acid from C to S at position 81.
+The protein's natural variant, known as in strain: ECOR 26, ECOR 27, ECOR 29, ECOR 30, ECOR 33, ECOR 44, ECOR 45, ECOR 47, ECOR 58, ECOR 67, ECOR 68, ECOR 69 and ECOR 71, features a modification of the amino acid from K to T at position 82.
+The protein's natural variant, known as in strain: ECOR 27, ECOR 33, ECOR 38, ECOR 39, ECOR 41, ECOR 44, ECOR 45, ECOR 47, ECOR 51, ECOR 52, ECOR 53, ECOR 54, ECOR 55, ECOR 56, ECOR 57, ECOR 59, ECOR 60, ECOR 61, ECOR 63, ECOR 64, ECOR 65, ECOR 66 and ECOR 69, features a modification of the amino acid from V to A at position 83.
+The protein's natural variant, known as in strain: ECOR 28 and ECOR 30, features a modification of the amino acid from A to E at position 84.
+The natural variant of this protein is characterized by an amino acid alteration from K to R at position 124.
+The natural variant of this protein is characterized by an amino acid alteration from D to N at position 149.
+The natural variant of this protein is characterized by an amino acid alteration from T to A at position 248.
+The protein's natural variant, known as reduced infection with flaviviruses such as Yellow fever virus, Zika virus and Dengue virus; no effect on mobilization of neutral lipids from lipid droplets, features a modification of the amino acid from I to L at position 266.
+The protein's natural variant, known as reduced infection with Yellow fever virus, Zika virus and Dengue virus; no effect on mobilization of neutral lipids from lipid droplets, features a modification of the amino acid from I to V at position 266.
+The protein's natural variant, known as in strain: CE3, features a modification of the amino acid from GV to VA at position 12.
+The protein's natural variant, known as in strain: CE3, features a modification of the amino acid from W to C at position 43.
+The protein's natural variant, known as in strain: CE3, features a modification of the amino acid from IG to DP at position 46.
+The protein's natural variant, known as in strain: CE3, features a modification of the amino acid from DA to EP at position 248.
+The protein's natural variant, known as in strain: CE3, features a modification of the amino acid from I to N at position 278.
+The protein's natural variant, known as in strain: CE3, features a modification of the amino acid from AL to RF at position 283.
+The protein's natural variant, known as in strain: cv. Metz-0, features a modification of the amino acid from D to G at position 148.
+The protein's natural variant, known as in strain: cv. Kl-0, features a modification of the amino acid from T to I at position 196.
+The protein's natural variant, known as in strain: cv. No-0, features a modification of the amino acid from A to T at position 198.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, cv. No-0 and cv. RLD, features a modification of the amino acid from D to V at position 560.
+The protein's natural variant, known as in strain: cv. Nd-1, Nd-0 and cv. Kl-0, features a modification of the amino acid from F to C at position 604.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from G to K at position 298.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from D to A at position 300.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from AI to TL at position 303.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from S to R at position 306.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from D to E at position 309.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from V to L at position 320.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from GD to EE at position 325.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from H to D at position 329.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from LA to VV at position 338.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from R to H at position 341.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from K to Q at position 356.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from L to V at position 358.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from T to S at position 369.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from R to C at position 388.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from V to S at position 391.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from AAG to GVD at position 408.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from A to R at position 411.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from V to A at position 413.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from H to K at position 417.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from S to P at position 424.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from T to A at position 436.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from T to V at position 442.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from A to E at position 456.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from E to R at position 459.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from LM to FL at position 462.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from T to V at position 475.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from AG to SS at position 483.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from N to E at position 487.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from T to A at position 491.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from A to K at position 505.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from T to R at position 508.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from Q to K at position 510.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from QA to GT at position 513.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from R to Q at position 516.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from TV to VI at position 537.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from D to E at position 540.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from H to Y at position 567.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from H to N at position 573.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from H to R at position 596.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from V to D at position 598.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from G to K at position 600.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from M to I at position 605.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from V to T at position 619.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from P to S at position 645.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from I to M at position 672.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from G to D at position 678.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from H to Q at position 691.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from ED to DE at position 696.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from A to P at position 699.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from T to S at position 728.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from A to E at position 741.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from Q to R at position 748.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from D to E at position 751.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from T to M at position 790.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from SV to NA at position 813.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from R to K at position 816.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from I to M at position 841.
+The protein's natural variant, known as in strain: X, features a modification of the amino acid from P to S at position 870.
+The protein's natural variant, known as in allele b', features a modification of the amino acid from A to T at position 39.
+The protein's natural variant, known as in allele b', features a modification of the amino acid from S to G at position 42.
+The protein's natural variant, known as in allele b', features a modification of the amino acid from E to D at position 45.
+The protein's natural variant, known as in allele b', features a modification of the amino acid from M to I at position 95.
+The protein's natural variant, known as in allele b', features a modification of the amino acid from V to A at position 136.
+The protein's natural variant, known as in allele b', features a modification of the amino acid from V to I at position 139.
+The protein's natural variant, known as in allele b', features a modification of the amino acid from G to A at position 152.
+The protein's natural variant, known as in strain: ZW141 and ZW142, features a modification of the amino acid from D to E at position 252.
+The protein's natural variant, known as in strain: ZW106 and ZW133, features a modification of the amino acid from I to K at position 262.
+The protein's natural variant, known as in strain: ZW104, ZW141 and ZW143, features a modification of the amino acid from I to N at position 262.
+The protein's natural variant, known as in strain: ZW104, ZW106, ZW122, ZW133, ZW136, ZW139, ZW140, ZW141, ZW142 and ZW143, features a modification of the amino acid from C to G at position 268.
+The protein's natural variant, known as in strain: ZW122 and ZW136, features a modification of the amino acid from E to K at position 332.
+The protein's natural variant, known as in ATRAF;, features a modification of the amino acid from D to N at position 77.
+The protein's natural variant, known as in allele TF*C3; associated with a reduction in total iron binding capacity; risk factor for iron deficiency anemia in menstruating white women;, features a modification of the amino acid from G to S at position 277.
+The protein's natural variant, known as in allele TF*D1;, features a modification of the amino acid from D to G at position 296.
+The protein's natural variant, known as in allele TF*CHI;, features a modification of the amino acid from H to R at position 319.
+The protein's natural variant, known as in ATRAF;, features a modification of the amino acid from A to P at position 477.
+The protein's natural variant, known as in allele TF*C2;, features a modification of the amino acid from P to S at position 589.
+The protein's natural variant, known as in allele TF*BV;, features a modification of the amino acid from K to E at position 646.
+The protein's natural variant, known as in allele TF*B2;, features a modification of the amino acid from G to E at position 671.
+The protein's natural variant, known as in rfm2103; rifampicin resistant, features a modification of the amino acid from H to Y at position 482.
+The protein's natural variant, known as in strain: Isolate NK 13030, features a modification of the amino acid from A to T at position 23.
+The protein's natural variant, known as in strain: Isolate NK 13030, features a modification of the amino acid from V to M at position 39.
+The protein's natural variant, known as in strain: Isolate NK 13030, features a modification of the amino acid from M to I at position 156.
+The protein's natural variant, known as in strain: Isolate NK 13030, features a modification of the amino acid from C to S at position 209.
+The protein's natural variant, known as in strain: Isolate NK 13030, features a modification of the amino acid from V to I at position 338.
+The protein's natural variant, known as in strain: Isolate NK 13030, features a modification of the amino acid from H to Y at position 345.
+The protein's natural variant, known as in strain: B[RT500] isozyme 2, features a modification of the amino acid from L to R at position 28.
+The protein's natural variant, known as in strain: 1810, features a modification of the amino acid from W to G at position 30.
+The protein's natural variant, known as in strain: B[MB1428], features a modification of the amino acid from E to K at position 154.
+The protein's natural variant, known as in strain: 1810, features a modification of the amino acid from E to Q at position 154.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from L to V at position 146.
+The protein's natural variant, known as in strain: LEMB04 and LEMV99, features a modification of the amino acid from K to N at position 15.
+The protein's natural variant, known as in EDMD1; no loss of binding to F-actin, enhanced rate of actin polymerization and loss of binding to BCLAF1, features a modification of the amino acid from S to F at position 54.
+The protein's natural variant, known as in EDMD1; loss of binding to F-actin, features a modification of the amino acid from Q to H at position 133.
+The protein's natural variant, known as in EDMD1; no loss of binding to F-actin and enhanced rate of actin polymerization;, features a modification of the amino acid from P to H at position 183.
+The protein's natural variant, known as in EDMD1;, features a modification of the amino acid from P to T at position 183.
+The protein's natural variant, known as in wv, features a modification of the amino acid from G to S at position 156.
+The natural variant of this protein is characterized by an amino acid alteration from I to M at position 313.
+The natural variant of this protein is characterized by an amino acid alteration from M to L at position 344.
+The protein's natural variant, known as in strain: cv. Cvi-1, features a modification of the amino acid from K to Q at position 3.
+The protein's natural variant, known as in strain: cv. Per-1 and cv. Ser-1, features a modification of the amino acid from F to L at position 119.
+The protein's natural variant, known as in strain: cv. Ei-2, features a modification of the amino acid from Y to F at position 496.
+The protein's natural variant, known as in WARBM1; abolishes GEF activity towards RAB18; loss of RAB18 membrane association; no effect on GAP activity; no effect on GAP activity towards the RAB3 proteins RAB5A or RAB43;, features a modification of the amino acid from T to P at position 18.
+The protein's natural variant, known as in WARBM1; abolishes GEF activity towards RAB18; loss of RAB18 membrane association; no effect on GAP activity; no effect on GAP activity towards the RAB3 proteins RAB5A or RAB43;, features a modification of the amino acid from E to V at position 24.
+The natural variant of this protein is characterized by an amino acid alteration from S to T at position 3.
+The protein's natural variant, known as in strain: YJM 269, YJM 270, YJM 326 and YJM 1129, features a modification of the amino acid from T to A at position 13.
+The protein's natural variant, known as in strain: YJM 269, YJM 270, YJM 326 and YJM 1129, features a modification of the amino acid from R to H at position 111.
+The protein's natural variant, known as in strain: YJM 269, YJM 270, YJM 326 and YJM 1129, features a modification of the amino acid from S to L at position 149.
+The protein's natural variant, known as in strain: YJM 267, features a modification of the amino acid from S to T at position 165.
+The protein's natural variant, known as in strain: YJM 269, YJM 270, YJM 326 and YJM 1129, features a modification of the amino acid from I to T at position 202.
+The protein's natural variant, known as in strain: YJM 267, features a modification of the amino acid from E to Q at position 239.
+The protein's natural variant, known as in strain: SK1, V1-09, YJM 267, YJM 269, YJM 270, YJM 280, YJM 320,YJM 326, YJM 339 and YJM 1129, features a modification of the amino acid from I to V at position 428.
+The protein's natural variant, known as in mh; Piedmontese breed, features a modification of the amino acid from F to L at position 94.
+The protein's natural variant, known as in mh; Piedmontese breed, features a modification of the amino acid from C to Y at position 313.
+The protein's natural variant, known as in lplA1 or slr1; selenolipoate resistance mutation, features a modification of the amino acid from G to S at position 74.
+The protein's natural variant, known as in strain: UA67; confers resistance to nalidixic acid and ciprofloxacin, features a modification of the amino acid from A to T at position 70.
+The protein's natural variant, known as in strain: UA580R1, UA536, UA543 and UA549; confers resistance to nalidixic acid and ciprofloxacin, features a modification of the amino acid from T to I at position 86.
+The protein's natural variant, known as in strain: UA580R3; confers resistance to nalidixic acid and ciprofloxacin, features a modification of the amino acid from D to N at position 90.
+The protein's natural variant, known as in HMLR1; results in mild functional decrease in peroxisome biogenesis;, features a modification of the amino acid from R to P at position 581.
+The protein's natural variant, known as in PBD-CG1, features a modification of the amino acid from L to R at position 590.
+The protein's natural variant, known as in PBD-CG1;, features a modification of the amino acid from G to R at position 593.
+The protein's natural variant, known as in PBD1A, features a modification of the amino acid from L to P at position 597.
+The protein's natural variant, known as in PBD1A and PBD1B; decreased binding to PEX6; impaired protein import into peroxisomes;, features a modification of the amino acid from L to P at position 664.
+The protein's natural variant, known as in HMLR1; results in mild functional decrease in peroxisome biogenesis;, features a modification of the amino acid from L to W at position 705.
+The protein's natural variant, known as in PBD-CG1;, features a modification of the amino acid from R to G at position 798.
+The protein's natural variant, known as in PBD1A, PBD1B and PBD-CG1;, features a modification of the amino acid from G to D at position 843.
+The protein's natural variant, known as in PBD1A; impaired protein import into peroxisomes;, features a modification of the amino acid from R to W at position 949.
+The protein's natural variant, known as in PBD1A; impaired protein import into peroxisomes, features a modification of the amino acid from G to A at position 970.
+The protein's natural variant, known as in PBD1B and HMLR1;, features a modification of the amino acid from I to T at position 989.
+The protein's natural variant, known as in PBD1B;, features a modification of the amino acid from R to Q at position 998.
+The protein's natural variant, known as in PBD-CG1;, features a modification of the amino acid from A to E at position 1237.
+The natural variant of this protein is characterized by an amino acid alteration from H to A at position 17.
+The protein's natural variant, known as in ADTKD4; affects ER translocation and processing of nascent preprorenin, resulting in abolished prorenin and renin biosynthesis and secretion;, features a modification of the amino acid from L to R at position 16.
+The protein's natural variant, known as in RTD;, features a modification of the amino acid from D to N at position 104.
+The protein's natural variant, known as in RTD;, features a modification of the amino acid from R to K at position 230.
+The natural variant of this protein is characterized by an amino acid alteration from S to I at position 11.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 97.
+The natural variant of this protein is characterized by an amino acid alteration from L to V at position 109.
+The natural variant of this protein is characterized by an amino acid alteration from A to V at position 156.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 213.
+The natural variant of this protein is characterized by an amino acid alteration from M to I at position 318.
+The natural variant of this protein is characterized by an amino acid alteration from A to V at position 337.
+The protein's natural variant, known as in DBA19; unknown pathological significance;, features a modification of the amino acid from K to N at position 77.
+The natural variant of this protein is characterized by an amino acid alteration from A to T at position 103.
+The natural variant of this protein is characterized by an amino acid alteration from R to E at position 286.
+The protein's natural variant, known as in ARCND1;, features a modification of the amino acid from G to R at position 40.
+The protein's natural variant, known as in HMAHCHD; severely decreased adenosylhomocysteinase activity measured under reducing conditions; affects protein self-interaction and is able to form tetramers only under reducing conditions; does not affect nuclear-cytoplasmic protein distribution;, features a modification of the amino acid from R to C at position 49.
+The protein's natural variant, known as in HMAHCHD; affects nuclear-cytoplasmic protein distribution resulting in increased protein amount in the nucleus; results in protein aggregation and formation of inclusion bodies, features a modification of the amino acid from G to S at position 71.
+The protein's natural variant, known as in HMAHCHD; results in high molecular weight protein aggregates; severely decreased function in homocysteine synthesis; affects nuclear-cytoplasmic protein distribution resulting in slightly decreased protein amount in the nucleus;, features a modification of the amino acid from D to G at position 86.
+The natural variant of this protein is characterized by an amino acid alteration from D to N at position 86.
+The protein's natural variant, known as in HMAHCHD; affects nuclear-cytoplasmic protein distribution resulting in increased protein amount in the nucleus; severely decreased adenosylhomocysteinase activity; reduced thermal stability;, features a modification of the amino acid from A to V at position 89.
+The protein's natural variant, known as in HMAHCHD; affects nuclear-cytoplasmic protein distribution resulting in increased protein amount in the nucleus; reduced thermal stability; decreased adenosylhomocysteinase activity;, features a modification of the amino acid from Y to C at position 143.
+The protein's natural variant, known as in HMAHCHD; reduced tetramerization; affects nuclear-cytoplasmic protein distribution resulting in increased protein amount in the nucleus, features a modification of the amino acid from Y to D at position 328.
+The protein's natural variant, known as in clone 12, features a modification of the amino acid from T to P at position 78.
+The protein's natural variant, known as in clone 12, features a modification of the amino acid from L to P at position 89.
+The protein's natural variant, known as in clone 93, features a modification of the amino acid from A to V at position 164.
+The protein's natural variant, known as in FTDALS5; unknown pathological significance; impaired degradation by the ubiquitin proteasome system (UPS);, features a modification of the amino acid from S to G at position 3.
+The protein's natural variant, known as in FTDALS5; unknown pathological significance; impaired degradation by the ubiquitin proteasome system (UPS);, features a modification of the amino acid from K to R at position 97.
+The protein's natural variant, known as in FTDALS5; unknown pathological significance;, features a modification of the amino acid from T to I at position 181.
+The protein's natural variant, known as in FTDALS5; impaired degradation by the ubiquitin proteasome system (UPS);, features a modification of the amino acid from S to R at position 195.
+The protein's natural variant, known as in FTDALS5; unknown pathological significance; impaired degradation by the ubiquitin proteasome system (UPS);, features a modification of the amino acid from R to T at position 392.
+The protein's natural variant, known as in FTDALS5; unknown pathological significance; impaired degradation by the ubiquitin proteasome system (UPS);, features a modification of the amino acid from S to P at position 509.
+The protein's natural variant, known as in FTDALS5; unknown pathological significance;, features a modification of the amino acid from T to I at position 543.
+The protein's natural variant, known as in FTDALS5; increased 'Lys-48'-linked polyubiquitination of proteins targeted for proteasomal degradation, but no increase in 'Lys-63'-linked polyubiquitinated proteins; accumulation of ubiquitinated proteins including RRM2 and TARDBP/TDP43; impaired autophagosome-lysosome fusion; impaired degradation by the ubiquitin proteasome system (UPS); increased levels of ubiquitinated autophagy receptor SQSTM1/p62;, features a modification of the amino acid from S to G at position 621.
+The protein's natural variant, known as in FTDALS5; impaired degradation by the ubiquitin proteasome system (UPS);, features a modification of the amino acid from E to K at position 624.
+The protein's natural variant, known as in FTDALS5; unknown pathological significance; impaired degradation by the ubiquitin proteasome system (UPS);, features a modification of the amino acid from I to T at position 772.
+The protein's natural variant, known as in strain: CB4856; increased sensitivity to etoposide, teniposide and slightly increased sensitivity to XK469 and increased resistance to dactinomycin, features a modification of the amino acid from Q to M at position 797.
+The protein's natural variant, known as in DLACD; probable enzymatic loss-of-function; contrary to the wild-type protein, unable to restore basal D-lactate levels when tested in knockout zebrafish model;, features a modification of the amino acid from W to C at position 374.
+The protein's natural variant, known as in DLACD; probable enzymatic loss-of-function; contrary to the wild-type protein, unable to restore basal D-lactate levels when tested in knockout zebrafish model;, features a modification of the amino acid from T to M at position 463.
+The protein's natural variant, known as in SCA27A;, features a modification of the amino acid from F to S at position 145.
+The protein's natural variant, known as may increase risk for spina bifida;, features a modification of the amino acid from I to M at position 22.
+The protein's natural variant, known as in HMAE;, features a modification of the amino acid from V to M at position 56.
+The protein's natural variant, known as in HMAE, features a modification of the amino acid from A to T at position 129.
+The protein's natural variant, known as in HMAE, features a modification of the amino acid from C to R at position 405.
+The protein's natural variant, known as in HMAE;, features a modification of the amino acid from G to R at position 487.
+The protein's natural variant, known as in HMAE, features a modification of the amino acid from G to R at position 554.
+The protein's natural variant, known as in SPG5A;, features a modification of the amino acid from G to R at position 57.
+The protein's natural variant, known as in SPG5A;, features a modification of the amino acid from G to V at position 87.
+The natural variant of this protein is characterized by an amino acid alteration from H to Y at position 106.
+The protein's natural variant, known as in SPG5A; unknown pathological significance;, features a modification of the amino acid from G to D at position 147.
+The protein's natural variant, known as in SPG5A; unknown pathological significance, features a modification of the amino acid from G to R at position 198.
+The protein's natural variant, known as in SPG5A;, features a modification of the amino acid from F to S at position 216.
+The protein's natural variant, known as in SPG5A;, features a modification of the amino acid from H to L at position 285.
+The natural variant of this protein is characterized by an amino acid alteration from L to S at position 287.
+The protein's natural variant, known as in SPG5A;, features a modification of the amino acid from T to A at position 297.
+The protein's natural variant, known as in SPG5A; unknown pathological significance, features a modification of the amino acid from A to AA at position 316.
+The protein's natural variant, known as in SPG5A;, features a modification of the amino acid from S to F at position 363.
+The protein's natural variant, known as in SPG5A;, features a modification of the amino acid from R to C at position 417.
+The protein's natural variant, known as in SPG5A;, features a modification of the amino acid from R to H at position 417.
+The protein's natural variant, known as in SPG5A;, features a modification of the amino acid from G to A at position 443.
+The protein's natural variant, known as in SPG5A;, features a modification of the amino acid from F to I at position 470.
+The protein's natural variant, known as in SPG5A;, features a modification of the amino acid from R to C at position 486.
+The protein's natural variant, known as no effect on the interaction with P.falciparum RH5;, features a modification of the amino acid from K to N at position 152.
+The protein's natural variant, known as no effect on the interaction with P.falciparum RH5;, features a modification of the amino acid from V to L at position 176.
+The protein's natural variant, known as loss of interaction with P.falciparum RH5;, features a modification of the amino acid from L to P at position 206.
+The protein's natural variant, known as in Ok(A-); 2-fold reduction in the binding affinity for P.falciparum RH5 with reduced erythrocyte invasion by P.falciparum isolates 3D7 and Dd2;, features a modification of the amino acid from E to K at position 208.
+The protein's natural variant, known as loss of interaction with P.falciparum RH5;, features a modification of the amino acid from G to V at position 269.
+The protein's natural variant, known as in strain: CWL029 and TW-183, features a modification of the amino acid from N to D at position 379.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from S to A at position 777.
+The protein's natural variant, known as in allele CD1E*05;, features a modification of the amino acid from H to R at position 102.
+The protein's natural variant, known as in allele CD1E*02, allele CD1E*05 and CD1E*06;, features a modification of the amino acid from Q to R at position 106.
+The protein's natural variant, known as in allele CD1E*05;, features a modification of the amino acid from S to N at position 149.
+The protein's natural variant, known as in allele CD1E*03;, features a modification of the amino acid from R to W at position 164.
+The protein's natural variant, known as in allele CD1E*04; impairs localization to late endosomal compartments and lipid antigen presentation;, features a modification of the amino acid from L to P at position 194.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from T to I at position 653.
+The protein's natural variant, known as in PBD11B, features a modification of the amino acid from W to G at position 313.
+The protein's natural variant, known as in PBD11B; neonatal adrenoleukodystrophy;, features a modification of the amino acid from I to T at position 326.
+The protein's natural variant, known as in FHL5;, features a modification of the amino acid from L to P at position 209.
+The protein's natural variant, known as in FHL5; leads to a complete loss of the ability to interact with STX11;, features a modification of the amino acid from R to H at position 292.
+The protein's natural variant, known as in FHL5; leads to a complete loss of the ability to interact with STX11;, features a modification of the amino acid from R to Q at position 405.
+The protein's natural variant, known as in FHL5; leads to a complete loss of the ability to interact with STX11;, features a modification of the amino acid from R to W at position 405.
+The protein's natural variant, known as in FHL5; leads to a complete loss of the ability to interact with STX11;, features a modification of the amino acid from P to L at position 477.
+The protein's natural variant, known as in ODG7; unknown pathological significance;, features a modification of the amino acid from R to Q at position 135.
+The protein's natural variant, known as in COXPD5;, features a modification of the amino acid from R to H at position 170.
+The protein's natural variant, known as in ODG7; unknown pathological significance;, features a modification of the amino acid from R to H at position 202.
+The protein's natural variant, known as found in two consanguineous families with intellectual disability; unknown pathological significance;, features a modification of the amino acid from R to W at position 89.
+The protein's natural variant, known as in BFNS2; reduces the maximal heteromeric current by 40% with no alteration in voltage dependence of activation or deactivation kinetics;, features a modification of the amino acid from D to G at position 305.
+The protein's natural variant, known as in BFNS2;, features a modification of the amino acid from W to R at position 309.
+The protein's natural variant, known as in BFNS2; about 50% reduction of wild-type heteromeric current; ratio of 1:1; or 20%; ratio of 1:1:2;, features a modification of the amino acid from G to V at position 310.
+The protein's natural variant, known as in BFNS2; unknown pathological significance, features a modification of the amino acid from G to V at position 340.
+The protein's natural variant, known as has no statistically significant effect on the current or biophysical properties of the heteromeric channel;, features a modification of the amino acid from N to S at position 468.
+The protein's natural variant, known as rare variant; found in a patient with rolandic epilepsy and additional features such as mild developmental delay and abnormal behavior; unknown pathological significance;, features a modification of the amino acid from P to S at position 574.
+The protein's natural variant, known as found in patients with benign familial infantile seizures; unknown pathological significance;, features a modification of the amino acid from R to C at position 780.
+The protein's natural variant, known as in THMA1;, features a modification of the amino acid from R to Q at position 540.
+The protein's natural variant, known as in GT1; cells co-transfected with mutated alpha-IIb and wild-type beta-3 scarcely expressed the alpha-IIb/beta-3 complex;, features a modification of the amino acid from L to P at position 86.
+The protein's natural variant, known as in GT1, features a modification of the amino acid from A to V at position 139.
+The protein's natural variant, known as in GT1, features a modification of the amino acid from C to W at position 161.
+The protein's natural variant, known as in GT1; abolishes the binding function of alpha-IIb/beta-3 for soluble ligands without disturbing alpha-IIb/beta-3 expression; functional defect is likely caused by its allosteric effect rather than by a defect in the ligand-binding site itself, features a modification of the amino acid from Y to H at position 174.
+The protein's natural variant, known as in GT1; impairs surface expression of alpha-IIb/beta-3 and abrogates ligand binding to the activated integrin, features a modification of the amino acid from P to A at position 176.
+The protein's natural variant, known as in GT1; impairs surface expression of alpha-IIb/beta-3, features a modification of the amino acid from P to L at position 176.
+The protein's natural variant, known as in GT1; associated with abrogation of alpha-IIb/beta-3 complex formation, features a modification of the amino acid from F to C at position 202.
+The protein's natural variant, known as in GT1, features a modification of the amino acid from T to I at position 207.
+The protein's natural variant, known as in GT1; disrupts the structural conformation and the ligand binding properties of the heterodimeric complex; in addition the mutation appears to confer susceptibility to proteolysis;, features a modification of the amino acid from L to P at position 214.
+The protein's natural variant, known as in GT1, features a modification of the amino acid from F to L at position 222.
+The protein's natural variant, known as in GT1, features a modification of the amino acid from G to E at position 267.
+The protein's natural variant, known as in GT1; alters the heterodimer conformation thus impairing their intracellular transport;, features a modification of the amino acid from G to D at position 273.
+The protein's natural variant, known as in GT1; type I; impairs surface expression of alpha-IIb/beta-3, features a modification of the amino acid from F to S at position 320.
+The protein's natural variant, known as in GT1; expression of mutant subunit alpha-IIb/bet-3 is 28% of control; mutant pro-alpha-IIb subunit is retained in the endoplasmic reticulum;, features a modification of the amino acid from V to F at position 329.
+The protein's natural variant, known as in GT1; type I; impairs surface expression of alpha-IIb/beta-3;, features a modification of the amino acid from E to K at position 355.
+The protein's natural variant, known as in GT1; type II;, features a modification of the amino acid from R to H at position 358.
+The protein's natural variant, known as in GT1;, features a modification of the amino acid from G to D at position 380.
+The protein's natural variant, known as in GT1; expression of mutant subunit alpha-IIb/bet-3 is 11% of control; mutant pro-alpha-IIb subunit is retained in the endoplasmic reticulum;, features a modification of the amino acid from I to T at position 405.
+The protein's natural variant, known as in GT1;, features a modification of the amino acid from G to R at position 412.
+The protein's natural variant, known as in GT1; type I;, features a modification of the amino acid from G to D at position 449.
+The protein's natural variant, known as in GT1, features a modification of the amino acid from A to D at position 581.
+The protein's natural variant, known as in GT1; type I;, features a modification of the amino acid from I to T at position 596.
+The protein's natural variant, known as in GT1; type II; the rate of subunit maturation and the surface exposure of glycoprotein IIb/beta-3 are strongly reduced;, features a modification of the amino acid from C to R at position 705.
+The protein's natural variant, known as in GT1;, features a modification of the amino acid from L to V at position 752.
+The protein's natural variant, known as in GT1;, features a modification of the amino acid from R to P at position 755.
+The protein's natural variant, known as in GT1; type II;, features a modification of the amino acid from Q to P at position 778.
+The protein's natural variant, known as in GT1;, features a modification of the amino acid from L to P at position 847.
+The protein's natural variant, known as alloantigen HPA-3B;, features a modification of the amino acid from I to S at position 874.
+The protein's natural variant, known as in GT1; severe type 1 phenotype; the mutation prevented normal ITGA2B/ITGB3 complex expression on the cell surface;, features a modification of the amino acid from V to F at position 934.
+The protein's natural variant, known as in GT1; marked reduction in the rate of surface expression, features a modification of the amino acid from P to L at position 943.
+The protein's natural variant, known as in GT1; severe type 1 phenotype; the mutation prevented normal ITGA2B/ITGB3 complex expression on the cell surface; the mutation may interfere with correct folding of the protein;, features a modification of the amino acid from S to L at position 957.
+The protein's natural variant, known as in GT1; much reduced surface expression of alpha-IIb/beta-3 and a block in the maturation of pro-alpha-IIb;, features a modification of the amino acid from V to M at position 982.
+The protein's natural variant, known as in GT1 and BDPLT16; results in low surface expression of the mutant protein;, features a modification of the amino acid from R to Q at position 1026.
+The protein's natural variant, known as in BDPLT16; results in abnormal membrane ruffling and cytoplasmic protrusions as well as defective proplatelet formation;, features a modification of the amino acid from R to W at position 1026.
+The protein's natural variant, known as in BTDD; decreases hydroxylation of the protein; decreases the accuracy of translation; decreases levels of incorporation of the mutant protein into ribosomes and polysomes; patient cells become highly sensitive to oxidative stress;, features a modification of the amino acid from R to K at position 67.
+The protein's natural variant, known as in BTDD; decreases hydroxylation of the protein; decreases the accuracy of translation; decreases levels of incorporation of the mutant protein into polysomes; patient cells become highly sensitive to oxidative stress;, features a modification of the amino acid from F to I at position 120.
+The protein's natural variant, known as found in a tumor sample; unknown pathological significance; impaired localization to lysosomes and ability to regulate lysosome positioning, features a modification of the amino acid from K to N at position 97.
+The protein's natural variant, known as found in a tumor sample; unknown pathological significance; impaired localization to endosomes, features a modification of the amino acid from V to G at position 98.
+The protein's natural variant, known as found in a tumor sample; unknown pathological significance; abolished ability to regulate protein trafficking and localization, features a modification of the amino acid from C to R at position 268.
+The protein's natural variant, known as in an ovarian clear cell adenocarcinoma, features a modification of the amino acid from Q to H at position 564.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from V to L at position 695.
+The protein's natural variant, known as in an uterine cancer sample; somatic mutation;, features a modification of the amino acid from S to N at position 761.
+The protein's natural variant, known as in IDDSSA; altered autophagosome assembly shown in patient cells;, features a modification of the amino acid from V to M at position 249.
+The protein's natural variant, known as in 6B3-2, features a modification of the amino acid from A to V at position 47.
+The protein's natural variant, known as in 6B3-2, features a modification of the amino acid from P to H at position 52.
+The protein's natural variant, known as in 6B3-2, features a modification of the amino acid from L to I at position 82.
+The protein's natural variant, known as in 6B3-2, features a modification of the amino acid from PT to LI at position 93.
+The protein's natural variant, known as in 6B3-2, features a modification of the amino acid from P to S at position 98.
+The protein's natural variant, known as in 6B3-2, features a modification of the amino acid from L to I at position 108.
+The protein's natural variant, known as in 6B3-2, features a modification of the amino acid from T to I at position 289.
+The protein's natural variant, known as in 6B3-2, features a modification of the amino acid from G to S at position 350.
+The protein's natural variant, known as in 6B3-2, features a modification of the amino acid from FLGR to YLSK at position 357.
+The protein's natural variant, known as in 6B3-2, features a modification of the amino acid from IIV to VII at position 397.
+The protein's natural variant, known as in 6B3-2, features a modification of the amino acid from G to S at position 401.
+The protein's natural variant, known as in POF14; unknown pathological significance;, features a modification of the amino acid from D to Y at position 57.
+The protein's natural variant, known as in POF14; unknown pathological significance, features a modification of the amino acid from K to E at position 67.
+The protein's natural variant, known as in POF14; unknown pathological significance; also found at higher frequency in mothers of dizygotic twins than in controls;, features a modification of the amino acid from P to S at position 103.
+The protein's natural variant, known as found at higher frequency in mothers of dizygotic twins than in controls;, features a modification of the amino acid from T to I at position 121.
+The protein's natural variant, known as in POF14; unknown pathological significance;, features a modification of the amino acid from R to C at position 146.
+The protein's natural variant, known as in POF14; unknown pathological significance, features a modification of the amino acid from S to Y at position 186.
+The protein's natural variant, known as in POF14; unknown pathological significance;, features a modification of the amino acid from V to M at position 216.
+The protein's natural variant, known as in POF14; unknown pathological significance, features a modification of the amino acid from T to A at position 238.
+The protein's natural variant, known as found at higher frequency in mothers of dizygotic twins than in controls;, features a modification of the amino acid from P to L at position 374.
+The protein's natural variant, known as in POF14; unknown pathological significance;, features a modification of the amino acid from S to T at position 428.
+The protein's natural variant, known as found at higher frequency in mothers of dizygotic twins than in controls;, features a modification of the amino acid from R to C at position 454.
+The protein's natural variant, known as in strain: Serotype 5, features a modification of the amino acid from EQA to KQT at position 112.
+The protein's natural variant, known as in strain: Serotype 5, features a modification of the amino acid from D to H at position 328.
+The protein's natural variant, known as in strain: Serotype 5, features a modification of the amino acid from R to V at position 517.
+The protein's natural variant, known as in strain: Serotype 5, features a modification of the amino acid from N to G at position 556.
+The protein's natural variant, known as in strain: S 4074 / Serotype 1, features a modification of the amino acid from GQR to RAT at position 611.
+The protein's natural variant, known as in strain: Serotype 5, features a modification of the amino acid from RQ to PN at position 612.
+The protein's natural variant, known as in strain: Serotype 5, features a modification of the amino acid from DR to AS at position 672.
+The protein's natural variant, known as in strain: Serotype 5, features a modification of the amino acid from A to R at position 692.
+The protein's natural variant, known as in strain: ATCC 23235, features a modification of the amino acid from P to A at position 114.
+The natural variant of this protein is characterized by an amino acid alteration from L to V at position 302.
+The protein's natural variant, known as in PFBMFT6; unknown pathological significance; increased single-stranded DNA binding; increased telomeric DNA binding; has no effect on the formation of canonical replication protein A complex, features a modification of the amino acid from V to A at position 227.
+The protein's natural variant, known as in PFBMFT6; results in shortened telomeres and impaired hematopoiesis when expressed in iPSC-derived hematopoietic cells; increased single-stranded DNA binding; increased telomeric DNA binding; has no effect on the formation of canonical replication protein A complex, features a modification of the amino acid from E to K at position 240.
+The protein's natural variant, known as in PFBMFT6; unknown pathological significance; has DNA-binding properties similar to the wild-type; has no effect on the formation of canonical replication protein A complex, features a modification of the amino acid from T to A at position 270.
+The protein's natural variant, known as in AD4; likely benign variant;, features a modification of the amino acid from R to H at position 62.
+The protein's natural variant, known as in AD4; unknown pathological significance;, features a modification of the amino acid from R to W at position 71.
+The protein's natural variant, known as in AD4;, features a modification of the amino acid from T to P at position 122.
+The protein's natural variant, known as in AD4; increased mitochondrion-endoplasmic reticulum membrane tethering resulting in increased calcium transfer to mitochondria;, features a modification of the amino acid from T to R at position 122.
+The protein's natural variant, known as in AD4; unknown pathological significance, features a modification of the amino acid from E to K at position 126.
+The protein's natural variant, known as in CMD1V and AD4; unknown pathological significance;, features a modification of the amino acid from S to L at position 130.
+The protein's natural variant, known as in AD4; results in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio; loss of function as calcium-leak channel; results in calcium overload in the endoplasmic reticulum; increased mitochondrion-endoplasmic reticulum membrane tethering resulting in increased calcium transfer to mitochondria;, features a modification of the amino acid from N to I at position 141.
+The protein's natural variant, known as in AD4;, features a modification of the amino acid from N to Y at position 141.
+The protein's natural variant, known as in AD4; late-onset Alzheimer disease;, features a modification of the amino acid from V to I at position 148.
+The protein's natural variant, known as in AD4;, features a modification of the amino acid from M to I at position 239.
+The protein's natural variant, known as in AD4;, features a modification of the amino acid from M to V at position 239.
+The protein's natural variant, known as in breast cancer samples; infiltrating ductal carcinoma; somatic mutation, features a modification of the amino acid from K to N at position 117.
+The protein's natural variant, known as in GLC3E; enhanced proteasomal degradation, features a modification of the amino acid from C to Y at position 233.
+The protein's natural variant, known as in GLC3E; unknown pathological significance; 10-fold decrease of Tyr-1102 phosphorylation; no effect on membrane location;, features a modification of the amino acid from K to N at position 294.
+The protein's natural variant, known as in GLC3E; reduced response to ligand; loss of ligand-induced phosphorylation; no effect on basal membrane location;, features a modification of the amino acid from Y to C at position 611.
+The protein's natural variant, known as in VMCM; increased ligand-independent autophosphorylation and kinase activation; no effect on location at membrane;, features a modification of the amino acid from R to W at position 849.
+The protein's natural variant, known as in an ovarian serous carcinoma sample; somatic mutation;, features a modification of the amino acid from P to A at position 883.
+The protein's natural variant, known as in VMCM; increased ligand-independent autophosphorylation and kinase activation;, features a modification of the amino acid from Y to C at position 897.
+The protein's natural variant, known as found in a patient with multiple sporadic venous malformations; increased ligand-independent autophosphorylation; the hyperphosphorylation increases when associated with Leu-915, features a modification of the amino acid from Y to F at position 897.
+The protein's natural variant, known as found in a patient with solitary sporadic venous malformations; increased ligand-independent autophosphorylation, features a modification of the amino acid from Y to H at position 897.
+The protein's natural variant, known as in VMCM; also found in a patient with solitary sporadic venous malformations; increased ligand-independent autophosphorylation and kinase activation;, features a modification of the amino acid from Y to S at position 897.
+The protein's natural variant, known as found in patients with solitary and multiple sporadic venous malformations; increased ligand-independent autophosphorylation; novel location at endoplasmic reticulum and Golgi apparatus; partially retained at endoplasmic reticulum and Golgi apparatus;, features a modification of the amino acid from L to F at position 914.
+The protein's natural variant, known as found in a patient with solitary sporadic venous malformations; increased ligand-independent autophosphorylation;, features a modification of the amino acid from R to C at position 915.
+The protein's natural variant, known as in VMCM; strongly increased ligand-independent autophosphorylation and kinase activation;, features a modification of the amino acid from R to H at position 915.
+The protein's natural variant, known as found in a patient with multiple sporadic venous malformations; increased ligand-independent autophosphorylation; the autophosphorylation increases when associated with Phe-897, features a modification of the amino acid from R to L at position 915.
+The protein's natural variant, known as found in a patient with solitary sporadic venous malformations; increased ligand-independent autophosphorylation, features a modification of the amino acid from S to I at position 917.
+The protein's natural variant, known as in VMCM; strongly increased ligand-independent autophosphorylation and kinase activation;, features a modification of the amino acid from R to C at position 918.
+The protein's natural variant, known as in VMCM; increased ligand-independent autophosphorylation and kinase activation, features a modification of the amino acid from V to L at position 919.
+The protein's natural variant, known as in VMCM; increased ligand-independent autophosphorylation and kinase activation, features a modification of the amino acid from A to S at position 925.
+The protein's natural variant, known as in VMCM; strongly increased ligand-independent autophosphorylation and kinase activation, features a modification of the amino acid from K to N at position 1100.
+The protein's natural variant, known as in a renal clear cell carcinoma sample; somatic mutation, features a modification of the amino acid from A to V at position 1124.
+The protein's natural variant, known as in strain: Isolate S58, features a modification of the amino acid from V to M at position 98.
+The protein's natural variant, known as in strain: Isolate S58, features a modification of the amino acid from I to T at position 303.
+The protein's natural variant, known as in MLASA2;, features a modification of the amino acid from G to D at position 46.
+The protein's natural variant, known as in MLASA2; has a 2-fold reduction in catalytic activity and a reduction in affinity for tRNA-tyr resulting in an overall 9-fold loss of catalytic efficiency;, features a modification of the amino acid from F to L at position 52.
+The protein's natural variant, known as in LCA5; unknown pathological significance, features a modification of the amino acid from R to G at position 218.
+The protein's natural variant, known as in LRS;, features a modification of the amino acid from F to C at position 161.
+The protein's natural variant, known as in LRS;, features a modification of the amino acid from G to S at position 168.
+The protein's natural variant, known as in BOOMD;, features a modification of the amino acid from L to R at position 171.
+The protein's natural variant, known as in AO1;, features a modification of the amino acid from A to V at position 173.
+The protein's natural variant, known as in AO1, features a modification of the amino acid from S to P at position 188.
+The protein's natural variant, known as in AO1 and AO3;, features a modification of the amino acid from M to V at position 202.
+The protein's natural variant, known as in LRS;, features a modification of the amino acid from E to K at position 227.
+The protein's natural variant, known as in LRS;, features a modification of the amino acid from L to V at position 234.
+The protein's natural variant, known as in BOOMD;, features a modification of the amino acid from S to P at position 235.
+The protein's natural variant, known as in LRS;, features a modification of the amino acid from G to S at position 361.
+The protein's natural variant, known as in LRS;, features a modification of the amino acid from G to E at position 363.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from R to Q at position 566.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from N to K at position 663.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from T to K at position 703.
+The protein's natural variant, known as in AO3;, features a modification of the amino acid from G to R at position 751.
+The protein's natural variant, known as in LRS;, features a modification of the amino acid from L to R at position 1431.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from A to G at position 1534.
+The protein's natural variant, known as in LRS;, features a modification of the amino acid from G to R at position 1586.
+The protein's natural variant, known as in LRS;, features a modification of the amino acid from V to D at position 1592.
+The protein's natural variant, known as in LRS;, features a modification of the amino acid from P to L at position 1603.
+The protein's natural variant, known as in LRS;, features a modification of the amino acid from G to S at position 1691.
+The protein's natural variant, known as in LRS;, features a modification of the amino acid from G to R at position 1834.
+The protein's natural variant, known as found in a renal cell carcinoma sample; somatic mutation, features a modification of the amino acid from G to V at position 194.
+The protein's natural variant, known as found in a renal cell carcinoma sample; somatic mutation, features a modification of the amino acid from M to L at position 195.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from A to T at position 66.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from G to S at position 286.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from T to R at position 331.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from R to Q at position 556.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from A to T at position 53.
+The natural variant of this protein is characterized by an amino acid alteration from A to T at position 257.
+The natural variant of this protein is characterized by an amino acid alteration from E to Q at position 471.
+The protein's natural variant, known as in strain: PB826, features a modification of the amino acid from L to M at position 16.
+The protein's natural variant, known as in strain: ED3092 and ED3101, features a modification of the amino acid from M to T at position 21.
+The protein's natural variant, known as in strain: BW287, features a modification of the amino acid from Q to L at position 61.
+The protein's natural variant, known as in strain: JU403, features a modification of the amino acid from V to A at position 141.
+The protein's natural variant, known as in strain: EG4207A, features a modification of the amino acid from D to H at position 142.
+The protein's natural variant, known as increased grain length, width and weight, features a modification of the amino acid from S to K at position 163.
+The protein's natural variant, known as in HOMG7; increased positive regulation of TORC1 signaling; increased phosphorylation of the downstream molecule S6K1, features a modification of the amino acid from S to L at position 76.
+The protein's natural variant, known as in HOMG7; increased positive regulation of TORC1 signaling; increased phosphorylation of the downstream molecule S6K1, features a modification of the amino acid from S to W at position 76.
+The protein's natural variant, known as in HOMG7; increased positive regulation of TORC1 signaling; increased phosphorylation of the downstream molecule S6K1, features a modification of the amino acid from T to P at position 97.
+The protein's natural variant, known as in HOMG7; increased positive regulation of TORC1 signaling; increased phosphorylation of the downstream molecule S6K1, features a modification of the amino acid from P to L at position 119.
+The protein's natural variant, known as in HOMG7; increased positive regulation of TORC1 signaling; increased phosphorylation of the downstream molecule S6K1, features a modification of the amino acid from P to R at position 119.
+The protein's natural variant, known as in HOMG7; increased positive regulation of TORC1 signaling; increased phosphorylation of the downstream molecule S6K1, features a modification of the amino acid from I to K at position 221.
+The natural variant of this protein is characterized by an amino acid alteration from A to T at position 209.
+The protein's natural variant, known as in a lung squamous cell carcinoma sample; somatic mutation, features a modification of the amino acid from R to S at position 255.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation, features a modification of the amino acid from S to L at position 562.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation, features a modification of the amino acid from R to Q at position 677.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation, features a modification of the amino acid from W to R at position 1247.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from T to K at position 37.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from N to S at position 85.
+The protein's natural variant, known as in a pancreatic ductal adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from K to N at position 207.
+The protein's natural variant, known as in a lung large cell carcinoma sample; somatic mutation, features a modification of the amino acid from S to Y at position 229.
+The protein's natural variant, known as in a lung neuroendocrine carcinoma sample; somatic mutation, features a modification of the amino acid from S to F at position 449.
+The protein's natural variant, known as in a lung squamous cell carcinoma sample; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from G to L at position 518.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from I to L at position 621.
+The protein's natural variant, known as in a lung carcinoma sample; somatic mutation, features a modification of the amino acid from T to K at position 660.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation, features a modification of the amino acid from G to E at position 766.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from D to N at position 806.
+The protein's natural variant, known as in a lung carcinoma sample; somatic mutation;, features a modification of the amino acid from T to M at position 933.
+The protein's natural variant, known as in NEDSEBA; unknown pathological significance;, features a modification of the amino acid from A to T at position 574.
+The protein's natural variant, known as in strain: Z10, features a modification of the amino acid from KIFVFVALILAI to MIYVRVGRTQAS at position 16.
+The protein's natural variant, known as in strain: B205 and B208, features a modification of the amino acid from K to Q at position 5.
+The protein's natural variant, known as in strain: Z10, Z18, Z22 and Z24, features a modification of the amino acid from Q to H at position 20.
+The protein's natural variant, known as in strain: Z10 and Z22, features a modification of the amino acid from W to G at position 25.
+The protein's natural variant, known as in strain: Z24, features a modification of the amino acid from L to R at position 26.
+The protein's natural variant, known as in strain: Z10, Z18 and Z22, features a modification of the amino acid from L to W at position 26.
+The protein's natural variant, known as in strain: Z10 and Z18, features a modification of the amino acid from K to R at position 27.
+The protein's natural variant, known as in strain: B316, features a modification of the amino acid from Q to R at position 53.
+The protein's natural variant, known as in strain: B202, features a modification of the amino acid from A to T at position 54.
+The natural variant of this protein is characterized by an amino acid alteration from T to N at position 30.
+The protein's natural variant, known as found in patients with Brugada syndrome; loss of function in enhancing the expression of SCN5A at the cell membrane; unknown pathological significance;, features a modification of the amino acid from E to D at position 83.
+The protein's natural variant, known as in PCH2C;, features a modification of the amino acid from R to W at position 58.
+The protein's natural variant, known as in BDPLT21; decreased function in positive regulation of DNA-templated transcription;, features a modification of the amino acid from R to W at position 324.
+The protein's natural variant, known as in BDPLT21; loss of function in positive regulation of DNA-templated transcription; decreased localization to nucleus; no effect on protein abundance;, features a modification of the amino acid from R to Q at position 337.
+The protein's natural variant, known as in BDPLT21; loss of function in positive regulation of DNA-templated transcription;, features a modification of the amino acid from R to W at position 337.
+The protein's natural variant, known as in BDPLT21; loss of function in positive regulation of DNA-templated transcription;, features a modification of the amino acid from Y to C at position 343.
+The protein's natural variant, known as in BDPLT21; loss of function in positive regulation of DNA-templated transcription; decreased localization to nucleus; no effect on protein abundance;, features a modification of the amino acid from K to E at position 345.
+The protein's natural variant, known as in CCHLND; the mutant protein is present at normal levels in patient fibroblasts; the mutant protein fails to localize normally to the Golgi apparatus and instead shows punctate staining in the cytoplasm;, features a modification of the amino acid from A to P at position 110.
+The protein's natural variant, known as in SPG42; significant increase in the amount of nuclear phosphorylated SMAD1-SMAD5-SMAD8 protein complex; marked increase of the BMPR1A protein level; no change for BMPR2 protein level; decrease of BMPR1A degradation;, features a modification of the amino acid from S to R at position 113.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from V to A at position 400.
+The protein's natural variant, known as in pyrimethamine resistance, features a modification of the amino acid from S to I at position 106.
+The protein's natural variant, known as in cac-F; lethal at the larval stage 3; loss of synaptic transmission, features a modification of the amino acid from E to K at position 989.
+The protein's natural variant, known as in cac-S; exhibits defects in the patterning of courtship lovesong and a subtle abnormality in visual physiology, features a modification of the amino acid from F to I at position 1029.
+The protein's natural variant, known as in DYT16;, features a modification of the amino acid from P to L at position 222.
+The protein's natural variant, known as in MDBH; 50% reduction of cysteine-tRNA ligase activity, features a modification of the amino acid from R to H at position 341.
+The protein's natural variant, known as in MDBH; 84% reduction of cysteine-tRNA ligase activity, features a modification of the amino acid from S to L at position 359.
+The protein's natural variant, known as in MDBH; loss-of-function variant unable to rescue viability defects in a yeast complementation assay, features a modification of the amino acid from L to Q at position 400.
+The protein's natural variant, known as in allele gamma-II;, features a modification of the amino acid from V to M at position 60.
+The protein's natural variant, known as in allele gamma-II, features a modification of the amino acid from I to M at position 126.
+The protein's natural variant, known as in allele gamma-II, features a modification of the amino acid from S to T at position 132.
+The protein's natural variant, known as in allele gamma-II, features a modification of the amino acid from L to I at position 204.
+The protein's natural variant, known as in allele gamma-II;, features a modification of the amino acid from F to L at position 288.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from E to K at position 119.
+The protein's natural variant, known as in a breast pleomorphic lobular carcinoma sample; somatic mutation;, features a modification of the amino acid from E to D at position 272.
+The protein's natural variant, known as in SCDO1;, features a modification of the amino acid from G to D at position 385.
+The protein's natural variant, known as in C2D;, features a modification of the amino acid from C to Y at position 131.
+The protein's natural variant, known as in C2D;, features a modification of the amino acid from S to F at position 209.
+The protein's natural variant, known as may be associated with a reduced risk for age-related macular degeneration;, features a modification of the amino acid from E to D at position 318.
+The protein's natural variant, known as in C2D;, features a modification of the amino acid from G to R at position 464.
+The protein's natural variant, known as in DEE78; impaired GABA-gated chloride ion channel activity, features a modification of the amino acid from M to T at position 263.
+The protein's natural variant, known as in DEE78; impaired GABA-gated chloride ion channel activity, features a modification of the amino acid from V to A at position 284.
+The protein's natural variant, known as in DEE78; impaired GABA-gated chloride ion channel activity, features a modification of the amino acid from L to V at position 291.
+The protein's natural variant, known as in DEE78; impaired GABA-gated chloride ion channel activity, features a modification of the amino acid from T to K at position 292.
+The protein's natural variant, known as in DEE78; impaired GABA-gated chloride ion channel activity, features a modification of the amino acid from F to L at position 325.
+The protein's natural variant, known as in DEE78; unknown pathological significance, features a modification of the amino acid from N to H at position 335.
+The protein's natural variant, known as found in a patient with epilepsy; unknown pathological significance, features a modification of the amino acid from N to K at position 377.
+The protein's natural variant, known as in CVID14; increased protein abundance in patient-derived B lymphocytes; impairs immature B cell differentiation;, features a modification of the amino acid from S to N at position 551.
+The protein's natural variant, known as in GSD1A;, features a modification of the amino acid from M to R at position 5.
+The protein's natural variant, known as in GSD1A;, features a modification of the amino acid from T to A at position 16.
+The protein's natural variant, known as in GSD1A; complete loss of glucose-6-phosphatase activity and reduced enzyme stability;, features a modification of the amino acid from T to R at position 16.
+The protein's natural variant, known as in GSD1A;, features a modification of the amino acid from Q to R at position 20.
+The protein's natural variant, known as in GSD1A;, features a modification of the amino acid from D to V at position 38.
+The protein's natural variant, known as in GSD1A;, features a modification of the amino acid from Q to P at position 54.
+The protein's natural variant, known as in GSD1A, features a modification of the amino acid from W to R at position 63.
+The protein's natural variant, known as in GSD1A;, features a modification of the amino acid from A to P at position 65.
+The protein's natural variant, known as in GSD1A;, features a modification of the amino acid from G to R at position 68.
+The protein's natural variant, known as in GSD1A; loss of catalytic activity;, features a modification of the amino acid from K to N at position 76.
+The protein's natural variant, known as in GSD1A;, features a modification of the amino acid from W to R at position 77.
+The protein's natural variant, known as in GSD1A;, features a modification of the amino acid from G to R at position 81.
+The protein's natural variant, known as in GSD1A; complete loss of glucose-6-phosphatase activity; prevalent mutation in Ashkenazi Jewish population;, features a modification of the amino acid from R to C at position 83.
+The protein's natural variant, known as in GSD1A;, features a modification of the amino acid from R to H at position 83.
+The protein's natural variant, known as in GSD1A, features a modification of the amino acid from R to I at position 83.
+The protein's natural variant, known as in GSD1A;, features a modification of the amino acid from T to I at position 108.
+The protein's natural variant, known as in GSD1A;, features a modification of the amino acid from E to K at position 110.
+The protein's natural variant, known as in GSD1A;, features a modification of the amino acid from T to I at position 111.
+The protein's natural variant, known as in GSD1A, features a modification of the amino acid from P to L at position 113.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from P to L at position 116.
+The protein's natural variant, known as in GSD1A;, features a modification of the amino acid from H to L at position 119.
+The protein's natural variant, known as in GSD1A;, features a modification of the amino acid from G to D at position 122.
+The protein's natural variant, known as in GSD1A;, features a modification of the amino acid from A to T at position 124.
+The protein's natural variant, known as in GSD1A;, features a modification of the amino acid from W to L at position 156.
+The protein's natural variant, known as in GSD1A;, features a modification of the amino acid from V to A at position 166.
+The protein's natural variant, known as in GSD1A; complete loss of glucose-6-phosphatase activity;, features a modification of the amino acid from V to G at position 166.
+The protein's natural variant, known as in GSD1A; loss of catalytic glucose-6-phosphatase activity;, features a modification of the amino acid from R to Q at position 170.
+The protein's natural variant, known as in GSD1A, features a modification of the amino acid from F to C at position 177.
+The protein's natural variant, known as in GSD1A;, features a modification of the amino acid from P to A at position 178.
+The protein's natural variant, known as in GSD1A;, features a modification of the amino acid from P to S at position 178.
+The protein's natural variant, known as in GSD1A, features a modification of the amino acid from H to P at position 179.
+The protein's natural variant, known as in GSD1A;, features a modification of the amino acid from G to E at position 184.
+The protein's natural variant, known as in GSD1A;, features a modification of the amino acid from G to V at position 184.
+The protein's natural variant, known as in GSD1A;, features a modification of the amino acid from G to D at position 188.
+The protein's natural variant, known as in GSD1A; complete loss of activity;, features a modification of the amino acid from G to R at position 188.
+The protein's natural variant, known as in GSD1A;, features a modification of the amino acid from G to S at position 188.
+The protein's natural variant, known as in GSD1A; complete loss of glucose-6-phosphatase activity and reduced enzyme stability;, features a modification of the amino acid from Y to C at position 209.
+The protein's natural variant, known as in GSD1A, features a modification of the amino acid from L to P at position 211.
+The protein's natural variant, known as in GSD1A;, features a modification of the amino acid from G to R at position 222.
+The protein's natural variant, known as in GSD1A;, features a modification of the amino acid from W to R at position 236.
+The protein's natural variant, known as in GSD1A, features a modification of the amino acid from A to T at position 241.
+The protein's natural variant, known as in GSD1A, features a modification of the amino acid from T to I at position 255.
+The protein's natural variant, known as in GSD1A, features a modification of the amino acid from P to L at position 257.
+The protein's natural variant, known as in GSD1A;, features a modification of the amino acid from N to K at position 264.
+The protein's natural variant, known as in GSD1A, features a modification of the amino acid from L to P at position 265.
+The protein's natural variant, known as in GSD1A, features a modification of the amino acid from G to V at position 266.
+The protein's natural variant, known as in GSD1A;, features a modification of the amino acid from G to R at position 270.
+The protein's natural variant, known as in GSD1A;, features a modification of the amino acid from G to V at position 270.
+The protein's natural variant, known as in GSD1A, features a modification of the amino acid from G to W at position 270.
+The protein's natural variant, known as in GSD1A;, features a modification of the amino acid from R to C at position 295.
+The protein's natural variant, known as in GSD1A;, features a modification of the amino acid from S to P at position 298.
+The protein's natural variant, known as in GSD1A;, features a modification of the amino acid from F to L at position 322.
+The protein's natural variant, known as in GSD1A;, features a modification of the amino acid from V to F at position 338.
+The protein's natural variant, known as in GSD1A;, features a modification of the amino acid from I to N at position 341.
+The protein's natural variant, known as in GSD1A, features a modification of the amino acid from L to R at position 345.
+The protein's natural variant, known as in strain: FVB/N, features a modification of the amino acid from C to F at position 3.
+The protein's natural variant, known as in European red deer, features a modification of the amino acid from L to M at position 9.
+The protein's natural variant, known as in European red deer, features a modification of the amino acid from H to N at position 26.
+The natural variant of this protein is characterized by an amino acid alteration from Q to L at position 120.
+The natural variant of this protein is characterized by an amino acid alteration from R to C at position 261.
+The protein's natural variant, known as in strain: Ky-b, features a modification of the amino acid from A to V at position 308.
+The protein's natural variant, known as in strain: Ky-b, features a modification of the amino acid from E to D at position 368.
+The protein's natural variant, known as in strain: Ky-a, features a modification of the amino acid from I to T at position 713.
+The protein's natural variant, known as in allele B4 and allele B5, features a modification of the amino acid from A to V at position 17.
+The protein's natural variant, known as in allele B6, features a modification of the amino acid from S to T at position 56.
+The protein's natural variant, known as in allele B4, allele B5 and allele B6, features a modification of the amino acid from H to Q at position 120.
+The protein's natural variant, known as in allele B4, allele B5 and allele B6, features a modification of the amino acid from V to I at position 134.
+The protein's natural variant, known as in allele B4, allele B5 and allele B6, features a modification of the amino acid from A to G at position 152.
+The protein's natural variant, known as common variant that contributes to hyperglycinuria and iminoglycinuria in patients carrying variants in SLC36A2, SLC6A19 or SLC6A18; results in SLC6A20 inactivation due to a 8-fold decrease of Vmax;, features a modification of the amino acid from T to M at position 199.
+The protein's natural variant, known as in allele DHOD3, features a modification of the amino acid from M to T at position 2.
+The protein's natural variant, known as in alleles DHOD2 and DHOD3, features a modification of the amino acid from C to R at position 3.
+The protein's natural variant, known as in allele DHOD2, features a modification of the amino acid from F to V at position 63.
+The protein's natural variant, known as in alleles DHOD2 and DHOD3, features a modification of the amino acid from S to I at position 86.
+The protein's natural variant, known as in allele DHOD3, features a modification of the amino acid from L to V at position 98.
+The protein's natural variant, known as in alleles DHOD2 and DHOD3, features a modification of the amino acid from L to I at position 222.
+The protein's natural variant, known as in allele DHOD3, features a modification of the amino acid from T to R at position 285.
+The protein's natural variant, known as in allele DHOD2, features a modification of the amino acid from R to K at position 301.
+The protein's natural variant, known as in strain: RU259, features a modification of the amino acid from C to Y at position 71.
+The protein's natural variant, known as in strain: MD111, MD112, MD199, MD221, MDW86, RU00, RU01, RU07 and RU259, features a modification of the amino acid from V to M at position 235.
+The protein's natural variant, known as in strain: NC37, NC48, TT00, TT01, HW00 and HW09, features a modification of the amino acid from V to I at position 357.
+The protein's natural variant, known as in strain: NC37, features a modification of the amino acid from T to M at position 370.
+The protein's natural variant, known as in CAFD1; decreased interaction with regulatory subunit PRKAR2B, features a modification of the amino acid from G to R at position 137.
+The protein's natural variant, known as in PPNAD4; somatic mutation; the mutation results in cAMP-independent basal protein kinase activity and constitutive activation of protein kinase A;, features a modification of the amino acid from L to R at position 206.
+The protein's natural variant, known as in allele AFT1-1UP; which is constitutively activated, features a modification of the amino acid from C to F at position 291.
+The natural variant of this protein is characterized by an amino acid alteration from N to V at position 28.
+The natural variant of this protein is characterized by an amino acid alteration from R to A at position 36.
+The protein's natural variant, known as in GHOX-7D, features a modification of the amino acid from G to S at position 247.
+The natural variant of this protein is characterized by an amino acid alteration from E to G at position 68.
+The natural variant of this protein is characterized by an amino acid alteration from L to P at position 114.
+The natural variant of this protein is characterized by an amino acid alteration from A to V at position 130.
+The natural variant of this protein is characterized by an amino acid alteration from G to Q at position 398.
+The protein's natural variant, known as in strain: TN106, features a modification of the amino acid from K to R at position 70.
+The protein's natural variant, known as in strain: TN106, features a modification of the amino acid from S to T at position 73.
+The protein's natural variant, known as in PPKB; retains the ability to traffic to the cell membrane;, features a modification of the amino acid from A to E at position 38.
+The protein's natural variant, known as in PPKB; retains the ability to traffic to the cell membrane;, features a modification of the amino acid from I to S at position 45.
+The protein's natural variant, known as in PPKB; retains the ability to traffic to the cell membrane;, features a modification of the amino acid from N to D at position 123.
+The protein's natural variant, known as in PPKB; retains the ability to traffic to the cell membrane;, features a modification of the amino acid from I to F at position 177.
+The protein's natural variant, known as in PPKB; retains the ability to traffic to the cell membrane;, features a modification of the amino acid from R to C at position 188.
+The protein's natural variant, known as in strain: Isolate SP802 and Isolate SP805, features a modification of the amino acid from L to P at position 253.
+The protein's natural variant, known as in IECEE2; unknown pathological significance;, features a modification of the amino acid from M to T at position 79.
+The protein's natural variant, known as in IECEE2; unknown pathological significance;, features a modification of the amino acid from Y to H at position 244.
+The protein's natural variant, known as in IECEE2; unknown pathological significance;, features a modification of the amino acid from L to S at position 277.
+The protein's natural variant, known as in IECEE2; unknown pathological significance, features a modification of the amino acid from T to K at position 284.
+The protein's natural variant, known as in IECEE2; loss of localization to the cell membrane; retained intracellularly it affects the cell surface expression of the GABA receptor; decreased GABA receptor activity;, features a modification of the amino acid from T to P at position 287.
+The protein's natural variant, known as in IECEE2; unknown pathological significance, features a modification of the amino acid from R to P at position 293.
+The protein's natural variant, known as in IECEE2; unknown pathological significance;, features a modification of the amino acid from K to R at position 303.
+The protein's natural variant, known as in IECEE2; unknown pathological significance, features a modification of the amino acid from A to V at position 304.
+The protein's natural variant, known as in IECEE2; unknown pathological significance;, features a modification of the amino acid from V to I at position 316.
+The protein's natural variant, known as in strain: BALB/c and C57BL/6, features a modification of the amino acid from I to T at position 7.
+The protein's natural variant, known as in strain: BALB/c and C57BL/6, features a modification of the amino acid from T to A at position 77.
+The natural variant of this protein is characterized by an amino acid alteration from L to S at position 46.
+The natural variant of this protein is characterized by an amino acid alteration from M to I at position 70.
+The protein's natural variant, known as in C1QD;, features a modification of the amino acid from G to R at position 34.
+The natural variant of this protein is characterized by an amino acid alteration from F to Y at position 831.
+The protein's natural variant, known as in strain: Oregon-R, features a modification of the amino acid from L to P at position 892.
+The natural variant of this protein is characterized by an amino acid alteration from V to A at position 105.
+The protein's natural variant, known as in strain: ATCC 32221, features a modification of the amino acid from G to D at position 21.
+The protein's natural variant, known as in strain: ATCC 32221, features a modification of the amino acid from V to I at position 88.
+The protein's natural variant, known as in strain: ATCC 32221, features a modification of the amino acid from D to N at position 111.
+The protein's natural variant, known as in strain: ATCC 32221, features a modification of the amino acid from F to S at position 227.
+The protein's natural variant, known as in strain: ATCC 32221, features a modification of the amino acid from D to H at position 248.
+The natural variant of this protein is characterized by an amino acid alteration from F to L at position 67.
+The natural variant of this protein is characterized by an amino acid alteration from A to L at position 83.
+The natural variant of this protein is characterized by an amino acid alteration from G to L at position 100.
+The natural variant of this protein is characterized by an amino acid alteration from M to T at position 178.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 224.
+The natural variant of this protein is characterized by an amino acid alteration from D to E at position 238.
+The protein's natural variant, known as in PEHO; increased protein degradation; decreased protein abundance; does not affect localization to cytoplasm and nucleus;, features a modification of the amino acid from S to L at position 31.
+The protein's natural variant, known as in strain: 91001, features a modification of the amino acid from SGK to R at position 326.
+The protein's natural variant, known as found in a family with early-onset autosomal recessive parkinsonism and intellectual disability; unknown pathological significance;, features a modification of the amino acid from C to Y at position 52.
+The protein's natural variant, known as found in a family with early-onset autosomal recessive parkinsonism and intellectual disability; unknown pathological significance;, features a modification of the amino acid from H to Y at position 53.
+The protein's natural variant, known as in ECHS1D;, features a modification of the amino acid from A to V at position 2.
+The protein's natural variant, known as in ECHS1D, features a modification of the amino acid from F to S at position 33.
+The protein's natural variant, known as in ECHS1D;, features a modification of the amino acid from R to H at position 54.
+The protein's natural variant, known as in ECHS1D; decreases significantly enoyl-CoA hydratase activity; decreases significantly protein expression;, features a modification of the amino acid from N to S at position 59.
+The protein's natural variant, known as in ECHS1D;, features a modification of the amino acid from I to T at position 66.
+The protein's natural variant, known as in ECHS1D;, features a modification of the amino acid from E to Q at position 77.
+The protein's natural variant, known as in ECHS1D; unknown pathological significance;, features a modification of the amino acid from G to R at position 90.
+The protein's natural variant, known as in ECHS1D;, features a modification of the amino acid from A to T at position 132.
+The protein's natural variant, known as in ECHS1D; decreases enoyl-CoA hydratase activity of 70%; decreases significantly protein expression;, features a modification of the amino acid from A to V at position 138.
+The protein's natural variant, known as in ECHS1D, features a modification of the amino acid from D to G at position 150.
+The protein's natural variant, known as in ECHS1D;, features a modification of the amino acid from A to D at position 158.
+The protein's natural variant, known as in ECHS1D;, features a modification of the amino acid from Q to R at position 159.
+The protein's natural variant, known as in ECHS1D;, features a modification of the amino acid from G to S at position 195.
+The protein's natural variant, known as in ECHS1D;, features a modification of the amino acid from C to R at position 225.
+The protein's natural variant, known as in ECHS1D;, features a modification of the amino acid from K to E at position 273.
+The protein's natural variant, known as in ECHS1D; unknown pathological significance, features a modification of the amino acid from E to G at position 281.
+The protein's natural variant, known as in strain: Isolate TK 43176, features a modification of the amino acid from D to N at position 64.
+The protein's natural variant, known as in strain: Isolate TK 43176, features a modification of the amino acid from A to T at position 190.
+The protein's natural variant, known as in strain: Isolate TK 20579, features a modification of the amino acid from P to Q at position 253.
+The protein's natural variant, known as in strain: Isolate TK 20579 and Isolate TK 43176, features a modification of the amino acid from M to T at position 353.
+The protein's natural variant, known as in strain: Isolate TK 43176, features a modification of the amino acid from I to T at position 369.
+The protein's natural variant, known as risk factor for atopic dermatitis and asthma;, features a modification of the amino acid from E to G at position 237.
+The protein's natural variant, known as in GAMOS7; decreased function in nephrogenesis; unable to fully rescue morpholino-induced nephrogenesis defects in Xenopus; decreased protein amount detected by Western blot in patient cells; affects exon 4 splicing resulting in decreased levels of wild-type mature transcript; impairs assembly of nuclear pore complex;, features a modification of the amino acid from M to I at position 101.
+The protein's natural variant, known as in NPHS11; no effect on interaction with NUP133; no effect on localization to the nuclear pore;, features a modification of the amino acid from D to Y at position 157.
+The protein's natural variant, known as in GAMOS7; unknown pathological significance;, features a modification of the amino acid from C to Y at position 442.
+The protein's natural variant, known as in ODG6;, features a modification of the amino acid from D to N at position 447.
+The protein's natural variant, known as in NPHS11; decreased interaction with NUP133; changed localization to the nuclear pore with relocalization to the cytoplasm;, features a modification of the amino acid from D to A at position 831.
+The protein's natural variant, known as in NPHS11; decreased function in nephrogenesis; unable to fully rescue morpholino-induced nephrogenesis defects in Xenopus; decreased interaction with NUP133;, features a modification of the amino acid from Y to C at position 889.
+The protein's natural variant, known as in THI6-3; possesses TMP-PPASE activity only, features a modification of the amino acid from E to K at position 370.
+The protein's natural variant, known as in THI6-2; both enzyme activities greatly decreased, features a modification of the amino acid from G to D at position 476.
+The protein's natural variant, known as in THI6-1; both enzyme activities greatly decreased, features a modification of the amino acid from G to D at position 510.
+The natural variant of this protein is characterized by an amino acid alteration from V to A at position 78.
+The natural variant of this protein is characterized by an amino acid alteration from I to T at position 117.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from H to N at position 201.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from L to F at position 301.
+The protein's natural variant, known as in strain: NIZOR5, features a modification of the amino acid from Y to C at position 27.
+The protein's natural variant, known as rare functional variant; causes mild disruption of interstrand cross-link repair activity; partial loss of protein stability;, features a modification of the amino acid from R to C at position 150.
+The protein's natural variant, known as in XFEPS;, features a modification of the amino acid from R to P at position 153.
+The protein's natural variant, known as in XP-F;, features a modification of the amino acid from I to M at position 225.
+The protein's natural variant, known as in FANCQ;, features a modification of the amino acid from L to P at position 230.
+The protein's natural variant, known as in XPF/CS;, features a modification of the amino acid from C to R at position 236.
+The protein's natural variant, known as in XP-F, features a modification of the amino acid from R to W at position 454.
+The protein's natural variant, known as in XP-F;, features a modification of the amino acid from R to Q at position 490.
+The protein's natural variant, known as in XP-F, features a modification of the amino acid from E to K at position 502.
+The protein's natural variant, known as in XP-F;, features a modification of the amino acid from G to R at position 513.
+The protein's natural variant, known as in XP-F, features a modification of the amino acid from I to T at position 529.
+The protein's natural variant, known as in XP-F, features a modification of the amino acid from T to A at position 567.
+The protein's natural variant, known as in XPF/CS;, features a modification of the amino acid from R to W at position 589.
+The protein's natural variant, known as in XP-F, features a modification of the amino acid from L to P at position 608.
+The protein's natural variant, known as in FANCQ; disruption of interstrand cross-link repair activity; no effect on protein stability;, features a modification of the amino acid from R to S at position 689.
+The natural variant of this protein is characterized by an amino acid alteration from G to D at position 703.
+The natural variant of this protein is characterized by an amino acid alteration from I to T at position 717.
+The protein's natural variant, known as in FANCQ; disruption of interstrand cross-link repair activity; no effect on protein stability;, features a modification of the amino acid from S to F at position 786.
+The protein's natural variant, known as in XP-F; mild; significant residual repair activity;, features a modification of the amino acid from R to W at position 799.
+The protein's natural variant, known as in obesity; partial activity;, features a modification of the amino acid from T to A at position 11.
+The protein's natural variant, known as in obesity;, features a modification of the amino acid from S to F at position 30.
+The protein's natural variant, known as in obesity; shows the same affinity as the wild-type but significant impairment of cAMP-induced activity in response to melanotan II compared with the wild-type receptor, features a modification of the amino acid from S to Y at position 36.
+The protein's natural variant, known as in obesity;, features a modification of the amino acid from D to V at position 37.
+The protein's natural variant, known as in obesity;, features a modification of the amino acid from V to M at position 50.
+The protein's natural variant, known as in obesity;, features a modification of the amino acid from S to C at position 58.
+The protein's natural variant, known as in obesity; shows a partial cAMP response to alpha-MSH;, features a modification of the amino acid from N to S at position 62.
+The protein's natural variant, known as in obesity; loss of plasma membrane localization; loss of receptor function, features a modification of the amino acid from N to K at position 72.
+The protein's natural variant, known as in obesity;, features a modification of the amino acid from P to L at position 78.
+The protein's natural variant, known as in obesity; completely unable to generate cAMP in response to ligand; shows evidence of impaired cell surface expression;, features a modification of the amino acid from N to D at position 97.
+The protein's natural variant, known as in obesity; shows the same affinity as the wild-type but significant impairment of cAMP-induced activity in response to melanotan II compared with the wild-type receptor;, features a modification of the amino acid from I to S at position 102.
+The protein's natural variant, known as in obesity;, features a modification of the amino acid from I to T at position 102.
+The protein's natural variant, known as common variant associated with lower body mass index and obesity risk; also associated with lower risk for type 2 diabetes and coronary artery disease; increased MC4R signaling; increased surface expression;, features a modification of the amino acid from V to I at position 103.
+The protein's natural variant, known as in obesity; decreased MC4R signaling; shows evidence of impaired cell surface expression, features a modification of the amino acid from L to P at position 106.
+The protein's natural variant, known as no effect on MC4R signaling;, features a modification of the amino acid from T to M at position 112.
+The protein's natural variant, known as in obesity; completely unable to generate cAMP in response to ligand; shows evidence of impaired cell surface expression, features a modification of the amino acid from I to K at position 125.
+The protein's natural variant, known as in obesity; signaling properties in response to alpha-MSH, beta-MSH and gamma-1-MSH are impaired;, features a modification of the amino acid from S to L at position 127.
+The protein's natural variant, known as in obesity; shows a partial cAMP response to alpha-MSH;, features a modification of the amino acid from R to Q at position 165.
+The protein's natural variant, known as in obesity;, features a modification of the amino acid from R to W at position 165.
+The protein's natural variant, known as in obesity;, features a modification of the amino acid from I to V at position 170.
+The protein's natural variant, known as in obesity; shows a partial cAMP response to alpha-MSH;, features a modification of the amino acid from A to T at position 175.
+The protein's natural variant, known as in obesity; does not bind alpha-MSH;, features a modification of the amino acid from G to D at position 181.
+The protein's natural variant, known as in obesity; shows significantly impairment of cAMP-induced activity in response to melanotan II compared with the wild-type receptor;, features a modification of the amino acid from A to V at position 219.
+The protein's natural variant, known as in obesity;, features a modification of the amino acid from G to S at position 252.
+The protein's natural variant, known as in obesity; shows a partial cAMP response to alpha-MSH;, features a modification of the amino acid from V to I at position 253.
+The protein's natural variant, known as in obesity; completely unable to generate cAMP in response to ligand; shows impaired cell surface expression;, features a modification of the amino acid from C to R at position 271.
+The protein's natural variant, known as in obesity; no activity;, features a modification of the amino acid from C to Y at position 271.
+The protein's natural variant, known as in obesity;, features a modification of the amino acid from N to S at position 274.
+The protein's natural variant, known as in obesity; shows reduced cAMP response to alpha-MSH; retains normal affinity for the antagonist AGRP;, features a modification of the amino acid from I to S at position 316.
+The protein's natural variant, known as in obesity;, features a modification of the amino acid from I to T at position 317.
+The protein's natural variant, known as in obesity; does not bind alpha-MSH, features a modification of the amino acid from L to F at position 325.
+The protein's natural variant, known as in strain: biovar 5, features a modification of the amino acid from S to STGTDLQFAYITLGGFKVGIDESEFHTFTGYLGDVINDDVVAAGSYR at position 139.
+The protein's natural variant, known as in CMT2W; loss-of-function variant;, features a modification of the amino acid from T to I at position 132.
+The protein's natural variant, known as in CMT2W; loss-of-function variant;, features a modification of the amino acid from P to H at position 134.
+The protein's natural variant, known as in CMT2W; has a neurotoxic effect in an animal model; results in loss of function;, features a modification of the amino acid from R to Q at position 137.
+The protein's natural variant, known as in CMT2W; unknown pathological significance; fails to complement deletion of the yeast ortholog; decreases histidine-tRNA ligase activity; increases in the KM for ATP binding; does not disrupt dimerization;, features a modification of the amino acid from V to G at position 155.
+The protein's natural variant, known as in CMT2W; hypomorphic variant;, features a modification of the amino acid from D to E at position 175.
+The protein's natural variant, known as in CMT2W; unknown pathological significance;, features a modification of the amino acid from V to A at position 238.
+The protein's natural variant, known as in CMT2W; fails to complement deletion of the yeast ortholog; decreases histidine-tRNA ligase activity; increases in the KM for ATP binding; does not disrupt dimerization;, features a modification of the amino acid from Y to C at position 330.
+The protein's natural variant, known as in CMT2W; unknown pathological significance; fails to complement deletion of the yeast ortholog; decreases histidine-tRNA ligase activity; increases in the KM for ATP binding; does not disrupt dimerization;, features a modification of the amino acid from S to N at position 356.
+The protein's natural variant, known as in CMT2W; loss-of-function variant;, features a modification of the amino acid from D to Y at position 364.
+The protein's natural variant, known as in USH3B; unknown pathological significance;, features a modification of the amino acid from Y to S at position 454.
+The protein's natural variant, known as in CMT2W; unknown pathological significance;, features a modification of the amino acid from P to S at position 505.
+The protein's natural variant, known as in NEDGTH; unknown pathological significance; contrary to the wild type, it fails to rescue eye defects in Rpt2-null Drosophila, features a modification of the amino acid from I to T at position 328.
+The protein's natural variant, known as rare variant found in a Diamond-Blackfan anemia patient; unknown pathological significance;, features a modification of the amino acid from H to R at position 11.
+The protein's natural variant, known as in OI9; patients have white sclerae, normal dentition, no rhizomelia or severe deformity of long bones;, features a modification of the amino acid from M to R at position 9.
+The protein's natural variant, known as in KPLBS;, features a modification of the amino acid from G to S at position 154.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from E to K at position 2.
+The protein's natural variant, known as in beta-B20, features a modification of the amino acid from D to H at position 270.
+The natural variant of this protein is characterized by an amino acid alteration from Q to R at position 580.
+The protein's natural variant, known as in ARGIN; 12% of wild-type activity;, features a modification of the amino acid from I to T at position 11.
+The protein's natural variant, known as in ARGIN; 5.2% of wild-type activity;, features a modification of the amino acid from G to D at position 27.
+The protein's natural variant, known as in ARGIN; 9.3% of wild-type activity, features a modification of the amino acid from G to V at position 74.
+The protein's natural variant, known as in ARGIN; decreases erythrocyte arginase activity, features a modification of the amino acid from A to V at position 125.
+The protein's natural variant, known as in ARGIN; 9.3% of wild-type activity, features a modification of the amino acid from T to I at position 134.
+The protein's natural variant, known as in ARGIN;, features a modification of the amino acid from G to V at position 138.
+The protein's natural variant, known as in ARGIN; decreases erythrocyte arginase activity, features a modification of the amino acid from R to T at position 180.
+The protein's natural variant, known as in ARGIN; decreases erythrocyte arginase activity;, features a modification of the amino acid from G to R at position 235.
+The protein's natural variant, known as in ARGIN; 20.8% of wild-type activity;, features a modification of the amino acid from R to Q at position 308.
+The protein's natural variant, known as in IFAP2 and HMD; loss of sterol-regulated protein processing; loss of localization to the nucleus; decreased DNA-binding transcription factor activity RNA polymerase II-specific;, features a modification of the amino acid from R to C at position 527.
+The protein's natural variant, known as in HMD;, features a modification of the amino acid from R to H at position 527.
+The protein's natural variant, known as in IFAP2; loss of sterol-regulated protein processing; loss of localization to the nucleus; decreased DNA-binding transcription factor activity RNA polymerase II-specific;, features a modification of the amino acid from L to P at position 530.
+The protein's natural variant, known as in BMFS6; altered capacity to interact with MDM2 RING domain in a yeast two-hybrid assay; no effect on ATP binding; expressed at lower levels than wild-type; when expressed in a mouse model, leads to increased TP53 activity, decreased telomerase length and ultimately to bone marrow failure;, features a modification of the amino acid from T to M at position 454.
+The protein's natural variant, known as in allele APOA-IV*1D;, features a modification of the amino acid from V to M at position 13.
+The protein's natural variant, known as in Budapest-2, features a modification of the amino acid from E to K at position 44.
+The protein's natural variant, known as in Seattle-3;, features a modification of the amino acid from A to S at position 161.
+The protein's natural variant, known as in Seattle-1; may contribute to the development of familial combined hyperlipidemia;, features a modification of the amino acid from S to L at position 178.
+The protein's natural variant, known as in allele APOA-IV*3;, features a modification of the amino acid from E to K at position 185.
+The protein's natural variant, known as in allele APOA-IV*0A; associated with H-380;, features a modification of the amino acid from K to E at position 187.
+The protein's natural variant, known as in allele APOA-IV*3A;, features a modification of the amino acid from E to K at position 250.
+The protein's natural variant, known as in Seattle-2; may contribute to the development of familial combined hyperlipidemia;, features a modification of the amino acid from R to Q at position 264.
+The protein's natural variant, known as in Budapest-1;, features a modification of the amino acid from R to C at position 305.
+The protein's natural variant, known as in allele APOA-IV*1A and allele Budapest-1;, features a modification of the amino acid from T to S at position 367.
+The protein's natural variant, known as in allele APOA-IV*2 and allele APOA-IV*0A; associated with E-187 in allele APOA-IV*0A;, features a modification of the amino acid from Q to H at position 380.
+The protein's natural variant, known as in allele APOA-IV*0 and allele APOA-IV*5; allele APOA-IV*5 is further defined by a silent nucleotide substitution, features a modification of the amino acid from Q to QEQQQ at position 381.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from K to N at position 381.
+The protein's natural variant, known as in a glioblastoma multiforme sample; somatic mutation;, features a modification of the amino acid from P to S at position 28.
+The protein's natural variant, known as in an ovarian endometrioid sample; somatic mutation, features a modification of the amino acid from E to A at position 105.
+The protein's natural variant, known as in MDPT3; decreased localization to the nucleus;, features a modification of the amino acid from L to P at position 173.
+The protein's natural variant, known as in DEE41;, features a modification of the amino acid from G to R at position 82.
+The protein's natural variant, known as in DEE41;, features a modification of the amino acid from L to P at position 85.
+The protein's natural variant, known as in DEE41;, features a modification of the amino acid from P to R at position 289.
+The protein's natural variant, known as higher frequency of homozygotes in a cohort of non-familial cardiomyopathy Japanese patients as compared to healthy controls;, features a modification of the amino acid from N to K at position 654.
+The protein's natural variant, known as in strain: Isolate TK 34552 and Isolate TK 34560, features a modification of the amino acid from N to T at position 15.
+The protein's natural variant, known as in strain: Isolate TK 40095, Isolate TK 40403 and Isolate TK 40411, features a modification of the amino acid from A to G at position 152.
+The protein's natural variant, known as in strain: Isolate TK 40114 and Isolate TK 40403, features a modification of the amino acid from V to G at position 161.
+The protein's natural variant, known as in strain: Isolate TK 40043 and Isolate TK 40140, features a modification of the amino acid from D to H at position 171.
+The protein's natural variant, known as in strain: Isolate MVZ 168867, Isolate MVZ 192681, Isolate ROM 104264, Isolate ROM 104368, Isolate ROM 105930, Isolate TK 14522, Isolate TK 17624, Isolate TK 34552, Isolate TK 34555, Isolate TK 34560, Isolate TK 34836, Isolate TK 34842, Isolate TK 34963, Isolate TK 40043, Isolate TK 40082, Isolate TK 40084, Isolate TK 40095, Isolate TK 40099, Isolate TK 40107, Isolate TK 40111, Isolate TK 40114, Isolate TK 40139, Isolate TK 40314, Isolate TK 40318, Isolate TK 40398, Isolate TK 40399, Isolate TK 40401, Isolate TK 40402, Isolate TK 40403, Isolate TK 40406, Isolate TK 40408, Isolate TK 40409, Isolate TK 40410, Isolate TK 40411, Isolate TK 40414, Isolate TK 104603 and Isolate TK 104630, features a modification of the amino acid from T to A at position 190.
+The protein's natural variant, known as in strain: Isolate TK 40140, features a modification of the amino acid from F to I at position 220.
+The protein's natural variant, known as in strain: Isolate ROM 104264, features a modification of the amino acid from F to L at position 274.
+The protein's natural variant, known as in strain: Isolate TK 40403, features a modification of the amino acid from F to L at position 333.
+The protein's natural variant, known as in strain: Isolate TK 40314 and Isolate TK 40318, features a modification of the amino acid from V to A at position 356.
+The protein's natural variant, known as in allele CYP21A2*2, features a modification of the amino acid from L to LL at position 9.
+The protein's natural variant, known as in AH3; non-classic form; unknown pathological significance; no effect on steroid 21-monooxygenase activity, features a modification of the amino acid from L to M at position 12.
+The protein's natural variant, known as in AH3; salt wasting form; unknown pathological significance; no significant difference in steroid 21-monooxygenase activity;, features a modification of the amino acid from A to T at position 15.
+The protein's natural variant, known as decreased steroid 21-monooxygenase activity;, features a modification of the amino acid from R to C at position 16.
+The protein's natural variant, known as in AH3; non-classic form; 10% of non-classic AH3 Texan patients; 50% steroid 21-monooxygenase activity;, features a modification of the amino acid from P to L at position 30.
+The protein's natural variant, known as in AH3; does not affect membrane binding; enzyme function abolished, features a modification of the amino acid from P to Q at position 30.
+The protein's natural variant, known as in AH3; loss of activity;, features a modification of the amino acid from G to R at position 56.
+The protein's natural variant, known as in AH3; non-classic form; simple virilizing form when associated with a second mild mutation such as S-453 or L-30; activity is significantly reduced in association with S-453;, features a modification of the amino acid from H to L at position 62.
+The protein's natural variant, known as in AH3; no activity, features a modification of the amino acid from G to E at position 64.
+The protein's natural variant, known as in AH3; simple virilizing form;, features a modification of the amino acid from I to T at position 77.
+The protein's natural variant, known as in AH3, features a modification of the amino acid from G to V at position 90.
+The protein's natural variant, known as in allele CYP21A2*3;, features a modification of the amino acid from K to R at position 102.
+The protein's natural variant, known as in AH3;, features a modification of the amino acid from P to L at position 105.
+The protein's natural variant, known as in AH3; loss of activity;, features a modification of the amino acid from L to R at position 107.
+The protein's natural variant, known as in AH3; non-classic form; loss of steroid 21-monooxygenase activity;, features a modification of the amino acid from S to F at position 113.
+The protein's natural variant, known as in AH3; non-classic form; reduced activity; decreased affinity for 17-hydroxyprogesterone and progesterone;, features a modification of the amino acid from K to Q at position 121.
+The protein's natural variant, known as in AH3;, features a modification of the amino acid from R to H at position 124.
+The protein's natural variant, known as in AH3; loss of activity;, features a modification of the amino acid from L to P at position 142.
+The protein's natural variant, known as in AH3; salt wasting form; loss of activity, features a modification of the amino acid from L to P at position 167.
+The protein's natural variant, known as in AH3; loss of hydroxylase activity toward 17-hydroxyprogesterone and progesterone, features a modification of the amino acid from C to R at position 169.
+The protein's natural variant, known as in AH3, features a modification of the amino acid from C to Y at position 169.
+The protein's natural variant, known as in AH3; simple virilizing form; 1-4% activity;, features a modification of the amino acid from I to N at position 172.
+The protein's natural variant, known as in AH3;, features a modification of the amino acid from G to A at position 178.
+The protein's natural variant, known as in AH3; loss of enzymatic activity toward 17-hydroxyprogesterone and progesterone;, features a modification of the amino acid from G to R at position 178.
+The protein's natural variant, known as in allele CYP21A2*4;, features a modification of the amino acid from D to E at position 183.
+The protein's natural variant, known as in AH3; exhibits low enzymatic activity toward 17-hydroxyprogesterone and progesterone, features a modification of the amino acid from Y to H at position 191.
+The protein's natural variant, known as in AH3;, features a modification of the amino acid from L to F at position 198.
+The protein's natural variant, known as decreased steroid 21-monooxygenase activity;, features a modification of the amino acid from S to G at position 202.
+The protein's natural variant, known as in AH3; non-classic form; pathogenicity uncertain, features a modification of the amino acid from V to L at position 211.
+The protein's natural variant, known as in AH3, features a modification of the amino acid from I to T at position 230.
+The protein's natural variant, known as in AH3, features a modification of the amino acid from R to K at position 233.
+The protein's natural variant, known as in AH3; salt wasting form;, features a modification of the amino acid from I to N at position 236.
+The protein's natural variant, known as in AH3; salt wasting form;, features a modification of the amino acid from V to E at position 237.
+The protein's natural variant, known as in AH3; salt wasting form;, features a modification of the amino acid from M to K at position 239.
+The protein's natural variant, known as in AH3;, features a modification of the amino acid from L to P at position 261.
+The protein's natural variant, known as decreased steroid 21-monooxygenase activity;, features a modification of the amino acid from P to L at position 267.
+The protein's natural variant, known as in allele CYP21A2*5;, features a modification of the amino acid from S to T at position 268.
+The protein's natural variant, known as in AH3; salt wasting form, features a modification of the amino acid from V to G at position 281.
+The protein's natural variant, known as in AH3; non-classic form; 50% activity; most common variant; normal KM but 20% reduced Vmax;, features a modification of the amino acid from V to L at position 281.
+The protein's natural variant, known as in AH3; exhibits low enzymatic activity toward 17-hydroxyprogesterone and progesterone, features a modification of the amino acid from H to N at position 282.
+The protein's natural variant, known as in AH3, features a modification of the amino acid from M to L at position 283.
+The protein's natural variant, known as in AH3, features a modification of the amino acid from G to C at position 291.
+The protein's natural variant, known as in AH3;, features a modification of the amino acid from G to R at position 291.
+The protein's natural variant, known as in AH3; salt wasting form; less then 1% activity;, features a modification of the amino acid from G to S at position 291.
+The protein's natural variant, known as in AH3; salt wasting form; less then 1% activity, features a modification of the amino acid from G to D at position 292.
+The protein's natural variant, known as in AH3; salt wasting form;, features a modification of the amino acid from L to F at position 300.
+The protein's natural variant, known as in AH3, features a modification of the amino acid from S to Y at position 301.
+The protein's natural variant, known as in AH3; loss of enzymatic activity toward 17-hydroxyprogesterone and progesterone, features a modification of the amino acid from W to R at position 302.
+The protein's natural variant, known as in hyperandrogenism; due to 21-hydroxylase deficiency; non-classic type; residual activity of 46% for conversion of 17-hydroxyprogesterone and 26% for conversion of progesterone compared with the normal enzyme;, features a modification of the amino acid from V to M at position 304.
+The protein's natural variant, known as in AH3, features a modification of the amino acid from L to M at position 317.
+The protein's natural variant, known as in AH3; simple virilizing form; 4% activity, features a modification of the amino acid from E to K at position 320.
+The protein's natural variant, known as in AH3; non-classic form; 50% activity;, features a modification of the amino acid from R to H at position 339.
+The protein's natural variant, known as in AH3; simple virilizing form;, features a modification of the amino acid from R to P at position 341.
+The protein's natural variant, known as in AH3; non-classic form; mild;, features a modification of the amino acid from R to W at position 341.
+The protein's natural variant, known as in AH3; salt wasting form;, features a modification of the amino acid from R to C at position 354.
+The protein's natural variant, known as in AH3; salt wasting form;, features a modification of the amino acid from R to H at position 354.
+The protein's natural variant, known as in AH3; salt wasting form; 0.15% activity, features a modification of the amino acid from R to P at position 356.
+The protein's natural variant, known as in AH3; simple virilizing form; mild; 0.65% activity;, features a modification of the amino acid from R to Q at position 356.
+The protein's natural variant, known as in AH3; salt wasting form;, features a modification of the amino acid from R to W at position 356.
+The protein's natural variant, known as in AH3; no activity, features a modification of the amino acid from A to V at position 362.
+The protein's natural variant, known as in AH3, features a modification of the amino acid from L to W at position 363.
+The protein's natural variant, known as in AH3;, features a modification of the amino acid from H to Y at position 365.
+The protein's natural variant, known as in AH3;, features a modification of the amino acid from R to W at position 369.
+The protein's natural variant, known as in hyperandrogenism; due to 21-hydroxylase deficiency; almost completely abolished enzyme activity;, features a modification of the amino acid from G to S at position 375.
+The protein's natural variant, known as in AH3; salt wasting form;, features a modification of the amino acid from E to D at position 380.
+The protein's natural variant, known as in AH3; very low residual activity;, features a modification of the amino acid from R to C at position 408.
+The protein's natural variant, known as in AH3; very low activity;, features a modification of the amino acid from G to S at position 424.
+The protein's natural variant, known as in AH3; loss of enzymatic activity toward 17-hydroxyprogesterone and progesterone;, features a modification of the amino acid from R to C at position 426.
+The protein's natural variant, known as in AH3; loss of enzymatic activity toward 17-hydroxyprogesterone;, features a modification of the amino acid from R to H at position 426.
+The protein's natural variant, known as in AH3;, features a modification of the amino acid from R to C at position 435.
+The protein's natural variant, known as decreased steroid 21-monooxygenase activity;, features a modification of the amino acid from T to M at position 450.
+The protein's natural variant, known as in AH3; salt wasting form; loss of steroid 21-monooxygenase activity, features a modification of the amino acid from T to P at position 450.
+The protein's natural variant, known as in AH3; non-classic form; simple virilizing form when associated with L-62; 50% of activity; almost completely abolished enzyme activity when associated with S-375;, features a modification of the amino acid from P to S at position 453.
+The protein's natural variant, known as in AH3;, features a modification of the amino acid from R to L at position 479.
+The protein's natural variant, known as in AH3; reduced enzyme activity to 70% of normal;, features a modification of the amino acid from P to S at position 482.
+The protein's natural variant, known as in AH3; moderate; 1-2% of activity;, features a modification of the amino acid from R to P at position 483.
+The protein's natural variant, known as in AH3;, features a modification of the amino acid from R to Q at position 483.
+The protein's natural variant, known as in AH3; salt wasting form;, features a modification of the amino acid from R to W at position 483.
+The protein's natural variant, known as in allele CYP21A2*6;, features a modification of the amino acid from N to S at position 493.
+The protein's natural variant, known as in PRCD, features a modification of the amino acid from C to Y at position 2.
+The protein's natural variant, known as in NSLH1; creates a N-myristoylation site, resulting in myristoylation of the protein and aberrant targeting to the plasma membrane;, features a modification of the amino acid from S to G at position 2.
+The protein's natural variant, known as in NSLH1; significantly decreases ERK1/2 activity; does not affect cytoplasm and nucleus localization; does not affect SHOC2-MRAS-RAF1 complex assembly; impairs interaction with phosphatase 1c;, features a modification of the amino acid from M to I at position 173.
+The protein's natural variant, known as in allele ALS2-2, features a modification of the amino acid from Y to F at position 183.
+The protein's natural variant, known as in allele ALS2-2, features a modification of the amino acid from T to A at position 412.
+The protein's natural variant, known as in allele ALS2-2, features a modification of the amino acid from T to S at position 438.
+The protein's natural variant, known as in allele ALS2-2, features a modification of the amino acid from N to S at position 470.
+The protein's natural variant, known as in allele ALS2-2, features a modification of the amino acid from IRVH to VRFR at position 504.
+The protein's natural variant, known as in allele ALS2-2, features a modification of the amino acid from V to I at position 530.
+The protein's natural variant, known as in allele ALS2-2, features a modification of the amino acid from I to T at position 533.
+The protein's natural variant, known as in allele ALS2-2, features a modification of the amino acid from NVP to GGS at position 651.
+The protein's natural variant, known as in allele ALS2-2, features a modification of the amino acid from A to E at position 661.
+The protein's natural variant, known as in allele ALS2-2, features a modification of the amino acid from G to S at position 663.
+The protein's natural variant, known as in allele ALS2-2, features a modification of the amino acid from N to D at position 687.
+The protein's natural variant, known as in allele ALS2-2, features a modification of the amino acid from G to S at position 726.
+The protein's natural variant, known as in allele ALS2-2, features a modification of the amino acid from L to S at position 729.
+The protein's natural variant, known as in allele ALS2-2, features a modification of the amino acid from G to GG at position 785.
+The protein's natural variant, known as in allele ALS2-2, features a modification of the amino acid from T to I at position 796.
+The protein's natural variant, known as in allele ALS2-2, features a modification of the amino acid from G to S at position 808.
+The protein's natural variant, known as in allele ALS2-2, features a modification of the amino acid from G to D at position 820.
+The protein's natural variant, known as in allele ALS2-2, features a modification of the amino acid from Q to P at position 830.
+The protein's natural variant, known as in allele ALS2-2, features a modification of the amino acid from H to Y at position 859.
+The protein's natural variant, known as in allele ALS2-2, features a modification of the amino acid from G to A at position 861.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from K to R at position 365.
+The protein's natural variant, known as in beta-3/Indianapolis; allele ADH1B*3; decreased NAD(H) binding;, features a modification of the amino acid from R to C at position 370.
+The protein's natural variant, known as in allele pvr2(15), haplotype C1, features a modification of the amino acid from A to T at position 15.
+The protein's natural variant, known as in allele pvr2(17), haplotype R1, features a modification of the amino acid from A to V at position 15.
+The protein's natural variant, known as in allele pvr1, haplotype I1. In allele pvr2(21), haplotype P1, features a modification of the amino acid from T to A at position 51.
+The protein's natural variant, known as in allele pvr2(13), haplotype N1. In allele pvr2(14), haplotype O1. In allele pvr2(11), haplotype H1. In allele pvr2(12), haplotype K1. In haplotype Sh, features a modification of the amino acid from N to D at position 65.
+The protein's natural variant, known as in strain: SC81, allele pvr2(5). In allele pvr1, haplotype I1. In allele pvr2(10), haplotype D1, features a modification of the amino acid from P to T at position 66.
+The protein's natural variant, known as in strain: Yolo Y and CDP06433; alleles pvr1-1 and pvr2(1). In strain: HD-C69; PI201234 and Perennial; allele pvr2(3). In strain: Florida VR2; Dempsey; CDP06188 and Chay Angolano; alleles pvr1-2 and pvr2(2), features a modification of the amino acid from V to E at position 67.
+The protein's natural variant, known as in strain: Maroc 1 and LP1, allele pvr2(6), features a modification of the amino acid from AKSKQAA to VEKSKQDD at position 74.
+The protein's natural variant, known as in strain: Chile de Arbol, allele pvr2(9), features a modification of the amino acid from AKSKQA to EKSKQD at position 73.
+The protein's natural variant, known as in strain: PI195301, allele pvr2(8), features a modification of the amino acid from A to E at position 68.
+The protein's natural variant, known as in strain: CDP00620, allele pvr1(+), haplotypes F1 and F2. In allele pvr2(17), haplotype R1. In allele pvr2(15), haplotype C1. In allele pvr2(22), haplotype Q1. In allele pvr2(16), haplotype G1. In allele pvr2(19), haplotype L1. In allele pvr2(18), haplotype J1. In allele pvr2(13), haplotype N1. In allele pvr2(14), haplotype O1. In allele pvr2(11), haplotype H1. In allele pvr2(12), haplotype K1. In haplotype Sh. In allele pvr2(20), haplotype M1. In allele pvr1, haplotype I1. In allele pvr2(10), haplotype D1. In allele pvr2(21), haplotype P1, features a modification of the amino acid from K to R at position 71.
+The protein's natural variant, known as in strain: SC81, allele pvr2(5). In allele pvr2(12), haplotype K1. In allele pvr2(10), haplotype D1, features a modification of the amino acid from A to D at position 73.
+The protein's natural variant, known as in allele pvr2(20), features a modification of the amino acid from A to T at position 73.
+The protein's natural variant, known as in allele pvr2(13), haplotype N1. In haplotype Sh, features a modification of the amino acid from A to D at position 74.
+The protein's natural variant, known as in allele pvr2(22), haplotype Q1, features a modification of the amino acid from S to I at position 77.
+The protein's natural variant, known as in strain: Yolo Y and CDP06433; alleles pvr1-1 and pvr2(1). In strain: Florida VR2; Dempsey; CDP06188 and Chay Angolano; alleles pvr1-2 and pvr2(2). In strain: Serrano Vera Cruz; allele pvr2(7). In allele pvr2(19), features a modification of the amino acid from L to R at position 79.
+The protein's natural variant, known as in allele pvr1, haplotype I1. In allele pvr2(8). In allele pvr2(10), haplotype D1, features a modification of the amino acid from G to R at position 107.
+The protein's natural variant, known as in strain: Florida VR2; CDP06188; Dempsey and Chay Angolano; alleles pvr1-2 and pvr2(2), features a modification of the amino acid from D to N at position 109.
+The protein's natural variant, known as in allele pvr2(16), haplotype G1. In haplotype Sh, features a modification of the amino acid from T to I at position 131.
+The protein's natural variant, known as in allele pvr2(18), haplotype J1, features a modification of the amino acid from E to G at position 160.
+The protein's natural variant, known as in strain: HD-C69, PI201234 and Perennial, allele pvr2(3), features a modification of the amino acid from D to G at position 205.
+The protein's natural variant, known as in allele pvr2(11), haplotype H1, features a modification of the amino acid from D to H at position 213.
+The protein's natural variant, known as in allele pvr2(18), haplotype J1, features a modification of the amino acid from D to E at position 214.
+The protein's natural variant, known as in allele pvr2(18), haplotype J1, features a modification of the amino acid from K to A at position 216.
+The protein's natural variant, known as in allele pvr2(10), haplotype D1, features a modification of the amino acid from L to F at position 218.
+The protein's natural variant, known as in allele pvr2(11), haplotype H1, features a modification of the amino acid from L to R at position 218.
+The protein's natural variant, known as in strain: SC81, allele pvr2(5). In allele pvr2(18), haplotype J1, features a modification of the amino acid from D to N at position 219.
+The protein's natural variant, known as in haplotype Sh, features a modification of the amino acid from N to S at position 221.
+The protein's natural variant, known as in IEHDCM; reduced folding stability as measured by differential scanning calorimetry of the mutant protein; impairs interaction with FAS;, features a modification of the amino acid from C to W at position 105.
+The protein's natural variant, known as in strain: Isolate PI578675, features a modification of the amino acid from L to P at position 260.
+The protein's natural variant, known as in DA1C; unknown pathological significance, features a modification of the amino acid from A to V at position 33.
+The protein's natural variant, known as in DA1C;, features a modification of the amino acid from C to F at position 157.
+The protein's natural variant, known as in DA1C;, features a modification of the amino acid from C to R at position 157.
+The protein's natural variant, known as in DA1C; unknown pathological significance, features a modification of the amino acid from G to S at position 163.
+The protein's natural variant, known as in strain: Isolate 94SAK2, features a modification of the amino acid from I to V at position 98.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation, features a modification of the amino acid from S to L at position 249.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation, features a modification of the amino acid from P to T at position 421.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from I to V at position 421.
+The protein's natural variant, known as in CDAN2; the mutant protein is unstable with less than 5% of protein detectable compared to wild-type;, features a modification of the amino acid from R to W at position 14.
+The protein's natural variant, known as in CDAN2; the mutant protein is unstable with less than 5% of protein detectable compared to wild-type;, features a modification of the amino acid from E to K at position 109.
+The protein's natural variant, known as in CWS7; unknown pathological significance;, features a modification of the amino acid from V to L at position 164.
+The protein's natural variant, known as in CDAN2; unknown pathological significance; the mutant protein is expressed as the wild-type;, features a modification of the amino acid from D to G at position 239.
+The protein's natural variant, known as in CDAN2, features a modification of the amino acid from D to A at position 348.
+The natural variant of this protein is characterized by an amino acid alteration from Q to R at position 386.
+The protein's natural variant, known as in CDAN2; unknown pathological significance, features a modification of the amino acid from S to L at position 436.
+The protein's natural variant, known as in CDAN2; unknown pathological significance;, features a modification of the amino acid from R to C at position 497.
+The protein's natural variant, known as in CDAN2;, features a modification of the amino acid from R to W at position 530.
+The protein's natural variant, known as in CWS7; aberrant aggregation; causes mislocalization of the protein in the cytoplasm; reduces interaction with SAR1A; confers endoplasmic reticulum (ER) stress-mediated cell growth advantage;, features a modification of the amino acid from V to G at position 594.
+The protein's natural variant, known as in CDAN2, features a modification of the amino acid from S to L at position 603.
+The protein's natural variant, known as in CDAN2;, features a modification of the amino acid from R to C at position 701.
+The protein's natural variant, known as in MRD46; decreased protein abundance; decreased potassium ion transmembrane transport; changed voltage-gated potassium channel activity; changed gating properties;, features a modification of the amino acid from V to G at position 145.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from W to G at position 191.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to C at position 244.
+The protein's natural variant, known as in MRD46; decreased protein abundance; decreased potassium ion transmembrane transport; changed voltage-gated potassium channel activity; changed gating properties;, features a modification of the amino acid from L to I at position 341.
+The protein's natural variant, known as in MRD46; no effect on protein abundance; no effect on potassium ion transmembrane transport; increased voltage-gated potassium channel activity; changed gating properties resulting in a gain of function;, features a modification of the amino acid from P to R at position 369.
+The protein's natural variant, known as in MRD46; no effect on protein abundance; no effect on potassium ion transmembrane transport; changed voltage-gated potassium channel activity; changed gating properties;, features a modification of the amino acid from S to I at position 429.
+The protein's natural variant, known as in strain: SLCC7509 and SLCC7510, features a modification of the amino acid from E to D at position 32.
+The protein's natural variant, known as in strain: SLCC7510, features a modification of the amino acid from E to G at position 407.
+The protein's natural variant, known as in strain: SLCC7509, features a modification of the amino acid from A to T at position 553.
+The protein's natural variant, known as in strain: SLCC7510, features a modification of the amino acid from I to F at position 627.
+The protein's natural variant, known as in strain: SLCC7509, features a modification of the amino acid from E to D at position 674.
+The protein's natural variant, known as in prfA* mutant which constitutively overexpresses virulence genes. Presumably blocks prfA in a cofactor-independent transcriptionally active conformation, features a modification of the amino acid from G to S at position 145.
+The protein's natural variant, known as in allele CD94-01 and allele CD94-03, features a modification of the amino acid from L to S at position 65.
+The protein's natural variant, known as in allele CD94-01 and allele CD94-03, features a modification of the amino acid from F to L at position 85.
+The protein's natural variant, known as in allele CD94-01 and allele CD94-03, features a modification of the amino acid from G to S at position 96.
+The protein's natural variant, known as in allele CD94-01 and allele CD94-03, features a modification of the amino acid from P to L at position 116.
+The protein's natural variant, known as in allele CD94-04, features a modification of the amino acid from F to L at position 155.
+The protein's natural variant, known as in allele CD94-04, features a modification of the amino acid from N to T at position 167.
+The protein's natural variant, known as in allele CD94-03, features a modification of the amino acid from P to S at position 168.
+The protein's natural variant, known as in allele CD94-04, features a modification of the amino acid from Y to H at position 176.
+The protein's natural variant, known as in strain: BT054, features a modification of the amino acid from V to A at position 36.
+The protein's natural variant, known as in strain: BT054, features a modification of the amino acid from QT to RI at position 43.
+The protein's natural variant, known as in strain: BT054, features a modification of the amino acid from Q to R at position 50.
+The protein's natural variant, known as in strain: BT054, features a modification of the amino acid from S to P at position 68.
+The protein's natural variant, known as in strain: BT054, features a modification of the amino acid from I to V at position 96.
+The protein's natural variant, known as in strain: BT054, features a modification of the amino acid from VI to AV at position 105.
+The protein's natural variant, known as in strain: BT054, features a modification of the amino acid from E to G at position 107.
+The protein's natural variant, known as in strain: BT054, features a modification of the amino acid from N to T at position 125.
+The protein's natural variant, known as in strain: BT054, features a modification of the amino acid from A to T at position 137.
+The protein's natural variant, known as in strain: BT054, features a modification of the amino acid from K to E at position 151.
+The protein's natural variant, known as in strain: MO124, features a modification of the amino acid from N to T at position 152.
+The protein's natural variant, known as in strain: MO124, features a modification of the amino acid from A to S at position 174.
+The protein's natural variant, known as in strain: BT054, features a modification of the amino acid from I to V at position 178.
+The protein's natural variant, known as in strain: MO124, features a modification of the amino acid from T to I at position 188.
+The protein's natural variant, known as in strain: BT054, features a modification of the amino acid from C to G at position 194.
+The protein's natural variant, known as in strain: MO124, features a modification of the amino acid from C to GSG at position 194.
+The protein's natural variant, known as in strain: MO124, features a modification of the amino acid from T to P at position 198.
+The protein's natural variant, known as in strain: BT054 and MO124, features a modification of the amino acid from T to A at position 204.
+The protein's natural variant, known as in strain: BT054 and MO124, features a modification of the amino acid from Y to F at position 218.
+The protein's natural variant, known as in strain: BT054, features a modification of the amino acid from S to R at position 228.
+The protein's natural variant, known as in strain: MO124, features a modification of the amino acid from M to T at position 229.
+The protein's natural variant, known as in strain: BT054, features a modification of the amino acid from I to V at position 230.
+The protein's natural variant, known as in strain: MO124, features a modification of the amino acid from TD to AN at position 238.
+The protein's natural variant, known as in strain: MO124, features a modification of the amino acid from A to E at position 241.
+The protein's natural variant, known as in strain: BT054 and MO124, features a modification of the amino acid from G to V at position 243.
+The protein's natural variant, known as in strain: BT054 and MO124, features a modification of the amino acid from A to S at position 253.
+The protein's natural variant, known as in strain: BT054 and MO124, features a modification of the amino acid from K to Q at position 259.
+The protein's natural variant, known as in strain: BT054 and MO124, features a modification of the amino acid from A to V at position 275.
+The protein's natural variant, known as in strain: PB826, features a modification of the amino acid from V to M at position 24.
+The protein's natural variant, known as in strain: ED3101, features a modification of the amino acid from W to S at position 25.
+The protein's natural variant, known as in strain: ED3092 and ED3101, features a modification of the amino acid from I to V at position 76.
+The protein's natural variant, known as in strain: BW287, EG4181, EG4207A, HK104, HK105, JU403, JU439, JU516, JU793, PB800 and PB826, features a modification of the amino acid from L to F at position 85.
+The protein's natural variant, known as in strain: ED3092 and ED3101, features a modification of the amino acid from N to S at position 91.
+The protein's natural variant, known as in strain: HK104 and HK105, features a modification of the amino acid from V to A at position 125.
+The protein's natural variant, known as in strain: ED3092 and ED3101, features a modification of the amino acid from L to F at position 128.
+The protein's natural variant, known as in strain: ED3092 and ED3101, features a modification of the amino acid from V to T at position 137.
+The protein's natural variant, known as in strain: ED3092 and ED3101, features a modification of the amino acid from L to V at position 164.
+The protein's natural variant, known as in strain: ED3083, features a modification of the amino acid from S to L at position 190.
+The protein's natural variant, known as in strain: BW287, EG4181, EG4207A, HK104, HK105, JU403, JU439, JU516, JU793, PB800 and PB826, features a modification of the amino acid from G to S at position 194.
+The protein's natural variant, known as in strain: JU403, JU439, JU516 and JU793, features a modification of the amino acid from T to I at position 202.
+The protein's natural variant, known as in strain: ED3092 and ED3101, features a modification of the amino acid from A to M at position 203.
+The protein's natural variant, known as in strain: BW287, JU403, JU439, JU516, JU793 and PB826, features a modification of the amino acid from A to V at position 203.
+The protein's natural variant, known as in strain: JU726, features a modification of the amino acid from I to T at position 209.
+The protein's natural variant, known as in strain: ED3092 and ED3101, features a modification of the amino acid from N to S at position 259.
+The protein's natural variant, known as in strain: EG4181, EG4207A and PB800, features a modification of the amino acid from L to F at position 262.
+The protein's natural variant, known as in strain: ED3092 and ED3101, features a modification of the amino acid from G to S at position 264.
+The protein's natural variant, known as in strain: BW287, ED3033, ED3034, ED3035, ED3037, ED3092, ED3101, EG4181, EG4207A, HK104, HK105, JU403, JU439, JU516, JU725, JU793, PB800, PB826 and VT847, features a modification of the amino acid from S to N at position 265.
+The protein's natural variant, known as in CDGIIb; loss of activity;, features a modification of the amino acid from R to T at position 486.
+The protein's natural variant, known as in CDGIIb; loss of activity;, features a modification of the amino acid from F to L at position 652.
+The protein's natural variant, known as in HL deficiency, features a modification of the amino acid from V to VHYTVAV at position 134.
+The protein's natural variant, known as in HL deficiency;, features a modification of the amino acid from S to F at position 289.
+The protein's natural variant, known as in HL deficiency;, features a modification of the amino acid from T to M at position 405.
+The protein's natural variant, known as in strain: 3380, features a modification of the amino acid from L to F at position 349.
+The protein's natural variant, known as variant Marburg II;, features a modification of the amino acid from E to Q at position 393.
+The protein's natural variant, known as in NMTC5; associated with disease susceptibility; variant Marburg I; could be a prominent risk predictor of carotid stenosis; impairs the pro-urokinase activating potency; increased cell migration and increased cell proliferation; dominant negative effect;, features a modification of the amino acid from G to E at position 534.
+The protein's natural variant, known as streptomycin resistant, features a modification of the amino acid from K to N at position 43.
+The protein's natural variant, known as streptomycin resistant, features a modification of the amino acid from K to R at position 43.
+The protein's natural variant, known as streptomycin resistant, features a modification of the amino acid from K to T at position 43.
+The protein's natural variant, known as streptomycin resistant, features a modification of the amino acid from R to L at position 86.
+The protein's natural variant, known as streptomycin resistant, features a modification of the amino acid from K to E at position 88.
+The protein's natural variant, known as streptomycin resistant, features a modification of the amino acid from K to R at position 88.
+The protein's natural variant, known as streptomycin resistant, features a modification of the amino acid from P to H at position 91.
+The natural variant of this protein is characterized by an amino acid alteration from Y to D at position 139.
+The protein's natural variant, known as reduces ornithine transport activity;, features a modification of the amino acid from G to C at position 159.
+The protein's natural variant, known as increases ornithine transport activity;, features a modification of the amino acid from V to G at position 181.
+The protein's natural variant, known as in DFNA70; increases the apoptotic process; no effect on cell proliferation and cell cycle phase;, features a modification of the amino acid from R to C at position 44.
+The natural variant of this protein is characterized by an amino acid alteration from S to A at position 29.
+The natural variant of this protein is characterized by an amino acid alteration from N to D at position 49.
+The natural variant of this protein is characterized by an amino acid alteration from D to E at position 59.
+The natural variant of this protein is characterized by an amino acid alteration from M to E at position 76.
+The protein's natural variant, known as slight increase in protein expression and enzyme activity with octopamine as substrate;, features a modification of the amino acid from N to S at position 9.
+The protein's natural variant, known as significant decrease in protein expression and enzyme activity with octopamine as substrate;, features a modification of the amino acid from T to A at position 98.
+The protein's natural variant, known as no significant effect on protein expression and enzyme activity with octopamine as substrate;, features a modification of the amino acid from R to C at position 112.
+The protein's natural variant, known as no significant effect on protein expression and enzyme activity with octopamine as substrate;, features a modification of the amino acid from A to T at position 175.
+The protein's natural variant, known as in mutant SUL-D, features a modification of the amino acid from E to EIE at position 67.
+The protein's natural variant, known as in a lung small cell carcinoma sample; somatic mutation, features a modification of the amino acid from R to L at position 168.
+The protein's natural variant, known as in a lung neuroendocrine carcinoma sample; somatic mutation;, features a modification of the amino acid from R to W at position 724.
+The protein's natural variant, known as in strain: Nv2001_f0516, Nv2001_f0517, Nv2001_f0565, Nv2001_f0567, Nv2001_f0622, Nv2001_f0652, Nv2001_f0665, Nv2001_f0668, Nv2001_f0684, Nv2001_f0688, Nv2001_f0763, Nv2001_f0828, Nv2001_f0811, NVIII-2, NVIII-5 and NVIII-m15, features a modification of the amino acid from M to I at position 2.
+The protein's natural variant, known as in strain: NVIII-1, features a modification of the amino acid from T to S at position 5.
+The protein's natural variant, known as in strain: Nv2001_f0779 and Nv2001_f0555, features a modification of the amino acid from A to G at position 12.
+The protein's natural variant, known as in strain: NVIII-m11, features a modification of the amino acid from K to M at position 104.
+The protein's natural variant, known as in GLC1G; unknown pathological significance;, features a modification of the amino acid from Y to C at position 97.
+The protein's natural variant, known as in GLC1G; unknown pathological significance; requires 2 nucleotide substitutions, features a modification of the amino acid from Y to P at position 216.
+The protein's natural variant, known as in GLC1G;, features a modification of the amino acid from N to S at position 355.
+The protein's natural variant, known as in GLC1G; unknown pathological significance;, features a modification of the amino acid from T to A at position 403.
+The protein's natural variant, known as in GLC1G; unknown pathological significance, features a modification of the amino acid from H to L at position 411.
+The protein's natural variant, known as in GLC1G; unknown pathological significance, features a modification of the amino acid from H to Y at position 411.
+The protein's natural variant, known as in GLC1G; unknown pathological significance;, features a modification of the amino acid from P to R at position 487.
+The protein's natural variant, known as in GLC1G;, features a modification of the amino acid from R to Q at position 529.
+The protein's natural variant, known as in FAR1-22P; induces cell cycle arrest in the absence of alpha-factor, features a modification of the amino acid from S to P at position 87.
+The protein's natural variant, known as in strain: Isolate PL05, features a modification of the amino acid from L to P at position 198.
+The protein's natural variant, known as in SEMDFA;, features a modification of the amino acid from G to C at position 41.
+The natural variant of this protein is characterized by an amino acid alteration from T to S at position 37.
+The natural variant of this protein is characterized by an amino acid alteration from E to K at position 126.
+The protein's natural variant, known as in strain: pgn2, features a modification of the amino acid from W to R at position 248.
+The protein's natural variant, known as in strain: BLG2/Msf, features a modification of the amino acid from G to W at position 344.
+The protein's natural variant, known as in RP80; unknown pathological significance;, features a modification of the amino acid from P to L at position 71.
+The protein's natural variant, known as in SRTD9;, features a modification of the amino acid from L to F at position 152.
+The protein's natural variant, known as in SRTD9; partial to complete loss of basal body localization and increase of cytoplasmic localization; partial loss of function;, features a modification of the amino acid from G to R at position 212.
+The protein's natural variant, known as in SRTD9, features a modification of the amino acid from I to M at position 233.
+The protein's natural variant, known as in SRTD9; disease phenotype consistent with Mainzer-Saldino syndrome, features a modification of the amino acid from E to G at position 267.
+The protein's natural variant, known as in SRTD9;, features a modification of the amino acid from R to W at position 280.
+The protein's natural variant, known as in SRTD9; impairs centrosomal localization;, features a modification of the amino acid from V to M at position 292.
+The protein's natural variant, known as in SRTD9; partial to complete loss of basal body localization and increase of cytoplasmic localization;, features a modification of the amino acid from Y to C at position 311.
+The protein's natural variant, known as in RP80; unknown pathological significance;, features a modification of the amino acid from C to R at position 329.
+The protein's natural variant, known as in RP80; unknown pathological significance;, features a modification of the amino acid from C to Y at position 333.
+The protein's natural variant, known as in RP80; unknown pathological significance;, features a modification of the amino acid from A to T at position 341.
+The protein's natural variant, known as in RP80; unknown pathological significance;, features a modification of the amino acid from A to P at position 418.
+The protein's natural variant, known as in RP80; also found in a patient with Leber congenital amaurosis and renal failure; unknown pathological significance; decreased localization to the basal body;, features a modification of the amino acid from L to P at position 440.
+The protein's natural variant, known as in RP80; unknown pathological significance; decreased localization to the basal body;, features a modification of the amino acid from T to M at position 484.
+The protein's natural variant, known as in SRTD9;, features a modification of the amino acid from G to E at position 522.
+The protein's natural variant, known as in SRTD9;, features a modification of the amino acid from R to Q at position 576.
+The protein's natural variant, known as in RP80; unknown pathological significance;, features a modification of the amino acid from C to W at position 663.
+The protein's natural variant, known as in SRTD9 and RP80; unknown pathological significance; partial to complete loss of basal body localization and increase of cytoplasmic localization;, features a modification of the amino acid from E to K at position 664.
+The protein's natural variant, known as no effect on localization to the basal body;, features a modification of the amino acid from L to R at position 777.
+The protein's natural variant, known as in RP80; unknown pathological significance;, features a modification of the amino acid from E to K at position 790.
+The protein's natural variant, known as in RP80; unknown pathological significance;, features a modification of the amino acid from R to C at position 871.
+The protein's natural variant, known as in RP80; unknown pathological significance; decreased localization to the basal body;, features a modification of the amino acid from S to P at position 939.
+The protein's natural variant, known as in RP80; unknown pathological significance;, features a modification of the amino acid from A to V at position 974.
+The protein's natural variant, known as in RP80; unknown pathological significance;, features a modification of the amino acid from G to R at position 1276.
+The protein's natural variant, known as in SRTD9; disease phenotype consistent with Mainzer-Saldino syndrome;, features a modification of the amino acid from C to R at position 1360.
+The protein's natural variant, known as in RP80; unknown pathological significance;, features a modification of the amino acid from L to P at position 1399.
+The natural variant of this protein is characterized by an amino acid alteration from T to I at position 43.
+The natural variant of this protein is characterized by an amino acid alteration from N to D at position 86.
+The natural variant of this protein is characterized by an amino acid alteration from F to L at position 96.
+The natural variant of this protein is characterized by an amino acid alteration from V to M at position 173.
+The natural variant of this protein is characterized by an amino acid alteration from R to K at position 316.
+The protein's natural variant, known as in NDNC4;, features a modification of the amino acid from Q to R at position 65.
+The protein's natural variant, known as in NDNC4;, features a modification of the amino acid from C to F at position 95.
+The protein's natural variant, known as in NDNC4;, features a modification of the amino acid from C to R at position 107.
+The protein's natural variant, known as in NDNC4;, features a modification of the amino acid from C to Y at position 118.
+The protein's natural variant, known as in MRXSBL, features a modification of the amino acid from P to PEFSLLMNGLKIFIKCL at position 199.
+The natural variant of this protein is characterized by an amino acid alteration from H to R at position 284.
+The protein's natural variant, known as likely benign variant; does not modify the functional properties of the protein, features a modification of the amino acid from P to T at position 378.
+The natural variant of this protein is characterized by an amino acid alteration from A to T at position 505.
+The protein's natural variant, known as does not modify the functional properties of the protein;, features a modification of the amino acid from E to K at position 787.
+The protein's natural variant, known as requires 2 nucleotide substitutions;, features a modification of the amino acid from A to M at position 952.
+The protein's natural variant, known as does not modify the functional properties of the protein;, features a modification of the amino acid from R to W at position 1550.
+The protein's natural variant, known as does not modify the functional properties of the protein;, features a modification of the amino acid from N to S at position 1834.
+The protein's natural variant, known as in strain: HP439, features a modification of the amino acid from S to G at position 20.
+The protein's natural variant, known as in strain: HP439, features a modification of the amino acid from A to V at position 31.
+The protein's natural variant, known as in strain: HP439, features a modification of the amino acid from I to V at position 76.
+The protein's natural variant, known as in strain: HP439, features a modification of the amino acid from G to S at position 87.
+The protein's natural variant, known as in strain: HP439, features a modification of the amino acid from M to I at position 182.
+The protein's natural variant, known as in strain: HP500, features a modification of the amino acid from I to V at position 202.
+The protein's natural variant, known as in strain: HP500, features a modification of the amino acid from H to N at position 217.
+The protein's natural variant, known as in strain: HP500, features a modification of the amino acid from I to V at position 264.
+The protein's natural variant, known as in CBG deficiency; Leuven; decreased cortisol-binding affinity;, features a modification of the amino acid from L to H at position 115.
+The protein's natural variant, known as in CBG deficiency; Lyon; decreased cortisol-binding affinity;, features a modification of the amino acid from D to N at position 389.
+The protein's natural variant, known as in MDCCAID; decreased phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity;, features a modification of the amino acid from V to M at position 23.
+The protein's natural variant, known as in MDCCAID; decreased phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; shows normal localization indistinguishable from the wild-type;, features a modification of the amino acid from I to T at position 50.
+The protein's natural variant, known as in MDCCAID; decreased phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity;, features a modification of the amino acid from M to V at position 93.
+The protein's natural variant, known as in MDCCAID; no phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity;, features a modification of the amino acid from G to S at position 140.
+The protein's natural variant, known as in MDCCAID; no phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity;, features a modification of the amino acid from D to N at position 269.
+The protein's natural variant, known as in MDCCAID; no phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; shows normal localization indistinguishable from the wild-type;, features a modification of the amino acid from Y to C at position 300.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from S to F at position 315.
+The protein's natural variant, known as in MDCCAID; shows a diffuse perinuclear mislocalization;, features a modification of the amino acid from I to T at position 363.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from G to R at position 797.
+The protein's natural variant, known as in MMCAT;, features a modification of the amino acid from L to P at position 202.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to K at position 382.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from K to T at position 455.
+The protein's natural variant, known as in MMCAT;, features a modification of the amino acid from C to W at position 577.
+The protein's natural variant, known as in LMP7k/LMP7s/LMPf/LMP7r/LMPcas4/LMPg7, features a modification of the amino acid from G to R at position 272.
+The protein's natural variant, known as in LMP7q, features a modification of the amino acid from A to S at position 275.
+The protein's natural variant, known as in CLCRP1; impairs ability to act as a disulfide isomerase enzyme;, features a modification of the amino acid from Y to C at position 393.
+The protein's natural variant, known as in NEDSPLB; unknown pathological significance;, features a modification of the amino acid from R to W at position 119.
+The protein's natural variant, known as in NEDSPLB; unknown pathological significance;, features a modification of the amino acid from S to R at position 472.
+The protein's natural variant, known as in NEDSPLB;, features a modification of the amino acid from L to P at position 777.
+The protein's natural variant, known as in NEDSPLB; unknown pathological significance;, features a modification of the amino acid from E to K at position 1152.
+The protein's natural variant, known as in NEDSPLB; unknown pathological significance, features a modification of the amino acid from A to T at position 1198.
+The protein's natural variant, known as in NEDSPLB; unknown pathological significance, features a modification of the amino acid from H to R at position 1295.
+The protein's natural variant, known as in SPG84; unknown pathological significance;, features a modification of the amino acid from V to M at position 1556.
+The protein's natural variant, known as in GIDID2; decreased interaction with TTC7A resulting in reduced PI4K complex stability; no effect on kinase activity;, features a modification of the amino acid from Y to D at position 1623.
+The protein's natural variant, known as in NEDSPLB;, features a modification of the amino acid from D to N at position 1664.
+The protein's natural variant, known as in SPG84; unknown pathological significance, features a modification of the amino acid from T to I at position 1720.
+The protein's natural variant, known as in NEDSPLB; unknown pathological significance;, features a modification of the amino acid from R to W at position 1733.
+The protein's natural variant, known as in NEDSPLB, features a modification of the amino acid from K to T at position 1808.
+The protein's natural variant, known as in NEDSPLB; loss of kinase activity; no effect on protein abundance;, features a modification of the amino acid from D to N at position 1854.
+The protein's natural variant, known as in NEDSPLB, features a modification of the amino acid from G to E at position 1925.
+The protein's natural variant, known as in NEDSPLB; unknown pathological significance;, features a modification of the amino acid from G to R at position 1925.
+The protein's natural variant, known as in NEDSPLB, features a modification of the amino acid from Y to C at position 1937.
+The protein's natural variant, known as in NEDSPLB; unknown pathological significance;, features a modification of the amino acid from N to S at position 1987.
+The protein's natural variant, known as in NEDSPLB; unknown pathological significance;, features a modification of the amino acid from M to T at position 2041.
+The protein's natural variant, known as in GEFSP2;, features a modification of the amino acid from R to T at position 27.
+The protein's natural variant, known as found in a patient with an unclassified form of epilepsy; also found in a patient with epilepsy-aphasia and febrile seizures plus; unknown pathological significance;, features a modification of the amino acid from D to N at position 45.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from G to V at position 58.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from L to F at position 61.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from F to L at position 63.
+The protein's natural variant, known as in DRVT; borderline phenotype;, features a modification of the amino acid from I to T at position 68.
+The protein's natural variant, known as in GEFSP2;, features a modification of the amino acid from S to P at position 74.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from E to D at position 78.
+The protein's natural variant, known as in DRVT; borderline phenotype;, features a modification of the amino acid from D to H at position 79.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from D to N at position 79.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from Y to C at position 84.
+The protein's natural variant, known as in DRVT and ICEGTC;, features a modification of the amino acid from F to S at position 90.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from I to T at position 91.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from A to P at position 98.
+The protein's natural variant, known as in DRVT and ICEGTC;, features a modification of the amino acid from R to Q at position 101.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from R to W at position 101.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from S to G at position 103.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from T to I at position 105.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from L to R at position 108.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from T to I at position 112.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from P to T at position 113.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from R to S at position 118.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from I to N at position 124.
+The protein's natural variant, known as in DRVT; borderline phenotype;, features a modification of the amino acid from H to D at position 127.
+The protein's natural variant, known as in FEB3A; loss of function;, features a modification of the amino acid from M to T at position 145.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from T to P at position 162.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from I to K at position 171.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from I to R at position 171.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from A to T at position 175.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from A to V at position 175.
+The protein's natural variant, known as in DRVT; results in a non-functional channel;, features a modification of the amino acid from G to E at position 177.
+The protein's natural variant, known as in ICEGTC, features a modification of the amino acid from F to S at position 178.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from C to R at position 179.
+The protein's natural variant, known as found in a child with developmental disabilities; unknown pathological significance, features a modification of the amino acid from R to Q at position 187.
+The protein's natural variant, known as in GEFSP2; results in increased membrane excitability as suggested by increased resistance to cumulative inactivation during high frequency activation;, features a modification of the amino acid from D to V at position 188.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from W to R at position 190.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from N to K at position 191.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from N to Y at position 191.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from D to G at position 194.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from D to N at position 194.
+The protein's natural variant, known as in DRVT; borderline phenotype with spike wave activity;, features a modification of the amino acid from T to R at position 199.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from T to K at position 217.
+The protein's natural variant, known as in GEFSP2; also found in patients with Panayiotopoulos syndrome;, features a modification of the amino acid from F to L at position 218.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from A to E at position 223.
+The protein's natural variant, known as in DEE6B;, features a modification of the amino acid from T to M at position 226.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from T to R at position 226.
+The protein's natural variant, known as in DRVT; borderline phenotype with spike wave activity in some patients; results in a non-functional channel;, features a modification of the amino acid from I to S at position 227.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from I to T at position 227.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from S to P at position 228.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from G to S at position 232.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from L to R at position 233.
+The protein's natural variant, known as in DRVT; borderline phenotype with spike wave activity in some patients;, features a modification of the amino acid from A to T at position 239.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from A to V at position 239.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from S to Y at position 243.
+The protein's natural variant, known as in ICEGTC, features a modification of the amino acid from I to M at position 252.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from I to N at position 252.
+The protein's natural variant, known as in GEFSP2, features a modification of the amino acid from T to I at position 254.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from S to R at position 259.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from G to W at position 265.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from C to R at position 277.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from W to C at position 280.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from W to R at position 280.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from P to A at position 281.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from P to L at position 281.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from P to S at position 281.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from E to V at position 289.
+The protein's natural variant, known as in ICEGTC, features a modification of the amino acid from H to R at position 290.
+The protein's natural variant, known as in GEFSP2, features a modification of the amino acid from S to G at position 291.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from T to I at position 297.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from R to I at position 322.
+The natural variant of this protein is characterized by an amino acid alteration from A to V at position 333.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from S to F at position 340.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from A to V at position 342.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from G to D at position 343.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from C to R at position 345.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from C to W at position 351.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from G to D at position 355.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from R to G at position 356.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from N to I at position 357.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from P to T at position 358.
+The protein's natural variant, known as in DRVT and ICEGTC;, features a modification of the amino acid from N to S at position 359.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from T to P at position 363.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from T to R at position 363.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from D to E at position 366.
+The protein's natural variant, known as in GEFSP2;, features a modification of the amino acid from R to Q at position 377.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from L to Q at position 378.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from M to R at position 379.
+The protein's natural variant, known as probable disease-associated variant found in a patient with an unclassified form of epilepsy, features a modification of the amino acid from D to N at position 382.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from F to L at position 383.
+The protein's natural variant, known as in DRVT; borderline phenotype;, features a modification of the amino acid from W to R at position 384.
+The protein's natural variant, known as in GEFSP2;, features a modification of the amino acid from Y to H at position 388.
+The protein's natural variant, known as in DRVT; also in a patient with myoclonic astatic epilepsy;, features a modification of the amino acid from R to C at position 393.
+The protein's natural variant, known as in DRVT and ICEGTC; results in a non-functional channel;, features a modification of the amino acid from R to H at position 393.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from R to S at position 393.
+The protein's natural variant, known as probable disease-associated variant found in a patient with cryptogenic generalized epilepsy;, features a modification of the amino acid from A to P at position 395.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from M to V at position 400.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from F to L at position 403.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from F to V at position 403.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from V to F at position 406.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from L to W at position 409.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from Y to N at position 413.
+The protein's natural variant, known as probable disease-associated variant found in a patient with cryptogenic generalized epilepsy;, features a modification of the amino acid from V to E at position 422.
+The protein's natural variant, known as in DEE6B, features a modification of the amino acid from V to L at position 422.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from Y to C at position 426.
+The protein's natural variant, known as in DRVT; results in decreased peak current densities; causes a negative shift in the half-maximal steady-state inactivation and delayed recovery from fast inactivation;, features a modification of the amino acid from Y to N at position 426.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from S to F at position 525.
+The protein's natural variant, known as found in a patient with intractable epilepsy and in a patient with generalized epilepsy with febril seizures; also found in patients with autism; unknown pathological significance;, features a modification of the amino acid from R to Q at position 542.
+The protein's natural variant, known as probable disease-associated variant found in a patient with drug-resistant epilepsy and mild cognitive impairment;, features a modification of the amino acid from E to D at position 616.
+The protein's natural variant, known as in DRVT; also found in a patient with cryptogenic generalized epilepsy;, features a modification of the amino acid from S to G at position 626.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from D to G at position 674.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from N to D at position 762.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from L to P at position 783.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from M to T at position 785.
+The protein's natural variant, known as in GEFSP2;, features a modification of the amino acid from Y to C at position 790.
+The protein's natural variant, known as probable disease-associated variant found in patients with Panayiotopoulos syndrome;, features a modification of the amino acid from Y to F at position 790.
+The protein's natural variant, known as in ICEGTC; results in increased peak current density and delayed slow inactivation onset; recovery from slow inactivation is delayed;, features a modification of the amino acid from T to S at position 808.
+The protein's natural variant, known as in DRVT; borderline phenotype, features a modification of the amino acid from T to I at position 812.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from T to R at position 812.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from L to R at position 842.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from S to R at position 843.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from E to K at position 846.
+The protein's natural variant, known as in GEFSP2 and DRVT; causes a positive shift in the voltage dependence of channel activation, slower recovery from slow inactivation and lower levels of current compared with the wild-type channel;, features a modification of the amino acid from R to C at position 859.
+The protein's natural variant, known as in GEFSP2; results in impaired channel fast inactivation and significantly increased persistent current;, features a modification of the amino acid from R to H at position 859.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from R to G at position 862.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from R to Q at position 862.
+The protein's natural variant, known as in DRVT; results in impaired channel fast inactivation and significantly increased persistent current, features a modification of the amino acid from R to G at position 865.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from T to K at position 875.
+The protein's natural variant, known as in GEFSP2 and DRVT; borderline phenotype;, features a modification of the amino acid from T to M at position 875.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from L to I at position 876.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from L to P at position 890.
+The protein's natural variant, known as in DRVT; borderline phenotype, features a modification of the amino acid from V to F at position 896.
+The protein's natural variant, known as in ICEGTC;, features a modification of the amino acid from V to I at position 896.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from V to L at position 896.
+The protein's natural variant, known as in GEFSP2, features a modification of the amino acid from I to T at position 899.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from F to C at position 902.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from C to F at position 927.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from R to C at position 931.
+The protein's natural variant, known as probable disease-associated variant found in a patient with an unclassified form of epilepsy;, features a modification of the amino acid from R to H at position 931.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from W to C at position 932.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from H to P at position 933.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from M to I at position 934.
+The protein's natural variant, known as in GEFSP2, features a modification of the amino acid from N to H at position 935.
+The protein's natural variant, known as in DRVT; unknown pathological significance, features a modification of the amino acid from H to P at position 939.
+The protein's natural variant, known as in DRVT; results in a non-functional channel;, features a modification of the amino acid from H to Q at position 939.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from H to Y at position 939.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from S to F at position 940.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from L to P at position 942.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from I to N at position 943.
+The protein's natural variant, known as in DRVT and ICEGTC;, features a modification of the amino acid from V to A at position 944.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from V to E at position 944.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from F to L at position 945.
+The protein's natural variant, known as in DRVT; loss-of-function mutation resulting in complete absence of sodium current;, features a modification of the amino acid from R to C at position 946.
+The protein's natural variant, known as in DRVT and GEFSP2; GEFSP2 phenotype consists of partial epilepsy with antecedent febrile seizures and seizure aggravation by antiepileptic drugs; loss-of-function mutation resulting in complete absence of sodium current;, features a modification of the amino acid from R to H at position 946.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from R to S at position 946.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from C to S at position 949.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from C to Y at position 949.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from G to E at position 950.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from G to R at position 950.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from W to G at position 952.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from E to K at position 954.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from M to K at position 956.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from W to L at position 957.
+The protein's natural variant, known as in DRVT; results in a non-functional channel;, features a modification of the amino acid from C to R at position 959.
+The protein's natural variant, known as in GEFSP2, features a modification of the amino acid from M to T at position 960.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from M to V at position 960.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from M to K at position 973.
+The protein's natural variant, known as in GEFSP2;, features a modification of the amino acid from M to V at position 973.
+The protein's natural variant, known as in DRVT and GEFSP2, features a modification of the amino acid from M to I at position 976.
+The protein's natural variant, known as in GEFSP2; unknown pathological significance, features a modification of the amino acid from I to M at position 978.
+The protein's natural variant, known as in ICEGTC; loss-of-function mutation resulting in absence of sodium current;, features a modification of the amino acid from G to R at position 979.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from G to V at position 979.
+The protein's natural variant, known as found in a patient with acute encephalopathy with biphasic seizures and late reduced diffusion; unknown pathological significance, features a modification of the amino acid from V to L at position 982.
+The protein's natural variant, known as in ICEGTC; reduced function; decreased peak current density; results in a negative shift of inactivation and positive shift of activation;, features a modification of the amino acid from V to A at position 983.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from N to I at position 985.
+The protein's natural variant, known as in DRVT; complete loss of function;, features a modification of the amino acid from L to F at position 986.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from L to P at position 986.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from F to L at position 987.
+The protein's natural variant, known as in DRVT; borderline phenotype, features a modification of the amino acid from S to R at position 993.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from D to G at position 998.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from NL to LIS at position 1000.
+The protein's natural variant, known as probable disease-associated variant found in a patient with an unclassified form of epilepsy;, features a modification of the amino acid from D to E at position 1006.
+The protein's natural variant, known as in ICEGTC; results in reduced peak current density and hyperpolarizing shift in inactivation;, features a modification of the amino acid from N to I at position 1011.
+The protein's natural variant, known as associated with autism;, features a modification of the amino acid from I to T at position 1034.
+The protein's natural variant, known as associated with autism, features a modification of the amino acid from F to L at position 1038.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from E to K at position 1068.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 1079.
+The protein's natural variant, known as in FHM3;, features a modification of the amino acid from T to S at position 1174.
+The protein's natural variant, known as in GEFSP2; causes hyperpolarized shifts in the voltage dependence of activation and steady-state inactivation;, features a modification of the amino acid from W to R at position 1204.
+The protein's natural variant, known as in GEFSP2, features a modification of the amino acid from W to S at position 1204.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from L to P at position 1207.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from R to K at position 1208.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from T to K at position 1210.
+The protein's natural variant, known as in ICEGTC;, features a modification of the amino acid from R to Q at position 1213.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from E to K at position 1221.
+The protein's natural variant, known as in DRVT and GEFSP2, features a modification of the amino acid from L to F at position 1230.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from S to R at position 1231.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from S to T at position 1231.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from G to R at position 1233.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from E to D at position 1238.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from D to G at position 1239.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from D to Y at position 1239.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from R to Q at position 1245.
+The protein's natural variant, known as in GEFSP2, features a modification of the amino acid from K to N at position 1249.
+The protein's natural variant, known as in GEFSP2;, features a modification of the amino acid from T to M at position 1250.
+The protein's natural variant, known as in ICEGTC, features a modification of the amino acid from Y to C at position 1254.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from A to D at position 1255.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from T to P at position 1260.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from F to L at position 1263.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from L to P at position 1265.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from E to A at position 1266.
+The protein's natural variant, known as in GEFSP2;, features a modification of the amino acid from K to T at position 1270.
+The protein's natural variant, known as found in a child with sporadic epilepsy; unknown pathological significance, features a modification of the amino acid from G to A at position 1275.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from G to V at position 1275.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from W to S at position 1284.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from L to P at position 1287.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from D to N at position 1288.
+The protein's natural variant, known as in FEB3A; also found in patients with early infantile epileptic encephalopathy; unknown pathological significance;, features a modification of the amino acid from E to D at position 1308.
+The protein's natural variant, known as in GEFSP2;, features a modification of the amino acid from L to F at position 1309.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from R to G at position 1316.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from R to S at position 1316.
+The protein's natural variant, known as in DRVT; borderline phenotype, features a modification of the amino acid from A to V at position 1320.
+The protein's natural variant, known as in ICEGTC, features a modification of the amino acid from R to T at position 1325.
+The protein's natural variant, known as probable disease-associated variant found in a patient with an unclassified form of epilepsy, features a modification of the amino acid from A to D at position 1326.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from A to P at position 1326.
+The protein's natural variant, known as in ICEGTC and DRVT, features a modification of the amino acid from S to P at position 1328.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from V to M at position 1335.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from A to V at position 1339.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from I to M at position 1344.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from P to L at position 1345.
+The protein's natural variant, known as in DEE6B, features a modification of the amino acid from P to S at position 1345.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from V to G at position 1350.
+The protein's natural variant, known as in GEFSP2; complete loss of function;, features a modification of the amino acid from V to L at position 1353.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from L to P at position 1355.
+The protein's natural variant, known as in ICEGTC, features a modification of the amino acid from F to L at position 1357.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from W to R at position 1358.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from W to S at position 1358.
+The protein's natural variant, known as in GEFSP2 and ICEGTC;, features a modification of the amino acid from V to I at position 1366.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from N to K at position 1367.
+The protein's natural variant, known as in DRVT; borderline phenotype, features a modification of the amino acid from A to P at position 1370.
+The protein's natural variant, known as in ICEGTC, features a modification of the amino acid from C to R at position 1376.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from N to H at position 1378.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from N to T at position 1378.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from F to V at position 1385.
+The protein's natural variant, known as in DRVT; some patients have a borderline DRVT phenotype;, features a modification of the amino acid from V to M at position 1390.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from N to S at position 1391.
+The protein's natural variant, known as in DRVT; borderline phenotype, features a modification of the amino acid from H to P at position 1393.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from T to I at position 1394.
+The protein's natural variant, known as in DRVT; some patients have a borderline DRVT phenotype;, features a modification of the amino acid from C to G at position 1396.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from C to Y at position 1396.
+The protein's natural variant, known as in GEFSP2, features a modification of the amino acid from N to D at position 1414.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from N to Y at position 1414.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from D to G at position 1416.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from N to S at position 1417.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from V to G at position 1418.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from Y to C at position 1422.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from L to F at position 1423.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from L to R at position 1426.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from Q to P at position 1427.
+The protein's natural variant, known as in GEFSP2;, features a modification of the amino acid from V to A at position 1428.
+The protein's natural variant, known as in ICEGTC, features a modification of the amino acid from A to D at position 1429.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from F to I at position 1431.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from G to E at position 1433.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from G to R at position 1433.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from G to V at position 1433.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from W to R at position 1434.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from I to M at position 1437.
+The protein's natural variant, known as found in a patient with autism; unknown pathological significance;, features a modification of the amino acid from A to V at position 1440.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from A to P at position 1441.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from Q to K at position 1450.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from Q to R at position 1450.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from P to L at position 1451.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from P to S at position 1451.
+The protein's natural variant, known as in DRVT; borderline phenotype, features a modification of the amino acid from Y to C at position 1453.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from E to K at position 1454.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from L to I at position 1461.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from Y to C at position 1462.
+The protein's natural variant, known as in DRVT and ICEGTC; borderline DRVT phenotype;, features a modification of the amino acid from Y to H at position 1462.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from F to S at position 1463.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from G to W at position 1470.
+The protein's natural variant, known as in DRVT; borderline phenotype, features a modification of the amino acid from F to S at position 1472.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from L to S at position 1475.
+The protein's natural variant, known as in DRVT; borderline phenotype, features a modification of the amino acid from N to K at position 1476.
+The protein's natural variant, known as probable disease-associated variant found in a patient with myoclonic astatic epilepsy;, features a modification of the amino acid from G to V at position 1480.
+The protein's natural variant, known as probable disease-associated variant found in a patient with an unclassified form of epilepsy, features a modification of the amino acid from I to M at position 1483.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from D to G at position 1484.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from N to Y at position 1485.
+The protein's natural variant, known as in FHM3;, features a modification of the amino acid from Q to H at position 1489.
+The protein's natural variant, known as in FHM3;, features a modification of the amino acid from Q to K at position 1489.
+The protein's natural variant, known as in FHM3;, features a modification of the amino acid from F to L at position 1499.
+The protein's natural variant, known as in DRVT; borderline phenotype, features a modification of the amino acid from E to K at position 1503.
+The protein's natural variant, known as in ICEGTC, features a modification of the amino acid from M to K at position 1511.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from L to S at position 1514.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from V to I at position 1538.
+The protein's natural variant, known as in a patient with cryptogenic focal epilepsy;, features a modification of the amino acid from F to S at position 1543.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from D to A at position 1544.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from D to G at position 1544.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from I to V at position 1545.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from M to R at position 1555.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from E to K at position 1561.
+The protein's natural variant, known as found in a patient with intractable epilepsy and patients with Dravet syndrome; found in a patient with acute necrotizing encephalopathy and also found in a patient with acute encephalopathy with biphasic seizures and late reduced diffusion; unknown pathological significance;, features a modification of the amino acid from R to C at position 1575.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from V to E at position 1579.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from G to E at position 1586.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from C to R at position 1588.
+The protein's natural variant, known as in DRVT; borderline phenotype, features a modification of the amino acid from L to H at position 1592.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from L to P at position 1592.
+The protein's natural variant, known as in DRVT; also found in a patient with cryptogenic focal epilepsy;, features a modification of the amino acid from R to C at position 1596.
+The protein's natural variant, known as in GEFSP2;, features a modification of the amino acid from R to H at position 1596.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from R to L at position 1596.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from N to I at position 1605.
+The protein's natural variant, known as in DRVT; borderline phenotype, features a modification of the amino acid from N to S at position 1605.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from D to G at position 1608.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from D to Y at position 1608.
+The protein's natural variant, known as in ICEGTC; results in greater levels of persistent non-inactivating current compared to wild-type;, features a modification of the amino acid from V to F at position 1611.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from V to I at position 1612.
+The protein's natural variant, known as in ICEGTC;, features a modification of the amino acid from M to V at position 1619.
+The protein's natural variant, known as in DRVT; borderline phenotype in some patients;, features a modification of the amino acid from V to L at position 1630.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from V to M at position 1630.
+The protein's natural variant, known as in ICEGTC; results in greater levels of persistent non-inactivating current compared to wild-type;, features a modification of the amino acid from P to S at position 1632.
+The protein's natural variant, known as probable disease-associated variant found in a patient with Lennon-Gastaut syndrome;, features a modification of the amino acid from R to Q at position 1636.
+The protein's natural variant, known as in DRVT; also found in a child with febrile status epilepticus who developed liver failure;, features a modification of the amino acid from V to E at position 1637.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from I to N at position 1638.
+The protein's natural variant, known as in DRVT; also found in a patient with an unclassified form of epilepsy, features a modification of the amino acid from I to T at position 1638.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from R to G at position 1639.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from R to S at position 1642.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from R to Q at position 1645.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from R to C at position 1648.
+The protein's natural variant, known as in GEFSP2 and DRVT;, features a modification of the amino acid from R to H at position 1648.
+The protein's natural variant, known as in FHM3, features a modification of the amino acid from L to Q at position 1649.
+The protein's natural variant, known as in DRVT; borderline phenotype, features a modification of the amino acid from A to E at position 1653.
+The protein's natural variant, known as in GEFSP2; exhibits a depolarizing shift in the voltage dependence of activation;, features a modification of the amino acid from I to M at position 1656.
+The protein's natural variant, known as in GEFSP2; exhibits a depolarizing shift in the voltage dependence of activation; shows a 50% reduction in current density and accelerates recovery from slow inactivation;, features a modification of the amino acid from R to C at position 1657.
+The protein's natural variant, known as probable disease-associated variant found in a patient with cryptogenic focal epilepsy;, features a modification of the amino acid from R to H at position 1657.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from T to M at position 1658.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from T to R at position 1658.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from L to P at position 1660.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from F to S at position 1661.
+The protein's natural variant, known as in DRVT; borderline phenotype;, features a modification of the amino acid from A to V at position 1662.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from M to K at position 1664.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from L to P at position 1667.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from P to A at position 1668.
+The protein's natural variant, known as in DRVT; borderline phenotype, features a modification of the amino acid from P to L at position 1668.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from A to E at position 1669.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from N to I at position 1672.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from I to T at position 1673.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from G to R at position 1674.
+The protein's natural variant, known as found in a patient acute encephalopathy with biphasic seizures and late reduced diffusion; unknown pathological significance, features a modification of the amino acid from G to S at position 1674.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from L to R at position 1675.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from L to F at position 1677.
+The protein's natural variant, known as probable disease-associated variant found in a patient with an unclassified form of epilepsy, features a modification of the amino acid from I to F at position 1683.
+The protein's natural variant, known as in DRVT; borderline phenotype, features a modification of the amino acid from I to T at position 1683.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from Y to D at position 1684.
+The protein's natural variant, known as in ICEGTC, features a modification of the amino acid from Y to S at position 1684.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from A to D at position 1685.
+The protein's natural variant, known as in GEFSP2; complete loss of function;, features a modification of the amino acid from A to V at position 1685.
+The protein's natural variant, known as in GEFSP2;, features a modification of the amino acid from F to S at position 1687.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from G to W at position 1688.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from F to S at position 1692.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from Y to C at position 1694.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from F to V at position 1707.
+The protein's natural variant, known as in ICEGTC; loss-of-function mutation resulting in absence of sodium current;, features a modification of the amino acid from T to I at position 1709.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from S to N at position 1713.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from M to K at position 1714.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from M to R at position 1714.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from C to R at position 1716.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from T to R at position 1721.
+The protein's natural variant, known as in ICEGTC, features a modification of the amino acid from A to P at position 1724.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from G to C at position 1725.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from W to R at position 1726.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from D to G at position 1727.
+The protein's natural variant, known as in GEFSP2, features a modification of the amino acid from P to L at position 1739.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from C to R at position 1741.
+The protein's natural variant, known as in GEFSP2;, features a modification of the amino acid from D to G at position 1742.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from G to E at position 1749.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from C to G at position 1756.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from G to E at position 1762.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from I to N at position 1763.
+The protein's natural variant, known as in GEFSP2; disease phenotype consists of partial epilepsy with antecedent febrile seizures and seizure aggravation by antiepileptic drugs; loss-of-function mutation resulting in complete absence of sodium current, features a modification of the amino acid from F to L at position 1765.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from I to F at position 1770.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from I to N at position 1770.
+The protein's natural variant, known as in DRVT; borderline phenotype, features a modification of the amino acid from I to T at position 1770.
+The protein's natural variant, known as in DRVT; borderline phenotype; also found in a patient with focal epilepsy, features a modification of the amino acid from I to F at position 1771.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from I to N at position 1771.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from S to F at position 1773.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from M to T at position 1780.
+The protein's natural variant, known as in DRVT and ICEGTC;, features a modification of the amino acid from Y to C at position 1781.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from Y to H at position 1781.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from I to M at position 1782.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from I to S at position 1782.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from A to T at position 1783.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from A to V at position 1783.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from E to K at position 1787.
+The protein's natural variant, known as in DRVT; unknown pathological significance;, features a modification of the amino acid from N to K at position 1788.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from A to T at position 1792.
+The protein's natural variant, known as in GEFSP2;, features a modification of the amino acid from E to K at position 1795.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from F to I at position 1808.
+The protein's natural variant, known as in ICEGTC; results in decreased peak current density but significantly greater levels of persistent non-inactivating current compared to wild-type channel;, features a modification of the amino acid from F to L at position 1808.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from WEKF to C at position 1815.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from W to G at position 1812.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from W to S at position 1812.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from F to S at position 1831.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from A to P at position 1832.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from L to F at position 1835.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from M to K at position 1852.
+The protein's natural variant, known as in GEFSP2; loss of function; defective trafficking to cell membrane and no inhibition of its interaction with SCN1B;, features a modification of the amino acid from M to T at position 1852.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from P to L at position 1855.
+The protein's natural variant, known as in GEFSP2;, features a modification of the amino acid from V to L at position 1857.
+The protein's natural variant, known as in ICEGTC, features a modification of the amino acid from R to W at position 1861.
+The protein's natural variant, known as in GEFSP2; causes a positive shift in the voltage dependence of sodium channel fast inactivation; causes an increase in the magnitude of the persistent current; causes delay in the kinetics of inactivation and significantly reduces interaction with SCN1B;, features a modification of the amino acid from D to Y at position 1866.
+The protein's natural variant, known as in GEFSP2;, features a modification of the amino acid from I to T at position 1867.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from G to E at position 1880.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from E to D at position 1881.
+The protein's natural variant, known as in DRVT; functional channel displaying decreased peak current densities but increased persistent current;, features a modification of the amino acid from T to I at position 1909.
+The protein's natural variant, known as in DRVT;, features a modification of the amino acid from I to T at position 1922.
+The protein's natural variant, known as in DRVT, features a modification of the amino acid from R to IIQ at position 1927.
+The protein's natural variant, known as in infantile spasms;, features a modification of the amino acid from E to G at position 1957.
+The protein's natural variant, known as found in a patient with febrile seizures and non-specific acute encephalopathy; unknown pathological significance, features a modification of the amino acid from M to L at position 1977.
+The protein's natural variant, known as found in a patient with epilepsy-aphasia and febrile seizures plus; unknown pathological significance;, features a modification of the amino acid from R to W at position 1988.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to W at position 1410.
+The protein's natural variant, known as in EHK, features a modification of the amino acid from S to P at position 194.
+The protein's natural variant, known as in PCH1D; reduced EXOSC9 and exosome levels in patient cells;, features a modification of the amino acid from L to P at position 14.
+The protein's natural variant, known as in DEE66; increased interaction with SIRT1; increased interaction with HDAC1; increased interaction with TRPV1;, features a modification of the amino acid from E to K at position 209.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 44.
+The natural variant of this protein is characterized by an amino acid alteration from R to Q at position 47.
+The natural variant of this protein is characterized by an amino acid alteration from E to D at position 55.
+The natural variant of this protein is characterized by an amino acid alteration from R to H at position 60.
+The natural variant of this protein is characterized by an amino acid alteration from N to S at position 61.
+The natural variant of this protein is characterized by an amino acid alteration from E to G at position 77.
+The natural variant of this protein is characterized by an amino acid alteration from G to A at position 95.
+The natural variant of this protein is characterized by an amino acid alteration from E to G at position 282.
+The natural variant of this protein is characterized by an amino acid alteration from G to D at position 298.
+The protein's natural variant, known as in MLA', features a modification of the amino acid from E to D at position 48.
+The protein's natural variant, known as in MLA', features a modification of the amino acid from N to T at position 145.
+The protein's natural variant, known as in MLA', features a modification of the amino acid from P to T at position 149.
+The protein's natural variant, known as in MLA', features a modification of the amino acid from DQ to EE at position 167.
+The protein's natural variant, known as in MLA', features a modification of the amino acid from T to S at position 173.
+The protein's natural variant, known as in MLA', features a modification of the amino acid from F to Y at position 177.
+The protein's natural variant, known as in MLA', features a modification of the amino acid from T to A at position 184.
+The protein's natural variant, known as in MLA', features a modification of the amino acid from Y to D at position 212.
+The protein's natural variant, known as in MLA', features a modification of the amino acid from A to E at position 217.
+The protein's natural variant, known as in MLA', features a modification of the amino acid from V to M at position 223.
+The protein's natural variant, known as in MLA', features a modification of the amino acid from I to F at position 251.
+The protein's natural variant, known as in MLA', features a modification of the amino acid from PP to ST at position 257.
+The protein's natural variant, known as in MLA', features a modification of the amino acid from T to S at position 264.
+The protein's natural variant, known as in MLA', features a modification of the amino acid from D to S at position 268.
+The natural variant of this protein is characterized by an amino acid alteration from N to S at position 319.
+The natural variant of this protein is characterized by an amino acid alteration from G to N at position 357.
+The natural variant of this protein is characterized by an amino acid alteration from G to Q at position 458.
+The natural variant of this protein is characterized by an amino acid alteration from C to V at position 495.
+The natural variant of this protein is characterized by an amino acid alteration from G to Y at position 524.
+The natural variant of this protein is characterized by an amino acid alteration from NGL to KGP at position 533.
+The natural variant of this protein is characterized by an amino acid alteration from N to S at position 531.
+The natural variant of this protein is characterized by an amino acid alteration from N to T at position 531.
+The natural variant of this protein is characterized by an amino acid alteration from GLAM to SLMV at position 535.
+The protein's natural variant, known as in ATRX, features a modification of the amino acid from G to E at position 175.
+The protein's natural variant, known as in ATRX;, features a modification of the amino acid from N to S at position 179.
+The protein's natural variant, known as in ATRX; impairs interaction with histone H3 peptides and reduces localization to pericentromeric heterochromatin foci;, features a modification of the amino acid from P to A at position 190.
+The protein's natural variant, known as in ATRX;, features a modification of the amino acid from P to L at position 190.
+The protein's natural variant, known as in ATRX, features a modification of the amino acid from P to S at position 190.
+The protein's natural variant, known as in ATRX, features a modification of the amino acid from L to F at position 192.
+The protein's natural variant, known as in ATRX, features a modification of the amino acid from V to I at position 194.
+The protein's natural variant, known as in ATRX, features a modification of the amino acid from C to S at position 200.
+The protein's natural variant, known as in ATRX; greatly impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3) and reduces localization to pericentromeric heterochromatin foci, features a modification of the amino acid from Q to P at position 219.
+The protein's natural variant, known as in ATRX, features a modification of the amino acid from C to R at position 220.
+The protein's natural variant, known as in MRXHF1;, features a modification of the amino acid from C to Y at position 220.
+The protein's natural variant, known as in ATRX, features a modification of the amino acid from W to S at position 222.
+The protein's natural variant, known as in ATRX, features a modification of the amino acid from C to F at position 243.
+The protein's natural variant, known as in ATRX; impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3) and reduces localization to pericentromeric heterochromatin foci;, features a modification of the amino acid from R to C at position 246.
+The protein's natural variant, known as in ATRX; impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3);, features a modification of the amino acid from R to L at position 246.
+The protein's natural variant, known as in ATRX, features a modification of the amino acid from G to C at position 249.
+The protein's natural variant, known as in ATRX; impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3); loss of heterochromatic localization, features a modification of the amino acid from G to D at position 249.
+The protein's natural variant, known as in MRXHF1;, features a modification of the amino acid from L to S at position 409.
+The protein's natural variant, known as in ATRX; unknown pathological significance, features a modification of the amino acid from V to G at position 1538.
+The protein's natural variant, known as in ATRX;, features a modification of the amino acid from V to F at position 1552.
+The protein's natural variant, known as in ATRX;, features a modification of the amino acid from H to R at position 1609.
+The protein's natural variant, known as in ATRX;, features a modification of the amino acid from C to R at position 1614.
+The protein's natural variant, known as in ATRX;, features a modification of the amino acid from T to M at position 1621.
+The protein's natural variant, known as in ATRX, features a modification of the amino acid from L to S at position 1645.
+The protein's natural variant, known as in ATRX;, features a modification of the amino acid from K to N at position 1650.
+The protein's natural variant, known as in ATRX; without alpha-thalassemia, features a modification of the amino acid from P to S at position 1713.
+The protein's natural variant, known as in ATRX; atypical; patients presents spastic paraplegia at birth;, features a modification of the amino acid from R to K at position 1742.
+The protein's natural variant, known as in ATRX, features a modification of the amino acid from Y to C at position 1847.
+The protein's natural variant, known as in ATRX; impairs ATPase activity;, features a modification of the amino acid from D to V at position 2035.
+The protein's natural variant, known as in MRXHF1; originally reported as Carpenter-Waziri syndrome;, features a modification of the amino acid from I to T at position 2050.
+The protein's natural variant, known as in ATRX; impairs ATPase activity;, features a modification of the amino acid from Y to H at position 2084.
+The protein's natural variant, known as in MRXHF1; originally reported as Juberg-Marsidi syndrome;, features a modification of the amino acid from R to Q at position 2131.
+The protein's natural variant, known as in ATRX;, features a modification of the amino acid from Y to C at position 2163.
+The protein's natural variant, known as in MRXHF1;, features a modification of the amino acid from R to G at position 2271.
+The protein's natural variant, known as in strain: DPF-2, DPF-30, DPF-62, MA-10.2, DPF-82.1, 178.7, DPF-13, MA-4.4, EM-10, VC-805, MA-4.2, DPF-46, DPF-77, VC-815 and 709.6, features a modification of the amino acid from N to K at position 368.
+The protein's natural variant, known as in LGMDR4;, features a modification of the amino acid from Q to E at position 11.
+The protein's natural variant, known as in LGMDR4;, features a modification of the amino acid from R to C at position 91.
+The protein's natural variant, known as in LGMDR4;, features a modification of the amino acid from R to L at position 91.
+The protein's natural variant, known as in LGMDR4;, features a modification of the amino acid from R to P at position 91.
+The protein's natural variant, known as in LGMDR4;, features a modification of the amino acid from M to K at position 100.
+The protein's natural variant, known as in LGMDR4;, features a modification of the amino acid from L to R at position 108.
+The protein's natural variant, known as in LGMDR4;, features a modification of the amino acid from S to F at position 114.
+The protein's natural variant, known as in LGMDR4;, features a modification of the amino acid from I to F at position 119.
+The protein's natural variant, known as in LGMDR4;, features a modification of the amino acid from G to D at position 139.
+The protein's natural variant, known as in LGMDR4;, features a modification of the amino acid from T to R at position 151.
+The protein's natural variant, known as in LGMDR4;, features a modification of the amino acid from G to S at position 167.
+The protein's natural variant, known as in LGMDR4, features a modification of the amino acid from T to A at position 182.
+The protein's natural variant, known as probable disease-associated variant found in a patient with a myopathy resembling Becker muscular dystrophy;, features a modification of the amino acid from Y to C at position 184.
+The protein's natural variant, known as in COXPD41; unknown pathological significance;, features a modification of the amino acid from F to L at position 136.
+The protein's natural variant, known as in DEE32; affects channel activity; mutant channels display voltage-dependent activation significantly shifted toward negative potentials compared to wild-type; no effect on channel sensitivity to 4-aminopyridine, features a modification of the amino acid from E to K at position 236.
+The protein's natural variant, known as in DEE32; dominant-negative mutation; loss of channel function;, features a modification of the amino acid from I to T at position 263.
+The protein's natural variant, known as in DEE32; causes a gain of function;, features a modification of the amino acid from R to Q at position 297.
+The protein's natural variant, known as in DEE32; causes a gain of function;, features a modification of the amino acid from L to F at position 298.
+The protein's natural variant, known as probable disease-associated variant found in a patient with drug-resistant epilepsy, features a modification of the amino acid from S to T at position 324.
+The protein's natural variant, known as in DEE32; loss of channel function;, features a modification of the amino acid from P to L at position 405.
+The protein's natural variant, known as in FIH1; dominant form; leads to inefficient processing of the precursor; the expressed mutant hormone is trapped intracellularly in the endoplasmic reticulum resulting in apoptosis; mutant protein-expressing cells also show marked up-regulation of the endoplasmic reticulum stress-responsive hormones HSPA5 and EIF2AK3 and the proapoptotic transcription factor DDIT3;, features a modification of the amino acid from C to R at position 18.
+The protein's natural variant, known as in FIH1; recessive form; might lead to inefficient processing of the precursor;, features a modification of the amino acid from S to P at position 23.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from H to Y at position 874.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from D to H at position 187.
+The protein's natural variant, known as in RBMX1A; unknown pathological significance, features a modification of the amino acid from C to F at position 101.
+The protein's natural variant, known as in RBMX1B; unknown pathological significance;, features a modification of the amino acid from C to R at position 104.
+The protein's natural variant, known as in SPM;, features a modification of the amino acid from W to S at position 122.
+The protein's natural variant, known as in RBMX1A;, features a modification of the amino acid from H to L at position 123.
+The protein's natural variant, known as in RBMX1A;, features a modification of the amino acid from H to Q at position 123.
+The protein's natural variant, known as in RBMX1A; the mutant protein initiates aggregation of the FHL1 protein causing reducing bodies formation; dominant-negative effect;, features a modification of the amino acid from H to Y at position 123.
+The protein's natural variant, known as in XMPMA, features a modification of the amino acid from T to TI at position 128.
+The protein's natural variant, known as in RBMX1A; the mutant protein initiates aggregation of the FHL1 protein causing reducing bodies formation; dominant-negative effect;, features a modification of the amino acid from C to F at position 132.
+The protein's natural variant, known as in RBMX1B, features a modification of the amino acid from C to S at position 150.
+The protein's natural variant, known as in RBMX1A; unknown pathological significance;, features a modification of the amino acid from C to Y at position 150.
+The protein's natural variant, known as in RBMX1B;, features a modification of the amino acid from C to R at position 153.
+The protein's natural variant, known as in RBMX1B;, features a modification of the amino acid from C to Y at position 153.
+The protein's natural variant, known as in SPM, features a modification of the amino acid from H to P at position 154.
+The protein's natural variant, known as in EDMD6;, features a modification of the amino acid from C to R at position 209.
+The protein's natural variant, known as in XMPMA;, features a modification of the amino acid from C to W at position 224.
+The protein's natural variant, known as in EDMD6; drastically reduced protein levels in muscle, features a modification of the amino acid from C to Y at position 276.
+The protein's natural variant, known as in XMPMA;, features a modification of the amino acid from V to M at position 280.
+The protein's natural variant, known as in strain: Berkeley and L28, features a modification of the amino acid from E to K at position 44.
+The protein's natural variant, known as in strain: L21 and L126, features a modification of the amino acid from E to D at position 72.
+The protein's natural variant, known as in strain: Berkeley and L28, features a modification of the amino acid from A to S at position 149.
+The protein's natural variant, known as in strain: L12, features a modification of the amino acid from Y to H at position 171.
+The protein's natural variant, known as in strain: L126, features a modification of the amino acid from R to S at position 215.
+The protein's natural variant, known as in RIFTD; unknown pathological significance, features a modification of the amino acid from P to T at position 71.
+The protein's natural variant, known as in RIFTD; decreased interaction with MUC2, features a modification of the amino acid from H to Y at position 117.
+The protein's natural variant, known as in RIFTD; unknown pathological significance, features a modification of the amino acid from G to E at position 143.
+The protein's natural variant, known as in strain: cv. VF36, features a modification of the amino acid from I to V at position 87.
+The natural variant of this protein is characterized by an amino acid alteration from E to G at position 54.
+The natural variant of this protein is characterized by an amino acid alteration from K to R at position 69.
+The protein's natural variant, known as does not affect enzyme activity;, features a modification of the amino acid from D to N at position 446.
+The natural variant of this protein is characterized by an amino acid alteration from A to H at position 29.
+The natural variant of this protein is characterized by an amino acid alteration from T to S at position 87.
+The natural variant of this protein is characterized by an amino acid alteration from T to A at position 122.
+The natural variant of this protein is characterized by an amino acid alteration from A to S at position 137.
+The protein's natural variant, known as strongly reduced cis-aconitate decarboxylase activity;, features a modification of the amino acid from T to M at position 97.
+The protein's natural variant, known as increased cis-aconitate decarboxylase activity, features a modification of the amino acid from N to S at position 152.
+The protein's natural variant, known as strongly reduced cis-aconitate decarboxylase activity; reduced protein stability, features a modification of the amino acid from H to Q at position 159.
+The protein's natural variant, known as strongly reduced cis-aconitate decarboxylase activity; reduced protein stability;, features a modification of the amino acid from H to R at position 159.
+The protein's natural variant, known as strongly reduced cis-aconitate decarboxylase activity; reduced protein stability;, features a modification of the amino acid from K to Q at position 272.
+The protein's natural variant, known as does not affect cis-aconitate decarboxylase activity, features a modification of the amino acid from R to H at position 273.
+The protein's natural variant, known as strongly reduced cis-aconitate decarboxylase activity; reduced protein stability;, features a modification of the amino acid from H to Y at position 277.
+The protein's natural variant, known as strongly reduced cis-aconitate decarboxylase activity; reduced protein stability;, features a modification of the amino acid from R to H at position 331.
+The protein's natural variant, known as in strain: Sterne, features a modification of the amino acid from A to S at position 299.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to C at position 831.
+The protein's natural variant, known as in AGS4, features a modification of the amino acid from DL to YP at position 3.
+The protein's natural variant, known as in AGS4; strongly impairs enzyme activity but not interaction with RNASEH2B and RNASEH2C;, features a modification of the amino acid from G to S at position 37.
+The natural variant of this protein is characterized by an amino acid alteration from N to D at position 99.
+The protein's natural variant, known as in AGS4;, features a modification of the amino acid from R to W at position 108.
+The protein's natural variant, known as in AGS4;, features a modification of the amino acid from R to W at position 186.
+The protein's natural variant, known as in AGS4;, features a modification of the amino acid from F to L at position 230.
+The protein's natural variant, known as in AGS4;, features a modification of the amino acid from R to Q at position 235.
+The protein's natural variant, known as in AGS4;, features a modification of the amino acid from T to M at position 240.
+The protein's natural variant, known as in AGS4;, features a modification of the amino acid from R to H at position 291.
+The protein's natural variant, known as resistance to benzimidazole, features a modification of the amino acid from E to G at position 198.
+The protein's natural variant, known as in allele DRB4*01:02, features a modification of the amino acid from D to G at position 105.
+The protein's natural variant, known as in allele DRB4*01:04, features a modification of the amino acid from T to N at position 106.
+The protein's natural variant, known as in allele DRB4*01:05, features a modification of the amino acid from Y to H at position 110.
+The protein's natural variant, known as in allele DRB4*01:07, features a modification of the amino acid from G to R at position 113.
+The protein's natural variant, known as in allele DRB4*01:06, features a modification of the amino acid from H to Y at position 141.
+The protein's natural variant, known as in allele DRB4*01:01 and allele DRB4*01:06, features a modification of the amino acid from G to S at position 164.
+The protein's natural variant, known as in strain: NCTC 12894, features a modification of the amino acid from K to R at position 101.
+The protein's natural variant, known as in strain: NCTC 12894, features a modification of the amino acid from D to N at position 105.
+The protein's natural variant, known as in strain: NCTC 12894, features a modification of the amino acid from E to K at position 176.
+The protein's natural variant, known as in strain: NCTC 12894, features a modification of the amino acid from S to A at position 219.
+The protein's natural variant, known as in strain: NCTC 12894, features a modification of the amino acid from GD to EGE at position 343.
+The protein's natural variant, known as in HLD23; shows decreased beta-catenin binding, features a modification of the amino acid from R to Q at position 363.
+The protein's natural variant, known as in HLD23; shows decreased beta-catenin binding, features a modification of the amino acid from R to Q at position 365.
+The protein's natural variant, known as influences skin pigmentation;, features a modification of the amino acid from Y to H at position 182.
+The protein's natural variant, known as found in a patient with ARSEGS; unknown pathological significance;, features a modification of the amino acid from S to C at position 19.
+The protein's natural variant, known as in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity, features a modification of the amino acid from C to Y at position 207.
+The protein's natural variant, known as in ARSEGS; complete loss of tyrosine 3-monooxygenase activity, features a modification of the amino acid from D to G at position 227.
+The protein's natural variant, known as in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity; shifted substrate specificity from tyrosine to phenylalanine and Dopa;, features a modification of the amino acid from R to H at position 233.
+The protein's natural variant, known as in ARSEGS; severe parkinsonian symptoms in early infancy; strongly reduced stability and tyrosine 3-monooxygenase activity; rare mutation;, features a modification of the amino acid from L to P at position 236.
+The protein's natural variant, known as in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity;, features a modification of the amino acid from A to T at position 241.
+The protein's natural variant, known as in ARSEGS; loss of about 40% of tyrosine 3-monooxygenase activity, features a modification of the amino acid from H to Y at position 246.
+The protein's natural variant, known as in ARSEGS; loss of about 50% of tyrosine 3-monooxygenase activity; shifted substrate specificity from tyrosine to phenylalanine and Dopa;, features a modification of the amino acid from G to S at position 247.
+The protein's natural variant, known as in ARSEGS, features a modification of the amino acid from P to L at position 251.
+The protein's natural variant, known as in ARSEGS; complete loss of tyrosine 3-monooxygenase activity, features a modification of the amino acid from E to G at position 259.
+The protein's natural variant, known as in ARSEGS; parkinsonian symptoms in infancy; no effect on tyrosine 3-monooxygenase activity;, features a modification of the amino acid from T to P at position 276.
+The protein's natural variant, known as in ARSEGS;, features a modification of the amino acid from C to F at position 279.
+The protein's natural variant, known as in ARSEGS;, features a modification of the amino acid from G to R at position 294.
+The protein's natural variant, known as in ARSEGS;, features a modification of the amino acid from R to Q at position 296.
+The protein's natural variant, known as in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity, features a modification of the amino acid from P to A at position 301.
+The protein's natural variant, known as in ARSEGS; complete loss of tyrosine 3-monooxygenase activity, features a modification of the amino acid from F to S at position 309.
+The protein's natural variant, known as in ARSEGS; parkinsonian symptoms in infancy; loss of about 80% of tyrosine 3-monooxygenase activity;, features a modification of the amino acid from T to M at position 314.
+The protein's natural variant, known as in ARSEGS;, features a modification of the amino acid from G to S at position 315.
+The protein's natural variant, known as in ARSEGS; complete loss of tyrosine 3-monooxygenase activity, features a modification of the amino acid from R to P at position 319.
+The protein's natural variant, known as in ARSEGS; complete loss of tyrosine 3-monooxygenase activity;, features a modification of the amino acid from R to W at position 328.
+The protein's natural variant, known as in ARSEGS; parkinsonian symptoms in infancy; no effect on tyrosine 3-monooxygenase activity;, features a modification of the amino acid from R to H at position 337.
+The protein's natural variant, known as in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity;, features a modification of the amino acid from C to F at position 359.
+The protein's natural variant, known as in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity; shifted substrate specificity from tyrosine to phenylalanine and Dopa;, features a modification of the amino acid from F to L at position 375.
+The protein's natural variant, known as in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity, features a modification of the amino acid from A to V at position 376.
+The protein's natural variant, known as in ARSEGS;, features a modification of the amino acid from I to T at position 382.
+The protein's natural variant, known as in ARSEGS;, features a modification of the amino acid from A to V at position 385.
+The protein's natural variant, known as in ARSEGS; no effect on tyrosine 3-monooxygenase activity, features a modification of the amino acid from L to M at position 387.
+The protein's natural variant, known as in ARSEGS; complete loss of tyrosine 3-monooxygenase activity, features a modification of the amino acid from I to T at position 394.
+The protein's natural variant, known as in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity;, features a modification of the amino acid from T to M at position 399.
+The protein's natural variant, known as in ARSEGS;, features a modification of the amino acid from G to R at position 408.
+The protein's natural variant, known as in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity; reduced affinity for L-tyrosine;, features a modification of the amino acid from Q to K at position 412.
+The protein's natural variant, known as in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity;, features a modification of the amino acid from G to R at position 414.
+The protein's natural variant, known as in ARSEGS; phenotype with prominent levodopa-responsive myoconus-dystonia (M-D);, features a modification of the amino acid from G to R at position 428.
+The protein's natural variant, known as in ARSEGS; complete loss of tyrosine 3-monooxygenase activity;, features a modification of the amino acid from R to P at position 441.
+The protein's natural variant, known as in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity, features a modification of the amino acid from S to G at position 467.
+The protein's natural variant, known as in ARSEGS; complete loss of tyrosine 3-monooxygenase activity;, features a modification of the amino acid from P to L at position 492.
+The protein's natural variant, known as in ARSEGS; parkinsonian symptoms in infancy; no effect on tyrosine 3-monooxygenase activity;, features a modification of the amino acid from T to M at position 494.
+The protein's natural variant, known as in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity;, features a modification of the amino acid from D to G at position 498.
+The protein's natural variant, known as in ARSEGS; complete loss of tyrosine 3-monooxygenase activity, features a modification of the amino acid from L to Q at position 510.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from P to A at position 283.
+The protein's natural variant, known as in MCT8 deficiency; impaired homodimerization;, features a modification of the amino acid from S to F at position 120.
+The protein's natural variant, known as in MCT8 deficiency; impaired thyroid hormone transporter activity; does not affect localization to the cell membrane;, features a modification of the amino acid from G to R at position 147.
+The protein's natural variant, known as in MCT8 deficiency; impaired homodimerization;, features a modification of the amino acid from A to T at position 150.
+The protein's natural variant, known as in MCT8 deficiency; does not affect homodimerization activity;, features a modification of the amino acid from A to V at position 150.
+The protein's natural variant, known as in MCT8 deficiency; increased homodimerization activity, features a modification of the amino acid from V to M at position 161.
+The protein's natural variant, known as in MCT8 deficiency; does not affect homodimerization activity;, features a modification of the amino acid from R to H at position 197.
+The protein's natural variant, known as in MCT8 deficiency; impaired thyroid hormone transporter activity; impaired localization to the cell membrane, features a modification of the amino acid from G to C at position 208.
+The protein's natural variant, known as in MCT8 deficiency; decreased thyroid hormone transport; decreased protein abundance; decreased localization to the plasma membrane;, features a modification of the amino acid from S to F at position 216.
+The protein's natural variant, known as in MCT8 deficiency; atypical form; characterized by developmental delay hypotonia and delayed myelination, features a modification of the amino acid from L to R at position 217.
+The protein's natural variant, known as in MCT8 deficiency; impaired thyroid hormone transporter activity; does not affect localization to the cell membrane, features a modification of the amino acid from P to L at position 247.
+The protein's natural variant, known as in MCT8 deficiency; impaired homodimerization;, features a modification of the amino acid from L to W at position 360.
+The protein's natural variant, known as in MCT8 deficiency; impaired homodimerization;, features a modification of the amino acid from R to C at position 371.
+The protein's natural variant, known as in MCT8 deficiency; impaired thyroid hormone transporter activity; does not affect localization to the cell membrane, features a modification of the amino acid from D to V at position 379.
+The protein's natural variant, known as in MCT8 deficiency; does not affect homodimerization activity;, features a modification of the amino acid from L to P at position 397.
+The protein's natural variant, known as in MCT8 deficiency; does not affect homodimerization activity;, features a modification of the amino acid from L to P at position 438.
+The protein's natural variant, known as in MCT8 deficiency; impaired thyroid hormone transporter activity; does not affect localization to the cell membrane, features a modification of the amino acid from P to L at position 463.
+The protein's natural variant, known as in MCT8 deficiency; does not affect homodimerization activity; impaired thyroid hormone transporter activity; impaired localization to the cell membrane, features a modification of the amino acid from G to D at position 484.
+The protein's natural variant, known as in MCT8 deficiency; results in a mild clinical phenotype; retains some residual thyroid hormone transporter activity, features a modification of the amino acid from G to E at position 490.
+The protein's natural variant, known as in MCT8 deficiency; loss of thyroid hormone transport;, features a modification of the amino acid from G to R at position 490.
+The protein's natural variant, known as in MCT8 deficiency; does not affect homodimerization activity;, features a modification of the amino acid from L to P at position 494.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from L to S at position 16.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from I to T at position 19.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from N to S at position 79.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from V to I at position 95.
+The natural variant of this protein is characterized by an amino acid alteration from L to V at position 1165.
+The protein's natural variant, known as in strain: JEC39, JEC55 and JEC60; confers resistance to cycloheximide, an inhibitor of polypeptide elongation, features a modification of the amino acid from P to L at position 56.
+The protein's natural variant, known as in strain: Usa7, Z36, Z50, Zim7, Zim10, Zim13, Zim15, Zim16, Zim18, Zim39 Zim41 and Zim42, features a modification of the amino acid from D to N at position 72.
+The protein's natural variant, known as in HAGGSD; strongly decreased glutamate-cysteine ligase activity;, features a modification of the amino acid from R to C at position 127.
+The protein's natural variant, known as in HAGGSD, features a modification of the amino acid from P to L at position 158.
+The protein's natural variant, known as in HAGGSD;, features a modification of the amino acid from H to L at position 370.
+The natural variant of this protein is characterized by an amino acid alteration from H to A at position 39.
+The natural variant of this protein is characterized by an amino acid alteration from G to L at position 40.
+The natural variant of this protein is characterized by an amino acid alteration from C to N at position 44.
+The natural variant of this protein is characterized by an amino acid alteration from H to S at position 47.
+The natural variant of this protein is characterized by an amino acid alteration from G to T at position 49.
+The natural variant of this protein is characterized by an amino acid alteration from A to Y at position 56.
+The natural variant of this protein is characterized by an amino acid alteration from V to L at position 57.
+The natural variant of this protein is characterized by an amino acid alteration from N to L at position 61.
+The natural variant of this protein is characterized by an amino acid alteration from T to S at position 64.
+The natural variant of this protein is characterized by an amino acid alteration from I to Y at position 75.
+The natural variant of this protein is characterized by an amino acid alteration from L to C at position 78.
+The natural variant of this protein is characterized by an amino acid alteration from D to V at position 81.
+The natural variant of this protein is characterized by an amino acid alteration from C to P at position 95.
+The natural variant of this protein is characterized by an amino acid alteration from V to T at position 98.
+The natural variant of this protein is characterized by an amino acid alteration from T to V at position 108.
+The natural variant of this protein is characterized by an amino acid alteration from V to L at position 111.
+The natural variant of this protein is characterized by an amino acid alteration from I to N at position 114.
+The natural variant of this protein is characterized by an amino acid alteration from A to T at position 115.
+The natural variant of this protein is characterized by an amino acid alteration from P to A at position 116.
+The natural variant of this protein is characterized by an amino acid alteration from S to A at position 118.
+The natural variant of this protein is characterized by an amino acid alteration from V to L at position 127.
+The natural variant of this protein is characterized by an amino acid alteration from M to L at position 128.
+The natural variant of this protein is characterized by an amino acid alteration from D to N at position 131.
+The natural variant of this protein is characterized by an amino acid alteration from V to A at position 133.
+The natural variant of this protein is characterized by an amino acid alteration from I to L at position 144.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from E to Q at position 204.
+The protein's natural variant, known as in strain: YPIII, features a modification of the amino acid from GLDARAKGIH to AGGLNARAKDPY at position 104.
+The protein's natural variant, known as in strain: YPIII, features a modification of the amino acid from A to S at position 124.
+The protein's natural variant, known as in strain: YPIII, features a modification of the amino acid from L to H at position 209.
+The protein's natural variant, known as in strain: YPIII, features a modification of the amino acid from KDN to EDT at position 239.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from L to I at position 360.
+The protein's natural variant, known as appears to be associated with differing disease incubation periods in goats experimentally infected with isolates of bovine spongiform encephalopathy or sheep scrapie, features a modification of the amino acid from I to M at position 142.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to W at position 386.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to W at position 395.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from A to V at position 471.
+The protein's natural variant, known as in strain: XCPA112, features a modification of the amino acid from S to N at position 105.
+The protein's natural variant, known as in strain: XCPA25, features a modification of the amino acid from E to D at position 227.
+The protein's natural variant, known as in strain: XCPA77, XCPA93 and XCPA126, features a modification of the amino acid from G to A at position 290.
+The protein's natural variant, known as in SPTCL; associated with disease susceptibility; results in dysregulated secretion of inflammatory cytokines by macrophages; affects protein folding; decreased localization at the cell membrane;, features a modification of the amino acid from Y to C at position 82.
+The protein's natural variant, known as in SPTCL; associated with disease susceptibility; affects protein folding; decreased localization at the cell membrane;, features a modification of the amino acid from I to M at position 97.
+The protein's natural variant, known as in SPTCL; may be associated with disease susceptibility;, features a modification of the amino acid from T to I at position 101.
+The protein's natural variant, known as in CPVT4; increased RYR2 calcium-release channel activity; not changed calcium-dependent inactivation of L-type calcium channel; not changed protein abundance; not changed structure; not changed thermal stability both in the absence and presence of calcium; no effect on the calcium binding affinity; significantly increased binding of RYR2; increased ryanodine-sensitive calcium-release channel activity; decreased of KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane;, features a modification of the amino acid from N to I at position 54.
+The protein's natural variant, known as in LQT14; significantly decreased of KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane; decreased thermal stability in presence of calcium ions; decreased interaction with RYR2;, features a modification of the amino acid from F to L at position 90.
+The protein's natural variant, known as in CPVT4; the mutant has significantly reduced calcium affinity compared to wild-type; calmodulin-RYR2 interaction is defective at low intracellular Ca(2+) concentrations and restored at moderate to high Ca(2+) concentrations; increased RYR2 calcium-release channel activity; decreased KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane;, features a modification of the amino acid from N to S at position 98.
+The protein's natural variant, known as in LQT14; reduction in calcium affinity; not changed protein abundance; not changed structure; significantly decreased thermal stability in presence of calcium; significantly decreased RYR2 interaction; increased ryanodine-sensitive calcium-release channel activity; decreased of KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane;, features a modification of the amino acid from D to G at position 130.
+The protein's natural variant, known as in LQT14; decreased calcium affinity; loss of CACNA1C calcium-dependent-inactivation; no effect on intracellular RYR2-mediated calcium release, features a modification of the amino acid from E to G at position 141.
+The protein's natural variant, known as in LQT14; loss-of-function variant causing impaired negative regulation of high voltage-gated calcium channel activity; impaired regulation of cardiac muscle cell action potential; decreased calcium ion binding, features a modification of the amino acid from E to V at position 141.
+The protein's natural variant, known as in LQT14; reduction in calcium affinity; not changed protein abundance; not changed structure; significantly decreased thermal stability in presence of calcium; no effect on RYR2 interaction; significantly reduced ryanodine-sensitive calcium-release channel activity; impaired negative regulation of high voltage-gated calcium channel activity; impaired regulation of cardiac muscle cell action potential;, features a modification of the amino acid from F to L at position 142.
+The protein's natural variant, known as in strain: CB4856 and CB4857, features a modification of the amino acid from A to S at position 12.
+The protein's natural variant, known as in strain: AB1, AB2, CB4852, CB4853, CB4855, CB4857, CB4858, KR314 and PB306, features a modification of the amino acid from I to M at position 466.
+The protein's natural variant, known as in strain: 129/SvEv; requires 2 nucleotide substitutions, features a modification of the amino acid from P to E at position 41.
+The protein's natural variant, known as in strain: 129/SvEv, features a modification of the amino acid from TIT to NIK at position 47.
+The protein's natural variant, known as in strain: 129/SvEv, features a modification of the amino acid from Q to H at position 52.
+The protein's natural variant, known as in strain: 129/SvEv, features a modification of the amino acid from R to W at position 55.
+The protein's natural variant, known as in strain: 129/SvEv, features a modification of the amino acid from Q to E at position 63.
+The protein's natural variant, known as in strain: 129/SvEv, features a modification of the amino acid from C to W at position 85.
+The protein's natural variant, known as in strain: 129/SvEv, features a modification of the amino acid from S to G at position 91.
+The protein's natural variant, known as in strain: 129/SvEv, features a modification of the amino acid from Q to R at position 102.
+The protein's natural variant, known as in strain: C57BL/6J, features a modification of the amino acid from R to T at position 143.
+The protein's natural variant, known as in strain: DBA/2J and DBA1/J, features a modification of the amino acid from N to S at position 541.
+The protein's natural variant, known as in strain: DBA/2J, DBA1/J, CE/J, A/HeJ, BALB/cJ, C57Br/cdJ, C57L/J, WSP2 and 129/J, features a modification of the amino acid from G to V at position 691.
+The protein's natural variant, known as in strain: DBA/2J, DBA1/J, CE/J, A/HeJ, BALB/cJ, C57Br/cdJ, C57L/J, WSP2 and 129/J, features a modification of the amino acid from H to R at position 801.
+The protein's natural variant, known as in strain: DBA/2J, DBA1/J, CE/J, A/HeJ, BALB/cJ, C57Br/cdJ, C57L/J, WSP2 and 129/J, features a modification of the amino acid from T to A at position 859.
+The protein's natural variant, known as in strain: DBA/2J, DBA1/J, CE/J, A/HeJ, BALB/cJ, C57Br/cdJ, C57L/J, WSP2 and 129/J, features a modification of the amino acid from S to N at position 880.
+The protein's natural variant, known as in strain: DBA/2J, DBA1/J, CE/J, A/HeJ, BALB/cJ, C57Br/cdJ, C57L/J, WSP2 and 129/J, features a modification of the amino acid from R to S at position 914.
+The protein's natural variant, known as in strain: DBA/2J, DBA1/J, CE/J, A/HeJ, BALB/cJ, C57Br/cdJ, C57L/J, WSP2 and 129/J, features a modification of the amino acid from A to V at position 977.
+The protein's natural variant, known as in strain: DBA/2J, DBA1/J, CE/J, A/HeJ, BALB/cJ, C57Br/cdJ, C57L/J, WSP2 and 129/J, features a modification of the amino acid from V to M at position 1338.
+The protein's natural variant, known as in strain: DBA/2J, DBA1/J, CE/J, A/HeJ, BALB/cJ, C57Br/cdJ, C57L/J, WSP2 and 129/J, features a modification of the amino acid from I to N at position 1433.
+The protein's natural variant, known as in strain: DBA/2J, DBA1/J, CE/J, A/HeJ, BALB/cJ, C57Br/cdJ, C57L/J, WSP2 and 129/J, features a modification of the amino acid from H to N at position 1767.
+The protein's natural variant, known as in allele NDOR1*1; shows a decrease in affinity for NADPH and a reduction in ferricyanide reductase activity;, features a modification of the amino acid from V to I at position 522.
+The protein's natural variant, known as in LCA1; unknown pathological significance;, features a modification of the amino acid from A to S at position 52.
+The protein's natural variant, known as in LCA1;, features a modification of the amino acid from T to M at position 55.
+The protein's natural variant, known as in LCA1, features a modification of the amino acid from E to V at position 103.
+The protein's natural variant, known as in LCA1; does not affect basal guanylate cyclase activity; reduces GUCA1A-induced guanylate cyclase activity;, features a modification of the amino acid from C to Y at position 105.
+The protein's natural variant, known as in LCA1;, features a modification of the amino acid from T to M at position 312.
+The protein's natural variant, known as in LCA1; does not affect basal guanylate cyclase activity; reduces GUCA1A-induced guanylate cyclase activity;, features a modification of the amino acid from L to P at position 325.
+The protein's natural variant, known as found in a patient with LCA1, features a modification of the amino acid from L to R at position 325.
+The protein's natural variant, known as in LCA1;, features a modification of the amino acid from A to S at position 362.
+The protein's natural variant, known as in LCA1, features a modification of the amino acid from LD to PN at position 406.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation;, features a modification of the amino acid from G to D at position 431.
+The protein's natural variant, known as in LCA1;, features a modification of the amino acid from R to C at position 438.
+The protein's natural variant, known as in LCA1; loss of activity;, features a modification of the amino acid from F to S at position 565.
+The protein's natural variant, known as in LCA1;, features a modification of the amino acid from I to V at position 573.
+The protein's natural variant, known as in LCA1, features a modification of the amino acid from W to L at position 640.
+The protein's natural variant, known as in LCA1;, features a modification of the amino acid from R to Q at position 660.
+The protein's natural variant, known as at homozygosity may be associated with Leber congenital amaurosis in some populations;, features a modification of the amino acid from P to S at position 701.
+The protein's natural variant, known as in LCA1; loss of basal and GUCA1A-induced guanylate cyclase activity; does not affect endoplasmic reticulum membrane localization;, features a modification of the amino acid from A to V at position 710.
+The protein's natural variant, known as in LCA1, features a modification of the amino acid from D to H at position 728.
+The protein's natural variant, known as in LCA1; requires 2 nucleotide substitutions, features a modification of the amino acid from I to A at position 734.
+The protein's natural variant, known as in LCA1 and CSNB1I;, features a modification of the amino acid from R to W at position 768.
+The protein's natural variant, known as in LCA1;, features a modification of the amino acid from M to R at position 784.
+The protein's natural variant, known as in LCA1;, features a modification of the amino acid from R to Q at position 795.
+The protein's natural variant, known as in CORD6, features a modification of the amino acid from ERT to DCM at position 839.
+The protein's natural variant, known as in CORD6;, features a modification of the amino acid from E to D at position 837.
+The protein's natural variant, known as in CORD6;, features a modification of the amino acid from R to C at position 838.
+The protein's natural variant, known as in CORD6, features a modification of the amino acid from R to G at position 838.
+The protein's natural variant, known as in CORD6;, features a modification of the amino acid from R to H at position 838.
+The protein's natural variant, known as in CORD6;, features a modification of the amino acid from R to P at position 838.
+The protein's natural variant, known as in CORD6; decreases basal and GUCA1A-induced guanylate cyclase activity; inhibition by RD3 is less effective; does not affect endoplasmic reticulum membrane localization;, features a modification of the amino acid from E to K at position 841.
+The protein's natural variant, known as in CORD6; decreases basal and GUCA1A-induced guanylate cyclase activity; inhibition by RD3 is less effective; does not affect endoplasmic reticulum membrane localization;, features a modification of the amino acid from K to N at position 846.
+The protein's natural variant, known as in CORD6, features a modification of the amino acid from T to A at position 849.
+The protein's natural variant, known as in LCA1; severely impairs basal and GUCA1A-induced guanylate cyclase activity;, features a modification of the amino acid from P to S at position 858.
+The protein's natural variant, known as in CORD6; loss basal and GUCA1A-induced guanylate cyclase activity; does not affect endoplasmic reticulum membrane localization;, features a modification of the amino acid from P to R at position 873.
+The protein's natural variant, known as in LCA1; increases basal and GUCA1A-induced guanylate cyclase activity; inhibition by RD3 is less effective; does not affect endoplasmic reticulum membrane localization;, features a modification of the amino acid from V to L at position 902.
+The protein's natural variant, known as in CACD1; unknown pathological significance;, features a modification of the amino acid from V to A at position 933.
+The protein's natural variant, known as in CORD6;, features a modification of the amino acid from I to T at position 949.
+The protein's natural variant, known as in LCA1; severely impairs basal and GUCA1A induced guanylate cyclase;, features a modification of the amino acid from L to P at position 954.
+The protein's natural variant, known as in LCA1, features a modification of the amino acid from S to L at position 1007.
+The protein's natural variant, known as in LCA1, features a modification of the amino acid from I to IGI at position 1027.
+The protein's natural variant, known as found in a renal cell carcinoma case; somatic mutation;, features a modification of the amino acid from I to V at position 341.
+The protein's natural variant, known as associated with increased risk of obesity; significantly decreases LCFA-induced intracellular calcium release.;, features a modification of the amino acid from R to H at position 254.
+The protein's natural variant, known as in strain: DH161; quinolone-resistant, features a modification of the amino acid from L to H at position 445.
+The protein's natural variant, known as in clone PXC204, features a modification of the amino acid from A to S at position 57.
+The protein's natural variant, known as in clone PXC204, features a modification of the amino acid from A to G at position 85.
+The protein's natural variant, known as in clone PXC204, features a modification of the amino acid from TP to SL at position 107.
+The protein's natural variant, known as in clone PXC204, features a modification of the amino acid from A to V at position 112.
+The protein's natural variant, known as in AKU;, features a modification of the amino acid from E to A at position 3.
+The protein's natural variant, known as in AKU;, features a modification of the amino acid from E to K at position 13.
+The protein's natural variant, known as in AKU, features a modification of the amino acid from D to N at position 18.
+The protein's natural variant, known as in AKU, features a modification of the amino acid from L to P at position 25.
+The protein's natural variant, known as in AKU, features a modification of the amino acid from Q to R at position 33.
+The protein's natural variant, known as in AKU;, features a modification of the amino acid from E to A at position 42.
+The protein's natural variant, known as in AKU;, features a modification of the amino acid from L to F at position 44.
+The protein's natural variant, known as in AKU;, features a modification of the amino acid from R to Q at position 53.
+The protein's natural variant, known as in AKU, features a modification of the amino acid from W to G at position 60.
+The protein's natural variant, known as in AKU;, features a modification of the amino acid from L to P at position 61.
+The protein's natural variant, known as in AKU;, features a modification of the amino acid from Y to C at position 62.
+The protein's natural variant, known as in AKU, features a modification of the amino acid from F to L at position 73.
+The protein's natural variant, known as in AKU, features a modification of the amino acid from P to T at position 92.
+The protein's natural variant, known as in AKU, features a modification of the amino acid from W to G at position 97.
+The protein's natural variant, known as in AKU, features a modification of the amino acid from W to R at position 97.
+The protein's natural variant, known as in AKU;, features a modification of the amino acid from G to R at position 115.
+The protein's natural variant, known as in AKU;, features a modification of the amino acid from L to P at position 116.
+The protein's natural variant, known as in AKU;, features a modification of the amino acid from C to F at position 120.
+The protein's natural variant, known as in AKU;, features a modification of the amino acid from C to W at position 120.
+The protein's natural variant, known as in AKU, features a modification of the amino acid from A to D at position 122.
+The protein's natural variant, known as in AKU;, features a modification of the amino acid from A to V at position 122.
+The protein's natural variant, known as in AKU;, features a modification of the amino acid from G to A at position 123.
+The protein's natural variant, known as in AKU;, features a modification of the amino acid from G to R at position 123.
+The protein's natural variant, known as in AKU, features a modification of the amino acid from L to P at position 137.
+The protein's natural variant, known as in AKU;, features a modification of the amino acid from G to A at position 152.
+The protein's natural variant, known as in AKU;, features a modification of the amino acid from D to G at position 153.
+The protein's natural variant, known as in AKU;, features a modification of the amino acid from P to L at position 158.
+The protein's natural variant, known as in AKU; loss of activity; most prevalent mutation in Slovak and Czech patients;, features a modification of the amino acid from G to R at position 161.
+The protein's natural variant, known as in AKU;, features a modification of the amino acid from E to D at position 168.
+The protein's natural variant, known as in AKU; loss of activity;, features a modification of the amino acid from E to K at position 168.
+The protein's natural variant, known as in AKU;, features a modification of the amino acid from F to L at position 169.
+The protein's natural variant, known as in AKU, features a modification of the amino acid from K to N at position 171.
+The natural variant of this protein is characterized by an amino acid alteration from M to T at position 172.
+The protein's natural variant, known as in AKU, features a modification of the amino acid from E to G at position 178.
+The protein's natural variant, known as in AKU;, features a modification of the amino acid from Q to R at position 183.
+The protein's natural variant, known as in AKU;, features a modification of the amino acid from R to G at position 187.
+The protein's natural variant, known as in AKU, features a modification of the amino acid from S to I at position 189.
+The protein's natural variant, known as in AKU;, features a modification of the amino acid from R to G at position 197.
+The protein's natural variant, known as in AKU;, features a modification of the amino acid from I to T at position 216.
+The protein's natural variant, known as in AKU, features a modification of the amino acid from G to W at position 217.
+The protein's natural variant, known as in AKU, features a modification of the amino acid from N to S at position 219.
+The protein's natural variant, known as in AKU;, features a modification of the amino acid from R to H at position 225.
+The protein's natural variant, known as in AKU, features a modification of the amino acid from R to L at position 225.
+The protein's natural variant, known as in AKU;, features a modification of the amino acid from R to P at position 225.
+The protein's natural variant, known as in AKU;, features a modification of the amino acid from F to S at position 227.
+The protein's natural variant, known as in AKU; complete loss of activity;, features a modification of the amino acid from P to S at position 230.
+The protein's natural variant, known as in AKU, features a modification of the amino acid from P to T at position 230.
+The protein's natural variant, known as in AKU, features a modification of the amino acid from V to F at position 245.
+The protein's natural variant, known as in AKU;, features a modification of the amino acid from Q to P at position 258.
+The protein's natural variant, known as in AKU;, features a modification of the amino acid from H to R at position 269.
+The protein's natural variant, known as in AKU;, features a modification of the amino acid from G to R at position 270.
+The protein's natural variant, known as in AKU;, features a modification of the amino acid from K to N at position 276.
+The protein's natural variant, known as in AKU;, features a modification of the amino acid from D to E at position 291.
+The protein's natural variant, known as in AKU;, features a modification of the amino acid from V to G at position 300.
+The protein's natural variant, known as in AKU, features a modification of the amino acid from R to P at position 321.
+The protein's natural variant, known as in AKU, features a modification of the amino acid from F to C at position 329.
+The protein's natural variant, known as in AKU;, features a modification of the amino acid from R to S at position 330.
+The protein's natural variant, known as in AKU, features a modification of the amino acid from N to D at position 337.
+The protein's natural variant, known as in AKU;, features a modification of the amino acid from P to L at position 359.
+The protein's natural variant, known as in AKU, features a modification of the amino acid from G to A at position 360.
+The protein's natural variant, known as in AKU;, features a modification of the amino acid from G to R at position 360.
+The protein's natural variant, known as in AKU;, features a modification of the amino acid from G to R at position 361.
+The protein's natural variant, known as in AKU, features a modification of the amino acid from G to E at position 362.
+The protein's natural variant, known as in AKU; loss of activity;, features a modification of the amino acid from M to V at position 368.
+The protein's natural variant, known as in AKU;, features a modification of the amino acid from T to N at position 369.
+The protein's natural variant, known as in AKU;, features a modification of the amino acid from H to R at position 371.
+The protein's natural variant, known as in AKU;, features a modification of the amino acid from P to L at position 373.
+The protein's natural variant, known as in AKU;, features a modification of the amino acid from D to H at position 374.
+The protein's natural variant, known as in AKU;, features a modification of the amino acid from E to Q at position 401.
+The protein's natural variant, known as found in a patient with severe intellectual disability, psychomotor delay, no speech, sleep disturbances, feeding problems, abnormal breething, deep-set eyes and short philtrum;, features a modification of the amino acid from R to H at position 174.
+The protein's natural variant, known as in LVNC7;, features a modification of the amino acid from V to F at position 943.
+The protein's natural variant, known as in BARMACS, features a modification of the amino acid from F to V at position 551.
+The protein's natural variant, known as in a breast infiltrating ductal carcinoma sample; somatic mutation;, features a modification of the amino acid from A to T at position 443.
+The protein's natural variant, known as in strain: M4243 and YSH6000T, features a modification of the amino acid from K to E at position 354.
+The protein's natural variant, known as in strain: M4243 and YSH6000T, features a modification of the amino acid from T to P at position 385.
+The protein's natural variant, known as in LiP;, features a modification of the amino acid from F to I at position 167.
+The protein's natural variant, known as in DEE89;, features a modification of the amino acid from E to K at position 509.
+The protein's natural variant, known as in BDPLT13; does not affect TXA2 binding; defective interaction with G proteins; impairs phospholipase C and adenylyl cyclase activation; isoform 1; has no effect on adenylyl cyclase inhibition; isoform 2;, features a modification of the amino acid from R to L at position 60.
+The protein's natural variant, known as in Okinawa habu, features a modification of the amino acid from PEQQ to EQRF at position 192.
+The protein's natural variant, known as in Okinawa habu, features a modification of the amino acid from D to N at position 271.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from S to F at position 220.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from A to T at position 599.
+The protein's natural variant, known as in strain: Zimbabwe30, features a modification of the amino acid from E to K at position 242.
+The natural variant of this protein is characterized by an amino acid alteration from S to R at position 44.
+The natural variant of this protein is characterized by an amino acid alteration from T to A at position 55.
+The natural variant of this protein is characterized by an amino acid alteration from D to G at position 28.
+The protein's natural variant, known as in COXPD13; the mutation alters multimerization of the protein;, features a modification of the amino acid from Q to R at position 387.
+The protein's natural variant, known as in DFNB70; results in a hypofunctional protein leading to disturbed enzyme trimerization and impaired mitochondrial RNA import;, features a modification of the amino acid from E to G at position 475.
+The protein's natural variant, known as after 20 antibiotic passages; confers resistance to various antibiotics, features a modification of the amino acid from G to GG at position 60.
+The protein's natural variant, known as also to GGGG, after 47 antibiotic passages; confers greater resistance than the above variant, features a modification of the amino acid from G to GGG at position 60.
+The protein's natural variant, known as after 32, 37 and 48 antibiotic passages; confers resistance to various antibiotics in combination with a 23S rRNA mutation and up to 3 mutations in protein L22, features a modification of the amino acid from H to L at position 70.
+The protein's natural variant, known as after 30 clindamycin passages; confers resistance to clindamycin and josamycin, features a modification of the amino acid from H to R at position 70.
+The protein's natural variant, known as in IKSHD; loss of fatty acid elongase activity, features a modification of the amino acid from S to F at position 165.
+The protein's natural variant, known as in strain: Isolate TK 11240, features a modification of the amino acid from I to V at position 234.
+The protein's natural variant, known as in strain: Isolate TK 11240, features a modification of the amino acid from P to Q at position 322.
+The protein's natural variant, known as may be associated with susceptibility to IDD;, features a modification of the amino acid from Q to R at position 279.
+The natural variant of this protein is characterized by an amino acid alteration from A to K at position 29.
+The protein's natural variant, known as in VERBRAS; unknown pathological significance, features a modification of the amino acid from S to N at position 736.
+The protein's natural variant, known as in a glioblastoma multiforme sample; somatic mutation, features a modification of the amino acid from G to S at position 67.
+The protein's natural variant, known as in HMN2A; no effect on cytoskeleton architecture; no effect on cytoplasmic location; no effect on interaction with BAG3;, features a modification of the amino acid from P to L at position 90.
+The protein's natural variant, known as in HMN2A; no effect on cytoskeleton architecture; no effect on cytoplasmic location; no effect on interaction with BAG3;, features a modification of the amino acid from N to T at position 138.
+The protein's natural variant, known as in HMN2A; strengthen interaction with HSPB1;, features a modification of the amino acid from K to E at position 141.
+The protein's natural variant, known as in HMN2A; no effect on cytoskeleton architecture; no effect on cytoplasmic location; increased interaction with BAG3;, features a modification of the amino acid from K to M at position 141.
+The protein's natural variant, known as in HMN2A; strengthen interaction with HSPB1; no effect on cytoskeleton architecture; no effect on cytoplasmic location; increased interaction with BAG3;, features a modification of the amino acid from K to N at position 141.
+The natural variant of this protein is characterized by an amino acid alteration from D to R at position 127.
+The natural variant of this protein is characterized by an amino acid alteration from R to T at position 131.
+The natural variant of this protein is characterized by an amino acid alteration from T to A at position 138.
+The natural variant of this protein is characterized by an amino acid alteration from I to F at position 358.
+The natural variant of this protein is characterized by an amino acid alteration from Q to L at position 430.
+The natural variant of this protein is characterized by an amino acid alteration from P to F at position 569.
+The protein's natural variant, known as in strain: AB1, AB2, CB4852, CB4853, CB4854, CB4855, CB4857, CB4858, KR314 and PB306, features a modification of the amino acid from C to F at position 66.
+The protein's natural variant, known as in strain: CB4855, features a modification of the amino acid from F to Y at position 112.
+The protein's natural variant, known as in strain: AB1, AB2, CB4852, CB4853, CB4854, CB4855, CB4857, CB4858, KR314 and PB306, features a modification of the amino acid from G to S at position 194.
+The protein's natural variant, known as in an ovarian mucinous carcinoma sample; somatic mutation;, features a modification of the amino acid from V to M at position 290.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation, features a modification of the amino acid from S to C at position 784.
+The protein's natural variant, known as in XP-D;, features a modification of the amino acid from G to R at position 47.
+The protein's natural variant, known as in XP-D, features a modification of the amino acid from T to A at position 76.
+The protein's natural variant, known as in TTD1 and XP-D;, features a modification of the amino acid from R to H at position 112.
+The protein's natural variant, known as in XP-D;, features a modification of the amino acid from D to N at position 234.
+The protein's natural variant, known as in TTD1;, features a modification of the amino acid from C to Y at position 259.
+The protein's natural variant, known as in XP-D and TTD1;, features a modification of the amino acid from L to V at position 461.
+The protein's natural variant, known as in XP-D; the corresponding mutation in fission yeast causes complete loss of activity;, features a modification of the amino acid from L to P at position 485.
+The protein's natural variant, known as in TTD1, features a modification of the amino acid from R to G at position 487.
+The protein's natural variant, known as in XP-D;, features a modification of the amino acid from R to Q at position 511.
+The protein's natural variant, known as in XP-D; mild;, features a modification of the amino acid from S to R at position 541.
+The protein's natural variant, known as in XP-D, features a modification of the amino acid from Y to C at position 542.
+The protein's natural variant, known as in XP-D, features a modification of the amino acid from EK to VSE at position 583.
+The protein's natural variant, known as in TTD1, features a modification of the amino acid from R to P at position 592.
+The protein's natural variant, known as in TTD1, features a modification of the amino acid from A to P at position 594.
+The protein's natural variant, known as in XP-D;, features a modification of the amino acid from R to L at position 601.
+The protein's natural variant, known as in XP-D;, features a modification of the amino acid from R to W at position 601.
+The protein's natural variant, known as in XP-D; combined with features of Cockayne syndrome;, features a modification of the amino acid from G to D at position 602.
+The natural variant of this protein is characterized by an amino acid alteration from R to C at position 616.
+The protein's natural variant, known as in XP-D and TTD1;, features a modification of the amino acid from R to P at position 616.
+The protein's natural variant, known as in XP-D and COFS2;, features a modification of the amino acid from R to W at position 616.
+The protein's natural variant, known as in TTD1;, features a modification of the amino acid from R to C at position 658.
+The protein's natural variant, known as in TTD1, features a modification of the amino acid from R to G at position 658.
+The protein's natural variant, known as in TTD1;, features a modification of the amino acid from R to H at position 658.
+The protein's natural variant, known as in TTD1;, features a modification of the amino acid from C to R at position 663.
+The protein's natural variant, known as in XP-D;, features a modification of the amino acid from R to W at position 666.
+The protein's natural variant, known as in TTD1, features a modification of the amino acid from D to G at position 673.
+The protein's natural variant, known as in XP-D/CS; severe form, features a modification of the amino acid from G to R at position 675.
+The protein's natural variant, known as in XP-D and COFS2;, features a modification of the amino acid from D to N at position 681.
+The protein's natural variant, known as in XP-D;, features a modification of the amino acid from R to Q at position 683.
+The protein's natural variant, known as in XP-D; vitamin D-mediated activation of CYP24A1 is impaired in patient fibroblasts due to altered TFIIH-dependent phosphorylation of ETS1, subsequent impaired cooperation of ETS1 with VDR and altered VDR recruitment to CYP24A1 promoter;, features a modification of the amino acid from R to W at position 683.
+The protein's natural variant, known as in TTD1;, features a modification of the amino acid from G to R at position 713.
+The protein's natural variant, known as in TTD1;, features a modification of the amino acid from R to W at position 722.
+The protein's natural variant, known as in TTD1;, features a modification of the amino acid from A to P at position 725.
+The protein's natural variant, known as may be associated with increased susceptibility to DNA damage;, features a modification of the amino acid from K to Q at position 751.
+The protein's natural variant, known as in strain: KS3/2, features a modification of the amino acid from K to E at position 3.
+The protein's natural variant, known as in strain: NCTC 11638, features a modification of the amino acid from S to N at position 22.
+The protein's natural variant, known as in strain: NCTC 11638, features a modification of the amino acid from A to T at position 27.
+The protein's natural variant, known as in strain: NCTC 11638, features a modification of the amino acid from G to E at position 50.
+The protein's natural variant, known as in strain: NCTC 11638, features a modification of the amino acid from A to T at position 61.
+The protein's natural variant, known as in strain: NCTC 11638, features a modification of the amino acid from P to S at position 65.
+The protein's natural variant, known as in strain: NCTC 11638, features a modification of the amino acid from P to S at position 78.
+The protein's natural variant, known as in strain: NCTC 11638, features a modification of the amino acid from QKD to EEN at position 92.
+The protein's natural variant, known as in strain: NCTC 11638, features a modification of the amino acid from P to L at position 99.
+The protein's natural variant, known as in strain: NCTC 11638, features a modification of the amino acid from N to S at position 107.
+The protein's natural variant, known as in strain: NCTC 11638, features a modification of the amino acid from K to Q at position 109.
+The protein's natural variant, known as in strain: NCTC 11638, features a modification of the amino acid from T to A at position 144.
+The protein's natural variant, known as in strain: NCTC 11638, features a modification of the amino acid from DI to NL at position 191.
+The protein's natural variant, known as in strain: NCTC 11638, features a modification of the amino acid from I to V at position 251.
+The protein's natural variant, known as in strain: NCTC 11638, features a modification of the amino acid from Q to K at position 317.
+The protein's natural variant, known as may be associated with brown coat color phenotype, features a modification of the amino acid from A to G at position 3.
+The natural variant of this protein is characterized by an amino acid alteration from S to Y at position 19.
+The natural variant of this protein is characterized by an amino acid alteration from R to S at position 28.
+The natural variant of this protein is characterized by an amino acid alteration from A to V at position 31.
+The natural variant of this protein is characterized by an amino acid alteration from D to A at position 44.
+The protein's natural variant, known as in SCAR32; unknown pathological significance;, features a modification of the amino acid from A to G at position 142.
+The protein's natural variant, known as in PPPCD, features a modification of the amino acid from D to H at position 190.
+The protein's natural variant, known as in SCAR32; unstable protein leading to its degradation, reduced glutathione peroxidase activity and reduced PRDX5 protein levels in patient fibroblasts;, features a modification of the amino acid from D to N at position 202.
+The protein's natural variant, known as in allele CYP1A1*6;, features a modification of the amino acid from M to I at position 331.
+The protein's natural variant, known as in allele CYP1A1*8;, features a modification of the amino acid from I to N at position 448.
+The protein's natural variant, known as in allele CYP1A1*4; displays similar catalytic efficiency toward estrogens when compared to the wild-type enzyme.;, features a modification of the amino acid from T to N at position 461.
+The protein's natural variant, known as in allele CYP1A1*2B and allele CYP1A1*2C; displays 5.7- and 12-fold increase in catalytic efficiency in the formation of 2-hydroxylated estrogens, 17beta-estradiol and estrone respectively.;, features a modification of the amino acid from I to V at position 462.
+The protein's natural variant, known as in allele CYP1A1*9;, features a modification of the amino acid from R to C at position 464.
+The protein's natural variant, known as in allele CYP1A1*5;, features a modification of the amino acid from R to S at position 464.
+The protein's natural variant, known as in allele CYP1A1*10;, features a modification of the amino acid from R to W at position 477.
+The protein's natural variant, known as in allele CYP1A1*11;, features a modification of the amino acid from P to R at position 492.
+The natural variant of this protein is characterized by an amino acid alteration from L to V at position 89.
+The protein's natural variant, known as in MC3DN6;, features a modification of the amino acid from W to C at position 96.
+The protein's natural variant, known as in MC3DN6;, features a modification of the amino acid from L to F at position 215.
+The natural variant of this protein is characterized by an amino acid alteration from S to T at position 54.
+The protein's natural variant, known as may possibly contribute to susceptibility to systemic lupus erythematosus; increases autophosphorylation and interaction with PI3-kinase subunit p85;, features a modification of the amino acid from E to K at position 763.
+The protein's natural variant, known as in SEDT; loss-of-function mutation, features a modification of the amino acid from D to Y at position 47.
+The protein's natural variant, known as in SEDT; loss of interaction with ENO1, PITX1 and SF1;, features a modification of the amino acid from S to L at position 73.
+The protein's natural variant, known as in SEDT; mild form; loss of interaction with ENO1, PITX1 and SF1;, features a modification of the amino acid from F to S at position 83.
+The protein's natural variant, known as in SEDT; loss of interaction with ENO1, PITX1 and SF1, features a modification of the amino acid from V to D at position 130.
+The protein's natural variant, known as in T(-)B(+)NK(-) SCID;, features a modification of the amino acid from Y to C at position 100.
+The protein's natural variant, known as in T(-)B(+)NK(-) SCID; likely benign variant;, features a modification of the amino acid from P to R at position 151.
+The protein's natural variant, known as in T(-)B(+)NK(-) SCID;, features a modification of the amino acid from D to E at position 169.
+The protein's natural variant, known as in T(-)B(+)NK(-) SCID, features a modification of the amino acid from E to G at position 481.
+The protein's natural variant, known as in a gastric adenocarcinoma sample; somatic mutation, features a modification of the amino acid from L to P at position 527.
+The protein's natural variant, known as in T(-)B(+)NK(-) SCID;, features a modification of the amino acid from R to W at position 582.
+The protein's natural variant, known as in T(-)B(+)NK(-) SCID;, features a modification of the amino acid from G to S at position 589.
+The protein's natural variant, known as in T(-)B(+)NK(-) SCID; constitutive phosphorylation, features a modification of the amino acid from C to R at position 759.
+The protein's natural variant, known as in T(-)B(+)NK(-) SCID, features a modification of the amino acid from L to S at position 910.
+The protein's natural variant, known as in MPD7; unknown pathological significance, features a modification of the amino acid from P to T at position 7.
+The protein's natural variant, known as in MPD7; unknown pathological significance, features a modification of the amino acid from A to V at position 13.
+The protein's natural variant, known as in MPD7; unknown pathological significance, features a modification of the amino acid from P to A at position 27.
+The protein's natural variant, known as in MPD7; unknown pathological significance, features a modification of the amino acid from S to N at position 78.
+The protein's natural variant, known as in AGU; uncertain pathological significance;, features a modification of the amino acid from V to L at position 12.
+The protein's natural variant, known as in AGU;, features a modification of the amino acid from G to D at position 60.
+The protein's natural variant, known as in AGU; specifically prevents the proteolytic activation cleavage of AGA in the endoplasmic reticulum;, features a modification of the amino acid from S to P at position 72.
+The protein's natural variant, known as in AGU;, features a modification of the amino acid from G to E at position 100.
+The protein's natural variant, known as in AGU;, features a modification of the amino acid from A to V at position 101.
+The protein's natural variant, known as in AGU;, features a modification of the amino acid from F to S at position 135.
+The protein's natural variant, known as in AGU;, features a modification of the amino acid from R to Q at position 161.
+The protein's natural variant, known as in AGU; most frequent mutation; abolishes autocatalytic cleavage and enzyme activity;, features a modification of the amino acid from C to S at position 163.
+The protein's natural variant, known as in AGU;, features a modification of the amino acid from G to E at position 252.
+The protein's natural variant, known as in AGU;, features a modification of the amino acid from G to R at position 252.
+The protein's natural variant, known as in AGU;, features a modification of the amino acid from T to I at position 257.
+The protein's natural variant, known as in AGU;, features a modification of the amino acid from G to R at position 302.
+The protein's natural variant, known as in AGU;, features a modification of the amino acid from C to R at position 306.
+The protein's natural variant, known as in GIDID1; reduced interaction with PI4KA;, features a modification of the amino acid from E to K at position 71.
+The protein's natural variant, known as in GIDID1, features a modification of the amino acid from L to P at position 346.
+The protein's natural variant, known as in GIDID1, features a modification of the amino acid from L to P at position 399.
+The protein's natural variant, known as in GIDID1;, features a modification of the amino acid from S to L at position 539.
+The protein's natural variant, known as in GIDID1, features a modification of the amino acid from A to D at position 551.
+The protein's natural variant, known as in GIDID1;, features a modification of the amino acid from K to R at position 606.
+The protein's natural variant, known as in GIDID1;, features a modification of the amino acid from S to P at position 672.
+The protein's natural variant, known as in GIDID1;, features a modification of the amino acid from L to P at position 823.
+The protein's natural variant, known as in GIDID1; reduced interaction with PI4KA;, features a modification of the amino acid from A to T at position 832.
+The protein's natural variant, known as in breast cancer; seems to form misfolded oligomers that are retained within the Golgi complex and are not targeted to caveolae or the plasma membrane; loss of interaction with VCP;, features a modification of the amino acid from P to L at position 132.
+The protein's natural variant, known as in LCCS11; abolishes cell surface localization; abolishes interaction with NFASC;, features a modification of the amino acid from A to E at position 32.
+The protein's natural variant, known as in LCCS11; abolishes cell surface localization; abolishes interaction with NFASC;, features a modification of the amino acid from A to P at position 475.
+The protein's natural variant, known as in EPM2; does not significantly alters the subcellular location as compared to the wild-type, features a modification of the amino acid from S to R at position 22.
+The protein's natural variant, known as in EPM2;, features a modification of the amino acid from C to S at position 26.
+The protein's natural variant, known as in EPM2;, features a modification of the amino acid from F to S at position 33.
+The protein's natural variant, known as in EPM2; loss of interaction with EPM2A; increased levels of PPP1R3C and glycogen;, features a modification of the amino acid from C to Y at position 46.
+The protein's natural variant, known as in EPM2;, features a modification of the amino acid from E to Q at position 67.
+The protein's natural variant, known as in EPM2, features a modification of the amino acid from C to Y at position 68.
+The protein's natural variant, known as in EPM2; severely reduced interaction with EPM2A; increased levels of PPP1R3C and glycogen;, features a modification of the amino acid from P to A at position 69.
+The protein's natural variant, known as in EPM2, features a modification of the amino acid from L to P at position 87.
+The protein's natural variant, known as in EPM2; the mutant protein targeted exclusively nucleus as compared to predominantly cytoplasmic and partially nuclear localization of the wild-type protein;, features a modification of the amino acid from L to P at position 126.
+The protein's natural variant, known as in EPM2; severely reduced interaction with EPM2A; increased levels of PPP1R3C and glycogen;, features a modification of the amino acid from D to N at position 146.
+The protein's natural variant, known as in EPM2, features a modification of the amino acid from I to M at position 153.
+The protein's natural variant, known as in EPM2;, features a modification of the amino acid from C to R at position 160.
+The protein's natural variant, known as in EPM2;, features a modification of the amino acid from I to N at position 198.
+The protein's natural variant, known as in EPM2, features a modification of the amino acid from W to R at position 219.
+The protein's natural variant, known as in EPM2, features a modification of the amino acid from D to A at position 233.
+The protein's natural variant, known as in EPM2, features a modification of the amino acid from D to N at position 245.
+The protein's natural variant, known as in EPM2, features a modification of the amino acid from R to K at position 253.
+The protein's natural variant, known as in EPM2; loss of interaction with EPM2A; increased levels of PPP1R3C and glycogen;, features a modification of the amino acid from L to P at position 261.
+The protein's natural variant, known as in EPM2, features a modification of the amino acid from P to H at position 264.
+The protein's natural variant, known as in EPM2; significantly alters the distribution of the protein; a great majority of cells expressing the mutant form formed perinuclear inclusion when compared with the wild-type form, features a modification of the amino acid from L to P at position 279.
+The protein's natural variant, known as in EPM2; loss of interaction with EPM2A;, features a modification of the amino acid from Q to P at position 302.
+The protein's natural variant, known as in EPM2;, features a modification of the amino acid from D to A at position 308.
+The protein's natural variant, known as in allele D, features a modification of the amino acid from I to S at position 12.
+The protein's natural variant, known as in allele B and allele D, features a modification of the amino acid from K to R at position 32.
+The protein's natural variant, known as in allele B, features a modification of the amino acid from K to A at position 35.
+The protein's natural variant, known as in allele C, features a modification of the amino acid from G to C at position 39.
+The protein's natural variant, known as in allele E, features a modification of the amino acid from P to S at position 43.
+The protein's natural variant, known as in allele C, features a modification of the amino acid from E to D at position 68.
+The protein's natural variant, known as in allele E, features a modification of the amino acid from N to K at position 85.
+The protein's natural variant, known as in allele C, features a modification of the amino acid from N to M at position 85.
+The protein's natural variant, known as in allele C, features a modification of the amino acid from N to K at position 93.
+The protein's natural variant, known as in allele C, allele D and allele E, features a modification of the amino acid from C to G at position 96.
+The protein's natural variant, known as found in a patient with pulmonary arterial hypertension; unknown pathological significance, features a modification of the amino acid from L to H at position 42.
+The natural variant of this protein is characterized by an amino acid alteration from L to M at position 85.
+The protein's natural variant, known as found in a patient with pulmonary arterial hypertension; unknown pathological significance, features a modification of the amino acid from T to P at position 114.
+The protein's natural variant, known as found in a patient with pulmonary arterial hypertension; unknown pathological significance, features a modification of the amino acid from P to R at position 170.
+The protein's natural variant, known as found in a patient with pulmonary arterial hypertension; unknown pathological significance, features a modification of the amino acid from R to P at position 184.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from G to S at position 300.
+The natural variant of this protein is characterized by an amino acid alteration from T to S at position 51.
+The protein's natural variant, known as in AROD; strongly reduced aromatase activity; 81% reduction of androstenedione metabolism compared to wild-type;, features a modification of the amino acid from R to H at position 192.
+The protein's natural variant, known as 1.6 fold decrease in affinity for androstenedione substrate; slightly affects PKA-mediated reduction in catalytic activity as measured in vitro by estrone synthesis from androstenedione (49% decrease compared with 36% for the wild-type protein); no effect on PKG/PRKG1-mediated reduction in catalytic activity in vitro;, features a modification of the amino acid from R to C at position 264.
+The protein's natural variant, known as 2.5 fold decrease in affinity for androstenedione substrate; slightly affects PKA-mediated reduction in catalytic activity as measured by estrone synthesis from androstenedione in vitro (28% decrease compared with 36% for the wild-type protein) and PKG/PRKG1-mediated reduction in catalytic activity in vitro (15% decrease compared with 30% for the wild-type protein);, features a modification of the amino acid from R to H at position 264.
+The protein's natural variant, known as found in deaf patients; unknown pathological significance, features a modification of the amino acid from S to P at position 314.
+The protein's natural variant, known as in AROD; 0.4% of wild-type activity;, features a modification of the amino acid from R to Q at position 365.
+The protein's natural variant, known as in AROD;, features a modification of the amino acid from R to C at position 375.
+The protein's natural variant, known as in AROD; 1.1% of wild-type activity;, features a modification of the amino acid from R to C at position 435.
+The protein's natural variant, known as in AROD; complete loss of activity;, features a modification of the amino acid from C to Y at position 437.
+The natural variant of this protein is characterized by an amino acid alteration from N to V at position 30.
+The protein's natural variant, known as in RP32; reduces ion channel activity; no impact on interaction with CALR; no impact on ER localization;, features a modification of the amino acid from D to E at position 25.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from V to M at position 126.
+The protein's natural variant, known as in PAMDDFS; unknown pathological significance;, features a modification of the amino acid from R to C at position 297.
+The protein's natural variant, known as in PAMDDFS; unknown pathological significance;, features a modification of the amino acid from R to C at position 333.
+The protein's natural variant, known as in PAMDDFS; unknown pathological significance;, features a modification of the amino acid from A to P at position 615.
+The protein's natural variant, known as in SPGF54; reduces the protein stability. Increases the kinetics of actin polymerisation;, features a modification of the amino acid from F to I at position 35.
+The protein's natural variant, known as in Lille-1;, features a modification of the amino acid from D to N at position 26.
+The protein's natural variant, known as in Rouen-1;, features a modification of the amino acid from G to V at position 31.
+The protein's natural variant, known as in DYSFIBRIN; fibrinogen Metz 1/Hershey III;, features a modification of the amino acid from R to C at position 35.
+The protein's natural variant, known as in Kyoto-2;, features a modification of the amino acid from P to L at position 37.
+The protein's natural variant, known as in Aarhus-1;, features a modification of the amino acid from R to G at position 38.
+The protein's natural variant, known as in Munich-1; requires 2 nucleotide substitutions, features a modification of the amino acid from R to N at position 38.
+The protein's natural variant, known as in Detroit-1;, features a modification of the amino acid from R to S at position 38.
+The protein's natural variant, known as in Canterbury;, features a modification of the amino acid from V to D at position 39.
+The protein's natural variant, known as in CAFBN; hypofibrinogenemia; heterozygous; decreased fibrinogen complex assembly; no effect on fibrinogen complex secretion, features a modification of the amino acid from C to R at position 55.
+The natural variant of this protein is characterized by an amino acid alteration from S to T at position 66.
+The protein's natural variant, known as in CAFBN; hypofibrinogenemia; heterozygous; no effect on fibrinogen complex assembly; no effect on fibrinogen complex secretion, features a modification of the amino acid from R to P at position 129.
+The protein's natural variant, known as in Lima, features a modification of the amino acid from R to S at position 160.
+The protein's natural variant, known as in CAFBN; hypofibrinogenemia; heterozygous; impaired fibrinogen complex assembly, features a modification of the amino acid from C to W at position 184.
+The protein's natural variant, known as in Caracas-2;, features a modification of the amino acid from S to N at position 453.
+The protein's natural variant, known as in AMYL8;, features a modification of the amino acid from E to V at position 545.
+The protein's natural variant, known as in DYSFIBRIN; fibrinogen Dusart/Paris-5;, features a modification of the amino acid from R to C at position 573.
+The protein's natural variant, known as in AMYL8;, features a modification of the amino acid from R to L at position 573.
+The protein's natural variant, known as in allele E, features a modification of the amino acid from Q to R at position 3.
+The protein's natural variant, known as in allele C, allele D, allele E, allele F and allele G, features a modification of the amino acid from L to I at position 5.
+The protein's natural variant, known as in allele C, allele D and allele G, features a modification of the amino acid from D to E at position 8.
+The protein's natural variant, known as in allele E and allele F, features a modification of the amino acid from G to R at position 12.
+The protein's natural variant, known as in allele E, features a modification of the amino acid from L to I at position 27.
+The protein's natural variant, known as in allele F, features a modification of the amino acid from A to T at position 35.
+The protein's natural variant, known as in allele B, features a modification of the amino acid from A to S at position 42.
+The protein's natural variant, known as in allele D, allele E, allele F and allele G, features a modification of the amino acid from H to Y at position 69.
+The protein's natural variant, known as in allele E, features a modification of the amino acid from V to I at position 75.
+The protein's natural variant, known as in allele G, features a modification of the amino acid from R to H at position 103.
+The protein's natural variant, known as in allele G, features a modification of the amino acid from A to T at position 104.
+The protein's natural variant, known as in allele D, features a modification of the amino acid from N to D at position 118.
+The protein's natural variant, known as in allele D, allele E and allele G, features a modification of the amino acid from D to E at position 124.
+The protein's natural variant, known as in allele E, features a modification of the amino acid from S to Y at position 128.
+The protein's natural variant, known as in allele C, features a modification of the amino acid from G to S at position 166.
+The protein's natural variant, known as in allele F, features a modification of the amino acid from E to K at position 172.
+The protein's natural variant, known as in allele C, allele D, allele E, allele F and allele G, features a modification of the amino acid from S to P at position 187.
+The protein's natural variant, known as in allele C, allele F and allele G, features a modification of the amino acid from H to P at position 189.
+The protein's natural variant, known as in allele C, allele D, allele E, allele F and allele G, features a modification of the amino acid from Q to R at position 249.
+The protein's natural variant, known as in allele G, features a modification of the amino acid from K to R at position 252.
+The protein's natural variant, known as in allele E, features a modification of the amino acid from R to Q at position 259.
+The protein's natural variant, known as in allele G, features a modification of the amino acid from N to D at position 269.
+The protein's natural variant, known as in allele G, features a modification of the amino acid from V to I at position 306.
+The protein's natural variant, known as in allele G, features a modification of the amino acid from L to F at position 330.
+The protein's natural variant, known as in allele C, allele D, allele E and allele F, features a modification of the amino acid from A to V at position 331.
+The protein's natural variant, known as in allele G, features a modification of the amino acid from A to V at position 338.
+The protein's natural variant, known as in allele F, features a modification of the amino acid from G to R at position 339.
+The protein's natural variant, known as in allele G, features a modification of the amino acid from NWYQSKVSQQNP to KWYQLEASQQNS at position 355.
+The protein's natural variant, known as in allele E, features a modification of the amino acid from G to A at position 358.
+The protein's natural variant, known as in allele G, features a modification of the amino acid from QGQR to RAQT at position 370.
+The protein's natural variant, known as in allele C, allele D, allele E, allele F and allele G, features a modification of the amino acid from K to R at position 402.
+The protein's natural variant, known as in allele C and allele G, features a modification of the amino acid from H to R at position 406.
+The protein's natural variant, known as in CsEv1C and CsEv1E, features a modification of the amino acid from I to M at position 6.
+The protein's natural variant, known as in CsEv1D, features a modification of the amino acid from ACFALV to VCLFLI at position 14.
+The protein's natural variant, known as in CsEv1D, features a modification of the amino acid from K to N at position 26.
+The protein's natural variant, known as in CsEv1D, features a modification of the amino acid from D to T at position 29.
+The protein's natural variant, known as in CsEv1E, features a modification of the amino acid from K to E at position 40.
+The protein's natural variant, known as in CsEv1E, features a modification of the amino acid from H to G at position 43.
+The protein's natural variant, known as in CsEv1E, features a modification of the amino acid from T to K at position 46.
+The protein's natural variant, known as in CsEv1C and CsEv1D, features a modification of the amino acid from T to L at position 46.
+The protein's natural variant, known as in MSUD1B;, features a modification of the amino acid from R to H at position 170.
+The protein's natural variant, known as in MSUD1B;, features a modification of the amino acid from R to P at position 183.
+The protein's natural variant, known as in MSUD1B, features a modification of the amino acid from H to R at position 206.
+The protein's natural variant, known as in MSUD1B;, features a modification of the amino acid from G to S at position 278.
+The protein's natural variant, known as in MSUD1B, features a modification of the amino acid from Q to R at position 346.
+The protein's natural variant, known as in strain: Kenya-HLa3, Kenya-HLa6, Kakamega-b1 and Makindu-b1, features a modification of the amino acid from K to T at position 119.
+The protein's natural variant, known as in strain: Ann Arbor1, DPCNBW, Kakamega-b1, Kakamega-b3, Kakamega-b4, Kenya-HLa3, Kenya-HLa6, Makindu-b5 and Reids2, features a modification of the amino acid from G to S at position 749.
+The protein's natural variant, known as in IDDSSAD; unknown pathological significance;, features a modification of the amino acid from D to G at position 77.
+The protein's natural variant, known as in DEE76; unknown pathological significance;, features a modification of the amino acid from R to Q at position 130.
+The protein's natural variant, known as in DEE76;, features a modification of the amino acid from L to P at position 206.
+The protein's natural variant, known as in IDDSSAD; probable gain-of-function mutation;, features a modification of the amino acid from G to R at position 343.
+The protein's natural variant, known as in DEE76;, features a modification of the amino acid from G to S at position 349.
+The protein's natural variant, known as in EPP1;, features a modification of the amino acid from G to C at position 55.
+The protein's natural variant, known as in EPP1;, features a modification of the amino acid from P to R at position 62.
+The protein's natural variant, known as in EPP1; enzyme totally inactive, features a modification of the amino acid from I to K at position 71.
+The protein's natural variant, known as in EPP1; enzyme retains 18% of activity;, features a modification of the amino acid from Q to L at position 139.
+The protein's natural variant, known as in EPP1; enzyme totally inactive, features a modification of the amino acid from S to P at position 151.
+The protein's natural variant, known as in EPP1;, features a modification of the amino acid from E to K at position 178.
+The protein's natural variant, known as in EPP1; enzyme totally inactive, features a modification of the amino acid from L to R at position 182.
+The protein's natural variant, known as in EPP1;, features a modification of the amino acid from I to T at position 186.
+The protein's natural variant, known as in EPP1; enzyme retains 72% of activity;, features a modification of the amino acid from Y to H at position 191.
+The protein's natural variant, known as in EPP1; enzyme totally inactive, features a modification of the amino acid from P to T at position 192.
+The protein's natural variant, known as in EPP1; enzyme retains 12% of activity;, features a modification of the amino acid from C to Y at position 236.
+The protein's natural variant, known as in EPP1; enzyme retains 52% of activity, features a modification of the amino acid from F to L at position 260.
+The protein's natural variant, known as in EPP1, features a modification of the amino acid from S to L at position 264.
+The protein's natural variant, known as in EPP1; unchanged activity; but increased thermolability;, features a modification of the amino acid from M to I at position 267.
+The protein's natural variant, known as in EPP1; enzyme almost inactive, features a modification of the amino acid from T to I at position 283.
+The protein's natural variant, known as in EPP1; enzyme totally inactive, features a modification of the amino acid from M to K at position 288.
+The protein's natural variant, known as in EPP1; enzyme retains 19% of activity;, features a modification of the amino acid from P to L at position 334.
+The protein's natural variant, known as in EPP1;, features a modification of the amino acid from V to G at position 362.
+The protein's natural variant, known as in EPP1; enzyme retains 37% of activity, features a modification of the amino acid from K to N at position 379.
+The protein's natural variant, known as in EPP1; loss of activity, features a modification of the amino acid from H to P at position 386.
+The protein's natural variant, known as in EPP1; enzyme almost inactive, features a modification of the amino acid from C to S at position 406.
+The protein's natural variant, known as in EPP1; enzyme almost inactive;, features a modification of the amino acid from C to Y at position 406.
+The protein's natural variant, known as in EPP1; no detectable enzymatic activity, features a modification of the amino acid from NPVC to KSVG at position 411.
+The protein's natural variant, known as in EPP1; reduced activity;, features a modification of the amino acid from F to S at position 417.
+The protein's natural variant, known as in strain: LEW/NHsd, ACI/SegHsd, DA/Bkl and F344/NHsd, features a modification of the amino acid from I to V at position 230.
+The protein's natural variant, known as in strain: LEW/NHsd, ACI/SegHsd, DA/Bkl, F344/NHsd and BN/SsNHsd, features a modification of the amino acid from H to P at position 295.
+The protein's natural variant, known as in NEDCFSA;, features a modification of the amino acid from N to S at position 1331.
+The protein's natural variant, known as in NEDCFSA;, features a modification of the amino acid from Y to S at position 1379.
+The protein's natural variant, known as complete loss of function;, features a modification of the amino acid from R to S at position 149.
+The protein's natural variant, known as complete loss of function;, features a modification of the amino acid from I to R at position 260.
+The protein's natural variant, known as reduced function;, features a modification of the amino acid from R to W at position 277.
+The protein's natural variant, known as in 6% of African-Americans;, features a modification of the amino acid from V to A at position 281.
+The protein's natural variant, known as in 3.5% of Asian-American; reduced function;, features a modification of the amino acid from I to F at position 305.
+The natural variant of this protein is characterized by an amino acid alteration from S to T at position 357.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from M to MLGKGRQRRRRQRQRQSPVPRPSDRPAGLGLAKPARRALPTPEPGRKSSDSSLASPGAALQTGPVVRGSGADPEAGFAQPPTRAGPLEGAFNSRTRQATM at position 1.
+The natural variant of this protein is characterized by an amino acid alteration from V to A at position 17.
+The natural variant of this protein is characterized by an amino acid alteration from L to F at position 60.
+The natural variant of this protein is characterized by an amino acid alteration from I to T at position 93.
+The natural variant of this protein is characterized by an amino acid alteration from Q to R at position 114.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from A to V at position 511.
+The protein's natural variant, known as in GSD4; loss of activity;, features a modification of the amino acid from L to P at position 224.
+The protein's natural variant, known as in GSD4; loss of activity;, features a modification of the amino acid from F to L at position 257.
+The protein's natural variant, known as in GSD4; non-progressive form; impairs protein stability; 50% residual activity;, features a modification of the amino acid from Y to S at position 329.
+The protein's natural variant, known as in GSD4; loss of activity;, features a modification of the amino acid from R to C at position 515.
+The protein's natural variant, known as in APBN;, features a modification of the amino acid from R to H at position 515.
+The protein's natural variant, known as in GSD4 and APBN;, features a modification of the amino acid from R to Q at position 524.
+The protein's natural variant, known as in GSD4;, features a modification of the amino acid from H to R at position 545.
+The protein's natural variant, known as in GSD4; childhood neuromuscular form; 15 to 25% residual activity;, features a modification of the amino acid from H to R at position 628.
+The protein's natural variant, known as associated with a significant decrease in urinary kallikrein activity;, features a modification of the amino acid from R to H at position 77.
+The protein's natural variant, known as not associated with changes in urinary kallikrein activity;, features a modification of the amino acid from E to Q at position 145.
+The protein's natural variant, known as in TAM1; increased calcium-dependent susceptibility to proteolytic degradation; decreased calcium-dependent aggregation; decreased calcium-dependent polymerization; no effect on subcellular localization; no effect on the subcellular localization of STIM1; decreased calcium content of intracellular stores; loss of the ability to inhibit store-operated calcium entry (SOCE) activity;, features a modification of the amino acid from D to N at position 44.
+The protein's natural variant, known as in TAM1; increased calcium-dependent susceptibility to proteolytic degradation; decreased calcium-dependent aggregation; decreased calcium-dependent polymerization; no effect on subcellular localization; no effect on the subcellular localization of STIM1; decreased calcium content of intracellular stores; no effect of the ability to inhibit store-operated calcium entry (SOCE) activity; muscle fibers with the mutation have significantly decreased calcium-dependent sensitivity to caffeine, features a modification of the amino acid from G to D at position 103.
+The protein's natural variant, known as in VMCQA; no effect on calcium-dependent susceptibility to proteolytic degradation; increased calcium-dependent aggregation; causes impaired polymerization of the protein; no effect on subcellular localization; decreased calcium content of sarcoplasmic reticulum stores; reduced sarcoplasmic reticulum calcium release during excitation-contraction coupling;, features a modification of the amino acid from D to G at position 244.
+The protein's natural variant, known as in TAM1; no effect on calcium-dependent susceptibility to proteolytic degradation; increased moderately calcium-dependent aggregation; increased moderately calcium-dependent polymerization; no effect on subcellular localization; no effect on the subcellular localization of STIM1; decreased calcium content of intracellular stores; loss of the ability to inhibit store-operated calcium entry (SOCE) activity;, features a modification of the amino acid from I to T at position 385.
+The natural variant of this protein is characterized by an amino acid alteration from S to L at position 362.
+The natural variant of this protein is characterized by an amino acid alteration from A to T at position 4.
+The protein's natural variant, known as in Sr5.3, features a modification of the amino acid from F to L at position 7.
+The protein's natural variant, known as in strain: HK104, HK105, PB800 and PB826, features a modification of the amino acid from T to N at position 30.
+The protein's natural variant, known as in strain: HK104, HK105, PB800 and PB826, features a modification of the amino acid from I to S at position 40.
+The protein's natural variant, known as in strain: HK104, HK105, PB800 and PB826, features a modification of the amino acid from Q to E at position 57.
+The protein's natural variant, known as in strain: HK104, HK105, PB800 and PB826, features a modification of the amino acid from A to T at position 120.
+The natural variant of this protein is characterized by an amino acid alteration from M to V at position 195.
+The protein's natural variant, known as in strain: 975, features a modification of the amino acid from V to D at position 261.
+The protein's natural variant, known as in strain: 975, features a modification of the amino acid from G to P at position 345.
+The protein's natural variant, known as in CHOCNS; unknown pathological significance, features a modification of the amino acid from A to T at position 142.
+The protein's natural variant, known as in CHOCNS; unknown pathological significance, features a modification of the amino acid from D to Y at position 175.
+The protein's natural variant, known as in CHOCNS; unknown pathological significance, features a modification of the amino acid from I to M at position 293.
+The protein's natural variant, known as in a breast infiltrating ductal carcinoma sample; somatic mutation;, features a modification of the amino acid from K to E at position 500.
+The protein's natural variant, known as in CHOCNS, features a modification of the amino acid from R to C at position 867.
+The protein's natural variant, known as in CHOCNS; unknown pathological significance, features a modification of the amino acid from L to P at position 871.
+The protein's natural variant, known as in CHOCNS, features a modification of the amino acid from R to P at position 876.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample and CHOCNS; somatic mutation;, features a modification of the amino acid from R to W at position 876.
+The protein's natural variant, known as in CHOCNS; unknown pathological significance, features a modification of the amino acid from R to Q at position 1299.
+The protein's natural variant, known as in a lung large cell carcinoma sample; somatic mutation, features a modification of the amino acid from E to K at position 1315.
+The protein's natural variant, known as in CHOCNS; unknown pathological significance, features a modification of the amino acid from R to P at position 1350.
+The protein's natural variant, known as found in a patient with chronic pancreatitis; unknown pathological significance; catalytic activity comparable to that of wild type; the mutant undergoes proteolytic degradation during trypsin-mediated activation;, features a modification of the amino acid from G to R at position 18.
+The protein's natural variant, known as found in patients with chronic pancreatitis; unknown pathological significance;, features a modification of the amino acid from R to Q at position 29.
+The protein's natural variant, known as in PCTT; associated with disease susceptibility; highly reduced catalytic efficiency, features a modification of the amino acid from G to V at position 32.
+The protein's natural variant, known as found in a patient with chronic pancreatitis; unknown pathological significance; catalytic activity comparable to that of wild type, features a modification of the amino acid from D to Y at position 35.
+The protein's natural variant, known as rare variant; results in normal secretion and activity;, features a modification of the amino acid from R to Q at position 37.
+The protein's natural variant, known as rare variant that may be associated with susceptibility to pancreatitis; results in markedly reduced protein secretion;, features a modification of the amino acid from Q to R at position 48.
+The protein's natural variant, known as found in a patient with chronic pancreatitis; unknown pathological significance; the mutant is not secreted;, features a modification of the amino acid from G to R at position 61.
+The protein's natural variant, known as in PCTT; associated with susceptibility to disease; results in markedly reduced protein secretion;, features a modification of the amino acid from A to T at position 73.
+The protein's natural variant, known as found in a patient with chronic pancreatitis; unknown pathological significance, features a modification of the amino acid from K to N at position 151.
+The protein's natural variant, known as in PCTT; associated with susceptibility to disease; the mutant is not secreted, features a modification of the amino acid from C to Y at position 155.
+The protein's natural variant, known as rare variant; found in a patient with chronic pancreatitis; unknown pathological significance;, features a modification of the amino acid from R to H at position 162.
+The protein's natural variant, known as in PCTT; associated with disease susceptibility; impaired catalytic activity;, features a modification of the amino acid from Q to R at position 178.
+The protein's natural variant, known as rare variant; found in a patient with chronic pancreatitis; unknown pathological significance;, features a modification of the amino acid from M to V at position 200.
+The natural variant of this protein is characterized by an amino acid alteration from I to M at position 209.
+The protein's natural variant, known as in PCTT; associated with susceptibility to disease; results in markedly reduced protein secretion and loss of activity;, features a modification of the amino acid from G to R at position 217.
+The protein's natural variant, known as in PCTT; associated with susceptibility to disease; reduced protein secretion; impaired catalytic activity;, features a modification of the amino acid from G to S at position 217.
+The natural variant of this protein is characterized by an amino acid alteration from G to S at position 218.
+The protein's natural variant, known as rare variant; results in impaired protein secretion, features a modification of the amino acid from L to R at position 220.
+The protein's natural variant, known as found in a patient with chronic pancreatitis; unknown pathological significance, features a modification of the amino acid from E to K at position 225.
+The protein's natural variant, known as in PCTT; associated with susceptibility to disease; slightly reduced activity;, features a modification of the amino acid from V to I at position 235.
+The protein's natural variant, known as found in patients with chronic pancreatitis; unknown pathological significance, features a modification of the amino acid from S to A at position 239.
+The protein's natural variant, known as found in patients with chronic pancreatitis; unknown pathological significance, features a modification of the amino acid from S to C at position 239.
+The protein's natural variant, known as found in patients with chronic pancreatitis; unknown pathological significance, features a modification of the amino acid from K to E at position 247.
+The protein's natural variant, known as in PCTT; associated with disease susceptibility; results in reduced protein secretion and loss of activity;, features a modification of the amino acid from P to L at position 249.
+The protein's natural variant, known as in PCTT; associated with disease susceptibility; results in altered enzyme specificity and loss of activity, features a modification of the amino acid from V to E at position 250.
+The protein's natural variant, known as found in a patient with chronic pancreatitis; unknown pathological significance; mutant protein secretion, activity and trypsin-mediated degradation are comparable to those of wild-type;, features a modification of the amino acid from R to Q at position 254.
+The protein's natural variant, known as in PCTT; associated with susceptibility to disease; results in reduced secretion; normal activity; the mutant undergoes proteolytic degradation during trypsin-mediated activation;, features a modification of the amino acid from R to W at position 254.
+The protein's natural variant, known as found in patients with chronic pancreatitis; unknown pathological significance;, features a modification of the amino acid from A to T at position 257.
+The protein's natural variant, known as found in a patient with chronic pancreatitis; unknown pathological significance;, features a modification of the amino acid from N to S at position 263.
+The protein's natural variant, known as in HAE8; unknown pathological significance, features a modification of the amino acid from T to S at position 144.
+The protein's natural variant, known as in SPH5; Nippon/Fukuoka;, features a modification of the amino acid from A to T at position 112.
+The protein's natural variant, known as in SPH5; Komatsu;, features a modification of the amino acid from D to Y at position 145.
+The protein's natural variant, known as in SPH5; Tozeur;, features a modification of the amino acid from R to Q at position 280.
+The protein's natural variant, known as in SPH5; Shiga;, features a modification of the amino acid from R to C at position 287.
+The protein's natural variant, known as in strain: cv. Little Marvel, features a modification of the amino acid from A to W at position 29.
+The protein's natural variant, known as in BDC;, features a modification of the amino acid from M to V at position 173.
+The protein's natural variant, known as in BDC; decrease of induction of SMAD protein signal transduction with either BMPR1A or BMPR1B; less induction of chondrgenesis; no phosphorylation of SMAD1-SMAD5-SMAD8 protein complex; reduction of protein level; abnormal proteolysis product, features a modification of the amino acid from T to P at position 201.
+The protein's natural variant, known as in BDC, features a modification of the amino acid from T to N at position 203.
+The protein's natural variant, known as in BDC; no induction of SMAD protein signal transduction via BMPR1A; less induction of chondrgenesis; no phosphorylation of SMAD1-SMAD5-SMAD8 protein complex; reduction of protein level; abnormal proteolysis product, features a modification of the amino acid from L to P at position 263.
+The protein's natural variant, known as in SYM1B; the mature GDF5 protein is detected as the wild-type in the supernatant derived from the mutant transfected cells;, features a modification of the amino acid from L to R at position 373.
+The protein's natural variant, known as in AMD2B;, features a modification of the amino acid from R to Q at position 378.
+The protein's natural variant, known as in BDA2; reduces activity; impairs processing;, features a modification of the amino acid from R to Q at position 380.
+The protein's natural variant, known as in BDA1C; less effective than wild-type in stimulating chondrogenesis; impairs BMP signaling through BMPR1A;, features a modification of the amino acid from R to C at position 399.
+The protein's natural variant, known as in AMD2A;, features a modification of the amino acid from C to Y at position 400.
+The protein's natural variant, known as in SYNS2 and BDA1C; reduced interaction with NOG; reduces affinity to BMPR1A; impairs BMP signaling through BMPR1A; impairs chondrogenesis, features a modification of the amino acid from W to R at position 414.
+The protein's natural variant, known as in AMD2B;, features a modification of the amino acid from P to T at position 436.
+The protein's natural variant, known as in SYNS2 and SYM1B; increased biological activity when compared to wild-type; normal binding to BMPR1B ectodomain but increased binding to that of BMPR1A;, features a modification of the amino acid from R to L at position 438.
+The protein's natural variant, known as in AMD2B; located on the same allele as L-437 del and L-440, features a modification of the amino acid from S to T at position 439.
+The protein's natural variant, known as in AMD2B; located on the same allele as L-437 del and T-439, features a modification of the amino acid from H to L at position 440.
+The protein's natural variant, known as in AMD2B, SYNS2 and BDA2; the mutant is almost inactive; loss of binding to BMPR1A and BMPR1B ectodomains; no induction of SMAD1-SMAD5-SMAD8 protein complex phosphorylation; impairs nuclear translocation of phosphotylated SMAD1-SMAD5-SMAD8 protein complex; no ability to induce SMAD protein signal transduction; binds to NOG;, features a modification of the amino acid from L to P at position 441.
+The protein's natural variant, known as in SYNS2, features a modification of the amino acid from N to K at position 445.
+The protein's natural variant, known as in SYNS2; resistant to NOG inhibition; no change in binding with MPR1A and BMPR1B; strong induction of chondrogenesis, features a modification of the amino acid from N to T at position 445.
+The protein's natural variant, known as in SYNS2; reduction in binding affinity with BMPR2; no change in binding affinity with BMPR1A; no change in binding affinity with BMPR1B; decreases induction of SMAD1-SMAD5-SMAD8 protein complex phosphorylation; delay of phosphotylated SMAD1-SMAD5-SMAD8 protein complex nuclear translocation; strong reduction of SMAD protein signal transduction; reduction of chondrocyte differentiation; strong improvement of chondrogenesis; decrease of NOG binding; resistant to NOG inhibition; no chondrogenesis inhibition;, features a modification of the amino acid from S to N at position 475.
+The protein's natural variant, known as in BDC, features a modification of the amino acid from V to M at position 486.
+The protein's natural variant, known as in SYM1B;, features a modification of the amino acid from E to K at position 491.
+The protein's natural variant, known as may be associated with ASRT5;, features a modification of the amino acid from P to L at position 22.
+The protein's natural variant, known as may be associated with ASRT5; abolishes phosphorylation of Ser-110; abolishes interaction with PIN1; no effect on cytoplasmic localization; reduces protein stability;, features a modification of the amino acid from P to A at position 111.
+The protein's natural variant, known as may be associated with ASRT5;, features a modification of the amino acid from V to M at position 134.
+The protein's natural variant, known as may be associated with ASRT5;, features a modification of the amino acid from L to V at position 400.
+The protein's natural variant, known as may be associated with ASRT5;, features a modification of the amino acid from R to Q at position 429.
+The protein's natural variant, known as in MRXSSR; a reduced spermine/spermidine ratio is observed in patient lymphoblastoid cells consistent with impaired spermine biosynthesis;, features a modification of the amino acid from G to S at position 56.
+The protein's natural variant, known as in MRXSSR;, features a modification of the amino acid from F to L at position 58.
+The protein's natural variant, known as in MRXSSR; a reduced spermine/spermidine ratio is observed in patient lymphoblastoid cells consistent with impaired spermine biosynthesis;, features a modification of the amino acid from G to E at position 67.
+The protein's natural variant, known as in MRXSSR;, features a modification of the amino acid from V to G at position 132.
+The protein's natural variant, known as in MRXSSR; mild disease phenotype; a reduced spermine/spermidine ratio is observed in patient lymphoblastoid cells consistent with impaired spermine biosynthesis;, features a modification of the amino acid from Y to C at position 328.
+The protein's natural variant, known as in a lung neuroendocrine carcinoma sample; somatic mutation, features a modification of the amino acid from L to I at position 554.
+The protein's natural variant, known as in an ovarian mucinous carcinoma sample; somatic mutation, features a modification of the amino acid from G to A at position 663.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation, features a modification of the amino acid from C to Y at position 1003.
+The protein's natural variant, known as in a breast infiltrating ductal carcinoma sample; somatic mutation, features a modification of the amino acid from E to K at position 1022.
+The protein's natural variant, known as in TEM-4, features a modification of the amino acid from L to F at position 19.
+The protein's natural variant, known as in TEM-2, TEM-3, TEM-8, TEM-16 and TEM-24, features a modification of the amino acid from Q to K at position 37.
+The protein's natural variant, known as in IRT-4, features a modification of the amino acid from M to L at position 67.
+The protein's natural variant, known as in TEM-3, TEM-4, TEM-6, TEM-8, TEM-16 and TEM-24, features a modification of the amino acid from E to K at position 102.
+The protein's natural variant, known as in TEM-6 and TEM-16, features a modification of the amino acid from R to H at position 162.
+The protein's natural variant, known as in TEM-5, TEM-8 and TEM-24, features a modification of the amino acid from R to S at position 162.
+The protein's natural variant, known as in TEM-5 and TEM-24, features a modification of the amino acid from A to T at position 235.
+The protein's natural variant, known as in TEM-3, TEM-4 and TEM-8, features a modification of the amino acid from G to S at position 236.
+The protein's natural variant, known as in TEM-5 and TEM-24, features a modification of the amino acid from E to K at position 237.
+The protein's natural variant, known as in TEM-4, features a modification of the amino acid from T to M at position 261.
+The protein's natural variant, known as in IRT-4, features a modification of the amino acid from N to D at position 272.
+The natural variant of this protein is characterized by an amino acid alteration from D to N at position 600.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 257.
+The natural variant of this protein is characterized by an amino acid alteration from L to V at position 292.
+The protein's natural variant, known as no alteration in ligand-mediated receptor activity;, features a modification of the amino acid from I to V at position 36.
+The protein's natural variant, known as no alteration in ligand-mediated receptor activity;, features a modification of the amino acid from A to T at position 46.
+The protein's natural variant, known as no alteration in ligand-mediated receptor activity;, features a modification of the amino acid from R to L at position 55.
+The protein's natural variant, known as decrease in ligand-mediated and ligand-independent receptor activity;, features a modification of the amino acid from R to S at position 131.
+The protein's natural variant, known as increase in ligand-mediated receptor activity;, features a modification of the amino acid from H to R at position 133.
+The protein's natural variant, known as no alteration in ligand-mediated receptor activity;, features a modification of the amino acid from H to R at position 137.
+The protein's natural variant, known as no alteration in ligand-mediated receptor activity;, features a modification of the amino acid from F to L at position 273.
+The protein's natural variant, known as in an ovarian mucinous carcinoma sample; somatic mutation, features a modification of the amino acid from K to E at position 275.
+The protein's natural variant, known as in a breast mucinous carcinoma sample; somatic mutation, features a modification of the amino acid from G to A at position 655.
+The natural variant of this protein is characterized by an amino acid alteration from G to E at position 1703.
+The protein's natural variant, known as found in a patient with hearing loss; unknown pathological significance, features a modification of the amino acid from S to SS at position 116.
+The protein's natural variant, known as found in a patient with hearing loss; unknown pathological significance;, features a modification of the amino acid from V to M at position 306.
+The protein's natural variant, known as found in a patient with hearing loss; unknown pathological significance;, features a modification of the amino acid from E to D at position 385.
+The protein's natural variant, known as benign variant; originally reported as possible disease-causing mutation in a patient with hearing loss;, features a modification of the amino acid from G to E at position 662.
+The protein's natural variant, known as found in a patient with hearing loss; unknown pathological significance;, features a modification of the amino acid from G to D at position 674.
+The protein's natural variant, known as found in a patient with hearing loss; unknown pathological significance;, features a modification of the amino acid from S to P at position 910.
+The protein's natural variant, known as in strain: N16961, features a modification of the amino acid from S to A at position 10.
+The protein's natural variant, known as in strain: O17, features a modification of the amino acid from S to L at position 68.
+The protein's natural variant, known as in PBD6B, features a modification of the amino acid from L to R at position 177.
+The protein's natural variant, known as in PBD6B, features a modification of the amino acid from C to F at position 276.
+The protein's natural variant, known as in PBD6B; neonatal adrenoleukodystrophy; abolished E3 ubiquitin-protein ligase activity;, features a modification of the amino acid from H to Q at position 290.
+The protein's natural variant, known as in PBD6A, features a modification of the amino acid from C to F at position 296.
+The protein's natural variant, known as in PBD6B, features a modification of the amino acid from R to Q at position 311.
+The protein's natural variant, known as in strain: BALB/c, features a modification of the amino acid from H to R at position 186.
+The protein's natural variant, known as in strain: BALB/c, features a modification of the amino acid from A to T at position 455.
+The protein's natural variant, known as in strain: BALB/c, features a modification of the amino acid from C to Y at position 752.
+The protein's natural variant, known as in strain: BALB/c, features a modification of the amino acid from D to N at position 1006.
+The protein's natural variant, known as in STL1O;, features a modification of the amino acid from C to Y at position 57.
+The protein's natural variant, known as in SEDSTN;, features a modification of the amino acid from G to R at position 207.
+The protein's natural variant, known as in STL1;, features a modification of the amino acid from G to D at position 240.
+The protein's natural variant, known as in STL1O;, features a modification of the amino acid from G to D at position 267.
+The protein's natural variant, known as in STL1, features a modification of the amino acid from G to R at position 270.
+The protein's natural variant, known as in CZECHD;, features a modification of the amino acid from R to C at position 275.
+The protein's natural variant, known as in STL1, features a modification of the amino acid from G to D at position 282.
+The protein's natural variant, known as in KD; abnormal allele expressed in the cartilage;, features a modification of the amino acid from G to D at position 303.
+The protein's natural variant, known as in DRRD;, features a modification of the amino acid from G to R at position 318.
+The protein's natural variant, known as in spondylometaphyseal dysplasia; congenital type;, features a modification of the amino acid from G to R at position 354.
+The protein's natural variant, known as in SEDC, features a modification of the amino acid from G to R at position 375.
+The protein's natural variant, known as in SEDC, features a modification of the amino acid from G to S at position 447.
+The protein's natural variant, known as in STL1;, features a modification of the amino acid from G to A at position 453.
+The protein's natural variant, known as in ACG2;, features a modification of the amino acid from G to D at position 453.
+The protein's natural variant, known as in ACG2, features a modification of the amino acid from G to V at position 453.
+The protein's natural variant, known as in SEMDSTWK;, features a modification of the amino acid from G to V at position 492.
+The protein's natural variant, known as in STL1, features a modification of the amino acid from G to R at position 501.
+The protein's natural variant, known as in SEMDSTWK;, features a modification of the amino acid from G to C at position 504.
+The protein's natural variant, known as in ACG2, features a modification of the amino acid from G to D at position 510.
+The protein's natural variant, known as in ACG2;, features a modification of the amino acid from G to S at position 513.
+The protein's natural variant, known as in ACG2;, features a modification of the amino acid from G to D at position 516.
+The protein's natural variant, known as in ACG2, features a modification of the amino acid from D to V at position 547.
+The protein's natural variant, known as in STL1;, features a modification of the amino acid from R to C at position 565.
+The protein's natural variant, known as in DRRD;, features a modification of the amino acid from L to F at position 667.
+The protein's natural variant, known as in ANFH1;, features a modification of the amino acid from G to S at position 717.
+The protein's natural variant, known as in ACG2, features a modification of the amino acid from G to V at position 717.
+The protein's natural variant, known as in OSCDP; also in mild spondyloepiphyseal dysplasia and precocious osteoarthritis;, features a modification of the amino acid from R to C at position 719.
+The protein's natural variant, known as in ACG2, features a modification of the amino acid from G to A at position 771.
+The protein's natural variant, known as in ACG2, features a modification of the amino acid from G to D at position 771.
+The protein's natural variant, known as in SEDC and hypochondrogenesis; lethal;, features a modification of the amino acid from G to S at position 774.
+The protein's natural variant, known as in ACG2, features a modification of the amino acid from G to R at position 780.
+The protein's natural variant, known as in ACG2, features a modification of the amino acid from G to R at position 795.
+The protein's natural variant, known as in hypochondrogenesis, features a modification of the amino acid from G to A at position 804.
+The protein's natural variant, known as in SEDC;, features a modification of the amino acid from G to S at position 855.
+The protein's natural variant, known as in ACG2 and SEDC;, features a modification of the amino acid from G to R at position 891.
+The protein's natural variant, known as in ACG2, features a modification of the amino acid from G to E at position 894.
+The protein's natural variant, known as in SEMDSTWK, features a modification of the amino acid from G to V at position 897.
+The protein's natural variant, known as in EDMMD and STL1;, features a modification of the amino acid from R to C at position 904.
+The protein's natural variant, known as in SEMDSTWK;, features a modification of the amino acid from G to C at position 909.
+The protein's natural variant, known as in ACG2, features a modification of the amino acid from G to D at position 948.
+The protein's natural variant, known as in ACG2;, features a modification of the amino acid from G to S at position 969.
+The protein's natural variant, known as in ACG2, features a modification of the amino acid from G to S at position 981.
+The protein's natural variant, known as in SEDC;, features a modification of the amino acid from R to C at position 989.
+The protein's natural variant, known as in SEMDSTWK;, features a modification of the amino acid from R to G at position 992.
+The protein's natural variant, known as in hypochondrogenesis;, features a modification of the amino acid from G to S at position 1005.
+The protein's natural variant, known as in ACG2, features a modification of the amino acid from G to V at position 1017.
+The protein's natural variant, known as in hypochondrogenesis; lethal;, features a modification of the amino acid from G to E at position 1053.
+The protein's natural variant, known as in ACG2, features a modification of the amino acid from G to V at position 1065.
+The protein's natural variant, known as in ACG2;, features a modification of the amino acid from G to C at position 1110.
+The protein's natural variant, known as in hypochondrogenesis, features a modification of the amino acid from G to C at position 1113.
+The protein's natural variant, known as in ACG2, features a modification of the amino acid from G to R at position 1119.
+The protein's natural variant, known as in ACG2, features a modification of the amino acid from G to S at position 1143.
+The protein's natural variant, known as in STL1, features a modification of the amino acid from G to A at position 1158.
+The protein's natural variant, known as in ANFH1 and LCPD;, features a modification of the amino acid from G to S at position 1170.
+The protein's natural variant, known as in SEDC;, features a modification of the amino acid from G to R at position 1173.
+The protein's natural variant, known as in SEDC, features a modification of the amino acid from G to S at position 1176.
+The protein's natural variant, known as mutation found in a patient with features of multiple epiphyseal dysplasia; features overlap with SEDC, features a modification of the amino acid from G to V at position 1176.
+The protein's natural variant, known as mutation found in a patient with features of multiple epiphyseal dysplasia; features overlap with SEDC, features a modification of the amino acid from G to R at position 1179.
+The protein's natural variant, known as in SEDC, features a modification of the amino acid from I to IGPSGKDGANGIPGPI at position 1184.
+The protein's natural variant, known as in ACG2, features a modification of the amino acid from G to R at position 1188.
+The protein's natural variant, known as in SEDC;, features a modification of the amino acid from G to S at position 1197.
+The protein's natural variant, known as in VPED;, features a modification of the amino acid from G to D at position 1305.
+The protein's natural variant, known as in ANFH1;, features a modification of the amino acid from T to M at position 1383.
+The protein's natural variant, known as in PLSD-T; phenotype previously considered as achondrogenesis-hypochondrogenesis type 2, features a modification of the amino acid from T to N at position 1390.
+The protein's natural variant, known as in PLSD-T;, features a modification of the amino acid from Y to C at position 1391.
+The protein's natural variant, known as in SEDC;, features a modification of the amino acid from T to M at position 1439.
+The protein's natural variant, known as in PLSD-T, features a modification of the amino acid from T to P at position 1448.
+The protein's natural variant, known as in PLSD-T, features a modification of the amino acid from D to H at position 1469.
+The protein's natural variant, known as in PLSD-T, features a modification of the amino acid from C to G at position 1485.
+The protein's natural variant, known as in DFNB67;, features a modification of the amino acid from Y to C at position 127.
+The protein's natural variant, known as in DFNB67;, features a modification of the amino acid from R to W at position 158.
+The protein's natural variant, known as in DFNB67;, features a modification of the amino acid from T to M at position 165.
+The protein's natural variant, known as in DFNB67;, features a modification of the amino acid from R to L at position 176.
+The protein's natural variant, known as in AIIDE; constitutive gain of function resulting in increased receptor signaling pathway via JAK-STAT; no effect on protein abundance, features a modification of the amino acid from A to D at position 634.
+The protein's natural variant, known as in AIIDE; increased activation of protein kinase activity; constitutive gain of function through the transactivation of associated JAK kinases; increased receptor signaling pathway via JAK-STAT, features a modification of the amino acid from S to I at position 703.
+The protein's natural variant, known as in strain: SP#5 and ZR1; reduced susceptibility to evernimicin, features a modification of the amino acid from I to S at position 52.
+The protein's natural variant, known as in strain: Isolate 661nigra, features a modification of the amino acid from T to A at position 44.
+The protein's natural variant, known as in strain: Isolate 661nigra, features a modification of the amino acid from S to F at position 53.
+The protein's natural variant, known as found in a family with myoclonus and dystonia; also found in a sporadic case; unknown pathological significance; single-channel currents of the mutant are smaller than wild-type, likely due to channel stabilization in the lower current amplitude open state; voltage-dependent activation and inactivation as well as ion selectivity are unchanged;, features a modification of the amino acid from R to H at position 1389.
+The natural variant of this protein is characterized by an amino acid alteration from T to S at position 66.
+The protein's natural variant, known as in MTDPS20; may affect exon 9 splicing; decreased interaction with POLG; does not rescue cerebellar defects in a LIG3 deficiency zebrafish model, features a modification of the amino acid from K to N at position 537.
+The protein's natural variant, known as in MTDPS20; severely decreased protein levels, features a modification of the amino acid from P to L at position 609.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from D to N at position 717.
+The protein's natural variant, known as in MTDPS20; severely decreased protein levels; does not rescue cerebellar defects in a LIG3 deficiency zebrafish model, features a modification of the amino acid from G to R at position 964.
+The protein's natural variant, known as in MTDPS20; severely decreased protein levels, features a modification of the amino acid from C to Y at position 999.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from G to R at position 36.
+The protein's natural variant, known as in MRXSR;, features a modification of the amino acid from R to W at position 148.
+The protein's natural variant, known as in MRXSR;, features a modification of the amino acid from P to S at position 150.
+The natural variant of this protein is characterized by an amino acid alteration from S to SQGPGI at position 166.
+The protein's natural variant, known as in PEOB4; decreased protein levels;, features a modification of the amino acid from E to K at position 44.
+The protein's natural variant, known as in NCPH1; impairs adenosine triphosphate binding; reduction of activity;, features a modification of the amino acid from N to S at position 46.
+The protein's natural variant, known as in MTDPS3;, features a modification of the amino acid from R to K at position 142.
+The protein's natural variant, known as in PEOB4; decreased protein levels;, features a modification of the amino acid from N to K at position 154.
+The protein's natural variant, known as unknown pathological significance;, features a modification of the amino acid from Q to R at position 170.
+The protein's natural variant, known as in MTDPS3;, features a modification of the amino acid from E to K at position 227.
+The protein's natural variant, known as in MTDPS3; significant reduction of activity;, features a modification of the amino acid from L to S at position 250.
+The protein's natural variant, known as reduction of activity;, features a modification of the amino acid from L to R at position 266.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from D to H at position 1155.
+The protein's natural variant, known as in HH15;, features a modification of the amino acid from P to S at position 218.
+The protein's natural variant, known as in HH15; 15 to 30% reduction in enzymatic activity compared to wild-type;, features a modification of the amino acid from R to Q at position 306.
+The protein's natural variant, known as in HH15; with anosmia; results in Kallmann syndrome in the presence of FGFR1 mutation Gln-250; approximately 50% reduction in enzymatic activity compared to wild-type;, features a modification of the amino acid from R to W at position 306.
+The protein's natural variant, known as in HH15; approximately 30% reduction in enzymatic activity compared to wild-type when heparan sulfate is the acceptor substrate;, features a modification of the amino acid from R to Q at position 323.
+The protein's natural variant, known as in HH15; with or without anosmia; results in Kallmann syndrome in the presence of NSMF mutation Ala-480; 25 to 35% reduction in enzymatic activity compared to wild-type;, features a modification of the amino acid from R to W at position 382.
+The protein's natural variant, known as in HH15; with anosmia; 30 to 70% reduction in enzymatic activity compared to wild-type, features a modification of the amino acid from M to V at position 404.
+The protein's natural variant, known as in WD; affects copper-induced relocalization; the mutant is constitutively trafficked to the basolateral membrane instead of staying in the TGN under low copper conditions; does not affect interaction with COMMD1;, features a modification of the amino acid from N to S at position 41.
+The protein's natural variant, known as in WD; unknown pathological significance;, features a modification of the amino acid from Y to N at position 44.
+The protein's natural variant, known as in WD; decreased copper transport activity; decreased ATPase activity; increased interaction with COMMD1; decreased localization to trans-Golgi network; increased degradation;, features a modification of the amino acid from G to V at position 85.
+The protein's natural variant, known as in WD; unknown pathological significance;, features a modification of the amino acid from C to R at position 108.
+The protein's natural variant, known as in WD; unknown pathological significance;, features a modification of the amino acid from R to W at position 136.
+The protein's natural variant, known as in WD; unknown pathological significance;, features a modification of the amino acid from R to W at position 148.
+The natural variant of this protein is characterized by an amino acid alteration from V to L at position 149.
+The protein's natural variant, known as in WD; unknown pathological significance;, features a modification of the amino acid from C to F at position 157.
+The protein's natural variant, known as in WD; unknown pathological significance, features a modification of the amino acid from G to V at position 170.
+The natural variant of this protein is characterized by an amino acid alteration from V to L at position 290.
+The protein's natural variant, known as in WD; unknown pathological significance;, features a modification of the amino acid from S to C at position 382.
+The protein's natural variant, known as no effect on copper transport activity;, features a modification of the amino acid from S to A at position 406.
+The protein's natural variant, known as decreased copper transport rates; no effect on ATPase activity;, features a modification of the amino acid from V to L at position 456.
+The natural variant of this protein is characterized by an amino acid alteration from L to V at position 466.
+The protein's natural variant, known as in WD; unknown pathological significance; does not affect interaction with COMMD1;, features a modification of the amino acid from A to S at position 486.
+The protein's natural variant, known as in WD; decreased copper transport activity; decreased ATPase activity; does not affect interaction with COMMD1;, features a modification of the amino acid from L to S at position 492.
+The protein's natural variant, known as in WD; unknown pathological significance; no effect on copper transport activity; does not affect interaction with COMMD1, features a modification of the amino acid from Y to H at position 532.
+The protein's natural variant, known as in WD; likely benign variant;, features a modification of the amino acid from V to A at position 536.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from P to L at position 539.
+The protein's natural variant, known as in WD; unknown pathological significance; does not affect interaction with COMMD1;, features a modification of the amino acid from E to K at position 541.
+The protein's natural variant, known as in WD; unknown pathological significance, features a modification of the amino acid from L to P at position 549.
+The protein's natural variant, known as in WD; increased interaction with COMMD1; decreased localization to trans-Glogi network;, features a modification of the amino acid from G to D at position 591.
+The protein's natural variant, known as in WD; unknown pathological significance;, features a modification of the amino acid from G to S at position 591.
+The protein's natural variant, known as in WD; unknown pathological significance;, features a modification of the amino acid from V to I at position 597.
+The protein's natural variant, known as in WD; unknown pathological significance; increased interaction with COMMD1, features a modification of the amino acid from A to P at position 604.
+The protein's natural variant, known as in WD; unknown pathological significance;, features a modification of the amino acid from V to G at position 606.
+The protein's natural variant, known as in WD; unknown pathological significance, features a modification of the amino acid from FD to Y at position 609.
+The protein's natural variant, known as in WD; unknown pathological significance;, features a modification of the amino acid from G to C at position 614.
+The protein's natural variant, known as in WD; unknown pathological significance; does not affect interaction with COMMD1;, features a modification of the amino acid from R to Q at position 616.
+The protein's natural variant, known as in WD; decreased copper transport activity; increased ATPase activity; does not affect interaction with COMMD1;, features a modification of the amino acid from R to W at position 616.
+The protein's natural variant, known as in WD; unknown pathological significance; no effect on protein abundance; no effect on protein localization; may have an effect on copper transport activity; no effect on ATPase activity; does not affect interaction with COMMD1;, features a modification of the amino acid from G to A at position 626.
+The protein's natural variant, known as in WD; unknown pathological significance; no effect on protein abundance; no effect on protein localization; no effect on copper transport activity;, features a modification of the amino acid from H to Y at position 639.
+The protein's natural variant, known as in WD; unknown pathological significance; no effect on protein abundance; no effect on protein localization; no effect on copper transport activity; does not affect interaction with COMMD1;, features a modification of the amino acid from L to S at position 641.
+The protein's natural variant, known as in WD; unknown pathological significance; no effect on protein abundance; no effect on protein localization; no effect on copper transport activity; does not affect interaction with COMMD1;, features a modification of the amino acid from D to H at position 642.
+The protein's natural variant, known as in WD; also found in a patient with hypoceruloplasminemia without clinical manifestations of WD in the central nervous system or liver; a liver biopsy of the patient with hypoceruloplasminemia shows no copper or iron accumulation in Kupffer cells or hepatocytes; due to a nucleotide substitution that also results in out-of-frame partial skipping of exon 6, stop gain and reduced expression of the truncated protein; variant R-645 has no effect on protein localization; no effect on copper transport; does not affect interaction with COMMD1;, features a modification of the amino acid from M to R at position 645.
+The protein's natural variant, known as in WD; unknown pathological significance; no effect on protein abundance; altered copper-induced relocalization; no effect on copper transport activity, features a modification of the amino acid from S to Y at position 653.
+The protein's natural variant, known as in WD; unknown pathological significance;, features a modification of the amino acid from S to R at position 657.
+The protein's natural variant, known as in WD; unknown pathological significance;, features a modification of the amino acid from M to I at position 665.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from P to L at position 690.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from G to R at position 691.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from S to C at position 693.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from C to Y at position 703.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from L to P at position 708.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from G to A at position 710.
+The protein's natural variant, known as in WD, features a modification of the amino acid from G to R at position 710.
+The protein's natural variant, known as in WD; decreased copper transport activity; no effect on ATPase activity;, features a modification of the amino acid from G to S at position 710.
+The protein's natural variant, known as in WD, features a modification of the amino acid from G to V at position 710.
+The protein's natural variant, known as in WD, features a modification of the amino acid from G to E at position 711.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from G to R at position 711.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from G to W at position 711.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from Y to C at position 713.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from S to P at position 721.
+The natural variant of this protein is characterized by an amino acid alteration from R to G at position 723.
+The protein's natural variant, known as in WD; unknown pathological significance;, features a modification of the amino acid from M to V at position 729.
+The protein's natural variant, known as in WD; unknown pathological significance, features a modification of the amino acid from V to A at position 731.
+The protein's natural variant, known as in WD; unknown pathological significance, features a modification of the amino acid from L to H at position 732.
+The protein's natural variant, known as in WD; unknown pathological significance, features a modification of the amino acid from L to P at position 732.
+The protein's natural variant, known as in WD; unknown pathological significance, features a modification of the amino acid from T to R at position 737.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from Y to C at position 741.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from S to P at position 744.
+The protein's natural variant, known as in WD; unknown pathological significance;, features a modification of the amino acid from L to P at position 745.
+The protein's natural variant, known as in WD, features a modification of the amino acid from I to F at position 747.
+The protein's natural variant, known as in WD, features a modification of the amino acid from A to G at position 756.
+The protein's natural variant, known as in WD; decreased copper transport activity; increased ATPase activity;, features a modification of the amino acid from P to L at position 760.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from D to G at position 765.
+The protein's natural variant, known as in WD; unknown pathological significance;, features a modification of the amino acid from D to H at position 765.
+The protein's natural variant, known as in WD; decreased copper transport activity; increased ATPase activity; decreased localization to TGN and reduced capacity to redistribute to cytoplasmic vesicles under high-copper levels;, features a modification of the amino acid from D to N at position 765.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from T to M at position 766.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from T to R at position 766.
+The protein's natural variant, known as in WD, features a modification of the amino acid from P to H at position 768.
+The protein's natural variant, known as in WD, features a modification of the amino acid from M to I at position 769.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from M to R at position 769.
+The protein's natural variant, known as in WD; possible decreased copper transport activity; increased ATPase activity;, features a modification of the amino acid from M to V at position 769.
+The protein's natural variant, known as in WD, features a modification of the amino acid from L to P at position 776.
+The protein's natural variant, known as in WD; unknown pathological significance; no effect on copper transport activity; decreased localization to TGN and reduced capacity to redistribute to cytoplasmic vesicles under high-copper levels;, features a modification of the amino acid from L to V at position 776.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from R to G at position 778.
+The protein's natural variant, known as in WD; most common mutation; decreased copper transport activity; extensively localized throughout the cell in the distribution pattern of the endoplasmic reticulum;, features a modification of the amino acid from R to L at position 778.
+The protein's natural variant, known as in WD; decreased copper transport activity;, features a modification of the amino acid from R to Q at position 778.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from R to W at position 778.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from W to G at position 779.
+The protein's natural variant, known as in WD; decreased copper ion transmembrane transporter activity;, features a modification of the amino acid from T to I at position 788.
+The protein's natural variant, known as in WD; unknown pathological significance;, features a modification of the amino acid from L to F at position 795.
+The protein's natural variant, known as in WD, features a modification of the amino acid from L to R at position 795.
+The protein's natural variant, known as in WD, features a modification of the amino acid from R to S at position 816.
+The natural variant of this protein is characterized by an amino acid alteration from V to L at position 825.
+The protein's natural variant, known as in WD; unknown pathological significance;, features a modification of the amino acid from R to P at position 827.
+The protein's natural variant, known as in WD; yeast complementation assays show that the variant does not rescue iron-uptake deficiency of yeast mutant ccc2;, features a modification of the amino acid from R to W at position 827.
+The protein's natural variant, known as decreased copper transport activity; no effect on ATPase activity;, features a modification of the amino acid from K to R at position 832.
+The protein's natural variant, known as in WD; unknown pathological significance;, features a modification of the amino acid from G to E at position 836.
+The protein's natural variant, known as in WD; decreased copper transport activity; increased ATPase activity;, features a modification of the amino acid from P to L at position 840.
+The protein's natural variant, known as in WD; decreased copper transport activity; increased ATPase activity;, features a modification of the amino acid from I to T at position 857.
+The protein's natural variant, known as in WD; unknown pathological significance, features a modification of the amino acid from T to A at position 858.
+The protein's natural variant, known as in WD, features a modification of the amino acid from A to T at position 861.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 864.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from G to R at position 869.
+The protein's natural variant, known as in WD, features a modification of the amino acid from G to V at position 869.
+The protein's natural variant, known as in WD; unknown pathological significance;, features a modification of the amino acid from A to P at position 874.
+The protein's natural variant, known as in WD; decreased copper transport activity; increased ATPase activity; decreased localization to the TGN;, features a modification of the amino acid from A to V at position 874.
+The protein's natural variant, known as individuals heterozygous for Wilson disease mutations on the R-875 background may manifest the disease phenotype under conditions of copper deficiency; affects protein folding; localized to the ER and absent from TGN under low copper conditions; in response to high copper levels it relocalizes to vesicles and properly cycle back to TGN;, features a modification of the amino acid from G to R at position 875.
+The protein's natural variant, known as in WD; requires 2 nucleotide substitutions, features a modification of the amino acid from G to V at position 875.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from V to M at position 890.
+The protein's natural variant, known as in WD; unknown pathological significance;, features a modification of the amino acid from G to D at position 891.
+The protein's natural variant, known as in WD, features a modification of the amino acid from G to V at position 891.
+The protein's natural variant, known as in WD, features a modification of the amino acid from Q to R at position 898.
+The protein's natural variant, known as in WD; unknown pathological significance, features a modification of the amino acid from I to F at position 899.
+The protein's natural variant, known as in WD, features a modification of the amino acid from D to E at position 918.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from D to N at position 918.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from R to G at position 919.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from R to W at position 919.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from S to N at position 921.
+The protein's natural variant, known as in WD; unknown pathological significance;, features a modification of the amino acid from S to R at position 921.
+The protein's natural variant, known as in WD; unknown pathological significance;, features a modification of the amino acid from T to P at position 933.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from T to M at position 935.
+The protein's natural variant, known as in WD; unknown pathological significance;, features a modification of the amino acid from L to V at position 936.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from W to C at position 939.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from G to C at position 943.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from G to D at position 943.
+The protein's natural variant, known as in WD; no effect on copper transport activity; normally localized to TGN network but unable to redistribute to cytoplasmic vesicles in response to copper;, features a modification of the amino acid from G to S at position 943.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from V to G at position 949.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from I to F at position 967.
+The protein's natural variant, known as in WD; decreased copper transport activity; increased ATPase activity; no effect on localization;, features a modification of the amino acid from R to Q at position 969.
+The protein's natural variant, known as in WD; unknown pathological significance;, features a modification of the amino acid from R to W at position 969.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from A to V at position 971.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from T to M at position 974.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from S to Y at position 975.
+The protein's natural variant, known as in WD; loss of copper transport activity;, features a modification of the amino acid from T to M at position 977.
+The protein's natural variant, known as in WD; unknown pathological significance;, features a modification of the amino acid from C to Y at position 980.
+The protein's natural variant, known as in WD; unknown pathological significance;, features a modification of the amino acid from A to T at position 982.
+The protein's natural variant, known as in WD; unknown pathological significance;, features a modification of the amino acid from A to V at position 982.
+The protein's natural variant, known as in WD, features a modification of the amino acid from C to Y at position 985.
+The protein's natural variant, known as in WD; unknown pathological significance, features a modification of the amino acid from L to P at position 987.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from G to R at position 988.
+The protein's natural variant, known as in WD; unknown pathological significance, features a modification of the amino acid from A to P at position 990.
+The protein's natural variant, known as in WD; yeast complementation assays show that the variant mildly rescue iron-uptake deficiency of yeast mutant ccc2;, features a modification of the amino acid from T to M at position 991.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from P to H at position 992.
+The protein's natural variant, known as in WD; common mutation; decreased copper transport activity; no effect on ATPase activity;, features a modification of the amino acid from P to L at position 992.
+The protein's natural variant, known as in WD; unknown pathological significance; no effect on copper transport activity;, features a modification of the amino acid from V to A at position 995.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from M to T at position 996.
+The protein's natural variant, known as in WD, features a modification of the amino acid from G to D at position 998.
+The protein's natural variant, known as in WD; yeast complementation assays show that the variant does not rescue iron-uptake deficiency of yeast mutant ccc2;, features a modification of the amino acid from G to R at position 1000.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from A to T at position 1003.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from A to V at position 1003.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from Q to P at position 1004.
+The protein's natural variant, known as in WD; unknown pathological significance;, features a modification of the amino acid from K to E at position 1010.
+The protein's natural variant, known as in WD; unknown pathological significance;, features a modification of the amino acid from K to R at position 1010.
+The protein's natural variant, known as in WD; yeast complementation assays show that the variant does not rescue iron-uptake deficiency of yeast mutant ccc2;, features a modification of the amino acid from K to T at position 1010.
+The protein's natural variant, known as in WD; unknown pathological significance, features a modification of the amino acid from G to R at position 1012.
+The protein's natural variant, known as in WD; unknown pathological significance;, features a modification of the amino acid from G to V at position 1012.
+The protein's natural variant, known as in WD; unknown pathological significance;, features a modification of the amino acid from M to I at position 1017.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from A to V at position 1018.
+The protein's natural variant, known as in WD; unknown pathological significance;, features a modification of the amino acid from I to V at position 1021.
+The protein's natural variant, known as in WD; unknown pathological significance;, features a modification of the amino acid from V to A at position 1024.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from T to I at position 1029.
+The protein's natural variant, known as in WD; unknown pathological significance, features a modification of the amino acid from T to A at position 1031.
+The protein's natural variant, known as in WD, features a modification of the amino acid from T to I at position 1031.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from T to A at position 1033.
+The protein's natural variant, known as in WD, features a modification of the amino acid from T to S at position 1033.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from G to V at position 1035.
+The protein's natural variant, known as in WD; copper ion transmembrane transporter activity;, features a modification of the amino acid from V to I at position 1036.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from R to K at position 1038.
+The protein's natural variant, known as in WD, features a modification of the amino acid from R to P at position 1041.
+The protein's natural variant, known as in WD; unknown pathological significance; no effect on copper transport activity;, features a modification of the amino acid from R to W at position 1041.
+The protein's natural variant, known as in WD; yeast complementation assays show that the variant does not rescue iron-uptake deficiency of yeast mutant ccc2;, features a modification of the amino acid from L to P at position 1043.
+The protein's natural variant, known as in WD; loss of copper transport activity; no effect on ATPase activity;, features a modification of the amino acid from P to L at position 1052.
+The protein's natural variant, known as in WD; unknown pathological significance, features a modification of the amino acid from A to V at position 1058.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from G to E at position 1061.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from A to V at position 1063.
+The protein's natural variant, known as in WD; does not bind ATP; the mutant is stable and is properly targeted to the TGN;, features a modification of the amino acid from E to A at position 1064.
+The protein's natural variant, known as in WD; loss of copper transport activity; loss of ATPase activity;, features a modification of the amino acid from E to K at position 1064.
+The protein's natural variant, known as in WD, features a modification of the amino acid from A to P at position 1065.
+The protein's natural variant, known as in WD; common mutation;, features a modification of the amino acid from E to G at position 1068.
+The protein's natural variant, known as in WD; common mutation; decreased copper transport activity; loss of ATPase activity; cannot form an acylphosphate intermediate during catalysis; does not alter the folding of the nucleotide-binding domain; decreased stability; does not localize to late endosomes;, features a modification of the amino acid from H to Q at position 1069.
+The protein's natural variant, known as in WD; unknown pathological significance;, features a modification of the amino acid from P to S at position 1070.
+The protein's natural variant, known as in WD; unknown pathological significance;, features a modification of the amino acid from A to V at position 1074.
+The protein's natural variant, known as in WD; decreased copper transport activity; no effect on ATPase activity; decreased localization to the TGN;, features a modification of the amino acid from L to F at position 1083.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from G to E at position 1089.
+The protein's natural variant, known as in WD, features a modification of the amino acid from G to V at position 1089.
+The protein's natural variant, known as in WD; unknown pathological significance;, features a modification of the amino acid from C to Y at position 1091.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from F to L at position 1094.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from Q to P at position 1095.
+The protein's natural variant, known as in WD, features a modification of the amino acid from P to R at position 1098.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from G to S at position 1099.
+The protein's natural variant, known as in WD; yeast complementation assays show that the variant does not rescue iron-uptake deficiency of yeast mutant ccc2;, features a modification of the amino acid from G to R at position 1101.
+The protein's natural variant, known as in WD; yeast complementation assays show that the variant intermediately rescue iron-uptake deficiency of yeast mutant ccc2;, features a modification of the amino acid from I to T at position 1102.
+The protein's natural variant, known as in WD, features a modification of the amino acid from C to F at position 1104.
+The protein's natural variant, known as in WD, features a modification of the amino acid from C to S at position 1104.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from C to Y at position 1104.
+The protein's natural variant, known as in WD; marked impairment in copper transport;, features a modification of the amino acid from V to D at position 1106.
+The protein's natural variant, known as in WD; unknown pathological significance;, features a modification of the amino acid from V to I at position 1106.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from G to D at position 1111.
+The protein's natural variant, known as in WD; unknown pathological significance, features a modification of the amino acid from L to M at position 1113.
+The protein's natural variant, known as in WD; unknown pathological significance, features a modification of the amino acid from E to K at position 1136.
+The protein's natural variant, known as no effect on copper transport activity;, features a modification of the amino acid from V to A at position 1140.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from Q to H at position 1142.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from V to M at position 1146.
+The protein's natural variant, known as in WD; yeast complementation assays show that the variant mildly rescue iron-uptake deficiency of yeast mutant ccc2;, features a modification of the amino acid from I to T at position 1148.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from G to A at position 1149.
+The protein's natural variant, known as in WD; unknown pathological significance, features a modification of the amino acid from G to E at position 1149.
+The protein's natural variant, known as in WD; yeast complementation assays show that the variant does not rescue iron-uptake deficiency of yeast mutant ccc2;, features a modification of the amino acid from R to C at position 1151.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from R to H at position 1151.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from W to C at position 1153.
+The protein's natural variant, known as in WD, features a modification of the amino acid from W to R at position 1153.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from D to N at position 1164.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from A to S at position 1168.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from M to T at position 1169.
+The protein's natural variant, known as in WD; moderate impairment in copper transport;, features a modification of the amino acid from M to V at position 1169.
+The protein's natural variant, known as in WD; yeast complementation assays show that the variant fully rescue iron-uptake deficiency of yeast mutant ccc2, features a modification of the amino acid from E to G at position 1173.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from E to K at position 1173.
+The protein's natural variant, known as in WD; yeast complementation assays show that the variant mildly rescue iron-uptake deficiency of yeast mutant ccc2;, features a modification of the amino acid from G to E at position 1176.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from G to R at position 1176.
+The protein's natural variant, known as in WD; unknown pathological significance;, features a modification of the amino acid from T to A at position 1178.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from A to G at position 1183.
+The protein's natural variant, known as in WD; unknown pathological significance; no effect on copper transport activity, features a modification of the amino acid from A to T at position 1183.
+The protein's natural variant, known as in WD, features a modification of the amino acid from G to C at position 1186.
+The protein's natural variant, known as in WD; unknown pathological significance; no effect on copper transport activity;, features a modification of the amino acid from G to S at position 1186.
+The protein's natural variant, known as in WD; unknown pathological significance, features a modification of the amino acid from A to G at position 1202.
+The protein's natural variant, known as in WD; loss of copper transport activity; no effect on ATPase activity;, features a modification of the amino acid from G to V at position 1213.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from V to M at position 1216.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from T to M at position 1220.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from G to E at position 1221.
+The protein's natural variant, known as in WD, features a modification of the amino acid from D to N at position 1222.
+The protein's natural variant, known as in WD; decreased copper transport activity; loss of ATPase activity, features a modification of the amino acid from D to V at position 1222.
+The protein's natural variant, known as in WD, features a modification of the amino acid from D to Y at position 1222.
+The protein's natural variant, known as in WD; yeast complementation assays show that the variant fully rescue iron-uptake deficiency of yeast mutant ccc2, features a modification of the amino acid from R to T at position 1228.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from I to V at position 1230.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from T to P at position 1232.
+The protein's natural variant, known as in WD; yeast complementation assays show that the variant does not rescue iron-uptake deficiency of yeast mutant ccc2;, features a modification of the amino acid from V to G at position 1239.
+The protein's natural variant, known as in WD, features a modification of the amino acid from P to T at position 1245.
+The protein's natural variant, known as in WD, features a modification of the amino acid from K to N at position 1248.
+The protein's natural variant, known as in WD; unknown pathological significance;, features a modification of the amino acid from A to G at position 1250.
+The protein's natural variant, known as in WD, features a modification of the amino acid from V to I at position 1252.
+The protein's natural variant, known as in WD, features a modification of the amino acid from L to I at position 1255.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from Q to R at position 1256.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from V to F at position 1262.
+The protein's natural variant, known as in WD; unknown pathological significance;, features a modification of the amino acid from G to E at position 1266.
+The protein's natural variant, known as in WD; common mutation;, features a modification of the amino acid from G to R at position 1266.
+The protein's natural variant, known as in WD; decreased copper transport activity; loss of ATPase activity, features a modification of the amino acid from G to V at position 1266.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from D to A at position 1267.
+The protein's natural variant, known as in WD; yeast complementation assays show that the variant does not rescue iron-uptake deficiency of yeast mutant ccc2, features a modification of the amino acid from D to V at position 1267.
+The protein's natural variant, known as in WD; unknown pathological significance;, features a modification of the amino acid from G to R at position 1268.
+The protein's natural variant, known as in WD; loss of copper transport activity; increased ATPase activity; does not affect localization to late endosomes;, features a modification of the amino acid from N to S at position 1270.
+The protein's natural variant, known as in WD, features a modification of the amino acid from D to N at position 1271.
+The protein's natural variant, known as in WD; decreased copper transport activity; increased ATPase activity;, features a modification of the amino acid from P to L at position 1273.
+The protein's natural variant, known as in WD; unknown pathological significance, features a modification of the amino acid from A to V at position 1278.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from D to G at position 1279.
+The protein's natural variant, known as in WD, features a modification of the amino acid from D to Y at position 1279.
+The protein's natural variant, known as in WD; unknown pathological significance;, features a modification of the amino acid from G to D at position 1281.
+The protein's natural variant, known as in WD; yeast complementation assays show that the variant mildly rescue iron-uptake deficiency of yeast mutant ccc2;, features a modification of the amino acid from G to S at position 1287.
+The protein's natural variant, known as in WD; unknown pathological significance;, features a modification of the amino acid from T to M at position 1288.
+The protein's natural variant, known as in WD; unknown pathological significance;, features a modification of the amino acid from E to K at position 1293.
+The protein's natural variant, known as in WD; yeast complementation assays show that the variant does not rescue iron-uptake deficiency of yeast mutant ccc2;, features a modification of the amino acid from A to D at position 1295.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from D to N at position 1296.
+The protein's natural variant, known as in WD; unknown pathological significance;, features a modification of the amino acid from V to I at position 1298.
+The protein's natural variant, known as in WD; unknown pathological significance, features a modification of the amino acid from V to L at position 1298.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from L to P at position 1305.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from S to R at position 1310.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from R to P at position 1322.
+The protein's natural variant, known as in WD, features a modification of the amino acid from L to V at position 1327.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from A to T at position 1328.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from Y to S at position 1331.
+The protein's natural variant, known as in WD, features a modification of the amino acid from N to D at position 1332.
+The protein's natural variant, known as in WD; unknown pathological significance, features a modification of the amino acid from N to K at position 1332.
+The protein's natural variant, known as in WD, features a modification of the amino acid from I to T at position 1336.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from G to D at position 1341.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from G to R at position 1341.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from G to S at position 1341.
+The protein's natural variant, known as in WD, features a modification of the amino acid from G to V at position 1341.
+The protein's natural variant, known as in WD; unknown pathological significance;, features a modification of the amino acid from G to S at position 1347.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from P to S at position 1352.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from W to R at position 1353.
+The protein's natural variant, known as in WD, features a modification of the amino acid from G to C at position 1355.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from G to S at position 1355.
+The protein's natural variant, known as in WD, features a modification of the amino acid from A to S at position 1358.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from M to I at position 1359.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from S to F at position 1363.
+The protein's natural variant, known as in WD;, features a modification of the amino acid from L to P at position 1368.
+The protein's natural variant, known as in WD; unknown pathological significance;, features a modification of the amino acid from S to L at position 1369.
+The protein's natural variant, known as in WD; increased protein degradation; the mutant has a diffuse cytoplasmic localization pattern and is absent from TGN under conditions of low-copper levels;, features a modification of the amino acid from L to P at position 1373.
+The protein's natural variant, known as in WD; increased protein degradation; the mutant has a diffuse cytoplasmic localization pattern and is absent from TGN under conditions of low-copper levels;, features a modification of the amino acid from L to R at position 1373.
+The protein's natural variant, known as in WD; unknown pathological significance; localized at the TGN as the wild-type under conditions of low-copper levels;, features a modification of the amino acid from C to S at position 1375.
+The protein's natural variant, known as in WD; unknown pathological significance; localized at the TGN as the wild-type under conditions of low-copper levels;, features a modification of the amino acid from P to S at position 1379.
+The protein's natural variant, known as in WD; unknown pathological significance, features a modification of the amino acid from S to Y at position 1431.
+The protein's natural variant, known as in WD; unknown pathological significance;, features a modification of the amino acid from S to F at position 1432.
+The protein's natural variant, known as in WD; unknown pathological significance; localized at the TGN as the wild-type under conditions of low-copper levels;, features a modification of the amino acid from T to M at position 1434.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from Q to R at position 2031.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from S to G at position 2063.
+The protein's natural variant, known as in strain: NC304, NC322, NC359, NC361, NC375 and NC399, features a modification of the amino acid from E to D at position 48.
+The protein's natural variant, known as in strain: NC304, NC322, NC359, NC361 and NC399, features a modification of the amino acid from A to V at position 136.
+The protein's natural variant, known as in strain: Canton-S, NC301, NC304, NC319, NC322, NC335, NC350, NC357, NC358, NC359, NC361, NC362, NC375 and NC399, features a modification of the amino acid from R to S at position 174.
+The protein's natural variant, known as in strain: NC335, features a modification of the amino acid from R to S at position 336.
+The protein's natural variant, known as in strain: Canton-S and SB2040, features a modification of the amino acid from H to P at position 553.
+The natural variant of this protein is characterized by an amino acid alteration from M to V at position 156.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from A to D at position 110.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from S to I at position 531.
+The protein's natural variant, known as in DYT6, features a modification of the amino acid from S to F at position 6.
+The protein's natural variant, known as in DYT6;, features a modification of the amino acid from S to P at position 6.
+The protein's natural variant, known as in DYT6, features a modification of the amino acid from A to D at position 7.
+The protein's natural variant, known as in DYT6, features a modification of the amino acid from Y to C at position 8.
+The protein's natural variant, known as in DYT6;, features a modification of the amino acid from G to C at position 9.
+The protein's natural variant, known as in DYT6, features a modification of the amino acid from N to K at position 12.
+The protein's natural variant, known as in DYT6, features a modification of the amino acid from R to H at position 13.
+The protein's natural variant, known as in DYT6; lower activity than wild-type, features a modification of the amino acid from K to E at position 16.
+The protein's natural variant, known as in DYT6;, features a modification of the amino acid from D to G at position 17.
+The protein's natural variant, known as in DYT6, features a modification of the amino acid from S to C at position 21.
+The protein's natural variant, known as in DYT6, features a modification of the amino acid from S to T at position 21.
+The protein's natural variant, known as in DYT6; lower activity than wild-type;, features a modification of the amino acid from H to P at position 23.
+The protein's natural variant, known as in DYT6; lower activity than wild-type;, features a modification of the amino acid from K to E at position 24.
+The protein's natural variant, known as in DYT6; lower activity than wild-type;, features a modification of the amino acid from P to L at position 26.
+The protein's natural variant, known as in DYT6, features a modification of the amino acid from P to R at position 26.
+The protein's natural variant, known as in DYT6, features a modification of the amino acid from R to P at position 29.
+The protein's natural variant, known as in DYT6;, features a modification of the amino acid from R to Q at position 29.
+The protein's natural variant, known as in DYT6, features a modification of the amino acid from P to R at position 30.
+The protein's natural variant, known as in DYT6; lower activity than wild-type, features a modification of the amino acid from L to H at position 32.
+The protein's natural variant, known as in DYT6, features a modification of the amino acid from A to T at position 39.
+The protein's natural variant, known as in DYT6, features a modification of the amino acid from C to F at position 54.
+The protein's natural variant, known as in DYT6, features a modification of the amino acid from E to G at position 56.
+The protein's natural variant, known as in DYT6, features a modification of the amino acid from H to N at position 57.
+The protein's natural variant, known as in DYT6, features a modification of the amino acid from T to I at position 59.
+The protein's natural variant, known as in DYT6, features a modification of the amino acid from L to R at position 72.
+The protein's natural variant, known as in DYT6, features a modification of the amino acid from N to I at position 75.
+The protein's natural variant, known as in DYT6; mild phenotype; does not affect activity;, features a modification of the amino acid from I to V at position 80.
+The protein's natural variant, known as in DYT6; affects DNA-binding;, features a modification of the amino acid from F to L at position 81.
+The protein's natural variant, known as in DYT6;, features a modification of the amino acid from C to R at position 83.
+The protein's natural variant, known as in DYT6;, features a modification of the amino acid from K to R at position 89.
+The protein's natural variant, known as in DYT6;, features a modification of the amino acid from F to S at position 132.
+The protein's natural variant, known as in DYT6, features a modification of the amino acid from N to K at position 136.
+The protein's natural variant, known as in DYT6;, features a modification of the amino acid from N to S at position 136.
+The protein's natural variant, known as in DYT6, features a modification of the amino acid from Y to C at position 137.
+The protein's natural variant, known as in DYT6; no effect on dimerization;, features a modification of the amino acid from M to V at position 143.
+The protein's natural variant, known as in DYT6; no effect on dimerization, features a modification of the amino acid from I to T at position 149.
+The protein's natural variant, known as in DYT6; no effect on dimerization, features a modification of the amino acid from H to P at position 150.
+The protein's natural variant, known as in DYT6; no effect on dimerization;, features a modification of the amino acid from A to T at position 166.
+The protein's natural variant, known as in DYT6; no effect on dimerization;, features a modification of the amino acid from R to Q at position 169.
+The protein's natural variant, known as in DYT6; no effect on dimerization, features a modification of the amino acid from C to R at position 170.
+The protein's natural variant, known as in DYT6; no effect on dimerization;, features a modification of the amino acid from E to G at position 174.
+The protein's natural variant, known as in DYT6; no effect on dimerization, features a modification of the amino acid from L to P at position 177.
+The protein's natural variant, known as in DYT6; no effect on dimerization, features a modification of the amino acid from L to S at position 180.
+The protein's natural variant, known as in DYT6, features a modification of the amino acid from Q to K at position 187.
+The protein's natural variant, known as in DYT6;, features a modification of the amino acid from D to N at position 192.
+The natural variant of this protein is characterized by an amino acid alteration from N to S at position 271.
+The protein's natural variant, known as in 1.0101, 1.0104/SIN1, 1.0106/SIN3 and 1.0108/SIN5, features a modification of the amino acid from R to G at position 6.
+The protein's natural variant, known as in 1.0103/SA2S2, features a modification of the amino acid from S to G at position 36.
+The protein's natural variant, known as in 1.0103/SA2S2, features a modification of the amino acid from W to L at position 40.
+The protein's natural variant, known as in 1.0103/SA2S2, features a modification of the amino acid from T to A at position 41.
+The protein's natural variant, known as in 1.0105/SIN2, features a modification of the amino acid from D to E at position 43.
+The protein's natural variant, known as in 1.0103/SA2S2, features a modification of the amino acid from D to Y at position 43.
+The protein's natural variant, known as in 1.0103/SA2S2 and 1.0105/SIN2, features a modification of the amino acid from D to G at position 44.
+The protein's natural variant, known as in 1.0108/SIN5, features a modification of the amino acid from R to K at position 61.
+The protein's natural variant, known as in 1.0101, 1.0103/SA2S2, 1.0104/SIN1, 1.0105/SIN2 and 1.0107/SIN4, features a modification of the amino acid from G to E at position 100.
+The protein's natural variant, known as in 1.0106/SIN3 and 1.0108/SIN5, features a modification of the amino acid from H to Q at position 108.
+The protein's natural variant, known as in 1.0106/SIN3 and 1.0108/SIN5, features a modification of the amino acid from L to V at position 109.
+The protein's natural variant, known as in 1.0103/SA2S2, features a modification of the amino acid from H to Q at position 111.
+The protein's natural variant, known as in 1.0104/SIN1, features a modification of the amino acid from K to R at position 125.
+The protein's natural variant, known as in 1.0101, 1.0105/SIN2, 1.0106/SIN3, 1.0107/SIN4 and 1.0108/SIN5, features a modification of the amino acid from R to P at position 130.
+The protein's natural variant, known as in 1.0104/SIN1, features a modification of the amino acid from K to Q at position 138.
+The protein's natural variant, known as in XDAT; severe impairment of ZFPM1 binding and erythroid differentiation in vitro;, features a modification of the amino acid from V to M at position 205.
+The protein's natural variant, known as in XDAT; partially disrupts the interaction with ZFPM1;, features a modification of the amino acid from G to S at position 208.
+The protein's natural variant, known as in XLTT; does not affect ZFPM1 binding; reduced affinity to palindromic GATA sites; supports erythroid maturation less efficiently than wild-type GATA1;, features a modification of the amino acid from R to Q at position 216.
+The protein's natural variant, known as in XDAT; partially disrupts the interaction with ZFPM1;, features a modification of the amino acid from D to G at position 218.
+The protein's natural variant, known as in XDAT; stronger loss of affinity than of G-218-GATA1 for ZFPM1 and disturbed GATA1 self-association;, features a modification of the amino acid from D to Y at position 218.
+The protein's natural variant, known as in HAEADA; altered transcriptional activity at canonical GATA1 target genes, affecting both silencing and activation of select genes necessary for effective terminal red cell production; may affect binding to specific genomic loci; partial loss of nuclear localization;, features a modification of the amino acid from R to C at position 307.
+The protein's natural variant, known as in HAEADA; altered transcriptional activity at canonical GATA1 target genes, affecting both silencing and activation of select genes necessary for effective terminal red cell production; partial loss of nuclear localization, features a modification of the amino acid from R to H at position 307.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from F to C at position 361.
+The protein's natural variant, known as found in a renal cell carcinoma sample; somatic mutation, features a modification of the amino acid from S to F at position 42.
+The protein's natural variant, known as in BMFS1; affects protein localization to ER;, features a modification of the amino acid from R to H at position 207.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from S to C at position 68.
+The protein's natural variant, known as associated with susceptibility to alcoholism;, features a modification of the amino acid from N to K at position 172.
+The protein's natural variant, known as in a patient with Parkinson disease;, features a modification of the amino acid from K to E at position 46.
+The protein's natural variant, known as in GD;, features a modification of the amino acid from V to L at position 54.
+The protein's natural variant, known as in GD; neuronopathic and perinatal lethal forms; loss of glucosylceramidase activity;, features a modification of the amino acid from C to S at position 55.
+The protein's natural variant, known as in GD1, features a modification of the amino acid from C to W at position 62.
+The protein's natural variant, known as in GD1; very low glucosylceramidase activity, features a modification of the amino acid from D to N at position 63.
+The protein's natural variant, known as in GD, features a modification of the amino acid from F to V at position 76.
+The protein's natural variant, known as in GD2, features a modification of the amino acid from E to K at position 80.
+The protein's natural variant, known as in GD;, features a modification of the amino acid from T to I at position 82.
+The protein's natural variant, known as in GD;, features a modification of the amino acid from G to E at position 85.
+The protein's natural variant, known as in GD; decreased glucosylceramidase activity; 20% of normal activity;, features a modification of the amino acid from R to Q at position 87.
+The protein's natural variant, known as in GD; mild;, features a modification of the amino acid from R to W at position 87.
+The protein's natural variant, known as in GD; mild; decreased glucosylceramidase activity; 8% of normal activity; increases susceptibility to proteolytic degradation;, features a modification of the amino acid from K to N at position 118.
+The protein's natural variant, known as in GD, features a modification of the amino acid from A to T at position 129.
+The protein's natural variant, known as in GD2;, features a modification of the amino acid from S to L at position 146.
+The protein's natural variant, known as in GD, features a modification of the amino acid from G to E at position 152.
+The protein's natural variant, known as in GD, features a modification of the amino acid from N to D at position 156.
+The protein's natural variant, known as in GD1; very low glucosylceramidase activity;, features a modification of the amino acid from I to S at position 158.
+The protein's natural variant, known as in GD;, features a modification of the amino acid from I to T at position 158.
+The protein's natural variant, known as in GD2; decreased glucosylceramidase activity; 13% of normal activity;, features a modification of the amino acid from R to Q at position 159.
+The protein's natural variant, known as in GD; severe;, features a modification of the amino acid from R to W at position 159.
+The protein's natural variant, known as in GD; decreased glucosylceramidase activity; 16% of normal activity;, features a modification of the amino acid from P to L at position 161.
+The protein's natural variant, known as in GD; mild;, features a modification of the amino acid from P to S at position 161.
+The protein's natural variant, known as in GD; loss of glucosylceramidase activity; increases susceptibility to proteolytic degradation;, features a modification of the amino acid from M to V at position 162.
+The protein's natural variant, known as in GD; decreased glucosylceramidase activity; 9% of normal activity; increases susceptibility to proteolytic degradation;, features a modification of the amino acid from D to V at position 166.
+The protein's natural variant, known as in GD1 and GD2; also found in a patient with Parkinson disease;, features a modification of the amino acid from R to C at position 170.
+The protein's natural variant, known as in GD;, features a modification of the amino acid from R to L at position 170.
+The protein's natural variant, known as in GD;, features a modification of the amino acid from T to I at position 173.
+The protein's natural variant, known as in GD;, features a modification of the amino acid from T to P at position 173.
+The protein's natural variant, known as in GD;, features a modification of the amino acid from A to E at position 175.
+The protein's natural variant, known as in GD; decreased glucosylceramide catabolic process;, features a modification of the amino acid from D to H at position 179.
+The protein's natural variant, known as in GD; severe; decreased protein abundance; decreased glucosylceramide catabolic process;, features a modification of the amino acid from K to Q at position 196.
+The protein's natural variant, known as in GD;, features a modification of the amino acid from P to L at position 198.
+The protein's natural variant, known as in GD1; decreased glucosylceramide catabolic process, features a modification of the amino acid from P to S at position 198.
+The protein's natural variant, known as in GD, features a modification of the amino acid from P to T at position 198.
+The protein's natural variant, known as in GD; decreased glucosylceramidase activity; 5% of normal activity;, features a modification of the amino acid from I to N at position 200.
+The protein's natural variant, known as in GD;, features a modification of the amino acid from I to S at position 200.
+The protein's natural variant, known as in GD;, features a modification of the amino acid from H to P at position 201.
+The protein's natural variant, known as in GD;, features a modification of the amino acid from R to C at position 209.
+The protein's natural variant, known as in GD;, features a modification of the amino acid from R to P at position 209.
+The protein's natural variant, known as in GD, decreased glucosylceramidase activity; 12% of normal activity;, features a modification of the amino acid from L to F at position 213.
+The protein's natural variant, known as in GD, features a modification of the amino acid from A to D at position 215.
+The protein's natural variant, known as in GD2, features a modification of the amino acid from P to S at position 217.
+The protein's natural variant, known as in GD1; very low glucosylceramidase activity;, features a modification of the amino acid from P to L at position 221.
+The protein's natural variant, known as in GD;, features a modification of the amino acid from P to T at position 221.
+The protein's natural variant, known as in GD; gene conversion;, features a modification of the amino acid from W to R at position 223.
+The protein's natural variant, known as in GD; decreased glucosylceramidase activity; 4% of normal activity; increases susceptibility to proteolytic degradation, features a modification of the amino acid from L to F at position 224.
+The protein's natural variant, known as in GD2; decreased glucosylceramide catabolic process, features a modification of the amino acid from N to I at position 227.
+The protein's natural variant, known as in GD; gene conversion;, features a modification of the amino acid from N to K at position 227.
+The protein's natural variant, known as in GD and GD3; decreased glucosylceramide catabolic process;, features a modification of the amino acid from N to S at position 227.
+The protein's natural variant, known as in GD;, features a modification of the amino acid from G to V at position 228.
+The protein's natural variant, known as in GD2;, features a modification of the amino acid from A to E at position 229.
+The protein's natural variant, known as in GD, features a modification of the amino acid from A to T at position 229.
+The protein's natural variant, known as in GD1; very low glucosylceramidase activity;, features a modification of the amino acid from V to E at position 230.
+The protein's natural variant, known as in GD1; gene conversion;, features a modification of the amino acid from V to G at position 230.
+The protein's natural variant, known as in GD; also found in a patient with Parkinson disease; decreased glucosylceramidase activity; 7% of normal activity;, features a modification of the amino acid from G to E at position 232.
+The protein's natural variant, known as in GD; severe;, features a modification of the amino acid from G to E at position 234.
+The protein's natural variant, known as in GD, features a modification of the amino acid from G to W at position 234.
+The protein's natural variant, known as in GD2; gene conversion;, features a modification of the amino acid from S to P at position 235.
+The protein's natural variant, known as in GD; severe; loss of glucosylceramidase activity; increases susceptibility to proteolytic degradation;, features a modification of the amino acid from K to E at position 237.
+The protein's natural variant, known as in GD;, features a modification of the amino acid from G to E at position 241.
+The protein's natural variant, known as in GD1 and GD2; gene conversion;, features a modification of the amino acid from G to R at position 241.
+The protein's natural variant, known as in GD;, features a modification of the amino acid from Y to C at position 244.
+The protein's natural variant, known as in GD;, features a modification of the amino acid from Y to H at position 251.
+The protein's natural variant, known as in GD2; gene conversion;, features a modification of the amino acid from F to I at position 252.
+The protein's natural variant, known as in GD; mild;, features a modification of the amino acid from F to Y at position 255.
+The protein's natural variant, known as in GD1, features a modification of the amino acid from F to L at position 266.
+The protein's natural variant, known as in GD;, features a modification of the amino acid from T to R at position 270.
+The protein's natural variant, known as in GD2; loss of glucosylceramide catabolic process, features a modification of the amino acid from E to K at position 274.
+The protein's natural variant, known as in GD, features a modification of the amino acid from S to P at position 276.
+The protein's natural variant, known as in GD1; loss of glucosylceramide catabolic process, features a modification of the amino acid from P to T at position 284.
+The protein's natural variant, known as in GD1;, features a modification of the amino acid from G to V at position 289.
+The protein's natural variant, known as in GDPL;, features a modification of the amino acid from F to L at position 290.
+The protein's natural variant, known as in GD1 and GD2;, features a modification of the amino acid from H to Q at position 294.
+The protein's natural variant, known as in GD2; also found in a patient with Parkinson disease;, features a modification of the amino acid from R to Q at position 296.
+The protein's natural variant, known as in GD2; decreased glucosylceramidase activity; 4% of normal activity, features a modification of the amino acid from F to L at position 298.
+The protein's natural variant, known as in GD1, features a modification of the amino acid from R to G at position 301.
+The protein's natural variant, known as in GD; decreased glucosylceramidase activity; 5% of normal activity;, features a modification of the amino acid from L to I at position 303.
+The protein's natural variant, known as in GD;, features a modification of the amino acid from G to D at position 304.
+The protein's natural variant, known as in GD3; loss of glucosylceramide catabolic process, features a modification of the amino acid from G to R at position 304.
+The protein's natural variant, known as in GD; mild;, features a modification of the amino acid from P to R at position 305.
+The protein's natural variant, known as in GD; decreased glucosylceramidase activity; less than 5% of normal activity;, features a modification of the amino acid from S to N at position 310.
+The protein's natural variant, known as in GD1;, features a modification of the amino acid from R to C at position 324.
+The protein's natural variant, known as in GD2;, features a modification of the amino acid from R to H at position 324.
+The protein's natural variant, known as in GD; mild;, features a modification of the amino acid from P to L at position 328.
+The protein's natural variant, known as in GD;, features a modification of the amino acid from K to I at position 342.
+The protein's natural variant, known as in GD2; decreased glucosylceramidase activity; 16% of normal activity; increases susceptibility to proteolytic degradation;, features a modification of the amino acid from Y to C at position 343.
+The protein's natural variant, known as in GD1, features a modification of the amino acid from I to S at position 347.
+The protein's natural variant, known as in GD;, features a modification of the amino acid from A to V at position 348.
+The protein's natural variant, known as in GDPL;, features a modification of the amino acid from H to R at position 350.
+The protein's natural variant, known as in GD; mild;, features a modification of the amino acid from W to C at position 351.
+The protein's natural variant, known as in GD1; loss of glucosylceramide catabolic process;, features a modification of the amino acid from W to S at position 351.
+The protein's natural variant, known as in GD, features a modification of the amino acid from Y to H at position 352.
+The protein's natural variant, known as in GD;, features a modification of the amino acid from D to H at position 354.
+The protein's natural variant, known as in GD;, features a modification of the amino acid from A to D at position 357.
+The protein's natural variant, known as in GD; decreased glucosylceramidase activity; 6% of normal activity;, features a modification of the amino acid from T to I at position 362.
+The protein's natural variant, known as in GD; unknown pathological significance;, features a modification of the amino acid from L to P at position 363.
+The protein's natural variant, known as in GD2;, features a modification of the amino acid from G to R at position 364.
+The protein's natural variant, known as in GD and GD1; mild; decreased glucosylceramidase activity; 42% of normal activity;, features a modification of the amino acid from E to K at position 365.
+The protein's natural variant, known as in GD;, features a modification of the amino acid from A to T at position 380.
+The protein's natural variant, known as in GD2; loss of glucosylceramidase activity;, features a modification of the amino acid from C to G at position 381.
+The protein's natural variant, known as in GD; decreased glucosylceramidase activity; 12% of normal activity;, features a modification of the amino acid from E to K at position 388.
+The protein's natural variant, known as in GD;, features a modification of the amino acid from V to L at position 391.
+The protein's natural variant, known as in GD;, features a modification of the amino acid from R to G at position 392.
+The protein's natural variant, known as in GD; decreased glucosylceramidase activity; 5% of normal activity;, features a modification of the amino acid from R to W at position 392.
+The protein's natural variant, known as in GD; mild;, features a modification of the amino acid from R to Q at position 398.
+The protein's natural variant, known as in GD;, features a modification of the amino acid from M to I at position 400.
+The protein's natural variant, known as in GD; decreased glucosylceramidase activity; 8% of normal activity; increases susceptibility to proteolytic degradation;, features a modification of the amino acid from Y to C at position 402.
+The protein's natural variant, known as in GD; mild;, features a modification of the amino acid from S to T at position 403.
+The protein's natural variant, known as in GD, features a modification of the amino acid from S to G at position 405.
+The protein's natural variant, known as in GD;, features a modification of the amino acid from S to N at position 405.
+The protein's natural variant, known as in GD1; loss of glucosylceramide catabolic process;, features a modification of the amino acid from S to R at position 405.
+The protein's natural variant, known as in GD;, features a modification of the amino acid from T to M at position 408.
+The protein's natural variant, known as in GD1; mild; common mutation; associated with susceptibility to Parkinson disease; increased proteasomal degradation; decreased protein abundance; decreased glucosylceramide catabolic process; no effect on glucosylceramidase activity; alters interaction with saposin-C;, features a modification of the amino acid from N to S at position 409.
+The protein's natural variant, known as in GD; decreased glucosylceramidase activity; 15% of normal activity; increases susceptibility to proteolytic degradation;, features a modification of the amino acid from L to V at position 410.
+The protein's natural variant, known as in GD; mild;, features a modification of the amino acid from V to L at position 414.
+The protein's natural variant, known as in GD; mild;, features a modification of the amino acid from G to S at position 416.
+The protein's natural variant, known as in GD;, features a modification of the amino acid from W to G at position 417.
+The protein's natural variant, known as in GD2; also found in a patient with Parkinson disease;, features a modification of the amino acid from D to A at position 419.
+The protein's natural variant, known as in GD; decreased glucosylceramidase activity; 4% of normal activity, features a modification of the amino acid from D to H at position 419.
+The protein's natural variant, known as in GD and GD1; loss of glucosylceramide catabolic process, features a modification of the amino acid from D to N at position 419.
+The protein's natural variant, known as in GD1; loss of glucosylceramide catabolic process, features a modification of the amino acid from W to C at position 420.
+The protein's natural variant, known as in GD; decreased glucosylceramidase activity; 22% of normal activity, features a modification of the amino acid from N to K at position 421.
+The protein's natural variant, known as in GD;, features a modification of the amino acid from P to L at position 426.
+The protein's natural variant, known as in GD2, features a modification of the amino acid from G to E at position 428.
+The protein's natural variant, known as in GD; decreased glucosylceramidase activity; 17% of normal activity, features a modification of the amino acid from G to R at position 429.
+The protein's natural variant, known as in GD;, features a modification of the amino acid from P to L at position 430.
+The protein's natural variant, known as in GD2;, features a modification of the amino acid from N to I at position 431.
+The protein's natural variant, known as in GD, features a modification of the amino acid from W to R at position 432.
+The protein's natural variant, known as in GD; severe; decreased glucosylceramidase activity; 12% of normal activity;, features a modification of the amino acid from V to L at position 433.
+The protein's natural variant, known as in GD1; mild;, features a modification of the amino acid from N to T at position 435.
+The protein's natural variant, known as in GD; decreased glucosylceramidase activity; 6% of normal activity; alters protein stability and increases susceptibility to proteolytic degradation;, features a modification of the amino acid from F to S at position 436.
+The protein's natural variant, known as in GDPL;, features a modification of the amino acid from V to F at position 437.
+The protein's natural variant, known as in GD3;, features a modification of the amino acid from V to L at position 437.
+The protein's natural variant, known as in GD1 and GD2; decreased glucosylceramidase activity; 14% of normal activity; increases susceptibility to proteolytic degradation;, features a modification of the amino acid from D to N at position 438.
+The protein's natural variant, known as in GD, features a modification of the amino acid from D to Y at position 438.
+The protein's natural variant, known as in GD1;, features a modification of the amino acid from P to L at position 440.
+The protein's natural variant, known as in GD3, features a modification of the amino acid from I to F at position 441.
+The protein's natural variant, known as in GD; mild;, features a modification of the amino acid from I to T at position 441.
+The protein's natural variant, known as in GD1 and GD3C; at homozygosity it causes GD3C; also found in a patient with Parkinson disease; gene conversion; very low glucosylceramidase activity; alters protein stability;, features a modification of the amino acid from D to H at position 448.
+The protein's natural variant, known as in GD; severe; very low activity; alters protein stability;, features a modification of the amino acid from D to V at position 448.
+The protein's natural variant, known as in GD;, features a modification of the amino acid from F to I at position 450.
+The protein's natural variant, known as in GD, features a modification of the amino acid from Y to H at position 451.
+The protein's natural variant, known as in GD, features a modification of the amino acid from K to Q at position 452.
+The protein's natural variant, known as in GD2;, features a modification of the amino acid from P to R at position 454.
+The protein's natural variant, known as in GD; loss of glucosylceramidase activity; increases susceptibility to proteolytic degradation, features a modification of the amino acid from M to V at position 455.
+The protein's natural variant, known as in GD, features a modification of the amino acid from F to V at position 456.
+The protein's natural variant, known as in GD;, features a modification of the amino acid from Y to C at position 457.
+The protein's natural variant, known as in GD1; associated with R-490; loss of glucosylceramidase activity, features a modification of the amino acid from G to D at position 460.
+The protein's natural variant, known as in GD; severe, features a modification of the amino acid from K to E at position 464.
+The protein's natural variant, known as in a patient with Parkinson disease;, features a modification of the amino acid from D to N at position 482.
+The protein's natural variant, known as in GD1 and GD2; common mutation; associated with susceptibility to Parkinson disease; gene conversion; alters protein stability; increased proteasomal degradation; decreased protein abundance; very low glucosylceramide catabolic process; no effect on glucosylceramidase activity;, features a modification of the amino acid from L to P at position 483.
+The protein's natural variant, known as in GD; severe;, features a modification of the amino acid from L to R at position 483.
+The protein's natural variant, known as in GD, features a modification of the amino acid from A to P at position 485.
+The protein's natural variant, known as in GD1, features a modification of the amino acid from V to E at position 486.
+The protein's natural variant, known as in GD1; associated with D-460;, features a modification of the amino acid from H to R at position 490.
+The protein's natural variant, known as in GD; gene conversion;, features a modification of the amino acid from A to P at position 495.
+The natural variant of this protein is characterized by an amino acid alteration from V to L at position 497.
+The protein's natural variant, known as in GD; decreased glucosylceramidase activity; 10% of normal activity; increases susceptibility to proteolytic degradation;, features a modification of the amino acid from L to P at position 500.
+The protein's natural variant, known as in GD2, features a modification of the amino acid from N to K at position 501.
+The protein's natural variant, known as in GD; also found in patients with Parkinson disease; no effect on protein abundance; decreased glucosylceramidase activity; 37% of normal activity;, features a modification of the amino acid from R to C at position 502.
+The protein's natural variant, known as in GD; loss of glucosylceramidase activity; increases susceptibility to proteolytic degradation, features a modification of the amino acid from R to P at position 502.
+The natural variant of this protein is characterized by an amino acid alteration from L to P at position 509.
+The protein's natural variant, known as in GD2, features a modification of the amino acid from D to Y at position 513.
+The protein's natural variant, known as in GD;, features a modification of the amino acid from G to S at position 517.
+The protein's natural variant, known as in GD3;, features a modification of the amino acid from T to I at position 530.
+The protein's natural variant, known as in GD; mild;, features a modification of the amino acid from R to C at position 535.
+The protein's natural variant, known as in GD; mild;, features a modification of the amino acid from R to H at position 535.
+The protein's natural variant, known as in strain: St_L028 and St_L033, features a modification of the amino acid from P to L at position 1256.
+The protein's natural variant, known as in strain: In_L019, features a modification of the amino acid from A to S at position 1322.
+The protein's natural variant, known as in strain: In_L019, features a modification of the amino acid from S to N at position 1503.
+The protein's natural variant, known as in USH1J and DFNB48; decreases interaction with TMC1 and TMC2;, features a modification of the amino acid from E to D at position 64.
+The protein's natural variant, known as in DFNB48; unknown pathological significance; decreases interaction with TMC1 and TMC2; no loss of localization to stereocilia; does not affect ATP-induced calcium release;, features a modification of the amino acid from R to W at position 66.
+The protein's natural variant, known as found in a family with deafness carrying a likely pathogenic mutation in PDZD7; unknown pathological significance;, features a modification of the amino acid from V to M at position 75.
+The protein's natural variant, known as in DFNB48; decreases interaction with TMC1 and TMC2; no loss of localization to stereocilia; does not affect ATP-induced calcium release;;, features a modification of the amino acid from F to S at position 91.
+The protein's natural variant, known as in DFNB48; inhibits the ability to decrease ATP-induced calcium release; decreases interaction with TMC1 and TMC2;, features a modification of the amino acid from C to W at position 99.
+The protein's natural variant, known as in DFNB48; stimulates the ability to decrease ATP-induced calcium release; decreases interaction with TMC1 and TMC2;, features a modification of the amino acid from I to T at position 123.
+The protein's natural variant, known as in DFNB48; inhibits the ability to decrease ATP-induced calcium release; ; decreases interaction with TMC1 and TMC2; does not affect the localization in the cuticular plate or to the tip of stereocilia; does not affect binding with WHRN;, features a modification of the amino acid from R to W at position 186.
+The protein's natural variant, known as in protein A', features a modification of the amino acid from P to Q at position 72.
+The protein's natural variant, known as in MO2.2, features a modification of the amino acid from D to A at position 8.
+The protein's natural variant, known as in HYDM1; unknown pathological significance;, features a modification of the amino acid from Q to R at position 310.
+The protein's natural variant, known as in HYDM1; unknown pathological significance;, features a modification of the amino acid from L to I at position 311.
+The protein's natural variant, known as in HYDM1; unknown pathological significance;, features a modification of the amino acid from V to I at position 319.
+The protein's natural variant, known as in HYDM1; unknown pathological significance;, features a modification of the amino acid from K to N at position 379.
+The protein's natural variant, known as in HYDM1;, features a modification of the amino acid from L to R at position 398.
+The protein's natural variant, known as in HYDM1; unknown pathological significance;, features a modification of the amino acid from A to T at position 481.
+The protein's natural variant, known as in HYDM1; unknown pathological significance;, features a modification of the amino acid from K to R at position 511.
+The protein's natural variant, known as in HYDM1;, features a modification of the amino acid from P to S at position 651.
+The protein's natural variant, known as in HYDM1;, features a modification of the amino acid from R to P at position 693.
+The protein's natural variant, known as in HYDM1;, features a modification of the amino acid from R to Q at position 693.
+The protein's natural variant, known as in HYDM1;, features a modification of the amino acid from R to W at position 693.
+The protein's natural variant, known as in HYDM1;, features a modification of the amino acid from P to A at position 716.
+The protein's natural variant, known as in HYDM1; unknown pathological significance;, features a modification of the amino acid from A to V at position 719.
+The protein's natural variant, known as in HYDM1;, features a modification of the amino acid from R to W at position 721.
+The protein's natural variant, known as in HYDM1;, features a modification of the amino acid from C to Y at position 761.
+The protein's natural variant, known as in HYDM1; unknown pathological significance, features a modification of the amino acid from N to T at position 799.
+The protein's natural variant, known as in HYDM1;, features a modification of the amino acid from N to S at position 913.
+The protein's natural variant, known as in DSMA5;, features a modification of the amino acid from Y to C at position 5.
+The protein's natural variant, known as in strain: 85P, features a modification of the amino acid from A to T at position 155.
+The protein's natural variant, known as in strain: 85P, features a modification of the amino acid from A to E at position 182.
+The protein's natural variant, known as in strain: 85P, features a modification of the amino acid from AQ to GA at position 191.
+The protein's natural variant, known as in strain: 85P, features a modification of the amino acid from A to T at position 335.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from Q to E at position 159.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from H to P at position 360.
+The protein's natural variant, known as in pdxH null mutation suppressor, features a modification of the amino acid from G to S at position 194.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from R to Q at position 537.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from Q to E at position 31.
+The protein's natural variant, known as in SPGF67; unknown pathological significance, features a modification of the amino acid from H to Y at position 283.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to W at position 511.
+The protein's natural variant, known as in strain: cv. Q903; susceptibility to pathogens, features a modification of the amino acid from M to V at position 190.
+The protein's natural variant, known as in strain: cv. Q903; susceptibility to pathogens, features a modification of the amino acid from V to E at position 473.
+The protein's natural variant, known as may increase susceptibility for developing pheochromocytoma, paraganglioma, intestinal carcinoid tumor and breast, renal and uterus carcinoma; associated with increased manganese superoxide dismutase expression; associated with increased reactive oxygen species; associated with 1.9-fold increase in both AKT and MAPK expression;, features a modification of the amino acid from G to S at position 12.
+The protein's natural variant, known as may increase susceptibility for developing paraganglioma, breast and thyroid carcinoma; may be involved in somatic Merkel cell carcinoma; associated with increased manganese superoxide dismutase expression; associated with increased reactive oxygen species; associated with a 2.0-fold increase in AKT expression and a 1.7-fold increase in MAPK expression;, features a modification of the amino acid from H to R at position 50.
+The protein's natural variant, known as in MC2DN3; results in impaired mitochondrial complex II assembly; results in impaired cellular respiration;, features a modification of the amino acid from E to K at position 69.
+The protein's natural variant, known as in PGL1 and pheochromocytoma;, features a modification of the amino acid from P to L at position 81.
+The protein's natural variant, known as in MC2DN3; results in highly reduced protein expression; results in impaired cellular respiration;, features a modification of the amino acid from D to G at position 92.
+The protein's natural variant, known as in PGL1 and pheochromocytoma;, features a modification of the amino acid from D to Y at position 92.
+The protein's natural variant, known as in PGL1;, features a modification of the amino acid from H to L at position 102.
+The protein's natural variant, known as in PGL1;, features a modification of the amino acid from Y to C at position 114.
+The protein's natural variant, known as in PGL1;, features a modification of the amino acid from L to P at position 139.
+The protein's natural variant, known as found in an individual with features of Cowden syndrome; unknown pathological significance; associated with increased manganese superoxide dismutase expression; associated with normal reactive oxygen species; associated with no change in AKT expression but a 1.2-fold increase of MAPK expression;, features a modification of the amino acid from H to N at position 145.
+The protein's natural variant, known as in PGL1;, features a modification of the amino acid from G to V at position 148.
+The protein's natural variant, known as in SPG26;, features a modification of the amino acid from R to C at position 300.
+The protein's natural variant, known as in SPG26;, features a modification of the amino acid from D to A at position 433.
+The protein's natural variant, known as in strain: SARC9 / s3015, features a modification of the amino acid from S to L at position 55.
+The protein's natural variant, known as in strain: SARC9 / s3015, features a modification of the amino acid from I to R at position 97.
+The protein's natural variant, known as in strain: SARC9 / s3015, features a modification of the amino acid from S to C at position 182.
+The protein's natural variant, known as in allele 6A and allele 6A(5);, features a modification of the amino acid from V to A at position 19.
+The protein's natural variant, known as in allele 6A(2);, features a modification of the amino acid from L to V at position 50.
+The protein's natural variant, known as in ILD1; impaired secretion, features a modification of the amino acid from V to M at position 178.
+The protein's natural variant, known as in ILD1, features a modification of the amino acid from Y to H at position 208.
+The protein's natural variant, known as in ILD1; impaired secretion, features a modification of the amino acid from W to R at position 211.
+The protein's natural variant, known as may be associated with susceptibility to idiopathic pulmonary fibrosis in smokers; allele 6A(4) and allele 6A(5); does not affect secretion;, features a modification of the amino acid from R to W at position 219.
+The protein's natural variant, known as in ILD1; unknown pathological significance; impaired secretion, features a modification of the amino acid from V to M at position 225.
+The protein's natural variant, known as in endotoxin nonresponder, features a modification of the amino acid from C to Y at position 95.
+The natural variant of this protein is characterized by an amino acid alteration from A to T at position 120.
+The protein's natural variant, known as in CHNG6; no effect on T3 binding; no effect on thyroid hormone-dependent transcriptional activation;, features a modification of the amino acid from A to V at position 263.
+The protein's natural variant, known as in CHNG6; atypical phenotype; weak reduction in transcriptional activation, features a modification of the amino acid from N to Y at position 359.
+The protein's natural variant, known as in strain: cv. Cvi-0, features a modification of the amino acid from V to I at position 90.
+The protein's natural variant, known as in strain: cv. Cvi-0 and cv. Landsberg erecta, features a modification of the amino acid from Q to E at position 210.
+The protein's natural variant, known as in strain: cv. Cvi-0 and cv. Landsberg erecta, features a modification of the amino acid from DA to ES at position 268.
+The protein's natural variant, known as in strain: cv. Cvi-0 and cv. Landsberg erecta, features a modification of the amino acid from N to K at position 329.
+The protein's natural variant, known as in strain: cv. Goe-0, features a modification of the amino acid from V to I at position 6.
+The protein's natural variant, known as in SRXY7;, features a modification of the amino acid from L to P at position 162.
+The protein's natural variant, known as in GDMN; unknown pathological significance; Reduces cleavage efficiency in in vitro time course;, features a modification of the amino acid from E to K at position 212.
+The protein's natural variant, known as in T2D; risk factor;, features a modification of the amino acid from S to N at position 59.
+The protein's natural variant, known as in clone P-beta-1, features a modification of the amino acid from G to GE at position 172.
+The protein's natural variant, known as in ALKUS, features a modification of the amino acid from H to R at position 208.
+The protein's natural variant, known as in strain: cv. Cvi-1, cv. Fe-1a, cv. Nd-1 and cv. Wei-0, features a modification of the amino acid from K to T at position 3.
+The protein's natural variant, known as in strain: cv. Cvi-1, cv. Fe-1a, cv. Nd-1 and cv. Wei-0, features a modification of the amino acid from A to V at position 6.
+The protein's natural variant, known as in strain: cv. Cvi-1, cv. Fe-1a, cv. Nd-1 and cv. Wei-0, features a modification of the amino acid from I to T at position 14.
+The protein's natural variant, known as in strain: cv. Cvi-1, cv. Fe-1a, cv. Nd-1 and cv. Wei-0, features a modification of the amino acid from K to N at position 77.
+The protein's natural variant, known as in strain: cv. Cvi-1, cv. Fe-1a, cv. Nd-1 and cv. Wei-0, features a modification of the amino acid from N to K at position 87.
+The protein's natural variant, known as in strain: Globigii, features a modification of the amino acid from F to L at position 17.
+The protein's natural variant, known as in strain: Globigii, features a modification of the amino acid from G to S at position 44.
+The natural variant of this protein is characterized by an amino acid alteration from A to S at position 46.
+The protein's natural variant, known as in a bladder carcinoma NOS sample; somatic mutation, features a modification of the amino acid from H to Q at position 611.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation, features a modification of the amino acid from S to F at position 1035.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation, features a modification of the amino acid from P to L at position 1145.
+The protein's natural variant, known as in strain: Isolate MR-M981, features a modification of the amino acid from T to I at position 2.
+The protein's natural variant, known as in strain: Isolate MR-M981, features a modification of the amino acid from S to N at position 16.
+The protein's natural variant, known as in strain: Isolate MR-M981, features a modification of the amino acid from I to T at position 189.
+The protein's natural variant, known as in strain: Isolate MR-M981, features a modification of the amino acid from I to V at position 295.
+The protein's natural variant, known as in strain: Isolate MR-M981, features a modification of the amino acid from A to T at position 334.
+The protein's natural variant, known as in OCA3;, features a modification of the amino acid from A to T at position 24.
+The protein's natural variant, known as associated with blond hair in individuals from the Solomon Islands; rare or absent outside of Oceania;, features a modification of the amino acid from R to C at position 93.
+The protein's natural variant, known as in OCA3;, features a modification of the amino acid from R to Q at position 356.
+The protein's natural variant, known as in DEE38; loss of protein stability; yeast complementation assays show that the variant does partially rescue cell growth;, features a modification of the amino acid from G to R at position 189.
+The protein's natural variant, known as in VMD5;, features a modification of the amino acid from F to L at position 124.
+The protein's natural variant, known as found in a patient with vitelliform macular dystrophy; unknown pathological significance;, features a modification of the amino acid from A to P at position 243.
+The protein's natural variant, known as found in a patient with retinitis pigmentosa; unknown pathological significance, features a modification of the amino acid from S to P at position 379.
+The protein's natural variant, known as found in a patient with vitelliform macular dystrophy; unknown pathological significance, features a modification of the amino acid from G to D at position 1008.
+The protein's natural variant, known as found in a patient with VMD5; unknown pathological significance, features a modification of the amino acid from F to S at position 1016.
+The protein's natural variant, known as found in a patient with vitelliform macular dystophy; unknown pathological significance, features a modification of the amino acid from Y to C at position 1042.
+The protein's natural variant, known as in VMD5;, features a modification of the amino acid from C to F at position 1077.
+The protein's natural variant, known as probable disease-associated variant found in a patient with non-specific intellectual disability syndrome, features a modification of the amino acid from H to N at position 484.
+The protein's natural variant, known as probable disease-associated variant found in a patient with non-specific intellectual disability syndrome, features a modification of the amino acid from N to K at position 486.
+The protein's natural variant, known as in BIS, features a modification of the amino acid from R to Q at position 505.
+The protein's natural variant, known as in BIS, features a modification of the amino acid from G to V at position 513.
+The protein's natural variant, known as in BIS, features a modification of the amino acid from R to C at position 525.
+The protein's natural variant, known as in BIS, features a modification of the amino acid from R to H at position 525.
+The protein's natural variant, known as in BIS, features a modification of the amino acid from L to V at position 529.
+The protein's natural variant, known as in BIS, features a modification of the amino acid from D to N at position 534.
+The protein's natural variant, known as probable disease-associated variant found in a patient with non-specific intellectual disability syndrome, features a modification of the amino acid from L to P at position 719.
+The protein's natural variant, known as in NCBRS;, features a modification of the amino acid from G to A at position 752.
+The protein's natural variant, known as in NCBRS;, features a modification of the amino acid from K to R at position 755.
+The protein's natural variant, known as in NCBRS;, features a modification of the amino acid from T to I at position 756.
+The protein's natural variant, known as in NCBRS;, features a modification of the amino acid from D to H at position 851.
+The protein's natural variant, known as in NCBRS;, features a modification of the amino acid from E to D at position 852.
+The protein's natural variant, known as in NCBRS;, features a modification of the amino acid from E to K at position 852.
+The protein's natural variant, known as in NCBRS, features a modification of the amino acid from H to N at position 854.
+The protein's natural variant, known as in NCBRS;, features a modification of the amino acid from H to R at position 854.
+The protein's natural variant, known as in NCBRS;, features a modification of the amino acid from R to G at position 855.
+The protein's natural variant, known as in NCBRS;, features a modification of the amino acid from R to Q at position 855.
+The protein's natural variant, known as in NCBRS, features a modification of the amino acid from T to I at position 880.
+The protein's natural variant, known as in NCBRS;, features a modification of the amino acid from G to R at position 881.
+The protein's natural variant, known as in NCBRS;, features a modification of the amino acid from G to V at position 881.
+The protein's natural variant, known as in NCBRS;, features a modification of the amino acid from P to L at position 883.
+The protein's natural variant, known as in BIS, features a modification of the amino acid from E to V at position 929.
+The protein's natural variant, known as probable disease-associated variant found in a patient with non-specific intellectual disability syndrome, features a modification of the amino acid from I to T at position 932.
+The protein's natural variant, known as in BIS, features a modification of the amino acid from R to C at position 937.
+The protein's natural variant, known as in BIS, features a modification of the amino acid from R to H at position 937.
+The protein's natural variant, known as in BIS, features a modification of the amino acid from R to L at position 937.
+The protein's natural variant, known as in NCBRS;, features a modification of the amino acid from H to Y at position 939.
+The protein's natural variant, known as in NCBRS;, features a modification of the amino acid from L to F at position 946.
+The protein's natural variant, known as in NCBRS;, features a modification of the amino acid from L to S at position 946.
+The protein's natural variant, known as probable disease-associated variant found in a patient with non-specific intellectual disability syndrome, features a modification of the amino acid from K to E at position 1014.
+The protein's natural variant, known as in NCBRS;, features a modification of the amino acid from R to C at position 1105.
+The protein's natural variant, known as in NCBRS;, features a modification of the amino acid from R to P at position 1105.
+The protein's natural variant, known as in NCBRS;, features a modification of the amino acid from L to P at position 1135.
+The protein's natural variant, known as in NCBRS;, features a modification of the amino acid from S to R at position 1146.
+The protein's natural variant, known as in NCBRS;, features a modification of the amino acid from D to V at position 1158.
+The protein's natural variant, known as in NCBRS;, features a modification of the amino acid from R to G at position 1159.
+The protein's natural variant, known as in NCBRS;, features a modification of the amino acid from R to L at position 1159.
+The protein's natural variant, known as in NCBRS;, features a modification of the amino acid from R to Q at position 1159.
+The protein's natural variant, known as in NCBRS;, features a modification of the amino acid from R to H at position 1162.
+The protein's natural variant, known as in NCBRS;, features a modification of the amino acid from A to P at position 1188.
+The protein's natural variant, known as in NCBRS;, features a modification of the amino acid from A to V at position 1201.
+The protein's natural variant, known as in NCBRS;, features a modification of the amino acid from G to C at position 1202.
+The protein's natural variant, known as in NCBRS;, features a modification of the amino acid from D to G at position 1205.
+The protein's natural variant, known as in NCBRS;, features a modification of the amino acid from R to W at position 1213.
+The protein's natural variant, known as in NCBRS, features a modification of the amino acid from Q to E at position 1241.
+The protein's natural variant, known as associated with schizophrenia in some populations; results in reduced localization to the nucleus; decreased interaction with chromatin;, features a modification of the amino acid from D to E at position 1546.
+The protein's natural variant, known as in a glioblastoma multiforme sample; somatic mutation;, features a modification of the amino acid from S to F at position 280.
+The natural variant of this protein is characterized by an amino acid alteration from L to P at position 70.
+The natural variant of this protein is characterized by an amino acid alteration from I to F at position 24.
+The protein's natural variant, known as in strain: 2CPA51, features a modification of the amino acid from A to T at position 19.
+The protein's natural variant, known as in strain: 2CPA51, features a modification of the amino acid from H to R at position 29.
+The protein's natural variant, known as in clone B2, features a modification of the amino acid from C to S at position 40.
+The protein's natural variant, known as in clone B3, features a modification of the amino acid from SSD to CTN at position 43.
+The protein's natural variant, known as in CDAN1A;, features a modification of the amino acid from N to S at position 599.
+The protein's natural variant, known as in CDAN1A;, features a modification of the amino acid from P to L at position 672.
+The protein's natural variant, known as in CDAN1A, features a modification of the amino acid from E to K at position 698.
+The protein's natural variant, known as in CDAN1A; partially disrupts ASF1 binding and loss the ability to arrest cells in S phase and inhibit DNA synthesis;, features a modification of the amino acid from R to W at position 714.
+The protein's natural variant, known as in CDAN1A;, features a modification of the amino acid from F to I at position 868.
+The protein's natural variant, known as in CDAN1A;, features a modification of the amino acid from V to M at position 869.
+The protein's natural variant, known as in CDAN1A; partially disrupts ASF1 binding;, features a modification of the amino acid from R to W at position 1042.
+The protein's natural variant, known as in CDAN1A;, features a modification of the amino acid from D to V at position 1043.
+The protein's natural variant, known as in CDAN1A;, features a modification of the amino acid from P to L at position 1130.
+The protein's natural variant, known as in mil; allele m93; lack of S1P-mediated signaling, features a modification of the amino acid from R to H at position 150.
+The protein's natural variant, known as in mil; allele te273; lack of S1P-mediated signaling, features a modification of the amino acid from R to C at position 167.
+The protein's natural variant, known as in OI10;, features a modification of the amino acid from L to P at position 78.
+The protein's natural variant, known as in MC4DN13; mistargeted to the mitochondrial matrix; loss of interaction with SCO2 and MT-CO2;, features a modification of the amino acid from W to C at position 59.
+The protein's natural variant, known as in MC4DN13;, features a modification of the amino acid from W to R at position 66.
+The protein's natural variant, known as in CAFDADD; no significant effect on phosphorylation of MAPK1 and/or MAPK3;, features a modification of the amino acid from K to E at position 346.
+The protein's natural variant, known as in CAFDADD; decreased phosphorylation of MAPK1 and/or MAPK3;, features a modification of the amino acid from R to G at position 371.
+The protein's natural variant, known as in CAFDADD; decreased phosphorylation of MAPK1 and/or MAPK3;, features a modification of the amino acid from T to A at position 601.
+The protein's natural variant, known as in CAFDADD; decreased phosphorylation of MAPK1 and/or MAPK3;, features a modification of the amino acid from R to Q at position 655.
+The protein's natural variant, known as in BARTS2, features a modification of the amino acid from V to E at position 72.
+The protein's natural variant, known as in BARTS2, features a modification of the amino acid from D to Y at position 74.
+The protein's natural variant, known as in BARTS2;, features a modification of the amino acid from W to C at position 99.
+The protein's natural variant, known as in BARTS2;, features a modification of the amino acid from D to H at position 108.
+The protein's natural variant, known as in BARTS2;, features a modification of the amino acid from P to L at position 110.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from S to F at position 115.
+The protein's natural variant, known as in BARTS2;, features a modification of the amino acid from V to E at position 122.
+The protein's natural variant, known as in BARTS2;, features a modification of the amino acid from N to K at position 124.
+The protein's natural variant, known as in BARTS2;, features a modification of the amino acid from G to E at position 167.
+The protein's natural variant, known as in BARTS2;, features a modification of the amino acid from A to T at position 198.
+The protein's natural variant, known as in BARTS2;, features a modification of the amino acid from A to V at position 214.
+The protein's natural variant, known as in BARTS2;, features a modification of the amino acid from S to R at position 219.
+The protein's natural variant, known as in BARTS2;, features a modification of the amino acid from V to G at position 315.
+The protein's natural variant, known as in BARTS2;, features a modification of the amino acid from M to T at position 357.
+The protein's natural variant, known as does not affect interaction with PCSK9;, features a modification of the amino acid from V to L at position 98.
+The protein's natural variant, known as in CAVIPMR;, features a modification of the amino acid from T to M at position 82.
+The protein's natural variant, known as found in patients with retinitis pigmentosa; unknown pathological significance;, features a modification of the amino acid from A to T at position 144.
+The protein's natural variant, known as in CAVIPMR; unknown pathological significance;, features a modification of the amino acid from G to R at position 471.
+The protein's natural variant, known as in CAVIPMR;, features a modification of the amino acid from G to R at position 868.
+The protein's natural variant, known as in strain: USDA 61, features a modification of the amino acid from V to A at position 151.
+The protein's natural variant, known as in CMD1DD; unknown pathological significance, features a modification of the amino acid from P to T at position 52.
+The protein's natural variant, known as in CMD1DD; unknown pathological significance;, features a modification of the amino acid from L to I at position 83.
+The protein's natural variant, known as in CMD1DD; unknown pathological significance;, features a modification of the amino acid from T to S at position 177.
+The protein's natural variant, known as in CMD1DD; unknown pathological significance, features a modification of the amino acid from M to L at position 194.
+The protein's natural variant, known as in CMD1DD; unknown pathological significance, features a modification of the amino acid from M to V at position 196.
+The protein's natural variant, known as in CMD1DD; unknown pathological significance;, features a modification of the amino acid from G to V at position 259.
+The protein's natural variant, known as in CMD1DD; unknown pathological significance;, features a modification of the amino acid from R to W at position 392.
+The protein's natural variant, known as in CMD1DD; unknown pathological significance;, features a modification of the amino acid from S to L at position 455.
+The protein's natural variant, known as in CMD1DD;, features a modification of the amino acid from V to I at position 535.
+The protein's natural variant, known as in CMD1DD, features a modification of the amino acid from Q to P at position 598.
+The protein's natural variant, known as in CMD1DD;, features a modification of the amino acid from R to Q at position 634.
+The protein's natural variant, known as in CMD1DD; impaired mRNA splicing of TTN (Titin) mRNA;, features a modification of the amino acid from R to W at position 634.
+The protein's natural variant, known as in CMD1DD; causes the formation of anomalous isoforms in TTN (Titin); impaired localization to the nucleus, leading to mislocalization to the cytoplasm, features a modification of the amino acid from S to A at position 635.
+The protein's natural variant, known as in CMD1DD; impaired localization to the nucleus, leading to mislocalization to the cytoplasm;, features a modification of the amino acid from R to C at position 636.
+The protein's natural variant, known as in CMD1DD; also found in patients with left ventricular non-compaction;, features a modification of the amino acid from R to H at position 636.
+The protein's natural variant, known as in CMD1DD; impaired splicing of target mRNAs, such as TTN, CAMK2D and CACNA1C; decreased localization to the nucleus associated with relocalization to P-body and stress granules;, features a modification of the amino acid from R to S at position 636.
+The protein's natural variant, known as in CMD1DD; also found in patients with left ventricular non-compaction;, features a modification of the amino acid from S to G at position 637.
+The protein's natural variant, known as in CMD1DD; impaired localization to the nucleus, leading to mislocalization to the cytoplasm;, features a modification of the amino acid from P to L at position 638.
+The protein's natural variant, known as in CMD1DD; unknown pathological significance;, features a modification of the amino acid from D to G at position 674.
+The protein's natural variant, known as in CMD1DD;, features a modification of the amino acid from R to Q at position 716.
+The protein's natural variant, known as in CMD1DD; unknown pathological significance;, features a modification of the amino acid from D to N at position 888.
+The protein's natural variant, known as in CMD1DD; unknown pathological significance;, features a modification of the amino acid from M to K at position 905.
+The protein's natural variant, known as in CMD1DD; decreased stability; impaired mRNA splicing of target mRNAs;, features a modification of the amino acid from E to K at position 913.
+The protein's natural variant, known as in CMD1DD; impaired mRNA splicing of target mRNAs; does not affect nuclear localization, features a modification of the amino acid from V to A at position 914.
+The protein's natural variant, known as in CMD1DD; unknown pathological significance;, features a modification of the amino acid from P to S at position 1039.
+The protein's natural variant, known as in CMD1DD; unknown pathological significance;, features a modification of the amino acid from R to W at position 1057.
+The protein's natural variant, known as in CMD1DD; unknown pathological significance;, features a modification of the amino acid from P to R at position 1081.
+The protein's natural variant, known as in CMD1DD; unknown pathological significance;, features a modification of the amino acid from E to K at position 1206.
+The protein's natural variant, known as in minor forms, features a modification of the amino acid from T to V at position 31.
+The protein's natural variant, known as in minor forms, features a modification of the amino acid from K to T at position 52.
+The protein's natural variant, known as in minor forms, features a modification of the amino acid from E to D at position 59.
+The protein's natural variant, known as in minor forms, features a modification of the amino acid from V to I at position 72.
+The protein's natural variant, known as in minor forms, features a modification of the amino acid from I to V at position 81.
+The protein's natural variant, known as in minor forms, features a modification of the amino acid from N to Q at position 110.
+The protein's natural variant, known as in minor forms, features a modification of the amino acid from L to G at position 112.
+The protein's natural variant, known as in XLID12;, features a modification of the amino acid from L to F at position 313.
+The protein's natural variant, known as in XLID12; reduced amounts of protein; reduced amounts of other THO complex subunits; the mutant protein has a significantly shorter half-life;, features a modification of the amino acid from L to P at position 438.
+The protein's natural variant, known as in XLID12; reduced amounts of mutant protein; reduced amounts of other THO complex subunits; the mutant protein has a significantly shorter half-life;, features a modification of the amino acid from I to T at position 800.
+The protein's natural variant, known as in XLID12; normal amounts of mutant protein; normal amounts of other THO complex subunits;, features a modification of the amino acid from S to P at position 1012.
+The protein's natural variant, known as in SSMCF;, features a modification of the amino acid from C to Y at position 3.
+The protein's natural variant, known as in FA10D; St. Louis II; strongly reduced activity; not activated by factor VIIa and tissue factor;, features a modification of the amino acid from E to G at position 47.
+The protein's natural variant, known as in FA10D;, features a modification of the amino acid from G to V at position 51.
+The protein's natural variant, known as in FA10D; Ketchikan;, features a modification of the amino acid from E to G at position 54.
+The protein's natural variant, known as in FA10D; Vorarlberg; converts prothrombin at a normal rate but shows decreased affinity for calcium;, features a modification of the amino acid from E to K at position 54.
+The protein's natural variant, known as in FA10D; Tokyo;, features a modification of the amino acid from E to Q at position 72.
+The protein's natural variant, known as in FA10D; Riyadh;, features a modification of the amino acid from E to K at position 91.
+The protein's natural variant, known as in FA10D; uncertain pathological significance; detected in patients carrying K-54 or P-374; slightly reduced activity;, features a modification of the amino acid from E to K at position 142.
+The protein's natural variant, known as in FA10D, features a modification of the amino acid from C to Y at position 149.
+The protein's natural variant, known as in FA10D, features a modification of the amino acid from C to Y at position 151.
+The protein's natural variant, known as in FA10D; unknown pathological significance;, features a modification of the amino acid from G to D at position 262.
+The protein's natural variant, known as in FA10D; may affect splicing;, features a modification of the amino acid from G to R at position 289.
+The protein's natural variant, known as in FA10D;, features a modification of the amino acid from E to K at position 304.
+The protein's natural variant, known as in FA10D; Stockton; 50% decrease in specific activity;, features a modification of the amino acid from D to N at position 322.
+The protein's natural variant, known as in FA10D;, features a modification of the amino acid from R to W at position 327.
+The protein's natural variant, known as in FA10D;, features a modification of the amino acid from V to M at position 338.
+The protein's natural variant, known as in FA10D;, features a modification of the amino acid from E to K at position 350.
+The protein's natural variant, known as in FA10D; Roma;, features a modification of the amino acid from T to M at position 358.
+The protein's natural variant, known as in FA10D;, features a modification of the amino acid from G to S at position 363.
+The protein's natural variant, known as in FA10D; San Antonio;, features a modification of the amino acid from R to C at position 366.
+The protein's natural variant, known as in FA10D; Marseille; decreased cleavage by factor IXa; normal catalytic efficiency for prothrombin;, features a modification of the amino acid from S to P at position 374.
+The protein's natural variant, known as in FA10D; partial loss of activity, features a modification of the amino acid from V to A at position 382.
+The protein's natural variant, known as in FA10D; Friuli;, features a modification of the amino acid from P to S at position 383.
+The protein's natural variant, known as in FA10D; Padua 4;, features a modification of the amino acid from C to F at position 390.
+The protein's natural variant, known as in FA10D;, features a modification of the amino acid from C to R at position 404.
+The protein's natural variant, known as in FA10D; almost complete loss of activity;, features a modification of the amino acid from G to S at position 406.
+The protein's natural variant, known as in FA10D; Padua 3;, features a modification of the amino acid from G to R at position 420.
+The protein's natural variant, known as in FA10D; significant loss of activity;, features a modification of the amino acid from G to D at position 421.
+The protein's natural variant, known as in FA10D; San Giovanni Rotondo, features a modification of the amino acid from K to N at position 448.
+The protein's natural variant, known as in MGORS8;, features a modification of the amino acid from T to I at position 466.
+The protein's natural variant, known as in DSMA2; unknown pathological significance;, features a modification of the amino acid from L to Q at position 65.
+The protein's natural variant, known as in ALS16; the mutation decreases the viability of motor neurons; the mutant protein is shifted to lower density membranes and forms detergent-resistant complexes; there is an almost 2-fold increase in apoptosis in response to stress compared to controls;, features a modification of the amino acid from E to Q at position 102.
+The protein's natural variant, known as in DHRD; misfolded, accumulates in cells due to inefficient secretion; induces the formation of deposits between Bruch's membrane and the retinal pigment epithelium where it accumulates;, features a modification of the amino acid from R to W at position 345.
+The protein's natural variant, known as loss of 15-lipoxygenase activity;, features a modification of the amino acid from A to D at position 416.
+The protein's natural variant, known as does not affect arachidonate 15-lipoxygenase activity; does not impact enzyme structure;, features a modification of the amino acid from R to H at position 486.
+The protein's natural variant, known as does not affect arachidonate 15-lipoxygenase activity; does not impact enzyme structure;, features a modification of the amino acid from Q to R at position 656.
+The protein's natural variant, known as does not affect arachidonate 15-lipoxygenase activity; destabilizes the enzyme structure;, features a modification of the amino acid from I to V at position 676.
+The protein's natural variant, known as in CMS10; results in a significant reduction of AChR clusters;, features a modification of the amino acid from E to K at position 3.
+The protein's natural variant, known as in CMS10; results in a significant reduction of AChR clusters, features a modification of the amino acid from P to T at position 31.
+The protein's natural variant, known as in CMS10; results in reduced stimulation of MUSK autophosphorylation, features a modification of the amino acid from A to V at position 33.
+The protein's natural variant, known as does not affect AChR clusters number or complexity;, features a modification of the amino acid from S to L at position 45.
+The protein's natural variant, known as in CMS10; results in a decrease of branched, c-shaped and perforated AChR clusters;, features a modification of the amino acid from T to M at position 77.
+The protein's natural variant, known as in CMS10; results in a significant reduction of AChR clusters, features a modification of the amino acid from G to C at position 109.
+The protein's natural variant, known as in CMS10;, features a modification of the amino acid from V to M at position 116.
+The protein's natural variant, known as in CMS10, features a modification of the amino acid from H to Q at position 132.
+The protein's natural variant, known as in CMS10; results in a significant reduction of AChR clusters;, features a modification of the amino acid from V to L at position 139.
+The protein's natural variant, known as in CMS10;, features a modification of the amino acid from P to L at position 146.
+The protein's natural variant, known as in CMS10, features a modification of the amino acid from L to R at position 157.
+The protein's natural variant, known as in CMS10; reduced stimulation of MUSK autophosphorylation when associated with A-174; results in a significant reduction of AChR clusters;, features a modification of the amino acid from R to Q at position 158.
+The protein's natural variant, known as in CMS10; results in a significant reduction of AChR clusters;, features a modification of the amino acid from G to R at position 161.
+The protein's natural variant, known as in CMS10; results in a significant reduction of AChR clusters;, features a modification of the amino acid from G to R at position 166.
+The protein's natural variant, known as in CMS10; results in a significant reduction of AChR clusters;, features a modification of the amino acid from G to D at position 171.
+The protein's natural variant, known as in CMS10, features a modification of the amino acid from G to R at position 171.
+The protein's natural variant, known as in CMS10;, features a modification of the amino acid from G to R at position 172.
+The protein's natural variant, known as in CMS10; results in a significant reduction of AChR clusters;, features a modification of the amino acid from G to A at position 180.
+The protein's natural variant, known as in CMS10, features a modification of the amino acid from G to V at position 180.
+The protein's natural variant, known as in CMS10;, features a modification of the amino acid from P to H at position 469.
+The protein's natural variant, known as in a lymphoid cancer cell line; somatic mutation, features a modification of the amino acid from S to L at position 29.
+The protein's natural variant, known as in a prostate cancer cell line; somatic mutation;, features a modification of the amino acid from R to C at position 59.
+The protein's natural variant, known as in lung cancer cell line; somatic mutation, features a modification of the amino acid from T to A at position 299.
+The protein's natural variant, known as in a prostate cancer cell line; somatic mutation;, features a modification of the amino acid from R to Q at position 360.
+The protein's natural variant, known as in a breast cancer cell line; somatic mutation, features a modification of the amino acid from E to K at position 516.
+The protein's natural variant, known as in a prostate cancer cell line; somatic mutation;, features a modification of the amino acid from R to C at position 556.
+The protein's natural variant, known as in one individual with lung cancer;, features a modification of the amino acid from R to H at position 556.
+The protein's natural variant, known as in a cancer cell line;, features a modification of the amino acid from R to H at position 558.
+The protein's natural variant, known as in a breast cancer cell line; somatic mutation;, features a modification of the amino acid from E to K at position 569.
+The protein's natural variant, known as in a cancer cell line;, features a modification of the amino acid from R to H at position 572.
+The protein's natural variant, known as in NCPH2; unknown pathological significance, features a modification of the amino acid from I to T at position 47.
+The protein's natural variant, known as in NCPH2; unknown pathological significance, features a modification of the amino acid from P to L at position 109.
+The protein's natural variant, known as in NCPH2; unknown pathological significance; strong decrease in protein level;, features a modification of the amino acid from L to P at position 204.
+The protein's natural variant, known as in NCPH2; unknown pathological significance, features a modification of the amino acid from L to F at position 223.
+The protein's natural variant, known as found in patients with CHD; unknown pathological significance;, features a modification of the amino acid from I to V at position 71.
+The protein's natural variant, known as probable disease-associated variant found in patients with CHD; associated with CHD susceptibility; significantly reduced autophosphorylation; decreased NTRK3 signaling associated with decreased apoptosis in absence of NTF3;, features a modification of the amino acid from T to M at position 93.
+The protein's natural variant, known as in a gastric adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from T to R at position 149.
+The protein's natural variant, known as found in patients with CHD; unknown pathological significance; no change in autophosphorylation; no effect on NTRK3 signaling;, features a modification of the amino acid from N to I at position 163.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from V to L at position 307.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation, features a modification of the amino acid from L to Q at position 336.
+The protein's natural variant, known as probable disease-associated variant found in patients with CHD; associated with CHD susceptibility; no change in autophosphorylation; changed NTRK3 signaling with decreased apoptosis in absence of NTF3;, features a modification of the amino acid from I to F at position 533.
+The protein's natural variant, known as in a lung carcinoma sample; somatic mutation, features a modification of the amino acid from A to S at position 664.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation, features a modification of the amino acid from H to Y at position 677.
+The protein's natural variant, known as in a lung large cell carcinoma sample; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from R to F at position 735.
+The protein's natural variant, known as in a lung carcinoma sample; somatic mutation, features a modification of the amino acid from W to C at position 736.
+The protein's natural variant, known as in a lung carcinoma sample; somatic mutation, features a modification of the amino acid from R to P at position 745.
+The protein's natural variant, known as in a lung carcinoma sample; somatic mutation, features a modification of the amino acid from Y to F at position 766.
+The protein's natural variant, known as probable disease-associated variant found in patients with CHD; associated with CHD susceptibility; no change in autophosphorylation; changed NTRK3 signaling with decreased apoptosis in absence of NTF3;, features a modification of the amino acid from I to M at position 817.
+The protein's natural variant, known as associated with lower plasma lactoferrin concentrations;, features a modification of the amino acid from R to RR at position 22.
+The protein's natural variant, known as decreased antibacterial activity against Gram-positive bacteria; seems to reduce susceptibility to localized juvenile periodontitis; associated with increased plasma lactoferrin concentrations and possibly with susceptibility to coronary artery stenosis;, features a modification of the amino acid from K to R at position 47.
+The protein's natural variant, known as in BDPLT8, features a modification of the amino acid from H to Q at position 187.
+The protein's natural variant, known as in BDPLT8;, features a modification of the amino acid from R to Q at position 256.
+The protein's natural variant, known as in BDPLT8;, features a modification of the amino acid from R to W at position 265.
+The protein's natural variant, known as in frog brain, features a modification of the amino acid from L to I at position 21.
+The protein's natural variant, known as in frog brain, features a modification of the amino acid from S to E at position 24.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from Q to E at position 807.
+The protein's natural variant, known as in AGS2;, features a modification of the amino acid from P to H at position 43.
+The protein's natural variant, known as in AGS2; heterozygous compound with T-177;, features a modification of the amino acid from L to R at position 60.
+The protein's natural variant, known as in AGS2; reduces stability of the RNase complex;, features a modification of the amino acid from W to L at position 73.
+The protein's natural variant, known as in AGS2; reduces stability of the RNase complex;, features a modification of the amino acid from G to S at position 83.
+The protein's natural variant, known as in AGS2; heterozygous compound with T-177; reduces stability of the RNase complex;, features a modification of the amino acid from H to R at position 86.
+The protein's natural variant, known as in AGS2;, features a modification of the amino acid from L to F at position 138.
+The protein's natural variant, known as in AGS2;, features a modification of the amino acid from S to I at position 159.
+The protein's natural variant, known as in AGS2;, features a modification of the amino acid from K to T at position 162.
+The protein's natural variant, known as in AGS2; heterozygous compound with T-177;, features a modification of the amino acid from T to I at position 163.
+The protein's natural variant, known as in AGS2; frequent mutation;, features a modification of the amino acid from A to T at position 177.
+The protein's natural variant, known as in AGS2;, features a modification of the amino acid from V to M at position 183.
+The protein's natural variant, known as in AGS2;, features a modification of the amino acid from V to G at position 185.
+The protein's natural variant, known as in AGS2; heterozygous compound with a nonsense mutation; reduces stability of the RNase complex;, features a modification of the amino acid from Y to H at position 219.
+The protein's natural variant, known as in AGS2;, features a modification of the amino acid from S to P at position 229.
+The natural variant of this protein is characterized by an amino acid alteration from S to N at position 9.
+The protein's natural variant, known as in ANES;, features a modification of the amino acid from L to P at position 351.
+The protein's natural variant, known as in MC4DN4; no effect on synthesis of cytochrome c oxidase subunit II; reduced stability of newly synthesized cytochrome c oxidase subunit II; reduced copper-binding;, features a modification of the amino acid from P to L at position 174.
+The protein's natural variant, known as in CNM6; unknown pathological significance;, features a modification of the amino acid from R to W at position 250.
+The protein's natural variant, known as in an ovarian endometrioid sample; somatic mutation, features a modification of the amino acid from A to T at position 281.
+The protein's natural variant, known as in SFMMP; produces protein aggregation;, features a modification of the amino acid from F to C at position 368.
+The protein's natural variant, known as in SFMMP; mild destabilization of the protein, features a modification of the amino acid from A to S at position 505.
+The protein's natural variant, known as in allele CYP2D6*87;, features a modification of the amino acid from A to V at position 5.
+The protein's natural variant, known as in allele CYP2D6*35;, features a modification of the amino acid from V to M at position 11.
+The protein's natural variant, known as in allele CYP2D6*21 and allele CYP2D6*46;, features a modification of the amino acid from R to H at position 26.
+The protein's natural variant, known as in allele CYP2D6*22;, features a modification of the amino acid from R to C at position 28.
+The protein's natural variant, known as in allele CYP2D6*10 and allele CYP2D6*14; poor debrisquone metabolism;, features a modification of the amino acid from P to S at position 34.
+The protein's natural variant, known as in allele CYP2D6*12; impaired metabolism of sparteine;, features a modification of the amino acid from G to R at position 42.
+The protein's natural variant, known as in allele CYP2D6*23;, features a modification of the amino acid from A to V at position 85.
+The protein's natural variant, known as in allele CYP2D6*88;, features a modification of the amino acid from V to A at position 104.
+The protein's natural variant, known as in allele CYP2D6*17; poor debrisquone metabolism;, features a modification of the amino acid from T to I at position 107.
+The protein's natural variant, known as in allele CYP2D6*89; >90% decrease of monooxygenase activity towards dextromethorphan and bufuralol;, features a modification of the amino acid from L to S at position 142.
+The protein's natural variant, known as in allele CYP2D6*90;, features a modification of the amino acid from K to R at position 147.
+The protein's natural variant, known as in allele CYP2D6*45A, allele CYP2D6*45B and allele CYP2D6*46;, features a modification of the amino acid from E to K at position 155.
+The protein's natural variant, known as in allele CYP2D6*91, features a modification of the amino acid from C to S at position 161.
+The natural variant of this protein is characterized by an amino acid alteration from F to L at position 164.
+The protein's natural variant, known as in allele CYP2D6*14; poor debrisquone metabolism;, features a modification of the amino acid from G to R at position 169.
+The protein's natural variant, known as in allele CYP2D6*6B and allele CYP2D6*6C;, features a modification of the amino acid from G to E at position 212.
+The protein's natural variant, known as >90% decrease of monooxygenase activity towards dextromethorphan and bufuralol;, features a modification of the amino acid from E to K at position 215.
+The protein's natural variant, known as in allele CYP2D6*33;, features a modification of the amino acid from A to S at position 237.
+The protein's natural variant, known as in allele CYP2D6*93; >90% decrease of monooxygenase activity towards dextromethorphan and bufuralol, features a modification of the amino acid from T to P at position 249.
+The protein's natural variant, known as in allele CYP2D6*2, allele CYP2D6*12, allele CYP2D6*14, allele CYP2D6*17, allele CYP2D6*45A, allele CYP2D6*45B and allele CYP2D6*46; significantly reduced monooxygenase activity toward anandamide; slight decrease of monooxygenase activity towards bufuralol;, features a modification of the amino acid from R to C at position 296.
+The protein's natural variant, known as in allele CYP2D6*24;, features a modification of the amino acid from I to L at position 297.
+The protein's natural variant, known as in allele CYP2D6*7; loss of activity;, features a modification of the amino acid from H to P at position 324.
+The natural variant of this protein is characterized by an amino acid alteration from V to M at position 327.
+The protein's natural variant, known as in allele CYP2D6*94;, features a modification of the amino acid from D to G at position 337.
+The protein's natural variant, known as in allele CYP2D6*25;, features a modification of the amino acid from R to G at position 343.
+The protein's natural variant, known as in allele CYP2D6*26, features a modification of the amino acid from I to T at position 369.
+The protein's natural variant, known as in allele CYP2D6*27;, features a modification of the amino acid from E to K at position 410.
+The protein's natural variant, known as >90% decrease of monooxygenase activity towards dextromethorphan and bufuralol;, features a modification of the amino acid from R to C at position 440.
+The protein's natural variant, known as in allele CYP2D6*97, features a modification of the amino acid from F to L at position 457.
+The protein's natural variant, known as in allele CYP2D6*98, features a modification of the amino acid from H to D at position 463.
+The protein's natural variant, known as in allele CYP2D6*2, allele CYP2D6*10, allele CYP2D6*12, allele CYP2D6*14, allele CYP2D6*17, allele CYP2D6*45A, allele CYP2D6*45B and allele CYP2D6*46; impaired metabolism of sparteine;, features a modification of the amino acid from S to T at position 486.
+The protein's natural variant, known as in HOMG4; affects basolateral sorting of pro-EGF preventing the hormone to stimulate EGFR; lack of TRPM6 activation;, features a modification of the amino acid from P to L at position 1070.
+The protein's natural variant, known as in CBAS1, features a modification of the amino acid from G to S at position 19.
+The protein's natural variant, known as in CBAS1; loss of activity;, features a modification of the amino acid from E to K at position 147.
+The protein's natural variant, known as in strain: D273-10B/A, features a modification of the amino acid from E to G at position 36.
+The protein's natural variant, known as in strain: D273-10B/A and NCYC 74, features a modification of the amino acid from G to K at position 217.
+The protein's natural variant, known as in strain: D273-10B/A and NCYC 74, features a modification of the amino acid from N to D at position 346.
+The protein's natural variant, known as in variant F, features a modification of the amino acid from R to H at position 31.
+The protein's natural variant, known as in variant G, features a modification of the amino acid from R to C at position 118.
+The protein's natural variant, known as in variant G and variant H, features a modification of the amino acid from T to I at position 156.
+The protein's natural variant, known as in variant B and variant B2, features a modification of the amino acid from T to I at position 157.
+The protein's natural variant, known as in variant B and variant B2, features a modification of the amino acid from D to A at position 169.
+The protein's natural variant, known as in variant B2, features a modification of the amino acid from I to T at position 174.
+The protein's natural variant, known as in variant E, features a modification of the amino acid from S to G at position 176.
+The protein's natural variant, known as in subsp. Pelzelni, features a modification of the amino acid from V to I at position 91.
+The protein's natural variant, known as in RN-, features a modification of the amino acid from R to Q at position 250.
+The protein's natural variant, known as in SCAR11; shows intracellular localization different from that of the wild-type protein; forms a reticular pattern in the cytoplasm; does not show submembranous distribution; is abnormally retained in the endoplasmic reticulum consistent to improper folding;, features a modification of the amino acid from G to D at position 439.
+The protein's natural variant, known as in transposon Tn21, features a modification of the amino acid from I to M at position 96.
+The protein's natural variant, known as in transposon Tn21, features a modification of the amino acid from D to E at position 128.
+The protein's natural variant, known as in plasmid pLMO229, features a modification of the amino acid from K to R at position 201.
+The protein's natural variant, known as in strain: FDA 574, features a modification of the amino acid from F to S at position 80.
+The protein's natural variant, known as in strain: FDA 574, features a modification of the amino acid from K to E at position 84.
+The protein's natural variant, known as in allele CYP2B6*10;, features a modification of the amino acid from Q to L at position 21.
+The protein's natural variant, known as in allele CYP2B6*2 and allele CYP2B6*10;, features a modification of the amino acid from R to C at position 22.
+The protein's natural variant, known as in allele CYP2B6*11;, features a modification of the amino acid from M to V at position 46.
+The protein's natural variant, known as in allele CYP2B6*12;, features a modification of the amino acid from G to E at position 99.
+The protein's natural variant, known as in allele CYP2B6*8 and allele CYP2B6*13;, features a modification of the amino acid from K to E at position 139.
+The protein's natural variant, known as in allele CYP2B6*14;, features a modification of the amino acid from R to Q at position 140.
+The protein's natural variant, known as in allele CYP2B6*6, allele CYP2B6*7, allele CYP2B6*9 and allele CYP2B6*13;, features a modification of the amino acid from Q to H at position 172.
+The protein's natural variant, known as in allele CYP2B6*3;, features a modification of the amino acid from S to R at position 259.
+The protein's natural variant, known as in allele CYP2B6*4, allele CYP2B6*6, allele CYP2B6*7 and allele CYP2B6*13; slight decrease in activity;, features a modification of the amino acid from K to R at position 262.
+The protein's natural variant, known as in allele CYP2B6*15;, features a modification of the amino acid from I to N at position 391.
+The protein's natural variant, known as in allele CYP2B6*5 and allele CYP2B6*7;, features a modification of the amino acid from R to C at position 487.
+The protein's natural variant, known as in subspecies Rhodorus, features a modification of the amino acid from V to I at position 90.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from H to Q at position 361.
+The protein's natural variant, known as in strain: CBS 120.49 / N400, features a modification of the amino acid from D to N at position 73.
+The protein's natural variant, known as in strain: CBS 120.49 / N400, features a modification of the amino acid from R to G at position 109.
+The protein's natural variant, known as in strain: CBS 120.49 / N400, features a modification of the amino acid from S to A at position 145.
+The protein's natural variant, known as in strain: CBS 120.49 / N400, features a modification of the amino acid from S to A at position 192.
+The protein's natural variant, known as in strain: CBS 120.49 / N400, features a modification of the amino acid from A to G at position 233.
+The protein's natural variant, known as found in a renal cell carcinoma sample; somatic mutation, features a modification of the amino acid from L to H at position 1168.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from E to K at position 423.
+The protein's natural variant, known as in CONDCA; decreased tubulin deglutamylation shown by in vitro functional expression of the homologous murine variant;, features a modification of the amino acid from Y to D at position 694.
+The protein's natural variant, known as in CONDCA; unknown pathological significance;, features a modification of the amino acid from R to C at position 799.
+The protein's natural variant, known as in CONDCA; decreased tubulin deglutamylation asshown by in vitro functional expression of the homologous murine variant;, features a modification of the amino acid from T to M at position 851.
+The protein's natural variant, known as in CONDCA; unknown pathological significance, features a modification of the amino acid from R to C at position 910.
+The protein's natural variant, known as in CONDCA; decreased tubulin deglutamylation shown by in vitro functional expression of the homologous murine variant;, features a modification of the amino acid from R to W at position 918.
+The protein's natural variant, known as in CONDCA; decreased tubulin deglutamylation shown by in vitro functional expression of the homologous murine variant;, features a modification of the amino acid from H to L at position 990.
+The protein's natural variant, known as in strain: ISP 5236, features a modification of the amino acid from ALVARC to GSRRAI at position 39.
+The protein's natural variant, known as in strain: ISP 5236, features a modification of the amino acid from DGSRTL to GRFADV at position 120.
+The protein's natural variant, known as in strain: ISP 5236, features a modification of the amino acid from GWASAVAE to AVGVGREP at position 188.
+The protein's natural variant, known as in strain: ISP 5236, features a modification of the amino acid from G to A at position 225.
+The protein's natural variant, known as in strain: ISP 5236, features a modification of the amino acid from S to A at position 262.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from D to A at position 16.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from R to G at position 20.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from S to I at position 26.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from F to L at position 29.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from I to T at position 30.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from I to S at position 31.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from A to T at position 32.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from N to T at position 33.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from V to F at position 41.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from Y to C at position 43.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from N to Y at position 45.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from G to V at position 47.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from C to Y at position 49.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from G to D at position 53.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from G to R at position 53.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from Y to H at position 54.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from S to L at position 55.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from R to Q at position 56.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from A to P at position 57.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from E to A at position 58.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from E to D at position 58.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from E to G at position 58.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from C to W at position 64.
+The protein's natural variant, known as in LQT2; decreased protein stability;, features a modification of the amino acid from C to Y at position 64.
+The protein's natural variant, known as in LQT2; decreased protein stability;, features a modification of the amino acid from T to P at position 65.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from C to G at position 66.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from F to L at position 68.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from H to N at position 70.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from H to R at position 70.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from G to R at position 71.
+The protein's natural variant, known as in LQT2; unknown pathological significance, features a modification of the amino acid from PRTQRRAAA to RPV at position 80.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from P to L at position 72.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from P to Q at position 72.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from T to M at position 74.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from T to P at position 74.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from T to R at position 74.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from A to P at position 78.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from A to V at position 85.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from L to P at position 86.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from L to R at position 86.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from V to G at position 94.
+The protein's natural variant, known as in LQT2; digenic; the patient also carries mutation N-1819 on SCN5A;, features a modification of the amino acid from R to G at position 100.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from R to Q at position 100.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from R to W at position 100.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from D to A at position 102.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from F to Y at position 106.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from C to R at position 108.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from P to S at position 114.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from F to C at position 125.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from P to L at position 141.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from G to A at position 149.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from R to H at position 164.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from R to W at position 176.
+The natural variant of this protein is characterized by an amino acid alteration from G to GGAG at position 189.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from M to V at position 218.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from G to S at position 238.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from R to G at position 242.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from P to S at position 251.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from D to N at position 259.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from A to D at position 277.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from M to T at position 291.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from R to L at position 301.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from G to W at position 306.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from R to C at position 312.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from G to S at position 314.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from S to L at position 320.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from D to N at position 323.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from R to C at position 328.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from P to S at position 347.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from H to R at position 402.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from W to S at position 410.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from L to P at position 413.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from Y to C at position 420.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from T to M at position 421.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from A to T at position 422.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from P to H at position 426.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from Y to C at position 427.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from Y to H at position 427.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from Y to S at position 427.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from S to L at position 428.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from F to L at position 431.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from T to M at position 436.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from P to L at position 440.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from E to D at position 444.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from P to L at position 451.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from D to Y at position 456.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from D to Y at position 460.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from D to Y at position 466.
+The protein's natural variant, known as in LQT2; aberrant protein folding increases the association of mutant KCNH2 with CANX and results in defective protein trafficking;, features a modification of the amino acid from N to D at position 470.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from T to N at position 473.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from T to I at position 474.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from Y to C at position 475.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from V to I at position 476.
+The protein's natural variant, known as in LQT2; bradycardia-induced;, features a modification of the amino acid from A to T at position 490.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from Y to C at position 493.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from Y to S at position 493.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from D to H at position 501.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from D to N at position 501.
+The protein's natural variant, known as in LQT2; located on the same allele as Pro-528;, features a modification of the amino acid from K to N at position 525.
+The protein's natural variant, known as in LQT2; located on the same allele as Asn-525;, features a modification of the amino acid from R to P at position 528.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from R to Q at position 531.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from R to W at position 531.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from R to C at position 534.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from R to L at position 534.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from L to S at position 552.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from A to E at position 558.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from A to P at position 558.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from L to H at position 559.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from A to T at position 561.
+The protein's natural variant, known as in LQT2; the mutation reduces wild-type channel expression;, features a modification of the amino acid from A to V at position 561.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from H to P at position 562.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from H to R at position 562.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from L to P at position 564.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from A to T at position 565.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from C to S at position 566.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from W to R at position 568.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from Y to H at position 569.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from I to L at position 571.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from I to V at position 571.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from G to C at position 572.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from G to D at position 572.
+The protein's natural variant, known as in LQT2; severe form;, features a modification of the amino acid from G to R at position 572.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from G to S at position 572.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from G to V at position 572.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from R to C at position 582.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from R to L at position 582.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from G to R at position 584.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from G to S at position 584.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from W to C at position 585.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from N to D at position 588.
+The protein's natural variant, known as in SQT1;, features a modification of the amino acid from N to K at position 588.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from I to K at position 593.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from I to R at position 593.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from I to T at position 593.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from G to D at position 594.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from P to H at position 596.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from P to L at position 596.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from P to R at position 596.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from Y to C at position 597.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from S to R at position 599.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from G to C at position 601.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from G to S at position 601.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from G to S at position 604.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from P to L at position 605.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from P to S at position 605.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from D to G at position 609.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from D to H at position 609.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from D to N at position 609.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from Y to H at position 611.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from V to L at position 612.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from T to M at position 613.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from A to V at position 614.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from L to F at position 615.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from L to V at position 615.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from Y to C at position 616.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from S to R at position 621.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from L to F at position 622.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from T to I at position 623.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from G to A at position 626.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from G to D at position 626.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from G to S at position 626.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from F to L at position 627.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from G to S at position 628.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from G to V at position 628.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from N to D at position 629.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from N to I at position 629.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from N to K at position 629.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from N to S at position 629.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from V to A at position 630.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from V to L at position 630.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from P to S at position 632.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from N to S at position 633.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from T to I at position 634.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from N to D at position 635.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from N to I at position 635.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from N to K at position 635.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from E to D at position 637.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from E to K at position 637.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from K to E at position 638.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from K to N at position 638.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from F to L at position 640.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from F to V at position 640.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from S to F at position 641.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from V to F at position 644.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from V to L at position 644.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from M to I at position 645.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from M to L at position 645.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from G to S at position 648.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from F to C at position 656.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from G to R at position 657.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from S to L at position 660.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from I to T at position 662.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from L to P at position 678.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from H to Y at position 687.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from L to P at position 693.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from R to C at position 696.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from R to P at position 696.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from I to V at position 711.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from P to L at position 721.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from I to F at position 728.
+The protein's natural variant, known as in LQT2; impairs channel function; exhibits reduced activating currents compared to wild-type; cell surface trafficking is not impaired; does not exert dominant-negative effects on wild-type channel; the half-maximal activation voltage is not significantly affected by the mutation, features a modification of the amino acid from R to P at position 744.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from G to V at position 749.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from R to Q at position 752.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from R to W at position 752.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from K to N at position 757.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from D to Y at position 767.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from V to A at position 770.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from D to Y at position 774.
+The protein's natural variant, known as predisposes to LQT2 and torsades de pointes while taking the drug amiodarone; in vitro studies confirmed a significant reduction in potassium currents; the ECG abnormalities reversed on drug withdrawal;, features a modification of the amino acid from R to W at position 784.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from E to D at position 788.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from E to K at position 788.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from R to W at position 791.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from G to W at position 800.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from F to C at position 805.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from F to S at position 805.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from G to E at position 806.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from S to L at position 818.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from S to P at position 818.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from G to R at position 820.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from V to M at position 822.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from R to W at position 823.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from D to G at position 837.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from D to Y at position 837.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from P to S at position 846.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from N to H at position 861.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from N to I at position 861.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from R to C at position 885.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from R to H at position 887.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from R to C at position 894.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from R to L at position 894.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from G to R at position 903.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from S to L at position 906.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from A to V at position 913.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from P to L at position 917.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from R to Q at position 920.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from R to W at position 920.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from R to Q at position 922.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from R to W at position 922.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from G to A at position 924.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from G to E at position 924.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from G to R at position 925.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from S to N at position 937.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from R to C at position 948.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from P to L at position 968.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from T to I at position 983.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from N to I at position 996.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from R to Q at position 1005.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from R to H at position 1007.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from R to W at position 1033.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from G to D at position 1036.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from V to M at position 1038.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from L to P at position 1049.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from L to V at position 1066.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from Y to C at position 1078.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from P to L at position 1093.
+The protein's natural variant, known as in LQT2;, features a modification of the amino acid from M to V at position 1115.
+The protein's natural variant, known as in LQT2; unknown pathological significance;, features a modification of the amino acid from H to Y at position 1153.
+The protein's natural variant, known as in strain: cv. Lz-0, features a modification of the amino acid from A to T at position 640.
+The protein's natural variant, known as in strain: cv. Lz-0, features a modification of the amino acid from R to L at position 686.
+The protein's natural variant, known as in colon cancer;, features a modification of the amino acid from K to R at position 61.
+The protein's natural variant, known as in HRH; Gravesend, features a modification of the amino acid from G to D at position 7.
+The protein's natural variant, known as in LNS; HB, features a modification of the amino acid from V to G at position 8.
+The protein's natural variant, known as in LNS; FG, features a modification of the amino acid from G to D at position 16.
+The protein's natural variant, known as in HRH; Urangan;, features a modification of the amino acid from G to S at position 16.
+The protein's natural variant, known as in HRH; Mashad; strongly reduces enzymatic activity, features a modification of the amino acid from D to V at position 20.
+The protein's natural variant, known as in HRH; Reduces enzymatic activity, features a modification of the amino acid from C to F at position 23.
+The protein's natural variant, known as in HRH; JS, features a modification of the amino acid from C to W at position 23.
+The protein's natural variant, known as in LNS; Detroit;, features a modification of the amino acid from L to P at position 41.
+The protein's natural variant, known as in LNS; Isar, features a modification of the amino acid from I to F at position 42.
+The protein's natural variant, known as in LNS; Heapey, features a modification of the amino acid from I to T at position 42.
+The protein's natural variant, known as in LNS; Salamanca, features a modification of the amino acid from MD to RN at position 44.
+The protein's natural variant, known as in LNS; Japan, features a modification of the amino acid from D to Y at position 44.
+The protein's natural variant, known as in LNS; RJK 2163;, features a modification of the amino acid from R to K at position 45.
+The protein's natural variant, known as in HRH; AD and DD;, features a modification of the amino acid from R to H at position 48.
+The protein's natural variant, known as in LNS; LW;, features a modification of the amino acid from A to P at position 50.
+The protein's natural variant, known as in LNS; 1265, features a modification of the amino acid from A to V at position 50.
+The protein's natural variant, known as in HRH; Toronto;, features a modification of the amino acid from R to G at position 51.
+The protein's natural variant, known as in LNS; Banbury, features a modification of the amino acid from R to P at position 51.
+The protein's natural variant, known as in Edinburgh;, features a modification of the amino acid from D to G at position 52.
+The protein's natural variant, known as in HRH; MG, features a modification of the amino acid from V to A at position 53.
+The protein's natural variant, known as in HRH; TE, features a modification of the amino acid from V to M at position 53.
+The protein's natural variant, known as in LNS; Japan-1, features a modification of the amino acid from M to L at position 54.
+The protein's natural variant, known as in LNS; Montreal;, features a modification of the amino acid from M to T at position 57.
+The protein's natural variant, known as in HRH; Toowong;, features a modification of the amino acid from G to R at position 58.
+The protein's natural variant, known as in HRH; Reduces enzymatic activity;, features a modification of the amino acid from H to R at position 60.
+The protein's natural variant, known as enzyme activity 37% of normal; asymptomatic, features a modification of the amino acid from H to R at position 61.
+The protein's natural variant, known as in LNS; Asia, features a modification of the amino acid from A to P at position 64.
+The protein's natural variant, known as in LNS; Asia, features a modification of the amino acid from L to P at position 65.
+The protein's natural variant, known as in LNS; New Haven/1510, Asia;, features a modification of the amino acid from G to E at position 70.
+The protein's natural variant, known as in LNS; Yale;, features a modification of the amino acid from G to R at position 71.
+The protein's natural variant, known as in LNS; Asia, features a modification of the amino acid from Y to C at position 72.
+The protein's natural variant, known as in LNS; Flint/RJK 892/DW/Perth/1522, Japan;, features a modification of the amino acid from F to L at position 74.
+The protein's natural variant, known as in LNS; Asia, features a modification of the amino acid from L to Q at position 78.
+The protein's natural variant, known as in HRH; Swan;, features a modification of the amino acid from L to V at position 78.
+The protein's natural variant, known as in HRH; Arlington;, features a modification of the amino acid from D to V at position 80.
+The protein's natural variant, known as in HRH; Munich;, features a modification of the amino acid from S to R at position 104.
+The protein's natural variant, known as in HRH; London;, features a modification of the amino acid from S to L at position 110.
+The protein's natural variant, known as in HRH; Asia, features a modification of the amino acid from T to P at position 124.
+The protein's natural variant, known as in LNS; Midland/RJK 896;, features a modification of the amino acid from V to D at position 130.
+The protein's natural variant, known as in LNS; RJK 1784, features a modification of the amino acid from L to S at position 131.
+The protein's natural variant, known as in HRH; Ann-Arbor;, features a modification of the amino acid from I to M at position 132.
+The protein's natural variant, known as in LNS; Runcorn, features a modification of the amino acid from I to T at position 132.
+The protein's natural variant, known as in HRH; Yeronga, features a modification of the amino acid from D to G at position 135.
+The protein's natural variant, known as in LNS; RJK 1210;, features a modification of the amino acid from M to K at position 143.
+The protein's natural variant, known as in LNS; RW, features a modification of the amino acid from M to MA at position 143.
+The protein's natural variant, known as in LNS; Asia, features a modification of the amino acid from L to P at position 147.
+The protein's natural variant, known as in LNS; Asia, features a modification of the amino acid from K to E at position 159.
+The protein's natural variant, known as in LNS; Asia, features a modification of the amino acid from K to KV at position 159.
+The protein's natural variant, known as in HRH; Milwaukee/RJK 949;, features a modification of the amino acid from A to S at position 161.
+The protein's natural variant, known as in LNS; Farnham, features a modification of the amino acid from S to R at position 162.
+The protein's natural variant, known as in HRH; Brisbane;, features a modification of the amino acid from T to I at position 168.
+The protein's natural variant, known as in LNS; Marlow;, features a modification of the amino acid from P to L at position 176.
+The protein's natural variant, known as in LNS; Roanne, features a modification of the amino acid from D to V at position 177.
+The protein's natural variant, known as in LNS; RJK 2185;, features a modification of the amino acid from D to Y at position 177.
+The protein's natural variant, known as in HRH; Japan-2, features a modification of the amino acid from VG to GR at position 180.
+The protein's natural variant, known as in HRH; JF, features a modification of the amino acid from I to T at position 183.
+The protein's natural variant, known as in HRH; Asia, features a modification of the amino acid from D to G at position 185.
+The protein's natural variant, known as in HRH and LNS; Asia, features a modification of the amino acid from V to A at position 188.
+The protein's natural variant, known as in HRH; Asia, features a modification of the amino acid from A to V at position 192.
+The protein's natural variant, known as in HRH; Moose-Jaw; results in cooperativity and decreased substrate affinities;, features a modification of the amino acid from D to E at position 194.
+The protein's natural variant, known as in LNS; Kinston/RJK 2188;, features a modification of the amino acid from D to N at position 194.
+The protein's natural variant, known as in HRH; Dirranbandi, Asia, features a modification of the amino acid from Y to C at position 195.
+The protein's natural variant, known as in LNS; New Briton/RJK 950;, features a modification of the amino acid from F to V at position 199.
+The protein's natural variant, known as in HRH; Ashville;, features a modification of the amino acid from D to G at position 201.
+The protein's natural variant, known as in HRH; RB, features a modification of the amino acid from D to N at position 201.
+The protein's natural variant, known as in LNS; GM, features a modification of the amino acid from D to Y at position 201.
+The protein's natural variant, known as in LNS; RJK 1874;, features a modification of the amino acid from H to D at position 204.
+The protein's natural variant, known as in LNS; 779, features a modification of the amino acid from H to R at position 204.
+The protein's natural variant, known as in LNS; Reading/RJK 1727, features a modification of the amino acid from C to Y at position 206.
+The protein's natural variant, known as in allele APOH*1;, features a modification of the amino acid from S to N at position 107.
+The protein's natural variant, known as loss of phosphatidylserine-binding;, features a modification of the amino acid from C to G at position 325.
+The protein's natural variant, known as in allele APOH*3W; loss of phosphatidylserine-binding;, features a modification of the amino acid from W to S at position 335.
+The protein's natural variant, known as in strain: cv. Bla-1, cv. Bs-1, cv. Ita-0 and cv. Kas-1, features a modification of the amino acid from L to I at position 76.
+The protein's natural variant, known as in strain: cv. Lisse-2, features a modification of the amino acid from H to Q at position 128.
+The protein's natural variant, known as in strain: cv. Gr-3, features a modification of the amino acid from I to T at position 169.
+The protein's natural variant, known as in strain: cv. Co-1, features a modification of the amino acid from N to D at position 230.
+The protein's natural variant, known as in MEGD;, features a modification of the amino acid from L to P at position 103.
+The protein's natural variant, known as in MEGD;, features a modification of the amino acid from L to S at position 193.
+The protein's natural variant, known as in MEGD;, features a modification of the amino acid from F to S at position 350.
+The protein's natural variant, known as in strain: 23, 3700, 3759, LIM1, LIM2 and LIM3, features a modification of the amino acid from E to D at position 534.
+The protein's natural variant, known as in strain: 23, 3700, 3759, LIM1, LIM2 and LIM3, features a modification of the amino acid from K to N at position 864.
+The protein's natural variant, known as in strain: cv. Bla-10, cv. Cvi-0, cv. Ga-0 and cv. Ts-5, features a modification of the amino acid from F to FF at position 14.
+The protein's natural variant, known as in strain: cv. El-0, Gy-0 and Kn-0, features a modification of the amino acid from A to E at position 25.
+The protein's natural variant, known as in strain: cv. El-0, Gy-0 and Kn-0, features a modification of the amino acid from D to E at position 38.
+The protein's natural variant, known as in strain: cv. Gu-0 and cv. Ove-0, features a modification of the amino acid from I to V at position 61.
+The protein's natural variant, known as in strain: cv. Se-0, features a modification of the amino acid from G to V at position 244.
+The protein's natural variant, known as in strain: Isolate XJ03057, features a modification of the amino acid from A to R at position 62.
+The protein's natural variant, known as in strain: Isolate XJ03057 and Isolate XJ03165, features a modification of the amino acid from T to M at position 89.
+The protein's natural variant, known as in strain: Isolate XJ03165, features a modification of the amino acid from I to T at position 153.
+The protein's natural variant, known as in strain: Isolate XJ03165, features a modification of the amino acid from M to V at position 309.
+The protein's natural variant, known as in CILD38; loss of ciliary axoneme inner dynein arm and outer dynein arm structures in patient respiratory epithelial cells;, features a modification of the amino acid from H to R at position 259.
+The protein's natural variant, known as in strain: BALB/c, features a modification of the amino acid from T to P at position 490.
+The protein's natural variant, known as in strain: BALB/c, features a modification of the amino acid from A to S at position 659.
+The protein's natural variant, known as in haplotype CNT1, features a modification of the amino acid from M to V at position 10.
+The protein's natural variant, known as in haplotype CNT1, features a modification of the amino acid from S to N at position 37.
+The protein's natural variant, known as associated with autosomal recessive retinitis pigmentosa;, features a modification of the amino acid from S to L at position 44.
+The protein's natural variant, known as in RP37;, features a modification of the amino acid from G to R at position 56.
+The protein's natural variant, known as in ESCS;, features a modification of the amino acid from R to Q at position 76.
+The protein's natural variant, known as in ESCS;, features a modification of the amino acid from R to W at position 76.
+The protein's natural variant, known as in ESCS;, features a modification of the amino acid from G to V at position 88.
+The protein's natural variant, known as in ESCS;, features a modification of the amino acid from R to H at position 97.
+The protein's natural variant, known as associated with ESCS;, features a modification of the amino acid from R to Q at position 104.
+The protein's natural variant, known as in ESCS;, features a modification of the amino acid from R to W at position 104.
+The protein's natural variant, known as in ESCS;, features a modification of the amino acid from E to K at position 121.
+The protein's natural variant, known as in ESCS, features a modification of the amino acid from W to S at position 234.
+The protein's natural variant, known as in ESCS;, features a modification of the amino acid from A to E at position 256.
+The protein's natural variant, known as in ESCS; impairs protein folding;, features a modification of the amino acid from L to P at position 263.
+The protein's natural variant, known as associated with autosomal recessive retinitis pigmentosa;, features a modification of the amino acid from G to S at position 287.
+The protein's natural variant, known as in ESCS; impairs protein folding and stability;, features a modification of the amino acid from R to G at position 309.
+The protein's natural variant, known as in ESCS; impairs protein folding and stability and hinders the ability to form stable dimers;, features a modification of the amino acid from R to Q at position 311.
+The protein's natural variant, known as associated with autosomal recessive retinitis pigmentosa, features a modification of the amino acid from K to R at position 324.
+The protein's natural variant, known as associated with ESCS; impairs protein folding and stability, features a modification of the amino acid from R to G at position 334.
+The protein's natural variant, known as in ESCS; impairs protein folding and stability;, features a modification of the amino acid from L to P at position 336.
+The protein's natural variant, known as in ESCS; impairs protein folding and stability, features a modification of the amino acid from L to V at position 353.
+The protein's natural variant, known as in ESCS;, features a modification of the amino acid from R to P at position 385.
+The protein's natural variant, known as in ESCS; impairs protein folding and stability;, features a modification of the amino acid from M to K at position 407.
+The protein's natural variant, known as in strain: IFO 3336, features a modification of the amino acid from N to S at position 89.
+The protein's natural variant, known as in strain: Asahikawa, features a modification of the amino acid from L to F at position 139.
+The protein's natural variant, known as in strain: IFO 16449, features a modification of the amino acid from TT to QQ at position 325.
+The protein's natural variant, known as in strain: IFO 3336, features a modification of the amino acid from R to S at position 360.
+The natural variant of this protein is characterized by an amino acid alteration from M to Q at position 3.
+The natural variant of this protein is characterized by an amino acid alteration from V to L at position 32.
+The natural variant of this protein is characterized by an amino acid alteration from V to L at position 50.
+The protein's natural variant, known as in HNA;, features a modification of the amino acid from R to W at position 106.
+The protein's natural variant, known as in HNA;, features a modification of the amino acid from S to F at position 111.
+The protein's natural variant, known as in Mambaquaretin-8, features a modification of the amino acid from A to S at position 27.
+The protein's natural variant, known as in VP; abolishes enzyme activity; impairs protein folding and/or stability, features a modification of the amino acid from G to D at position 11.
+The protein's natural variant, known as in VP, features a modification of the amino acid from G to S at position 11.
+The protein's natural variant, known as in VP; strongly decreases enzyme activity; impairs protein folding and/or stability;, features a modification of the amino acid from I to T at position 12.
+The protein's natural variant, known as in VP; strongly decreases enzyme activity; impairs protein folding and/or stability;, features a modification of the amino acid from L to F at position 15.
+The protein's natural variant, known as in VP; strongly decreases enzyme activity; more resistant to thermal denaturation than wild-type enzyme; abolishes mitochondrial protein targeting and localization;, features a modification of the amino acid from H to P at position 20.
+The protein's natural variant, known as in VP; decreases enzyme activity, features a modification of the amino acid from E to V at position 34.
+The protein's natural variant, known as in VP; strongly decreases enzyme activity; impairs protein folding and/or stability, features a modification of the amino acid from R to P at position 38.
+The protein's natural variant, known as in VP; strongly decreases enzyme activity; impairs protein folding and/or stability, features a modification of the amino acid from G to A at position 40.
+The protein's natural variant, known as in VP; abolishes enzyme activity; impairs protein folding and/or stability;, features a modification of the amino acid from G to E at position 40.
+The protein's natural variant, known as in VP;, features a modification of the amino acid from G to R at position 57.
+The protein's natural variant, known as in VP; strongly decreases enzyme activity; does not affect mitochondrial protein targeting and localization; more resistant to thermal denaturation than wild-type enzyme;, features a modification of the amino acid from R to W at position 59.
+The protein's natural variant, known as in VP; strongly decreases enzyme activity; impairs protein folding and/or stability, features a modification of the amino acid from L to P at position 73.
+The protein's natural variant, known as in VP; decreases enzyme activity, features a modification of the amino acid from S to F at position 76.
+The protein's natural variant, known as in VP; strongly decreases enzyme activity; impairs protein folding and/or stability, features a modification of the amino acid from V to G at position 84.
+The protein's natural variant, known as in VP; abolishes enzyme activity; impairs protein folding and/or stability, features a modification of the amino acid from L to P at position 85.
+The protein's natural variant, known as in VP; strongly decreases enzyme activity, features a modification of the amino acid from H to P at position 106.
+The protein's natural variant, known as in VP; slightly decreases enzyme activity;, features a modification of the amino acid from R to P at position 138.
+The protein's natural variant, known as in VP; strongly decreases enzyme activity;, features a modification of the amino acid from G to D at position 139.
+The protein's natural variant, known as in VP; strongly decreases enzyme activity, features a modification of the amino acid from D to V at position 143.
+The protein's natural variant, known as in VP; strongly decreases enzyme activity, features a modification of the amino acid from R to C at position 152.
+The protein's natural variant, known as in VP; strongly decreases enzyme activity, features a modification of the amino acid from L to P at position 154.
+The protein's natural variant, known as in VP, features a modification of the amino acid from V to L at position 158.
+The protein's natural variant, known as in VP; strongly decreases enzyme activity, features a modification of the amino acid from V to M at position 158.
+The protein's natural variant, known as in VP; strongly decreases enzyme activity; does not affect mitochondrial protein targeting and localization;, features a modification of the amino acid from R to C at position 168.
+The protein's natural variant, known as in VP; strongly decreases enzyme activity;, features a modification of the amino acid from R to H at position 168.
+The protein's natural variant, known as in VP; strongly decreases enzyme activity, features a modification of the amino acid from G to E at position 169.
+The protein's natural variant, known as in VP, features a modification of the amino acid from A to V at position 172.
+The protein's natural variant, known as in VP; strongly decreases enzyme activity;, features a modification of the amino acid from L to V at position 178.
+The protein's natural variant, known as in VP; no effect on enzyme activity, features a modification of the amino acid from A to V at position 205.
+The protein's natural variant, known as in VP; decreases enzyme activity; impairs protein folding and/or stability;, features a modification of the amino acid from R to C at position 217.
+The protein's natural variant, known as in VP; abolishes enzyme activity; impairs protein folding and/or stability, features a modification of the amino acid from W to G at position 224.
+The protein's natural variant, known as in VP, features a modification of the amino acid from W to R at position 224.
+The protein's natural variant, known as in VP; strongly decreases enzyme activity; impairs protein folding and/or stability;, features a modification of the amino acid from G to R at position 232.
+The protein's natural variant, known as in VP, features a modification of the amino acid from G to S at position 232.
+The protein's natural variant, known as in VP, features a modification of the amino acid from L to S at position 236.
+The protein's natural variant, known as found in patients with the homozygous variant of variegate porphyria; unknown pathological significance; results in reduction of activity in a prokariotyc expression system but has normal activity when expressed in an eukaryotic system;, features a modification of the amino acid from P to R at position 256.
+The protein's natural variant, known as in VP; strongly decreases enzyme activity; impairs protein folding and/or stability, features a modification of the amino acid from V to D at position 282.
+The protein's natural variant, known as in VP; strongly decreases enzyme activity; impairs protein folding and/or stability, features a modification of the amino acid from I to N at position 283.
+The protein's natural variant, known as in VP, features a modification of the amino acid from V to M at position 290.
+The protein's natural variant, known as in VP; strongly decreases enzyme activity; impairs protein folding and/or stability, features a modification of the amino acid from L to P at position 295.
+The protein's natural variant, known as in VP; strongly decreases enzyme activity, features a modification of the amino acid from G to R at position 330.
+The protein's natural variant, known as in VP; abolishes activity; impairs protein folding and/or stability, features a modification of the amino acid from G to A at position 332.
+The protein's natural variant, known as in VP; strongly decreases enzyme activity; impairs protein folding and/or stability, features a modification of the amino acid from V to G at position 335.
+The protein's natural variant, known as in VP; results in enzyme activity decrease; impairs protein folding and/or stability; more resistant to thermal denaturation than wild-type enzyme;, features a modification of the amino acid from Y to C at position 348.
+The protein's natural variant, known as in VP; decreases enzyme activity;, features a modification of the amino acid from D to A at position 349.
+The protein's natural variant, known as in VP; abolishes activity; impairs protein folding and/or stability, features a modification of the amino acid from S to P at position 350.
+The protein's natural variant, known as in VP; strongly decreases enzyme activity; impairs protein folding and/or stability;, features a modification of the amino acid from G to R at position 358.
+The protein's natural variant, known as in VP; strongly decreases enzyme activity; impairs protein folding and/or stability;, features a modification of the amino acid from A to D at position 397.
+The protein's natural variant, known as in VP; strongly decreases enzyme activity;, features a modification of the amino acid from L to F at position 401.
+The protein's natural variant, known as in VP, features a modification of the amino acid from P to R at position 420.
+The protein's natural variant, known as in VP; decreases enzyme activity, features a modification of the amino acid from Y to C at position 422.
+The protein's natural variant, known as in VP; decreases enzyme activity; impairs protein folding and/or stability;, features a modification of the amino acid from A to P at position 433.
+The protein's natural variant, known as in VP; strongly decreases enzyme activity, features a modification of the amino acid from L to P at position 444.
+The protein's natural variant, known as in VP; abolishes enzyme activity; impairs protein folding and/or stability, features a modification of the amino acid from G to R at position 448.
+The protein's natural variant, known as in VP; strongly decreases enzyme activity, features a modification of the amino acid from S to P at position 450.
+The protein's natural variant, known as in VP; strongly decreases enzyme activity;, features a modification of the amino acid from G to R at position 453.
+The protein's natural variant, known as in VP, features a modification of the amino acid from G to V at position 453.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 28.
+The protein's natural variant, known as in strain: Isolate SIM7, features a modification of the amino acid from S to L at position 78.
+The protein's natural variant, known as in strain: Isolate SIM1, Isolate SIM3 and Isolate SIM6, features a modification of the amino acid from E to D at position 146.
+The protein's natural variant, known as in strain: Isolate SIM3 and Isolate SIM6, features a modification of the amino acid from Y to F at position 150.
+The protein's natural variant, known as in strain: Isolate SIM3, Isolate SIM6 and Isolate SIM7, features a modification of the amino acid from G to S at position 195.
+The protein's natural variant, known as in strain: Isolate SIM3, Isolate SIM6 and Isolate SIM7, features a modification of the amino acid from L to M at position 232.
+The protein's natural variant, known as in strain: Isolate SIM3, Isolate SIM6 and Isolate SIM7, features a modification of the amino acid from S to A at position 285.
+The protein's natural variant, known as in strain: Isolate SIM7, features a modification of the amino acid from P to L at position 304.
+The protein's natural variant, known as in strain: Isolate SIM1, Isolate SIM3 and Isolate SIM6, features a modification of the amino acid from M to I at position 355.
+The protein's natural variant, known as in strain: Oregon-R and Berkeley, features a modification of the amino acid from P to S at position 246.
+The protein's natural variant, known as in strain: Oregon-R and Berkeley, features a modification of the amino acid from P to Q at position 303.
+The protein's natural variant, known as in PCH1C;, features a modification of the amino acid from A to V at position 2.
+The protein's natural variant, known as in PCH1C;, features a modification of the amino acid from S to T at position 272.
+The protein's natural variant, known as in CDG1M; 2% residual dolichol kinase activity; fails to complement the temperature-sensitive phenotype of DK1-deficient yeast cells;, features a modification of the amino acid from C to S at position 99.
+The protein's natural variant, known as in CDG1M; 4% residual dolichol kinase activity; fails to complement the temperature-sensitive phenotype of DK1-deficient yeast cells;, features a modification of the amino acid from Y to S at position 441.
+The protein's natural variant, known as in MRD66; decreased calcium ion export across plasma membrane; decreased localization to plasma membrane, features a modification of the amino acid from D to G at position 239.
+The protein's natural variant, known as in MRD66; decreased calcium ion export across plasma membrane; decreased localization to plasma membrane, features a modification of the amino acid from T to I at position 264.
+The natural variant of this protein is characterized by an amino acid alteration from M to R at position 267.
+The protein's natural variant, known as in MRD66; decreased calcium ion export across plasma membrane, features a modification of the amino acid from T to K at position 425.
+The protein's natural variant, known as in MRD66; decreased calcium ion export across plasma membrane, features a modification of the amino acid from H to R at position 459.
+The protein's natural variant, known as found in a patient with developmental delay; unknown pathological significance; no effect on calcium ion export across plasma membrane, features a modification of the amino acid from I to T at position 598.
+The protein's natural variant, known as in MRD66; decreased calcium ion export across plasma membrane, features a modification of the amino acid from R to P at position 763.
+The protein's natural variant, known as no effect on calcium ion export across plasma membrane;, features a modification of the amino acid from G to S at position 779.
+The protein's natural variant, known as in MRD66; decreased calcium ion export across plasma membrane, features a modification of the amino acid from R to C at position 789.
+The protein's natural variant, known as in MRD66; decreased calcium ion export across plasma membrane, features a modification of the amino acid from E to K at position 824.
+The protein's natural variant, known as in MRD66; decreased calcium ion export across plasma membrane, features a modification of the amino acid from Q to R at position 857.
+The protein's natural variant, known as in MRD66; decreased calcium ion export across plasma membrane; decreased localization to plasma membrane, features a modification of the amino acid from R to Q at position 991.
+The protein's natural variant, known as in neamine-resistant mutant nea301, features a modification of the amino acid from H to P at position 31.
+The protein's natural variant, known as prevents 30S subunit assembly at 42 degrees Celsius, features a modification of the amino acid from S to F at position 68.
+The protein's natural variant, known as in strain: BKK11, BKK13, BKK16, BKK4, BKK5, BKK7 and BKK8, features a modification of the amino acid from E to A at position 373.
+The protein's natural variant, known as in strain: BKK9, features a modification of the amino acid from E to G at position 373.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from R to T at position 313.
+The protein's natural variant, known as in WSMN; loss of function mutation; expression of the mutation in neuroblastoma cells results in low levels of the mutant protein;, features a modification of the amino acid from T to K at position 168.
+The protein's natural variant, known as in WSMN; impaired localization to cytoplasmic vesicles;, features a modification of the amino acid from G to R at position 192.
+The protein's natural variant, known as in strain: 2001, features a modification of the amino acid from A to T at position 6.
+The protein's natural variant, known as in strain: Kronenbourg, Madibou4, Primus20, Primus25, ZH34 and ZH83, features a modification of the amino acid from N to H at position 24.
+The protein's natural variant, known as in strain: Kronenbourg, Madibou4, Primus20, Primus25, ZH34 and ZH83, features a modification of the amino acid from N to Y at position 70.
+The protein's natural variant, known as in strain: Kronenbourg, Madibou4, Primus20, Primus25, ZH34 and ZH83, features a modification of the amino acid from S to A at position 71.
+The protein's natural variant, known as in strain: AA1, features a modification of the amino acid from P to L at position 322.
+The protein's natural variant, known as in strain: KLH4 and KLH6, features a modification of the amino acid from S to T at position 327.
+The protein's natural variant, known as in strain: Reids2, features a modification of the amino acid from S to R at position 360.
+The protein's natural variant, known as in strain: 5-17-88b#5, features a modification of the amino acid from A to T at position 465.
+The protein's natural variant, known as in SCAN3;, features a modification of the amino acid from D to G at position 6.
+The protein's natural variant, known as in SCAN3; unknown pathological significance;, features a modification of the amino acid from R to W at position 39.
+The protein's natural variant, known as in SCAN3; results in increased proteasomal degradation; decreased protein levels; decreased amount of protein imported in the mitochondrion intermembrane space;, features a modification of the amino acid from Y to C at position 137.
+The protein's natural variant, known as in SCAN3; unknown pathological significance;, features a modification of the amino acid from S to I at position 149.
+The natural variant of this protein is characterized by an amino acid alteration from A to V at position 36.
+The natural variant of this protein is characterized by an amino acid alteration from A to D at position 70.
+The natural variant of this protein is characterized by an amino acid alteration from I to T at position 175.
+The protein's natural variant, known as in strain: SARC16 / s3014, features a modification of the amino acid from A to T at position 63.
+The protein's natural variant, known as in strain: SARC16 / s3014, features a modification of the amino acid from A to E at position 73.
+The protein's natural variant, known as in strain: SARC16 / s3014, features a modification of the amino acid from A to T at position 76.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 49.
+The natural variant of this protein is characterized by an amino acid alteration from M to K at position 245.
+The natural variant of this protein is characterized by an amino acid alteration from I to T at position 269.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 276.
+The natural variant of this protein is characterized by an amino acid alteration from C to S at position 299.
+The natural variant of this protein is characterized by an amino acid alteration from S to N at position 39.
+The protein's natural variant, known as in strain: cv. An-2 and cv. Su-0, features a modification of the amino acid from E to D at position 124.
+The protein's natural variant, known as in strain: cv. An-2 and cv. Su-0, features a modification of the amino acid from K to N at position 141.
+The protein's natural variant, known as in strain: cv. An-2 and cv. Su-0, features a modification of the amino acid from Q to H at position 176.
+The protein's natural variant, known as in strain: cv. An-2 and cv. Su-0, features a modification of the amino acid from Q to K at position 186.
+The protein's natural variant, known as in strain: cv. An-2 and cv. Su-0, features a modification of the amino acid from F to L at position 209.
+The protein's natural variant, known as in strain: cv. An-2 and cv. Su-0, features a modification of the amino acid from T to I at position 220.
+The protein's natural variant, known as in strain: cv. An-2 and cv. Su-0, features a modification of the amino acid from V to I at position 236.
+The protein's natural variant, known as in BVSYS; the mutation impairs interaction with the Mediator complex;, features a modification of the amino acid from Y to C at position 39.
+The protein's natural variant, known as found in a patient with syndromic intellectual disability; unknown pathological significance;, features a modification of the amino acid from R to W at position 140.
+The protein's natural variant, known as in CMT2B2;, features a modification of the amino acid from A to V at position 335.
+The protein's natural variant, known as in NEDHCAS;, features a modification of the amino acid from S to F at position 53.
+The protein's natural variant, known as in NEDHCAS; unknown pathological significance, features a modification of the amino acid from L to P at position 86.
+The protein's natural variant, known as in NEDHCAS;, features a modification of the amino acid from A to V at position 87.
+The protein's natural variant, known as in NEDHCAS;, features a modification of the amino acid from D to N at position 88.
+The protein's natural variant, known as in NEDHCAS;, features a modification of the amino acid from Y to S at position 160.
+The protein's natural variant, known as in NEDHCAS; unknown pathological significance;, features a modification of the amino acid from A to V at position 184.
+The protein's natural variant, known as in NEDHCAS; unknown pathological significance, features a modification of the amino acid from M to K at position 246.
+The protein's natural variant, known as in NEDHCAS;, features a modification of the amino acid from C to R at position 275.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from P to L at position 434.
+The protein's natural variant, known as in CVA16-4, features a modification of the amino acid from S to T at position 3.
+The protein's natural variant, known as in isoform 2, features a modification of the amino acid from P to A at position 2.
+The protein's natural variant, known as in isoform 2, features a modification of the amino acid from S to C at position 43.
+The protein's natural variant, known as in isoform 2, features a modification of the amino acid from V to L at position 74.
+The protein's natural variant, known as in MEOAL; unknown pathological significance; expressed at low levels in fibroblasts and muscles from a homozygous patient;, features a modification of the amino acid from M to L at position 4.
+The protein's natural variant, known as in MEOAL; strongly reduced protein expression in muscle in affected homozygous patients compared to control individuals;, features a modification of the amino acid from P to L at position 144.
+The protein's natural variant, known as in strain: J106, features a modification of the amino acid from K to N at position 109.
+The protein's natural variant, known as in MRCH-III, features a modification of the amino acid from L to PL at position 126.
+The protein's natural variant, known as in strain: Daizo and J106, features a modification of the amino acid from M to I at position 139.
+The protein's natural variant, known as in strain: J106, features a modification of the amino acid from E to V at position 146.
+The protein's natural variant, known as probable disease-associated variant found in patients with atrial fibrillation; gain of function; no effect on subcellular localization;, features a modification of the amino acid from P to S at position 91.
+The protein's natural variant, known as probable disease-associated variant found in patients with atrial fibrillation; gain of function; no effect on subcellular localization;, features a modification of the amino acid from A to T at position 177.
+The protein's natural variant, known as in AVSD5; increased transcriptional activity;, features a modification of the amino acid from A to V at position 178.
+The protein's natural variant, known as in ASD9 and TOF; loss of transcriptional activity;, features a modification of the amino acid from S to N at position 184.
+The protein's natural variant, known as in TOF; uncertain pathological significance; does not affect transcriptional activity;, features a modification of the amino acid from L to V at position 198.
+The protein's natural variant, known as probable disease-associated variant found in patients with atrial fibrillation; significant loss of transcriptional activator activity, features a modification of the amino acid from Y to S at position 235.
+The protein's natural variant, known as in PACHD;, features a modification of the amino acid from T to A at position 452.
+The protein's natural variant, known as in PACHD; loss of transcriptional activity;, features a modification of the amino acid from R to C at position 456.
+The protein's natural variant, known as in PACHD;, features a modification of the amino acid from R to H at position 456.
+The protein's natural variant, known as in PACHD; loss of transcriptional activity;, features a modification of the amino acid from N to D at position 466.
+The protein's natural variant, known as in CTHM; persistent truncus arteriosus; loss of transcriptional activity;, features a modification of the amino acid from N to H at position 466.
+The protein's natural variant, known as in PACHD; loss of transcriptional activity;, features a modification of the amino acid from A to T at position 467.
+The protein's natural variant, known as probable disease-associated variant found in patients with atrial fibrillation; significant loss of transcriptional activator activity, features a modification of the amino acid from G to V at position 469.
+The protein's natural variant, known as in PACHD; loss of transcriptional activity, features a modification of the amino acid from K to Q at position 473.
+The protein's natural variant, known as probable disease-associated variant found in patients with atrial fibrillation; gain of function; no effect on subcellular localization;, features a modification of the amino acid from A to G at position 543.
+The protein's natural variant, known as probable disease-associated variant found in patients with atrial fibrillation; gain of function; no effect on subcellular localization;, features a modification of the amino acid from R to L at position 585.
+The natural variant of this protein is characterized by an amino acid alteration from A to T at position 53.
+The natural variant of this protein is characterized by an amino acid alteration from F to L at position 5.
+The natural variant of this protein is characterized by an amino acid alteration from L to I at position 6.
+The natural variant of this protein is characterized by an amino acid alteration from S to P at position 22.
+The natural variant of this protein is characterized by an amino acid alteration from P to L at position 64.
+The natural variant of this protein is characterized by an amino acid alteration from E to K at position 82.
+The natural variant of this protein is characterized by an amino acid alteration from L to M at position 88.
+The natural variant of this protein is characterized by an amino acid alteration from H to Q at position 94.
+The natural variant of this protein is characterized by an amino acid alteration from A to D at position 118.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 123.
+The natural variant of this protein is characterized by an amino acid alteration from V to A at position 137.
+The natural variant of this protein is characterized by an amino acid alteration from R to K at position 140.
+The protein's natural variant, known as in hevamine-B, features a modification of the amino acid from L to R at position 296.
+The protein's natural variant, known as in hevamine-B, features a modification of the amino acid from E to K at position 306.
+The protein's natural variant, known as impaired response to androstenone and androstadienone;, features a modification of the amino acid from P to L at position 79.
+The protein's natural variant, known as high sensitivity to androstenone and androstadienone;, features a modification of the amino acid from S to N at position 84.
+The protein's natural variant, known as impaired response to androstenone and androstadienone; when associated with M-133;, features a modification of the amino acid from R to W at position 88.
+The protein's natural variant, known as impaired response to androstenone and androstadienone; when associated with W-88;, features a modification of the amino acid from T to M at position 133.
+The protein's natural variant, known as in AH1; partial loss of activity;, features a modification of the amino acid from E to G at position 169.
+The protein's natural variant, known as in AH1; partial loss of activity;, features a modification of the amino acid from E to K at position 169.
+The protein's natural variant, known as in AH1; partial loss of activity;, features a modification of the amino acid from R to L at position 182.
+The protein's natural variant, known as in AH1;, features a modification of the amino acid from R to T at position 217.
+The protein's natural variant, known as in AH1; partial loss of activity;, features a modification of the amino acid from A to V at position 218.
+The protein's natural variant, known as in AH1;, features a modification of the amino acid from M to T at position 225.
+The protein's natural variant, known as in AH1; partial loss of activity;, features a modification of the amino acid from L to P at position 275.
+The protein's natural variant, known as in RP92; unknown pathological significance; slightly decreased hexokinase activity;, features a modification of the amino acid from T to M at position 58.
+The natural variant of this protein is characterized by an amino acid alteration from R to K at position 51.
+The natural variant of this protein is characterized by an amino acid alteration from R to K at position 52.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from E to D at position 996.
+The natural variant of this protein is characterized by an amino acid alteration from V to L at position 230.
+The protein's natural variant, known as in SMALED2A; causes Golgi fragmentation; affects interaction with RAB6A and DNAI1 and the subcellular location of the protein;, features a modification of the amino acid from S to L at position 107.
+The protein's natural variant, known as in SMALED2A; causes Golgi fragmentation;, features a modification of the amino acid from N to T at position 188.
+The protein's natural variant, known as in SMALED2A;, features a modification of the amino acid from I to F at position 189.
+The protein's natural variant, known as in SMALED2B;, features a modification of the amino acid from Q to R at position 194.
+The protein's natural variant, known as in SMALED2A; the mutation causes increased interaction with dynein; the mutant protein accumulates abnormally in the perinuclear region where it forms ring-like structures that colocalize with RAB6A;, features a modification of the amino acid from R to P at position 501.
+The protein's natural variant, known as in SMALED2A;, features a modification of the amino acid from K to T at position 508.
+The protein's natural variant, known as in SMALED2B, features a modification of the amino acid from C to W at position 542.
+The protein's natural variant, known as in SMALED2B;, features a modification of the amino acid from R to C at position 694.
+The protein's natural variant, known as in SMALED2A; causes Golgi fragmentation;, features a modification of the amino acid from T to M at position 703.
+The protein's natural variant, known as in SMALED2A; affects interaction with RAB6A and DNAI1 and the subcellular location of the protein;, features a modification of the amino acid from E to G at position 774.
+The protein's natural variant, known as in allele Thy-1.1, features a modification of the amino acid from Q to R at position 108.
+The protein's natural variant, known as de novo variant found in a patient with intellectual disability;, features a modification of the amino acid from L to F at position 178.
+The protein's natural variant, known as in BACD1; unknown pathological significance; contrary to wild-type, undetectable expression in hepatocytes, features a modification of the amino acid from D to V at position 69.
+The protein's natural variant, known as in BACD1;, features a modification of the amino acid from M to V at position 76.
+The protein's natural variant, known as in BACD1; unknown pathological significance, features a modification of the amino acid from P to T at position 84.
+The protein's natural variant, known as in BACD1; unknown pathological significance; contrary to wild-type, undetectable expression in hepatocytes, features a modification of the amino acid from G to R at position 386.
+The natural variant of this protein is characterized by an amino acid alteration from N to D at position 73.
+The natural variant of this protein is characterized by an amino acid alteration from T to M at position 234.
+The natural variant of this protein is characterized by an amino acid alteration from W to G at position 281.
+The natural variant of this protein is characterized by an amino acid alteration from T to M at position 291.
+The natural variant of this protein is characterized by an amino acid alteration from L to M at position 368.
+The protein's natural variant, known as in strain: B, features a modification of the amino acid from G to D at position 264.
+The protein's natural variant, known as in strain: B, features a modification of the amino acid from Q to K at position 351.
+The natural variant of this protein is characterized by an amino acid alteration from M to MADAPKEGRLTRFLDFTQLM at position 1.
+The protein's natural variant, known as in strain: A2-M8; confers resistance to the allylamine antifungal terbinafine, features a modification of the amino acid from L to F at position 251.
+The protein's natural variant, known as in strain: cv. Lisse, features a modification of the amino acid from L to I at position 114.
+The protein's natural variant, known as in strain: cv. Bretagny, features a modification of the amino acid from Y to F at position 244.
+The protein's natural variant, known as in SVIA-1, SVIA-2 and SVIA-5, features a modification of the amino acid from S to P at position 51.
+The protein's natural variant, known as in SVIA-4, features a modification of the amino acid from S to P at position 54.
+The protein's natural variant, known as in SVIA-3, features a modification of the amino acid from P to S at position 55.
+The protein's natural variant, known as in SVIA-5, features a modification of the amino acid from T to A at position 59.
+The protein's natural variant, known as in SVIA-2 and SVIA-5, features a modification of the amino acid from Y to S at position 67.
+The protein's natural variant, known as in nusB5; abolishes antitermination, features a modification of the amino acid from Y to D at position 18.
+The protein's natural variant, known as found in a patient with developmental delay, hypotonia since birth and dysmorphic features such as triangular face, brachycephaly epicanthal fold, hypertelorism, broad nasal bridge and strabismus; unknown pathological significance, features a modification of the amino acid from E to K at position 661.
+The protein's natural variant, known as associated with higher plasma triglyceride concentration in subjects with hypercholesterolemia;, features a modification of the amino acid from G to S at position 2.
+The protein's natural variant, known as mutation carriers have increased HDL cholesterol levels and a reduction in cholesterol efflux from macrophages;, features a modification of the amino acid from P to S at position 297.
+The protein's natural variant, known as rare variant; associated with high HDL-cholesterol levels and increased risk for coronary heart disease; results in highly reduced cholesterol uptake from HDL; markedly reduced localization at the cell surface;, features a modification of the amino acid from P to L at position 376.
+The protein's natural variant, known as in SRTD8; does not affect interaction with DYNC2I2;, features a modification of the amino acid from T to M at position 749.
+The natural variant of this protein is characterized by an amino acid alteration from P to S at position 182.
+The protein's natural variant, known as associated with thrombocytosis; results in altered MPL expression;, features a modification of the amino acid from K to N at position 39.
+The protein's natural variant, known as in CAMT;, features a modification of the amino acid from R to C at position 102.
+The protein's natural variant, known as in CAMT; loss of function; loss of membrane localization, impaired glycosylation;, features a modification of the amino acid from R to P at position 102.
+The protein's natural variant, known as in CAMT; loss of function;, features a modification of the amino acid from F to S at position 104.
+The protein's natural variant, known as in THCYT2; gain of function; loss of membrane localization, impaired glycosylation;, features a modification of the amino acid from P to L at position 106.
+The protein's natural variant, known as in CAMT;, features a modification of the amino acid from P to L at position 136.
+The protein's natural variant, known as in CAMT;, features a modification of the amino acid from W to R at position 154.
+The protein's natural variant, known as in CAMT, features a modification of the amino acid from R to L at position 257.
+The protein's natural variant, known as in CAMT;, features a modification of the amino acid from P to T at position 275.
+The protein's natural variant, known as in CAMT;, features a modification of the amino acid from W to C at position 435.
+The protein's natural variant, known as in THCYT2; activating mutation; induces MPL autonomous dimerization and signal activation in the absence of the ligand;, features a modification of the amino acid from S to N at position 505.
+The protein's natural variant, known as in MMM; somatic mutation; requires 2 nucleotide substitutions;, features a modification of the amino acid from W to K at position 515.
+The protein's natural variant, known as in THCYT2 and MMM; somatic mutation in myelofibrosis with myeloid metaplasia; results in cytokine-independent growth and thrombopoietin hypersensitivity; results in constitutive activation of JAK-STAT signaling pathway;, features a modification of the amino acid from W to L at position 515.
+The protein's natural variant, known as in CAMT;, features a modification of the amino acid from L to W at position 594.
+The protein's natural variant, known as confers resistance to cycloheximide, an inhibitor of polypeptide elongation, features a modification of the amino acid from P to Q at position 56.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from H to N at position 445.
+The protein's natural variant, known as in Ole e 1.0102, Ole e 1.0103 and Ole e 1.0105, features a modification of the amino acid from I to V at position 3.
+The protein's natural variant, known as in Ole e I.4, features a modification of the amino acid from V to I at position 8.
+The protein's natural variant, known as in Ole e I.4, features a modification of the amino acid from H to Y at position 12.
+The protein's natural variant, known as in strain: cv. Zard; variant 2. In Ole e I.4, features a modification of the amino acid from I to V at position 13.
+The protein's natural variant, known as in strain: cv. Bella de Espana; variants 1 and 2, cv. Loaime, cv. Lucio, cv. Menara; variants 1 and 2, cv. Picholine marocaine and cv. Picual; variant 1, features a modification of the amino acid from Q to I at position 14.
+The protein's natural variant, known as in strain: cv. Picual; variant 1, features a modification of the amino acid from G to L at position 15.
+The protein's natural variant, known as in strain: cv. Arbequina; variants 1 and 2 and cv. Bella de Espana; variant 3, features a modification of the amino acid from G to Q at position 15.
+The protein's natural variant, known as in strain: cv. Bella de Espana; variants 1 and 2, cv. Menara; variants 1 and 2 and cv. Picholine marocaine, features a modification of the amino acid from G to R at position 15.
+The protein's natural variant, known as in strain: cv. Picual; variant 3, features a modification of the amino acid from G to S at position 15.
+The protein's natural variant, known as in strain: cv. Loaime and cv. Picual; variant 2, features a modification of the amino acid from G to W at position 15.
+The protein's natural variant, known as in strain: cv. Arbequina; variant 1, features a modification of the amino acid from Q to A at position 16.
+The protein's natural variant, known as in strain: cv. Arbequina; variant 2, cv. Bella de Espana; variant 3 and cv. Picual; variant 3, features a modification of the amino acid from Q to D at position 16.
+The protein's natural variant, known as in strain: cv. Acebuche, features a modification of the amino acid from Q to R at position 16.
+The protein's natural variant, known as in strain: cv. Bella de Espana; variants 1 and 2, cv. Loaime, cv. Menara; variants 1 and 2, cv. Picholine marocaine and cv. Picual; variants 1 and 2, features a modification of the amino acid from Q to T at position 16.
+The protein's natural variant, known as in strain: cv. Rowghani; variant 3 and cv. Zard; variant 2, features a modification of the amino acid from V to I at position 17.
+The protein's natural variant, known as in strain: cv. Arbequina; variant 2, cv. Bella de Espana; variant 3, cv. Hojiblanca and cv. Picual; variant 3, features a modification of the amino acid from V to S at position 17.
+The protein's natural variant, known as in strain: cv. Acebuche, features a modification of the amino acid from V to T at position 17.
+The protein's natural variant, known as in strain: cv. Bella de Espana; variant 1, features a modification of the amino acid from Y to F at position 18.
+The protein's natural variant, known as in strain: cv. Menara; variant 2, features a modification of the amino acid from Y to H at position 18.
+The protein's natural variant, known as in strain: cv. Bella de Espana; variant 2 and cv. Picual; variant 2, features a modification of the amino acid from Y to S at position 18.
+The protein's natural variant, known as in strain: cv. Acebuche, features a modification of the amino acid from Y to V at position 18.
+The protein's natural variant, known as in strain: cv. Bella de Espana; variant 2, features a modification of the amino acid from C to Q at position 19.
+The protein's natural variant, known as in strain: cv. Arbequina; variant 2 and cv. Bella de Espana; variant 1, features a modification of the amino acid from C to R at position 19.
+The protein's natural variant, known as in strain: cv. Bella de Espana; variant 3, features a modification of the amino acid from C to S at position 19.
+The protein's natural variant, known as in strain: cv. Acebuche, features a modification of the amino acid from C to T at position 19.
+The protein's natural variant, known as in strain: cv. Acebuche and cv. Bella de Espana; variant 3, features a modification of the amino acid from D to G at position 20.
+The protein's natural variant, known as in strain: cv. Bella de Espana; variant 1, features a modification of the amino acid from D to V at position 20.
+The protein's natural variant, known as in strain: cv. Bella de Espana; variant 3, features a modification of the amino acid from T to H at position 21.
+The protein's natural variant, known as in strain: cv. Acebuche, features a modification of the amino acid from T to Y at position 21.
+The protein's natural variant, known as in strain: cv. Bella de Espana; variant 2, features a modification of the amino acid from R to C at position 23.
+The natural variant of this protein is characterized by an amino acid alteration from R to P at position 23.
+The protein's natural variant, known as in strain: cv. Rowghani; variant 3. In Ole e 1.0105, features a modification of the amino acid from A to S at position 24.
+The protein's natural variant, known as in Ole e I.4, features a modification of the amino acid from A to T at position 24.
+The protein's natural variant, known as in strain: cv. Bella de Espana; variants 1, 2 and 3 and cv. Rowghani; variants 3 and 4. In Ole e 1.0105, Ole e I.3 and Ole e I.4, features a modification of the amino acid from G to R at position 25.
+The protein's natural variant, known as in strain: cv. Zard; variant 2; 50% loss of IgG binding, features a modification of the amino acid from T to A at position 28.
+The protein's natural variant, known as in Ole e I.4, features a modification of the amino acid from L to F at position 30.
+The protein's natural variant, known as in strain: cv. Zard; variant 2, features a modification of the amino acid from P to L at position 35.
+The protein's natural variant, known as in strain: cv. Bella de Espana; variants 1, 2 and 3, cv. Hojiblanca and cv. Zard; variant 2. In Ole e I.4, features a modification of the amino acid from S to G at position 38.
+The protein's natural variant, known as in strain: cv. Arbequina; variants 1 and 2, cv. Bella de Espana; variants 1, 2 and 3, cv. Hojiblanca, cv. Loaime, cv. Lucio, cv. Menara; variants 1 and 2, cv. Picholine marocaine, cv. Picual; variants 1 and 2, cv. Rowghani; variants 2, 3 and 4 and cv. Zard; variants 1 and 2. In Ole e 1.0102, Ole e 1.0103, Ole e 1.0105, Ole e I.3 and Ole e I.4, features a modification of the amino acid from L to V at position 39.
+The protein's natural variant, known as in strain: cv. Rowghani; variants 2, 3 and 4 and cv. Zard; variants 1 and 2. In Ole e 1.0105, features a modification of the amino acid from K to R at position 44.
+The protein's natural variant, known as in strain: cv. Zard; variant 1 and cv. Rowghani; variants 2 and 3. In Ole e 1.0105, features a modification of the amino acid from D to E at position 45.
+The protein's natural variant, known as in strain: cv. Bella de Espana; variants 1, 2 and 3, cv. Hojiblanca and cv. Rowghani; variant 4. In Ole e I.3 and Ole e I.4, features a modification of the amino acid from K to G at position 46.
+The natural variant of this protein is characterized by an amino acid alteration from K to I at position 46.
+The protein's natural variant, known as in strain: cv. Arbequina; variants 1 and 2, features a modification of the amino acid from K to R at position 46.
+The protein's natural variant, known as in strain: cv. Zard; variant 2, features a modification of the amino acid from K to S at position 46.
+The protein's natural variant, known as in strain: cv. Rowghani; variant 2 and cv. Zard; variants 1 and 2, features a modification of the amino acid from E to K at position 47.
+The protein's natural variant, known as in strain: cv. Zard; variant 2, features a modification of the amino acid from N to K at position 48.
+The protein's natural variant, known as in Ole e I.4, features a modification of the amino acid from D to K at position 50.
+The protein's natural variant, known as in strain: cv. Bella de Espana; variants 1, 2 and 3, cv. Hojiblanca and cv. Zard; variant 2, features a modification of the amino acid from D to N at position 50.
+The protein's natural variant, known as in strain: cv. Rowghani; variant 4. In Ole e I.3, features a modification of the amino acid from D to S at position 50.
+The protein's natural variant, known as in strain: cv. Arbequina; variants 1 and 2, cv. Hojiblanca, cv. Loaime, cv. Lucio, cv. Menara; variants 1 and 2, cv. Picholine marocaine, cv. Picual; variants 1 and 2, cv. Rowghani, variants 2, 3 and 4 and cv. Zard; variants 1 and 2. In Ole e 1.0105, Ole e I.3 and Ole e I.4, features a modification of the amino acid from V to I at position 51.
+The protein's natural variant, known as in strain: cv. Rowghani; variant 3. In Ole e 1.0102, 1.0103 and 1.0105, features a modification of the amino acid from V to I at position 56.
+The protein's natural variant, known as in strain: cv. Rowghani; variant 4, features a modification of the amino acid from Y to S at position 58.
+The protein's natural variant, known as in strain: cv. Bella de Espana; variants 1, 2 and 3, cv. Rowghani; variant 4 and cv. Zard; variant 2. In Ole e I.3 and Ole e I.4, features a modification of the amino acid from V to I at position 69.
+The protein's natural variant, known as in strain: cv. Rowghani; variant 4. In Ole e I.3, features a modification of the amino acid from N to D at position 75.
+The protein's natural variant, known as in strain: cv. Zard; variant 2, features a modification of the amino acid from I to V at position 80.
+The protein's natural variant, known as in strain: cv. Zard; variant 2, features a modification of the amino acid from T to N at position 81.
+The protein's natural variant, known as in strain: cv. Zard; variant 2, features a modification of the amino acid from L to S at position 82.
+The protein's natural variant, known as in strain: cv. Bella de Espana; variants 1, 2 and 3 and cv. Zard; variant 2. In Ole e I.4, features a modification of the amino acid from I to L at position 83.
+The protein's natural variant, known as in strain: cv. Bella de Espana; variants 1, 2 and 3, cv. Rowghani; variant 4 and cv. Zard; variant 2. In Ole e I.3 and Ole e I.4, features a modification of the amino acid from G to S at position 86.
+The natural variant of this protein is characterized by an amino acid alteration from R to S at position 87.
+The protein's natural variant, known as in strain: cv. Arbequina; variants 1 and 2, cv. Bella de Espana; variants 1, 2 and 3, cv. Hojiblanca, cv. Loaime, cv. Picual; variants 1 and 2, cv. Rowghani; variants 3 and 4 and cv. Zard; variant 2. In Ole e 1.0105, Ole e I.3 and Ole e I.4, features a modification of the amino acid from N to D at position 91.
+The protein's natural variant, known as in strain: cv. Rowghani; variant 3 and cv. Zard; variant 2. In Ole e 1.0105, features a modification of the amino acid from T to I at position 95.
+The protein's natural variant, known as in strain: cv. Bella de Espana; variants 1, 2 and 3 and cv. Rowghani; variant 4. In Ole e I.3, features a modification of the amino acid from T to V at position 95.
+The protein's natural variant, known as in strain: cv. Acebuche, cv. Arbequina; variants 1 and 2, cv. Bella de Espana; variants 1, 2 and 3, cv. Hojiblanca, cv. Picual; variant 3, cv. Rowghani; variants 1 and 4 and cv. Zard; variant 2. In Ole e I.2, Ole e I.3 and Ole e I.4, features a modification of the amino acid from A to V at position 99.
+The protein's natural variant, known as in strain: cv. Zard; variant 2, features a modification of the amino acid from K to R at position 100.
+The protein's natural variant, known as in Ole e I.4, features a modification of the amino acid from L to V at position 103.
+The protein's natural variant, known as in strain: cv. Zard; variant 2, features a modification of the amino acid from K to R at position 104.
+The protein's natural variant, known as in strain: cv. Acebuche, cv. Arbequina; variant 1 and 2, cv. Hojiblanca, cv. Loaime, cv. Lucio, cv. Menara; variants 1 and 2, cv. Picholine marocaine, cv. Picual; variants 1, 2 and 3, cv. Rowghani; variants 1, 2 and 3 and cv. Zard; variant 1. In Ole e 1.0102, Ole e 1.0103, Ole e 1.0105, Ole e I.2 and Ole e I.4, features a modification of the amino acid from K to I at position 106.
+The protein's natural variant, known as in strain: cv. Zard; variant 2, features a modification of the amino acid from K to L at position 106.
+The protein's natural variant, known as in strain: cv. Bella de Espana; variants 1, 2 and 3 and cv. Rowghani; variant 4. In Ole e I.3, features a modification of the amino acid from K to M at position 106.
+The protein's natural variant, known as in Ole e 1.0103, features a modification of the amino acid from N to S at position 108.
+The natural variant of this protein is characterized by an amino acid alteration from N to D at position 111.
+The protein's natural variant, known as in strain: cv. Zard; variant 2, features a modification of the amino acid from R to C at position 115.
+The protein's natural variant, known as in strain: cv. Bella de Espana; variants 1, 2 and 3, cv. Hojiblanca, cv. Rowghani; variant 2 and cv. Zard; variants 1 and 2. In Ole e I.3 and Ole e I.4, features a modification of the amino acid from V to I at position 117.
+The protein's natural variant, known as in strain: cv. Zard; variant 2, features a modification of the amino acid from N to K at position 118.
+The protein's natural variant, known as in Ole e 1.0102, features a modification of the amino acid from G to R at position 121.
+The protein's natural variant, known as in strain: cv. Zard; variant 1 and cv. Rowghani; variant 2. In Ole e 1.0102 and Ole e 1.0103, features a modification of the amino acid from F to Y at position 123.
+The protein's natural variant, known as in strain: cv. Zard; variant 2, features a modification of the amino acid from K to N at position 125.
+The protein's natural variant, known as in strain: cv. Zard; variant 2, features a modification of the amino acid from E to K at position 126.
+The protein's natural variant, known as in strain: cv. Bella de Espana; variants 1, 2 and 3, cv. Rowghani; variant 4 and cv. Zard; variant 2. In Ole e I.3 and Ole e I.4, features a modification of the amino acid from A to P at position 132.
+The protein's natural variant, known as in strain: cv. Bella de Espana; variants 1, 2 and 3, cv. Rowghani; variant 4 and cv. Zard; variant 2. In Ole e I.3 and Ole e I.4, features a modification of the amino acid from Y to F at position 135.
+The protein's natural variant, known as in strain: cv. Rowghani; variant 2, features a modification of the amino acid from G to D at position 139.
+The protein's natural variant, known as in strain: cv. Bella de Espana; variants 1, 2 and 3, cv. Rowghani; variant 4 and cv. Zard; variant 2, features a modification of the amino acid from N to D at position 144.
+The protein's natural variant, known as in strain: cv. Picual; variant 3, features a modification of the amino acid from N to T at position 144.
+The protein's natural variant, known as in strain: cv. Acebuche, features a modification of the amino acid from M to HGMSR at position 145.
+The protein's natural variant, known as in strain: cv. Zard; variant 2, features a modification of the amino acid from M to L at position 145.
+The protein's natural variant, known as in strain: cv. Picual; variant 3, features a modification of the amino acid from M to WNVTI at position 145.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from S to C at position 552.
+The natural variant of this protein is characterized by an amino acid alteration from G to D at position 103.
+The natural variant of this protein is characterized by an amino acid alteration from N to T at position 318.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 331.
+The natural variant of this protein is characterized by an amino acid alteration from K to R at position 413.
+The protein's natural variant, known as in CRMCC2;, features a modification of the amino acid from R to T at position 135.
+The protein's natural variant, known as in CRMCC2;, features a modification of the amino acid from D to Y at position 157.
+The protein's natural variant, known as in strain: Z17561, features a modification of the amino acid from T to A at position 12.
+The protein's natural variant, known as in strain: Z17561, features a modification of the amino acid from I to L at position 23.
+The protein's natural variant, known as in strain: Z17561, features a modification of the amino acid from Q to E at position 95.
+The protein's natural variant, known as in strain: Z17561, features a modification of the amino acid from A to V at position 98.
+The protein's natural variant, known as in strain: Z17561, features a modification of the amino acid from L to Q at position 122.
+The protein's natural variant, known as in strain: cv. f02-04, features a modification of the amino acid from A to V at position 103.
+The protein's natural variant, known as in strain: cv. f02-04, features a modification of the amino acid from H to R at position 137.
+The protein's natural variant, known as in strain: cv. f02-04, features a modification of the amino acid from DFFKNED to NFFKTEN at position 177.
+The protein's natural variant, known as in strain: cv. f02-04, features a modification of the amino acid from R to K at position 262.
+The protein's natural variant, known as in strain: cv. f02-04, features a modification of the amino acid from I to V at position 268.
+The protein's natural variant, known as in strain: cv. f02-04, features a modification of the amino acid from S to P at position 450.
+The natural variant of this protein is characterized by an amino acid alteration from R to T at position 21.
+The protein's natural variant, known as in SPH1, features a modification of the amino acid from L to R at position 276.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from D to H at position 332.
+The protein's natural variant, known as in SPH1;, features a modification of the amino acid from V to I at position 463.
+The protein's natural variant, known as in Brueggen;, features a modification of the amino acid from R to H at position 619.
+The natural variant of this protein is characterized by an amino acid alteration from V to A at position 750.
+The natural variant of this protein is characterized by an amino acid alteration from D to E at position 845.
+The protein's natural variant, known as in SPH1, features a modification of the amino acid from I to T at position 1054.
+The natural variant of this protein is characterized by an amino acid alteration from E to D at position 1286.
+The natural variant of this protein is characterized by an amino acid alteration from S to T at position 1392.
+The protein's natural variant, known as in Duesseldorf;, features a modification of the amino acid from D to N at position 1592.
+The natural variant of this protein is characterized by an amino acid alteration from S to L at position 698.
+The protein's natural variant, known as found in a family with an early age of onset of diabetes; unknown pathological significance; reduced the stability and catalytic activity, features a modification of the amino acid from G to D at position 288.
+The natural variant of this protein is characterized by an amino acid alteration from T to I at position 215.
+The natural variant of this protein is characterized by an amino acid alteration from G to D at position 11.
+The natural variant of this protein is characterized by an amino acid alteration from P to G at position 12.
+The natural variant of this protein is characterized by an amino acid alteration from P to R at position 12.
+The natural variant of this protein is characterized by an amino acid alteration from Y to GY at position 13.
+The natural variant of this protein is characterized by an amino acid alteration from R to A at position 15.
+The natural variant of this protein is characterized by an amino acid alteration from H to A at position 22.
+The natural variant of this protein is characterized by an amino acid alteration from E to D at position 26.
+The natural variant of this protein is characterized by an amino acid alteration from Y to I at position 86.
+The natural variant of this protein is characterized by an amino acid alteration from A to V at position 101.
+The natural variant of this protein is characterized by an amino acid alteration from V to A at position 103.
+The natural variant of this protein is characterized by an amino acid alteration from I to A at position 106.
+The natural variant of this protein is characterized by an amino acid alteration from R to L at position 127.
+The natural variant of this protein is characterized by an amino acid alteration from D to N at position 134.
+The protein's natural variant, known as in COXPD1;, features a modification of the amino acid from S to Y at position 57.
+The protein's natural variant, known as in COXPD1;, features a modification of the amino acid from N to S at position 174.
+The protein's natural variant, known as in COXPD1;, features a modification of the amino acid from R to W at position 250.
+The protein's natural variant, known as in COXPD1;, features a modification of the amino acid from M to R at position 496.
+The protein's natural variant, known as in MT-20-IB, features a modification of the amino acid from S to A at position 66.
+The protein's natural variant, known as in DFNB28;, features a modification of the amino acid from G to R at position 1019.
+The protein's natural variant, known as increased light damage susceptibility, features a modification of the amino acid from M to L at position 450.
+The protein's natural variant, known as in strain: GN-8, features a modification of the amino acid from TT to LL at position 28.
+The protein's natural variant, known as in strain: GN-8, features a modification of the amino acid from D to A at position 42.
+The protein's natural variant, known as in strain: GN-8, features a modification of the amino acid from N to M at position 929.
+The protein's natural variant, known as in MC5DN3;, features a modification of the amino acid from Y to C at position 12.
+The natural variant of this protein is characterized by an amino acid alteration from E to G at position 51.
+The protein's natural variant, known as in CADASIL2, features a modification of the amino acid from S to R at position 121.
+The protein's natural variant, known as in CADASIL2, features a modification of the amino acid from A to S at position 123.
+The protein's natural variant, known as in CADASIL2, features a modification of the amino acid from R to G at position 133.
+The protein's natural variant, known as in CADASIL2; loss of proteolytic activity;, features a modification of the amino acid from R to L at position 166.
+The protein's natural variant, known as in CADASIL2; loss of proteolytic activity;, features a modification of the amino acid from A to P at position 173.
+The protein's natural variant, known as in CARASIL; has 21 to 50% normal protease activity; is unable to suppress TGF-beta activity;, features a modification of the amino acid from A to T at position 252.
+The protein's natural variant, known as in CADASIL2; partial loss of proteolytic activity, features a modification of the amino acid from S to G at position 284.
+The protein's natural variant, known as in CADASIL2; loss of proteolytic activity;, features a modification of the amino acid from S to R at position 284.
+The protein's natural variant, known as in CADASIL2; loss of proteolytic activity, features a modification of the amino acid from P to Q at position 285.
+The protein's natural variant, known as in CADASIL2; loss of proteolytic activity, features a modification of the amino acid from F to V at position 286.
+The protein's natural variant, known as in CARASIL; has 21 to 50% normal protease activity; is unable to suppress TGF-beta activity;, features a modification of the amino acid from V to M at position 297.
+The protein's natural variant, known as in CADASIL2; unknown pathological significance; small decrease, if any, in proteolytic activity;, features a modification of the amino acid from D to H at position 450.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from R to T at position 471.
+The protein's natural variant, known as in FEPS1; 5-fold increase in inward current when stimulated by the agonist cinnamaldehyde compared to wild-type at normal neuronal resting potential; consistent with a gain of function mutation;, features a modification of the amino acid from N to S at position 855.
+The protein's natural variant, known as in OLMS1; gain of function mutation; results in constitutive channel activation;, features a modification of the amino acid from G to C at position 573.
+The protein's natural variant, known as in OLMS1; gain of function mutation; results in constitutive channel activation;, features a modification of the amino acid from G to S at position 573.
+The protein's natural variant, known as in FNEPPK2; gain of function mutation;, features a modification of the amino acid from Q to P at position 580.
+The protein's natural variant, known as in OLMS1; gain of function mutation; results in constitutive channel activation;, features a modification of the amino acid from W to G at position 692.
+The protein's natural variant, known as in PVOD2;, features a modification of the amino acid from R to Q at position 585.
+The protein's natural variant, known as in PVOD2;, features a modification of the amino acid from L to R at position 643.
+The protein's natural variant, known as in a lung neuroendocrine carcinoma sample; somatic mutation, features a modification of the amino acid from H to Y at position 939.
+The protein's natural variant, known as in one allele, features a modification of the amino acid from V to A at position 127.
+The protein's natural variant, known as in strain: 3CPA81, features a modification of the amino acid from E to A at position 45.
+The protein's natural variant, known as in strain: 3CPA2, features a modification of the amino acid from K to R at position 74.
+The protein's natural variant, known as in strain: FrV3-1, features a modification of the amino acid from S to I at position 93.
+The protein's natural variant, known as in strain: 3CPA2, features a modification of the amino acid from S to G at position 135.
+The protein's natural variant, known as in strain: 3CPA2, features a modification of the amino acid from K to N at position 187.
+The protein's natural variant, known as in strain: AUS, features a modification of the amino acid from D to Y at position 210.
+The protein's natural variant, known as in strain: 3CPA43 and 3CPA81, features a modification of the amino acid from H to N at position 330.
+The protein's natural variant, known as in strain: 3CPA43, features a modification of the amino acid from P to S at position 342.
+The protein's natural variant, known as in strain: 3CPA43 and 3CPA81, features a modification of the amino acid from D to Y at position 458.
+The protein's natural variant, known as in strain: B28, features a modification of the amino acid from T to I at position 475.
+The protein's natural variant, known as in strain: 3CPA126, features a modification of the amino acid from S to P at position 601.
+The protein's natural variant, known as in strain: AUS, features a modification of the amino acid from G to R at position 634.
+The protein's natural variant, known as in XLID41; causes reduced binding and recycling of RAB3A;, features a modification of the amino acid from L to P at position 92.
+The protein's natural variant, known as in XLID41;, features a modification of the amino acid from R to P at position 423.
+The protein's natural variant, known as in strain: C57BL/6; contains an in-frame 33 bp imperfect duplication, features a modification of the amino acid from L to LEVSPVLPSSSL at position 1243.
+The natural variant of this protein is characterized by an amino acid alteration from A to P at position 2083.
+The protein's natural variant, known as in RP11; mislocation of the protein in the cytoplasm and reduced interaction with PRPF6; the result may be a deficiency in splicing function in the retina;, features a modification of the amino acid from A to E at position 194.
+The protein's natural variant, known as in RP11; mislocation of the protein in the cytoplasm, but no effect on interaction with PRPF6; the result may be a deficiency in splicing function in the retina;, features a modification of the amino acid from A to P at position 216.
+The protein's natural variant, known as in NNO2;, features a modification of the amino acid from I to T at position 182.
+The protein's natural variant, known as found in a patient with high hyperopia; unknown pathological significance;, features a modification of the amino acid from P to T at position 222.
+The protein's natural variant, known as requires 2 nucleotide substitutions, features a modification of the amino acid from S to D at position 259.
+The protein's natural variant, known as found in a patient with high hyperopia; unknown pathological significance;, features a modification of the amino acid from R to W at position 517.
+The protein's natural variant, known as found in a patient with high hyperopia; unknown pathological significance;, features a modification of the amino acid from R to C at position 539.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from I to M at position 292.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from M to L at position 647.
+The protein's natural variant, known as may influence risk for Lewy body disorders;, features a modification of the amino acid from P to L at position 2.
+The protein's natural variant, known as may influence risk for Lewy body disorders;, features a modification of the amino acid from G to R at position 4.
+The protein's natural variant, known as may influence risk for Lewy body disorders;, features a modification of the amino acid from P to S at position 14.
+The protein's natural variant, known as may influence risk for Lewy body disorders;, features a modification of the amino acid from P to L at position 34.
+The protein's natural variant, known as may influence risk for Lewy body disorders;, features a modification of the amino acid from A to V at position 37.
+The protein's natural variant, known as may influence risk for Lewy body disorders;, features a modification of the amino acid from A to V at position 49.
+The protein's natural variant, known as in PARK22; does not affect subcellular location;, features a modification of the amino acid from T to I at position 61.
+The protein's natural variant, known as may influence risk for Lewy body disorders;, features a modification of the amino acid from A to V at position 93.
+The protein's natural variant, known as in PARK22; unknown pathological significance; does not affect subcellular location;, features a modification of the amino acid from R to Q at position 145.
+The protein's natural variant, known as in ARVD11; unknown pathological significance;, features a modification of the amino acid from R to C at position 132.
+The protein's natural variant, known as in ARVD11; fails to undergo complete processing into a mature form; fails to localize at the desmosomes;, features a modification of the amino acid from R to C at position 203.
+The protein's natural variant, known as in ARVD11;, features a modification of the amino acid from I to T at position 231.
+The protein's natural variant, known as in ARVD11; can be processed into a mature form but shows a higher pro-protein to mature protein ratio; only a proportion of the partly functional mutant is incorporated into the desmosomes;, features a modification of the amino acid from T to M at position 275.
+The protein's natural variant, known as in ARVD11;, features a modification of the amino acid from T to A at position 340.
+The protein's natural variant, known as in ARVD11, features a modification of the amino acid from V to M at position 364.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to Q at position 498.
+The protein's natural variant, known as found in a child with spina bifida; unknown pathological significance; reduced induction of autophagy, features a modification of the amino acid from T to M at position 80.
+The protein's natural variant, known as found in a fetus with encephalocele; unknown pathological significance; reduced induction of autophagy, features a modification of the amino acid from L to F at position 364.
+The protein's natural variant, known as found in a child with spina bifida; unknown pathological significance; reduced induction of autophagy, features a modification of the amino acid from S to F at position 833.
+The protein's natural variant, known as found in a fetus with encephalocele and spina bifida; unknown pathological significance; reduced induction of autophagy, features a modification of the amino acid from M to V at position 974.
+The protein's natural variant, known as found in a fetus with anencephaly and spina bifida; unknown pathological significance; does not impair induction of autophagy, features a modification of the amino acid from S to F at position 1043.
+The protein's natural variant, known as in HOMG2; fails to localize to plasma membrane;, features a modification of the amino acid from G to R at position 41.
+The protein's natural variant, known as in strain: AM30, features a modification of the amino acid from G to S at position 104.
+The protein's natural variant, known as in DBPD; no dehydrogenase activity;, features a modification of the amino acid from G to S at position 16.
+The protein's natural variant, known as in DBPD;, features a modification of the amino acid from R to P at position 106.
+The protein's natural variant, known as in PRLTS1;, features a modification of the amino acid from Y to C at position 217.
+The protein's natural variant, known as in DBPD; the mutation leads to an unstable protein;, features a modification of the amino acid from N to Y at position 457.
+The natural variant of this protein is characterized by an amino acid alteration from A to I at position 53.
+The natural variant of this protein is characterized by an amino acid alteration from LR to IV at position 82.
+The natural variant of this protein is characterized by an amino acid alteration from W to E at position 85.
+The natural variant of this protein is characterized by an amino acid alteration from S to V at position 92.
+The natural variant of this protein is characterized by an amino acid alteration from V to L at position 94.
+The natural variant of this protein is characterized by an amino acid alteration from N to T at position 124.
+The natural variant of this protein is characterized by an amino acid alteration from Q to L at position 128.
+The natural variant of this protein is characterized by an amino acid alteration from E to V at position 132.
+The natural variant of this protein is characterized by an amino acid alteration from KS to AA at position 139.
+The natural variant of this protein is characterized by an amino acid alteration from D to G at position 142.
+The natural variant of this protein is characterized by an amino acid alteration from IK to VR at position 154.
+The natural variant of this protein is characterized by an amino acid alteration from A to L at position 163.
+The natural variant of this protein is characterized by an amino acid alteration from K to G at position 165.
+The protein's natural variant, known as in strain: W, features a modification of the amino acid from G to E at position 75.
+The protein's natural variant, known as in strain: W, features a modification of the amino acid from I to V at position 179.
+The protein's natural variant, known as in strain: W, features a modification of the amino acid from G to N at position 182.
+The protein's natural variant, known as in BHC; decrease in DNA-binding; no effect on transcription activation from thyroglobulin/TG, nor from pulmonary surfactant-associated protein C/SFTPC gene promoters, features a modification of the amino acid from Q to H at position 172.
+The protein's natural variant, known as in BHC; unknown pathological significance, features a modification of the amino acid from R to P at position 179.
+The protein's natural variant, known as in CAHTP, features a modification of the amino acid from T to R at position 203.
+The protein's natural variant, known as in CAHTP;, features a modification of the amino acid from V to F at position 205.
+The protein's natural variant, known as in BHC;, features a modification of the amino acid from W to L at position 208.
+The protein's natural variant, known as in BHC; loss of transcription activation, features a modification of the amino acid from W to S at position 208.
+The protein's natural variant, known as in BHC;, features a modification of the amino acid from R to S at position 213.
+The protein's natural variant, known as in NMTC1; loss of transcription regulatory region DNA binding; decreased transcription factor activity, sequence-specific DNA binding; tested for the thyroglobulin gene; associated with dominant impairment of thyroid-specific genes transcription and increased thyroid cells proliferation;, features a modification of the amino acid from A to V at position 339.
+The protein's natural variant, known as in strain: canine, features a modification of the amino acid from Q to A at position 3.
+The protein's natural variant, known as in strain: canine, features a modification of the amino acid from GDL to VEF at position 12.
+The protein's natural variant, known as in strain: canine, features a modification of the amino acid from W to L at position 15.
+The protein's natural variant, known as in strain: canine, features a modification of the amino acid from ID to AE at position 18.
+The protein's natural variant, known as in strain: canine, features a modification of the amino acid from N to E at position 21.
+The protein's natural variant, known as in strain: canine, features a modification of the amino acid from T to I at position 24.
+The protein's natural variant, known as in a gastric adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from L to P at position 291.
+The protein's natural variant, known as in a gastric adenocarcinoma sample; somatic mutation, features a modification of the amino acid from F to I at position 398.
+The protein's natural variant, known as in NPHS17; unknown pathological significance;, features a modification of the amino acid from A to V at position 477.
+The protein's natural variant, known as in NPHS17; decreased function in nephrogenesis; unable to fully rescue morpholino-induced nephrogenesis defects in Xenopus; decreased interaction with NUP160;, features a modification of the amino acid from A to P at position 581.
+The protein's natural variant, known as in NPHS17; loss of function in nephrogenesis; unable to rescue morpholino-induced nephrogenesis defects in Xenopus; decreased interaction with NUP160;, features a modification of the amino acid from R to W at position 645.
+The protein's natural variant, known as in strain: HU1069, features a modification of the amino acid from L to Q at position 73.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from A to T at position 296.
+The protein's natural variant, known as in strain: ATCC 26032 / G217B, features a modification of the amino acid from N to D at position 28.
+The protein's natural variant, known as in strain: ATCC 26032 / G217B, features a modification of the amino acid from D to E at position 60.
+The protein's natural variant, known as in strain: ATCC 26032 / G217B, features a modification of the amino acid from S to N at position 83.
+The protein's natural variant, known as in strain: 60190, features a modification of the amino acid from V to I at position 10.
+The protein's natural variant, known as in strain: 60190, features a modification of the amino acid from L to F at position 105.
+The protein's natural variant, known as in strain: 60190, features a modification of the amino acid from D to E at position 193.
+The protein's natural variant, known as in strain: 60190, features a modification of the amino acid from T to A at position 220.
+The protein's natural variant, known as in strain: 60190, features a modification of the amino acid from S to N at position 302.
+The protein's natural variant, known as in strain: 60190, features a modification of the amino acid from T to A at position 353.
+The protein's natural variant, known as in strain: 60190, features a modification of the amino acid from A to D at position 379.
+The protein's natural variant, known as in strain: 60190, features a modification of the amino acid from I to V at position 415.
+The protein's natural variant, known as in strain: 60190, features a modification of the amino acid from E to Q at position 457.
+The protein's natural variant, known as in strain: 60190, features a modification of the amino acid from YI to CV at position 481.
+The protein's natural variant, known as in strain: 60190, features a modification of the amino acid from EV to KL at position 488.
+The protein's natural variant, known as in strain: 60190, features a modification of the amino acid from D to N at position 493.
+The protein's natural variant, known as in strain: 60190, features a modification of the amino acid from D to N at position 505.
+The protein's natural variant, known as in IBMPFD2;, features a modification of the amino acid from D to V at position 302.
+The protein's natural variant, known as in AAAS;, features a modification of the amino acid from Q to K at position 15.
+The protein's natural variant, known as in AAAS;, features a modification of the amino acid from H to R at position 160.
+The protein's natural variant, known as in AAAS;, features a modification of the amino acid from S to P at position 263.
+The natural variant of this protein is characterized by an amino acid alteration from E to Q at position 317.
+The protein's natural variant, known as in strain: Subline 5, features a modification of the amino acid from I to V at position 208.
+The protein's natural variant, known as in strain: Subline 5 and Subline 7, features a modification of the amino acid from I to T at position 252.
+The protein's natural variant, known as in strain: Subline 5, features a modification of the amino acid from E to G at position 289.
+The protein's natural variant, known as in strain: Subline 8, features a modification of the amino acid from D to G at position 295.
+The protein's natural variant, known as in strain: Subline 8, features a modification of the amino acid from V to A at position 417.
+The protein's natural variant, known as in strain: Subline 7, features a modification of the amino acid from L to P at position 499.
+The protein's natural variant, known as in MYOCL1; the mutation may alter post-translational modification of the protein;, features a modification of the amino acid from E to Q at position 21.
+The protein's natural variant, known as in MYOCL1;, features a modification of the amino acid from A to T at position 80.
+The protein's natural variant, known as in strain: SO5076, features a modification of the amino acid from R to W at position 13.
+The protein's natural variant, known as in HGCLAS;, features a modification of the amino acid from R to H at position 249.
+The protein's natural variant, known as in isoform 2, features a modification of the amino acid from Q to H at position 31.
+The protein's natural variant, known as in isoform 2, features a modification of the amino acid from L to P at position 36.
+The protein's natural variant, known as in strain: CC-2290 / S1 D2 and CC-503, features a modification of the amino acid from N to D at position 45.
+The protein's natural variant, known as in strain: 212, features a modification of the amino acid from A to S at position 156.
+The protein's natural variant, known as in strain: B31 and KA, features a modification of the amino acid from D to N at position 279.
+The protein's natural variant, known as in PKNPY, features a modification of the amino acid from I to L at position 311.
+The protein's natural variant, known as in PKNPY, features a modification of the amino acid from Y to S at position 314.
+The natural variant of this protein is characterized by an amino acid alteration from S to P at position 31.
+The natural variant of this protein is characterized by an amino acid alteration from G to Q at position 34.
+The natural variant of this protein is characterized by an amino acid alteration from S to H at position 35.
+The natural variant of this protein is characterized by an amino acid alteration from S to Q at position 35.
+The natural variant of this protein is characterized by an amino acid alteration from F to V at position 40.
+The natural variant of this protein is characterized by an amino acid alteration from K to E at position 43.
+The natural variant of this protein is characterized by an amino acid alteration from K to Q at position 43.
+The natural variant of this protein is characterized by an amino acid alteration from W to H at position 46.
+The natural variant of this protein is characterized by an amino acid alteration from W to N at position 46.
+The natural variant of this protein is characterized by an amino acid alteration from K to R at position 51.
+The natural variant of this protein is characterized by an amino acid alteration from K to Y at position 51.
+The protein's natural variant, known as in strain: Red-eye, features a modification of the amino acid from G to R at position 58.
+The natural variant of this protein is characterized by an amino acid alteration from A to T at position 30.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from I to M at position 67.
+The protein's natural variant, known as in BCD;, features a modification of the amino acid from W to R at position 44.
+The protein's natural variant, known as in BCD;, features a modification of the amino acid from G to S at position 61.
+The protein's natural variant, known as in BCD;, features a modification of the amino acid from E to D at position 79.
+The protein's natural variant, known as in BCD;, features a modification of the amino acid from I to T at position 111.
+The protein's natural variant, known as in BCD;, features a modification of the amino acid from M to V at position 123.
+The protein's natural variant, known as in BCD; impaired omega hydroxylase activity;, features a modification of the amino acid from H to P at position 331.
+The protein's natural variant, known as in BCD;, features a modification of the amino acid from S to P at position 341.
+The protein's natural variant, known as in BCD;, features a modification of the amino acid from R to H at position 508.
+The protein's natural variant, known as in strain: D4, features a modification of the amino acid from DD to GG at position 285.
+The protein's natural variant, known as in strain: D3, features a modification of the amino acid from D to G at position 284.
+The protein's natural variant, known as in DEE80; strongly decreased protein levels; slightly decreased cell surface presence of GPI-anchored proteins;, features a modification of the amino acid from R to Q at position 71.
+The protein's natural variant, known as in DEE80, features a modification of the amino acid from S to P at position 90.
+The protein's natural variant, known as in DEE80; unknown pathological significance;, features a modification of the amino acid from D to H at position 155.
+The protein's natural variant, known as in DEE80; no effect on protein levels; decreased cell surface presence of GPI-anchored proteins;, features a modification of the amino acid from R to H at position 232.
+The protein's natural variant, known as in DEE80; strongly decreased protein levels; decreased cell surface presence of GPI-anchored proteins, features a modification of the amino acid from Q to QRCQ at position 282.
+The protein's natural variant, known as in DEE80; decreased protein levels; decreased cell surface presence of GPI-anchored proteins;, features a modification of the amino acid from V to L at position 286.
+The protein's natural variant, known as in DEE80; decreased protein levels; decreased cell surface presence of GPI-anchored proteins;, features a modification of the amino acid from A to P at position 388.
+The protein's natural variant, known as in DEE80; decreased protein levels; slightly decreased cell surface presence of GPI-anchored proteins;, features a modification of the amino acid from H to R at position 407.
+The protein's natural variant, known as in DEE80; unknown pathological significance;, features a modification of the amino acid from I to M at position 537.
+The natural variant of this protein is characterized by an amino acid alteration from F to L at position 141.
+The protein's natural variant, known as in a aLLTEL/AML1+ sample; somatic mutation, features a modification of the amino acid from G to A at position 99.
+The protein's natural variant, known as in MMAA; abolishes protein levels; decreases protein stability;, features a modification of the amino acid from L to P at position 89.
+The protein's natural variant, known as in MMAA; decreases protein levels; no effect on binding to GDP; decreases by 55% GTPase activity; abolishes interaction with MUT; impairs GTPase activity stimulation by MUT; highly reduces release of AdoCbl by MMAB, features a modification of the amino acid from R to G at position 98.
+The protein's natural variant, known as in MMAA; highly decreases protein levels; decreases protein stability;, features a modification of the amino acid from R to Q at position 145.
+The protein's natural variant, known as in MMAA; highly decreases protein levels; decreases protein stability; no effect on binding to GDP; no effect on GTPase activity; abolishes interaction with MUT; impairs GTPase activity stimulation by MUT; highly reduces release of AdoCbl by MMAB, features a modification of the amino acid from G to E at position 147.
+The protein's natural variant, known as in MMAA; decreases protein levels; no effect on binding to GDP; no effect on GTPase activity; abolishes interaction with MUT; impairs GTPase activity stimulation by MUT; highly reduces release of AdoCbl by MMAB;, features a modification of the amino acid from G to R at position 188.
+The protein's natural variant, known as in MMAA; no effect on protein levels; no effect on binding to GDP; no effect on GTPase activity; no effect on interaction with MUT; impairs GTPase activity stimulation by MUT; reduces release of AdoCbl by MMAB;, features a modification of the amino acid from G to D at position 192.
+The protein's natural variant, known as in MMAA; unknown pathological significance; decreases protein levels; no effect on binding to GDP; no effect on GTPase activity; no effect on interaction with MUT; impairs GTPase activity stimulation by MUT; reduces release of AdoCbl by MMAB;, features a modification of the amino acid from R to Q at position 196.
+The protein's natural variant, known as in MMAA; decreases protein levels; no effect on binding to GDP; no effect on GTPase activity; abolishes interaction with MUT; impairs GTPase activity stimulation by MUT; highly reduces release of AdoCbl by MMAB;, features a modification of the amino acid from Y to C at position 207.
+The protein's natural variant, known as in MMAA; decreases protein levels; no effect on binding to GDP; no effect on GTPase activity; abolishes interaction with MUT; impairs GTPase activity stimulation by MUT; highly reduces release of AdoCbl by MMAB, features a modification of the amino acid from R to S at position 209.
+The protein's natural variant, known as in MMAA; decreases protein levels; no effect on binding to GDP; no effect on GTPase activity; abolishes interaction with MUT; impairs GTPase activity stimulation by MUT; highly reduces release of AdoCbl by MMAB;, features a modification of the amino acid from G to E at position 218.
+The protein's natural variant, known as in MMAA; decreases protein levels; no effect on binding to GDP; no effect on GTPase activity; abolishes interaction with MUT; impairs GTPase activity stimulation by MUT; highly reduces release of AdoCbl by MMAB;, features a modification of the amino acid from V to M at position 220.
+The protein's natural variant, known as in MMAA; highly decreases protein levels; decreases protein stability, features a modification of the amino acid from I to F at position 241.
+The protein's natural variant, known as in MMAA; no effect on protein levels; no effect on binding to GDP; no effect on GTPase activity; abolishes interaction with MUT; impairs GTPase activity stimulation by MUT; highly reduces release of AdoCbl by MMAB;, features a modification of the amino acid from T to N at position 243.
+The protein's natural variant, known as in MMAA; decreases protein levels; no effect on binding to GDP; no effect on GTPase activity; no effect on interaction with MUT; impairs GTPase activity stimulation by MUT; reduces release of AdoCbl by MMAB, features a modification of the amino acid from E to K at position 250.
+The protein's natural variant, known as in MMAA; highly decreases protein levels, features a modification of the amino acid from D to N at position 258.
+The protein's natural variant, known as in MMAA, features a modification of the amino acid from G to D at position 274.
+The protein's natural variant, known as in MMAA; decreases protein levels; no effect on binding to GDP; no effect on GTPase activity; no effect on interaction with MUT; impairs GTPase activity stimulation by MUT; slightly reduces release of AdoCbl by MMAB, features a modification of the amino acid from G to S at position 274.
+The protein's natural variant, known as in MMAA; decreases protein levels; no effect on binding to GDP; no effect on GTPase activity; no effect on interaction with MUT; impairs GTPase activity stimulation by MUT; reduces release of AdoCbl by MMAB, features a modification of the amino acid from K to E at position 276.
+The protein's natural variant, known as in MMAA; highly decreases protein levels; decreases protein stability;, features a modification of the amino acid from A to D at position 287.
+The protein's natural variant, known as in MMAA; decreases protein levels; highly decreases binding to GDP; no effect on GTPase activity; abolishes interaction with MUT; impairs GTPase activity stimulation by MUT; highly reduces release of AdoCbl by MMAB;, features a modification of the amino acid from D to V at position 292.
+The protein's natural variant, known as in MMAA; decreases protein levels; decreases protein stability; no effect on binding to GDP; no effect on GTPase activity; no effect on interaction with MUT; impairs GTPase activity stimulation by MUT; reduces release of AdoCbl by MMAB, features a modification of the amino acid from R to G at position 359.
+The protein's natural variant, known as in MMAA; decreases protein levels;, features a modification of the amino acid from R to Q at position 359.
+The protein's natural variant, known as in MMAA; highly decreases protein levels; decreases protein stability, features a modification of the amino acid from G to V at position 399.
+The protein's natural variant, known as found in a family with familial combined hyperlipemia; unknown pathological significance; associated with increased plasma triglyceride, plasma cholesterol, low-density lipoprotein cholesterol, apolipoprotein B and ASP;, features a modification of the amino acid from S to I at position 323.
+The protein's natural variant, known as influences plasma cholesterol levels; associated with increased total cholesterol and non-high-density lipoprotein cholesterol;, features a modification of the amino acid from K to R at position 45.
+The protein's natural variant, known as in 50%, this form is not glycosylated, features a modification of the amino acid from Q to K at position 37.
+The protein's natural variant, known as in strain: Coolidgei, features a modification of the amino acid from M to T at position 15.
+The protein's natural variant, known as in strain: Austericus and Rufinus, features a modification of the amino acid from V to I at position 20.
+The protein's natural variant, known as in strain: Rufinus, features a modification of the amino acid from D to E at position 42.
+The protein's natural variant, known as in strain: Oreas, features a modification of the amino acid from F to L at position 56.
+The protein's natural variant, known as in strain: Coolidgei, features a modification of the amino acid from I to T at position 84.
+The protein's natural variant, known as in strain: Austericus, Coolidgei and Rufinus, features a modification of the amino acid from D to N at position 85.
+The protein's natural variant, known as in strain: Rufinus, features a modification of the amino acid from Y to H at position 104.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from S to R at position 19.
+The protein's natural variant, known as in HEMA; severe, features a modification of the amino acid from R to T at position 22.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from Y to C at position 24.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from Y to C at position 25.
+The protein's natural variant, known as in HEMA; severe, features a modification of the amino acid from L to P at position 26.
+The protein's natural variant, known as in HEMA; severe;, features a modification of the amino acid from L to R at position 26.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from E to V at position 30.
+The protein's natural variant, known as in HEMA; moderate, features a modification of the amino acid from W to G at position 33.
+The protein's natural variant, known as in HEMA; mild/severe;, features a modification of the amino acid from Y to C at position 35.
+The protein's natural variant, known as in HEMA; severe, features a modification of the amino acid from Y to H at position 35.
+The protein's natural variant, known as in HEMA; severe/moderate;, features a modification of the amino acid from G to C at position 41.
+The protein's natural variant, known as in HEMA; severe, features a modification of the amino acid from R to C at position 48.
+The protein's natural variant, known as in HEMA;, features a modification of the amino acid from R to K at position 48.
+The protein's natural variant, known as in HEMA; severe, features a modification of the amino acid from K to E at position 67.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from K to N at position 67.
+The protein's natural variant, known as in HEMA; moderate-severe;, features a modification of the amino acid from L to P at position 69.
+The protein's natural variant, known as in HEMA; moderate, features a modification of the amino acid from E to K at position 72.
+The protein's natural variant, known as in HEMA; moderate, features a modification of the amino acid from D to E at position 75.
+The protein's natural variant, known as in HEMA; moderate-severe, features a modification of the amino acid from D to Y at position 75.
+The protein's natural variant, known as in HEMA;, features a modification of the amino acid from P to R at position 83.
+The protein's natural variant, known as in HEMA; severe;, features a modification of the amino acid from G to D at position 89.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from G to V at position 89.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from G to A at position 92.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from G to V at position 92.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from A to P at position 97.
+The protein's natural variant, known as in HEMA; severe;, features a modification of the amino acid from E to K at position 98.
+The protein's natural variant, known as in HEMA; severe;, features a modification of the amino acid from V to D at position 99.
+The protein's natural variant, known as in HEMA; severe;, features a modification of the amino acid from D to G at position 101.
+The protein's natural variant, known as in HEMA; severe sporadic, features a modification of the amino acid from D to H at position 101.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from D to V at position 101.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from V to D at position 104.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from K to T at position 108.
+The protein's natural variant, known as in HEMA; moderate;, features a modification of the amino acid from M to V at position 110.
+The protein's natural variant, known as in HEMA; severe, features a modification of the amino acid from A to T at position 111.
+The protein's natural variant, known as in HEMA; moderate, features a modification of the amino acid from A to V at position 111.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from H to R at position 113.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from H to Y at position 113.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from L to F at position 117.
+The protein's natural variant, known as in HEMA; severe;, features a modification of the amino acid from L to R at position 117.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from G to S at position 121.
+The protein's natural variant, known as in HEMA; severe, features a modification of the amino acid from E to V at position 129.
+The protein's natural variant, known as in HEMA; severe;, features a modification of the amino acid from G to R at position 130.
+The protein's natural variant, known as in HEMA; severe;, features a modification of the amino acid from E to D at position 132.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from Y to C at position 133.
+The protein's natural variant, known as in HEMA; severe;, features a modification of the amino acid from D to G at position 135.
+The protein's natural variant, known as in HEMA; severe sporadic, features a modification of the amino acid from D to Y at position 135.
+The protein's natural variant, known as in HEMA; severe, features a modification of the amino acid from T to A at position 137.
+The protein's natural variant, known as in HEMA; moderate;, features a modification of the amino acid from T to I at position 137.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from S to R at position 138.
+The protein's natural variant, known as in HEMA; severe familial;, features a modification of the amino acid from E to K at position 141.
+The protein's natural variant, known as in HEMA; moderate;, features a modification of the amino acid from D to H at position 145.
+The protein's natural variant, known as in HEMA; severe, features a modification of the amino acid from V to D at position 147.
+The protein's natural variant, known as in HEMA; moderate;, features a modification of the amino acid from Y to H at position 155.
+The protein's natural variant, known as in HEMA; moderate, features a modification of the amino acid from V to A at position 159.
+The protein's natural variant, known as in HEMA; moderate, features a modification of the amino acid from N to K at position 163.
+The protein's natural variant, known as in HEMA; moderate;, features a modification of the amino acid from G to D at position 164.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from G to V at position 164.
+The protein's natural variant, known as in HEMA; severe;, features a modification of the amino acid from P to S at position 165.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from C to W at position 172.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from S to P at position 176.
+The protein's natural variant, known as in HEMA; moderate;, features a modification of the amino acid from S to P at position 179.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from V to E at position 181.
+The protein's natural variant, known as in HEMA; mild/moderate;, features a modification of the amino acid from V to M at position 181.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from K to T at position 185.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from D to G at position 186.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from D to N at position 186.
+The protein's natural variant, known as in HEMA; severe, features a modification of the amino acid from D to Y at position 186.
+The protein's natural variant, known as in HEMA; moderate;, features a modification of the amino acid from S to L at position 189.
+The protein's natural variant, known as in HEMA;, features a modification of the amino acid from L to F at position 191.
+The protein's natural variant, known as in HEMA; severe familial, features a modification of the amino acid from G to R at position 193.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from L to P at position 195.
+The protein's natural variant, known as in HEMA; severe;, features a modification of the amino acid from C to G at position 198.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from S to N at position 202.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from S to R at position 202.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from F to V at position 214.
+The protein's natural variant, known as in HEMA; moderate, features a modification of the amino acid from L to H at position 217.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from A to D at position 219.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from A to T at position 219.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from V to G at position 220.
+The protein's natural variant, known as in HEMA; moderate;, features a modification of the amino acid from D to V at position 222.
+The protein's natural variant, known as in HEMA; severe, features a modification of the amino acid from E to K at position 223.
+The protein's natural variant, known as in HEMA; moderate;, features a modification of the amino acid from G to W at position 224.
+The protein's natural variant, known as in HEMA; moderate;, features a modification of the amino acid from T to I at position 252.
+The protein's natural variant, known as in HEMA; severe, features a modification of the amino acid from V to F at position 253.
+The protein's natural variant, known as in HEMA; severe, features a modification of the amino acid from N to I at position 254.
+The protein's natural variant, known as in HEMA; severe, features a modification of the amino acid from G to V at position 255.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from L to P at position 261.
+The protein's natural variant, known as in HEMA; moderate, features a modification of the amino acid from P to L at position 262.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from G to S at position 263.
+The protein's natural variant, known as in HEMA; severe;, features a modification of the amino acid from G to E at position 266.
+The protein's natural variant, known as in HEMA; moderate;, features a modification of the amino acid from C to Y at position 267.
+The protein's natural variant, known as in HEMA;, features a modification of the amino acid from W to C at position 274.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from H to L at position 275.
+The protein's natural variant, known as in HEMA; severe;, features a modification of the amino acid from G to R at position 278.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from G to D at position 280.
+The protein's natural variant, known as in HEMA; moderate, features a modification of the amino acid from E to K at position 284.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from V to G at position 285.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from E to G at position 291.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from E to K at position 291.
+The protein's natural variant, known as in HEMA; moderate;, features a modification of the amino acid from T to I at position 294.
+The protein's natural variant, known as in HEMA; moderate, features a modification of the amino acid from F to L at position 295.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from V to A at position 297.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from N to I at position 299.
+The protein's natural variant, known as in HEMA; severe/mild;, features a modification of the amino acid from R to C at position 301.
+The protein's natural variant, known as in HEMA; severe;, features a modification of the amino acid from R to H at position 301.
+The protein's natural variant, known as in HEMA; severe;, features a modification of the amino acid from R to L at position 301.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from A to E at position 303.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from A to P at position 303.
+The protein's natural variant, known as in HEMA; moderate, features a modification of the amino acid from I to S at position 307.
+The protein's natural variant, known as in HEMA; moderate;, features a modification of the amino acid from S to L at position 308.
+The protein's natural variant, known as in HEMA; mild/moderate;, features a modification of the amino acid from F to S at position 312.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from T to A at position 314.
+The protein's natural variant, known as in HEMA; moderate, features a modification of the amino acid from T to I at position 314.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from A to V at position 315.
+The protein's natural variant, known as in HEMA; severe, features a modification of the amino acid from G to E at position 323.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from L to P at position 326.
+The protein's natural variant, known as in HEMA; severe;, features a modification of the amino acid from L to P at position 327.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from L to V at position 327.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from C to F at position 329.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from I to V at position 331.
+The protein's natural variant, known as in HEMA; moderate, features a modification of the amino acid from M to T at position 339.
+The protein's natural variant, known as in HEMA;, features a modification of the amino acid from E to K at position 340.
+The protein's natural variant, known as in HEMA;, features a modification of the amino acid from V to A at position 345.
+The protein's natural variant, known as in HEMA; severe;, features a modification of the amino acid from V to L at position 345.
+The protein's natural variant, known as in HEMA; severe;, features a modification of the amino acid from C to R at position 348.
+The protein's natural variant, known as in HEMA; moderate;, features a modification of the amino acid from C to S at position 348.
+The protein's natural variant, known as in HEMA; mild/severe, features a modification of the amino acid from C to Y at position 348.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from Y to C at position 365.
+The protein's natural variant, known as in HEMA; Okayama; moderate/severe; abolishes the normal cleavage by thrombin;, features a modification of the amino acid from R to C at position 391.
+The protein's natural variant, known as in HEMA; Kumamoto; mild/moderate; abolishes the normal cleavage by thrombin;, features a modification of the amino acid from R to H at position 391.
+The protein's natural variant, known as in HEMA; severe; abolishes the normal cleavage by thrombin, features a modification of the amino acid from R to P at position 391.
+The protein's natural variant, known as in HEMA; mild; abolishes normal cleavage by thrombin;, features a modification of the amino acid from S to L at position 392.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from S to P at position 392.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from A to S at position 394.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from W to G at position 401.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from I to F at position 405.
+The protein's natural variant, known as in HEMA; severe;, features a modification of the amino acid from I to S at position 405.
+The protein's natural variant, known as in HEMA; severe/moderate;, features a modification of the amino acid from E to G at position 409.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from W to G at position 412.
+The protein's natural variant, known as in HEMA; severe;, features a modification of the amino acid from W to R at position 412.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from K to I at position 427.
+The protein's natural variant, known as in HEMA; moderate;, features a modification of the amino acid from L to F at position 431.
+The protein's natural variant, known as in HEMA; moderate, features a modification of the amino acid from L to S at position 431.
+The protein's natural variant, known as in HEMA; severe, features a modification of the amino acid from R to P at position 437.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from R to W at position 437.
+The protein's natural variant, known as in HEMA; not severe;, features a modification of the amino acid from I to F at position 438.
+The protein's natural variant, known as in HEMA; severe;, features a modification of the amino acid from G to D at position 439.
+The protein's natural variant, known as in HEMA; moderate, features a modification of the amino acid from G to S at position 439.
+The protein's natural variant, known as in HEMA; severe;, features a modification of the amino acid from G to V at position 439.
+The protein's natural variant, known as in HEMA;, features a modification of the amino acid from Y to C at position 442.
+The protein's natural variant, known as in HEMA; severe;, features a modification of the amino acid from K to R at position 444.
+The protein's natural variant, known as in HEMA; severe, features a modification of the amino acid from Y to D at position 450.
+The protein's natural variant, known as in HEMA; mild/moderate;, features a modification of the amino acid from Y to N at position 450.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from T to I at position 454.
+The protein's natural variant, known as in HEMA; mild-moderate/severe;, features a modification of the amino acid from F to C at position 455.
+The protein's natural variant, known as in HEMA; severe sporadic;, features a modification of the amino acid from G to E at position 466.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from P to L at position 470.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from P to R at position 470.
+The protein's natural variant, known as in HEMA; mild sporadic, features a modification of the amino acid from P to T at position 470.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from G to E at position 474.
+The protein's natural variant, known as in HEMA; severe;, features a modification of the amino acid from G to R at position 474.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from G to V at position 474.
+The protein's natural variant, known as in HEMA; moderate, features a modification of the amino acid from E to K at position 475.
+The protein's natural variant, known as in HEMA; moderate, features a modification of the amino acid from G to V at position 477.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from D to N at position 478.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from T to R at position 479.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from F to C at position 484.
+The protein's natural variant, known as in HEMA; moderate;, features a modification of the amino acid from A to G at position 488.
+The protein's natural variant, known as in HEMA;, features a modification of the amino acid from R to G at position 490.
+The protein's natural variant, known as in HEMA; moderate;, features a modification of the amino acid from Y to C at position 492.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from Y to H at position 492.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from I to T at position 494.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from P to R at position 496.
+The protein's natural variant, known as in HEMA; severe/moderate;, features a modification of the amino acid from G to R at position 498.
+The protein's natural variant, known as in HEMA;, features a modification of the amino acid from R to H at position 503.
+The protein's natural variant, known as in HEMA; moderate;, features a modification of the amino acid from G to S at position 513.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from G to V at position 513.
+The protein's natural variant, known as in HEMA; requires 2 nucleotide substitutions, features a modification of the amino acid from I to Y at position 522.
+The protein's natural variant, known as in HEMA; moderate, features a modification of the amino acid from K to E at position 529.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from W to G at position 532.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from P to T at position 540.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from T to S at position 541.
+The protein's natural variant, known as in HEMA; moderate;, features a modification of the amino acid from D to N at position 544.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from R to W at position 546.
+The protein's natural variant, known as in HEMA; mild/moderate;, features a modification of the amino acid from R to C at position 550.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from R to G at position 550.
+The protein's natural variant, known as in HEMA; mild/moderate;, features a modification of the amino acid from R to H at position 550.
+The protein's natural variant, known as in HEMA; severe, features a modification of the amino acid from S to P at position 553.
+The protein's natural variant, known as in HEMA; moderate, features a modification of the amino acid from S to C at position 554.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from S to G at position 554.
+The protein's natural variant, known as in HEMA; moderate, features a modification of the amino acid from V to D at position 556.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from R to T at position 560.
+The protein's natural variant, known as in HEMA; severe;, features a modification of the amino acid from D to G at position 561.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from D to H at position 561.
+The protein's natural variant, known as in HEMA; severe, features a modification of the amino acid from D to Y at position 561.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from I to T at position 567.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from P to R at position 569.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from S to F at position 577.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from V to A at position 578.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from D to A at position 579.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from D to H at position 579.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from N to S at position 583.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from Q to H at position 584.
+The protein's natural variant, known as in HEMA; moderate;, features a modification of the amino acid from Q to K at position 584.
+The protein's natural variant, known as in HEMA;, features a modification of the amino acid from Q to R at position 584.
+The protein's natural variant, known as in HEMA; moderate-severe, features a modification of the amino acid from I to R at position 585.
+The protein's natural variant, known as in HEMA; severe/moderate;, features a modification of the amino acid from I to T at position 585.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from M to V at position 586.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from D to G at position 588.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from D to Y at position 588.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from L to Q at position 594.
+The protein's natural variant, known as in HEMA; severe;, features a modification of the amino acid from S to P at position 596.
+The protein's natural variant, known as in HEMA;, features a modification of the amino acid from N to D at position 601.
+The protein's natural variant, known as in HEMA;, features a modification of the amino acid from N to K at position 601.
+The protein's natural variant, known as in HEMA; mild familial;, features a modification of the amino acid from R to G at position 602.
+The protein's natural variant, known as in HEMA;, features a modification of the amino acid from S to I at position 603.
+The protein's natural variant, known as in HEMA; severe, features a modification of the amino acid from S to R at position 603.
+The protein's natural variant, known as in HEMA; severe;, features a modification of the amino acid from W to C at position 604.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from Y to H at position 605.
+The protein's natural variant, known as in HEMA; severe;, features a modification of the amino acid from Y to S at position 605.
+The protein's natural variant, known as in HEMA; moderate;, features a modification of the amino acid from N to I at position 609.
+The protein's natural variant, known as in HEMA; mild/moderate; secretion impaired;, features a modification of the amino acid from R to C at position 612.
+The protein's natural variant, known as in HEMA; severe, features a modification of the amino acid from N to K at position 631.
+The protein's natural variant, known as in HEMA;, features a modification of the amino acid from N to S at position 631.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from M to I at position 633.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from S to N at position 635.
+The protein's natural variant, known as in HEMA; severe sporadic/moderate, features a modification of the amino acid from N to D at position 637.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from N to I at position 637.
+The protein's natural variant, known as in HEMA; mild; secretion impaired, features a modification of the amino acid from N to S at position 637.
+The protein's natural variant, known as in HEMA; moderate, features a modification of the amino acid from Y to C at position 639.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from L to V at position 644.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from L to F at position 650.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from V to A at position 653.
+The protein's natural variant, known as in HEMA; severe;, features a modification of the amino acid from V to M at position 653.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from L to P at position 659.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from A to V at position 663.
+The protein's natural variant, known as in HEMA; moderate-severe, features a modification of the amino acid from Q to P at position 664.
+The protein's natural variant, known as in HEMA; moderate;, features a modification of the amino acid from F to L at position 677.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from M to I at position 681.
+The protein's natural variant, known as in HEMA;, features a modification of the amino acid from V to F at position 682.
+The protein's natural variant, known as in HEMA; severe;, features a modification of the amino acid from Y to C at position 683.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from Y to N at position 683.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from T to R at position 686.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from F to L at position 698.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from M to T at position 699.
+The protein's natural variant, known as in HEMA; severe, features a modification of the amino acid from M to V at position 699.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from M to I at position 701.
+The protein's natural variant, known as in HEMA; moderate, features a modification of the amino acid from G to V at position 705.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from G to W at position 710.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from N to I at position 713.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from R to L at position 717.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from R to W at position 717.
+The protein's natural variant, known as in HEMA; severe/moderate, features a modification of the amino acid from G to D at position 720.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from G to S at position 720.
+The protein's natural variant, known as in HEMA; severe;, features a modification of the amino acid from M to I at position 721.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from M to L at position 721.
+The protein's natural variant, known as in HEMA; moderate;, features a modification of the amino acid from A to T at position 723.
+The protein's natural variant, known as in HEMA; severe, features a modification of the amino acid from L to Q at position 725.
+The protein's natural variant, known as in HEMA; severe;, features a modification of the amino acid from V to F at position 727.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from E to K at position 739.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from Y to C at position 742.
+The protein's natural variant, known as in HEMA;, features a modification of the amino acid from P to R at position 947.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from V to L at position 1012.
+The protein's natural variant, known as in HEMA; moderate;, features a modification of the amino acid from E to K at position 1057.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from H to Y at position 1066.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from Q to K at position 1336.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from N to K at position 1460.
+The protein's natural variant, known as in HEMA;, features a modification of the amino acid from A to S at position 1610.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from I to T at position 1698.
+The protein's natural variant, known as in HEMA; severe, features a modification of the amino acid from Y to C at position 1699.
+The protein's natural variant, known as in HEMA; moderate;, features a modification of the amino acid from Y to F at position 1699.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from E to K at position 1701.
+The protein's natural variant, known as in HEMA; mild sporadic, features a modification of the amino acid from Q to H at position 1705.
+The protein's natural variant, known as in HEMA; East Hartford; severe/moderate/mild; abolishes thrombin cleavage at the light chain;, features a modification of the amino acid from R to C at position 1708.
+The protein's natural variant, known as in HEMA; mild; abolishes thrombin cleavage at the light chain;, features a modification of the amino acid from R to H at position 1708.
+The protein's natural variant, known as in HEMA; moderate, features a modification of the amino acid from T to S at position 1714.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from R to G at position 1715.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from A to V at position 1720.
+The protein's natural variant, known as in HEMA; severe;, features a modification of the amino acid from E to K at position 1723.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from D to V at position 1727.
+The protein's natural variant, known as in HEMA; moderate;, features a modification of the amino acid from Y to C at position 1728.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from R to G at position 1740.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from K to Q at position 1751.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from F to L at position 1762.
+The protein's natural variant, known as in HEMA;, features a modification of the amino acid from R to H at position 1768.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from G to R at position 1769.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from L to P at position 1771.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from L to F at position 1775.
+The protein's natural variant, known as in HEMA; moderate;, features a modification of the amino acid from L to V at position 1775.
+The protein's natural variant, known as in HEMA; moderate, features a modification of the amino acid from L to P at position 1777.
+The protein's natural variant, known as in HEMA; severe/moderate;, features a modification of the amino acid from G to E at position 1779.
+The protein's natural variant, known as in HEMA; severe;, features a modification of the amino acid from G to R at position 1779.
+The protein's natural variant, known as in HEMA; moderate, features a modification of the amino acid from P to L at position 1780.
+The protein's natural variant, known as in HEMA; severe sporadic;, features a modification of the amino acid from I to R at position 1782.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from D to H at position 1788.
+The protein's natural variant, known as in HEMA; severe;, features a modification of the amino acid from M to T at position 1791.
+The protein's natural variant, known as in HEMA; severe;, features a modification of the amino acid from A to P at position 1798.
+The protein's natural variant, known as in HEMA; requires 2 nucleotide substitutions, features a modification of the amino acid from S to H at position 1799.
+The protein's natural variant, known as in HEMA; moderate;, features a modification of the amino acid from R to C at position 1800.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from R to G at position 1800.
+The protein's natural variant, known as in HEMA; moderate/severe;, features a modification of the amino acid from R to H at position 1800.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from P to A at position 1801.
+The protein's natural variant, known as in HEMA; moderate, features a modification of the amino acid from Y to C at position 1802.
+The protein's natural variant, known as in HEMA; severe;, features a modification of the amino acid from S to Y at position 1803.
+The protein's natural variant, known as in HEMA; severe, features a modification of the amino acid from F to S at position 1804.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from L to F at position 1808.
+The protein's natural variant, known as in HEMA; mild; unknown pathological significance; decreases binding with VWF and phospholipid; no effect on reaction with F9, F2 and F10; decreases specific activity by 30%; patient develops inhibitor alloantibodies, features a modification of the amino acid from P to L at position 1828.
+The protein's natural variant, known as in HEMA; moderate;, features a modification of the amino acid from M to I at position 1842.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from P to S at position 1844.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from T to P at position 1845.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from E to G at position 1848.
+The protein's natural variant, known as in HEMA; moderate/severe, features a modification of the amino acid from A to T at position 1853.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from A to V at position 1853.
+The protein's natural variant, known as in HEMA; moderate, features a modification of the amino acid from S to C at position 1858.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from K to E at position 1864.
+The protein's natural variant, known as in HEMA; severe;, features a modification of the amino acid from D to N at position 1865.
+The protein's natural variant, known as in HEMA; severe;, features a modification of the amino acid from D to Y at position 1865.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from H to P at position 1867.
+The protein's natural variant, known as in HEMA; moderate;, features a modification of the amino acid from H to R at position 1867.
+The protein's natural variant, known as in HEMA; severe, features a modification of the amino acid from G to D at position 1869.
+The protein's natural variant, known as in HEMA; severe;, features a modification of the amino acid from G to V at position 1869.
+The protein's natural variant, known as in HEMA; severe sporadic, features a modification of the amino acid from G to E at position 1872.
+The protein's natural variant, known as in HEMA; severe;, features a modification of the amino acid from P to R at position 1873.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from L to P at position 1875.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from V to L at position 1876.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from C to R at position 1877.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from C to Y at position 1877.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from L to P at position 1882.
+The protein's natural variant, known as in HEMA; severe, features a modification of the amino acid from R to I at position 1888.
+The protein's natural variant, known as in HEMA; moderate, features a modification of the amino acid from E to G at position 1894.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from I to F at position 1901.
+The protein's natural variant, known as in HEMA;, features a modification of the amino acid from E to D at position 1904.
+The protein's natural variant, known as in HEMA; severe;, features a modification of the amino acid from E to K at position 1904.
+The protein's natural variant, known as in HEMA; moderate;, features a modification of the amino acid from S to C at position 1907.
+The protein's natural variant, known as in HEMA; severe;, features a modification of the amino acid from S to R at position 1907.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from W to L at position 1908.
+The protein's natural variant, known as in HEMA; moderate, features a modification of the amino acid from Y to C at position 1909.
+The protein's natural variant, known as in HEMA; severe, features a modification of the amino acid from A to T at position 1939.
+The protein's natural variant, known as in HEMA; unknown pathological significance, features a modification of the amino acid from A to V at position 1939.
+The protein's natural variant, known as in HEMA; severe/moderate;, features a modification of the amino acid from N to D at position 1941.
+The protein's natural variant, known as in HEMA; severe/moderate;, features a modification of the amino acid from N to S at position 1941.
+The protein's natural variant, known as in HEMA; moderate, features a modification of the amino acid from G to A at position 1942.
+The protein's natural variant, known as in HEMA; moderate, features a modification of the amino acid from M to V at position 1945.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from L to F at position 1951.
+The protein's natural variant, known as in HEMA; moderate;, features a modification of the amino acid from R to L at position 1960.
+The protein's natural variant, known as in HEMA; mild/moderate;, features a modification of the amino acid from R to Q at position 1960.
+The protein's natural variant, known as in HEMA; severe, features a modification of the amino acid from L to P at position 1963.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from S to I at position 1965.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from M to I at position 1966.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from M to V at position 1966.
+The protein's natural variant, known as in HEMA; moderate;, features a modification of the amino acid from G to D at position 1967.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from S to R at position 1968.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from N to T at position 1971.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from H to L at position 1973.
+The protein's natural variant, known as in HEMA; moderate;, features a modification of the amino acid from G to V at position 1979.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from H to P at position 1980.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from H to Y at position 1980.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from F to I at position 1982.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from R to Q at position 1985.
+The protein's natural variant, known as in HEMA; moderate;, features a modification of the amino acid from L to P at position 1994.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from Y to C at position 1998.
+The protein's natural variant, known as in HEMA; moderate-severe;, features a modification of the amino acid from G to A at position 2000.
+The protein's natural variant, known as in HEMA; sporadic, features a modification of the amino acid from T to R at position 2004.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from M to I at position 2007.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from G to R at position 2013.
+The protein's natural variant, known as in HEMA; moderate;, features a modification of the amino acid from W to C at position 2015.
+The protein's natural variant, known as in HEMA; severe familial, features a modification of the amino acid from R to P at position 2016.
+The protein's natural variant, known as in HEMA; severe/moderate/mild;, features a modification of the amino acid from R to W at position 2016.
+The protein's natural variant, known as in HEMA; moderate;, features a modification of the amino acid from E to G at position 2018.
+The protein's natural variant, known as in HEMA; severe;, features a modification of the amino acid from G to D at position 2022.
+The protein's natural variant, known as in HEMA;, features a modification of the amino acid from G to R at position 2028.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from S to N at position 2030.
+The protein's natural variant, known as in HEMA;, features a modification of the amino acid from V to A at position 2035.
+The protein's natural variant, known as in HEMA; moderate, features a modification of the amino acid from Y to C at position 2036.
+The protein's natural variant, known as in HEMA; mild/moderate;, features a modification of the amino acid from N to S at position 2038.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from C to Y at position 2040.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from G to E at position 2045.
+The protein's natural variant, known as in HEMA; severe sporadic, features a modification of the amino acid from G to V at position 2045.
+The protein's natural variant, known as in HEMA; severe, features a modification of the amino acid from I to S at position 2051.
+The protein's natural variant, known as in HEMA; severe, features a modification of the amino acid from I to N at position 2056.
+The protein's natural variant, known as in HEMA; moderate, features a modification of the amino acid from A to P at position 2058.
+The protein's natural variant, known as in HEMA; moderate;, features a modification of the amino acid from W to R at position 2065.
+The protein's natural variant, known as in HEMA; severe sporadic;, features a modification of the amino acid from P to L at position 2067.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from A to V at position 2070.
+The protein's natural variant, known as in HEMA; severe;, features a modification of the amino acid from S to N at position 2082.
+The protein's natural variant, known as in HEMA; severe;, features a modification of the amino acid from S to F at position 2088.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from D to G at position 2093.
+The protein's natural variant, known as in HEMA; severe familial, features a modification of the amino acid from D to Y at position 2093.
+The protein's natural variant, known as in HEMA;, features a modification of the amino acid from H to D at position 2101.
+The protein's natural variant, known as in HEMA; moderate, features a modification of the amino acid from T to N at position 2105.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from Q to E at position 2106.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from Q to P at position 2106.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from Q to R at position 2106.
+The protein's natural variant, known as in HEMA; severe;, features a modification of the amino acid from G to S at position 2107.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from R to C at position 2109.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from I to F at position 2117.
+The protein's natural variant, known as in HEMA; mild-moderate; affinity for VWF reduced 8-fold, features a modification of the amino acid from I to S at position 2117.
+The protein's natural variant, known as in HEMA; moderate, features a modification of the amino acid from Q to R at position 2119.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from F to C at position 2120.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from F to L at position 2120.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from Y to C at position 2124.
+The protein's natural variant, known as in HEMA; severe;, features a modification of the amino acid from R to P at position 2135.
+The protein's natural variant, known as in HEMA; moderate; affinity for VWF reduced 80-fold;, features a modification of the amino acid from S to Y at position 2138.
+The protein's natural variant, known as in HEMA; severe, features a modification of the amino acid from T to N at position 2141.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from M to V at position 2143.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from F to C at position 2145.
+The protein's natural variant, known as in HEMA; moderate;, features a modification of the amino acid from N to S at position 2148.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from N to D at position 2157.
+The protein's natural variant, known as in HEMA; severe;, features a modification of the amino acid from P to L at position 2162.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from R to C at position 2169.
+The protein's natural variant, known as in HEMA; severe/mild; affinity for VWF reduced 3-fold;, features a modification of the amino acid from R to H at position 2169.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from P to L at position 2172.
+The protein's natural variant, known as in HEMA; moderate;, features a modification of the amino acid from P to Q at position 2172.
+The protein's natural variant, known as in HEMA; severe, features a modification of the amino acid from P to R at position 2172.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from T to A at position 2173.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from T to I at position 2173.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from H to D at position 2174.
+The protein's natural variant, known as in HEMA; mild/moderate;, features a modification of the amino acid from R to C at position 2178.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from R to H at position 2178.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from R to L at position 2178.
+The protein's natural variant, known as in HEMA; severe/moderate;, features a modification of the amino acid from R to C at position 2182.
+The protein's natural variant, known as in HEMA; severe/moderate;, features a modification of the amino acid from R to H at position 2182.
+The protein's natural variant, known as in HEMA; moderate/severe, features a modification of the amino acid from R to P at position 2182.
+The protein's natural variant, known as in HEMA; moderate;, features a modification of the amino acid from M to R at position 2183.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from M to V at position 2183.
+The protein's natural variant, known as in HEMA; severe;, features a modification of the amino acid from L to S at position 2185.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from L to W at position 2185.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from S to I at position 2192.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from C to G at position 2193.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from P to R at position 2196.
+The protein's natural variant, known as in HEMA; severe sporadic, features a modification of the amino acid from G to V at position 2198.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from E to D at position 2200.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from I to T at position 2204.
+The protein's natural variant, known as in HEMA; moderate, features a modification of the amino acid from I to N at position 2209.
+The protein's natural variant, known as in HEMA; moderate;, features a modification of the amino acid from A to P at position 2211.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from A to P at position 2220.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from P to L at position 2224.
+The protein's natural variant, known as in HEMA; severe;, features a modification of the amino acid from R to G at position 2228.
+The protein's natural variant, known as in HEMA; moderate;, features a modification of the amino acid from R to L at position 2228.
+The protein's natural variant, known as in HEMA; moderate-severe, features a modification of the amino acid from R to P at position 2228.
+The protein's natural variant, known as in HEMA; severe/moderate;, features a modification of the amino acid from R to Q at position 2228.
+The protein's natural variant, known as in HEMA;, features a modification of the amino acid from L to F at position 2229.
+The protein's natural variant, known as in HEMA; moderate;, features a modification of the amino acid from W to C at position 2248.
+The protein's natural variant, known as in HEMA; moderate, features a modification of the amino acid from W to S at position 2248.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from V to A at position 2251.
+The protein's natural variant, known as in HEMA;, features a modification of the amino acid from V to E at position 2251.
+The protein's natural variant, known as in HEMA; moderate, features a modification of the amino acid from V to VQ at position 2262.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from T to A at position 2264.
+The protein's natural variant, known as in HEMA; moderate;, features a modification of the amino acid from Q to R at position 2265.
+The protein's natural variant, known as in HEMA; severe sporadic, features a modification of the amino acid from F to C at position 2279.
+The protein's natural variant, known as in HEMA;, features a modification of the amino acid from F to I at position 2279.
+The protein's natural variant, known as in HEMA; severe, features a modification of the amino acid from I to T at position 2281.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from D to G at position 2286.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from W to L at position 2290.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from G to V at position 2304.
+The protein's natural variant, known as in HEMA; moderate/mild;, features a modification of the amino acid from D to A at position 2307.
+The protein's natural variant, known as in HEMA; mild/severe;, features a modification of the amino acid from P to L at position 2319.
+The protein's natural variant, known as in HEMA; mild;, features a modification of the amino acid from P to S at position 2319.
+The protein's natural variant, known as in HEMA; severe/moderate; may cause reduced phospholipid binding;, features a modification of the amino acid from R to C at position 2323.
+The protein's natural variant, known as in HEMA; moderate;, features a modification of the amino acid from R to G at position 2323.
+The protein's natural variant, known as in HEMA; mild; may cause reduced phospholipid binding;, features a modification of the amino acid from R to H at position 2323.
+The protein's natural variant, known as in HEMA; mild, features a modification of the amino acid from R to L at position 2323.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from R to G at position 2326.
+The protein's natural variant, known as in HEMA; severe/moderate; may cause reduced phospholipid binding;, features a modification of the amino acid from R to L at position 2326.
+The protein's natural variant, known as in HEMA; severe sporadic;, features a modification of the amino acid from R to P at position 2326.
+The protein's natural variant, known as in HEMA; moderate/mild; may cause reduced phospholipid binding;, features a modification of the amino acid from R to Q at position 2326.
+The protein's natural variant, known as in HEMA; severe, features a modification of the amino acid from Q to P at position 2330.
+The protein's natural variant, known as in HEMA; severe, features a modification of the amino acid from W to R at position 2332.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from I to F at position 2336.
+The protein's natural variant, known as in HEMA; moderate, features a modification of the amino acid from R to T at position 2339.
+The protein's natural variant, known as in HEMA; moderate, features a modification of the amino acid from G to C at position 2344.
+The protein's natural variant, known as in HEMA;, features a modification of the amino acid from G to D at position 2344.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from G to S at position 2344.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from C to S at position 2345.
+The protein's natural variant, known as in HEMA, features a modification of the amino acid from C to Y at position 2345.
+The protein's natural variant, known as in CSNBO2;, features a modification of the amino acid from V to D at position 380.
+The protein's natural variant, known as in CSNBO2;, features a modification of the amino acid from P to H at position 391.
+The protein's natural variant, known as in strain: MT-3 and MT-4, features a modification of the amino acid from A to S at position 196.
+The protein's natural variant, known as in strain: MT-3 and MT-4, features a modification of the amino acid from R to K at position 203.
+The protein's natural variant, known as in strain: MT-3 and MT-4, features a modification of the amino acid from I to L at position 347.
+The natural variant of this protein is characterized by an amino acid alteration from R to RASPAQ at position 73.
+The protein's natural variant, known as in strain: ATCC 19609, features a modification of the amino acid from R to G at position 82.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation, features a modification of the amino acid from A to T at position 123.
+The protein's natural variant, known as in DFNB74; abolishes zinc-binding and enzymatic activity;, features a modification of the amino acid from C to G at position 89.
+The protein's natural variant, known as in SIDDIS;, features a modification of the amino acid from G to R at position 232.
+The protein's natural variant, known as decreases interaction with SH2D1A and INPP5D 2-fold, reduced T-cell response;, features a modification of the amino acid from M to V at position 602.
+The protein's natural variant, known as in IDDSADF, features a modification of the amino acid from E to Q at position 20.
+The protein's natural variant, known as in IDDSADF, features a modification of the amino acid from L to V at position 48.
+The protein's natural variant, known as in IDDSADF; unknown pathological significance, features a modification of the amino acid from K to E at position 119.
+The protein's natural variant, known as in IDDSADF; unknown pathological significance, features a modification of the amino acid from E to K at position 147.
+The protein's natural variant, known as in IDDSADF, features a modification of the amino acid from R to C at position 188.
+The protein's natural variant, known as in IDDSADF, features a modification of the amino acid from R to H at position 188.
+The protein's natural variant, known as in IDDSADF; unknown pathological significance, features a modification of the amino acid from R to Q at position 697.
+The protein's natural variant, known as in DFNA74; increased 3',5'-cyclic-AMP phosphodiesterase activity; increased 3',5'-cyclic-GMP phosphodiesterase activity; approximately 10-fold increase in 3',5'-cyclic-AMP and 3-fold for 3',5'-cyclic-GMP compared to wild-type;, features a modification of the amino acid from A to S at position 260.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from Y to C at position 83.
+The protein's natural variant, known as in DFNB26; results in dysregulation of MET-signaling pathway genes expression; does not affect interaction with METTL13;, features a modification of the amino acid from G to E at position 116.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from T to N at position 387.
+The protein's natural variant, known as in allele TASK-5A and allele TASK-5C;, features a modification of the amino acid from E to G at position 95.
+The protein's natural variant, known as in allele TASK-5A and allele TASK-5C;, features a modification of the amino acid from T to P at position 260.
+The protein's natural variant, known as in allele TASK-5A;, features a modification of the amino acid from P to H at position 261.
+The protein's natural variant, known as in allele TASK-5A and allele TASK-5C;, features a modification of the amino acid from L to P at position 323.
+The natural variant of this protein is characterized by an amino acid alteration from Y to F at position 54.
+The protein's natural variant, known as found in a patient with multiple endocrine tumors; germline mutation; reduced expression levels; shows impaired binding to CDK2;, features a modification of the amino acid from P to L at position 69.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from T to N at position 147.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from I to M at position 120.
+The protein's natural variant, known as in NPHS24; unknown pathological significance; affects the regulation of filopodia formation, features a modification of the amino acid from E to Q at position 121.
+The protein's natural variant, known as in NPHS24; unknown pathological significance; affects the regulation of filopodia formation, features a modification of the amino acid from R to Q at position 335.
+The protein's natural variant, known as in NPHS24; unknown pathological significance; affects the regulation of filopodia formation, features a modification of the amino acid from P to H at position 582.
+The protein's natural variant, known as in NPHS24; unknown pathological significance; affects the regulation of filopodia formation, features a modification of the amino acid from S to L at position 1028.
+The natural variant of this protein is characterized by an amino acid alteration from F to Y at position 416.
+The protein's natural variant, known as in MCPH17; impairs kinase activity; exhibits abnormal mitotic cytokinesis; exhibits multipolar spindles; increases the neurons apoptotic process;, features a modification of the amino acid from G to V at position 106.
+The protein's natural variant, known as in MCPH17; impairs kinase activity; exhibits abnormal mitotic cytokinesis; exhibits multipolar spindles; increases the neurons apoptotic process;, features a modification of the amino acid from K to Q at position 126.
+The natural variant of this protein is characterized by an amino acid alteration from L to F at position 183.
+The protein's natural variant, known as in MCPH17; impairs kinase activity; exhibits abnormal mitotic cytokinesis; exhibits multipolar spindles; increases the neurons apoptotic process;, features a modification of the amino acid from D to V at position 230.
+The natural variant of this protein is characterized by an amino acid alteration from S to R at position 86.
+The natural variant of this protein is characterized by an amino acid alteration from S to Q at position 309.
+The natural variant of this protein is characterized by an amino acid alteration from H to Y at position 322.
+The protein's natural variant, known as in strain: B141, M2, M40 and MJ2, features a modification of the amino acid from V to L at position 10.
+The protein's natural variant, known as in strain: B208, features a modification of the amino acid from L to I at position 12.
+The protein's natural variant, known as in strain: Z24, features a modification of the amino acid from A to V at position 43.
+The protein's natural variant, known as in strain: MA1, features a modification of the amino acid from A to V at position 54.
+The protein's natural variant, known as in strain: B222, B226, Z10, Z22, Z18 and Z24, features a modification of the amino acid from A to G at position 59.
+The protein's natural variant, known as in ISOD; 2% of activity;, features a modification of the amino acid from R to Q at position 217.
+The protein's natural variant, known as in ISOD, features a modification of the amino acid from I to L at position 258.
+The protein's natural variant, known as in ISOD;, features a modification of the amino acid from A to D at position 265.
+The protein's natural variant, known as in ISOD;, features a modification of the amino acid from R to Q at position 268.
+The protein's natural variant, known as in ISOD;, features a modification of the amino acid from G to S at position 362.
+The protein's natural variant, known as in ISOD;, features a modification of the amino acid from R to H at position 366.
+The protein's natural variant, known as in ISOD;, features a modification of the amino acid from K to R at position 379.
+The protein's natural variant, known as in ISOD, features a modification of the amino acid from Q to R at position 396.
+The protein's natural variant, known as in ISOD, features a modification of the amino acid from S to Y at position 427.
+The protein's natural variant, known as in ISOD, features a modification of the amino acid from W to R at position 450.
+The protein's natural variant, known as in ISOD;, features a modification of the amino acid from G to D at position 530.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from G to E at position 316.
+The protein's natural variant, known as in DEDISB; decreased protein abundance;, features a modification of the amino acid from D to N at position 798.
+The protein's natural variant, known as in allele Gogo-TAP1b, features a modification of the amino acid from I to V at position 233.
+The protein's natural variant, known as in allele Gogo-TAP1b, features a modification of the amino acid from T to M at position 273.
+The protein's natural variant, known as in allele Gogo-TAP1b, features a modification of the amino acid from C to S at position 619.
+The protein's natural variant, known as in allele Gogo-TAP1c, features a modification of the amino acid from P to R at position 629.
+The protein's natural variant, known as in thermosensitive mutant pheS5; might cause subunit disaggregation due to electrostatic repulsion, features a modification of the amino acid from G to D at position 98.
+The protein's natural variant, known as decreased affinity for Phe, features a modification of the amino acid from G to D at position 191.
+The natural variant of this protein is characterized by an amino acid alteration from K to L at position 8.
+The natural variant of this protein is characterized by an amino acid alteration from E to D at position 35.
+The natural variant of this protein is characterized by an amino acid alteration from E to D at position 36.
+The natural variant of this protein is characterized by an amino acid alteration from K to T at position 39.
+The natural variant of this protein is characterized by an amino acid alteration from H to N at position 43.
+The protein's natural variant, known as in toxin V(II)2A, features a modification of the amino acid from M to V at position 52.
+The protein's natural variant, known as in toxin V(II)2A, features a modification of the amino acid from N to S at position 55.
+The protein's natural variant, known as in strain: MA97_6, features a modification of the amino acid from L to I at position 54.
+The protein's natural variant, known as in strain: ZIM(S)49 and ZIM(H)44, features a modification of the amino acid from S to A at position 132.
+The protein's natural variant, known as in strain: CT97_3, MFL97_1 and ZIM(S)37, features a modification of the amino acid from D to N at position 151.
+The protein's natural variant, known as in strain: ZIM(S)49 and ZIM(H)44, features a modification of the amino acid from F to V at position 281.
+The protein's natural variant, known as in strain: DPF96_3.0, HFL97_15, JFL97_1, JFL97_9 and ZIM(S)37, features a modification of the amino acid from H to N at position 357.
+The protein's natural variant, known as in strain: ZIM(S)35, features a modification of the amino acid from T to N at position 387.
+The protein's natural variant, known as in strain: ZIM(H)23, features a modification of the amino acid from A to V at position 407.
+The protein's natural variant, known as in mutant TRPB8, features a modification of the amino acid from G to R at position 281.
+The protein's natural variant, known as in strain: K12 / W3110 / ATCC 27325 / DSM 5911, features a modification of the amino acid from A to V at position 130.
+The natural variant of this protein is characterized by an amino acid alteration from I to L at position 4.
+The natural variant of this protein is characterized by an amino acid alteration from V to A at position 14.
+The natural variant of this protein is characterized by an amino acid alteration from A to S at position 24.
+The natural variant of this protein is characterized by an amino acid alteration from S to A at position 75.
+The natural variant of this protein is characterized by an amino acid alteration from T to S at position 129.
+The protein's natural variant, known as in AI1B and AI1C; decreased phosphorylation by FAM20C;, features a modification of the amino acid from S to L at position 216.
+The protein's natural variant, known as in a breast infiltrating ductal carcinoma sample; somatic mutation;, features a modification of the amino acid from S to L at position 236.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from L to V at position 110.
+The protein's natural variant, known as in ASGD2; unknown pathological significance;, features a modification of the amino acid from M to V at position 82.
+The protein's natural variant, known as in ASGD2; significant reduction of sequence-specific DNA binding transcription factor activity;, features a modification of the amino acid from R to L at position 90.
+The protein's natural variant, known as in CTRCT34; decreases DNAJB1 expression;, features a modification of the amino acid from E to K at position 103.
+The protein's natural variant, known as in CTRCT34; decreases DNAJB1 expression;, features a modification of the amino acid from N to K at position 117.
+The protein's natural variant, known as in ASGD2; complete loss of DNA binding; significant reduction of sequence-specific DNA binding transcription factor activity, features a modification of the amino acid from R to G at position 120.
+The protein's natural variant, known as in AAT11;, features a modification of the amino acid from G to D at position 137.
+The protein's natural variant, known as in AAT11;, features a modification of the amino acid from D to H at position 153.
+The protein's natural variant, known as in strain: IOL-207, features a modification of the amino acid from C to S at position 20.
+The natural variant of this protein is characterized by an amino acid alteration from C to V at position 955.
+The protein's natural variant, known as in strain: CWL029 and TW-183, features a modification of the amino acid from T to A at position 108.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from S to R at position 266.
+The protein's natural variant, known as in CMO-1 deficiency; the enzyme is inactive, features a modification of the amino acid from N to NRL at position 140.
+The protein's natural variant, known as in CMO-2 deficiency; reduces 18-hydroxylase and abolishes 18-oxidase activities; leaves 11 beta-hydroxylase activity intact;, features a modification of the amino acid from R to W at position 181.
+The protein's natural variant, known as in CMO-2 deficiency;, features a modification of the amino acid from T to I at position 185.
+The protein's natural variant, known as in CMO-2 deficiency; slightly reduced 11-beta-hydroxylase activity, greatly decreased 18-hydroxylase activity and absent 18-oxidase activity when associated with A-386.;, features a modification of the amino acid from E to D at position 198.
+The protein's natural variant, known as in CMO-2 deficiency; small but consistent reduction in the production of 18-hydroxycorticosterone; slightly reduced 11-beta-hydroxylase activity, greatly decreased 18-hydroxylase activity and absent 18-oxidase activity when associated with D-198.;, features a modification of the amino acid from V to A at position 386.
+The protein's natural variant, known as in CMO-1 deficiency; abolishes the 18-hydroxylase activity required for conversion of 11-deoxycorticosterone to aldosterone;, features a modification of the amino acid from L to P at position 461.
+The protein's natural variant, known as in CMO-2 deficiency;, features a modification of the amino acid from T to A at position 498.
+The protein's natural variant, known as in strain: Isolate AMNH 101508, features a modification of the amino acid from L to F at position 18.
+The protein's natural variant, known as in strain: LSU1037-1, LSU1037-5, LSU1062-1, LSU1062-3, LSU2003-1 and LSU2003-7, features a modification of the amino acid from I to V at position 42.
+The protein's natural variant, known as in strain: 85P, HPK5, LSU1037-1, LSU1037-5, LSU1062-1, LSU1062-3, LSU2003-1 and LSU2003-7, features a modification of the amino acid from I to V at position 45.
+The protein's natural variant, known as in strain: LSU2003-1 and LSU2003-7, features a modification of the amino acid from V to A at position 47.
+The protein's natural variant, known as in strain: LSU2003-1 and LSU2003-7, features a modification of the amino acid from S to F at position 51.
+The protein's natural variant, known as in strain: LSU2003-7, features a modification of the amino acid from L to V at position 53.
+The protein's natural variant, known as in strain: 85P, HPK5 and NQ1712, features a modification of the amino acid from H to N at position 54.
+The protein's natural variant, known as in strain: LSU1037-1, LSU1037-5, LSU1062-1, LSU1062-3, LSU2003-1, LSU2003-7 and NQ1712, features a modification of the amino acid from A to V at position 66.
+The protein's natural variant, known as in strain: 85P and HPK5, features a modification of the amino acid from S to N at position 74.
+The protein's natural variant, known as in strain: HPK5, features a modification of the amino acid from G to E at position 77.
+The protein's natural variant, known as in strain: HPK5, features a modification of the amino acid from N to S at position 94.
+The protein's natural variant, known as in strain: HPK5, features a modification of the amino acid from G to N at position 98.
+The protein's natural variant, known as in strain: LSU1037-1, LSU1037-5, LSU1062-1, LSU1062-3, LSU2003-1 and LSU2003-7, features a modification of the amino acid from I to V at position 116.
+The protein's natural variant, known as in strain: LSU1037-1, features a modification of the amino acid from P to L at position 171.
+The protein's natural variant, known as in AO2; significant loss of sulfate transport;, features a modification of the amino acid from G to E at position 255.
+The protein's natural variant, known as in EDM4;, features a modification of the amino acid from F to S at position 256.
+The protein's natural variant, known as in AO2 and EDM4; reduced sulfate transport; significant reduction in sulfate-oxalate exchange activity; no effect on cell membrane localization;, features a modification of the amino acid from R to W at position 279.
+The protein's natural variant, known as in ACG1B; significant loss of sulfate transport;, features a modification of the amino acid from N to D at position 425.
+The protein's natural variant, known as in diatrophic dysplasia; broad bone-platyspondylic variant; no effect on sulfate transport and cell membrane localization;, features a modification of the amino acid from Q to P at position 454.
+The protein's natural variant, known as in EDM4; no effect on sulfate transport and cell membrane localization;, features a modification of the amino acid from C to S at position 653.
+The protein's natural variant, known as in ACG1B; reduced sulfate transport; loss of cell membrane localization;, features a modification of the amino acid from G to V at position 678.
+The protein's natural variant, known as in AO2 and EDM4; no effect on sulfate transport and cell membrane localization;, features a modification of the amino acid from A to V at position 715.
+The protein's natural variant, known as in MRT5; impairs proper intracellular localization;, features a modification of the amino acid from G to R at position 679.
+The natural variant of this protein is characterized by an amino acid alteration from PRS to SRY at position 23.
+The protein's natural variant, known as in HLD21; decrease in expression levels of RNA polymerase III-transcribed genes such as 5S and 7S ribosomal RNAs;, features a modification of the amino acid from R to W at position 41.
+The protein's natural variant, known as in vestibular schwannoma; loss of ability to interact with the CUL4A-RBX1-DDB1-VprBP/DCAF1 E3 ubiquitin-protein ligase complex, features a modification of the amino acid from L to R at position 46.
+The protein's natural variant, known as in NF2; loss of ability to interact with the CUL4A-RBX1-DDB1-VprBP/DCAF1 E3 ubiquitin-protein ligase complex;, features a modification of the amino acid from F to S at position 62.
+The protein's natural variant, known as in NF2, features a modification of the amino acid from M to V at position 77.
+The protein's natural variant, known as in vestibular schwannoma, features a modification of the amino acid from K to E at position 79.
+The protein's natural variant, known as in NF2, features a modification of the amino acid from E to G at position 106.
+The protein's natural variant, known as in sporadic meningioma, features a modification of the amino acid from L to I at position 117.
+The protein's natural variant, known as in NF2, features a modification of the amino acid from C to R at position 133.
+The protein's natural variant, known as in NF2; loss of ability to interact with the CUL4A-RBX1-DDB1-VprBP/DCAF1 E3 ubiquitin-protein ligase complex, features a modification of the amino acid from L to P at position 141.
+The protein's natural variant, known as in NF2, features a modification of the amino acid from G to C at position 197.
+The protein's natural variant, known as in vestibular schwannoma; changed interaction with SCHIP1;, features a modification of the amino acid from V to M at position 219.
+The protein's natural variant, known as in NF2;, features a modification of the amino acid from N to Y at position 220.
+The protein's natural variant, known as in NF2; also found in retinal hamartoma; severe, features a modification of the amino acid from L to R at position 234.
+The protein's natural variant, known as in breast ductal carcinoma, features a modification of the amino acid from I to F at position 273.
+The protein's natural variant, known as in sporadic meningioma, features a modification of the amino acid from L to F at position 339.
+The protein's natural variant, known as in NF2;, features a modification of the amino acid from T to M at position 352.
+The protein's natural variant, known as in NF2;, features a modification of the amino acid from L to P at position 360.
+The protein's natural variant, known as in melanoma, features a modification of the amino acid from K to I at position 364.
+The protein's natural variant, known as in NF2;, features a modification of the amino acid from K to E at position 413.
+The protein's natural variant, known as in vestibular schwannoma;, features a modification of the amino acid from R to C at position 418.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from E to K at position 463.
+The protein's natural variant, known as in NF2, features a modification of the amino acid from K to T at position 533.
+The protein's natural variant, known as in NF2; late onset;, features a modification of the amino acid from L to P at position 535.
+The protein's natural variant, known as in NF2; mild;, features a modification of the amino acid from Q to P at position 538.
+The protein's natural variant, known as in NF2, features a modification of the amino acid from L to H at position 539.
+The protein's natural variant, known as in NF2, features a modification of the amino acid from K to M at position 579.
+The protein's natural variant, known as in strain: Gbab1064e, Gbab1068c, Gbab5010bs, Gbab5011f, Gbab5024h, Gbbkj16034a, Gbjo4i, Gbjo8h, Gbjo12g, Gbjo15as, Gbng3334as and Gbng3365b, features a modification of the amino acid from T to A at position 9.
+The protein's natural variant, known as in strain: Gbab1068c, Gbab5011f and Gbab5024h, features a modification of the amino acid from A to S at position 15.
+The protein's natural variant, known as in strain: Gbbkj16015a, Gbbkj16024b, Gbbkj16025b, Gbbkj16032b and Gbng3347f, features a modification of the amino acid from L to F at position 18.
+The protein's natural variant, known as in strain: Gbab1068c, Gbab5010bs, Gbab5011f, Gbab5024h, Gbbkj16015a, Gbbkj16024b, Gbbkj16025b, Gbbkj16032b, Gbbkj16034a, Gbjo4i, Gbjo6e, Gbjo7h, Gbjo8h, Gbjo9a, Gbjo12g, Gbjo14c, Gbjo15as, Gbjo22d, Gbng3336g, Gbng3339b, Gbng3340f and Gbng3347f, features a modification of the amino acid from S to G at position 34.
+The protein's natural variant, known as in strain: Gbng3343c, features a modification of the amino acid from AN to VS at position 38.
+The protein's natural variant, known as in strain: Gbng3337bs, features a modification of the amino acid from A to G at position 37.
+The protein's natural variant, known as in strain: Gbab1068c, Gbab5011f, Gbab5024h and Gbng3336g, features a modification of the amino acid from A to V at position 37.
+The protein's natural variant, known as in strain: Gbjo6e, features a modification of the amino acid from H to L at position 51.
+The protein's natural variant, known as in strain: Gbng3365b, features a modification of the amino acid from S to R at position 69.
+The protein's natural variant, known as in strain: KWA, features a modification of the amino acid from SS to NN at position 76.
+The protein's natural variant, known as in strain: Gbjo3a, features a modification of the amino acid from K to R at position 95.
+The protein's natural variant, known as in plasmid pYVa127/90, features a modification of the amino acid from S to P at position 81.
+The protein's natural variant, known as in plasmid pYVa127/90, features a modification of the amino acid from P to S at position 114.
+The protein's natural variant, known as in 3MC3; severely decreased secretion;, features a modification of the amino acid from C to W at position 176.
+The protein's natural variant, known as in allele PXR*2;, features a modification of the amino acid from P to S at position 27.
+The protein's natural variant, known as in allele PXR*3;, features a modification of the amino acid from G to R at position 36.
+The protein's natural variant, known as in allele PXR*4;, features a modification of the amino acid from R to Q at position 122.
+The protein's natural variant, known as in CAFD2;, features a modification of the amino acid from S to L at position 54.
+The protein's natural variant, known as in CAFD2, features a modification of the amino acid from H to N at position 88.
+The protein's natural variant, known as in CAFD2; increased sensitivity to cAMP activation;, features a modification of the amino acid from H to R at position 88.
+The protein's natural variant, known as in CAFD2; increased sensitivity to cAMP activation; decreased interaction with regulatory subunits PRKAR1A and PRKAR2B, features a modification of the amino acid from G to R at position 235.
+The protein's natural variant, known as in strain: Leghorn, features a modification of the amino acid from L to S at position 837.
+The protein's natural variant, known as in strain: Leghorn, features a modification of the amino acid from W to C at position 932.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from L to M at position 235.
+The protein's natural variant, known as in PSS3; results in decreased enzyme activity; the mutant protein shows reduced glycosylation;, features a modification of the amino acid from R to W at position 77.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to H at position 247.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from R to H at position 143.
+The protein's natural variant, known as in a renal clear cell carcinoma sample; somatic mutation, features a modification of the amino acid from G to S at position 171.
+The protein's natural variant, known as in a glioblastoma multiforme sample; somatic mutation, features a modification of the amino acid from G to R at position 177.
+The protein's natural variant, known as in MRD59; gain-of-function variant affecting regulation of neurite formation and arborization; results in constitutive autophosphorylation;, features a modification of the amino acid from R to P at position 292.
+The protein's natural variant, known as in NYS1, features a modification of the amino acid from F to S at position 16.
+The protein's natural variant, known as in NYS1, features a modification of the amino acid from G to E at position 24.
+The protein's natural variant, known as in NYS1;, features a modification of the amino acid from G to R at position 24.
+The protein's natural variant, known as in NYS1, features a modification of the amino acid from G to W at position 24.
+The protein's natural variant, known as in NYS1;, features a modification of the amino acid from L to R at position 142.
+The protein's natural variant, known as in NYS1;, features a modification of the amino acid from R to W at position 146.
+The protein's natural variant, known as in NYS1, features a modification of the amino acid from H to R at position 208.
+The protein's natural variant, known as in NYS1; decreased RAC1 activity, features a modification of the amino acid from L to P at position 212.
+The protein's natural variant, known as in NYS1, features a modification of the amino acid from N to D at position 221.
+The protein's natural variant, known as in NYS1, features a modification of the amino acid from W to G at position 225.
+The protein's natural variant, known as in NYS1, features a modification of the amino acid from A to T at position 226.
+The protein's natural variant, known as in NYS1;, features a modification of the amino acid from R to C at position 229.
+The protein's natural variant, known as in NYS1;, features a modification of the amino acid from R to G at position 229.
+The protein's natural variant, known as in NYS1;, features a modification of the amino acid from L to V at position 231.
+The protein's natural variant, known as in NYS1, features a modification of the amino acid from R to G at position 261.
+The protein's natural variant, known as in NYS1;, features a modification of the amino acid from R to Q at position 261.
+The protein's natural variant, known as in NYS1, features a modification of the amino acid from A to P at position 266.
+The protein's natural variant, known as in NYS1;, features a modification of the amino acid from C to F at position 271.
+The protein's natural variant, known as in NYS1, features a modification of the amino acid from C to S at position 271.
+The protein's natural variant, known as in NYS1;, features a modification of the amino acid from C to Y at position 271.
+The protein's natural variant, known as in NYS1, features a modification of the amino acid from H to P at position 275.
+The protein's natural variant, known as in NYS1;, features a modification of the amino acid from G to R at position 296.
+The protein's natural variant, known as in NYS1;, features a modification of the amino acid from Y to C at position 301.
+The protein's natural variant, known as in NYS1, features a modification of the amino acid from Q to R at position 306.
+The protein's natural variant, known as in NYS1, features a modification of the amino acid from S to L at position 340.
+The protein's natural variant, known as in sacT30 mutant, features a modification of the amino acid from D to Y at position 96.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from G to E at position 29.
+The protein's natural variant, known as in TTD4;, features a modification of the amino acid from M to V at position 144.
+The protein's natural variant, known as in strain: Nv2001_m0595 and NVIII-m11, features a modification of the amino acid from T to A at position 11.
+The protein's natural variant, known as in strain: Nv2001_m0592, features a modification of the amino acid from R to P at position 63.
+The protein's natural variant, known as in strain: NVIII-41, features a modification of the amino acid from E to K at position 82.
+The natural variant of this protein is characterized by an amino acid alteration from H to R at position 8.
+The natural variant of this protein is characterized by an amino acid alteration from V to L at position 28.
+The natural variant of this protein is characterized by an amino acid alteration from R to C at position 286.
+The protein's natural variant, known as in MEDS2; unknown pathological significance, features a modification of the amino acid from G to V at position 97.
+The protein's natural variant, known as in MEDS2; no effect on differentiation and function of pancreatic beta cells; increased endoplasmic reticulum stress-induced apoptosis; decreased in C-peptide levels associated with increased proinsulin accumulation, features a modification of the amino acid from I to S at position 98.
+The protein's natural variant, known as in MEDS2; unknown pathological significance, features a modification of the amino acid from A to V at position 181.
+The protein's natural variant, known as in MEDS2; unknown pathological significance, features a modification of the amino acid from W to R at position 218.
+The protein's natural variant, known as in DPSL; unknown pathological significance; when transfected in HEK293T cells it results in slightly reduced WNT signaling; decreased protein expression in transfected cells;, features a modification of the amino acid from I to V at position 96.
+The protein's natural variant, known as in DPSL; unknown pathological significance; when transfected in HEK293T cells it results in slightly reduced WNT signaling; decreased protein expression in transfected cells, features a modification of the amino acid from G to C at position 363.
+The protein's natural variant, known as in DPSL; unknown pathological significance; when transfected in HEK293T cells has no effect on WNT signaling; decreased protein expression in transfected cells;, features a modification of the amino acid from D to G at position 844.
+The protein's natural variant, known as in minor variant, features a modification of the amino acid from Q to E at position 64.
+The natural variant of this protein is characterized by an amino acid alteration from M to T at position 238.
+The protein's natural variant, known as in JEB4, features a modification of the amino acid from S to C at position 265.
+The protein's natural variant, known as in JEB4, features a modification of the amino acid from G to V at position 627.
+The protein's natural variant, known as in JEB4;, features a modification of the amino acid from G to D at position 633.
+The protein's natural variant, known as in ERED;, features a modification of the amino acid from T to I at position 939.
+The protein's natural variant, known as in JEB4;, features a modification of the amino acid from R to Q at position 1303.
+The protein's natural variant, known as in BDPLT19; patient platelets show impaired activation;, features a modification of the amino acid from I to M at position 74.
+The protein's natural variant, known as in AMRS, features a modification of the amino acid from R to C at position 25.
+The protein's natural variant, known as in susceptible haplotype, features a modification of the amino acid from R to K at position 154.
+The protein's natural variant, known as in susceptible haplotype, features a modification of the amino acid from E to K at position 173.
+The protein's natural variant, known as in susceptible haplotype, features a modification of the amino acid from Y to F at position 775.
+The protein's natural variant, known as in susceptible haplotype, features a modification of the amino acid from L to P at position 782.
+The protein's natural variant, known as in susceptible haplotype, features a modification of the amino acid from KGA to EGE at position 810.
+The protein's natural variant, known as in susceptible haplotype, features a modification of the amino acid from G to R at position 847.
+The protein's natural variant, known as in susceptible haplotype, features a modification of the amino acid from N to S at position 879.
+The protein's natural variant, known as in susceptible haplotype, features a modification of the amino acid from I to K at position 884.
+The protein's natural variant, known as in susceptible haplotype, features a modification of the amino acid from F to Y at position 890.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from K to N at position 313.
+The protein's natural variant, known as in putative neurotoxin 8, features a modification of the amino acid from P to R at position 101.
+The protein's natural variant, known as in allele alpha-2A;, features a modification of the amino acid from R to K at position 46.
+The protein's natural variant, known as in allele alpha-2C;, features a modification of the amino acid from H to R at position 57.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from S to L at position 177.
+The protein's natural variant, known as in AMYL-TTR; amyloid polyneuropathy;, features a modification of the amino acid from C to R at position 30.
+The protein's natural variant, known as in AMYL-TTR;, features a modification of the amino acid from L to P at position 32.
+The natural variant of this protein is characterized by an amino acid alteration from M to I at position 33.
+The protein's natural variant, known as in AMYL-TTR; amyloid polyneuropathy, features a modification of the amino acid from D to E at position 38.
+The protein's natural variant, known as in AMYL-TTR; leptomeningeal amyloidosis; leads to unfolding and exposure of N-118 to glycosylation by STT3B and subsequent degradation by the ERAD pathway;, features a modification of the amino acid from D to G at position 38.
+The protein's natural variant, known as in AMYL-TTR; late-onset amyloid polyneuropathy with carpal tunnel syndrome;, features a modification of the amino acid from V to I at position 40.
+The protein's natural variant, known as in AMYL-TTR, features a modification of the amino acid from S to N at position 43.
+The protein's natural variant, known as in AMYL-TTR; amyloid polyneuropathy;, features a modification of the amino acid from P to S at position 44.
+The protein's natural variant, known as in AMYL-TTR; amyloid polyneuropathy, features a modification of the amino acid from V to M at position 48.
+The protein's natural variant, known as in AMYL-TTR; amyloid polyneuropathy;, features a modification of the amino acid from V to A at position 50.
+The protein's natural variant, known as in AMYL-TTR;, features a modification of the amino acid from V to G at position 50.
+The protein's natural variant, known as in AMYL-TTR; amyloid polyneuropathy;, features a modification of the amino acid from V to L at position 50.
+The protein's natural variant, known as in AMYL-TTR; amyloid polyneuropathy; by far the most frequent mutation;, features a modification of the amino acid from V to M at position 50.
+The protein's natural variant, known as in a patient with amyloidosis, features a modification of the amino acid from F to C at position 53.
+The protein's natural variant, known as in AMYL-TTR; Jewish 'SKO' amyloid polyneuropathy;, features a modification of the amino acid from F to I at position 53.
+The protein's natural variant, known as in AMYL-TTR; amyloid polyneuropathy;, features a modification of the amino acid from F to L at position 53.
+The protein's natural variant, known as in AMYL-TTR; amyloid polyneuropathy, features a modification of the amino acid from F to V at position 53.
+The protein's natural variant, known as in AMYL-TTR, features a modification of the amino acid from R to T at position 54.
+The protein's natural variant, known as in AMYL-TTR; amyloid polyneuropathy, features a modification of the amino acid from K to N at position 55.
+The protein's natural variant, known as in AMYL-TTR; amyloid polyneuropathy;, features a modification of the amino acid from A to P at position 56.
+The protein's natural variant, known as in AMYL-TTR, features a modification of the amino acid from D to A at position 58.
+The protein's natural variant, known as in AMYL-TTR, features a modification of the amino acid from D to V at position 58.
+The protein's natural variant, known as in AMYL-TTR, features a modification of the amino acid from W to L at position 61.
+The protein's natural variant, known as in AMYL-TTR;, features a modification of the amino acid from E to D at position 62.
+The protein's natural variant, known as in AMYL-TTR; amyloid polyneuropathy;, features a modification of the amino acid from E to G at position 62.
+The protein's natural variant, known as in AMYL-TTR;, features a modification of the amino acid from F to S at position 64.
+The protein's natural variant, known as in AMYL-TTR; amyloid cardiomyopathy;, features a modification of the amino acid from A to D at position 65.
+The protein's natural variant, known as in AMYL-TTR, features a modification of the amino acid from A to S at position 65.
+The protein's natural variant, known as in AMYL-TTR; amyloid cardiomyopathy;, features a modification of the amino acid from A to T at position 65.
+The protein's natural variant, known as in AMYL-TTR; amyloid polyneuropathy;, features a modification of the amino acid from G to A at position 67.
+The protein's natural variant, known as in AMYL-TTR, features a modification of the amino acid from G to E at position 67.
+The protein's natural variant, known as in AMYL-TTR; amyloid polyneuropathy;, features a modification of the amino acid from G to R at position 67.
+The protein's natural variant, known as in AMYL-TTR; amyloid polyneuropathy with carpal tunnel syndrome, features a modification of the amino acid from G to V at position 67.
+The protein's natural variant, known as in AMYL-TTR; amyloid polyneuropathy;, features a modification of the amino acid from T to A at position 69.
+The protein's natural variant, known as in AMYL-TTR, features a modification of the amino acid from T to I at position 69.
+The protein's natural variant, known as in AMYL-TTR; amyloid cardiomyopathy;, features a modification of the amino acid from S to I at position 70.
+The protein's natural variant, known as in AMYL-TTR; amyloid polyneuropathy;, features a modification of the amino acid from S to R at position 70.
+The protein's natural variant, known as in AMYL-TTR; amyloid polyneuropathy, features a modification of the amino acid from S to P at position 72.
+The protein's natural variant, known as in AMYL-TTR;, features a modification of the amino acid from G to E at position 73.
+The protein's natural variant, known as in AMYL-TTR; amyloid polyneuropathy, features a modification of the amino acid from E to G at position 74.
+The protein's natural variant, known as in AMYL-TTR; early-onset amyloid polyneuropathy, features a modification of the amino acid from E to K at position 74.
+The protein's natural variant, known as in AMYL-TTR; amyloid polyneuropathy;, features a modification of the amino acid from L to P at position 75.
+The protein's natural variant, known as in AMYL-TTR, features a modification of the amino acid from L to Q at position 75.
+The protein's natural variant, known as in AMYL-TTR; amyloid polyneuropathy;, features a modification of the amino acid from L to H at position 78.
+The protein's natural variant, known as in AMYL-TTR; amyloid polyneuropathy;, features a modification of the amino acid from L to R at position 78.
+The protein's natural variant, known as in AMYL-TTR; amyloid cardiomyopathy;, features a modification of the amino acid from T to K at position 79.
+The protein's natural variant, known as in AMYL-TTR; amyloid polyneuropathy and cardiomyopathy;, features a modification of the amino acid from T to A at position 80.
+The protein's natural variant, known as in AMYL-TTR, features a modification of the amino acid from E to G at position 81.
+The protein's natural variant, known as in AMYL-TTR; amyloid polyneuropathy;, features a modification of the amino acid from E to K at position 81.
+The protein's natural variant, known as in AMYL-TTR; amyloid polyneuropathy;, features a modification of the amino acid from F to L at position 84.
+The protein's natural variant, known as in AMYL-TTR; amyloid cardiomyopathy;, features a modification of the amino acid from I to L at position 88.
+The protein's natural variant, known as in AMYL-TTR; leptomeningeal amyloidosis; vitreous amyloid in some patients;, features a modification of the amino acid from Y to H at position 89.
+The protein's natural variant, known as in AMYL-TTR; amyloid polyneuropathy;, features a modification of the amino acid from K to N at position 90.
+The protein's natural variant, known as in AMYL-TTR; amyloid polyneuropathy;, features a modification of the amino acid from V to A at position 91.
+The protein's natural variant, known as in AMYL-TTR; amyloid polyneuropathy, features a modification of the amino acid from I to V at position 93.
+The protein's natural variant, known as in AMYL-TTR; amyloid polyneuropathy;, features a modification of the amino acid from S to Y at position 97.
+The protein's natural variant, known as in AMYL-TTR;, features a modification of the amino acid from Y to F at position 98.
+The protein's natural variant, known as in AMYL-TTR; vitrous amyloid, features a modification of the amino acid from I to N at position 104.
+The protein's natural variant, known as in AMYL-TTR; amyloid polyneuropathy; almost no RBP binding;, features a modification of the amino acid from I to S at position 104.
+The protein's natural variant, known as in AMYL-TTR, features a modification of the amino acid from I to T at position 104.
+The protein's natural variant, known as in AMYL-TTR; amyloid polyneuropathy, features a modification of the amino acid from E to K at position 109.
+The protein's natural variant, known as in AMYL-TTR; amyloid polyneuropathy and cardiomyopathy;, features a modification of the amino acid from E to Q at position 109.
+The protein's natural variant, known as in AMYL-TTR; amyloid polyneuropathy, features a modification of the amino acid from A to S at position 111.
+The protein's natural variant, known as in a patient with amyloidosis, features a modification of the amino acid from V to A at position 114.
+The protein's natural variant, known as in AMYL-TTR; amyloid polyneuropathy;, features a modification of the amino acid from A to G at position 117.
+The protein's natural variant, known as in AMYL-TTR;, features a modification of the amino acid from A to S at position 117.
+The natural variant of this protein is characterized by an amino acid alteration from P to R at position 122.
+The protein's natural variant, known as in AMYL-TTR;, features a modification of the amino acid from T to N at position 126.
+The protein's natural variant, known as in AMYL-TTR, features a modification of the amino acid from I to M at position 127.
+The protein's natural variant, known as in AMYL-TTR; amyloid polyneuropathy;, features a modification of the amino acid from I to V at position 127.
+The protein's natural variant, known as in DTTRH; increased affinity for thyroxine;, features a modification of the amino acid from A to T at position 129.
+The protein's natural variant, known as in AMYL-TTR;, features a modification of the amino acid from L to M at position 131.
+The protein's natural variant, known as in AMYL-TTR; amyloid polyneuropathy;, features a modification of the amino acid from Y to C at position 134.
+The protein's natural variant, known as in CTS1; amyloid deposit on carpal tunnel; patients show no other abnormalities;, features a modification of the amino acid from Y to H at position 134.
+The protein's natural variant, known as in AMYL-TTR; amyloid polyneuropathy;, features a modification of the amino acid from Y to S at position 136.
+The protein's natural variant, known as requires 2 nucleotide substitutions, features a modification of the amino acid from Y to V at position 136.
+The protein's natural variant, known as in Chicago variant;, features a modification of the amino acid from T to M at position 139.
+The protein's natural variant, known as in AMYL-TTR;, features a modification of the amino acid from A to S at position 140.
+The protein's natural variant, known as in AMYL-TTR, features a modification of the amino acid from V to A at position 142.
+The protein's natural variant, known as in AMYL-TTR;, features a modification of the amino acid from V to I at position 142.
+The protein's natural variant, known as in AMYL-TTR;, features a modification of the amino acid from N to S at position 144.
+The natural variant of this protein is characterized by an amino acid alteration from V to M at position 21.
+The protein's natural variant, known as in DEE25; no loss of localization to plasma membrane; loss of function in citrate transport;, features a modification of the amino acid from T to M at position 142.
+The protein's natural variant, known as loss of localization to plasma membrane; loss of function in citrate transport;, features a modification of the amino acid from G to E at position 219.
+The protein's natural variant, known as in DEE25; loss of function in citrate transport; loss of localization to plasma membrane;, features a modification of the amino acid from G to R at position 219.
+The protein's natural variant, known as in DEE25; loss of function in citrate transport; no effect on localization to plasma membrane;, features a modification of the amino acid from T to M at position 227.
+The protein's natural variant, known as no effect on localization to plasma membrane; no effect on its function in citrate transport;, features a modification of the amino acid from D to N at position 243.
+The protein's natural variant, known as loss of localization to plasma membrane; loss of function in citrate transport;, features a modification of the amino acid from L to P at position 420.
+The protein's natural variant, known as in DEE25; loss of localization to plasma membrane; loss of function in citrate transport;, features a modification of the amino acid from S to L at position 427.
+The protein's natural variant, known as no effect on localization to plasma membrane; reduced function in citrate transport; increased Km and Vmax values compared with that of wild type with citrate as substrate;, features a modification of the amino acid from L to R at position 485.
+The protein's natural variant, known as in DEE25; loss of function in citrate transport; loss of localization to plasma membrane;, features a modification of the amino acid from L to P at position 488.
+The protein's natural variant, known as in DEE25; loss of function in citrate transport; no effect on localization to plasma membrane;, features a modification of the amino acid from D to H at position 524.
+The protein's natural variant, known as in an ovarian mucinous carcinoma sample; somatic mutation, features a modification of the amino acid from D to G at position 399.
+The protein's natural variant, known as found in a patient with neurodevelopmental disorder with hypotonia, dysmorphic facies and skin abnormalities; unknown pathological significance, features a modification of the amino acid from S to C at position 271.
+The protein's natural variant, known as in ATELS1, features a modification of the amino acid from N to I at position 861.
+The protein's natural variant, known as in strain: CBS 6938 / CCRC 22365 / VKMY-2793, features a modification of the amino acid from E to K at position 307.
+The protein's natural variant, known as in GM1G1 and GM1G2; decrease in galactosidase activity;, features a modification of the amino acid from R to C at position 49.
+The protein's natural variant, known as in GM1G3;, features a modification of the amino acid from R to H at position 49.
+The protein's natural variant, known as in GM1G3; no effect on catalytic activity; decreased protein stability;, features a modification of the amino acid from I to T at position 51.
+The protein's natural variant, known as in GM1G1; loss of galactosidase activity; severe mutation;, features a modification of the amino acid from R to C at position 59.
+The protein's natural variant, known as in GM1G1; with cardiac involvement in some patients; loss of galactosidase activity; severe mutation;, features a modification of the amino acid from R to H at position 59.
+The protein's natural variant, known as in GM1G2; 7.4% of wild-type galactosidase activity;, features a modification of the amino acid from R to Q at position 68.
+The protein's natural variant, known as in GM1G2 and GM1G1; loss of galactosidase activity;, features a modification of the amino acid from R to W at position 68.
+The protein's natural variant, known as in GM1G3, features a modification of the amino acid from K to E at position 73.
+The protein's natural variant, known as in GM1G3; mild phenotype;, features a modification of the amino acid from T to M at position 82.
+The protein's natural variant, known as in MPS4B; decrease in galactosidase activity;, features a modification of the amino acid from Y to C at position 83.
+The protein's natural variant, known as in MPS4B; 2-5% of wild-type galactosidase activity;, features a modification of the amino acid from Y to H at position 83.
+The protein's natural variant, known as in GM1G1;, features a modification of the amino acid from R to S at position 121.
+The protein's natural variant, known as in GM1G1; decrease in galactosidase activity;, features a modification of the amino acid from G to R at position 123.
+The protein's natural variant, known as in GM1G1; 4.3% of wild-type galactosidase activity;, features a modification of the amino acid from M to T at position 132.
+The protein's natural variant, known as in GM1G2; unknown pathological significance, features a modification of the amino acid from G to R at position 134.
+The protein's natural variant, known as in GM1G1;, features a modification of the amino acid from G to V at position 134.
+The protein's natural variant, known as in GM1G1;, features a modification of the amino acid from P to S at position 136.
+The protein's natural variant, known as in GM1G3 and GM1G2;, features a modification of the amino acid from R to C at position 148.
+The protein's natural variant, known as in GM1G1;, features a modification of the amino acid from R to S at position 148.
+The protein's natural variant, known as in MPS4B; 2.0% of wild-type galactosidase activity;, features a modification of the amino acid from S to F at position 149.
+The protein's natural variant, known as in GM1G1, features a modification of the amino acid from D to V at position 151.
+The protein's natural variant, known as in GM1G1; complete lack of protein; loss of galactosidase activity, features a modification of the amino acid from D to Y at position 151.
+The protein's natural variant, known as in GM1G2 and GM1G3; 6.7% of wild-type galactosidase activity;, features a modification of the amino acid from L to R at position 155.
+The protein's natural variant, known as in GM1G1; loss of galactosidase activity, features a modification of the amino acid from L to S at position 162.
+The protein's natural variant, known as in GM1G1; loss of galactosidase activity;, features a modification of the amino acid from L to P at position 173.
+The protein's natural variant, known as in GM1G1; loss of galactosidase activity, features a modification of the amino acid from Q to R at position 184.
+The protein's natural variant, known as in GM1G1; 3.4% of wild-type galactosidase activity;, features a modification of the amino acid from G to D at position 190.
+The protein's natural variant, known as in MPS4B; 17.4% of wild-type galactosidase activity, features a modification of the amino acid from D to Y at position 198.
+The protein's natural variant, known as in GM1G1, features a modification of the amino acid from Y to C at position 199.
+The protein's natural variant, known as in GM1G1 and GM1G2; no effect on intrinsic catalytic activity; decreased protein stability; 8.4% of wild-type galactosidase activity; activity severely reduced in transfection with variant F-436;, features a modification of the amino acid from R to C at position 201.
+The protein's natural variant, known as in GM1G1 and GM1G2; also in a patient with a slowly progressive GM1-gangliosidosis form; 36.2% of wild-type galactosidase activity;, features a modification of the amino acid from R to H at position 201.
+The protein's natural variant, known as in GM1G1;, features a modification of the amino acid from R to C at position 208.
+The protein's natural variant, known as in GM1G3, features a modification of the amino acid from D to Y at position 214.
+The protein's natural variant, known as in GM1G1;, features a modification of the amino acid from V to A at position 216.
+The protein's natural variant, known as in GM1G1; decrease in galactosidase activity, features a modification of the amino acid from L to P at position 236.
+The protein's natural variant, known as in GM1G1; loss of galactosidase activity; severe mutation; causes a rapid degradation of the protein precursor;, features a modification of the amino acid from T to M at position 239.
+The protein's natural variant, known as in GM1G1, features a modification of the amino acid from V to M at position 240.
+The protein's natural variant, known as in GM1G1; 2.4% of wild-type galactosidase activity;, features a modification of the amino acid from Q to H at position 255.
+The protein's natural variant, known as in GM1G2; decrease in galactosidase activity;, features a modification of the amino acid from G to E at position 262.
+The protein's natural variant, known as in GM1G3, features a modification of the amino acid from P to S at position 263.
+The protein's natural variant, known as in GM1G2, features a modification of the amino acid from L to S at position 264.
+The protein's natural variant, known as in GM1G3;, features a modification of the amino acid from N to S at position 266.
+The protein's natural variant, known as in GM1G3; originally classified as Morquio syndrome;, features a modification of the amino acid from Y to D at position 270.
+The protein's natural variant, known as in GM1G1, features a modification of the amino acid from G to D at position 272.
+The protein's natural variant, known as in MPS4B; decreased galactosidase activity;, features a modification of the amino acid from W to L at position 273.
+The protein's natural variant, known as in GM1G1 and GM1G3;, features a modification of the amino acid from H to Y at position 281.
+The protein's natural variant, known as in GM1G3; decrease in galactosidase activity, features a modification of the amino acid from L to F at position 297.
+The protein's natural variant, known as in GM1G2; decrease in galactosidase activity, features a modification of the amino acid from F to L at position 314.
+The protein's natural variant, known as in GM1G1;, features a modification of the amino acid from Y to C at position 316.
+The protein's natural variant, known as in GM1G1; unknown pathological significance, features a modification of the amino acid from N to H at position 318.
+The protein's natural variant, known as in GM1G1; 5.0% of wild-type galactosidase activity, features a modification of the amino acid from T to I at position 329.
+The protein's natural variant, known as in GM1G1; unknown pathological significance, features a modification of the amino acid from Y to C at position 331.
+The protein's natural variant, known as in GM1G1; 2.3% of wild-type galactosidase activity, features a modification of the amino acid from D to E at position 332.
+The protein's natural variant, known as in GM1G1; decrease in galactosidase activity;, features a modification of the amino acid from D to N at position 332.
+The protein's natural variant, known as in GM1G2; 3.0% of wild-type galactosidase activity; the mutant protein is localized in the lysosomal-endosomal compartment, features a modification of the amino acid from Y to H at position 333.
+The protein's natural variant, known as in GM1G1 and GM1G2; loss of galactosidase activity;, features a modification of the amino acid from L to P at position 337.
+The protein's natural variant, known as in GM1G1;, features a modification of the amino acid from K to N at position 346.
+The protein's natural variant, known as in GM1G1, features a modification of the amino acid from Y to C at position 347.
+The protein's natural variant, known as in MPS4B; 24.0% of wild-type galactosidase activity, features a modification of the amino acid from P to A at position 397.
+The protein's natural variant, known as in MPS4B; 1.1% of wild-type galactosidase activity;, features a modification of the amino acid from Q to P at position 408.
+The protein's natural variant, known as in GM1G2; decrease in galactosidase activity, features a modification of the amino acid from G to V at position 414.
+The protein's natural variant, known as in GM1G3; decrease in galactosidase activity, features a modification of the amino acid from T to K at position 420.
+The protein's natural variant, known as in GM1G1; loss of galactosidase activity;, features a modification of the amino acid from T to P at position 420.
+The protein's natural variant, known as in GM1G1;, features a modification of the amino acid from L to R at position 422.
+The protein's natural variant, known as in GM1-gangliosidosis; unclassified clinical type;, features a modification of the amino acid from S to L at position 434.
+The protein's natural variant, known as seems to have a modulating action in the expression of the severity of other mutations;, features a modification of the amino acid from L to F at position 436.
+The protein's natural variant, known as in GM1G3 and MPS4B; mild form; 5.7% of wild-type galactosidase activity;, features a modification of the amino acid from G to E at position 438.
+The protein's natural variant, known as in GM1G1; loss of galactosidase activity;, features a modification of the amino acid from D to N at position 441.
+The protein's natural variant, known as in GM1G1;, features a modification of the amino acid from R to Q at position 442.
+The protein's natural variant, known as in MPS4B; loss of galactosidase activity, features a modification of the amino acid from Y to C at position 444.
+The protein's natural variant, known as in GM1G3;, features a modification of the amino acid from R to Q at position 457.
+The protein's natural variant, known as in MPS4B; loss of galactosidase activity;, features a modification of the amino acid from R to C at position 482.
+The protein's natural variant, known as in MPS4B and GM1G1; severe decrease in galactosidase activity;, features a modification of the amino acid from R to H at position 482.
+The protein's natural variant, known as in MPS4B; mild form; fibroblasts from MPS4B compound heterozygotes for K-484 and A-500 have 1.9% of wild-type galactosidase activity;, features a modification of the amino acid from N to K at position 484.
+The protein's natural variant, known as in GM1G1;, features a modification of the amino acid from D to N at position 491.
+The protein's natural variant, known as in GM1G1, features a modification of the amino acid from D to Y at position 491.
+The protein's natural variant, known as in GM1G2; decrease in galactosidase activity;, features a modification of the amino acid from K to N at position 493.
+The protein's natural variant, known as in GM1G1;, features a modification of the amino acid from G to C at position 494.
+The protein's natural variant, known as in MPS4B; loss of galactosidase activity, features a modification of the amino acid from G to S at position 494.
+The protein's natural variant, known as in MPS4B; mild form; 2.1% of wild-type galactosidase activity;, features a modification of the amino acid from T to A at position 500.
+The protein's natural variant, known as in MPS4B; also in a patient with a slowly progressive form of GM1-gangliosidosis; loss of galactosidase activity;, features a modification of the amino acid from W to C at position 509.
+The protein's natural variant, known as in GM1G1; decrease in galactosidase activity, features a modification of the amino acid from L to P at position 514.
+The protein's natural variant, known as in GM1G1; mild phenotype; unknown pathological significance; reduction of galactosidase activity;, features a modification of the amino acid from R to C at position 521.
+The protein's natural variant, known as results in near-normal activity corresponding to 60%-100% of the wild-type depending on the expression system;, features a modification of the amino acid from S to G at position 532.
+The protein's natural variant, known as in GM1G1;, features a modification of the amino acid from P to L at position 549.
+The protein's natural variant, known as in GM1-gangliosidosis; unclassified clinical type, features a modification of the amino acid from G to E at position 554.
+The protein's natural variant, known as in GM1G1;, features a modification of the amino acid from K to R at position 578.
+The protein's natural variant, known as in GM1G1 and GM1G2; loss of galactosidase activity; severe mutation;, features a modification of the amino acid from G to D at position 579.
+The protein's natural variant, known as in GM1G1; loss of galactosidase activity;, features a modification of the amino acid from R to C at position 590.
+The protein's natural variant, known as in GM1G2;, features a modification of the amino acid from R to H at position 590.
+The protein's natural variant, known as in GM1G1; with cardiac involvement in some patients; loss of galactosidase activity; severe mutation; causes a rapid degradation of the protein precursor;, features a modification of the amino acid from Y to C at position 591.
+The protein's natural variant, known as in GM1G1; with cardiac involvement in some patients; loss of galactosidase activity; severe mutation; causes a rapid degradation of the protein precursor;, features a modification of the amino acid from Y to N at position 591.
+The protein's natural variant, known as reduction of galactosidase activity;, features a modification of the amino acid from R to W at position 595.
+The protein's natural variant, known as in GM1G2; decrease in galactosidase activity, features a modification of the amino acid from P to L at position 597.
+The protein's natural variant, known as in GM1G1; 2.1% of wild-type galactosidase activity, features a modification of the amino acid from P to S at position 597.
+The protein's natural variant, known as in GM1G2; decrease in galactosidase activity, features a modification of the amino acid from T to I at position 600.
+The protein's natural variant, known as in GM1G2, features a modification of the amino acid from E to G at position 632.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from L to R at position 137.
+The protein's natural variant, known as does not affect arachidonate 15-lipoxygenase activity. Does not affect protein affinity for (9Z,12Z)-octadecadienoate.;, features a modification of the amino acid from R to Q at position 205.
+The protein's natural variant, known as 36% of arachidonate 15-lipoxygenase activity, features a modification of the amino acid from R to W at position 402.
+The protein's natural variant, known as loss of arachidonate 15-lipoxygenase activity, features a modification of the amino acid from G to E at position 422.
+The protein's natural variant, known as 46% of arachidonate 15-lipoxygenase activity. Does not affect protein affinity for (9Z,12Z)-octadecadienoate, features a modification of the amino acid from G to R at position 422.
+The protein's natural variant, known as loss of catalytic activity; Loss of arachidonate 15-lipoxygenase activity.;, features a modification of the amino acid from T to M at position 560.
+The protein's natural variant, known as does not affect arachidonate 15-lipoxygenase activity. Does not affect protein affinity for (9Z,12Z)-octadecadienoate, features a modification of the amino acid from P to S at position 617.
+The protein's natural variant, known as in MCOPCTI; loss of DNA binding capacity;, features a modification of the amino acid from R to P at position 200.
+The protein's natural variant, known as in MCOPCTI; loss of DNA binding capacity at consensus sequences; abnormal and prolonged expression of MITF and WLS; mislocalization of CTNNB1;, features a modification of the amino acid from R to Q at position 200.
+The protein's natural variant, known as in MCOP2, features a modification of the amino acid from G to A at position 223.
+The protein's natural variant, known as in MCOPCB3; the patient also has cataracts;, features a modification of the amino acid from G to R at position 223.
+The protein's natural variant, known as in MCOP2;, features a modification of the amino acid from R to W at position 227.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from N to I at position 1337.
+The natural variant of this protein is characterized by an amino acid alteration from Y to S at position 221.
+The natural variant of this protein is characterized by an amino acid alteration from R to S at position 281.
+The protein's natural variant, known as in DKCX;, features a modification of the amino acid from A to V at position 2.
+The protein's natural variant, known as in DKCX;, features a modification of the amino acid from F to V at position 36.
+The protein's natural variant, known as in HHS;, features a modification of the amino acid from I to T at position 38.
+The protein's natural variant, known as in DKCX;, features a modification of the amino acid from K to E at position 39.
+The protein's natural variant, known as in DKCX;, features a modification of the amino acid from P to R at position 40.
+The protein's natural variant, known as in DKCX;, features a modification of the amino acid from E to K at position 41.
+The protein's natural variant, known as in HHS; increases interaction with SHQ1;, features a modification of the amino acid from T to M at position 49.
+The protein's natural variant, known as in DKCX; results in mislocalization of the telomerase complex without affecting telomerase activity, features a modification of the amino acid from L to V at position 54.
+The protein's natural variant, known as in DKCX; due to a 2 nucleotide inversion;, features a modification of the amino acid from L to S at position 56.
+The protein's natural variant, known as in DKCX;, features a modification of the amino acid from R to T at position 65.
+The protein's natural variant, known as in DKCX; decreases interaction with SHQ1;, features a modification of the amino acid from T to A at position 66.
+The protein's natural variant, known as in DKCX;, features a modification of the amino acid from L to F at position 72.
+The protein's natural variant, known as in DKCX; requires 2 nucleotide substitutions;, features a modification of the amino acid from L to Y at position 72.
+The protein's natural variant, known as in HHS; no effect on interaction with SHQ1;, features a modification of the amino acid from S to G at position 121.
+The protein's natural variant, known as in DKCX;, features a modification of the amino acid from L to F at position 317.
+The protein's natural variant, known as in DKCX;, features a modification of the amino acid from L to V at position 321.
+The protein's natural variant, known as in DKCX;, features a modification of the amino acid from R to Q at position 322.
+The protein's natural variant, known as in DKCX; increases interaction with SHQ1;, features a modification of the amino acid from M to I at position 350.
+The protein's natural variant, known as in DKCX; decreases interaction with SHQ1;, features a modification of the amino acid from M to T at position 350.
+The protein's natural variant, known as in DKCX and HHS; increases interaction with SHQ1;, features a modification of the amino acid from A to V at position 353.
+The protein's natural variant, known as in DKCX;, features a modification of the amino acid from G to E at position 402.
+The protein's natural variant, known as in DKCX;, features a modification of the amino acid from G to R at position 402.
+The protein's natural variant, known as in DKCX;, features a modification of the amino acid from P to L at position 409.
+The protein's natural variant, known as in a pancreatic ductal adenocarcinoma sample; somatic mutation, features a modification of the amino acid from Q to K at position 244.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from L to V at position 140.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from R to W at position 188.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from E to Q at position 488.
+The natural variant of this protein is characterized by an amino acid alteration from T to A at position 98.
+The protein's natural variant, known as in strain: NZF4; confers resistance to the herbicide norflurazon, features a modification of the amino acid from V to G at position 403.
+The natural variant of this protein is characterized by an amino acid alteration from G to D at position 379.
+The protein's natural variant, known as in DFNB100; Impaired diphosphoinositol-pentakisphosphate kinase activity;, features a modification of the amino acid from R to H at position 837.
+The protein's natural variant, known as in LW(B);, features a modification of the amino acid from Q to R at position 100.
+The protein's natural variant, known as in strain: FA, features a modification of the amino acid from S to G at position 243.
+The protein's natural variant, known as in FRFB;, features a modification of the amino acid from G to C at position 45.
+The protein's natural variant, known as in FRFB;, features a modification of the amino acid from G to S at position 49.
+The protein's natural variant, known as in NDAGSCW;, features a modification of the amino acid from V to M at position 22.
+The protein's natural variant, known as in NDAGSCW;, features a modification of the amino acid from A to T at position 68.
+The protein's natural variant, known as in MRD1; unknown pathological significance;, features a modification of the amino acid from T to I at position 144.
+The protein's natural variant, known as in MRD1; unknown pathological significance;, features a modification of the amino acid from R to H at position 461.
+The protein's natural variant, known as in MRD1; unknown pathological significance;, features a modification of the amino acid from D to E at position 654.
+The protein's natural variant, known as in MRD1; unknown pathological significance;, features a modification of the amino acid from A to T at position 655.
+The protein's natural variant, known as in MRD1; unknown pathological significance;, features a modification of the amino acid from A to T at position 857.
+The protein's natural variant, known as in MRD1; unknown pathological significance;, features a modification of the amino acid from T to I at position 1048.
+The protein's natural variant, known as in DBA21; unknown pathological significance, features a modification of the amino acid from C to R at position 134.
+The protein's natural variant, known as in DBA21; unknown pathological significance, features a modification of the amino acid from P to L at position 240.
+The protein's natural variant, known as in DBA21; severe decrease of protein levels in patient cells; results in impaired biogenesis of 60S ribosomal subunits, features a modification of the amino acid from C to Y at position 446.
+The protein's natural variant, known as in DBA21; severe decrease of protein levels in patient cells; bone marrow patient cells show abnormal acceleration of erythrocyte maturation suggesting impaired function; affects function in RPL5 nuclear import as shown in patient cells, features a modification of the amino acid from G to E at position 584.
+The protein's natural variant, known as in SRXY3; without adrenal failure;, features a modification of the amino acid from V to M at position 15.
+The protein's natural variant, known as in SRXY3; without adrenal failure; markedly impaired transcriptional activity;, features a modification of the amino acid from C to S at position 33.
+The protein's natural variant, known as in SRXY3; with adrenal failure;, features a modification of the amino acid from G to E at position 35.
+The protein's natural variant, known as in SRXY3; loss of DNA-binding; significantly decreased transactivator activity, features a modification of the amino acid from T to P at position 40.
+The protein's natural variant, known as in SRXY3; without adrenal failure, features a modification of the amino acid from C to Y at position 65.
+The protein's natural variant, known as in SRXY3; without adrenal failure;, features a modification of the amino acid from M to I at position 78.
+The protein's natural variant, known as in SRXY3; without adrenal failure; markedly impaired transcriptional activity;, features a modification of the amino acid from R to H at position 84.
+The protein's natural variant, known as in SRXY3; without adrenal failure;, features a modification of the amino acid from G to S at position 91.
+The protein's natural variant, known as in SRXY3, SRXX4 and AINR; decreased transactivator activity; no effect on nuclear location;, features a modification of the amino acid from R to Q at position 92.
+The protein's natural variant, known as in SRXY3 and SRXX4; decreased transactivator activity; loss of DNA binding, at least to some known consensus target sequences; no effect on nuclear location;, features a modification of the amino acid from R to W at position 92.
+The protein's natural variant, known as in SPGF8 and POF7; activity levels similar to wild-type;, features a modification of the amino acid from G to A at position 123.
+The protein's natural variant, known as in SPGF8 and POF7; loss of activity;, features a modification of the amino acid from P to L at position 129.
+The protein's natural variant, known as in SPGF8; impairs transactivational activity;, features a modification of the amino acid from P to L at position 131.
+The protein's natural variant, known as in SPGF8; impairs transactivational activity;, features a modification of the amino acid from R to C at position 191.
+The protein's natural variant, known as in SPGF8; impairs transactivational activity;, features a modification of the amino acid from G to S at position 212.
+The protein's natural variant, known as in SPGF8; impairs transactivational activity;, features a modification of the amino acid from D to N at position 238.
+The protein's natural variant, known as in AINR;, features a modification of the amino acid from R to L at position 255.
+The protein's natural variant, known as in POF7; without adrenal failure; partial loss of activity;, features a modification of the amino acid from D to N at position 293.
+The protein's natural variant, known as in SRXY3; without adrenal failure;, features a modification of the amino acid from L to Q at position 437.
+The protein's natural variant, known as found in a renal cell carcinoma case; somatic mutation, features a modification of the amino acid from P to R at position 203.
+The protein's natural variant, known as found in a patient with features of Robinow syndrome; unknown pathological significance;, features a modification of the amino acid from P to L at position 142.
+The protein's natural variant, known as probable disease-associated variant found in a patient with features of Robinow syndrome;, features a modification of the amino acid from G to S at position 434.
+The protein's natural variant, known as in OMOD2; also found in a patient with features of Robinow syndrome;, features a modification of the amino acid from G to V at position 434.
+The protein's natural variant, known as in SBCADD; loss of protein expression; loss of 2-methylbutyryl-CoA dehydrogenase activity;, features a modification of the amino acid from L to F at position 255.
+The protein's natural variant, known as in Amy-P, features a modification of the amino acid from L to I at position 7.
+The protein's natural variant, known as in Amy-P, features a modification of the amino acid from T to A at position 398.
+The protein's natural variant, known as in allele A, features a modification of the amino acid from I to V at position 7.
+The protein's natural variant, known as in strain: Xanthi; allele 1, features a modification of the amino acid from E to G at position 8.
+The protein's natural variant, known as in strain: T024242; alleles A, eIF4E2b and eIFiso4E-T, features a modification of the amino acid from PPASATETVA to LPAPDTVE at position 22.
+The protein's natural variant, known as in strain: T024242; alleles A, eIF4E2b and eIFiso4E-T, features a modification of the amino acid from AWGSS to VWASA at position 51.
+The protein's natural variant, known as in strain: T024242; alleles A, eIF4E2b and eIFiso4E-T, features a modification of the amino acid from S to N at position 101.
+The protein's natural variant, known as in strain: Xanthi; allele 1, features a modification of the amino acid from V to I at position 107.
+The protein's natural variant, known as in strain: S10809, features a modification of the amino acid from DKLSLWTKTASNEAIQMSIGRKWKEIIDAE to RRYVEWLPVYVGVRINFPYGLRLPPMKQFR at position 178.
+The protein's natural variant, known as in strain: T024242; alleles eIF4E2b and eIFiso4E-T, features a modification of the amino acid from K to R at position 156.
+The protein's natural variant, known as in strain: T024242; alleles eIF4E2b and eIFiso4E-T, features a modification of the amino acid from I to A at position 163.
+The protein's natural variant, known as in eIFiso4E-S, features a modification of the amino acid from M to V at position 165.
+The protein's natural variant, known as in strain: T024242; allele eIFiso4E-T, features a modification of the amino acid from RERSA to KERSV at position 194.
+The protein's natural variant, known as in allele eIF4E2b, features a modification of the amino acid from R to K at position 190.
+The natural variant of this protein is characterized by an amino acid alteration from G to D at position 55.
+The protein's natural variant, known as in strain: SB146, features a modification of the amino acid from V to I at position 79.
+The protein's natural variant, known as no effect on PKD1 and PKD2 localization to the cell surface;, features a modification of the amino acid from Q to R at position 95.
+The protein's natural variant, known as likely benign variant; no effect on PKD1 and PKD2 localization to the cell surface, features a modification of the amino acid from T to A at position 232.
+The protein's natural variant, known as likely benign variant; no effect on PKD1 and PKD2 localization to the cell surface;, features a modification of the amino acid from R to C at position 309.
+The protein's natural variant, known as in PKD3; fails to promote PKD1 and PKD2 localization to the cell surface;, features a modification of the amino acid from T to R at position 383.
+The protein's natural variant, known as in PKD3; fails to promote PKD1 and PKD2 localization to the cell surface;, features a modification of the amino acid from R to L at position 400.
+The protein's natural variant, known as found in a patient with polycystic liver disease; unknown pathological significance;, features a modification of the amino acid from R to P at position 590.
+The protein's natural variant, known as found in a patient affected by polycystic liver disease; unknown pathological significance; the patient carried additional PKHD1 variant; the mutation results in significantly reduced alpha-glucosidase activity; dbNP:rs753910059;, features a modification of the amino acid from H to N at position 785.
+The protein's natural variant, known as in PKD3; fails to promote PKD1 and PKD2 localization to the cell surface;, features a modification of the amino acid from R to W at position 817.
+The protein's natural variant, known as in DFNB23;, features a modification of the amino acid from R to G at position 134.
+The protein's natural variant, known as in USH1F;, features a modification of the amino acid from R to Q at position 134.
+The protein's natural variant, known as in USH1DF, features a modification of the amino acid from D to G at position 178.
+The protein's natural variant, known as in DFNB23;, features a modification of the amino acid from G to D at position 262.
+The protein's natural variant, known as in USH1F; benign variant;, features a modification of the amino acid from Q to K at position 1342.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from K to Q at position 100.
+The protein's natural variant, known as in LSIII-5, features a modification of the amino acid from I to K at position 40.
+The protein's natural variant, known as in a colon cancer sample;, features a modification of the amino acid from D to Y at position 418.
+The protein's natural variant, known as in a non-Hodgkin lymphoma sample;, features a modification of the amino acid from N to S at position 593.
+The protein's natural variant, known as may be associated with a reduced risk for gout; variant carriers have lower serum urate levels and increased renal urate excretion; results in strongly reduced urate transport; no change in SLC22A13/OAT10 protein levels; no change in cellular localization;, features a modification of the amino acid from R to C at position 377.
+The protein's natural variant, known as in strain: Isolate California-168, Isolate California-169, Isolate California-170, Isolate California-171, Isolate California-175, Isolate California-176, Isolate Idaho-1, Isolate Idaho-2, Isolate Idaho-7, Isolate Idaho-8, Isolate Idaho-10, Isolate Idaho-11, Isolate Idaho-12, Isolate Washington-899 and Isolate Washington-SOA, features a modification of the amino acid from T to A at position 32.
+The protein's natural variant, known as in strain: Isolate California-168, Isolate California-169, Isolate California-170, Isolate California-171, Isolate California-175, Isolate California-176, Isolate Idaho-1, Isolate Idaho-2, Isolate Idaho-7, Isolate Idaho-8, Isolate Idaho-10, Isolate Idaho-11, Isolate Idaho-12, Isolate Washington-899 and Isolate Washington-SOA, features a modification of the amino acid from N to D at position 40.
+The protein's natural variant, known as in strain: Isolate New Mexico-523, features a modification of the amino acid from I to F at position 70.
+The protein's natural variant, known as in strain: Isolate Washington-SOA, features a modification of the amino acid from V to L at position 97.
+The protein's natural variant, known as in strain: Isolate New Mexico-522, features a modification of the amino acid from V to F at position 100.
+The protein's natural variant, known as in strain: FVB, features a modification of the amino acid from L to P at position 12.
+The protein's natural variant, known as no effect on the cysteine S-conjugate N-acetyltransferase activity;, features a modification of the amino acid from E to K at position 104.
+The protein's natural variant, known as no effect on the cysteine S-conjugate N-acetyltransferase activity;, features a modification of the amino acid from F to S at position 143.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation, features a modification of the amino acid from A to V at position 933.
+The natural variant of this protein is characterized by an amino acid alteration from S to R at position 103.
+The protein's natural variant, known as in NNMS; unknown pathological significance, features a modification of the amino acid from L to P at position 257.
+The protein's natural variant, known as in NNMS; loss of palmitoyltransferase activity; unable to carry out SHH and DHH palmitoylation; does not affect HHAT protein levels, features a modification of the amino acid from G to V at position 287.
+The protein's natural variant, known as in a melanoma cell line; abolishes GTP-binding;, features a modification of the amino acid from G to E at position 448.
+The protein's natural variant, known as in a lung cancer cell line;, features a modification of the amino acid from N to S at position 450.
+The protein's natural variant, known as in lung adenocarcinoma, features a modification of the amino acid from G to E at position 47.
+The protein's natural variant, known as in lung adenocarcinoma;, features a modification of the amino acid from A to V at position 50.
+The natural variant of this protein is characterized by an amino acid alteration from A to S at position 70.
+The protein's natural variant, known as in strain: D, features a modification of the amino acid from A to P at position 196.
+The protein's natural variant, known as in strain: Serotype A2 / PH196, features a modification of the amino acid from KDA to QDS at position 106.
+The protein's natural variant, known as in strain: Serotype A2 / PH196, features a modification of the amino acid from K to Q at position 466.
+The protein's natural variant, known as in strain: Serotype A2 / PH196, features a modification of the amino acid from S to A at position 470.
+The protein's natural variant, known as in strain: Serotype A2 /PH196, features a modification of the amino acid from RQ to KK at position 495.
+The protein's natural variant, known as in strain: Serotype A2 / PH196, features a modification of the amino acid from D to E at position 568.
+The protein's natural variant, known as in strain: Serotype A2 / PH196, features a modification of the amino acid from P to S at position 572.
+The protein's natural variant, known as in strain: NZO, features a modification of the amino acid from V to I at position 541.
+The protein's natural variant, known as in strain: KKObese, features a modification of the amino acid from D to N at position 600.
+The protein's natural variant, known as in strain: NZO, features a modification of the amino acid from V to I at position 651.
+The protein's natural variant, known as in strain: NZO, features a modification of the amino acid from T to I at position 1044.
+The protein's natural variant, known as in 4764 Da polypeptide, features a modification of the amino acid from D to DD at position 179.
+The protein's natural variant, known as in strain: D273-10B, features a modification of the amino acid from D to G at position 651.
+The protein's natural variant, known as in CVID11; interferes with binding to IL21R, features a modification of the amino acid from L to P at position 56.
+The protein's natural variant, known as in strain: cv. Cha-0, features a modification of the amino acid from I to V at position 202.
+The protein's natural variant, known as in strain: cv. Gr-5, cv. Gran-2, cv. Gran-3, cv. Gran-5, cv. Gran-7, cv. Gran-8, cv. Gran-10, cv. Ita-0, cv. Ler, cv. Mh-0, cv. Per-1, cv. Rv-1, cv. Rv-3, cv. Rv-4, cv. Rv-5, cv. Rv-8, cv. Wlp-1, cv. Wlp-2, cv. Wlp-3, cv. Wlp-4, cv. Wlp-5, cv. Wlp-6, cv. Wlp-7, cv. Wlp-8, cv. Wlp-9 and cv. Wlp-10, features a modification of the amino acid from V to L at position 238.
+The protein's natural variant, known as in strain: cv. Rv-2, cv. Rv-9, cv. Rv-10, cv. Tv-1, cv. Tv-2, cv. TV-6, cv. Tv-7, cv. Tv-8, cv. Tv-9 and cv. Tv-10, features a modification of the amino acid from N to NRE at position 246.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from G to R at position 31.
+The protein's natural variant, known as found in a renal cell carcinoma sample; somatic mutation;, features a modification of the amino acid from F to L at position 114.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from C to F at position 553.
+The natural variant of this protein is characterized by an amino acid alteration from L to F at position 31.
+The protein's natural variant, known as in DEDSM; unknown pathological significance;, features a modification of the amino acid from R to H at position 37.
+The protein's natural variant, known as in RP59; 5-fold reduction in catalytic activity and reduced affinity for FPP but not for IPP.;, features a modification of the amino acid from K to E at position 42.
+The protein's natural variant, known as found in a patient with progressive myoclonus epilepsy; unknown pathological significance, features a modification of the amino acid from D to N at position 95.
+The protein's natural variant, known as found in a patient with progressive myoclonus epilepsy; unknown pathological significance;, features a modification of the amino acid from R to Q at position 205.
+The protein's natural variant, known as in DEDSM; also found in a patient with progressive myoclonus epilepsy and developmental delay; unknown pathological significance;, features a modification of the amino acid from R to Q at position 211.
+The natural variant of this protein is characterized by an amino acid alteration from A to AAAA at position 6.
+The natural variant of this protein is characterized by an amino acid alteration from Y to N at position 736.
+The natural variant of this protein is characterized by an amino acid alteration from L to V at position 756.
+The protein's natural variant, known as in CDG1U;, features a modification of the amino acid from Y to C at position 23.
+The protein's natural variant, known as probable disease-associated variant found in patients with phosphoribosyl pyrophosphate synthetase I deficiency;, features a modification of the amino acid from S to P at position 16.
+The protein's natural variant, known as in CMTX5;, features a modification of the amino acid from E to D at position 43.
+The protein's natural variant, known as in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP;, features a modification of the amino acid from D to H at position 52.
+The protein's natural variant, known as in DFNX1;, features a modification of the amino acid from D to N at position 65.
+The protein's natural variant, known as in DFNX1;, features a modification of the amino acid from A to T at position 87.
+The protein's natural variant, known as in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP;, features a modification of the amino acid from N to S at position 114.
+The protein's natural variant, known as in CMTX5;, features a modification of the amino acid from M to T at position 115.
+The protein's natural variant, known as in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP;, features a modification of the amino acid from L to I at position 129.
+The protein's natural variant, known as in ARTS;, features a modification of the amino acid from Q to P at position 133.
+The protein's natural variant, known as probable disease-associated variant found in a patient with an intermediate phenotype between ARTS and PRPS1 superactivity; normal PRPP synthetase activity in fibroblasts; loss of activity in erythrocytes;, features a modification of the amino acid from V to L at position 142.
+The protein's natural variant, known as in ARTS;, features a modification of the amino acid from L to P at position 152.
+The protein's natural variant, known as in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP;, features a modification of the amino acid from D to H at position 183.
+The protein's natural variant, known as in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP;, features a modification of the amino acid from A to V at position 190.
+The protein's natural variant, known as in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP;, features a modification of the amino acid from H to Q at position 193.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from D to H at position 203.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from V to G at position 219.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from H to D at position 231.
+The protein's natural variant, known as in DFNX1;, features a modification of the amino acid from I to T at position 290.
+The protein's natural variant, known as in DFNX1;, features a modification of the amino acid from G to R at position 306.
+The protein's natural variant, known as in 50% of the molecules, features a modification of the amino acid from S to A at position 95.
+The protein's natural variant, known as in very small amount, features a modification of the amino acid from Y to A at position 97.
+The protein's natural variant, known as in very small amount, features a modification of the amino acid from CK to GP at position 129.
+The natural variant of this protein is characterized by an amino acid alteration from V to A at position 866.
+The natural variant of this protein is characterized by an amino acid alteration from K to R at position 898.
+The natural variant of this protein is characterized by an amino acid alteration from S to G at position 926.
+The protein's natural variant, known as in strain: Isolate S104, features a modification of the amino acid from M to V at position 60.
+The protein's natural variant, known as in strain: C3H/He, features a modification of the amino acid from P to L at position 30.
+The protein's natural variant, known as in strain: C3H/He, features a modification of the amino acid from Q to H at position 281.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from S to T at position 140.
+The natural variant of this protein is characterized by an amino acid alteration from K to R at position 230.
+The protein's natural variant, known as in strain: IL1403, features a modification of the amino acid from G to S at position 25.
+The protein's natural variant, known as in strain: IL1403, features a modification of the amino acid from P to S at position 32.
+The protein's natural variant, known as in strain: IL1403, features a modification of the amino acid from V to F at position 79.
+The protein's natural variant, known as in strain: IL1403, features a modification of the amino acid from F to L at position 120.
+The protein's natural variant, known as in strain: IL1403, features a modification of the amino acid from F to V at position 226.
+The natural variant of this protein is characterized by an amino acid alteration from P to S at position 170.
+The natural variant of this protein is characterized by an amino acid alteration from A to T at position 630.
+The natural variant of this protein is characterized by an amino acid alteration from I to T at position 134.
+The protein's natural variant, known as in MFM1;, features a modification of the amino acid from S to I at position 2.
+The protein's natural variant, known as in MFM1;, features a modification of the amino acid from S to F at position 7.
+The protein's natural variant, known as in MFM1; some patients manifest a severe cardiac phenotype with right ventricular predominance;, features a modification of the amino acid from S to F at position 13.
+The protein's natural variant, known as in MFM1;, features a modification of the amino acid from R to C at position 16.
+The protein's natural variant, known as in MFM1; exhibits significantly delayed filament assembly kinetics when bound to NEB; enhanced binding affinity towards NEB;, features a modification of the amino acid from S to F at position 46.
+The protein's natural variant, known as in MFM1;, features a modification of the amino acid from S to Y at position 46.
+The protein's natural variant, known as in MFM1; the clinical picture is dominated by arrhythmogenic right ventricular cardiomyopathy and terminal heart failure; results in impaired filaments formation;, features a modification of the amino acid from N to S at position 116.
+The protein's natural variant, known as in CMD1I; results in impaired filaments formation, does not localize at intercalated disks;, features a modification of the amino acid from A to D at position 120.
+The protein's natural variant, known as in CMD1I; results in impaired filaments formation, does not localize at intercalated disks;, features a modification of the amino acid from L to P at position 136.
+The protein's natural variant, known as may play a role in cardiomyopathies and distal myopathies if combined with other DES mutations or mutations in other genes; does not affect the formation of a normal complete filamentous network;, features a modification of the amino acid from A to V at position 213.
+The protein's natural variant, known as found in a patient with severe arrhythmogenic right ventricular cardiomyopathy also carrying a pathogenic frameshift mutation in PKP2;, features a modification of the amino acid from K to E at position 241.
+The protein's natural variant, known as in MFM1; exhibits significantly delayed filament assembly kinetics when bound to NEB and NEBL; enhanced binding affinity towards NEB and NEBL;, features a modification of the amino acid from E to D at position 245.
+The protein's natural variant, known as in CMD1I; unknown pathological significance; does not affect filaments formation, features a modification of the amino acid from H to R at position 326.
+The protein's natural variant, known as in MFM1; mild adult-onset; unable to form a functional filamentous network;, features a modification of the amino acid from A to P at position 337.
+The protein's natural variant, known as in MFM1; results in the formation of a filamentous network disrupted by multiple breaks and clumps or large aggregates;, features a modification of the amino acid from L to R at position 338.
+The protein's natural variant, known as in MFM1; unable to form a filamentous network; abolishes binding to MTM1;, features a modification of the amino acid from N to D at position 342.
+The protein's natural variant, known as in MFM1; distal onset; incapable of forming filamentous networks;, features a modification of the amino acid from L to P at position 345.
+The protein's natural variant, known as in Kaeser syndrome and MFM1; incapable of de novo formation of a desmin intermediate filaments network; exerts a dominant negative effect on the ordered lateral arrangement of desmin subunits; may produce structural changes; forms subsarcolemmal aggregates;, features a modification of the amino acid from R to P at position 350.
+The protein's natural variant, known as in MFM1;, features a modification of the amino acid from R to P at position 355.
+The protein's natural variant, known as in MFM1; unable to polymerize and form an intracellular filamentous network; abolishes binding to MTM1;, features a modification of the amino acid from A to P at position 357.
+The protein's natural variant, known as in MFM1; heterozygous with I-393 gives a severe childhood-onset; unable to form a functional filamentous network in the presence of I-393; abolishes binding to MTM1;, features a modification of the amino acid from A to P at position 360.
+The protein's natural variant, known as in MFM1; unable to polymerize and form an intracellular filamentous network; does not affect binding to MTM1;, features a modification of the amino acid from L to P at position 370.
+The protein's natural variant, known as in MFM1;, features a modification of the amino acid from L to P at position 385.
+The protein's natural variant, known as in MFM1;, features a modification of the amino acid from Q to P at position 389.
+The protein's natural variant, known as in MFM1; heterozygous with P-360 gives a severe childhood-onset; filamentous network is not affected however several spots indicate focal disorganization;, features a modification of the amino acid from N to I at position 393.
+The protein's natural variant, known as in CMD1I; unknown pathological significance; impaired subcellular localization;, features a modification of the amino acid from L to P at position 398.
+The protein's natural variant, known as in MFM1; results in the formation of a filamentous network disrupted by multiple breaks and clumps or large aggregates;, features a modification of the amino acid from D to Y at position 399.
+The protein's natural variant, known as in MFM1; results in the formation of a filamentous network disrupted by multiple breaks and clumps or large aggregates;, features a modification of the amino acid from E to K at position 401.
+The protein's natural variant, known as in MFM1; unable to form a filamentous network;, features a modification of the amino acid from R to W at position 406.
+The protein's natural variant, known as in MFM1; found in a family with myofibrillar myopathy and arrhythmogenic right ventricular cardiomyopathy;, features a modification of the amino acid from P to S at position 419.
+The protein's natural variant, known as in MFM1; reveals a severe disturbance of filament-formation competence and filament-filament interactions;, features a modification of the amino acid from T to I at position 442.
+The protein's natural variant, known as in MFM1, features a modification of the amino acid from K to M at position 449.
+The protein's natural variant, known as in MFM1;, features a modification of the amino acid from K to T at position 449.
+The protein's natural variant, known as in CMD1I and MFM1; reveals a severe disturbance of filament-formation competence and filament-filament interactions; reduced interaction with CRYAB;, features a modification of the amino acid from I to M at position 451.
+The protein's natural variant, known as in MFM1; exhibits significantly delayed filament assembly kinetics when bound to NEB and NEBL; enhanced binding affinity towards NEB and NEBL;, features a modification of the amino acid from T to I at position 453.
+The protein's natural variant, known as in MFM1; reveals a severe disturbance of filament-formation competence and filament-filament interactions; increased interaction with CRYAB;, features a modification of the amino acid from R to W at position 454.
+The protein's natural variant, known as in MFM1; reveals a severe disturbance of filament-formation competence and filament-filament interactions;, features a modification of the amino acid from S to I at position 460.
+The protein's natural variant, known as in HPE5; 2-fold increase in luciferase activity;, features a modification of the amino acid from Q to P at position 36.
+The protein's natural variant, known as in HPE5, features a modification of the amino acid from D to N at position 37.
+The protein's natural variant, known as in HPE5, features a modification of the amino acid from D to N at position 128.
+The protein's natural variant, known as in HPE5; requires 2 nucleotide substitutions; 50% reduction of luciferase activity, features a modification of the amino acid from D to F at position 152.
+The natural variant of this protein is characterized by an amino acid alteration from H to HH at position 239.
+The protein's natural variant, known as in HPE5, features a modification of the amino acid from S to N at position 272.
+The protein's natural variant, known as in HPE5, features a modification of the amino acid from H to L at position 286.
+The protein's natural variant, known as in HPE5;, features a modification of the amino acid from H to Q at position 286.
+The protein's natural variant, known as in HPE5, features a modification of the amino acid from H to Y at position 286.
+The protein's natural variant, known as in HPE5, features a modification of the amino acid from H to Y at position 291.
+The protein's natural variant, known as in HPE5, features a modification of the amino acid from W to R at position 304.
+The protein's natural variant, known as in HPE5, features a modification of the amino acid from F to C at position 314.
+The protein's natural variant, known as in HPE5, features a modification of the amino acid from R to L at position 325.
+The protein's natural variant, known as in HPE5, features a modification of the amino acid from R to S at position 325.
+The protein's natural variant, known as in HPE5, features a modification of the amino acid from H to Y at position 327.
+The protein's natural variant, known as in HPE5, features a modification of the amino acid from C to F at position 335.
+The protein's natural variant, known as in HPE5, features a modification of the amino acid from R to P at position 373.
+The protein's natural variant, known as in HPE5, features a modification of the amino acid from Y to N at position 402.
+The protein's natural variant, known as in HPE5, features a modification of the amino acid from T to K at position 403.
+The protein's natural variant, known as in HPE5, features a modification of the amino acid from H to R at position 404.
+The protein's natural variant, known as in HPE5;, features a modification of the amino acid from R to W at position 409.
+The protein's natural variant, known as in HPE5;, features a modification of the amino acid from H to Q at position 415.
+The protein's natural variant, known as in HPE5; near-complete loss of luciferase activity, features a modification of the amino acid from A to AAAAAAAAAAA at position 470.
+The protein's natural variant, known as in strain: INSMA3008, features a modification of the amino acid from A to V at position 21.
+The protein's natural variant, known as in strain: CCUG 24846, features a modification of the amino acid from V to I at position 61.
+The protein's natural variant, known as in strain: CCUG 24846, features a modification of the amino acid from E to Q at position 136.
+The protein's natural variant, known as in strain: CCUG 24846 and INSMA3008, features a modification of the amino acid from A to T at position 146.
+The protein's natural variant, known as in strain: CCUG 24846 and INSMA3008, features a modification of the amino acid from A to V at position 151.
+The protein's natural variant, known as in strain: CCUG 24846 and INSMA3008, features a modification of the amino acid from GVG to NVD at position 173.
+The protein's natural variant, known as in strain: CH9802, features a modification of the amino acid from K to R at position 175.
+The protein's natural variant, known as in strain: CH9802, features a modification of the amino acid from G to A at position 201.
+The protein's natural variant, known as results in attenuation of insulin secretion; increased protein stability, features a modification of the amino acid from S to L at position 937.
+The protein's natural variant, known as in strain: 08FG, features a modification of the amino acid from L to V at position 12.
+The protein's natural variant, known as in RIEG3; decreased location at the nucleus; decreased transcription regulatory region DNA binding; decreased sequence-specific DNA binding transcription factor activity; no change on DNA bending activity, features a modification of the amino acid from P to L at position 79.
+The protein's natural variant, known as in RIEG3, features a modification of the amino acid from P to R at position 79.
+The protein's natural variant, known as in RIEG3; decreased location at the nucleus; decreased transcription regulatory region DNA binding; decreased sequence-specific DNA binding transcription factor activity; no change on DNA bending activity, features a modification of the amino acid from P to T at position 79.
+The protein's natural variant, known as in RIEG3; decreased location at the nucleus; decreased transcription regulatory region DNA binding; decreased sequence-specific DNA binding transcription factor activity;, features a modification of the amino acid from S to T at position 82.
+The protein's natural variant, known as in RIEG3; unknown pathological significance, features a modification of the amino acid from A to P at position 85.
+The protein's natural variant, known as in RIEG3; no change in location at the nucleus; decreased transcription regulatory region DNA binding; decreased sequence-specific DNA binding transcription factor activity;, features a modification of the amino acid from L to F at position 86.
+The protein's natural variant, known as in RIEG3; loss of protein stability;, features a modification of the amino acid from I to M at position 87.
+The protein's natural variant, known as in RIEG3; decreased location at the nucleus; decreased transcription regulatory region DNA binding; decreased sequence-specific DNA binding transcription factor activity; no change on DNA bending activity, features a modification of the amino acid from I to S at position 91.
+The protein's natural variant, known as in RIEG3; decreased location at the nucleus; decreased transcription regulatory region DNA binding; decreased sequence-specific DNA binding transcription factor activity; no change on DNA bending activity, features a modification of the amino acid from I to T at position 91.
+The protein's natural variant, known as in ASGD3;, features a modification of the amino acid from M to V at position 109.
+The protein's natural variant, known as in ASGD3 and RIEG3; decreased location at the nucleus; decreased transcription regulatory region DNA binding; decreased sequence-specific DNA binding transcription factor activity;, features a modification of the amino acid from F to S at position 112.
+The protein's natural variant, known as in RIEG3, features a modification of the amino acid from Y to S at position 115.
+The protein's natural variant, known as in ASGD3 and RIEG3; with glaucoma; decreased location at the nucleus; decreased transcription regulatory region DNA binding; decreased sequence-specific DNA binding transcription factor activity;, features a modification of the amino acid from I to M at position 126.
+The protein's natural variant, known as in RIEG3; hypomorphic mutation; decreased protein abundance; decreased protein stability; changed post-translational phosphorylation; decreased location at the nucleus; novel location at the cytoplasm; decreased transcription regulatory region DNA binding; decreased sequence-specific DNA binding transcription factor activity;, features a modification of the amino acid from I to S at position 126.
+The protein's natural variant, known as in RIEG3; decreased location at the nucleus; decreased transcription regulatory region DNA binding; decreased sequence-specific DNA binding transcription factor activity;, features a modification of the amino acid from R to H at position 127.
+The protein's natural variant, known as in RIEG3;, features a modification of the amino acid from R to L at position 127.
+The protein's natural variant, known as in RIEG3; no effect on protein abundance; increased protein stability; decreased location at nucleus; loss of transcription regulatory region DNA binding; loss of sequence-specific DNA binding transcription factor activity, features a modification of the amino acid from H to R at position 128.
+The protein's natural variant, known as in RIEG3; no effect on protein abundance; changed post-translational phosphorylation; novel location at aggresome, aggregation correspond to microtubule-dependent inclusion bodies; decreased location at the nucleus; decreased transcription regulatory region DNA binding; decreased sequence-specific DNA binding transcription factor activity;, features a modification of the amino acid from L to F at position 130.
+The protein's natural variant, known as in RIEG3 and ASGD3; with glaucoma; decreased location at the nucleus; decreased transcription regulatory region DNA binding; decreased sequence-specific DNA binding transcription factor activity;, features a modification of the amino acid from S to L at position 131.
+The protein's natural variant, known as in ASGD3, features a modification of the amino acid from S to W at position 131.
+The protein's natural variant, known as in RIEG3; decreased protein abundance; decreased protein stability; decreased location at nucleus; loss of transcription regulatory region DNA binding; loss of sequence-specific DNA binding transcription factor activity, features a modification of the amino acid from C to Y at position 135.
+The protein's natural variant, known as in ASGD3, features a modification of the amino acid from K to E at position 138.
+The protein's natural variant, known as in RIEG3, features a modification of the amino acid from G to D at position 149.
+The protein's natural variant, known as in ASGD3; no change in protein abundance; changed post-translational phosphorylation; changed protein structure; decreased location at the nucleus; novel location at the cytoplasm; increased protein aggregation, aggregation do not correspond to microtubule-dependent inclusion bodies; loss of transcription regulatory region DNA binding; loss of sequence-specific DNA binding transcription factor activity, features a modification of the amino acid from W to G at position 152.
+The protein's natural variant, known as in RIEG3 and ASGD3; no change in location at the nucleus; decreased transcription regulatory region DNA binding; decreased sequence-specific DNA binding transcription factor activity, features a modification of the amino acid from M to K at position 161.
+The protein's natural variant, known as in RIEG3; no effect on protein abundance; no effect on protein stability; no effect on location at nucleus; no effect on transcription regulatory region DNA binding; decreased sequence-specific DNA binding transcription factor activity, features a modification of the amino acid from M to V at position 161.
+The protein's natural variant, known as in RIEG3; no change in location at the nucleus; no effect on transcription regulatory region DNA binding; decreased sequence-specific DNA binding transcription factor activity, features a modification of the amino acid from G to R at position 165.
+The protein's natural variant, known as in RIEG3; no change in location at the nucleus; decreased transcription regulatory region DNA binding; decreased sequence-specific DNA binding transcription factor activity, features a modification of the amino acid from R to P at position 169.
+The protein's natural variant, known as in RIEG3; unknown pathological significance;, features a modification of the amino acid from R to W at position 170.
+The protein's natural variant, known as in ASGD3; no effect on protein abundance; increased protein stability; no effect on nuclear location; no effect on transcription regulatory region DNA binding; decreased sequence-specific DNA binding transcription factor activity;, features a modification of the amino acid from P to S at position 297.
+The protein's natural variant, known as no effect on protein abundance; no effect on protein stability; no effect on nuclear location; no effect on transcription regulatory region DNA binding; no effect on sequence-specific DNA binding transcription factor activity, features a modification of the amino acid from T to N at position 368.
+The protein's natural variant, known as in strain: SJL/J, features a modification of the amino acid from A to D at position 120.
+The protein's natural variant, known as in IFN-tau2B and IFN-tau2C, features a modification of the amino acid from D to N at position 6.
+The protein's natural variant, known as in IFN-tau2C, features a modification of the amino acid from E to V at position 135.
+The protein's natural variant, known as in IFN-tau2C, features a modification of the amino acid from M to V at position 146.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from L to I at position 623.
+The natural variant of this protein is characterized by an amino acid alteration from L to N at position 42.
+The natural variant of this protein is characterized by an amino acid alteration from N to D at position 59.
+The natural variant of this protein is characterized by an amino acid alteration from T to V at position 60.
+The natural variant of this protein is characterized by an amino acid alteration from K to R at position 303.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from G to D at position 153.
+The protein's natural variant, known as in strain: S3446 and 020, features a modification of the amino acid from L to F at position 5.
+The protein's natural variant, known as in strain: HF4, HF8, HF16, HF85, HF110, HF116 and HF175, features a modification of the amino acid from E to K at position 55.
+The protein's natural variant, known as in strain: HF130, features a modification of the amino acid from P to S at position 139.
+The protein's natural variant, known as in strain: HF4, HF8, HF16, HF79, HF85, HF110, HF113, HF116, HF147, HF175 and HF200, features a modification of the amino acid from P to A at position 201.
+The protein's natural variant, known as in strain: HF4, HF8, HF16, HF79, HF85, HF110, HF113, HF116, HF147, HF175 and HF200, features a modification of the amino acid from GA to KG at position 212.
+The protein's natural variant, known as in subsp. Manitobensis, features a modification of the amino acid from T to I at position 47.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from E to G at position 276.
+The natural variant of this protein is characterized by an amino acid alteration from A to S at position 529.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation, features a modification of the amino acid from R to Q at position 578.
+The natural variant of this protein is characterized by an amino acid alteration from S to L at position 37.
+The protein's natural variant, known as in HCC, features a modification of the amino acid from L to R at position 106.
+The protein's natural variant, known as in HCC;, features a modification of the amino acid from P to L at position 345.
+The protein's natural variant, known as in HCC;, features a modification of the amino acid from G to S at position 425.
+The protein's natural variant, known as in HCC; also found in hepatoblastoma;, features a modification of the amino acid from G to S at position 650.
+The protein's natural variant, known as in hepatoblastoma;, features a modification of the amino acid from R to Q at position 841.
+The protein's natural variant, known as in strain: cv. Granny Smith, features a modification of the amino acid from RIMSMM to SQ at position 459.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from D to E at position 15.
+The protein's natural variant, known as probable disease-associated variant found in a family with Brunner syndrome-like behavioral disturbances; reduced activity;, features a modification of the amino acid from C to F at position 266.
+The protein's natural variant, known as in a cancer; unknown pathological significance, features a modification of the amino acid from G to S at position 2.
+The protein's natural variant, known as in a cancer; unknown pathological significance, features a modification of the amino acid from S to F at position 239.
+The protein's natural variant, known as in PCH11; unknown pathological significance, features a modification of the amino acid from R to Q at position 518.
+The protein's natural variant, known as in SWILS; delayed anterograde vesicular trafficking from the ER to the Golgi and accelerated retrograde vesicular recycling from the Golgi to the ER, leading to a decrease in Golgi volume, as well as morphologic abnormalities with collapse of the Golgi stacks in affected fibroblasts; altered decorin/DCNGolgi-dependent glycosylation; no effect on protein expression;, features a modification of the amino acid from G to R at position 512.
+The protein's natural variant, known as in CDG2J; severe defects in glycosylation, features a modification of the amino acid from R to W at position 729.
+The protein's natural variant, known as in strain: cv. IPA-6, features a modification of the amino acid from I to V at position 3.
+The protein's natural variant, known as in strain: Oak Ridge, features a modification of the amino acid from S to P at position 17.
+The protein's natural variant, known as in strain: Oak Ridge, features a modification of the amino acid from G to A at position 21.
+The protein's natural variant, known as in strain: TS, features a modification of the amino acid from I to L at position 98.
+The protein's natural variant, known as in strain: TS, features a modification of the amino acid from K to N at position 114.
+The protein's natural variant, known as in strain: Oak Ridge, features a modification of the amino acid from S to L at position 292.
+The protein's natural variant, known as in strain: TS, features a modification of the amino acid from F to L at position 317.
+The protein's natural variant, known as in strain: TS, features a modification of the amino acid from V to I at position 320.
+The protein's natural variant, known as in strain: TS, features a modification of the amino acid from SK to ND at position 347.
+The protein's natural variant, known as in strain: TS, features a modification of the amino acid from D to T at position 351.
+The protein's natural variant, known as in strain: TS, features a modification of the amino acid from H to K at position 355.
+The protein's natural variant, known as in strain: TS, features a modification of the amino acid from Q to K at position 374.
+The protein's natural variant, known as in strain: TS, features a modification of the amino acid from V to P at position 379.
+The protein's natural variant, known as in strain: TS, features a modification of the amino acid from L to M at position 439.
+The protein's natural variant, known as found in a patient with idiopathic dilated cardiomyopathy; renders cells partially insensitive to amino acid deprivation and result in activated mTORC1 signaling, features a modification of the amino acid from S to Y at position 75.
+The protein's natural variant, known as in strain: ATCC 19257, features a modification of the amino acid from G to R at position 48.
+The protein's natural variant, known as in strain: ATCC 19257, features a modification of the amino acid from P to S at position 94.
+The protein's natural variant, known as in strain: NIRDHC-1, features a modification of the amino acid from D to E at position 191.
+The protein's natural variant, known as in strain: ATCC 19257 and NIRDHC-1, features a modification of the amino acid from L to V at position 318.
+The protein's natural variant, known as in IBD1; unknown pathological significance;, features a modification of the amino acid from D to N at position 113.
+The protein's natural variant, known as in IBD1; also found in patients with ulcerative colitis; unknown pathological significance;, features a modification of the amino acid from A to T at position 140.
+The protein's natural variant, known as in IBD1; unknown pathological significance;, features a modification of the amino acid from W to R at position 157.
+The protein's natural variant, known as in IBD1; unknown pathological significance;, features a modification of the amino acid from R to C at position 235.
+The protein's natural variant, known as in IBD1; unknown pathological significance; no disruption of NOD2-CARD9 interaction;, features a modification of the amino acid from L to R at position 248.
+The protein's natural variant, known as in IBD1; unknown pathological significance;, features a modification of the amino acid from D to N at position 291.
+The protein's natural variant, known as in IBD1; unknown pathological significance;, features a modification of the amino acid from T to S at position 294.
+The protein's natural variant, known as in IBD1; unknown pathological significance;, features a modification of the amino acid from A to V at position 301.
+The protein's natural variant, known as in IBD1; also found in patients with ulcerative colitis; unknown pathological significance;, features a modification of the amino acid from R to W at position 311.
+The protein's natural variant, known as in BLAUS; somatic mosaicism in 4.9% to 11% of peripheral blood cells; hyperactive; constitutive NF-kappa-B activation in absence of muramyl dipeptide stimulation; abolishes interaction with LDOC1, ANKHD1, PPP2R3B, ENTR1 and TRIM41; decreases interaction with RIPK2 and PPP1R12C; no effect on interaction with CHMP5;, features a modification of the amino acid from R to Q at position 334.
+The protein's natural variant, known as in BLAUS; no disruption of NOD2-CARD9 interaction; hyperactive; constitutive NF-kappa-B activation in absence of muramyl dipeptide stimulation;, features a modification of the amino acid from R to W at position 334.
+The protein's natural variant, known as in IBD1; unknown pathological significance;, features a modification of the amino acid from L to V at position 348.
+The protein's natural variant, known as in IBD1; unknown pathological significance;, features a modification of the amino acid from H to R at position 352.
+The protein's natural variant, known as in IBD1; unknown pathological significance; no disruption of NOD2-CARD9 interaction;, features a modification of the amino acid from D to A at position 357.
+The protein's natural variant, known as in IBD1; unknown pathological significance; no disruption of NOD2-CARD9 interaction;, features a modification of the amino acid from I to F at position 363.
+The protein's natural variant, known as in IBD1; unknown pathological significance;, features a modification of the amino acid from R to C at position 373.
+The protein's natural variant, known as in BLAUS; hyperactive;, features a modification of the amino acid from D to E at position 382.
+The protein's natural variant, known as in BLAUS; unknown pathological significance; hyperactive;, features a modification of the amino acid from E to G at position 383.
+The protein's natural variant, known as in BLAUS; hyperactive;, features a modification of the amino acid from E to K at position 383.
+The protein's natural variant, known as in IBD1; unknown pathological significance;, features a modification of the amino acid from N to S at position 414.
+The protein's natural variant, known as in IBD1; unknown pathological significance; no disruption of NOD2-CARD9 interaction;, features a modification of the amino acid from S to L at position 431.
+The protein's natural variant, known as in IBD1; unknown pathological significance;, features a modification of the amino acid from A to V at position 432.
+The protein's natural variant, known as in IBD1; unknown pathological significance; no disruption of NOD2-CARD9 interaction;, features a modification of the amino acid from E to K at position 441.
+The protein's natural variant, known as no disruption of NOD2-CARD9 interaction;, features a modification of the amino acid from P to A at position 463.
+The protein's natural variant, known as hyperactive;, features a modification of the amino acid from G to W at position 464.
+The protein's natural variant, known as in BLAUS; hyperactive; constitutive NF-kappa-B activation in absence of muramyl dipeptide stimulation;, features a modification of the amino acid from L to F at position 469.
+The protein's natural variant, known as does not affect activity;, features a modification of the amino acid from R to C at position 471.
+The protein's natural variant, known as in BLAUS; atypical form with cardiac infiltration; sporadic case; unknown pathological significance; hyperactive;, features a modification of the amino acid from G to D at position 481.
+The protein's natural variant, known as in BLAUS; unknown pathological significance; hyperactive;, features a modification of the amino acid from W to L at position 490.
+The protein's natural variant, known as in BLAUS; unknown pathological significance; hyperactive;, features a modification of the amino acid from C to Y at position 495.
+The protein's natural variant, known as in BLAUS; hyperactive;, features a modification of the amino acid from H to L at position 496.
+The protein's natural variant, known as in BLAUS, features a modification of the amino acid from E to D at position 498.
+The protein's natural variant, known as in BLAUS, features a modification of the amino acid from P to S at position 507.
+The protein's natural variant, known as in BLAUS; hyperactive;, features a modification of the amino acid from M to T at position 513.
+The protein's natural variant, known as in IBD1; unknown pathological significance; no disruption of NOD2-CARD9 interaction;, features a modification of the amino acid from L to V at position 550.
+The protein's natural variant, known as in BLAUS; unknown pathological significance; not hyperactive;, features a modification of the amino acid from R to C at position 587.
+The protein's natural variant, known as in BLAUS; hyperactive, features a modification of the amino acid from T to N at position 605.
+The protein's natural variant, known as in BLAUS; hyperactive;, features a modification of the amino acid from T to P at position 605.
+The protein's natural variant, known as in BLAUS and IBD1; unknown pathological significance;, features a modification of the amino acid from A to T at position 612.
+The protein's natural variant, known as in IBD1; unknown pathological significance; no disruption of NOD2-CARD9 interaction;, features a modification of the amino acid from A to V at position 612.
+The protein's natural variant, known as in BLAUS; hyperactive;, features a modification of the amino acid from N to K at position 670.
+The protein's natural variant, known as in IBD1; unknown pathological significance;, features a modification of the amino acid from R to W at position 684.
+The protein's natural variant, known as in IBD1 and YAOS; associated with disease susceptibility; decreased NF-kappa-B activation in response to muramyl dipeptide stimulation; no disruption of NOD2-CARD9 interaction; decreases half-life of protein; abolishes interaction with ANKHD1, ENTR1 and TRIM41; increases interaction with RIPK2 and PPP2R3B; decreases interaction with LDOC1 and PPP1R12C; no effect on interaction with CHMP5; decreased NF-kappa-B activation in response to muramyl dipeptide stimulation;, features a modification of the amino acid from R to W at position 702.
+The protein's natural variant, known as in IBD1; also found in patients with ulcerative colitis; unknown pathological significance;, features a modification of the amino acid from R to C at position 703.
+The protein's natural variant, known as in IBD1; unknown pathological significance;, features a modification of the amino acid from R to C at position 713.
+The protein's natural variant, known as in IBD1; unknown pathological significance;, features a modification of the amino acid from R to H at position 713.
+The protein's natural variant, known as in IBD1; unknown pathological significance;, features a modification of the amino acid from A to G at position 725.
+The protein's natural variant, known as in IBD1; also found in patients with ulcerative colitis; unknown pathological significance;, features a modification of the amino acid from A to V at position 755.
+The protein's natural variant, known as in IBD1; unknown pathological significance;, features a modification of the amino acid from A to V at position 758.
+The protein's natural variant, known as in IBD1; unknown pathological significance;, features a modification of the amino acid from R to C at position 760.
+The protein's natural variant, known as in IBD1; unknown pathological significance;, features a modification of the amino acid from E to K at position 778.
+The protein's natural variant, known as in IBD1; unknown pathological significance;, features a modification of the amino acid from R to W at position 790.
+The protein's natural variant, known as in IBD1; unknown pathological significance;, features a modification of the amino acid from V to M at position 793.
+The protein's natural variant, known as in IBD1; unknown pathological significance;, features a modification of the amino acid from E to K at position 843.
+The protein's natural variant, known as in IBD1; unknown pathological significance;, features a modification of the amino acid from N to S at position 852.
+The protein's natural variant, known as in IBD1; unknown pathological significance;, features a modification of the amino acid from N to S at position 853.
+The protein's natural variant, known as in IBD1; decreased NF-kappa-B activation in response to muramyl dipeptide stimulation;, features a modification of the amino acid from M to V at position 863.
+The protein's natural variant, known as in IBD1; unknown pathological significance, features a modification of the amino acid from A to T at position 885.
+The protein's natural variant, known as in IBD1 and YAOS; associated with disease susceptibility; decreased NF-kappa-B activation in response to muramyl dipeptide stimulation; decreases half-life of protein; abolishes interaction with ANKHD1, ENTR1 and TRIM41; decreases interaction with RIPK2 and PPP1R12C; no effect on interaction with CHMP5, LDOC1 and PPP2R3B;, features a modification of the amino acid from G to R at position 908.
+The protein's natural variant, known as in IBD1; unknown pathological significance;, features a modification of the amino acid from G to D at position 924.
+The protein's natural variant, known as in IBD1; abolished NF-kappa-B activation in response to muramyl dipeptide stimulation; decreased localization to the cell membrane, features a modification of the amino acid from LERNDTILEVWLRGNTFSLEEVDKLGCRDTRLLL to P at position 1040.
+The protein's natural variant, known as in EBS1C;, features a modification of the amino acid from K to N at position 116.
+The protein's natural variant, known as in EBS1C;, features a modification of the amino acid from M to I at position 119.
+The protein's natural variant, known as in EBS1A;, features a modification of the amino acid from M to T at position 119.
+The protein's natural variant, known as in EBS1B and EBS1C;, features a modification of the amino acid from M to V at position 119.
+The protein's natural variant, known as in EBS1A;, features a modification of the amino acid from Q to R at position 120.
+The protein's natural variant, known as in EBS1A and EBS1B;, features a modification of the amino acid from L to F at position 122.
+The protein's natural variant, known as in EBS1A;, features a modification of the amino acid from N to K at position 123.
+The protein's natural variant, known as in EBS1A;, features a modification of the amino acid from N to S at position 123.
+The protein's natural variant, known as in EBS1A;, features a modification of the amino acid from R to C at position 125.
+The protein's natural variant, known as in EBS1A;, features a modification of the amino acid from R to G at position 125.
+The protein's natural variant, known as in EBS1A;, features a modification of the amino acid from R to H at position 125.
+The protein's natural variant, known as probable disease-associated variant found in a patient with epidermolysis bullosa simplex with unspecified subtype;, features a modification of the amino acid from R to L at position 125.
+The protein's natural variant, known as in EBS1A, features a modification of the amino acid from R to S at position 125.
+The protein's natural variant, known as in EBS1A;, features a modification of the amino acid from Y to D at position 129.
+The protein's natural variant, known as in EBS1A; unknown pathological significance;, features a modification of the amino acid from L to P at position 130.
+The protein's natural variant, known as in EBS1C and EBS1B;, features a modification of the amino acid from V to L at position 133.
+The protein's natural variant, known as in EBS1C;, features a modification of the amino acid from V to M at position 133.
+The protein's natural variant, known as in EBS1B;, features a modification of the amino acid from R to P at position 134.
+The protein's natural variant, known as in EBS1B;, features a modification of the amino acid from L to P at position 143.
+The protein's natural variant, known as in EBS1D;, features a modification of the amino acid from E to A at position 144.
+The protein's natural variant, known as in EBS1C;, features a modification of the amino acid from R to C at position 148.
+The protein's natural variant, known as in EBS1C;, features a modification of the amino acid from R to P at position 211.
+The protein's natural variant, known as in EBS1B;, features a modification of the amino acid from A to D at position 247.
+The protein's natural variant, known as in EBS1C, features a modification of the amino acid from V to A at position 270.
+The protein's natural variant, known as in EBS1A;, features a modification of the amino acid from V to M at position 270.
+The protein's natural variant, known as in EBS1B and EBS1A;, features a modification of the amino acid from M to R at position 272.
+The protein's natural variant, known as in EBS1B and EBS1C;, features a modification of the amino acid from M to T at position 272.
+The protein's natural variant, known as in EBS1C;, features a modification of the amino acid from D to G at position 273.
+The protein's natural variant, known as in EBS1C;, features a modification of the amino acid from A to D at position 274.
+The protein's natural variant, known as in EBS1C;, features a modification of the amino acid from I to N at position 377.
+The protein's natural variant, known as in EBS1C; unknown pathological significance;, features a modification of the amino acid from I to T at position 377.
+The protein's natural variant, known as in EBS1B;, features a modification of the amino acid from L to P at position 384.
+The protein's natural variant, known as in EBS1C; also found in a patient with epidermolysis bullosa simplex with unspecified subtype;, features a modification of the amino acid from R to C at position 388.
+The protein's natural variant, known as in EBS1D;, features a modification of the amino acid from R to H at position 388.
+The protein's natural variant, known as in EBS1C;, features a modification of the amino acid from L to M at position 408.
+The protein's natural variant, known as in EBS1C; unknown pathological significance;, features a modification of the amino acid from I to F at position 412.
+The protein's natural variant, known as in EBS1B and EBS1C; unknown pathological significance;, features a modification of the amino acid from A to T at position 413.
+The protein's natural variant, known as in EBS1C;, features a modification of the amino acid from Y to C at position 415.
+The protein's natural variant, known as in EBS1B;, features a modification of the amino acid from Y to H at position 415.
+The protein's natural variant, known as in EBS1A;, features a modification of the amino acid from R to P at position 416.
+The protein's natural variant, known as in EBS1A;, features a modification of the amino acid from R to P at position 417.
+The protein's natural variant, known as in EBS1C, features a modification of the amino acid from L to Q at position 418.
+The protein's natural variant, known as in EBS1A;, features a modification of the amino acid from L to Q at position 419.
+The protein's natural variant, known as in EBS1C;, features a modification of the amino acid from E to K at position 422.
+The protein's natural variant, known as found in a patient with intellectual disability, seizures, mild hypotonia and no speech, features a modification of the amino acid from R to H at position 474.
+The protein's natural variant, known as in strain: Isolate C-182, features a modification of the amino acid from V to M at position 102.
+The protein's natural variant, known as in strain: Isolate C-182, features a modification of the amino acid from M to T at position 238.
+The protein's natural variant, known as in strain: Isolate C-182, features a modification of the amino acid from F to L at position 333.
+The natural variant of this protein is characterized by an amino acid alteration from I to F at position 159.
+The natural variant of this protein is characterized by an amino acid alteration from I to L at position 159.
+The protein's natural variant, known as in strain: Isolate IZEA7514, features a modification of the amino acid from V to I at position 39.
+The protein's natural variant, known as in CHN3, features a modification of the amino acid from P to Q at position 50.
+The protein's natural variant, known as in CHN3;, features a modification of the amino acid from L to P at position 212.
+The protein's natural variant, known as in LCCS7;, features a modification of the amino acid from C to R at position 323.
+The protein's natural variant, known as in CHN3;, features a modification of the amino acid from R to P at position 388.
+The protein's natural variant, known as in CHN3, features a modification of the amino acid from R to P at position 714.
+The protein's natural variant, known as in CHN3;, features a modification of the amino acid from R to C at position 764.
+The protein's natural variant, known as in strain: AR39 and J138, features a modification of the amino acid from Y to H at position 139.
+The protein's natural variant, known as in VICIS; relatively mild phenotype characterized by absence or later onset of cardiac or immunologic features; a normally spliced transcript with the missense variant and multiple misspliced transcripts are detected in patient cells; results in 50% decrease of mRNA levels in patient cells most probably due to nonsense-mediated decay of misspliced transcripts;, features a modification of the amino acid from Q to R at position 336.
+The protein's natural variant, known as in VICIS; unknown pathological significance; associated in cis with P-784;, features a modification of the amino acid from L to P at position 457.
+The protein's natural variant, known as in VICIS; unknown pathological significance; associated in cis with P-457;, features a modification of the amino acid from Q to P at position 784.
+The protein's natural variant, known as in VICIS; unknown pathological significance;, features a modification of the amino acid from G to E at position 1336.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from A to T at position 1511.
+The protein's natural variant, known as in VICIS;, features a modification of the amino acid from P to A at position 1827.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from C to Y at position 1865.
+The protein's natural variant, known as in VICIS; unknown pathological significance;, features a modification of the amino acid from C to R at position 2038.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from R to W at position 2056.
+The protein's natural variant, known as in VICIS; unknown pathological significance;, features a modification of the amino acid from L to P at position 2092.
+The protein's natural variant, known as in VICIS; unknown pathological significance;, features a modification of the amino acid from E to K at position 2414.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from T to M at position 60.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from D to H at position 62.
+The protein's natural variant, known as in GTLMNS, features a modification of the amino acid from D to N at position 62.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from E to K at position 68.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from H to N at position 69.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from R to Q at position 83.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from R to W at position 83.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from H to Y at position 90.
+The protein's natural variant, known as in GTLMNS; 27% residual Na(+) uptake activity; increased MAPK1/3 (ERK1/2) phosphorylation in response to IL18; no effect on localization at the plasma membrane;, features a modification of the amino acid from E to D at position 121.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from R to C at position 135.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from R to C at position 145.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from R to H at position 145.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from I to M at position 150.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from V to M at position 153.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from I to F at position 154.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from L to P at position 157.
+The protein's natural variant, known as in GTLMNS, features a modification of the amino acid from R to L at position 158.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from R to Q at position 158.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from T to M at position 163.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from A to V at position 166.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from W to R at position 172.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from S to L at position 178.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from T to K at position 180.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from G to D at position 186.
+The protein's natural variant, known as in GTLMNS; associated with deletion of N-566;, features a modification of the amino acid from I to T at position 192.
+The protein's natural variant, known as in GTLMNS, features a modification of the amino acid from T to I at position 194.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from R to Q at position 209.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from R to W at position 209.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from L to P at position 215.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from A to T at position 226.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from G to D at position 230.
+The protein's natural variant, known as in GTLMNS, features a modification of the amino acid from T to R at position 235.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from D to N at position 259.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from R to H at position 261.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from L to P at position 272.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from S to Y at position 283.
+The protein's natural variant, known as in GTLMNS, features a modification of the amino acid from K to R at position 284.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from T to M at position 304.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from T to P at position 304.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from A to V at position 313.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from G to V at position 316.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from R to W at position 321.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from R to W at position 334.
+The protein's natural variant, known as in GTLMNS, features a modification of the amino acid from G to A at position 342.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from P to L at position 349.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from G to E at position 374.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from G to V at position 374.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from T to M at position 382.
+The protein's natural variant, known as in GTLMNS; complete loss Na(+) uptake activity; partial loss of localization at the plasma membrane;, features a modification of the amino acid from T to I at position 392.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from R to C at position 399.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from C to R at position 421.
+The protein's natural variant, known as in GTLMNS, features a modification of the amino acid from QHSC to L at position 436.
+The protein's natural variant, known as in GTLMNS; does not affect MAPK1/3 (ERK1/2) phosphorylation in response to IL18;, features a modification of the amino acid from G to S at position 439.
+The protein's natural variant, known as in GTLMNS; 68% residual Na(+) uptake activity; partial loss of localization at the plasma membrane, features a modification of the amino acid from N to S at position 442.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from G to E at position 463.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from G to R at position 463.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from A to T at position 464.
+The protein's natural variant, known as in GTLMNS; 40% residual Na(+) uptake activity; increased MAPK1/3 (ERK1/2) phosphorylation in response to IL18; no effect on localization at the plasma membrane;, features a modification of the amino acid from S to C at position 475.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from K to E at position 478.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from D to N at position 486.
+The protein's natural variant, known as in GTLMNS; 48% residual Na(+) uptake activity; no effect on localization at the plasma membrane, features a modification of the amino acid from Y to H at position 489.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from G to C at position 496.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from R to C at position 507.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from A to T at position 523.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from N to S at position 534.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from F to L at position 536.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from L to P at position 542.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from S to G at position 546.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from S to L at position 555.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from P to H at position 560.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from P to R at position 560.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from A to E at position 569.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from A to V at position 569.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from V to M at position 578.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from A to V at position 588.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from G to S at position 613.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from S to L at position 615.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from S to W at position 615.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from L to P at position 623.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from G to V at position 630.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from R to C at position 642.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from R to G at position 642.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from R to H at position 642.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from P to L at position 643.
+The protein's natural variant, known as in GTLMNS, features a modification of the amino acid from V to M at position 647.
+The protein's natural variant, known as in GTLMNS, features a modification of the amino acid from T to R at position 649.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from R to C at position 655.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from R to H at position 655.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from R to L at position 655.
+The protein's natural variant, known as in GTLMNS, features a modification of the amino acid from M to I at position 672.
+The protein's natural variant, known as in GTLMNS, features a modification of the amino acid from V to L at position 677.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from V to M at position 677.
+The protein's natural variant, known as in GTLMNS, features a modification of the amino acid from I to IKAFYSDVI at position 713.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from G to V at position 729.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from G to R at position 731.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from P to R at position 735.
+The protein's natural variant, known as in GTLMNS, features a modification of the amino acid from L to R at position 738.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from G to R at position 741.
+The protein's natural variant, known as in GTLMNS; 54% residual Na(+) uptake activity; no effect on localization at the plasma membrane;, features a modification of the amino acid from P to L at position 751.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from S to T at position 824.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from D to N at position 839.
+The protein's natural variant, known as in GTLMNS, features a modification of the amino acid from L to F at position 849.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from L to H at position 849.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from L to P at position 850.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from R to C at position 852.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from R to H at position 852.
+The protein's natural variant, known as in GTLMNS, features a modification of the amino acid from R to S at position 852.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from R to C at position 862.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from G to S at position 867.
+The protein's natural variant, known as in GTLMNS, features a modification of the amino acid from R to H at position 871.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from M to T at position 872.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from R to Q at position 887.
+The protein's natural variant, known as increases sodium transport;, features a modification of the amino acid from R to C at position 919.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from R to W at position 934.
+The protein's natural variant, known as in GTLMNS; unknown pathological significance;, features a modification of the amino acid from R to W at position 935.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from R to Q at position 955.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from R to G at position 958.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from G to R at position 980.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from C to Y at position 985.
+The protein's natural variant, known as in GTLMNS;, features a modification of the amino acid from R to Q at position 1009.
+The protein's natural variant, known as in GTLMNS; 58% residual Na(+) uptake activity; decreased MAPK1/3 (ERK1/2) phosphorylation in response to IL18; partial loss of localization at the plasma membrane;, features a modification of the amino acid from Q to R at position 1021.
+The protein's natural variant, known as in cancer cells, may be associated with accelerated disease progression and increased tumor cell motility, possibly due to increased stability of the protease MMP14; leads to phosphorylation at residue Y-390, resulting in prolonged FGFR4 activity; increases interaction with STAT3, resulting in STAT3 phosphorylation and signaling activation.;, features a modification of the amino acid from G to R at position 388.
+The protein's natural variant, known as in breast pleomorphic lobular sample; somatic mutation;, features a modification of the amino acid from V to M at position 550.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation, features a modification of the amino acid from P to T at position 712.
+The protein's natural variant, known as in a lung neuroendocrine carcinoma sample; somatic mutation, features a modification of the amino acid from S to N at position 772.
+The natural variant of this protein is characterized by an amino acid alteration from A to V at position 55.
+The protein's natural variant, known as in STRL33.3, features a modification of the amino acid from D to A at position 25.
+The protein's natural variant, known as in strain: NC-100, features a modification of the amino acid from D to V at position 14.
+The protein's natural variant, known as in strain: CA-128, NC-005, NC-114 and NC-115, features a modification of the amino acid from G to R at position 40.
+The protein's natural variant, known as in strain: CA-001, CA-002, CA-003, CA-008, CA-009, CA-010, CA-011, CA-012, CA-015, CA-017, CA-018, CA-023, CA-026, CA-027, CA-030, CA-034, CA-035, CA-037, CA-040, CA-041, CA-043, CA-044, CA-046, CA-047, CA-048, CA-052, CA-055, CA-056, CA-057, CA-058, CA-060, CA-061, CA-062, CA-063, CA-064, CA-065, CA-066, CA-068, CA-069, CA-070, CA-072, CA-075, CA-081, CA-086, CA-087, CA-088, CA-090, CA-091, CA-093, CA-095, CA-105, CA-113, CA-114, CA-120, CA-126, CA-128, CA-129, CA-130, CA-132, CA-133, CA-136, CA-137, CA-140, CA-142, CA-144, CA-145, CA-147, Oregon-R, NC-001, NC-002, NC-003, NC-004, NC-005, NC-006, NC-008, NC-010, NC-011, NC-012, NC-014, NC-015, NC-017, NC-021, NC-022, NC-023, NC-025, NC-026, NC-027, NC-028, NC-029, NC-030, NC-032, NC-033, NC-034, NC-036, NC-040, NC-041, NC-042, NC-043, NC-044, NC-046, NC-047, NC-048, NC-049, NC-051, NC-052, NC-053, NC-054, NC-057, NC-058, NC-059, NC-060, NC-062, NC-064, NC-066, NC-067, NC-068, NC-069, NC-071, NC-072, NC-073, NC-074, NC-075, NC-077, NC-079, NC-080, NC-081, NC-084, NC-086, NC-087, NC-089, NC-091, NC-092, NC-094, NC-095, NC-096, NC-097, NC-098, NC-100, NC-101, NC-103, NC-104, NC-105, NC-107, NC-108, NC-110, NC-112, NC-113, NC-114, NC-115, NC-116, NC-118, NC-119, NC-121, NC-123, NC-124, NC-126, NC-127, NC-128, NC-129, NC-131, NC-134, NC-135, NC-136, NC-137, NC-138, NC-139, NC-141, NC-142, NC-144, NC-146, NC-147, NC-149 and NC-148, features a modification of the amino acid from I to V at position 61.
+The protein's natural variant, known as in strain: CA-027, features a modification of the amino acid from E to K at position 76.
+The protein's natural variant, known as in strain: NC-037, NC-038, NC-039 and NC-109, features a modification of the amino acid from R to W at position 79.
+The protein's natural variant, known as in strain: NC-053, features a modification of the amino acid from M to I at position 90.
+The protein's natural variant, known as in strain: NC-026 and NC-027, features a modification of the amino acid from A to E at position 301.
+The protein's natural variant, known as in strain: CA-017, CA-061, CA-062, CA-093, CA-132, CA-018, CA-027, CA-070, CA-075, CA-081, CA-086, CA-096, CA-100, CA-105, CA-126, CA-128, CA-130, CA-137, CA-142, CA-145, NC-024, NC-048, NC-071, NC-104, NC-005, NC-008, NC-018, NC-025, NC-028, NC-043, NC-046, NC-049, NC-054, NC-058, NC-070, NC-077, NC-095, NC-098, NC-101, NC-103, NC-114, NC-115, NC-119, NC-136 and NC-141, features a modification of the amino acid from R to H at position 309.
+The protein's natural variant, known as in strain: CA-003, CA-035, CA-062, CA-066, CA-081, CA-091, CA-126, CA-145, CA-010, CA-015, CA-017, CA-018, CA-023, CA-027, CA-030, CA-061, CA-064, CA-070, CA-072, CA-075, CA-086, CA-090, CA-093, CA-095, CA-096, CA-100, CA-105, CA-114, CA-128, CA-130, CA-132, CA-137, CA-142, NC-010, NC-022, NC-028, NC-036, NC-037, NC-054, NC-068, NC-092, NC-095, NC-108, NC-100, NC-111, NC-119, NC-125, NC-142, NC-001, NC-003, NC-005, NC-006, NC-008, NC-012, NC-014, NC-017, NC-018, NC-021, NC-023, NC-024, NC-025, NC-026, NC-027, NC-032, NC-038, NC-039, NC-043, NC-046, NC-048, NC-049, NC-053, NC-058, NC-059, NC-069, NC-070, NC-071, NC-073, NC-077, NC-084, NC-089, NC-094, NC-096, NC-097, NC-098, NC-101, NC-103, NC-104, NC-105, NC-107, NC-114, NC-115, NC-118, NC-121, NC-123, NC-124, NC-126, NC-127, NC-131, NC-136, NC-139, NC-141, NC-146 and NC-149, features a modification of the amino acid from S to G at position 310.
+The protein's natural variant, known as in strain: CA-040, CA-055 and CA-098, features a modification of the amino acid from T to I at position 460.
+The protein's natural variant, known as in strain: NC-003 and NC-142, features a modification of the amino acid from T to S at position 463.
+The protein's natural variant, known as in strain: CA-064, NC-015, NC-096, NC-108, NC-128, NC-135 and NC-137, features a modification of the amino acid from A to V at position 492.
+The protein's natural variant, known as in strain: DBA/2J, features a modification of the amino acid from D to N at position 216.
+The protein's natural variant, known as in beta-F, features a modification of the amino acid from A to D at position 58.
+The natural variant of this protein is characterized by an amino acid alteration from L to V at position 1012.
+The protein's natural variant, known as in DISPORD; complete loss of activity;, features a modification of the amino acid from Y to D at position 178.
+The protein's natural variant, known as in ABS1 and DISPORD; significant reduction of activity;, features a modification of the amino acid from A to P at position 284.
+The protein's natural variant, known as in ABS1 and DISPORD; significant reduction of activity;, features a modification of the amino acid from R to H at position 454.
+The protein's natural variant, known as in ABS1; significant reduction of activity;, features a modification of the amino acid from V to E at position 489.
+The natural variant of this protein is characterized by an amino acid alteration from R to Q at position 551.
+The protein's natural variant, known as in DISPORD; significant reduction of activity;, features a modification of the amino acid from C to Y at position 566.
+The protein's natural variant, known as in ABS1, features a modification of the amino acid from Y to C at position 575.
+The protein's natural variant, known as in DISPORD; significant reduction of activity;, features a modification of the amino acid from V to F at position 605.
+The protein's natural variant, known as in ABS1, features a modification of the amino acid from LKQDREHLW to R at position 617.
+The protein's natural variant, known as in long hair dog breeds, features a modification of the amino acid from S to STS at position 50.
+The protein's natural variant, known as in long hair dog breeds, features a modification of the amino acid from C to F at position 95.
+The natural variant of this protein is characterized by an amino acid alteration from G to S at position 22.
+The natural variant of this protein is characterized by an amino acid alteration from A to V at position 97.
+The protein's natural variant, known as in a patient with neurodevelopmental abnormalities; de novo variant; unknown pathological significance;, features a modification of the amino acid from S to L at position 93.
+The protein's natural variant, known as in a patient with neurodevelopmental abnormalities; de novo variant; unknown pathological significance, features a modification of the amino acid from G to V at position 98.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation, features a modification of the amino acid from A to T at position 269.
+The protein's natural variant, known as in MCCCHCM;, features a modification of the amino acid from G to S at position 517.
+The protein's natural variant, known as in a patient with neurodevelopmental abnormalities; de novo variant; unknown pathological significance, features a modification of the amino acid from A to T at position 915.
+The protein's natural variant, known as in a patient with neurodevelopmental abnormalities; de novo variant; unknown pathological significance, features a modification of the amino acid from P to R at position 1177.
+The protein's natural variant, known as in an ovarian serous carcinoma sample; somatic mutation;, features a modification of the amino acid from H to Y at position 1240.
+The protein's natural variant, known as in allele SAA3.2, features a modification of the amino acid from R to K at position 48.
+The protein's natural variant, known as in allele SAA3.2, features a modification of the amino acid from R to Q at position 64.
+The protein's natural variant, known as in allele SAA3.2, features a modification of the amino acid from G to C at position 93.
+The protein's natural variant, known as in allele SAA3.2, features a modification of the amino acid from F to A at position 108.
+The protein's natural variant, known as in ETL8; decreased affinity for GALR2; but no effect on affinity for GALR1 and GALR3; decreased activity in GALR2-mediated signaling; dominant-negative that inhibits GALR1-mediated signaling;, features a modification of the amino acid from A to E at position 39.
+The natural variant of this protein is characterized by an amino acid alteration from Q to T at position 64.
+The protein's natural variant, known as in strain: Han/Wistar, Han/Wistar-dv, Han/Wistar-siv and Han/Wistar-liv, features a modification of the amino acid from V to A at position 497.
+The protein's natural variant, known as in strain: Han/Wistar-siv and Han/Wistar-liv, features a modification of the amino acid from FQSPSILNEAYSADLSSIGHLQTAAHLPRLAEAQPLPDITPSGFL to IRAFYRE at position 853.
+The protein's natural variant, known as found in a patient with schizophrenia; found as somatic mutation in a colorectal cancer sample; unknown pathological significance; decreased localization to cell membrane; decreased function in synaptogenesis;, features a modification of the amino acid from V to I at position 206.
+The protein's natural variant, known as found in a patient with schizophrenia; unknown pathological significance; decreased localization to cell membrane; decreased function in synaptogenesis;, features a modification of the amino acid from I to V at position 578.
+The protein's natural variant, known as in oncogenic NEU, features a modification of the amino acid from V to E at position 658.
+The protein's natural variant, known as in oncogenic NEU, features a modification of the amino acid from V to E at position 659.
+The protein's natural variant, known as in DEVLO, features a modification of the amino acid from R to C at position 158.
+The protein's natural variant, known as in strain: DK429 and DK439; causes defects in fruiting body development and in sporulation, features a modification of the amino acid from G to E at position 134.
+The protein's natural variant, known as in allelic variant, features a modification of the amino acid from I to V at position 289.
+The protein's natural variant, known as in allelic variant, features a modification of the amino acid from E to A at position 338.
+The protein's natural variant, known as in allelic variant, features a modification of the amino acid from L to V at position 415.
+The protein's natural variant, known as in mutant TrpA46-Asp-PR3, features a modification of the amino acid from LQGFGISAPDQVKAAI to IAGFWYFRPGSGKSSD at position 224.
+The protein's natural variant, known as in a lung squamous cell carcinoma sample; somatic mutation, features a modification of the amino acid from R to L at position 12.
+The protein's natural variant, known as in ACL1.A3, features a modification of the amino acid from K to KK at position 134.
+The protein's natural variant, known as in FIH2; abolishes normal DNA binding ability of the protein;, features a modification of the amino acid from R to L at position 47.
+The protein's natural variant, known as in FIH2; the mutation causes loss-of-function; abolishes transactivation capacity despite normal subcellular localization, protein stability and DNA-binding specificity;, features a modification of the amino acid from G to S at position 63.
+The protein's natural variant, known as in FIH2; abolishes DNA binding ability;, features a modification of the amino acid from R to W at position 110.
+The protein's natural variant, known as shows normal transcriptional activity;, features a modification of the amino acid from G to S at position 203.
+The protein's natural variant, known as shows normal transcriptional activity;, features a modification of the amino acid from I to V at position 227.
+The protein's natural variant, known as in HRPT4; found on the same allele as Q-379; gain-of-function mutation; increases transcriptional activity;, features a modification of the amino acid from Q to E at position 251.
+The protein's natural variant, known as shows normal transcriptional activity;, features a modification of the amino acid from Y to D at position 282.
+The protein's natural variant, known as shows normal transcriptional activity;, features a modification of the amino acid from N to D at position 315.
+The protein's natural variant, known as in HRPT4; found on the same allele as E-251; gain-of-function mutation; increases transcriptional activity;, features a modification of the amino acid from L to Q at position 379.
+The protein's natural variant, known as in HRPT4; unknown pathological significance;, features a modification of the amino acid from V to M at position 382.
+The protein's natural variant, known as in HRPT4; gain-of-function mutation; increases transcriptional activity;, features a modification of the amino acid from Y to S at position 394.
+The protein's natural variant, known as in FIH2; exerts a dominant-negative effect to abolish transactivation capacity;, features a modification of the amino acid from N to H at position 502.
+The protein's natural variant, known as in strain: Isolate 3, features a modification of the amino acid from A to T at position 122.
+The protein's natural variant, known as in strain: Isolate 3, features a modification of the amino acid from A to S at position 314.
+The protein's natural variant, known as in GSD13; when associated with E-374;, features a modification of the amino acid from G to D at position 156.
+The protein's natural variant, known as in GSD13; when associated with D-156;, features a modification of the amino acid from G to E at position 374.
+The protein's natural variant, known as in Eur m 1.0102, features a modification of the amino acid from T to S at position 36.
+The protein's natural variant, known as in Eur m 1.0102, features a modification of the amino acid from M to N at position 126.
+The protein's natural variant, known as in Eur m 1.0102, features a modification of the amino acid from M to I at position 320.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from D to N at position 102.
+The protein's natural variant, known as in MPCD;, features a modification of the amino acid from G to E at position 72.
+The protein's natural variant, known as in NEDIDHA; unknown pathological significance;, features a modification of the amino acid from R to Q at position 392.
+The protein's natural variant, known as in NEDIDHA; unknown pathological significance;, features a modification of the amino acid from K to R at position 1296.
+The protein's natural variant, known as in NEDIDHA; unknown pathological significance;, features a modification of the amino acid from M to L at position 1674.
+The natural variant of this protein is characterized by an amino acid alteration from R to I at position 242.
+The protein's natural variant, known as in pepE1; deficient, features a modification of the amino acid from S to T at position 120.
+The protein's natural variant, known as in pepE1; deficient, features a modification of the amino acid from P to S at position 137.
+The protein's natural variant, known as in 50% of the molecules, features a modification of the amino acid from V to I at position 49.
+The protein's natural variant, known as in oncogenic form, features a modification of the amino acid from CQSLDSALLERKRLLSRK to GHQVIHEGSSTNDPNNSC at position 415.
+The protein's natural variant, known as in NEDHSCA; unknown pathological significance;, features a modification of the amino acid from T to M at position 124.
+The protein's natural variant, known as in NEDHSCA;, features a modification of the amino acid from N to S at position 138.
+The protein's natural variant, known as in NEDHSCA; unable to rescue surface expression of Emm in PIGG-null cells, features a modification of the amino acid from H to Y at position 214.
+The protein's natural variant, known as in NEDHSCA, features a modification of the amino acid from G to D at position 270.
+The protein's natural variant, known as in NEDHSCA;, features a modification of the amino acid from M to R at position 271.
+The protein's natural variant, known as in NEDHSCA;, features a modification of the amino acid from G to R at position 278.
+The protein's natural variant, known as in NEDHSCA; unknown pathological significance, features a modification of the amino acid from M to L at position 344.
+The protein's natural variant, known as in NEDHSCA; unknown pathological significance;, features a modification of the amino acid from S to L at position 497.
+The protein's natural variant, known as in NEDHSCA; unknown pathological significance;, features a modification of the amino acid from V to M at position 531.
+The protein's natural variant, known as found in SNIBFIS; unknown pathological significance, features a modification of the amino acid from K to N at position 538.
+The protein's natural variant, known as in NEDHSCA; almost complete loss of ethanolamine phosphate transferase activity as evidenced by abnormal accumulation of the GPI precursors H7 and H7' and absence of mature GPI precursor H8 in patient lymphoblasts; does not affect protein expression levels in transfected HEK293 cells;, features a modification of the amino acid from R to C at position 669.
+The protein's natural variant, known as in NEDHSCA; unknown pathological significance; shows a mild decrease in phosphotransferase activity;, features a modification of the amino acid from R to W at position 681.
+The protein's natural variant, known as in NEDHSCA; unknown pathological significance; shows a mild decrease in phosphotransferase activity, features a modification of the amino acid from E to D at position 696.
+The protein's natural variant, known as in NEDHSCA;, features a modification of the amino acid from Q to P at position 851.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from V to A at position 16.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from A to T at position 51.
+The protein's natural variant, known as in CPX;, features a modification of the amino acid from G to C at position 118.
+The protein's natural variant, known as in CPX, features a modification of the amino acid from M to V at position 121.
+The protein's natural variant, known as in CPX, features a modification of the amino acid from P to L at position 183.
+The protein's natural variant, known as in CPX, features a modification of the amino acid from S to SS at position 195.
+The protein's natural variant, known as in CPX;, features a modification of the amino acid from L to P at position 214.
+The natural variant of this protein is characterized by an amino acid alteration from F to Y at position 249.
+The protein's natural variant, known as in CPX;, features a modification of the amino acid from T to M at position 260.
+The protein's natural variant, known as in CPX;, features a modification of the amino acid from N to Y at position 264.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from D to N at position 307.
+The protein's natural variant, known as found in a patient with congenital bilateral cataract; unknown pathological significance;, features a modification of the amino acid from S to C at position 40.
+The protein's natural variant, known as found in a patient with congenital pediatric onset cataracts; unknown pathological significance;, features a modification of the amino acid from R to H at position 80.
+The protein's natural variant, known as in variants C, D, E, F and H, features a modification of the amino acid from T to S at position 13.
+The protein's natural variant, known as in variants C, D, E, F and H, features a modification of the amino acid from P to A at position 28.
+The protein's natural variant, known as in variants C, D, E, F and H, features a modification of the amino acid from I to T at position 29.
+The protein's natural variant, known as in variants C, D, E, F and H, features a modification of the amino acid from M to I at position 32.
+The protein's natural variant, known as in variants D, E and F, features a modification of the amino acid from N to S at position 79.
+The protein's natural variant, known as in variants D and E, features a modification of the amino acid from E to D at position 89.
+The protein's natural variant, known as in variants C, D, E, F and H, features a modification of the amino acid from A to S at position 99.
+The protein's natural variant, known as in variants C, D and E, features a modification of the amino acid from G to C at position 111.
+The protein's natural variant, known as in variant D, features a modification of the amino acid from D to N at position 121.
+The protein's natural variant, known as in variants C, D and E, features a modification of the amino acid from D to N at position 122.
+The protein's natural variant, known as in variant B, features a modification of the amino acid from V to F at position 123.
+The protein's natural variant, known as in variants C, D and E, features a modification of the amino acid from R to Q at position 131.
+The protein's natural variant, known as in a defective mutant, features a modification of the amino acid from G to D at position 48.
+The natural variant of this protein is characterized by an amino acid alteration from P to L at position 372.
+The protein's natural variant, known as in strain: MCL8544, features a modification of the amino acid from K to R at position 109.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from E to K at position 139.
+The protein's natural variant, known as in MDDGC14; causes protein aggregation;, features a modification of the amino acid from P to S at position 22.
+The protein's natural variant, known as in MDDGC14; the protein remains distributed in the cytoplasm and has no discernable changes compared to wild-type;, features a modification of the amino acid from D to H at position 27.
+The protein's natural variant, known as in MDDGB14; causes protein aggregation;, features a modification of the amino acid from P to L at position 32.
+The protein's natural variant, known as in MDDGC14, features a modification of the amino acid from P to S at position 32.
+The protein's natural variant, known as in MDDGC14;, features a modification of the amino acid from S to C at position 132.
+The protein's natural variant, known as in MDDGB14; the protein remains distributed in the cytoplasm and has no discernable changes compared to wild-type;, features a modification of the amino acid from R to C at position 185.
+The protein's natural variant, known as in MDDGC14;, features a modification of the amino acid from I to T at position 219.
+The protein's natural variant, known as in MDDGC14, features a modification of the amino acid from P to S at position 241.
+The protein's natural variant, known as in MDDGC14;, features a modification of the amino acid from V to M at position 254.
+The protein's natural variant, known as in MDDGB14 and MDDGC14;, features a modification of the amino acid from R to Q at position 287.
+The protein's natural variant, known as in MDDGC14;, features a modification of the amino acid from R to W at position 287.
+The protein's natural variant, known as in MDDGC14; slight reduction in protein abundance;, features a modification of the amino acid from R to W at position 293.
+The protein's natural variant, known as in MDDGC14;, features a modification of the amino acid from V to A at position 318.
+The protein's natural variant, known as in MDDGC14; no change in protein abundance;, features a modification of the amino acid from N to K at position 322.
+The protein's natural variant, known as in MDDGC14; causes protein aggregation;, features a modification of the amino acid from V to I at position 330.
+The protein's natural variant, known as in MDDGA14; causes protein aggregation;, features a modification of the amino acid from D to N at position 334.
+The protein's natural variant, known as in MDDGC14; slight reduction in protein abundance; shows an increased propensity to form punctate aggregates;, features a modification of the amino acid from G to R at position 340.
+The protein's natural variant, known as in MDDGC14; no change in protein abundance; shows an increased propensity to form punctate aggregates;, features a modification of the amino acid from R to H at position 357.
+The protein's natural variant, known as in CDAN1B; unknown pathological significance, features a modification of the amino acid from P to R at position 20.
+The protein's natural variant, known as in CDAN1B;, features a modification of the amino acid from Y to C at position 94.
+The protein's natural variant, known as in CDAN1B; no effect on gene expression and protein level; impaired erythroid cell differentiation; no effect on nuclear and cytoplasmic location;, features a modification of the amino acid from Y to S at position 94.
+The protein's natural variant, known as in CDAN1B; unknown pathological significance, features a modification of the amino acid from L to V at position 136.
+The protein's natural variant, known as in CDAN1B;, features a modification of the amino acid from L to Q at position 178.
+The protein's natural variant, known as in CDAN1B; reduced gene expression and protein level; impaired erythroid cell differentiation; increased S-phase of the cell-cycle; no effect on nuclear and cytoplasmic location, features a modification of the amino acid from H to P at position 230.
+The protein's natural variant, known as in CDAN1B; unknown pathological significance;, features a modification of the amino acid from Y to C at position 236.
+The protein's natural variant, known as in CDAN1B; unknown pathological significance, features a modification of the amino acid from Y to C at position 247.
+The protein's natural variant, known as in CDAN1B; unknown pathological significance, features a modification of the amino acid from I to T at position 273.
+The protein's natural variant, known as in COXPD21; decreased expression at mRNA and protein levels; decreased threonine-tRNA ligase activity; affects both Thr activation and transfer; decreased aminoacyl-tRNA editing activity; decreased protein stability; loss of homodimerization;, features a modification of the amino acid from P to L at position 282.
+The natural variant of this protein is characterized by an amino acid alteration from R to S at position 51.
+The natural variant of this protein is characterized by an amino acid alteration from V to D at position 61.
+The natural variant of this protein is characterized by an amino acid alteration from H to P at position 65.
+The protein's natural variant, known as associated with long-haired phenotype, features a modification of the amino acid from T to P at position 159.
+The protein's natural variant, known as in CMT4B3;, features a modification of the amino acid from M to V at position 418.
+The protein's natural variant, known as in CMT4B3;, features a modification of the amino acid from T to A at position 1565.
+The protein's natural variant, known as in allele B and allele D;, features a modification of the amino acid from M to T at position 148.
+The protein's natural variant, known as in allele D; requires 2 nucleotide substitutions, features a modification of the amino acid from I to A at position 181.
+The protein's natural variant, known as in allele B and allele C, features a modification of the amino acid from I to T at position 181.
+The protein's natural variant, known as in allele D;, features a modification of the amino acid from R to W at position 188.
+The protein's natural variant, known as in strain: Isolate BF-2, features a modification of the amino acid from S to N at position 3.
+The protein's natural variant, known as in SPGF22;, features a modification of the amino acid from N to I at position 64.
+The protein's natural variant, known as identified in warfarin-resistant animals; strongly reduces enzyme activity; abolishes inhibition by warfarin, features a modification of the amino acid from L to Q at position 120.
+The protein's natural variant, known as identified in warfarin-resistant animals; moderately reduces enzyme activity; decreases inhibition by warfarin, features a modification of the amino acid from L to Q at position 128.
+The protein's natural variant, known as identified in warfarin-resistant animals; strongly reduces enzyme activity; abolishes inhibition by warfarin, features a modification of the amino acid from Y to C at position 139.
+The protein's natural variant, known as identified in warfarin-resistant animals; strongly reduces enzyme activity; abolishes inhibition by warfarin, features a modification of the amino acid from Y to F at position 139.
+The protein's natural variant, known as identified in warfarin-resistant animals; strongly reduces enzyme activity; abolishes inhibition by warfarin, features a modification of the amino acid from Y to S at position 139.
+The protein's natural variant, known as in MRT52; no effect on general protein glycosylation;, features a modification of the amino acid from R to Q at position 53.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from T to K at position 380.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from G to S at position 499.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from E to D at position 16.
+The protein's natural variant, known as in SCN2; zero neutrophil count. marked monocytosis and reduced T- and B-lymphocyte number leading to recurrent infectious complications. Abolishes recognition of DNA binding site of zinc finger. Diminished repression activity and elevated ELA2 expression. No effect on repression of CDKN1A/p21 transcription;, features a modification of the amino acid from N to S at position 382.
+The protein's natural variant, known as in NI-CINA; Neutropenic and elevated monocytosis but no history of infectious complications. No effect on DNA binding but diminished GFI1 repression activity;, features a modification of the amino acid from K to R at position 403.
+The natural variant of this protein is characterized by an amino acid alteration from T to A at position 70.
+The natural variant of this protein is characterized by an amino acid alteration from V to M at position 196.
+The natural variant of this protein is characterized by an amino acid alteration from T to N at position 505.
+The natural variant of this protein is characterized by an amino acid alteration from R to Q at position 681.
+The natural variant of this protein is characterized by an amino acid alteration from R to H at position 689.
+The natural variant of this protein is characterized by an amino acid alteration from C to R at position 733.
+The natural variant of this protein is characterized by an amino acid alteration from Q to L at position 1007.
+The protein's natural variant, known as in FTDALS8; unknown pathological significance;, features a modification of the amino acid from P to S at position 229.
+The protein's natural variant, known as in FTDALS8; unknown pathological significance, features a modification of the amino acid from S to F at position 615.
+The protein's natural variant, known as abolished K63-deubiquitinase activity; decreased inhibition of NF-kappa-B; no impact on interaction with TBK1, OPTN and SQSTM, features a modification of the amino acid from D to G at position 681.
+The protein's natural variant, known as in FTDALS8; increased K63-deubiquitinase activity; increased inhibition of NF-kappa-B; no impact on interaction with TBK1, OPTN and SQSTM, features a modification of the amino acid from M to V at position 719.
+The protein's natural variant, known as in MFT1 and BRSS;, features a modification of the amino acid from E to G at position 747.
+The protein's natural variant, known as abolishes lipopolysaccharide binding and causes increased proteolytic degradation of the protein;, features a modification of the amino acid from P to L at position 333.
+The protein's natural variant, known as in strain: Isolate UP22, features a modification of the amino acid from I to V at position 353.
+The protein's natural variant, known as in strain: Isolate UP22, features a modification of the amino acid from G to V at position 360.
+The protein's natural variant, known as loss of response to propionate;, features a modification of the amino acid from R to W at position 174.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation, features a modification of the amino acid from W to R at position 716.
+The protein's natural variant, known as in KAR3-894, features a modification of the amino acid from N to K at position 378.
+The protein's natural variant, known as in KAR3-891, features a modification of the amino acid from S to L at position 462.
+The protein's natural variant, known as in KAR3-893, features a modification of the amino acid from E to D at position 521.
+The protein's natural variant, known as in KAR3-899, features a modification of the amino acid from R to S at position 550.
+The protein's natural variant, known as in KAR3-8912, features a modification of the amino acid from T to A at position 558.
+The protein's natural variant, known as in KAR3-898, features a modification of the amino acid from N to K at position 650.
+The protein's natural variant, known as in KAR3-897, features a modification of the amino acid from V to L at position 659.
+The natural variant of this protein is characterized by an amino acid alteration from S to F at position 78.
+The protein's natural variant, known as in DEE49; unknown pathological significance;, features a modification of the amino acid from D to G at position 541.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from P to T at position 14.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from G to E at position 929.
+The protein's natural variant, known as in strain: JCM 6156 and PB4, features a modification of the amino acid from E to D at position 161.
+The protein's natural variant, known as in strain: JCM 6156 and PB4, features a modification of the amino acid from S to N at position 245.
+The protein's natural variant, known as in strain: JCM 6156, features a modification of the amino acid from E to D at position 249.
+The protein's natural variant, known as in strain: PB4, features a modification of the amino acid from S to N at position 297.
+The protein's natural variant, known as in strain: PB4, features a modification of the amino acid from Y to F at position 358.
+The protein's natural variant, known as in strain: JCM 6156 and PB4, features a modification of the amino acid from S to A at position 360.
+The protein's natural variant, known as in MEHMO; unknown pathological significance;, features a modification of the amino acid from S to R at position 108.
+The protein's natural variant, known as in MEHMO; decreased interaction with the other eIF2 complex subunits EIF2S1 and EIF2S2;, features a modification of the amino acid from I to T at position 222.
+The protein's natural variant, known as in MEHMO; unknown pathological significance;, features a modification of the amino acid from I to M at position 259.
+The protein's natural variant, known as confers resistance to cycloheximide, an inhibitor of polypeptide elongation, features a modification of the amino acid from Q to E at position 38.
+The natural variant of this protein is characterized by an amino acid alteration from Y to H at position 538.
+The protein's natural variant, known as found in patients with symptoms of Parkinson disease; unknown pathological significance; reduced number of cytoplasmic inclusions in cells expressing C-621 compared with cells expressing wild-type (wt) protein when subjected to proteasomal inhibition; C-621 transfected cells are more susceptible to staurosporine-induced cell death than cells expressing wt protein;, features a modification of the amino acid from R to C at position 621.
+The natural variant of this protein is characterized by an amino acid alteration from E to Q at position 706.
+The protein's natural variant, known as found in a patient with Moyamoya disease; unknown pathological significance;, features a modification of the amino acid from H to Q at position 422.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from E to Q at position 696.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from N to S at position 985.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from S to L at position 1060.
+The protein's natural variant, known as found in hard wheats, including cv. Soissons, features a modification of the amino acid from W to R at position 73.
+The protein's natural variant, known as found in hard wheats, including cv. Buster and cv. Shamrock, features a modification of the amino acid from G to S at position 75.
+The protein's natural variant, known as found in cv. Chablis, but no mature PINB protein is found in this cultivar, features a modification of the amino acid from L to P at position 89.
+The protein's natural variant, known as in HEM12-6 and HEM12-12, features a modification of the amino acid from S to F at position 59.
+The protein's natural variant, known as in HEM12-14, features a modification of the amino acid from T to I at position 62.
+The protein's natural variant, known as in HEM12-3 and HEM12-13, features a modification of the amino acid from L to S at position 107.
+The protein's natural variant, known as in HEM12-2 and HEM12-11, features a modification of the amino acid from S to N at position 215.
+The protein's natural variant, known as in haplotype 2, features a modification of the amino acid from T to S at position 155.
+The protein's natural variant, known as in haplotype 2, features a modification of the amino acid from T to A at position 206.
+The protein's natural variant, known as in haplotype 2, features a modification of the amino acid from M to I at position 491.
+The natural variant of this protein is characterized by an amino acid alteration from I to L at position 9.
+The natural variant of this protein is characterized by an amino acid alteration from T to I at position 16.
+The natural variant of this protein is characterized by an amino acid alteration from Q to H at position 41.
+The natural variant of this protein is characterized by an amino acid alteration from T to R at position 59.
+The natural variant of this protein is characterized by an amino acid alteration from Q to H at position 122.
+The protein's natural variant, known as in ATELS2; loss-of-function variant; unable to rescue microcephaly and aberrant craniofacial patterning in zebrafish lacking SMC5; does not relocalize efficiently to sites of laser irradiation-induced DNA damage; no effect on interaction with SLF2, SMC6 and NSMCE2, features a modification of the amino acid from H to D at position 990.
+The protein's natural variant, known as in strain: Isolate HEG86-97, features a modification of the amino acid from I to V at position 156.
+The protein's natural variant, known as in strain: Isolate HEG86-97, features a modification of the amino acid from VLT to ALS at position 240.
+The protein's natural variant, known as in strain: Isolate HEG86-97, features a modification of the amino acid from M to A at position 360.
+The protein's natural variant, known as in a cutaneous metastatic melanoma sample; somatic mutation, features a modification of the amino acid from G to E at position 65.
+The protein's natural variant, known as in a cutaneous metastatic melanoma sample; somatic mutation;, features a modification of the amino acid from G to E at position 134.
+The protein's natural variant, known as in a cutaneous metastatic melanoma sample; somatic mutation;, features a modification of the amino acid from G to E at position 450.
+The protein's natural variant, known as in a cutaneous metastatic melanoma sample; somatic mutation, features a modification of the amino acid from S to F at position 482.
+The protein's natural variant, known as in a cutaneous metastatic melanoma sample; somatic mutation;, features a modification of the amino acid from G to D at position 502.
+The protein's natural variant, known as in HIHGHH; exhibits plasma membrane localization in serum-starved cells and produced inappropriate tonic nuclear exclusion of FOXO1 in preadipocytes;, features a modification of the amino acid from E to K at position 17.
+The protein's natural variant, known as in T2D; associated with typical metabolic dyslipidemia with elevated fastin triglyceride, high VLDL triglyceride/cholesterol ratios, low HDL cholesterol levels and high small dense LDL levels; de novo lipogenesis and liver fat are also significantly elevated in this subject;, features a modification of the amino acid from R to H at position 274.
+The protein's natural variant, known as in strain: Isolate 2, features a modification of the amino acid from T to M at position 237.
+The natural variant of this protein is characterized by an amino acid alteration from Y to I at position 3.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from L to H at position 92.
+The protein's natural variant, known as found in a patient with congenital cataracts, hearing loss, neurodegeneration, neonatal hypotonia and hypoglycemia, pericardial effusion and neurodevelopmental regression after infection; the patient also carries a mutation in SLC33A1; mutant protein does not interact with SOD1;, features a modification of the amino acid from R to W at position 163.
+The protein's natural variant, known as er-1 in strain: cv. Landsberg erecta; round leaves, compact inflorescence, blunt fruits, short and thick siliques and petioles, susceptibility to pathogens such as R.solanacearum, P.irregulare and P.cucumerina, abnormal cell-wall composition and increased canalization of rosette leaf number during long days. In er-101 and er-102, compact inflorescence with short siliques and pedicels, features a modification of the amino acid from I to K at position 750.
+The protein's natural variant, known as in strain: cv. Mt-0, features a modification of the amino acid from V to M at position 886.
+The protein's natural variant, known as found in a patient with infantile spasms and cortical abnormalities; somatic mutation; unknown pathological significance; able to rescue defective Gb3Cer expression in SLC35A2-deficient cells, features a modification of the amino acid from R to L at position 55.
+The protein's natural variant, known as in CDG2M, features a modification of the amino acid from R to P at position 55.
+The protein's natural variant, known as in CDG2M; reduced UDP-galactose transport in patient fibroblasts; no effect on localization to Golgi apparatus, features a modification of the amino acid from V to M at position 71.
+The protein's natural variant, known as in CDG2M; reduced UDP-galactose transport in patient fibroblasts; no effect on localization to Golgi apparatus, features a modification of the amino acid from C to F at position 82.
+The protein's natural variant, known as in CDG2M, features a modification of the amino acid from L to P at position 101.
+The protein's natural variant, known as in CDG2M, features a modification of the amino acid from A to P at position 116.
+The protein's natural variant, known as in CDG2M, features a modification of the amino acid from P to R at position 118.
+The protein's natural variant, known as in CDG2M; loss of UDP-galactose transport in patient fibroblasts; no effect on localization to Golgi apparatus, features a modification of the amino acid from Y to C at position 130.
+The protein's natural variant, known as in CDG2M; no effect on localization to Golgi apparatus, features a modification of the amino acid from L to F at position 175.
+The protein's natural variant, known as in CDG2M; unknown pathological significance, features a modification of the amino acid from G to S at position 188.
+The protein's natural variant, known as in CDG2M; has no effect on localization to Golgi; partially rescues defective Gb3Cer expression in SLC35A2-deficient cells;, features a modification of the amino acid from S to F at position 213.
+The protein's natural variant, known as in CDG2M; reduced UDP-galactose transport in patient fibroblasts; no effect on localization to Golgi apparatus, features a modification of the amino acid from L to P at position 233.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from W to C at position 252.
+The protein's natural variant, known as found in a patient with Rett syndrome-like phenotype; unknown pathological significance; able to rescue defective Gb3Cer expression in SLC35A2-deficient cells;, features a modification of the amino acid from V to M at position 258.
+The protein's natural variant, known as in CDG2M; fails to rescue defective galactosylation in SLC35A2-deficient cells; able to rescue defective Gb3Cer expression in SLC35A2-deficient cells, features a modification of the amino acid from G to V at position 266.
+The protein's natural variant, known as found in a patient with cerebral visual impairment; unknown pathological significance; able to rescue defective Gb3Cer expression in SLC35A2-deficient cells;, features a modification of the amino acid from Y to C at position 267.
+The protein's natural variant, known as in CDG2M; no effect on localization to Golgi apparatus, features a modification of the amino acid from G to D at position 273.
+The protein's natural variant, known as found in a patient with West syndrome; unknown pathological significance; does not rescue defective Gb3Cer expression in SLC35A2-deficient cells;, features a modification of the amino acid from G to R at position 282.
+The protein's natural variant, known as in CDG2M, features a modification of the amino acid from L to P at position 303.
+The protein's natural variant, known as found in a patient with non-lesional focal epilepsy; somatic mutation; unknown pathological significance; able to rescue defective Gb3Cer expression in SLC35A2-deficient cells, features a modification of the amino acid from S to P at position 304.
+The protein's natural variant, known as in CDG2M, features a modification of the amino acid from S to Y at position 312.
+The protein's natural variant, known as in CDG2M; reduced UDP-galactose transport in patient fibroblasts; no effect on localization to Golgi apparatus, features a modification of the amino acid from L to P at position 315.
+The protein's natural variant, known as in CDG2M; in patient fibroblasts, results in reduced UDP-galactose transport into the Golgi; able to rescue defective Gb3Cer expression in SLC35A2-deficient cells;, features a modification of the amino acid from V to I at position 331.
+The protein's natural variant, known as reduced sensitivity to quinine, features a modification of the amino acid from C to R at position 72.
+The natural variant of this protein is characterized by an amino acid alteration from C to S at position 72.
+The natural variant of this protein is characterized by an amino acid alteration from M to I at position 74.
+The natural variant of this protein is characterized by an amino acid alteration from N to E at position 75.
+The natural variant of this protein is characterized by an amino acid alteration from N to K at position 75.
+The protein's natural variant, known as reduced sensitivity to quinine, features a modification of the amino acid from K to I at position 76.
+The protein's natural variant, known as reduced sensitivity to quinine, features a modification of the amino acid from K to N at position 76.
+The protein's natural variant, known as in chloroquine resistance type 1; associated with S-220 and in chloroquine resistance type 2; associated with T-144, Y-160 and D-326; reduced sensitivity to drugs, features a modification of the amino acid from K to T at position 76.
+The natural variant of this protein is characterized by an amino acid alteration from H to Q at position 97.
+The natural variant of this protein is characterized by an amino acid alteration from H to R at position 123.
+The protein's natural variant, known as in chloroquine resistance type 2; associated with T-76, Y-160 and D-326, features a modification of the amino acid from A to T at position 144.
+The natural variant of this protein is characterized by an amino acid alteration from T to A at position 152.
+The protein's natural variant, known as in chloroquine resistance type 2; associated with T-76, T-144 and D-326, features a modification of the amino acid from L to Y at position 160.
+The protein's natural variant, known as may repel chloroquine from moving through the channel, leading to higher chloroquine accumulation at its site of action, features a modification of the amino acid from S to R at position 163.
+The natural variant of this protein is characterized by an amino acid alteration from T to A at position 205.
+The protein's natural variant, known as in chloroquine resistance type 1; associated with T-76, features a modification of the amino acid from A to S at position 220.
+The natural variant of this protein is characterized by an amino acid alteration from Q to E at position 271.
+The natural variant of this protein is characterized by an amino acid alteration from P to L at position 275.
+The protein's natural variant, known as in chloroquine resistance type 2; associated with T-76, T-144 and Y-160, features a modification of the amino acid from N to D at position 326.
+The natural variant of this protein is characterized by an amino acid alteration from N to S at position 326.
+The natural variant of this protein is characterized by an amino acid alteration from T to S at position 333.
+The natural variant of this protein is characterized by an amino acid alteration from S to N at position 334.
+The protein's natural variant, known as reduced sensitivity to quinine, features a modification of the amino acid from Q to K at position 352.
+The protein's natural variant, known as reduced sensitivity to quinine, features a modification of the amino acid from Q to R at position 352.
+The natural variant of this protein is characterized by an amino acid alteration from I to L at position 356.
+The natural variant of this protein is characterized by an amino acid alteration from I to T at position 356.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 356.
+The natural variant of this protein is characterized by an amino acid alteration from R to I at position 371.
+The natural variant of this protein is characterized by an amino acid alteration from R to T at position 371.
+The protein's natural variant, known as in EKVP2;, features a modification of the amino acid from G to D at position 12.
+The protein's natural variant, known as in EKVP2;, features a modification of the amino acid from R to H at position 22.
+The protein's natural variant, known as in EKVP2;, features a modification of the amino acid from T to P at position 85.
+The protein's natural variant, known as in EKVP2;, features a modification of the amino acid from F to L at position 137.
+The protein's natural variant, known as in EKVP2;, features a modification of the amino acid from F to Y at position 189.
+The protein's natural variant, known as in Ogura, male-sterile line, features a modification of the amino acid from I to L at position 124.
+The protein's natural variant, known as in LDS3;, features a modification of the amino acid from A to V at position 112.
+The protein's natural variant, known as in LDS3;, features a modification of the amino acid from E to K at position 239.
+The protein's natural variant, known as in LDS3;, features a modification of the amino acid from T to I at position 261.
+The protein's natural variant, known as in LDS3;, features a modification of the amino acid from R to K at position 279.
+The protein's natural variant, known as in LDS3;, features a modification of the amino acid from R to W at position 287.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from P to L at position 393.
+The natural variant of this protein is characterized by an amino acid alteration from D to Y at position 242.
+The natural variant of this protein is characterized by an amino acid alteration from L to P at position 243.
+The protein's natural variant, known as found in a clear cell renal carcinoma case; somatic mutation, features a modification of the amino acid from T to N at position 314.
+The protein's natural variant, known as in strain: EH15, features a modification of the amino acid from L to I at position 21.
+The protein's natural variant, known as in strain: EH15, features a modification of the amino acid from E to Q at position 52.
+The protein's natural variant, known as in strain: EH15, features a modification of the amino acid from L to H at position 147.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from S to I at position 33.
+The protein's natural variant, known as in SBM, features a modification of the amino acid from S to F at position 39.
+The protein's natural variant, known as in MFM3 and MFM3, features a modification of the amino acid from S to F at position 55.
+The protein's natural variant, known as in MFM3; does not abolish interaction with ACTN1;, features a modification of the amino acid from T to I at position 57.
+The protein's natural variant, known as in MFM3, features a modification of the amino acid from S to C at position 60.
+The protein's natural variant, known as in MFM3, features a modification of the amino acid from S to F at position 60.
+The protein's natural variant, known as in MFM3, features a modification of the amino acid from S to I at position 95.
+The natural variant of this protein is characterized by an amino acid alteration from G to S at position 174.
+The natural variant of this protein is characterized by an amino acid alteration from G to S at position 233.
+The natural variant of this protein is characterized by an amino acid alteration from S to G at position 299.
+The protein's natural variant, known as in the pyrimethamine-resistant isolates BUR-98 and BUR-151; interferes with inhibitor binding, features a modification of the amino acid from S to R at position 58.
+The protein's natural variant, known as in the pyrimethamine-resistant isolates BUR-98 and BUR-151, features a modification of the amino acid from S to N at position 117.
+The protein's natural variant, known as in SHFM1D;, features a modification of the amino acid from Q to P at position 178.
+The protein's natural variant, known as in strain: Charolais, Holstein and Limousin, features a modification of the amino acid from A to S at position 127.
+The protein's natural variant, known as in strain: Charolais and Limousin, features a modification of the amino acid from W to S at position 153.
+The protein's natural variant, known as in strain: Charolais, Holstein and Limousin, features a modification of the amino acid from R to W at position 262.
+The protein's natural variant, known as in strain: Charolais, features a modification of the amino acid from D to Y at position 358.
+The protein's natural variant, known as in strain: Limousin, features a modification of the amino acid from T to M at position 373.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from E to K at position 104.
+The protein's natural variant, known as in MRD45; unknown pathological significance;, features a modification of the amino acid from R to W at position 492.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from A to T at position 652.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from C to Y at position 74.
+The protein's natural variant, known as in BFNS1;, features a modification of the amino acid from T to A at position 114.
+The protein's natural variant, known as in BFNS1; with infantile seizures;, features a modification of the amino acid from Y to D at position 154.
+The protein's natural variant, known as in BFNS1;, features a modification of the amino acid from G to E at position 159.
+The protein's natural variant, known as in BFNS1;, features a modification of the amino acid from G to R at position 159.
+The protein's natural variant, known as in BFNS1; with infantile seizures;, features a modification of the amino acid from A to V at position 196.
+The protein's natural variant, known as in DEE7; gain-of-function mutation; results in loss of voltage-dependent channel gating and highly increased potassium currents;, features a modification of the amino acid from R to C at position 201.
+The protein's natural variant, known as found in a patient with isolated myokymia; leads to a shift of voltage-dependent activation;, features a modification of the amino acid from R to Q at position 207.
+The protein's natural variant, known as in BFNS1; phenotype manifestations include myokymia in some patients; leads to a shift of voltage-dependent activation of the channel and a dramatic slowing of activation upon depolarization;, features a modification of the amino acid from R to W at position 207.
+The protein's natural variant, known as in BFNS1; minor effect on maximal current but clearly exhibits a faster rate of deactivation;, features a modification of the amino acid from M to V at position 208.
+The protein's natural variant, known as in DEE7;, features a modification of the amino acid from R to C at position 210.
+The protein's natural variant, known as in BFNS1 and DEE7;, features a modification of the amino acid from R to Q at position 213.
+The protein's natural variant, known as in BFNS1; unknown pathological significance;, features a modification of the amino acid from R to W at position 213.
+The protein's natural variant, known as in BFNS1;, features a modification of the amino acid from R to W at position 214.
+The protein's natural variant, known as in BFNS1; also in patients with infantile seizures;, features a modification of the amino acid from T to A at position 217.
+The protein's natural variant, known as in BFNS1;, features a modification of the amino acid from H to Q at position 228.
+The protein's natural variant, known as in DEE7;, features a modification of the amino acid from T to P at position 234.
+The protein's natural variant, known as in BFNS1;, features a modification of the amino acid from L to F at position 243.
+The protein's natural variant, known as in DEE7; reduces channel currents by more than 50% in homomeric channels;, features a modification of the amino acid from S to W at position 247.
+The protein's natural variant, known as in DEE7; patient also manifests dyskinesia;, features a modification of the amino acid from D to E at position 266.
+The protein's natural variant, known as in DEE7;, features a modification of the amino acid from L to F at position 268.
+The protein's natural variant, known as in DEE7;, features a modification of the amino acid from T to I at position 276.
+The protein's natural variant, known as in BFNS1; 30%-60% reduction of wt current in heteromeric channels;, features a modification of the amino acid from Y to C at position 284.
+The protein's natural variant, known as in DEE7;, features a modification of the amino acid from R to S at position 291.
+The protein's natural variant, known as in DEE7;, features a modification of the amino acid from A to V at position 294.
+The protein's natural variant, known as in DEE7;, features a modification of the amino acid from G to S at position 301.
+The protein's natural variant, known as in BFNS1 and DEE7; 20%-40% reduction of wt current in heteromeric channels;, features a modification of the amino acid from A to T at position 306.
+The protein's natural variant, known as in BFNS1; moderate effect; less than 50% reduction in current compared with wt heteromeric channels;, features a modification of the amino acid from R to Q at position 333.
+The protein's natural variant, known as in BFNS1;, features a modification of the amino acid from R to G at position 353.
+The protein's natural variant, known as in BFNS1;, features a modification of the amino acid from S to F at position 358.
+The protein's natural variant, known as in BFNS1;, features a modification of the amino acid from R to W at position 547.
+The protein's natural variant, known as in BFNS1 and DEE7; decreases the voltage-dependence of the channel;, features a modification of the amino acid from K to N at position 554.
+The protein's natural variant, known as in DEE7, features a modification of the amino acid from P to S at position 561.
+The protein's natural variant, known as in DEE7;, features a modification of the amino acid from ML to IM at position 579.
+The protein's natural variant, known as in BFNS1;, features a modification of the amino acid from M to V at position 578.
+The protein's natural variant, known as in DEE7;, features a modification of the amino acid from R to Q at position 581.
+The protein's natural variant, known as in BFNS1;, features a modification of the amino acid from R to S at position 588.
+The protein's natural variant, known as in BFNS1;, features a modification of the amino acid from L to R at position 637.
+The protein's natural variant, known as found in a patient with continuous spikes and waves during sleep; unknown pathological significance;, features a modification of the amino acid from P to S at position 777.
+The protein's natural variant, known as in SCDO4;, features a modification of the amino acid from R to W at position 25.
+The protein's natural variant, known as in SCDO4;, features a modification of the amino acid from I to V at position 58.
+The protein's natural variant, known as in SCDO4;, features a modification of the amino acid from D to Y at position 186.
+The protein's natural variant, known as in LEPD; no effect on secretion; does not bind or activate LEPR;, features a modification of the amino acid from D to Y at position 100.
+The protein's natural variant, known as in LEPD;, features a modification of the amino acid from R to W at position 105.
+The protein's natural variant, known as in SK636, temperature-sensitive, features a modification of the amino acid from W to R at position 25.
+The protein's natural variant, known as in SK634, temperature-sensitive, features a modification of the amino acid from G to S at position 104.
+The protein's natural variant, known as in SK635, temperature-sensitive, features a modification of the amino acid from L to F at position 139.
+The protein's natural variant, known as in ECYT8;, features a modification of the amino acid from R to Q at position 62.
+The protein's natural variant, known as in ECYT8; mutation identified at protein level; marked decrease in synthase and mutase activities; no effect on phosphatase activity;, features a modification of the amino acid from R to C at position 90.
+The protein's natural variant, known as in CDLS4;, features a modification of the amino acid from P to R at position 376.
+The protein's natural variant, known as found in a radiation-sensitive cancer patient;, features a modification of the amino acid from G to R at position 481.
+The protein's natural variant, known as in CDLS4;, features a modification of the amino acid from C to R at position 585.
+The protein's natural variant, known as in MGS; causes delayed food transit along the gut, when tested in zebrafish; may affect RUNX1 and APOB expression;, features a modification of the amino acid from A to T at position 622.
+The protein's natural variant, known as in MGORS1;, features a modification of the amino acid from F to S at position 89.
+The protein's natural variant, known as in MGORS1;, features a modification of the amino acid from R to Q at position 105.
+The protein's natural variant, known as in MGORS1;, features a modification of the amino acid from E to G at position 127.
+The protein's natural variant, known as in MGORS1;, features a modification of the amino acid from R to W at position 666.
+The protein's natural variant, known as in MGORS1;, features a modification of the amino acid from R to Q at position 720.
+The natural variant of this protein is characterized by an amino acid alteration from D to E at position 17.
+The protein's natural variant, known as in Ly-6I.1, features a modification of the amino acid from A to E at position 6.
+The protein's natural variant, known as in Ly-6I.1, features a modification of the amino acid from K to R at position 68.
+The protein's natural variant, known as found in an esophageal cancer sample; esophageal squamous cell carcinoma; somatic mutation;, features a modification of the amino acid from S to P at position 29.
+The protein's natural variant, known as found in an esophageal cancer sample; esophageal squamous cell carcinoma; somatic mutation;, features a modification of the amino acid from K to E at position 119.
+The protein's natural variant, known as in BBS7;, features a modification of the amino acid from G to R at position 63.
+The protein's natural variant, known as in BBS7;, features a modification of the amino acid from I to F at position 66.
+The protein's natural variant, known as in BBS7;, features a modification of the amino acid from T to I at position 211.
+The protein's natural variant, known as found in a patient with Bardet-Biedl syndrome also carrying a frameshift mutation in BBS10 and variant R-834 in KIF7;, features a modification of the amino acid from Q to P at position 293.
+The protein's natural variant, known as in BBS7;, features a modification of the amino acid from H to R at position 323.
+The protein's natural variant, known as in a patient with Meckel-Gruber like syndrome also carrying Y-60 in TTC21B;, features a modification of the amino acid from Y to C at position 671.
+The protein's natural variant, known as in strain: Isolate KIZ211013, features a modification of the amino acid from S to A at position 57.
+The natural variant of this protein is characterized by an amino acid alteration from D to V at position 463.
+The protein's natural variant, known as in strain: BALB/c, features a modification of the amino acid from D to V at position 183.
+The protein's natural variant, known as in strain: BALB/c; loss of NK1.1 reactivity, features a modification of the amino acid from S to T at position 191.
+The protein's natural variant, known as in TGCT; somatic mutation;, features a modification of the amino acid from K to E at position 277.
+The protein's natural variant, known as in AHC; impairs transcriptional silencing of the StAR promoter;, features a modification of the amino acid from R to P at position 267.
+The protein's natural variant, known as in AHC, features a modification of the amino acid from L to P at position 278.
+The protein's natural variant, known as in AHC; the patient presents an inappropriate tall stature and renal ectopy, features a modification of the amino acid from V to G at position 287.
+The protein's natural variant, known as in AHC;, features a modification of the amino acid from W to C at position 291.
+The protein's natural variant, known as in AHC, features a modification of the amino acid from L to P at position 295.
+The protein's natural variant, known as in AHC; results in a severe loss of repressor activity;, features a modification of the amino acid from L to P at position 297.
+The protein's natural variant, known as in AHC, features a modification of the amino acid from A to P at position 300.
+The protein's natural variant, known as in AHC, features a modification of the amino acid from A to V at position 300.
+The protein's natural variant, known as in AHC, features a modification of the amino acid from E to K at position 377.
+The protein's natural variant, known as in AHC;, features a modification of the amino acid from Y to D at position 380.
+The protein's natural variant, known as in AHC;, features a modification of the amino acid from L to H at position 381.
+The protein's natural variant, known as in AHC;, features a modification of the amino acid from K to N at position 382.
+The protein's natural variant, known as in AHC, features a modification of the amino acid from V to G at position 385.
+The protein's natural variant, known as in AHC, features a modification of the amino acid from R to G at position 425.
+The protein's natural variant, known as in AHC, features a modification of the amino acid from R to T at position 425.
+The protein's natural variant, known as in AHC; mild phenotype;, features a modification of the amino acid from I to S at position 439.
+The protein's natural variant, known as in AHC; impairs RNA-binding activity;, features a modification of the amino acid from N to I at position 440.
+The protein's natural variant, known as in AHC, features a modification of the amino acid from L to R at position 466.
+The protein's natural variant, known as found in a patient with bilateral asymmetric microphthalmia, cataract and nystagmus; unknown pathological significance;, features a modification of the amino acid from T to A at position 165.
+The protein's natural variant, known as in VRJS; loss of function mutation; results in altered dosage of different PUF60 protein forms and abnormal splicing profile of several target genes;, features a modification of the amino acid from H to Y at position 169.
+The protein's natural variant, known as associated with the dilute coat color phenotype, features a modification of the amino acid from LRRKEEERLGGLKDRIKKESSQRELLSDAAHLNETHCARCLQPYRLLVAPKRQCLDCHLFTCQDCSHAHPEEEGWLCDPCHLARVVKMGSLEWYYGHLRARFKRFGSAKVIRSLCGRLQGGGGPEPSPGEGSGDSEQTEEDGELDTVAQAQPLGSKKKRLSIHGLDFDADSDGSTQSSGHPPYLSPVPMATDSLQTLTGEPRAKDTSQEAVVLEEADVGAPGCHPHPEEQTDSLSAARQDTLTEPRFPRQSCTTALGLAVTPGPGVISSSERLSSRYPADEGTSDDEDTGADGVASQSLTWRDCAPAESQHLTGHQPTDADREEETLKRKLEEMTSHISDQGASSEEEGSKEEEAGLNRKTSIEDLPGAAPEVLVASGQTSRQETSPRGPQELMQPGRTTDQELLELEDRVAVTASEVQQVESEVSNIKSKIAALQAAGLSVRPSGKPQRRSNLPIFLPRLVGRLGQTPKDPNAEPSDEVKVMTAPYLLRRKFSNPPKSQDKAGDSFDRQSAYRGSLTQRNPNSRKGVANHSFAKPVMTQRP to REGKKRKGWGD at position 569.
+The natural variant of this protein is characterized by an amino acid alteration from S to G at position 205.
+The natural variant of this protein is characterized by an amino acid alteration from T to A at position 223.
+The natural variant of this protein is characterized by an amino acid alteration from P to S at position 228.
+The natural variant of this protein is characterized by an amino acid alteration from C to F at position 250.
+The natural variant of this protein is characterized by an amino acid alteration from C to L at position 250.
+The natural variant of this protein is characterized by an amino acid alteration from C to R at position 250.
+The natural variant of this protein is characterized by an amino acid alteration from S to A at position 404.
+The protein's natural variant, known as in FASPS1; reduced in vitro phosphorylation by CSNK1E;, features a modification of the amino acid from S to G at position 662.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from L to V at position 823.
+The protein's natural variant, known as frequency in Caucasians 0.004 and in African-Americans 0.05; 40% increase in agonist-promoted Gi coupling;, features a modification of the amino acid from N to K at position 266.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from D to A at position 278.
+The protein's natural variant, known as in CDG2F; results in decreased CMP-sialic acid transmembrane transporter activity when expressed in a heterologous system; does not affect localization to Golgi apparatus, features a modification of the amino acid from Q to H at position 101.
+The protein's natural variant, known as in CDG2F, features a modification of the amino acid from T to R at position 156.
+The protein's natural variant, known as in CDG2F, features a modification of the amino acid from E to K at position 196.
+The natural variant of this protein is characterized by an amino acid alteration from S to G at position 232.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 234.
+The protein's natural variant, known as in NBIA7; primary fibroblasts from patients, who are compound heterozygous with E-113, show much higher intracellular iron content than fibroblasts from control individuals and abnormally elevated levels of transferrin receptor 1/TFRC at the cell surface;, features a modification of the amino acid from V to L at position 78.
+The protein's natural variant, known as in NBIA7; primary fibroblasts from patients, who are compound heterozygous with L-78, show much higher intracellular iron content than fibroblasts from control individuals and abnormally elevated levels of transferrin receptor 1/TFRC at the cell surface;, features a modification of the amino acid from A to E at position 113.
+The protein's natural variant, known as in UVM1; loss of DNAN-glycosylase activity, features a modification of the amino acid from R to W at position 468.
+The protein's natural variant, known as may be associated with PARK11;, features a modification of the amino acid from N to S at position 56.
+The protein's natural variant, known as in PARK11;, features a modification of the amino acid from T to A at position 112.
+The protein's natural variant, known as in PARK11; unknown pathological significance, features a modification of the amino acid from E to K at position 256.
+The protein's natural variant, known as in PARK11; unknown pathological significance;, features a modification of the amino acid from S to C at position 273.
+The protein's natural variant, known as in PARK11;, features a modification of the amino acid from I to V at position 278.
+The protein's natural variant, known as in PARK11;, features a modification of the amino acid from S to T at position 335.
+The protein's natural variant, known as in PARK11; unknown pathological significance, features a modification of the amino acid from A to V at position 345.
+The protein's natural variant, known as in PARK11; unknown pathological significance;, features a modification of the amino acid from D to E at position 349.
+The protein's natural variant, known as in PARK11; unknown pathological significance, features a modification of the amino acid from S to Y at position 377.
+The protein's natural variant, known as in PARK11; unknown pathological significance;, features a modification of the amino acid from N to T at position 457.
+The protein's natural variant, known as in PARK11; unknown pathological significance;, features a modification of the amino acid from P to S at position 473.
+The protein's natural variant, known as in PARK11; unknown pathological significance, features a modification of the amino acid from E to K at position 492.
+The protein's natural variant, known as in PARK11; unknown pathological significance, features a modification of the amino acid from H to Y at position 519.
+The protein's natural variant, known as in PARK11; unknown pathological significance, features a modification of the amino acid from L to F at position 580.
+The protein's natural variant, known as in PARK11, features a modification of the amino acid from R to G at position 589.
+The protein's natural variant, known as in PARK11;, features a modification of the amino acid from D to E at position 606.
+The protein's natural variant, known as in PARK11; unknown pathological significance, features a modification of the amino acid from D to H at position 1070.
+The protein's natural variant, known as in PARK11; unknown pathological significance;, features a modification of the amino acid from L to P at position 1209.
+The natural variant of this protein is characterized by an amino acid alteration from Q to QQ at position 1212.
+The protein's natural variant, known as in PARK11;, features a modification of the amino acid from V to I at position 1242.
+The protein's natural variant, known as in strain: cv. Ita-0, features a modification of the amino acid from K to N at position 135.
+The protein's natural variant, known as in strain: L2 and E/UW-5/Cx, features a modification of the amino acid from H to R at position 593.
+The protein's natural variant, known as in strain: Czech II, features a modification of the amino acid from L to P at position 46.
+The protein's natural variant, known as in strain: Czech II, features a modification of the amino acid from P to H at position 90.
+The protein's natural variant, known as in strain: Czech II, features a modification of the amino acid from A to G at position 114.
+The protein's natural variant, known as in strain: Czech II, features a modification of the amino acid from V to E at position 150.
+The protein's natural variant, known as in strain: Czech II, features a modification of the amino acid from C to R at position 220.
+The protein's natural variant, known as in strain: Czech II, features a modification of the amino acid from D to G at position 256.
+The protein's natural variant, known as in strain: Czech II, features a modification of the amino acid from C to R at position 287.
+The protein's natural variant, known as in strain: Czech II, features a modification of the amino acid from V to A at position 325.
+The protein's natural variant, known as in strain: Czech II, features a modification of the amino acid from R to K at position 556.
+The protein's natural variant, known as in strain: Czech II, features a modification of the amino acid from K to E at position 585.
+The natural variant of this protein is characterized by an amino acid alteration from P to L at position 135.
+The natural variant of this protein is characterized by an amino acid alteration from D to E at position 15.
+The protein's natural variant, known as in isozyme [Thr37]PLA2, features a modification of the amino acid from K to T at position 53.
+The natural variant of this protein is characterized by an amino acid alteration from F to S at position 7.
+The natural variant of this protein is characterized by an amino acid alteration from L to F at position 306.
+The natural variant of this protein is characterized by an amino acid alteration from H to Y at position 345.
+The natural variant of this protein is characterized by an amino acid alteration from I to T at position 348.
+The protein's natural variant, known as in alpha-R, features a modification of the amino acid from T to S at position 8.
+The protein's natural variant, known as in alpha-R, features a modification of the amino acid from V to I at position 55.
+The protein's natural variant, known as in alpha-Q, features a modification of the amino acid from G to D at position 71.
+The protein's natural variant, known as in alpha-R and alpha-T, features a modification of the amino acid from Q to H at position 78.
+The protein's natural variant, known as in MGORS5;, features a modification of the amino acid from T to R at position 323.
+The protein's natural variant, known as in NS1;, features a modification of the amino acid from T to I at position 2.
+The protein's natural variant, known as in NS1;, features a modification of the amino acid from T to A at position 42.
+The protein's natural variant, known as in NS1;, features a modification of the amino acid from N to K at position 58.
+The protein's natural variant, known as in NS1;, features a modification of the amino acid from T to A at position 59.
+The protein's natural variant, known as in NS1;, features a modification of the amino acid from G to A at position 60.
+The protein's natural variant, known as in myelodysplastic syndrome;, features a modification of the amino acid from G to V at position 60.
+The protein's natural variant, known as in NS1;, features a modification of the amino acid from D to G at position 61.
+The protein's natural variant, known as in NS1;, features a modification of the amino acid from D to N at position 61.
+The protein's natural variant, known as in JMML; also in myelodysplastic syndrome;, features a modification of the amino acid from D to V at position 61.
+The protein's natural variant, known as in JMML;, features a modification of the amino acid from D to Y at position 61.
+The protein's natural variant, known as in NS1; also in Noonan patients manifesting juvenile myelomonocytic leukemia;, features a modification of the amino acid from Y to D at position 62.
+The protein's natural variant, known as in NS1;, features a modification of the amino acid from Y to C at position 63.
+The protein's natural variant, known as in JMML; also in myelodysplastic syndrome;, features a modification of the amino acid from E to K at position 69.
+The protein's natural variant, known as in NS1;, features a modification of the amino acid from E to Q at position 69.
+The protein's natural variant, known as in acute myeloid leukemia; requires 2 nucleotide substitutions, features a modification of the amino acid from F to K at position 71.
+The protein's natural variant, known as in NS1; also found in myelodysplastic syndrome;, features a modification of the amino acid from F to L at position 71.
+The protein's natural variant, known as in NS1;, features a modification of the amino acid from A to G at position 72.
+The protein's natural variant, known as in NS1;, features a modification of the amino acid from A to S at position 72.
+The protein's natural variant, known as in JMML;, features a modification of the amino acid from A to T at position 72.
+The protein's natural variant, known as in JMML;, features a modification of the amino acid from A to V at position 72.
+The protein's natural variant, known as in NS1; also in Noonan patients manifesting juvenile myelomonocytic leukemia;, features a modification of the amino acid from T to I at position 73.
+The protein's natural variant, known as in JMML; also in myelodysplastic syndrome;, features a modification of the amino acid from E to A at position 76.
+The protein's natural variant, known as in NS1;, features a modification of the amino acid from E to D at position 76.
+The protein's natural variant, known as in JMML;, features a modification of the amino acid from E to G at position 76.
+The protein's natural variant, known as in JMML; increases protein tyrosine phosphatase activity against CDC73;, features a modification of the amino acid from E to K at position 76.
+The protein's natural variant, known as in JMML;, features a modification of the amino acid from E to V at position 76.
+The protein's natural variant, known as in NS1, features a modification of the amino acid from Q to P at position 79.
+The protein's natural variant, known as in NS1;, features a modification of the amino acid from Q to R at position 79.
+The protein's natural variant, known as in NS1;, features a modification of the amino acid from D to A at position 106.
+The protein's natural variant, known as in NS1;, features a modification of the amino acid from E to D at position 139.
+The protein's natural variant, known as in NS1;, features a modification of the amino acid from Q to R at position 256.
+The protein's natural variant, known as in NS1; increases MAPK signaling; increases protein tyrosine phosphatase activity; changed substrate selectivity for GAB1;, features a modification of the amino acid from L to F at position 261.
+The protein's natural variant, known as in NS1; increases MAPK signaling; increased protein tyrosine phosphatase activity;, features a modification of the amino acid from L to H at position 261.
+The protein's natural variant, known as in NS1; increases MAPK signaling; increased protein tyrosine phosphatase activity, features a modification of the amino acid from L to F at position 262.
+The protein's natural variant, known as in NS1; increases MAPK signaling; increased protein tyrosine phosphatase activity;, features a modification of the amino acid from L to R at position 262.
+The protein's natural variant, known as in NS1; increases MAPK signaling; increased protein tyrosine phosphatase activity;, features a modification of the amino acid from R to Q at position 265.
+The protein's natural variant, known as in NS1 and LPRD1; does not affect subcellular location; decreases protein tyrosine phosphatase activity against CDC73;, features a modification of the amino acid from Y to C at position 279.
+The protein's natural variant, known as in LPRD1;, features a modification of the amino acid from Y to S at position 279.
+The protein's natural variant, known as in NS1;, features a modification of the amino acid from I to V at position 282.
+The protein's natural variant, known as in NS1;, features a modification of the amino acid from F to L at position 285.
+The protein's natural variant, known as in NS1;, features a modification of the amino acid from F to S at position 285.
+The protein's natural variant, known as in NS1; common mutation;, features a modification of the amino acid from N to D at position 308.
+The protein's natural variant, known as in NS1; some patients also manifest giant cell lesions of bone and soft tissue;, features a modification of the amino acid from N to S at position 308.
+The protein's natural variant, known as in NS1; unknown pathological significance;, features a modification of the amino acid from I to V at position 309.
+The protein's natural variant, known as in NS1;, features a modification of the amino acid from T to M at position 411.
+The protein's natural variant, known as in LPRD1;, features a modification of the amino acid from A to T at position 461.
+The protein's natural variant, known as in LPRD1;, features a modification of the amino acid from G to A at position 464.
+The protein's natural variant, known as in LPRD1; does not affect subcellular location; decreases protein tyrosine phosphatase activity against CDC73;, features a modification of the amino acid from T to M at position 468.
+The protein's natural variant, known as in NS1; increased phosphatase activity;, features a modification of the amino acid from P to S at position 491.
+The protein's natural variant, known as in LPRD1;, features a modification of the amino acid from R to L at position 498.
+The protein's natural variant, known as in LPRD1; reduced phosphatase activity;, features a modification of the amino acid from R to W at position 498.
+The protein's natural variant, known as in NS1;, features a modification of the amino acid from R to K at position 501.
+The protein's natural variant, known as in NS1;, features a modification of the amino acid from S to T at position 502.
+The protein's natural variant, known as in JMML;, features a modification of the amino acid from G to A at position 503.
+The protein's natural variant, known as in NS1 and JMML; JMML patient also shows growth retardation and pulmonic stenosis;, features a modification of the amino acid from G to R at position 503.
+The protein's natural variant, known as in NS1;, features a modification of the amino acid from M to V at position 504.
+The protein's natural variant, known as in LPRD1; does not affect subcellular location; decreases protein tyrosine phosphatase activity against CDC73;, features a modification of the amino acid from Q to P at position 506.
+The protein's natural variant, known as in NS1, features a modification of the amino acid from Q to R at position 506.
+The protein's natural variant, known as in NS1 and LPRD1; does not affect subcellular location; decreases protein tyrosine phosphatase activity against CDC73;, features a modification of the amino acid from Q to E at position 510.
+The protein's natural variant, known as in LPRD1;, features a modification of the amino acid from Q to P at position 510.
+The protein's natural variant, known as in NS1; unknown pathological significance;, features a modification of the amino acid from L to F at position 560.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from Q to R at position 221.
+The protein's natural variant, known as in DKCB2;, features a modification of the amino acid from V to M at position 126.
+The protein's natural variant, known as in DKCB2;, features a modification of the amino acid from Y to H at position 139.
+The natural variant of this protein is characterized by an amino acid alteration from A to V at position 464.
+The natural variant of this protein is characterized by an amino acid alteration from A to S at position 554.
+The natural variant of this protein is characterized by an amino acid alteration from A to T at position 559.
+The natural variant of this protein is characterized by an amino acid alteration from V to A at position 572.
+The protein's natural variant, known as in MMDS6; exhibits temperature-sensitive defect in presequence processing activity, when tested in yeast;, features a modification of the amino acid from R to C at position 175.
+The protein's natural variant, known as in MMDS6; exhibits temperature-sensitive defect in presequence processing activity, when tested in yeast;, features a modification of the amino acid from R to H at position 175.
+The protein's natural variant, known as in MMDS6; exhibits temperature-sensitive defect in presequence processing activity, when tested in yeast;, features a modification of the amino acid from V to G at position 177.
+The protein's natural variant, known as in MMDS6; exhibits temperature-sensitive defect in presequence processing activity, when tested in yeast;, features a modification of the amino acid from A to P at position 201.
+The protein's natural variant, known as in MMDS6; small decrease in protein level; impaired frataxin/FXN processing, leading to the accumulation of an intermediate form, called iFXN;, features a modification of the amino acid from I to T at position 422.
+The protein's natural variant, known as in LCA16, features a modification of the amino acid from Q to R at position 117.
+The protein's natural variant, known as found in a patient with autosomal recessive retinitis pigmentosa;, features a modification of the amino acid from R to Q at position 162.
+The protein's natural variant, known as in SVD; overexpression produces a non-selective cation current that depolarizes transfected cells and increases their fragility;, features a modification of the amino acid from R to W at position 162.
+The protein's natural variant, known as in LCA16;, features a modification of the amino acid from L to P at position 241.
+The protein's natural variant, known as found in a patient with autosomal recessive retinitis pigmentosa;, features a modification of the amino acid from E to A at position 276.
+The protein's natural variant, known as in plasmid pYVa127/90, features a modification of the amino acid from K to E at position 15.
+The protein's natural variant, known as in plasmid pYVa127/90, features a modification of the amino acid from T to A at position 37.
+The protein's natural variant, known as in plasmid pYVa127/90, features a modification of the amino acid from H to Y at position 120.
+The protein's natural variant, known as in DBA5; may result in aberrant splicing;, features a modification of the amino acid from V to I at position 33.
+The protein's natural variant, known as in ENFL4; markedly increases receptor sensitivity to acetylcholine;, features a modification of the amino acid from I to N at position 279.
+The protein's natural variant, known as in BFIS6; unknown pathological significance;, features a modification of the amino acid from R to W at position 376.
+The protein's natural variant, known as de novo variant found in a patient with intellectual disability;, features a modification of the amino acid from R to H at position 296.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from R to W at position 40.
+The protein's natural variant, known as in an ovarian serous carcinoma sample; somatic mutation, features a modification of the amino acid from G to S at position 60.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation, features a modification of the amino acid from R to W at position 274.
+The protein's natural variant, known as in AI1J;, features a modification of the amino acid from R to C at position 76.
+The protein's natural variant, known as in AI1J;, features a modification of the amino acid from R to C at position 111.
+The protein's natural variant, known as in AI1J; unknown pathological significance;, features a modification of the amino acid from A to P at position 128.
+The protein's natural variant, known as in AI1J; unknown pathological significance;, features a modification of the amino acid from E to K at position 133.
+The protein's natural variant, known as in AI1J;, features a modification of the amino acid from S to L at position 238.
+The protein's natural variant, known as in strain: ATCC 7962, features a modification of the amino acid from L to F at position 34.
+The protein's natural variant, known as in strain: ATCC 7962, features a modification of the amino acid from V to G at position 182.
+The protein's natural variant, known as in strain: ATCC 7962, features a modification of the amino acid from I to M at position 237.
+The protein's natural variant, known as in strain: ATCC 7962, features a modification of the amino acid from I to T at position 629.
+The protein's natural variant, known as in strain: ATCC 7962, features a modification of the amino acid from C to Y at position 677.
+The protein's natural variant, known as in strain: ATCC 7962, features a modification of the amino acid from R to K at position 702.
+The protein's natural variant, known as in strain: ATCC 7962, features a modification of the amino acid from F to L at position 712.
+The protein's natural variant, known as in strain: ATCC 7962, features a modification of the amino acid from GI to AV at position 785.
+The protein's natural variant, known as in strain: ATCC 7962, features a modification of the amino acid from T to N at position 796.
+The protein's natural variant, known as in strain: ATCC 7962, features a modification of the amino acid from D to G at position 919.
+The protein's natural variant, known as in strain: ATCC 6633 / PCI 219, features a modification of the amino acid from V to I at position 5.
+The protein's natural variant, known as in strain: ATCC 6633 / PCI 219, features a modification of the amino acid from EL to DV at position 131.
+The protein's natural variant, known as in strain: ATCC 6633 / PCI 219, features a modification of the amino acid from A to T at position 201.
+The protein's natural variant, known as in strain: ATCC 6633 / PCI 219, features a modification of the amino acid from L to V at position 216.
+The natural variant of this protein is characterized by an amino acid alteration from N to S at position 109.
+The natural variant of this protein is characterized by an amino acid alteration from P to G at position 66.
+The natural variant of this protein is characterized by an amino acid alteration from N to G at position 72.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation, features a modification of the amino acid from E to K at position 18.
+The natural variant of this protein is characterized by an amino acid alteration from L to F at position 6.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 29.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 122.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 162.
+The natural variant of this protein is characterized by an amino acid alteration from T to A at position 195.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 345.
+The protein's natural variant, known as in SPG79B; has decreased binding to ubiquitin and significantly decreased hydrolase activity compared to wild-type;, features a modification of the amino acid from E to A at position 7.
+The protein's natural variant, known as may be associated with reduced risk for sporadic Parkinson disease; it confers protection from oxidative stress when expressed at physiological levels in neuroblastoma cells and primary cortical neurons; loss of dimerization ability; impaired ligase activity;, features a modification of the amino acid from S to Y at position 18.
+The protein's natural variant, known as in SPG79A; unknown pathological significance, features a modification of the amino acid from L to LL at position 52.
+The protein's natural variant, known as in PARK5; impaired enzymatic hydrolase activity; has about a 50% reduction in catalytic activity compared to wild-type protein;, features a modification of the amino acid from I to M at position 93.
+The protein's natural variant, known as in SPG79B; increased hydrolase activity; decreased protein abundance;, features a modification of the amino acid from R to Q at position 178.
+The protein's natural variant, known as in SPG79B; decreased protein abundance;, features a modification of the amino acid from A to D at position 216.
+The protein's natural variant, known as in unc mutant; uncouples receptors from adenylyl cyclases, features a modification of the amino acid from R to P at position 389.
+The protein's natural variant, known as in BOCD;, features a modification of the amino acid from P to L at position 132.
+The protein's natural variant, known as in MCDJ; constitutively activated; constitutively increases adenylate cyclase-activating G-protein coupled receptor signaling pathway; decreases the degree of N-glycosylation; does not affect homodimerization;, features a modification of the amino acid from H to R at position 223.
+The protein's natural variant, known as in MCDJ; constitutively activated;, features a modification of the amino acid from T to P at position 410.
+The protein's natural variant, known as in MCDJ; leads to agonist-independent cAMP formation which is less pronounced than that observed with the Pro-410 mutant;, features a modification of the amino acid from T to R at position 410.
+The protein's natural variant, known as in MCDJ;, features a modification of the amino acid from I to R at position 458.
+The protein's natural variant, known as in LIS10, features a modification of the amino acid from S to C at position 58.
+The protein's natural variant, known as in LIS10, features a modification of the amino acid from D to N at position 65.
+The protein's natural variant, known as in LIS10; unknown pathological significance, features a modification of the amino acid from I to T at position 68.
+The protein's natural variant, known as in LIS10; unknown pathological significance, features a modification of the amino acid from G to R at position 69.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from S to F at position 345.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from M to I at position 361.
+The protein's natural variant, known as in CDG1E;, features a modification of the amino acid from R to G at position 92.
+The protein's natural variant, known as in CDG1E; abolishes interaction with DPM3;, features a modification of the amino acid from G to V at position 152.
+The protein's natural variant, known as in CDG1E;, features a modification of the amino acid from S to P at position 248.
+The protein's natural variant, known as requires 2 nucleotide substitutions; might be implicated in the hereditary spastic paraplegia phenotype, features a modification of the amino acid from F to P at position 284.
+The protein's natural variant, known as in SPG7; function impaired;, features a modification of the amino acid from G to S at position 349.
+The protein's natural variant, known as in SPG7; function impaired;, features a modification of the amino acid from A to V at position 510.
+The protein's natural variant, known as in SPG7; function impaired;, features a modification of the amino acid from W to C at position 583.
+The protein's natural variant, known as might be implicated in the hereditary spastic paraplegia phenotype;, features a modification of the amino acid from S to L at position 635.
+The protein's natural variant, known as might be implicated in the hereditary spastic paraplegia phenotype, features a modification of the amino acid from D to H at position 650.
+The protein's natural variant, known as in SPG7;, features a modification of the amino acid from S to T at position 692.
+The protein's natural variant, known as in VCRL3; loss of protein expression, features a modification of the amino acid from C to R at position 49.
+The protein's natural variant, known as in VCRL3; decreased protein expression; decreased NAD(+) synthase (glutamine-hydrolyzing) activity;, features a modification of the amino acid from W to L at position 132.
+The protein's natural variant, known as in VCRL3; no effect on protein expression; decreased NAD(+) synthase (glutamine-hydrolyzing) activity;, features a modification of the amino acid from A to T at position 573.
+The protein's natural variant, known as in strain: Wistar, features a modification of the amino acid from RPT to NPP at position 442.
+The protein's natural variant, known as in strain: Lewis, features a modification of the amino acid from A to T at position 457.
+The protein's natural variant, known as in strain: Lewis, features a modification of the amino acid from M to I at position 555.
+The protein's natural variant, known as in strain: Wistar, features a modification of the amino acid from E to G at position 568.
+The protein's natural variant, known as in strain: Lewis, features a modification of the amino acid from T to I at position 583.
+The protein's natural variant, known as in strain: Lewis, features a modification of the amino acid from F to V at position 592.
+The protein's natural variant, known as in strain: Lewis, features a modification of the amino acid from N to K at position 624.
+The protein's natural variant, known as in strain: Lewis, features a modification of the amino acid from N to H at position 640.
+The protein's natural variant, known as in strain: Lewis, features a modification of the amino acid from V to I at position 774.
+The protein's natural variant, known as in strain: Lewis, features a modification of the amino acid from N to I at position 806.
+The protein's natural variant, known as in strain: Lewis, features a modification of the amino acid from T to I at position 850.
+The protein's natural variant, known as in strain: Lewis, features a modification of the amino acid from H to Q at position 898.
+The protein's natural variant, known as in IIAE5;, features a modification of the amino acid from R to W at position 118.
+The protein's natural variant, known as in a NIDDM patient, features a modification of the amino acid from M to MM at position 1.
+The protein's natural variant, known as probable disease-associated variant found in a patient with autism spectrum disorder; gain of function; increases channel activity; the mutant channel is activated at less depolarized potentials with an increased current density and impaired channel inactivation, features a modification of the amino acid from V to L at position 401.
+The protein's natural variant, known as in PASNA; the mutant channel is activated at less depolarized potentials; results in increased current density and impaired channel inactivation, features a modification of the amino acid from G to D at position 403.
+The protein's natural variant, known as in SANDD; the mutant channels are unable to conduct calcium ions currents and have abnormal voltage-dependent gating, features a modification of the amino acid from G to GG at position 403.
+The protein's natural variant, known as probable disease-associated variant found in a patient with autism spectrum disorder; gain of function; increases channel activity; the mutant channel is activated at less depolarized potentials with an increased current density and impaired channel inactivation;, features a modification of the amino acid from G to R at position 407.
+The protein's natural variant, known as probable disease-associated variant found in a patient with autism spectrum disorder; gain of function; increases channel activity; the mutant channel is activated at less depolarized potentials with an increased current density and impaired channel inactivation, features a modification of the amino acid from A to G at position 749.
+The protein's natural variant, known as in PASNA; the mutant channel is activated at less depolarized potentials; results in increased current density;, features a modification of the amino acid from I to M at position 750.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from G to A at position 175.
+The natural variant of this protein is characterized by an amino acid alteration from A to E at position 41.
+The protein's natural variant, known as in CDG2V; unknown pathological significance;, features a modification of the amino acid from D to G at position 61.
+The protein's natural variant, known as in CDG2V; unknown pathological significance, features a modification of the amino acid from D to N at position 456.
+The natural variant of this protein is characterized by an amino acid alteration from F to L at position 154.
+The natural variant of this protein is characterized by an amino acid alteration from C to R at position 350.
+The natural variant of this protein is characterized by an amino acid alteration from L to P at position 561.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from A to T at position 71.
+The protein's natural variant, known as in alpha-4B;, features a modification of the amino acid from A to T at position 74.
+The protein's natural variant, known as in alpha-4B;, features a modification of the amino acid from E to V at position 137.
+The protein's natural variant, known as in JBTS16;, features a modification of the amino acid from H to R at position 96.
+The protein's natural variant, known as in JBTS16;, features a modification of the amino acid from A to T at position 126.
+The protein's natural variant, known as in JBTS16;, features a modification of the amino acid from A to V at position 127.
+The protein's natural variant, known as in JBTS16;, features a modification of the amino acid from Y to C at position 130.
+The protein's natural variant, known as in PMDS2;, features a modification of the amino acid from R to C at position 54.
+The protein's natural variant, known as in PMDS2, features a modification of the amino acid from G to V at position 142.
+The protein's natural variant, known as in PMDS2;, features a modification of the amino acid from H to Q at position 282.
+The protein's natural variant, known as in PMDS2;, features a modification of the amino acid from R to Q at position 406.
+The protein's natural variant, known as in PMDS2, features a modification of the amino acid from D to G at position 426.
+The protein's natural variant, known as in PMDS2;, features a modification of the amino acid from V to A at position 458.
+The protein's natural variant, known as in PMDS2;, features a modification of the amino acid from D to H at position 491.
+The protein's natural variant, known as in PMDS2;, features a modification of the amino acid from R to C at position 504.
+The protein's natural variant, known as in SCAR28; decreased mitochondrial fusion;, features a modification of the amino acid from V to A at position 55.
+The protein's natural variant, known as found in a patient with a severe multisystemic growth disorder and cerebellar atrophy; unknown pathological significance;, features a modification of the amino acid from L to P at position 294.
+The protein's natural variant, known as acts as a disease modifier; patients carrying a mutated allele of spastin and L-44 on the other allele are affected by severe spastic paraplegia with an early age of onset; may decrease the activity of the alternative promoter which directs the synthesis of isoform 3 and isoform 4;, features a modification of the amino acid from S to L at position 44.
+The protein's natural variant, known as acts as a disease modifier; patients carrying a mutated allele of spastin and Q-45 on the other allele are affected by severe spastic paraplegia with an early age of onset;, features a modification of the amino acid from P to Q at position 45.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from A to T at position 95.
+The protein's natural variant, known as in SPG4; unknown pathological significance;, features a modification of the amino acid from P to T at position 97.
+The protein's natural variant, known as in SPG4; likely benign variant;, features a modification of the amino acid from V to I at position 162.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from L to V at position 195.
+The protein's natural variant, known as in SPG4; unknown pathological significance;, features a modification of the amino acid from V to D at position 201.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from P to L at position 293.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from R to H at position 309.
+The protein's natural variant, known as in SPG4; unknown pathological significance;, features a modification of the amino acid from L to S at position 314.
+The protein's natural variant, known as in SPG4; unknown pathological significance, features a modification of the amino acid from I to K at position 328.
+The protein's natural variant, known as in SPG4; unknown pathological significance, features a modification of the amino acid from I to L at position 328.
+The protein's natural variant, known as in SPG4; abrogates ATPase activity and promotes microtubule binding;, features a modification of the amino acid from I to K at position 344.
+The protein's natural variant, known as in SPG4; promotes microtubule binding;, features a modification of the amino acid from Q to K at position 347.
+The protein's natural variant, known as in SPG4; unknown pathological significance;, features a modification of the amino acid from E to K at position 356.
+The protein's natural variant, known as in SPG4; unknown pathological significance;, features a modification of the amino acid from L to V at position 360.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from P to L at position 361.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from S to C at position 362.
+The protein's natural variant, known as in SPG4, features a modification of the amino acid from L to P at position 363.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from R to M at position 364.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from R to T at position 364.
+The protein's natural variant, known as in SPG4; unknown pathological significance, features a modification of the amino acid from P to S at position 365.
+The protein's natural variant, known as in SPG4; unknown pathological significance;, features a modification of the amino acid from E to K at position 366.
+The protein's natural variant, known as in SPG4, features a modification of the amino acid from F to L at position 368.
+The protein's natural variant, known as in SPG4; unknown pathological significance, features a modification of the amino acid from F to V at position 368.
+The protein's natural variant, known as in SPG4; promotes microtubule binding and the formation of thick microtubule bundles, features a modification of the amino acid from G to R at position 370.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from R to G at position 372.
+The protein's natural variant, known as in SPG4; unknown pathological significance, features a modification of the amino acid from R to T at position 372.
+The protein's natural variant, known as in SPG4, features a modification of the amino acid from G to E at position 377.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from L to Q at position 378.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from L to R at position 378.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from L to H at position 380.
+The protein's natural variant, known as in SPG4; promotes microtubule binding and the formation of thick microtubule bundles;, features a modification of the amino acid from F to C at position 381.
+The protein's natural variant, known as in SPG4; unknown pathological significance;, features a modification of the amino acid from G to R at position 382.
+The protein's natural variant, known as in SPG4; abrogates ATPase activity, promotes microtubule binding and the formation of thick microtubule bundles;, features a modification of the amino acid from N to K at position 386.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from N to S at position 386.
+The protein's natural variant, known as in SPG4; unknown pathological significance, features a modification of the amino acid from N to Y at position 386.
+The protein's natural variant, known as in SPG4; abrogates ATPase activity, promotes microtubule binding and the formation of thick microtubule bundles and impairs traffic from the ER to Golgi;, features a modification of the amino acid from K to R at position 388.
+The protein's natural variant, known as in SPG4; unknown pathological significance;, features a modification of the amino acid from M to T at position 390.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from M to V at position 390.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from L to P at position 391.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from S to L at position 399.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from I to R at position 406.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from I to V at position 406.
+The protein's natural variant, known as in SPG4; unknown pathological significance, features a modification of the amino acid from S to I at position 407.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from S to R at position 407.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from A to T at position 409.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from S to R at position 410.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from S to L at position 413.
+The protein's natural variant, known as in SPG4; unknown pathological significance, features a modification of the amino acid from E to A at position 418.
+The protein's natural variant, known as in SPG4; unknown pathological significance;, features a modification of the amino acid from L to F at position 422.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from V to L at position 423.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from R to G at position 424.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from L to F at position 426.
+The protein's natural variant, known as in SPG4; promotes microtubule binding and the formation of thick microtubule bundles;, features a modification of the amino acid from L to V at position 426.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from P to L at position 435.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from S to F at position 436.
+The protein's natural variant, known as in SPG4, features a modification of the amino acid from S to P at position 436.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from D to G at position 441.
+The protein's natural variant, known as in SPG4, features a modification of the amino acid from D to N at position 441.
+The protein's natural variant, known as in SPG4, features a modification of the amino acid from D to V at position 441.
+The protein's natural variant, known as in SPG4; unknown pathological significance;, features a modification of the amino acid from S to N at position 445.
+The protein's natural variant, known as in SPG4; abrogates binding to the tail of beta-3-tubulin, abolishes microtubule severing and promotes the formation of thick microtubule bundles;, features a modification of the amino acid from C to Y at position 448.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from R to S at position 450.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from E to K at position 454.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from S to R at position 458.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from R to G at position 459.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from R to C at position 460.
+The protein's natural variant, known as in SPG4; promotes microtubule binding and the formation of thick microtubule bundles;, features a modification of the amino acid from R to L at position 460.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from R to S at position 460.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from L to P at position 461.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from T to A at position 463.
+The protein's natural variant, known as in SPG4; unknown pathological significance;, features a modification of the amino acid from E to A at position 464.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from D to V at position 470.
+The protein's natural variant, known as in SPG4; unknown pathological significance;, features a modification of the amino acid from D to Y at position 470.
+The protein's natural variant, known as in SPG4; unknown pathological significance;, features a modification of the amino acid from V to L at position 482.
+The protein's natural variant, known as in SPG4; unknown pathological significance, features a modification of the amino acid from A to T at position 485.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from A to V at position 485.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from P to L at position 489.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from L to F at position 492.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from D to G at position 493.
+The protein's natural variant, known as in SPG4, features a modification of the amino acid from R to G at position 498.
+The protein's natural variant, known as in SPG4; unknown pathological significance, features a modification of the amino acid from R to M at position 498.
+The protein's natural variant, known as in SPG4; abrogates ATPase activity, promotes microtubule binding and the formation of thick microtubule bundles;, features a modification of the amino acid from R to C at position 499.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from R to H at position 499.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from R to L at position 503.
+The protein's natural variant, known as in SPG4, features a modification of the amino acid from R to RR at position 503.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from R to W at position 503.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from E to D at position 512.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from R to G at position 514.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from L to P at position 534.
+The protein's natural variant, known as in SPG4; unknown pathological significance;, features a modification of the amino acid from L to V at position 534.
+The protein's natural variant, known as in SPG4; unknown pathological significance;, features a modification of the amino acid from T to I at position 550.
+The protein's natural variant, known as in SPG4; requires 2 nucleotide substitutions, features a modification of the amino acid from A to Y at position 551.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from D to G at position 555.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from D to N at position 555.
+The protein's natural variant, known as in SPG4; promotes microtubule binding and the formation of thick microtubule bundles, features a modification of the amino acid from A to V at position 556.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from G to D at position 559.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from G to R at position 559.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from R to G at position 562.
+The protein's natural variant, known as in SPG4; unknown pathological significance, features a modification of the amino acid from R to P at position 562.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from R to Q at position 562.
+The protein's natural variant, known as in SPG4; unknown pathological significance;, features a modification of the amino acid from N to H at position 579.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from I to T at position 580.
+The protein's natural variant, known as in SPG4, features a modification of the amino acid from D to H at position 584.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from S to R at position 595.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from W to C at position 607.
+The protein's natural variant, known as in SPG4; variant form with congenital arachnoid cysts;, features a modification of the amino acid from T to I at position 614.
+The protein's natural variant, known as in SPG4;, features a modification of the amino acid from T to I at position 615.
+The protein's natural variant, known as in strain: CWL029 and TW-183, features a modification of the amino acid from T to A at position 168.
+The protein's natural variant, known as in allele PCI*B;, features a modification of the amino acid from A to V at position 55.
+The protein's natural variant, known as in allele PCI*B;, features a modification of the amino acid from K to E at position 105.
+The protein's natural variant, known as in CDAN3A; results in loss of function; does not rescue defective cytokinesis when expressed in KIF3-deficient cells, features a modification of the amino acid from P to R at position 916.
+The protein's natural variant, known as in strain: Serovar B, features a modification of the amino acid from S to C at position 8.
+The protein's natural variant, known as in strain: Serovar B, features a modification of the amino acid from LL to FV at position 325.
+The natural variant of this protein is characterized by an amino acid alteration from L to P at position 7.
+The natural variant of this protein is characterized by an amino acid alteration from K to R at position 79.
+The protein's natural variant, known as in strain: DOH272 and AQ4901, features a modification of the amino acid from N to I at position 134.
+The protein's natural variant, known as in strain: AQ3810 and U-5474, features a modification of the amino acid from A to T at position 138.
+The protein's natural variant, known as in strain: DOH272 and AQ4901, features a modification of the amino acid from SLA to PLT at position 150.
+The protein's natural variant, known as in strain: Y-27669, AN-8917 and RIMD 2210086, features a modification of the amino acid from T to P at position 152.
+The protein's natural variant, known as in strain: AQ3815, features a modification of the amino acid from T to S at position 152.
+The protein's natural variant, known as in strain: AQ3815, features a modification of the amino acid from P to H at position 169.
+The protein's natural variant, known as in IXL; loss of steryl-sulfatase activity;, features a modification of the amino acid from S to L at position 341.
+The protein's natural variant, known as in IXL; loss of steryl-sulfatase activity;, features a modification of the amino acid from W to R at position 372.
+The protein's natural variant, known as in IXL; loss of steryl-sulfatase activity;, features a modification of the amino acid from W to S at position 372.
+The protein's natural variant, known as in IXL; strong decreases of steryl-sulfatase activity, features a modification of the amino acid from G to R at position 380.
+The protein's natural variant, known as in IXL; loss of steryl-sulfatase activity;, features a modification of the amino acid from H to R at position 444.
+The protein's natural variant, known as in IXL; loss of steryl-sulfatase activity;, features a modification of the amino acid from C to Y at position 446.
+The protein's natural variant, known as does not affect steryl-sulfatase activity;, features a modification of the amino acid from V to M at position 476.
+The protein's natural variant, known as in IXL, features a modification of the amino acid from Q to P at position 560.
+The protein's natural variant, known as in SDDHD; decreased of transketolase activity;, features a modification of the amino acid from R to C at position 318.
+The protein's natural variant, known as in MHICP;, features a modification of the amino acid from Q to K at position 186.
+The protein's natural variant, known as in a gastric adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from R to W at position 303.
+The protein's natural variant, known as in a lung large cell carcinoma sample; somatic mutation, features a modification of the amino acid from V to I at position 319.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation, features a modification of the amino acid from G to E at position 391.
+The protein's natural variant, known as found in two infertile brothers from a consanguineous family. The brothers present normal semen analysis, but both couples have no embryos for transfer after several IVF and intracytoplasmic sperm injection. The sperm of the affected brothers dysplay acrosomal ultrastructural defects;, features a modification of the amino acid from A to T at position 245.
+The protein's natural variant, known as in strain: B6, features a modification of the amino acid from V to A at position 57.
+The protein's natural variant, known as in MATINS;, features a modification of the amino acid from N to K at position 93.
+The protein's natural variant, known as in MATINS;, features a modification of the amino acid from A to T at position 95.
+The protein's natural variant, known as in MATINS;, features a modification of the amino acid from S to L at position 96.
+The protein's natural variant, known as in MATINS;, features a modification of the amino acid from K to N at position 373.
+The protein's natural variant, known as in MATINS;, features a modification of the amino acid from R to C at position 702.
+The protein's natural variant, known as in MATINS;, features a modification of the amino acid from R to H at position 702.
+The protein's natural variant, known as in DFNA17;, features a modification of the amino acid from R to H at position 705.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from K to N at position 810.
+The protein's natural variant, known as in MATINS;, features a modification of the amino acid from K to Q at position 910.
+The protein's natural variant, known as in MATINS;, features a modification of the amino acid from S to P at position 1114.
+The protein's natural variant, known as in MATINS;, features a modification of the amino acid from T to I at position 1155.
+The protein's natural variant, known as in MATINS;, features a modification of the amino acid from R to C at position 1165.
+The protein's natural variant, known as in MATINS;, features a modification of the amino acid from R to L at position 1165.
+The protein's natural variant, known as in DFNA17; unknown pathological significance;, features a modification of the amino acid from E to K at position 1228.
+The protein's natural variant, known as in MATINS; likely benign variant;, features a modification of the amino acid from R to W at position 1400.
+The protein's natural variant, known as in MATINS;, features a modification of the amino acid from D to H at position 1424.
+The protein's natural variant, known as in MATINS; results in reduced protein levels;, features a modification of the amino acid from D to N at position 1424.
+The protein's natural variant, known as in MATINS;, features a modification of the amino acid from D to Y at position 1424.
+The protein's natural variant, known as in MATINS;, features a modification of the amino acid from I to V at position 1816.
+The protein's natural variant, known as in MATINS;, features a modification of the amino acid from E to K at position 1841.
+The protein's natural variant, known as in MTDPS13;, features a modification of the amino acid from I to T at position 205.
+The protein's natural variant, known as in MTDPS13;, features a modification of the amino acid from L to P at position 481.
+The protein's natural variant, known as in MTDPS13;, features a modification of the amino acid from R to W at position 482.
+The protein's natural variant, known as in MTDPS13;, features a modification of the amino acid from I to N at position 551.
+The protein's natural variant, known as in MTDPS13;, features a modification of the amino acid from D to G at position 565.
+The protein's natural variant, known as in MTDPS13;, features a modification of the amino acid from G to A at position 568.
+The protein's natural variant, known as in MTDPS13;, features a modification of the amino acid from Q to P at position 597.
+The protein's natural variant, known as associated with short sleep phenotype; abolishes inhibition of CLOCK-BMAL1 and NPAS2/BMAL1 transactivation activities;, features a modification of the amino acid from Y to H at position 362.
+The protein's natural variant, known as associated with short sleep phenotype; heterogeneous phenotype; increases inhibition of CLOCK-BMAL1 and NPAS2/BMAL1 transactivation activities;, features a modification of the amino acid from P to Q at position 384.
+The protein's natural variant, known as associated with short sleep phenotype; abolishes inhibition of CLOCK-BMAL1 and NPAS2/BMAL1 transactivation activities;, features a modification of the amino acid from P to R at position 384.
+The protein's natural variant, known as in LYNCH5, CRC and ENDMC; unknown pathological significance; normal mismatch repair activity;, features a modification of the amino acid from A to V at position 20.
+The protein's natural variant, known as in LYNCH5; unknown pathological significance; normal mismatch repair activity;, features a modification of the amino acid from A to S at position 25.
+The protein's natural variant, known as in CRC; unknown pathological significance;, features a modification of the amino acid from G to A at position 54.
+The protein's natural variant, known as in CRC; unknown pathological significance;, features a modification of the amino acid from K to N at position 99.
+The protein's natural variant, known as in LYNCH5; unknown pathological significance; no impairment of heterodimerization with MSH2; normal mismatch repair activity;, features a modification of the amino acid from R to L at position 128.
+The protein's natural variant, known as in LYNCH5 and CRC; unknown pathological significance; normal mismatch repair activity;, features a modification of the amino acid from S to I at position 144.
+The protein's natural variant, known as in CRC; unknown pathological significance;, features a modification of the amino acid from S to I at position 285.
+The protein's natural variant, known as in multiple colorectal adenoma;, features a modification of the amino acid from K to R at position 295.
+The protein's natural variant, known as in LYNCH5; unknown pathological significance; normal mismatch repair activity;, features a modification of the amino acid from A to V at position 326.
+The protein's natural variant, known as in CRC, breast cancer and leukemia; unknown pathological significance;, features a modification of the amino acid from F to S at position 340.
+The protein's natural variant, known as in LYNCH5; unknown pathological significance; normal mismatch repair activity;, features a modification of the amino acid from L to V at position 396.
+The protein's natural variant, known as decreased mismatch repair activity;, features a modification of the amino acid from L to P at position 435.
+The protein's natural variant, known as in CRC and ENDMC; unknown pathological significance;, features a modification of the amino acid from L to P at position 449.
+The protein's natural variant, known as in LYNCH5; unknown pathological significance; normal mismatch repair activity;, features a modification of the amino acid from M to V at position 492.
+The protein's natural variant, known as in LYNCH5; unknown pathological significance; normal mismatch repair activity;, features a modification of the amino acid from S to C at position 503.
+The protein's natural variant, known as in CRC; unknown pathological significance; normal mismatch repair activity;, features a modification of the amino acid from Q to R at position 522.
+The protein's natural variant, known as in CRC and LYNCH5; decreased mismatch repair activity; loss of protein expression;, features a modification of the amino acid from G to R at position 566.
+The protein's natural variant, known as decreased mismatch repair activity;, features a modification of the amino acid from L to P at position 585.
+The protein's natural variant, known as in LYNCH5; unknown pathological significance; normal mismatch repair activity;, features a modification of the amino acid from K to N at position 610.
+The protein's natural variant, known as in CRC; unknown pathological significance;, features a modification of the amino acid from E to D at position 619.
+The protein's natural variant, known as in LYNCH5; unknown pathological significance; no impairment of heterodimerization with MSH2; normal mismatch repair activity;, features a modification of the amino acid from P to L at position 623.
+The protein's natural variant, known as normal mismatch repair activity;, features a modification of the amino acid from S to T at position 677.
+The protein's natural variant, known as in CRC; unknown pathological significance;, features a modification of the amino acid from G to A at position 685.
+The protein's natural variant, known as in HNPCC; unknown pathological significance;, features a modification of the amino acid from Q to E at position 698.
+The protein's natural variant, known as in CRC; unknown pathological significance;, features a modification of the amino acid from I to M at position 725.
+The protein's natural variant, known as in LYNCH5; unknown pathological significance; no impairment of heterodimerization with MSH2; normal mismatch repair activity;, features a modification of the amino acid from K to T at position 728.
+The protein's natural variant, known as in CRC; unknown pathological significance;, features a modification of the amino acid from R to Q at position 772.
+The protein's natural variant, known as in LYNCH5;, features a modification of the amino acid from R to W at position 772.
+The protein's natural variant, known as in CRC; unknown pathological significance;, features a modification of the amino acid from A to V at position 787.
+The protein's natural variant, known as in CRC; somatic mutation;, features a modification of the amino acid from V to A at position 800.
+The protein's natural variant, known as in CRC; unknown pathological significance;, features a modification of the amino acid from D to G at position 803.
+The protein's natural variant, known as in LYNCH5 and CRC; unknown pathological significance; normal mismatch repair activity;, features a modification of the amino acid from Y to C at position 850.
+The protein's natural variant, known as in CRC; unknown pathological significance;, features a modification of the amino acid from K to M at position 854.
+The protein's natural variant, known as in LYNCH5, CRC and ENDMC; unknown pathological significance; normal mismatch repair activity;, features a modification of the amino acid from V to A at position 878.
+The protein's natural variant, known as in LYNCH5; unknown pathological significance; normal mismatch repair activity, features a modification of the amino acid from G to KS at position 881.
+The protein's natural variant, known as in CRC and ENDMC; unknown pathological significance;, features a modification of the amino acid from R to H at position 901.
+The protein's natural variant, known as in CRC; sporadic; unknown pathological significance; normal mismatch repair activity;, features a modification of the amino acid from R to H at position 976.
+The protein's natural variant, known as in CRC; unknown pathological significance; normal mismatch repair activity;, features a modification of the amino acid from A to D at position 1021.
+The protein's natural variant, known as in LYNCH5; unknown pathological significance; normal mismatch repair activity;, features a modification of the amino acid from D to Y at position 1026.
+The protein's natural variant, known as in CRC; unknown pathological significance; somatic mutation;, features a modification of the amino acid from D to V at position 1031.
+The protein's natural variant, known as in CRC; unknown pathological significance;, features a modification of the amino acid from R to C at position 1076.
+The protein's natural variant, known as in LYNCH5; unknown pathological significance; normal mismatch repair activity;, features a modification of the amino acid from P to S at position 1087.
+The protein's natural variant, known as in CRC and LYNCH5; unknown pathological significance;, features a modification of the amino acid from P to T at position 1087.
+The protein's natural variant, known as in CRC and LYNCH5; unknown pathological significance; normal mismatch repair activity;, features a modification of the amino acid from R to H at position 1095.
+The protein's natural variant, known as in CRC; unknown pathological significance;, features a modification of the amino acid from T to M at position 1100.
+The protein's natural variant, known as in CRC; unknown pathological significance; somatic mutation;, features a modification of the amino acid from C to R at position 1158.
+The protein's natural variant, known as in LYNCH5;, features a modification of the amino acid from E to V at position 1163.
+The protein's natural variant, known as in LYNCH5; decreased mismatch repair activity; displays marked impairment of heterodimerization with MSH2;, features a modification of the amino acid from E to K at position 1193.
+The natural variant of this protein is characterized by an amino acid alteration from D to V at position 1213.
+The protein's natural variant, known as in CRC; unknown pathological significance;, features a modification of the amino acid from T to I at position 1219.
+The protein's natural variant, known as in LYNCH5; unknown pathological significance; normal mismatch repair activity;, features a modification of the amino acid from T to M at position 1225.
+The protein's natural variant, known as in CRC; unknown pathological significance;, features a modification of the amino acid from H to D at position 1248.
+The protein's natural variant, known as in CRC; unknown pathological significance;, features a modification of the amino acid from T to M at position 1284.
+The protein's natural variant, known as in CRC and LYNCH5; unknown pathological significance; normal mismatch repair activity;, features a modification of the amino acid from L to Q at position 1354.
+The protein's natural variant, known as in HACD59;, features a modification of the amino acid from C to Y at position 89.
+The protein's natural variant, known as in strain: Classical 569B / ATCC 25870 /Serotype O1, features a modification of the amino acid from K to Q at position 365.
+The protein's natural variant, known as in CPT1AD;, features a modification of the amino acid from R to C at position 123.
+The protein's natural variant, known as in CPT1AD;, features a modification of the amino acid from C to W at position 304.
+The protein's natural variant, known as in CPT1AD;, features a modification of the amino acid from T to I at position 314.
+The protein's natural variant, known as in CPT1AD;, features a modification of the amino acid from R to G at position 316.
+The protein's natural variant, known as in CPT1AD;, features a modification of the amino acid from F to V at position 343.
+The protein's natural variant, known as in CPT1AD; decreased stability;, features a modification of the amino acid from R to W at position 357.
+The protein's natural variant, known as in CPT1AD; reduced protein levels;, features a modification of the amino acid from E to G at position 360.
+The protein's natural variant, known as in CPT1AD; decreased activity;, features a modification of the amino acid from A to V at position 414.
+The protein's natural variant, known as in CPT1AD; loss of activity;, features a modification of the amino acid from D to G at position 454.
+The protein's natural variant, known as in CPT1AD;, features a modification of the amino acid from G to W at position 465.
+The protein's natural variant, known as in CPT1AD; decreased activity;, features a modification of the amino acid from P to L at position 479.
+The protein's natural variant, known as in CPT1AD;, features a modification of the amino acid from L to P at position 484.
+The protein's natural variant, known as in CPT1AD; decreased activity;, features a modification of the amino acid from Y to C at position 498.
+The protein's natural variant, known as in CPT1AD; loss of activity;, features a modification of the amino acid from G to E at position 709.
+The protein's natural variant, known as in CPT1AD; loss of activity;, features a modification of the amino acid from G to E at position 710.
+The protein's natural variant, known as in IMD14A; results in gain of function causing enhanced membrane association and kinase activity;, features a modification of the amino acid from E to K at position 1021.
+The protein's natural variant, known as in MRXSSD; abolishes histone methyltransferase activity; reduces transcriptional activation activity;, features a modification of the amino acid from F to S at position 315.
+The protein's natural variant, known as in IMD50; decreased protein abundance in T cell; loss of T cell proliferation after T cell activation; does not affect immunologic synapses formation; decreased T cell migration in response to activation by chemokines; increased T cell adhesion in response to activation by integrins;, features a modification of the amino acid from R to W at position 171.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from D to Y at position 371.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from L to M at position 390.
+The protein's natural variant, known as in LVNC1; unknown pathological significance;, features a modification of the amino acid from P to L at position 121.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from D to V at position 12.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from R to K at position 232.
+The protein's natural variant, known as in MNLIX;, features a modification of the amino acid from R to C at position 408.
+The protein's natural variant, known as in BDPLT11; results in abnormal protein migration and a loss of collagen binding;, features a modification of the amino acid from R to C at position 58.
+The protein's natural variant, known as in BDPLT11; shows strongly reduced membrane expression and decreased interaction with the snake toxin convulxin;, features a modification of the amino acid from S to N at position 175.
+The natural variant of this protein is characterized by an amino acid alteration from L to V at position 31.
+The protein's natural variant, known as in PDHBD;, features a modification of the amino acid from Y to C at position 132.
+The protein's natural variant, known as in PDHBD;, features a modification of the amino acid from P to S at position 344.
+The protein's natural variant, known as in NEDCHF; decreased interaction with YWHAB, features a modification of the amino acid from T to K at position 244.
+The protein's natural variant, known as in NEDCHF; decreased interaction with YWHAB, features a modification of the amino acid from E to G at position 247.
+The protein's natural variant, known as in NEDCHF, features a modification of the amino acid from P to A at position 248.
+The protein's natural variant, known as in NEDCHF, features a modification of the amino acid from P to L at position 248.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from P to R at position 727.
+The protein's natural variant, known as in RUSAT2; alters transcriptional regulation;, features a modification of the amino acid from R to W at position 929.
+The protein's natural variant, known as in RUSAT2; alters transcriptional regulation;, features a modification of the amino acid from H to R at position 930.
+The protein's natural variant, known as in RUSAT2; alters transcriptional regulation;, features a modification of the amino acid from T to A at position 935.
+The natural variant of this protein is characterized by an amino acid alteration from P to S at position 114.
+The protein's natural variant, known as in COXPD19; can form a normal complex with NFS1 but the desulfurase enzymatic activity of this complex is severely decreased compared to control;, features a modification of the amino acid from R to L at position 68.
+The protein's natural variant, known as in CORD22; unknown pathological significance;, features a modification of the amino acid from G to S at position 56.
+The natural variant of this protein is characterized by an amino acid alteration from SHDGPPV to CNDGPPA at position 188.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from V to E at position 166.
+The protein's natural variant, known as in strain: ATCC 6633, features a modification of the amino acid from L to W at position 8.
+The protein's natural variant, known as in strain: ATCC 6633, features a modification of the amino acid from A to T at position 13.
+The protein's natural variant, known as in strain: ATCC 6633, features a modification of the amino acid from A to S at position 32.
+The protein's natural variant, known as in strain: ATCC 6633, features a modification of the amino acid from G to R at position 84.
+The protein's natural variant, known as in strain: ATCC 6633, features a modification of the amino acid from D to E at position 111.
+The protein's natural variant, known as in strain: ATCC 6633, features a modification of the amino acid from E to K at position 146.
+The protein's natural variant, known as in strain: ATCC 6633, features a modification of the amino acid from T to N at position 155.
+The protein's natural variant, known as in strain: ATCC 6633, features a modification of the amino acid from G to S at position 194.
+The protein's natural variant, known as in strain: ATCC 6633, features a modification of the amino acid from K to Q at position 252.
+The protein's natural variant, known as in allotype C8BB;, features a modification of the amino acid from G to R at position 117.
+The protein's natural variant, known as in SPG54;, features a modification of the amino acid from D to H at position 660.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from E to Q at position 171.
+The protein's natural variant, known as in FA13BD; may disrupt a disulfide bond; impaired subcellular location leading to accumulation in the endoplasmic reticulum; impaired interaction with F13A1; impaired structure;, features a modification of the amino acid from C to R at position 25.
+The protein's natural variant, known as in FA13BD; impaired interaction with F13A1;, features a modification of the amino acid from I to N at position 101.
+The protein's natural variant, known as in FA13BD; unknown pathological significance;, features a modification of the amino acid from L to F at position 136.
+The protein's natural variant, known as in FA13BD; unknown pathological significance;, features a modification of the amino acid from V to I at position 237.
+The protein's natural variant, known as in FA13BD; may disrupt a disulfide bond; impaired interaction with F13A1; impaired structure;, features a modification of the amino acid from C to F at position 336.
+The protein's natural variant, known as in FA13BD; impaired interaction with F13A1, features a modification of the amino acid from V to E at position 421.
+The protein's natural variant, known as in FA13BD; impaired interaction with F13A1; impaired structure, features a modification of the amino acid from P to S at position 448.
+The protein's natural variant, known as in FA13BD;, features a modification of the amino acid from C to F at position 450.
+The protein's natural variant, known as in strain: NCTC 8798, features a modification of the amino acid from VN to ID at position 48.
+The protein's natural variant, known as in strain: NCTC 8798, features a modification of the amino acid from A to G at position 95.
+The protein's natural variant, known as in strain: NCTC 8798, features a modification of the amino acid from V to I at position 109.
+The protein's natural variant, known as in strain: Silvio X10/7, features a modification of the amino acid from P to T at position 2.
+The protein's natural variant, known as in strain: Silvio X10/7, features a modification of the amino acid from Q to K at position 5.
+The protein's natural variant, known as in allele TRS-2, features a modification of the amino acid from D to E at position 71.
+The protein's natural variant, known as in allele TRS-2 and strain Silvio X10/7, features a modification of the amino acid from K to Q at position 89.
+The protein's natural variant, known as in allele TRS-2, features a modification of the amino acid from P to N at position 90.
+The protein's natural variant, known as in allele TRS-2, features a modification of the amino acid from V to A at position 106.
+The protein's natural variant, known as in allele TRS-2, features a modification of the amino acid from K to N at position 132.
+The protein's natural variant, known as in allele TRS-2, features a modification of the amino acid from K to R at position 175.
+The protein's natural variant, known as in allele TRS-2 and strain Silvio X10/7, features a modification of the amino acid from D to E at position 184.
+The protein's natural variant, known as in allele TRS-2 and strain Silvio X10/7, features a modification of the amino acid from L to V at position 207.
+The protein's natural variant, known as in allele TRS-2 and strain Silvio X10/7, features a modification of the amino acid from T to N at position 218.
+The protein's natural variant, known as in strain: Silvio X10/7, features a modification of the amino acid from D to G at position 237.
+The protein's natural variant, known as in allele TRS-2, features a modification of the amino acid from D to S at position 237.
+The protein's natural variant, known as in allele TRS-2 and strain Silvio X10/7, features a modification of the amino acid from L to V at position 248.
+The protein's natural variant, known as in allele TRS-2, features a modification of the amino acid from A to T at position 265.
+The protein's natural variant, known as in strain: Silvio X10/7, features a modification of the amino acid from A to V at position 265.
+The protein's natural variant, known as in allele TRS-2 and strain Silvio X10/7, features a modification of the amino acid from L to I at position 283.
+The protein's natural variant, known as in allele TRS-2 and strain Silvio X10/7, features a modification of the amino acid from L to Q at position 288.
+The protein's natural variant, known as in allele TRS-2, features a modification of the amino acid from L to V at position 291.
+The protein's natural variant, known as in allele TRS-2 and strain Silvio X10/7, features a modification of the amino acid from C to H at position 293.
+The protein's natural variant, known as in strain: Silvio X10/7, features a modification of the amino acid from HS to YL at position 305.
+The protein's natural variant, known as in allele TRS-2, features a modification of the amino acid from S to C at position 365.
+The protein's natural variant, known as in allele TRS-2 and strain Silvio X10/7, features a modification of the amino acid from V to I at position 369.
+The protein's natural variant, known as in strain: Silvio X10/7, features a modification of the amino acid from E to G at position 381.
+The protein's natural variant, known as in allele TRS-2 and strain Silvio X10/7, features a modification of the amino acid from N to K at position 392.
+The protein's natural variant, known as in allele TRS-2 and strain Silvio X10/7, features a modification of the amino acid from H to Y at position 397.
+The protein's natural variant, known as in strain: Silvio X10/7, features a modification of the amino acid from L to M at position 487.
+The protein's natural variant, known as in strain: Silvio X10/7, features a modification of the amino acid from P to S at position 498.
+The protein's natural variant, known as in strain: Silvio X10/7, features a modification of the amino acid from V to I at position 526.
+The protein's natural variant, known as in allele TRS-2 and strain Silvio X10/7, features a modification of the amino acid from R to K at position 535.
+The protein's natural variant, known as in allele TRS-2 and strain Silvio X10/7, features a modification of the amino acid from D to N at position 562.
+The protein's natural variant, known as in strain: Silvio X10/7, features a modification of the amino acid from S to L at position 564.
+The protein's natural variant, known as in strain: Silvio X10/7, features a modification of the amino acid from K to T at position 604.
+The protein's natural variant, known as in allele TRS-2, features a modification of the amino acid from S to I at position 615.
+The protein's natural variant, known as in strain: Silvio X10/7, features a modification of the amino acid from S to R at position 615.
+The protein's natural variant, known as in allele TRS-2, features a modification of the amino acid from Q to P at position 624.
+The protein's natural variant, known as in strain: Silvio X10/7, features a modification of the amino acid from K to N at position 635.
+The protein's natural variant, known as in strain: Isolate R1042 and Isolate R1047, features a modification of the amino acid from N to S at position 13.
+The protein's natural variant, known as in strain: Isolate R1047, features a modification of the amino acid from M to I at position 21.
+The protein's natural variant, known as in strain: Isolate R1047, features a modification of the amino acid from P to A at position 54.
+The protein's natural variant, known as in strain: Isolate R906, features a modification of the amino acid from P to A at position 56.
+The protein's natural variant, known as in strain: Isolate R1042, features a modification of the amino acid from L to P at position 67.
+The protein's natural variant, known as in strain: Isolate R1042, features a modification of the amino acid from E to K at position 69.
+The protein's natural variant, known as in strain: Isolate R1042, features a modification of the amino acid from I to V at position 74.
+The protein's natural variant, known as in strain: Isolate R1042, features a modification of the amino acid from D to N at position 77.
+The protein's natural variant, known as in strain: Isolate R1042, features a modification of the amino acid from F to L at position 79.
+The protein's natural variant, known as in strain: Isolate R1047, features a modification of the amino acid from I to L at position 95.
+The protein's natural variant, known as in strain: Isolate R1042, features a modification of the amino acid from E to K at position 135.
+The protein's natural variant, known as in strain: Isolate R1042, features a modification of the amino acid from R to H at position 142.
+The protein's natural variant, known as in strain: Isolate R1042, features a modification of the amino acid from F to S at position 154.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from V to M at position 144.
+The protein's natural variant, known as in a glioblastoma multiforme sample; somatic mutation;, features a modification of the amino acid from V to M at position 496.
+The protein's natural variant, known as in GSD12; thermolabile;, features a modification of the amino acid from D to G at position 129.
+The protein's natural variant, known as in GSD12; reduces thermal stability; 3-fold decrease in catalytic efficiency mostly due to reduced substrate affinity;, features a modification of the amino acid from E to K at position 207.
+The protein's natural variant, known as in GSD12, features a modification of the amino acid from C to Y at position 339.
+The protein's natural variant, known as in GSD12; likely benign variant; does not affect thermal stability; 4-fold decrease in catalytic efficiency due to reduced enzyme activity;, features a modification of the amino acid from G to S at position 347.
+The protein's natural variant, known as in GDHS;, features a modification of the amino acid from R to C at position 660.
+The protein's natural variant, known as in GDHS;, features a modification of the amino acid from R to C at position 694.
+The protein's natural variant, known as probable disease-associated variant found in patients with familial dilated cardiomyopathy; impairs the formation of SCF complex; reduced ubiquitination of cellular proteins;, features a modification of the amino acid from G to R at position 243.
+The protein's natural variant, known as in strain: Isolate I679, features a modification of the amino acid from Y to H at position 345.
+The protein's natural variant, known as in FA, features a modification of the amino acid from Q to P at position 269.
+The protein's natural variant, known as in ICF3;, features a modification of the amino acid from R to C at position 274.
+The protein's natural variant, known as in ICF3;, features a modification of the amino acid from R to H at position 274.
+The protein's natural variant, known as in ICF3; unknown pathological significance, features a modification of the amino acid from G to V at position 294.
+The protein's natural variant, known as in ICF3; unknown pathological significance;, features a modification of the amino acid from R to H at position 304.
+The protein's natural variant, known as in SCA40; no effect on subcellular location; increases activation of the JNK signaling pathway; induces apoptosis;, features a modification of the amino acid from R to H at position 464.
+The protein's natural variant, known as in strain: Isolate 087, features a modification of the amino acid from D to E at position 2.
+The protein's natural variant, known as in strain: Isolate 079, features a modification of the amino acid from Y to D at position 3.
+The protein's natural variant, known as in strain: Isolate 087, features a modification of the amino acid from V to G at position 25.
+The protein's natural variant, known as in strain: Isolate 079, features a modification of the amino acid from M to K at position 100.
+The protein's natural variant, known as in strain: Isolate 089, features a modification of the amino acid from L to V at position 107.
+The protein's natural variant, known as in strain: Isolate 079, features a modification of the amino acid from V to G at position 134.
+The protein's natural variant, known as in strain: Isolate 085 and Isolate 089, features a modification of the amino acid from V to L at position 146.
+The protein's natural variant, known as in strain: Isolate 079, features a modification of the amino acid from T to I at position 340.
+The protein's natural variant, known as in plasmid pYVe227 and plasmid pYVa127/90, features a modification of the amino acid from F to L at position 114.
+The protein's natural variant, known as in plasmid pYVe227, features a modification of the amino acid from L to I at position 337.
+The protein's natural variant, known as in plasmid pYVe227, features a modification of the amino acid from G to R at position 621.
+The protein's natural variant, known as in DA2A and DA2B3;, features a modification of the amino acid from T to I at position 178.
+The protein's natural variant, known as in DA2B3;, features a modification of the amino acid from A to T at position 234.
+The protein's natural variant, known as in DA2B3;, features a modification of the amino acid from S to F at position 261.
+The protein's natural variant, known as in CPSFS1A;, features a modification of the amino acid from F to V at position 287.
+The protein's natural variant, known as in DA2B3; unknown pathological significance;, features a modification of the amino acid from S to C at position 292.
+The protein's natural variant, known as in CPSFS1A;, features a modification of the amino acid from T to R at position 333.
+The protein's natural variant, known as in DA2B3; unknown pathological significance;, features a modification of the amino acid from E to K at position 375.
+The protein's natural variant, known as in DA2B3; unknown pathological significance;, features a modification of the amino acid from D to G at position 462.
+The protein's natural variant, known as in DA2A, features a modification of the amino acid from E to G at position 498.
+The protein's natural variant, known as in DA2B3; unknown pathological significance;, features a modification of the amino acid from D to Y at position 517.
+The protein's natural variant, known as in DA2A;, features a modification of the amino acid from Y to S at position 583.
+The protein's natural variant, known as in DA2A;, features a modification of the amino acid from R to C at position 672.
+The protein's natural variant, known as in DA2A;, features a modification of the amino acid from R to H at position 672.
+The protein's natural variant, known as in DA2B3, features a modification of the amino acid from G to V at position 769.
+The protein's natural variant, known as in DA2A;, features a modification of the amino acid from V to D at position 825.
+The protein's natural variant, known as in DA2B3, features a modification of the amino acid from K to E at position 838.
+The protein's natural variant, known as in CPSFS1A, features a modification of the amino acid from N to NN at position 1072.
+The protein's natural variant, known as in CPSFS1A;, features a modification of the amino acid from Q to P at position 1075.
+The protein's natural variant, known as in CPSFS1A; unknown pathological significance;, features a modification of the amino acid from L to P at position 1344.
+The protein's natural variant, known as originally found in DA2B3 patients;, features a modification of the amino acid from D to A at position 1622.
+The protein's natural variant, known as originally found in DA2B3 patients;, features a modification of the amino acid from A to V at position 1637.
+The protein's natural variant, known as in strain: F-96S, F-274F, S-26F, S-94F, S-377F, S-510S, S-521F, S-521S, S-565F, S-968F and US-255F, features a modification of the amino acid from I to A at position 62.
+The protein's natural variant, known as in strain: F-775F, S-549S and S-1224F, features a modification of the amino acid from I to V at position 62.
+The protein's natural variant, known as in strain: F-775F, S-549S and S-1224F, features a modification of the amino acid from G to S at position 74.
+The protein's natural variant, known as in strain: S-26F, S-94F, S-438S, S-510S and S-521F, features a modification of the amino acid from T to N at position 327.
+The protein's natural variant, known as in strain: S-26F, S-94F, S-438S, S-510S and S-521F, features a modification of the amino acid from G to S at position 342.
+The protein's natural variant, known as in strain: S-521S, S-968F and US-255F, features a modification of the amino acid from S to SGAES at position 367.
+The protein's natural variant, known as in strain: F-611F, features a modification of the amino acid from H to Q at position 369.
+The natural variant of this protein is characterized by an amino acid alteration from R to N at position 33.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 37.
+The protein's natural variant, known as in Isolate Urko, features a modification of the amino acid from V to L at position 93.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation;, features a modification of the amino acid from R to C at position 185.
+The protein's natural variant, known as in a breast infiltrating ductal carcinoma sample; somatic mutation, features a modification of the amino acid from F to L at position 873.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation, features a modification of the amino acid from A to V at position 921.
+The protein's natural variant, known as in subsp. Gazella, features a modification of the amino acid from A to T at position 168.
+The protein's natural variant, known as in subsp. Gazella, features a modification of the amino acid from V to I at position 192.
+The natural variant of this protein is characterized by an amino acid alteration from N to T at position 104.
+The natural variant of this protein is characterized by an amino acid alteration from D to N at position 129.
+The protein's natural variant, known as in strain: Henzerling, features a modification of the amino acid from L to F at position 17.
+The protein's natural variant, known as in strain: Henzerling, features a modification of the amino acid from M to L at position 33.
+The protein's natural variant, known as in strain: Kerns, features a modification of the amino acid from N to D at position 60.
+The protein's natural variant, known as in strain: Xinqiao, features a modification of the amino acid from F to S at position 78.
+The protein's natural variant, known as in strain: Kerns, features a modification of the amino acid from G to S at position 79.
+The protein's natural variant, known as in strain: Scurry, features a modification of the amino acid from P to S at position 115.
+The protein's natural variant, known as in strain: Kerns and Scurry, features a modification of the amino acid from NYS to T at position 122.
+The protein's natural variant, known as in strain: Xinqiao, features a modification of the amino acid from T to I at position 125.
+The protein's natural variant, known as in strain: Kerns, features a modification of the amino acid from L to T at position 127.
+The protein's natural variant, known as in strain: Xinqiao, features a modification of the amino acid from L to F at position 131.
+The protein's natural variant, known as in strain: Kerns, features a modification of the amino acid from L to I at position 136.
+The protein's natural variant, known as in strain: Kerns, features a modification of the amino acid from VY to DD at position 148.
+The protein's natural variant, known as in strain: Kerns, features a modification of the amino acid from AG to SE at position 152.
+The protein's natural variant, known as in strain: Kerns, features a modification of the amino acid from VAVS to GPVG at position 171.
+The protein's natural variant, known as in strain: Xinqiao, features a modification of the amino acid from M to I at position 172.
+The protein's natural variant, known as in strain: Kerns, features a modification of the amino acid from L to M at position 176.
+The protein's natural variant, known as in strain: Kerns and Scurry, features a modification of the amino acid from GT to EA at position 223.
+The protein's natural variant, known as in strain: Kerns and Scurry, features a modification of the amino acid from S to L at position 228.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from G to R at position 390.
+The protein's natural variant, known as in strain: RKS3333, features a modification of the amino acid from Q to E at position 64.
+The protein's natural variant, known as in strain: RKS3333, features a modification of the amino acid from S to T at position 372.
+The natural variant of this protein is characterized by an amino acid alteration from G to GA at position 18.
+The protein's natural variant, known as 5.4-fold decrease in activity with p-nitrophenyl acetate as substrate; no change in affinity for p-nitrophenyl acetate; loss of activity with L- or D-methylphenidate as substrate;, features a modification of the amino acid from G to E at position 143.
+The protein's natural variant, known as in MRT69; impaired localization to the nucleolus;, features a modification of the amino acid from H to Y at position 729.
+The protein's natural variant, known as in MRT69; impaired localization to the nucleolus;, features a modification of the amino acid from H to Q at position 880.
+The protein's natural variant, known as in PC2;, features a modification of the amino acid from M to K at position 88.
+The protein's natural variant, known as in PC2 and SM;, features a modification of the amino acid from M to T at position 88.
+The protein's natural variant, known as in PC2, features a modification of the amino acid from L to P at position 91.
+The protein's natural variant, known as in PC2;, features a modification of the amino acid from N to D at position 92.
+The protein's natural variant, known as in SM;, features a modification of the amino acid from N to H at position 92.
+The protein's natural variant, known as in PC2;, features a modification of the amino acid from N to S at position 92.
+The protein's natural variant, known as in PC2 and SM;, features a modification of the amino acid from R to C at position 94.
+The protein's natural variant, known as in SM and PC2;, features a modification of the amino acid from R to H at position 94.
+The protein's natural variant, known as in PC2;, features a modification of the amino acid from R to P at position 94.
+The protein's natural variant, known as in PC2;, features a modification of the amino acid from L to P at position 95.
+The protein's natural variant, known as in PC2;, features a modification of the amino acid from L to Q at position 95.
+The protein's natural variant, known as in PC2;, features a modification of the amino acid from Y to D at position 98.
+The protein's natural variant, known as in PC2;, features a modification of the amino acid from L to P at position 99.
+The protein's natural variant, known as in PC2;, features a modification of the amino acid from V to M at position 102.
+The protein's natural variant, known as in PC2;, features a modification of the amino acid from N to D at position 109.
+The protein's natural variant, known as in PC2;, features a modification of the amino acid from L to P at position 388.
+The protein's natural variant, known as in PC2, features a modification of the amino acid from L to R at position 388.
+The protein's natural variant, known as in strain: P63, features a modification of the amino acid from I to V at position 138.
+The protein's natural variant, known as found in a clear cell renal carcinoma case; somatic mutation, features a modification of the amino acid from A to V at position 229.
+The protein's natural variant, known as found in a patient with global developmental delay; unknown pathological significance, features a modification of the amino acid from D to H at position 298.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from V to L at position 1293.
+The protein's natural variant, known as in HTGTI;, features a modification of the amino acid from R to P at position 229.
+The protein's natural variant, known as in strain: BH18/10, features a modification of the amino acid from Y to C at position 247.
+The natural variant of this protein is characterized by an amino acid alteration from R to C at position 33.
+The protein's natural variant, known as not a cause of male infertility;, features a modification of the amino acid from V to M at position 73.
+The protein's natural variant, known as in SPGF3; there is a reduced interactions with CFTR and complete failure to activate CFTR-dependent anion transport;, features a modification of the amino acid from R to Q at position 87.
+The protein's natural variant, known as not a cause of male infertility;, features a modification of the amino acid from I to V at position 148.
+The protein's natural variant, known as not a cause of male infertility;, features a modification of the amino acid from S to N at position 230.
+The protein's natural variant, known as not a cause of male infertility;, features a modification of the amino acid from I to V at position 639.
+The protein's natural variant, known as in SPGF3; there is a reduced interactions with CFTR and complete failure to activate CFTR-dependent anion transport;, features a modification of the amino acid from E to K at position 812.
+The protein's natural variant, known as in SPGF3; there is a reduced interactions with CFTR and complete failure to activate CFTR-dependent anion transport;, features a modification of the amino acid from R to C at position 954.
+The natural variant of this protein is characterized by an amino acid alteration from T to A at position 372.
+The protein's natural variant, known as found in a renal cell carcinoma sample; somatic mutation, features a modification of the amino acid from H to R at position 616.
+The protein's natural variant, known as in ICF4; unknown pathological significance;, features a modification of the amino acid from Q to R at position 699.
+The protein's natural variant, known as in NEDHLS, features a modification of the amino acid from T to A at position 26.
+The protein's natural variant, known as in NEDHLS, features a modification of the amino acid from C to G at position 29.
+The protein's natural variant, known as in NEDHLS, features a modification of the amino acid from A to P at position 41.
+The protein's natural variant, known as in NEDHLS, features a modification of the amino acid from R to W at position 64.
+The protein's natural variant, known as in NEDHLS, features a modification of the amino acid from D to Y at position 66.
+The protein's natural variant, known as in NEDHLS, features a modification of the amino acid from F to L at position 71.
+The protein's natural variant, known as in NEDHLS, features a modification of the amino acid from P to H at position 172.
+The protein's natural variant, known as in DFNB119, features a modification of the amino acid from G to V at position 176.
+The protein's natural variant, known as in NEDHLS, features a modification of the amino acid from V to E at position 245.
+The protein's natural variant, known as in NEDHLS, features a modification of the amino acid from F to S at position 360.
+The protein's natural variant, known as in NEDHLS, features a modification of the amino acid from V to E at position 364.
+The protein's natural variant, known as in NEDHLS, features a modification of the amino acid from T to I at position 400.
+The protein's natural variant, known as in NEDHLS, features a modification of the amino acid from L to P at position 438.
+The protein's natural variant, known as in DFNB119, features a modification of the amino acid from I to M at position 466.
+The protein's natural variant, known as in NEDHLS, features a modification of the amino acid from A to D at position 519.
+The protein's natural variant, known as in NEDHLS, features a modification of the amino acid from L to S at position 561.
+The protein's natural variant, known as in NEDHLS, features a modification of the amino acid from R to K at position 658.
+The protein's natural variant, known as in NEDHLS, features a modification of the amino acid from M to R at position 669.
+The protein's natural variant, known as in NEDHLS, features a modification of the amino acid from G to V at position 689.
+The protein's natural variant, known as in HTOCD; unknown pathological significance; displays gain of function; increased open state stability, reduced sensitivity to ATP inhibition and increased channel activity; almost completely abolishes high affinity sensitivity to glibenclamide, an inhibitor of ATP-sensitive potassium channels;, features a modification of the amino acid from V to M at position 65.
+The protein's natural variant, known as in HTOCD; unknown pathological significance; displays gain of function; displays reduced ATP sensitivity;, features a modification of the amino acid from C to S at position 176.
+The protein's natural variant, known as in SIDS; the mutant channel displays reduced potassium currents compared to wild type;, features a modification of the amino acid from V to I at position 346.
+The protein's natural variant, known as found in Brugada syndrome and other J-wave syndromes; unknown pathological significance; the mutant channel displays an increase in glibenclamide-sensitive potassium currents compared to wild type;, features a modification of the amino acid from S to L at position 422.
+The protein's natural variant, known as probable disease-associated variant found in a patient with autism spectrum disorder; decreased voltage-gated sodium channel activity; faster channel inactivation; loss of function, features a modification of the amino acid from D to N at position 12.
+The protein's natural variant, known as probable disease-associated variant found in a patient with autism spectrum disorder; decreased voltage-gated sodium channel activity; decreased expression; loss of function, features a modification of the amino acid from D to G at position 82.
+The protein's natural variant, known as in DEE11, features a modification of the amino acid from N to K at position 132.
+The protein's natural variant, known as in DEE11; responds to ketogenic diet, features a modification of the amino acid from M to I at position 136.
+The protein's natural variant, known as in DEE11, features a modification of the amino acid from E to G at position 169.
+The protein's natural variant, known as found in a patient with non-specific acute encephalopathy; unknown pathological significance;, features a modification of the amino acid from I to V at position 172.
+The protein's natural variant, known as in BFIS3; mutant channel inactivates more slowly than wild-type whereas the sodium channel conductance is not affected;, features a modification of the amino acid from R to W at position 188.
+The protein's natural variant, known as in DEE11; responds to ketogenic diet, features a modification of the amino acid from W to C at position 191.
+The protein's natural variant, known as probable disease-associated variant found in a patient with drug-resistant focal epilepsy;, features a modification of the amino acid from W to G at position 191.
+The protein's natural variant, known as in BFIS3; gain of function mutation; hyperpolarizing shift of the activation curve, features a modification of the amino acid from V to E at position 208.
+The protein's natural variant, known as in DEE11; the disease progresses to West syndrome, features a modification of the amino acid from G to D at position 211.
+The protein's natural variant, known as in DEE11; the disease progresses to West syndrome, features a modification of the amino acid from N to D at position 212.
+The protein's natural variant, known as in DEE11, features a modification of the amino acid from V to D at position 213.
+The protein's natural variant, known as in DEE11; unknown pathological significance, features a modification of the amino acid from T to K at position 218.
+The protein's natural variant, known as in DEE11, features a modification of the amino acid from R to G at position 220.
+The protein's natural variant, known as in BFIS3; increased voltage-gated sodium channel activity; modified voltage dependence of activation and inactivation; gain of function;, features a modification of the amino acid from R to Q at position 223.
+The protein's natural variant, known as in DEE11;, features a modification of the amino acid from T to S at position 236.
+The protein's natural variant, known as in BFIS3, features a modification of the amino acid from A to S at position 240.
+The protein's natural variant, known as in DEE11;, features a modification of the amino acid from V to I at position 251.
+The protein's natural variant, known as in BFIS3; increased voltage-gated sodium channel activity; increased persistent sodium current; gain of function;, features a modification of the amino acid from M to V at position 252.
+The protein's natural variant, known as in BFIS3; increased voltage-gated sodium channel activity; faster recovery from inactivation; gain of function;, features a modification of the amino acid from V to M at position 261.
+The protein's natural variant, known as in DEE11, features a modification of the amino acid from A to T at position 263.
+The protein's natural variant, known as in DEE11 and EA9; increased voltage-gated sodium channel activity; increased persistent sodium current; gain of function;, features a modification of the amino acid from A to V at position 263.
+The protein's natural variant, known as found in a patient with Dravet syndrome; unknown pathological significance, features a modification of the amino acid from D to N at position 322.
+The protein's natural variant, known as found in a patient with acute encephalopathy with biphasic seizures, late reduced diffusion and in a patient with Dravet syndrome; unknown pathological significance;, features a modification of the amino acid from F to V at position 328.
+The protein's natural variant, known as probable disease-associated variant found in a patient with autism spectrum disorder; loss of voltage-gated sodium channel activity; non-conducting; no dominant-negative effect, features a modification of the amino acid from R to H at position 379.
+The protein's natural variant, known as probable disease-associated variant found in a patient with early-onset seizures and Rett-like features, including autistic behavior, limited hand function with chorea and profound intellectual disability, features a modification of the amino acid from V to M at position 424.
+The protein's natural variant, known as in DEE11;, features a modification of the amino acid from E to G at position 430.
+The protein's natural variant, known as in BFIS3; unknown pathological significance, features a modification of the amino acid from E to Q at position 430.
+The protein's natural variant, known as probable disease-associated variant found in patients with GEFS+;, features a modification of the amino acid from A to T at position 467.
+The protein's natural variant, known as there is no significant effects on the voltage-dependence of the channel;, features a modification of the amino acid from A to V at position 575.
+The protein's natural variant, known as found in a patient with Dravet syndrome; unknown pathological significance, features a modification of the amino acid from D to N at position 649.
+The protein's natural variant, known as probable disease-associated variant found in a patient with autism spectrum disorder, features a modification of the amino acid from T to K at position 674.
+The protein's natural variant, known as in DEE11; hyperpolarizing shift of the activation curve and increased persitent current; gain of function, features a modification of the amino acid from T to I at position 773.
+The protein's natural variant, known as found in a patient with schizofrenia; unknown pathological significance, features a modification of the amino acid from R to P at position 850.
+The protein's natural variant, known as in DEE11; phenotype consistent with West syndrome; decreased neuronal excitability; decreased peak sodium current densities; loss of function;, features a modification of the amino acid from R to Q at position 853.
+The protein's natural variant, known as in DEE11, features a modification of the amino acid from R to L at position 856.
+The protein's natural variant, known as in DEE11, features a modification of the amino acid from I to M at position 873.
+The protein's natural variant, known as in DEE11; the disease progresses to West syndrome, features a modification of the amino acid from N to T at position 876.
+The protein's natural variant, known as in BFIS3;, features a modification of the amino acid from V to I at position 892.
+The protein's natural variant, known as in DEE11;, features a modification of the amino acid from A to V at position 896.
+The protein's natural variant, known as in DEE11;, features a modification of the amino acid from K to N at position 905.
+The protein's natural variant, known as in BFIS3; increased voltage-gated sodium channel activity; gain of function;, features a modification of the amino acid from K to E at position 908.
+The protein's natural variant, known as in DEE11; mild form with ataxia, features a modification of the amino acid from F to C at position 928.
+The protein's natural variant, known as probable disease-associated variant found in a patient with autism spectrum disorder; loss of voltage-gated sodium channel activity; non-conducting;, features a modification of the amino acid from R to C at position 937.
+The protein's natural variant, known as probable disease-associated variant found in a patient with autism spectrum disorder; loss of voltage-gated sodium channel activity; non-conducting;, features a modification of the amino acid from R to H at position 937.
+The protein's natural variant, known as found in a patient with autism; unknown pathological significance, features a modification of the amino acid from N to K at position 976.
+The protein's natural variant, known as in DEE11;, features a modification of the amino acid from S to I at position 987.
+The protein's natural variant, known as in DEE11; the disease progresses to West syndrome;, features a modification of the amino acid from E to K at position 999.
+The protein's natural variant, known as in DEE11, features a modification of the amino acid from E to V at position 999.
+The protein's natural variant, known as in BFIS3, features a modification of the amino acid from N to K at position 1001.
+The protein's natural variant, known as in BFIS3;, features a modification of the amino acid from L to I at position 1003.
+The protein's natural variant, known as found in a patient with acute encephalitis with refractory and repetitive partial seizures; unknown pathological significance;, features a modification of the amino acid from M to T at position 1128.
+The protein's natural variant, known as in DEE11; markedly altered channel voltage-dependence; responds to modified Atkins diet;, features a modification of the amino acid from E to K at position 1211.
+The protein's natural variant, known as in DEE11, features a modification of the amino acid from K to E at position 1260.
+The protein's natural variant, known as in DEE11, features a modification of the amino acid from K to Q at position 1260.
+The protein's natural variant, known as found in a patient with schizofrenia; unknown pathological significance;, features a modification of the amino acid from V to F at position 1282.
+The protein's natural variant, known as in DEE11; modified voltage-gated sodium channel activity; activated with lowered voltage sensitivity; disturbed fast and slow inactivation, features a modification of the amino acid from R to T at position 1312.
+The protein's natural variant, known as in DEE11;, features a modification of the amino acid from A to V at position 1316.
+The protein's natural variant, known as in BFIS3; modified voltage-gated sodium channel activity; modified voltage dependence of activation and inactivation;, features a modification of the amino acid from R to Q at position 1319.
+The protein's natural variant, known as in BFIS3; unknown pathological significance, features a modification of the amino acid from E to K at position 1321.
+The protein's natural variant, known as in DEE11; the disease progresses to West syndrome;, features a modification of the amino acid from M to V at position 1323.
+The protein's natural variant, known as in DEE11;, features a modification of the amino acid from V to D at position 1326.
+The protein's natural variant, known as in DEE11; the disease progresses to West syndrome, features a modification of the amino acid from V to L at position 1326.
+The protein's natural variant, known as in BFIS3; increased voltage-gated sodium channel activity; decreased overall channel availability during repetitive stimulation; gain of function; no effect on kinetics of activation or inactivation; no effect on voltage dependence of activation;, features a modification of the amino acid from L to F at position 1330.
+The protein's natural variant, known as in DEE11; the disease progresses to West syndrome, features a modification of the amino acid from S to Y at position 1336.
+The protein's natural variant, known as in DEE11, features a modification of the amino acid from M to T at position 1338.
+The protein's natural variant, known as in DEE11;, features a modification of the amino acid from L to P at position 1342.
+The protein's natural variant, known as in DEE11;, features a modification of the amino acid from C to Y at position 1344.
+The protein's natural variant, known as found in a patient with autism spectrum disorder; unknown pathological significance, features a modification of the amino acid from G to R at position 1372.
+The protein's natural variant, known as probable disease-associated variant found in a patient with autism spectrum disorder; loss of voltage-gated sodium channel activity; non-conducting, features a modification of the amino acid from C to R at position 1386.
+The protein's natural variant, known as probable disease-associated variant found in a patient with autism spectrum disorder; decreased voltage-gated sodium channel activity; faster channel inactivation; fewer channels contribution to macroscopic currents and fewer channels expressed on membrane;, features a modification of the amino acid from T to M at position 1420.
+The protein's natural variant, known as probable disease-associated variant found in a boy with infantile spasms and bitemporal glucose hypometabolism;, features a modification of the amino acid from K to E at position 1422.
+The protein's natural variant, known as probable disease-associated variant found in a patient with non-syndromic intellectual disability and epilepsy, features a modification of the amino acid from G to R at position 1460.
+The protein's natural variant, known as in DEE11; increased voltage-gated sodium channel activity; markedly altered the voltage-dependence of the channel; gain of function;, features a modification of the amino acid from I to M at position 1473.
+The protein's natural variant, known as in DEE11, features a modification of the amino acid from Q to P at position 1479.
+The protein's natural variant, known as in DEE11 and EA9; unknown pathological significance; no effect on voltage-gated sodium channel activity; higher current density when associated with G-1882;, features a modification of the amino acid from G to A at position 1522.
+The protein's natural variant, known as in BFIS3; unknown pathological significance, features a modification of the amino acid from Q to K at position 1531.
+The protein's natural variant, known as in DEE11;, features a modification of the amino acid from M to T at position 1548.
+The protein's natural variant, known as found in a patient with schizofrenia; unknown pathological significance;, features a modification of the amino acid from M to V at position 1559.
+The protein's natural variant, known as in BFIS3; increased voltage-gated sodium channel activity; impaired fast inactivation; no effect on kinetics of activation or inactivation; no effect on voltage dependence of activation; gain of function;, features a modification of the amino acid from L to V at position 1563.
+The protein's natural variant, known as in BFIS3; increased voltage-gated sodium channel activity; depolarized shift of steady-state inactivation; increased persistent sodium current; slower fast inactivation; accelerated recovery of fast inactivation; gain of function;, features a modification of the amino acid from Y to C at position 1589.
+The protein's natural variant, known as in DEE11;, features a modification of the amino acid from G to R at position 1593.
+The protein's natural variant, known as in BFIS3; unknown pathological significance, features a modification of the amino acid from I to S at position 1596.
+The protein's natural variant, known as in DEE11; the disease progresses to West syndrome, features a modification of the amino acid from T to N at position 1623.
+The protein's natural variant, known as in DEE11, features a modification of the amino acid from R to L at position 1629.
+The protein's natural variant, known as in EA9; unknown pathological significance;, features a modification of the amino acid from G to D at position 1634.
+The protein's natural variant, known as in DEE11, features a modification of the amino acid from G to V at position 1634.
+The protein's natural variant, known as in BFIS3; unknown pathological significance;, features a modification of the amino acid from K to N at position 1641.
+The protein's natural variant, known as in DEE11; also found in patients with familial episodic ataxia and impairment of speech development, features a modification of the amino acid from L to P at position 1650.
+The protein's natural variant, known as in DEE11, features a modification of the amino acid from L to W at position 1660.
+The protein's natural variant, known as probable disease-associated variant found in a patient with autism spectrum disorder, features a modification of the amino acid from G to R at position 1744.
+The protein's natural variant, known as found in a patient with schizofrenia; unknown pathological significance;, features a modification of the amino acid from D to A at position 1823.
+The protein's natural variant, known as in DEE11;, features a modification of the amino acid from L to F at position 1829.
+The protein's natural variant, known as in DEE11, features a modification of the amino acid from H to R at position 1853.
+The protein's natural variant, known as in EA9; gain of function mutation resulting in increased voltage-gated sodium channel activity; hyperpolarized activation; higher current density when associated with A-1522 compared to wild-type or G-1882 alone;, features a modification of the amino acid from R to G at position 1882.
+The protein's natural variant, known as in DEE11;, features a modification of the amino acid from R to L at position 1882.
+The protein's natural variant, known as in DEE11; increased neuronal excitability; increased peak sodium current densities; gain of function;, features a modification of the amino acid from R to Q at position 1882.
+The protein's natural variant, known as found in autism; unknown pathological significance, features a modification of the amino acid from R to T at position 1902.
+The protein's natural variant, known as in strain: ST 855, features a modification of the amino acid from V to A at position 263.
+The protein's natural variant, known as in strain: ST 855, features a modification of the amino acid from A to T at position 277.
+The protein's natural variant, known as in strain: ST 855, features a modification of the amino acid from A to V at position 281.
+The protein's natural variant, known as in strain: ST 855, features a modification of the amino acid from F to S at position 320.
+The protein's natural variant, known as in strain: ST 855, features a modification of the amino acid from Q to H at position 339.
+The protein's natural variant, known as in strain: ST 855, features a modification of the amino acid from R to T at position 359.
+The protein's natural variant, known as in strain: ST 855, features a modification of the amino acid from K to N at position 391.
+The protein's natural variant, known as in strain: ST 855, features a modification of the amino acid from S to R at position 532.
+The protein's natural variant, known as in strain: ST 855, features a modification of the amino acid from PN to HE at position 554.
+The protein's natural variant, known as found in patients with Inflammatory bowel disease; unknown pathological significance; does dot affect protein sialyltransferase activity;, features a modification of the amino acid from T to P at position 207.
+The protein's natural variant, known as found in patients with Inflammatory bowel disease; unknown pathological significance; reduced protein sialyltransferase activity;, features a modification of the amino acid from R to C at position 341.
+The protein's natural variant, known as probable disease-associated variant found in patients with Inflammatory bowel disease; impaired localization to the Golgi apparatus; abolished protein sialyltransferase activity, features a modification of the amino acid from R to Q at position 391.
+The protein's natural variant, known as found in patients with Inflammatory bowel disease; unknown pathological significance; reduced protein sialyltransferase activity;, features a modification of the amino acid from T to M at position 462.
+The protein's natural variant, known as in a neuroblastoma sample;, features a modification of the amino acid from R to H at position 351.
+The protein's natural variant, known as in a neuroblastoma sample, features a modification of the amino acid from K to E at position 489.
+The protein's natural variant, known as in MRMV4; changed localization; exclusively detected in the cytoplasm;, features a modification of the amino acid from C to R at position 601.
+The protein's natural variant, known as in MRMV4; changed localization; exclusively detected in the cytoplasm;, features a modification of the amino acid from C to S at position 601.
+The natural variant of this protein is characterized by an amino acid alteration from V to L at position 262.
+The protein's natural variant, known as found in a patient with intellectual disability; unknown pathological significance, features a modification of the amino acid from G to A at position 48.
+The protein's natural variant, known as in strain: 405 / Serotype 8, features a modification of the amino acid from R to A at position 44.
+The protein's natural variant, known as in strain: 405 / Serotype 8, features a modification of the amino acid from C to A at position 132.
+The protein's natural variant, known as in strain: 405 / Serotype 8, features a modification of the amino acid from GA to NT at position 186.
+The protein's natural variant, known as in strain: 405 / Serotype 8, features a modification of the amino acid from V to I at position 376.
+The protein's natural variant, known as in strain: KY02-C351 and KY02-C372, features a modification of the amino acid from K to N at position 5.
+The protein's natural variant, known as in strain: AK17, Berkeley, Canton-S, EP(X)496, KY02-C304, KY02-C305, KY02-C312, KY02-C341, KY02-C419, KY02-C470 and w cx, features a modification of the amino acid from I to V at position 19.
+The protein's natural variant, known as in strain: KY02-C331, KY02-C392 and Oregon-R, features a modification of the amino acid from M to I at position 23.
+The protein's natural variant, known as in strain: KY02-C493, features a modification of the amino acid from P to S at position 59.
+The protein's natural variant, known as in strain: KY02-C301, KY02-C302, KY02-C308, KY02-C309, KY02-C310, KY02-C311, KY02-C314, KY02-C315, KY02-C319, KY02-C320, KY02-C325, KY02-C327, KY02-C330, KY02-C332, KY02-C335, KY02-C337, KY02-C342, KY02-C343, KY02-C344, KY02-C346, KY02-C347, KY02-C349, KY02-C351, KY02-C352, KY02-C353, KY02-C355, KY02-C358, KY02-C361, KY02-C367, KY02-C368, KY02-C372, KY02-C374, KY02-C376, KY02-C377, KY02-C378, KY02-C379, KY02-C380, KY02-C381, KY02-C382, KY02-C383, KY02-C384, KY02-C388, KY02-C389, KY02-C390, KY02-C393, KY02-C396, KY02-C400, KY02-C402, KY02-C404, KY02-C411, KY02-C412, KY02-C413, KY02-C414, KY02-C420, KY02-C425, KY02-C426, KY02-C429, KY02-C432, KY02-C433, KY02-C434, KY02-C435, KY02-C436, KY02-C439, KY02-C441, KY02-C446, KY02-C447, KY02-C449, KY02-C451, KY02-C453, KY02-C457, KY02-C460, KY02-C462, KY02-C463, KY02-C467, KY02-C469, KY02-C476, KY02-C477, KY02-C480, KY02-C483, KY02-C484, KY02-C485, KY02-C486, KY02-C488, KY02-C490, KY02-C491, KY02-C492, KY02-C493, KY02-C494, KY02-C496, KY02-C497, KY02-C500, KY02-C504, KY02-C508, KY02-C510, KY02-C511, KY02-C514, KY02-C515, KY02-C516, KY02-C517, KY02-C519, KY02-C520 and Singapore, features a modification of the amino acid from C to S at position 73.
+The protein's natural variant, known as in strain: KY02-C302, KY02-C316, KY02-C346, KY02-C350, KY02-C351, KY02-C374, KY02-C379, KY02-C380, KY02-C384, KY02-C390, KY02-C396, KY02-C407, KY02-C425, KY02-C428, KY02-C439, KY02-C443, KY02-C456, KY02-C463, KY02-C478, KY02-C493, KY02-C497, KY02-C500, KY02-C504, KY02-C517 and Singapore, features a modification of the amino acid from T to A at position 164.
+The protein's natural variant, known as in strain: KY02-C336, features a modification of the amino acid from V to I at position 185.
+The protein's natural variant, known as in strain: AK10, KY02-C315, KY02-C335, KY02-C402, KY02-C469, KY02-C516, KY02-C310, KY02-C319, KY02-C320, KY02-C330, KY02-C336, KY02-C342, KY02-C347, KY02-C355, KY02-C358, KY02-C382, KY02-C393, KY02-C404, KY02-C411, KY02-C432, KY02-C435, KY02-C449, KY02-C467, KY02-C483, KY02-C486, KY02-C488, KY02-C492, KY02-C496, KY02-C514, KY02-C519, Tananarive and w cv, features a modification of the amino acid from L to H at position 216.
+The protein's natural variant, known as in strain: AK07, AK10, AK13, KY02-C351, KY02-C439, KY02-C510, KY02-C301, KY02-C302, KY02-C303, KY02-C304, KY02-C308, KY02-C310, KY02-C311, KY02-C315, KY02-C316, KY02-C319, KY02-C320, KY02-C325, KY02-C326, KY02-C330, KY02-C331, KY02-C332, KY02-C335, KY02-C336, KY02-C341, KY02-C342, KY02-C346, KY02-C347, KY02-C348, KY02-C349, KY02-C350, KY02-C352, KY02-C355, KY02-C356, KY02-C358, KY02-C359, KY02-C361, KY02-C362, KY02-C367, KY02-C372, KY02-C373, KY02-C374, KY02-C376, KY02-C378, KY02-C380, KY02-C382, KY02-C383, KY02-C384, KY02-C387, KY02-C388, KY02-C390, KY02-C392, KY02-C393, KY02-C394, KY02-C400, KY02-C402, KY02-C404, KY02-C407, KY02-C411, KY02-C412, KY02-C413, KY02-C417, KY02-C419, KY02-C421, KY02-C426, KY02-C428, KY02-C432, KY02-C433, KY02-C434, KY02-C435, KY02-C441, KY02-C443, KY02-C446, KY02-C449, KY02-C451, KY02-C453, KY02-C454, KY02-C456, KY02-C457, KY02-C460, KY02-C462, KY02-C463, KY02-C467, KY02-C469, KY02-C470, KY02-C477, KY02-C478, KY02-C480, KY02-C483, KY02-C484, KY02-C485, KY02-C486, KY02-C488, KY02-C489, KY02-C490, KY02-C492, KY02-C493, KY02-C494, KY02-C496, KY02-C497, KY02-C500, KY02-C504, KY02-C511, KY02-C513, KY02-C514, KY02-C515, KY02-C516, KY02-C517, KY02-C519, KY02-C520, Oregon-R, Singapore, Tananarive and w cv; decreased sensitivity to trehalose, features a modification of the amino acid from A to T at position 218.
+The protein's natural variant, known as in strain: KY02-C316, KY02-C350, KY02-C428, KY02-C443, KY02-C456 and KY02-C478, features a modification of the amino acid from S to N at position 248.
+The protein's natural variant, known as in strain: KY02-C304, KY02-C341, KY02-C419 and KY02-C470, features a modification of the amino acid from R to L at position 277.
+The protein's natural variant, known as in strain: KY02-C326, KY02-C348, KY02-C359, KY02-C362, KY02-C373, KY02-C394, KY02-C417, KY02-C434, KY02-C448, KY02-C451, KY02-C477 and KY02-C513, features a modification of the amino acid from P to S at position 333.
+The natural variant of this protein is characterized by an amino acid alteration from T to A at position 324.
+The natural variant of this protein is characterized by an amino acid alteration from R to K at position 60.
+The protein's natural variant, known as in strain: Isolate S59, features a modification of the amino acid from N to I at position 212.
+The protein's natural variant, known as in strain: Isolate S59, features a modification of the amino acid from D to E at position 252.
+The protein's natural variant, known as in strain: Isolate S59, features a modification of the amino acid from L to F at position 333.
+The protein's natural variant, known as probable disease-associated variant found in a patient with progressive spastic paraparesis and other neurological symptoms; enhances receptor surface expression; increases the constitutive signaling activity; does not affect interaction with GNAZ; promotes enhanced interaction with GNAI1; decreases interaction with SH3GL2;, features a modification of the amino acid from R to W at position 1465.
+The protein's natural variant, known as in MRT73; decreased complex formation with NAA25 and decreased N-acetylation catalytic activity in vitro for all 4 types of substrates; does not affect protein stability, features a modification of the amino acid from M to V at position 54.
+The protein's natural variant, known as in MRT73; strong decrease in N-acetylation catalytic activity in vitro for substrates Met-Glu, Met-Asn and Met-Gln, but not Met-Asp; does not affect protein stability, features a modification of the amino acid from A to V at position 80.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from R to C at position 1514.
+The protein's natural variant, known as in aequorin-3, features a modification of the amino acid from EA to GD at position 71.
+The protein's natural variant, known as in aequorin-3, features a modification of the amino acid from S to N at position 164.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from V to I at position 450.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from E to G at position 80.
+The protein's natural variant, known as found in a patient with syndromic developmental delay; unknown pathological significance, features a modification of the amino acid from M to L at position 195.
+The protein's natural variant, known as in strain: Isolate TCWC42413, features a modification of the amino acid from A to T at position 23.
+The protein's natural variant, known as in strain: Wistar, features a modification of the amino acid from Q to L at position 8.
+The protein's natural variant, known as in strain: Wistar, features a modification of the amino acid from D to G at position 89.
+The protein's natural variant, known as in strain: Wistar, features a modification of the amino acid from T to S at position 153.
+The protein's natural variant, known as in strain: Wistar, features a modification of the amino acid from G to A at position 179.
+The protein's natural variant, known as in strain: Wistar, features a modification of the amino acid from T to I at position 387.
+The natural variant of this protein is characterized by an amino acid alteration from Y to H at position 42.
+The protein's natural variant, known as decreased catalytic efficiency toward benzamidoxime; no effect on affinity for benzamidoxime; no effect on binding of the molybdenum cofactor;, features a modification of the amino acid from G to S at position 244.
+The protein's natural variant, known as decreased catalytic activity toward benzamidoxime; no effect on affinity for benzamidoxime; no effect on binding of the molybdenum cofactor;, features a modification of the amino acid from C to W at position 245.
+The protein's natural variant, known as in Lec15.1/B4-2-1 cell line, features a modification of the amino acid from G to E at position 10.
+The protein's natural variant, known as in RMS; impairs transport to the plasma membrane and reduces the affinity to bind insulin;, features a modification of the amino acid from N to K at position 42.
+The protein's natural variant, known as in LEPRCH; Verona-1;, features a modification of the amino acid from V to A at position 55.
+The protein's natural variant, known as in LEPRCH; abolishes post-translational processing;, features a modification of the amino acid from I to T at position 56.
+The protein's natural variant, known as in LEPRCH; Helmond; inhibits processing and transport;, features a modification of the amino acid from G to R at position 58.
+The protein's natural variant, known as in IRAN type A, features a modification of the amino acid from D to G at position 86.
+The protein's natural variant, known as in IRAN type A, features a modification of the amino acid from L to P at position 89.
+The protein's natural variant, known as in LEPRCH; Atlanta-1; abolishes insulin binding;, features a modification of the amino acid from R to P at position 113.
+The protein's natural variant, known as in LEPRCH; markedly impairs insulin binding;, features a modification of the amino acid from A to V at position 119.
+The protein's natural variant, known as in LEPRCH; inhibits receptor processing, features a modification of the amino acid from L to Q at position 120.
+The protein's natural variant, known as in LEPRCH; mild;, features a modification of the amino acid from I to M at position 146.
+The protein's natural variant, known as in IRAN type A;, features a modification of the amino acid from V to L at position 167.
+The protein's natural variant, known as in Ins resistance; severe;, features a modification of the amino acid from P to L at position 220.
+The protein's natural variant, known as in a gastric adenocarcinoma sample; somatic mutation, features a modification of the amino acid from C to R at position 228.
+The protein's natural variant, known as in RMS and LEPRCH; Winnipeg; may impair receptor processing;, features a modification of the amino acid from H to R at position 236.
+The protein's natural variant, known as in RMS;, features a modification of the amino acid from R to C at position 256.
+The protein's natural variant, known as in LEPRCH; Geldeimalsen;, features a modification of the amino acid from L to P at position 260.
+The protein's natural variant, known as in IRAN type A; inhibits receptor internalization;, features a modification of the amino acid from R to C at position 279.
+The protein's natural variant, known as in IRAN type A; interferes with receptor processing;, features a modification of the amino acid from R to H at position 279.
+The protein's natural variant, known as in IRAN type A, features a modification of the amino acid from C to Y at position 280.
+The protein's natural variant, known as in LEPRCH; abolishes post-translational processing, features a modification of the amino acid from C to Y at position 286.
+The protein's natural variant, known as in LEPRCH, features a modification of the amino acid from C to Y at position 301.
+The protein's natural variant, known as in RMS and LEPRCH, features a modification of the amino acid from S to L at position 350.
+The protein's natural variant, known as in RMS; may impair receptor processing;, features a modification of the amino acid from G to S at position 386.
+The protein's natural variant, known as in LEPRCH; Verona-1;, features a modification of the amino acid from G to R at position 393.
+The protein's natural variant, known as in IRAN type A;, features a modification of the amino acid from F to V at position 409.
+The protein's natural variant, known as in LEPRCH; impairs transport of the receptor to the cell surface;, features a modification of the amino acid from W to S at position 439.
+The protein's natural variant, known as in LEPRCH; partially inhibits receptor processing and autophosphorylation; strongly impairs ERK phosphorylation; induces wild-type levels of IRS-1 phosphorylation;, features a modification of the amino acid from N to D at position 458.
+The protein's natural variant, known as in LEPRCH; ARK-1;, features a modification of the amino acid from K to E at position 487.
+The protein's natural variant, known as in IRAN type A; unknown pathological significance;, features a modification of the amino acid from N to D at position 489.
+The protein's natural variant, known as in IRAN type A;, features a modification of the amino acid from N to S at position 489.
+The natural variant of this protein is characterized by an amino acid alteration from Q to K at position 492.
+The protein's natural variant, known as in RMS; decreases post-translational processing, features a modification of the amino acid from S to L at position 635.
+The protein's natural variant, known as in LEPRCH; impairs post-translational processing;, features a modification of the amino acid from V to F at position 657.
+The protein's natural variant, known as in LEPRCH; impairs post-translational processing, features a modification of the amino acid from W to R at position 659.
+The protein's natural variant, known as in IRAN type A;, features a modification of the amino acid from R to S at position 762.
+The protein's natural variant, known as in LEPRCH; abolishes post-translational processing, features a modification of the amino acid from Y to C at position 818.
+The protein's natural variant, known as in RMS; impairs post-translational processing;, features a modification of the amino acid from S to I at position 835.
+The protein's natural variant, known as in RMS; decreases post-translational processing;, features a modification of the amino acid from A to V at position 842.
+The protein's natural variant, known as in T2D;, features a modification of the amino acid from T to A at position 858.
+The protein's natural variant, known as in RMS; impairs post-translational processing, features a modification of the amino acid from P to L at position 874.
+The protein's natural variant, known as in RMS; impairs post-translational processing;, features a modification of the amino acid from N to S at position 878.
+The protein's natural variant, known as in LEPRCH; abolishes post-translational processing; abolishes insulin binding;, features a modification of the amino acid from I to T at position 925.
+The protein's natural variant, known as in LEPRCH; markedly impairs insulin binding;impairs post-translational processing;, features a modification of the amino acid from R to W at position 926.
+The protein's natural variant, known as in LEPRCH; impaired receptor processing; impairs post-translational processing, features a modification of the amino acid from T to M at position 937.
+The protein's natural variant, known as in RMS; reduces insulin binding, features a modification of the amino acid from P to T at position 997.
+The protein's natural variant, known as in IRAN type A;, features a modification of the amino acid from R to Q at position 1020.
+The natural variant of this protein is characterized by an amino acid alteration from I to F at position 1023.
+The protein's natural variant, known as in IRAN type A;, features a modification of the amino acid from G to V at position 1035.
+The protein's natural variant, known as in IRAN type A; unknown pathological significance;, features a modification of the amino acid from V to M at position 1054.
+The protein's natural variant, known as in IRAN type A;, features a modification of the amino acid from A to V at position 1055.
+The protein's natural variant, known as in IRAN type A, features a modification of the amino acid from A to D at position 1075.
+The protein's natural variant, known as in a subject with non-insulin dependent diabetes mellitus;, features a modification of the amino acid from K to E at position 1095.
+The protein's natural variant, known as in LEPRCH;, features a modification of the amino acid from R to W at position 1119.
+The protein's natural variant, known as in RMS; reduces insulin binding, features a modification of the amino acid from I to T at position 1143.
+The protein's natural variant, known as in T2D, features a modification of the amino acid from R to Q at position 1158.
+The protein's natural variant, known as in RMS; abolishes insulin binding;, features a modification of the amino acid from R to W at position 1158.
+The protein's natural variant, known as in IRAN type A;, features a modification of the amino acid from A to T at position 1161.
+The protein's natural variant, known as in IRAN type A; impairs proteolytic processing;, features a modification of the amino acid from A to E at position 1162.
+The protein's natural variant, known as in a patient with insulin resistance;, features a modification of the amino acid from M to I at position 1180.
+The protein's natural variant, known as in T2D;, features a modification of the amino acid from R to Q at position 1191.
+The protein's natural variant, known as in HHF5 and IRAN type A; interferes with kinase activation by insulin;, features a modification of the amino acid from R to Q at position 1201.
+The protein's natural variant, known as in LEPRCH and RMS; reduces insulin binding possibly due to reduced receptor levels on the cell surface;, features a modification of the amino acid from R to W at position 1201.
+The protein's natural variant, known as in IRAN type A; moderate;, features a modification of the amino acid from P to L at position 1205.
+The protein's natural variant, known as in IRAN type A; accelerates degradation of the protein and impairs kinase activity, features a modification of the amino acid from E to D at position 1206.
+The protein's natural variant, known as in LEPRCH, features a modification of the amino acid from E to K at position 1206.
+The protein's natural variant, known as in IRAN type A; accelerates degradation of the protein and impairs kinase activity;, features a modification of the amino acid from W to L at position 1220.
+The protein's natural variant, known as in IRAN type A;, features a modification of the amino acid from W to S at position 1227.
+The protein's natural variant, known as in IRAN type A;, features a modification of the amino acid from R to Q at position 1378.
+The protein's natural variant, known as in a glioblastoma multiforme sample; somatic mutation, features a modification of the amino acid from G to E at position 30.
+The protein's natural variant, known as in a gastric adenocarcinoma sample; somatic mutation, features a modification of the amino acid from R to G at position 558.
+The protein's natural variant, known as in a glioblastoma multiforme sample; somatic mutation, features a modification of the amino acid from P to L at position 714.
+The natural variant of this protein is characterized by an amino acid alteration from M to T at position 112.
+The natural variant of this protein is characterized by an amino acid alteration from A to T at position 136.
+The protein's natural variant, known as in scrapie; short incubation; sA allele, features a modification of the amino acid from A to V at position 136.
+The natural variant of this protein is characterized by an amino acid alteration from M to T at position 137.
+The natural variant of this protein is characterized by an amino acid alteration from L to F at position 141.
+The natural variant of this protein is characterized by an amino acid alteration from R to H at position 154.
+The protein's natural variant, known as in scrapie; low incidence, features a modification of the amino acid from R to H at position 171.
+The natural variant of this protein is characterized by an amino acid alteration from R to K at position 171.
+The protein's natural variant, known as linked to susceptibility to scrapie, features a modification of the amino acid from R to Q at position 171.
+The natural variant of this protein is characterized by an amino acid alteration from R to Q at position 211.
+The protein's natural variant, known as in strain: B, features a modification of the amino acid from E to D at position 75.
+The protein's natural variant, known as in strain: B, features a modification of the amino acid from AQ to PR at position 80.
+The protein's natural variant, known as in strain: B, features a modification of the amino acid from I to V at position 318.
+The protein's natural variant, known as in strain: B, features a modification of the amino acid from T to S at position 330.
+The protein's natural variant, known as in strain: KD735-15, features a modification of the amino acid from K to R at position 7.
+The protein's natural variant, known as in strain: KD735-15, features a modification of the amino acid from N to S at position 41.
+The protein's natural variant, known as in strain: KD735-15, features a modification of the amino acid from N to D at position 110.
+The protein's natural variant, known as in strain: KD735-15, features a modification of the amino acid from S to A at position 127.
+The protein's natural variant, known as in strain: KD735-15, features a modification of the amino acid from Y to N at position 547.
+The protein's natural variant, known as in CHAR;, features a modification of the amino acid from P to R at position 73.
+The protein's natural variant, known as in CHAR;, features a modification of the amino acid from R to C at position 236.
+The protein's natural variant, known as in CHAR;, features a modification of the amino acid from R to S at position 236.
+The protein's natural variant, known as in CHAR;, features a modification of the amino acid from A to D at position 275.
+The protein's natural variant, known as in CHAR;, features a modification of the amino acid from R to Q at position 285.
+The protein's natural variant, known as in CHAR;, features a modification of the amino acid from R to C at position 300.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from E to D at position 269.
+The protein's natural variant, known as affecting milk fat and protein concentration, features a modification of the amino acid from Y to S at position 578.
+The protein's natural variant, known as in alloantigen HPA-5B;, features a modification of the amino acid from E to K at position 534.
+The natural variant of this protein is characterized by an amino acid alteration from L to I at position 4.
+The natural variant of this protein is characterized by an amino acid alteration from L to P at position 4.
+The natural variant of this protein is characterized by an amino acid alteration from N to H at position 9.
+The natural variant of this protein is characterized by an amino acid alteration from R to G at position 11.
+The natural variant of this protein is characterized by an amino acid alteration from K to R at position 20.
+The natural variant of this protein is characterized by an amino acid alteration from E to D at position 45.
+The natural variant of this protein is characterized by an amino acid alteration from F to V at position 60.
+The natural variant of this protein is characterized by an amino acid alteration from N to K at position 61.
+The natural variant of this protein is characterized by an amino acid alteration from Q to E at position 80.
+The natural variant of this protein is characterized by an amino acid alteration from R to H at position 131.
+The natural variant of this protein is characterized by an amino acid alteration from P to S at position 133.
+The natural variant of this protein is characterized by an amino acid alteration from R to M at position 145.
+The natural variant of this protein is characterized by an amino acid alteration from R to K at position 155.
+The protein's natural variant, known as in CMM6; risk factor for disease development;, features a modification of the amino acid from T to M at position 241.
+The protein's natural variant, known as in strain: IFO 14297, features a modification of the amino acid from P to N at position 39.
+The protein's natural variant, known as in strain: IFO 14297, features a modification of the amino acid from E to K at position 184.
+The protein's natural variant, known as in strain: IFO 14297, features a modification of the amino acid from E to K at position 197.
+The protein's natural variant, known as in strain: IFO 14297, features a modification of the amino acid from P to L at position 313.
+The protein's natural variant, known as in strain: IFO 14297, features a modification of the amino acid from G to A at position 354.
+The protein's natural variant, known as in strain: IFO 14297, features a modification of the amino acid from Q to H at position 444.
+The protein's natural variant, known as in CBD;, features a modification of the amino acid from N to K at position 94.
+The protein's natural variant, known as in COD5; results in protein misfolding and retention in the endoplasmic reticulum;, features a modification of the amino acid from W to R at position 177.
+The protein's natural variant, known as in CBD and BCM;, features a modification of the amino acid from C to R at position 203.
+The protein's natural variant, known as in CBD;, features a modification of the amino acid from R to Q at position 330.
+The protein's natural variant, known as in strain: Isolate 704, features a modification of the amino acid from M to V at position 9.
+The protein's natural variant, known as in strain: Isolate 704, features a modification of the amino acid from R to H at position 52.
+The protein's natural variant, known as in strain: Isolate 704, features a modification of the amino acid from N to S at position 94.
+The protein's natural variant, known as in strain: 197, features a modification of the amino acid from I to T at position 56.
+The protein's natural variant, known as in strain: 197, features a modification of the amino acid from ENI to QNV at position 201.
+The protein's natural variant, known as in strain: Lig72, features a modification of the amino acid from L to M at position 302.
+The protein's natural variant, known as in strain: Lig74, features a modification of the amino acid from A to S at position 355.
+The protein's natural variant, known as in strain: Lig74, features a modification of the amino acid from E to Q at position 391.
+The protein's natural variant, known as in strain: Lig74, features a modification of the amino acid from L to I at position 394.
+The protein's natural variant, known as in strain: 197, features a modification of the amino acid from N to K at position 494.
+The protein's natural variant, known as in strain: Lig72, features a modification of the amino acid from L to M at position 496.
+The protein's natural variant, known as in CA5AD; decreased carbonate dehydratase activity; decreased protein thermal stability;, features a modification of the amino acid from S to P at position 233.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 76.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from V to M at position 95.
+The natural variant of this protein is characterized by an amino acid alteration from N to D at position 17.
+The natural variant of this protein is characterized by an amino acid alteration from E to A at position 122.
+The protein's natural variant, known as in hp1; induces exaggerated light responsiveness, features a modification of the amino acid from N to Y at position 311.
+The protein's natural variant, known as in trypsins IA/IB, features a modification of the amino acid from T to A at position 33.
+The protein's natural variant, known as in LGMDR3;, features a modification of the amino acid from P to L at position 30.
+The protein's natural variant, known as in LGMDR3;, features a modification of the amino acid from L to P at position 31.
+The protein's natural variant, known as in LGMDR3;, features a modification of the amino acid from R to C at position 34.
+The protein's natural variant, known as in LGMDR3;, features a modification of the amino acid from R to H at position 34.
+The protein's natural variant, known as in LGMDR3, features a modification of the amino acid from Y to H at position 62.
+The protein's natural variant, known as in LGMDR3, features a modification of the amino acid from G to E at position 68.
+The protein's natural variant, known as in LGMDR3;, features a modification of the amino acid from R to W at position 74.
+The protein's natural variant, known as in LGMDR3;, features a modification of the amino acid from L to F at position 76.
+The protein's natural variant, known as in LGMDR3;, features a modification of the amino acid from R to C at position 77.
+The protein's natural variant, known as in LGMDR3;, features a modification of the amino acid from R to C at position 81.
+The protein's natural variant, known as in LGMDR3;, features a modification of the amino acid from L to P at position 89.
+The protein's natural variant, known as in LGMDR3, features a modification of the amino acid from G to R at position 91.
+The protein's natural variant, known as in LGMDR3, features a modification of the amino acid from A to V at position 93.
+The protein's natural variant, known as in LGMDR3;, features a modification of the amino acid from D to G at position 97.
+The protein's natural variant, known as in LGMDR3;, features a modification of the amino acid from R to C at position 98.
+The protein's natural variant, known as in LGMDR3;, features a modification of the amino acid from R to H at position 98.
+The protein's natural variant, known as in LGMDR3;, features a modification of the amino acid from I to T at position 103.
+The protein's natural variant, known as in LGMDR3;, features a modification of the amino acid from I to T at position 124.
+The protein's natural variant, known as in LGMDR3; associated with G-137, features a modification of the amino acid from A to APGAQP at position 136.
+The protein's natural variant, known as in LGMDR3; associated with P-G-A-Q-P-136 ins;, features a modification of the amino acid from E to G at position 137.
+The protein's natural variant, known as in LGMDR3;, features a modification of the amino acid from E to K at position 137.
+The protein's natural variant, known as in LGMDR3, features a modification of the amino acid from L to F at position 158.
+The protein's natural variant, known as in LGMDR3;, features a modification of the amino acid from L to P at position 173.
+The protein's natural variant, known as in LGMDR3;, features a modification of the amino acid from V to A at position 175.
+The protein's natural variant, known as in LGMDR3;, features a modification of the amino acid from V to I at position 196.
+The protein's natural variant, known as in LGMDR3;, features a modification of the amino acid from P to H at position 205.
+The protein's natural variant, known as in LGMDR3, features a modification of the amino acid from P to Q at position 228.
+The protein's natural variant, known as in LGMDR3;, features a modification of the amino acid from V to A at position 242.
+The protein's natural variant, known as in LGMDR3;, features a modification of the amino acid from V to M at position 247.
+The protein's natural variant, known as in LGMDR3;, features a modification of the amino acid from R to C at position 284.
+The protein's natural variant, known as in AMC2; unknown pathological significance;, features a modification of the amino acid from V to E at position 98.
+The protein's natural variant, known as retains phosphatase activity towards Ins(1,3,4,5)P4 and PtdIns(3,4,5)P3; retains the ability to bind phospholipid membranes, features a modification of the amino acid from S to N at position 10.
+The protein's natural variant, known as in glioma;, features a modification of the amino acid from R to S at position 15.
+The protein's natural variant, known as loss of phosphatase activity towards Ins(1,3,4,5)P4; retains the ability to bind phospholipid membranes, features a modification of the amino acid from Y to C at position 16.
+The protein's natural variant, known as in malignant melanoma; somatic mutation;, features a modification of the amino acid from D to N at position 19.
+The protein's natural variant, known as reduced phosphatase activity towards Ins(1,3,4,5)P4; retains phosphatase activity towards PtdIns(3,4,5)P3;, features a modification of the amino acid from G to E at position 20.
+The protein's natural variant, known as loss of phosphatase activity towards Ins(1,3,4,5)P4;, features a modification of the amino acid from Y to S at position 27.
+The protein's natural variant, known as in CWS1, features a modification of the amino acid from A to D at position 34.
+The protein's natural variant, known as in CWS1;, features a modification of the amino acid from M to R at position 35.
+The protein's natural variant, known as in glioma;, features a modification of the amino acid from G to E at position 36.
+The protein's natural variant, known as in endometrial hyperplasia;, features a modification of the amino acid from G to R at position 36.
+The protein's natural variant, known as in glioma; retains phosphatase activity towards Ins(1,3,4,5)P4 and PtdIns(3,4,5)P3; retains the ability to bind phospholipid membranes, features a modification of the amino acid from L to R at position 42.
+The protein's natural variant, known as in CWS1;, features a modification of the amino acid from R to G at position 47.
+The protein's natural variant, known as in glioma; loss of protein phosphatase activity;, features a modification of the amino acid from L to W at position 57.
+The protein's natural variant, known as foun in a patient with macrocephaly, ventriculomegaly, vertebral anomalies, anal atresia, congenital cardiac disease, tracheoesophageal fistula, renal anomalies, radial dysplasia and other limb defects; unknown pathological significance;, features a modification of the amino acid from H to D at position 61.
+The protein's natural variant, known as loss of phosphatase activity towards Ins(1,3,4,5)P4;, features a modification of the amino acid from H to R at position 61.
+The protein's natural variant, known as in CWS1, features a modification of the amino acid from I to R at position 67.
+The protein's natural variant, known as in CWS1; loss of phosphatase activity towards Ins(1,3,4,5)P4 and PtdIns(3,4,5)P3; retains the ability to bind phospholipid membranes;, features a modification of the amino acid from Y to H at position 68.
+The protein's natural variant, known as in CWS1;, features a modification of the amino acid from L to P at position 70.
+The protein's natural variant, known as in CWS1; loss of phosphatase activity towards Ins(1,3,4,5)P4, features a modification of the amino acid from C to Y at position 71.
+The protein's natural variant, known as in MCEPHAS;, features a modification of the amino acid from H to R at position 93.
+The protein's natural variant, known as in CWS1;, features a modification of the amino acid from H to Y at position 93.
+The protein's natural variant, known as in CWS1; loss of phosphatase activity towards Ins(1,3,4,5)P4, features a modification of the amino acid from C to F at position 105.
+The protein's natural variant, known as in CWS1;, features a modification of the amino acid from C to Y at position 105.
+The protein's natural variant, known as in CWS1 and glioblastoma; loss of phosphatase activity towards Ins(1,3,4,5)P4;, features a modification of the amino acid from D to Y at position 107.
+The protein's natural variant, known as in CWS1 and LDD; loss of phosphatase activity towards Ins(1,3,4,5)P4;, features a modification of the amino acid from L to P at position 112.
+The protein's natural variant, known as loss of phosphatase activity towards Ins(1,3,4,5)P4, features a modification of the amino acid from L to R at position 112.
+The protein's natural variant, known as in multiple cancers;, features a modification of the amino acid from V to L at position 119.
+The protein's natural variant, known as in HNSCC;, features a modification of the amino acid from A to G at position 121.
+The protein's natural variant, known as in glioblastoma; loss of phosphatase activity towards Ins(1,3,4,5)P4, features a modification of the amino acid from A to P at position 121.
+The protein's natural variant, known as in CWS1;, features a modification of the amino acid from H to R at position 123.
+The protein's natural variant, known as in endometrial cancer; loss of protein phosphatase activity;, features a modification of the amino acid from H to Y at position 123.
+The protein's natural variant, known as in CWS1;, features a modification of the amino acid from C to R at position 124.
+The protein's natural variant, known as in CWS1; phosphatase-dead protein with neither lipid nor protein phosphatase activity;, features a modification of the amino acid from C to S at position 124.
+The protein's natural variant, known as in a patient with prostate cancer; reduced phosphatase activity towards PtdIns(3,4,5); shifts its activity from phosphatidylinositol phosphate 3-phosphatase to phosphatidylinositol phosphate 5-phosphatase; disrupts PI3K/ATK signaling; reduced cell migration, features a modification of the amino acid from A to G at position 126.
+The protein's natural variant, known as in CWS1; no lipid phosphatase activity but retains protein phosphatase activity; retains ability to inhibit focal adhesion formation;, features a modification of the amino acid from G to E at position 129.
+The protein's natural variant, known as in glioblastoma; severely reduced protein phosphatase activity; loss of phosphatase activity towards Ins(1,3,4,5)P4;, features a modification of the amino acid from G to R at position 129.
+The protein's natural variant, known as loss of phosphatase activity towards Ins(1,3,4,5)P4 and PtdIns(3,4,5)P3;, features a modification of the amino acid from R to G at position 130.
+The protein's natural variant, known as in CWS1 and endometrial hyperplasia; loss of phosphatase activity towards Ins(1,3,4,5)P4; retains ability to bind phospholipid membranes;, features a modification of the amino acid from R to L at position 130.
+The protein's natural variant, known as in CWS1; loss of phosphatase activity towards Ins(1,3,4,5)P4; retains ability to bind phospholipid membranes;, features a modification of the amino acid from R to Q at position 130.
+The protein's natural variant, known as in MCEPHAS;, features a modification of the amino acid from T to I at position 131.
+The protein's natural variant, known as in one patient with clinical findings suggesting hamartoma tumor syndrome;, features a modification of the amino acid from G to V at position 132.
+The protein's natural variant, known as loss of phosphatase activity towards Ins(1,3,4,5)P3, features a modification of the amino acid from V to I at position 133.
+The protein's natural variant, known as in prostate cancer; no effect on protein phosphatase activity; reduced phosphatase activity towards Ins(1,3,4,5)P3 but retains PtdIns(3,4,5)P3 phosphatase activity, features a modification of the amino acid from M to L at position 134.
+The protein's natural variant, known as in CWS1;, features a modification of the amino acid from I to V at position 135.
+The protein's natural variant, known as in CWS1; loss of phosphatase activity towards Ins(1,3,4,5)P3;, features a modification of the amino acid from C to Y at position 136.
+The protein's natural variant, known as in CWS1, features a modification of the amino acid from A to AN at position 137.
+The protein's natural variant, known as in CWS1; loss of phosphatase activity towards Ins(1,3,4,5)P4;, features a modification of the amino acid from Y to C at position 155.
+The protein's natural variant, known as in multiple cancers, features a modification of the amino acid from V to L at position 158.
+The protein's natural variant, known as in CWS1, features a modification of the amino acid from G to E at position 165.
+The protein's natural variant, known as in glioblastoma; severely reduced protein phosphatase activity; loss of phosphatase activity towards Ins(1,3,4,5)P4; retains ability to bind phospholipid membranes;, features a modification of the amino acid from G to R at position 165.
+The protein's natural variant, known as in CWS1;, features a modification of the amino acid from G to V at position 165.
+The protein's natural variant, known as in MCEPHAS;, features a modification of the amino acid from T to N at position 167.
+The protein's natural variant, known as in breast cancer; severely reduced protein phosphatase activity, features a modification of the amino acid from T to P at position 167.
+The protein's natural variant, known as loss of phosphatase activity towards Ins(1,3,4,5)P4; retains ability to bind phospholipid membranes, features a modification of the amino acid from S to N at position 170.
+The protein's natural variant, known as in CWS1; severely reduced protein phosphatase activity; loss of phosphatase activity towards Ins(1,3,4,5)P4;, features a modification of the amino acid from S to R at position 170.
+The protein's natural variant, known as in endometrial hyperplasia; loss of phosphatase activity towards Ins(1,3,4,5)P4 and PtdIns(3,4,5)P3; retains ability to bind phospholipid membranes;, features a modification of the amino acid from R to C at position 173.
+The protein's natural variant, known as loss of phosphatase activity towards Ins(1,3,4,5)P4;, features a modification of the amino acid from R to H at position 173.
+The protein's natural variant, known as loss of phosphatase activity towards Ins(1,3,4,5)P4;, features a modification of the amino acid from R to P at position 173.
+The protein's natural variant, known as loss of phosphatase activity towards Ins(1,3,4,5)P4;, features a modification of the amino acid from Y to N at position 174.
+The protein's natural variant, known as in endometrial hyperplasia, features a modification of the amino acid from V to A at position 191.
+The protein's natural variant, known as in malignant melanoma; somatic mutation;, features a modification of the amino acid from V to I at position 217.
+The protein's natural variant, known as reduced phosphatase activity towards Ins(1,3,4,5)P4; retains PtdIns(3,4,5)P3 phosphatase activity;, features a modification of the amino acid from S to F at position 227.
+The protein's natural variant, known as in GLM2; the patient also suffered from benign meningioma; not capable of inducing apoptosis; induced increased cell proliferation; led to high constitutive AKT1 activation which could not be increased further by stimulation with insulin;, features a modification of the amino acid from R to Q at position 234.
+The protein's natural variant, known as in MCEPHAS;, features a modification of the amino acid from F to S at position 241.
+The protein's natural variant, known as in CWS1;, features a modification of the amino acid from P to L at position 246.
+The protein's natural variant, known as loss of phosphatase activity towards Ins(1,3,4,5)P4; retains ability to bind phospholipid membranes, features a modification of the amino acid from G to C at position 251.
+The protein's natural variant, known as in MCEPHAS;, features a modification of the amino acid from D to G at position 252.
+The protein's natural variant, known as in CWS1; reduced phosphatase activity towards Ins(1,3,4,5)P4; retains ability to bind phospholipid membranes; predominantly nuclear;, features a modification of the amino acid from K to E at position 289.
+The protein's natural variant, known as in CWS1; reduced phosphatase activity towards Ins(1,3,4,5)P4; retains ability to bind phospholipid membranes, features a modification of the amino acid from D to G at position 331.
+The protein's natural variant, known as in CWS1; loss of interaction with NOP53; decreased phosphorylation at S-380; decreased stability; loss of phosphatase activity towards Ins(1,3,4,5)P4;, features a modification of the amino acid from F to V at position 341.
+The protein's natural variant, known as in CWS1; reduced phosphatase activity towards Ins(1,3,4,5)P4 but PtdIns(3,4,5)P3 phosphatase activity is similar to wild-type;, features a modification of the amino acid from K to N at position 342.
+The protein's natural variant, known as in CWS1; loss of interaction with NOP53; decreased phosphorylation at S-380; decreased stability; loss of phosphatase activity towards Ins(1,3,4,5)P4, features a modification of the amino acid from V to E at position 343.
+The protein's natural variant, known as in glioblastoma; reduced tumor suppressor activity; loss of interaction with NOP53; decreased phosphorylation at S-380; decreased stability; loss of phosphatase activity towards Ins(1,3,4,5)P4; reduced ability to inactivate AKT/PKB; retains ability to bind phospholipid membranes, features a modification of the amino acid from L to Q at position 345.
+The protein's natural variant, known as in CWS1; reduced phosphatase activity towards Ins(1,3,4,5)P4, features a modification of the amino acid from F to L at position 347.
+The protein's natural variant, known as in endometrial hyperplasia; reduced phosphatase activity towards PtdIns(3,4,5)P3; mildly reduced tumor suppressor activity; reduced ability to inactivate AKT/PKB, features a modification of the amino acid from T to I at position 348.
+The protein's natural variant, known as retains Ins(1,3,4,5)P4 and PtdIns(3,4,5)P3 phosphatase activity; retains ability to bind phospholipid membranes, features a modification of the amino acid from V to G at position 369.
+The protein's natural variant, known as retains Ins(1,3,4,5)P4 and PtdIns(3,4,5)P3 phosphatase activity; retains ability to bind phospholipid membranes, features a modification of the amino acid from T to I at position 401.
+The protein's natural variant, known as in RAUST; not changed histone methyltransferase activity H3-K36 specific, features a modification of the amino acid from C to Y at position 869.
+The protein's natural variant, known as in RAUST; decreased histone methyltransferase activity H3-K36 specific, features a modification of the amino acid from P to L at position 895.
+The protein's natural variant, known as in RAUST; decreased histone methyltransferase activity H3-K36 specific, features a modification of the amino acid from K to R at position 1019.
+The protein's natural variant, known as in RAUST, features a modification of the amino acid from E to K at position 1091.
+The protein's natural variant, known as in RAUST; decreased histone methyltransferase activity H3-K36 specific, features a modification of the amino acid from S to F at position 1137.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from N to S at position 812.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from G to R at position 1274.
+The protein's natural variant, known as in DEE109; loss-of-function variant affecting cell cycle regulation; unable to rescue aberrant cell cycle in FZR1-deficient mouse cortical cells; decreased protein levels in patient cells, features a modification of the amino acid from D to G at position 187.
+The protein's natural variant, known as in DEE109; fails to rescue neurodevelopmental defects in a Drosophila model system; does not affect nuclear localization, features a modification of the amino acid from D to N at position 187.
+The protein's natural variant, known as in DEE109; fails to rescue neurodevelopmental defects in a Drosophila model system; does not affect nuclear localization, features a modification of the amino acid from N to K at position 333.
+The protein's natural variant, known as in FDLAB;, features a modification of the amino acid from R to W at position 735.
+The protein's natural variant, known as in MPS6; intermediate form;, features a modification of the amino acid from S to F at position 65.
+The protein's natural variant, known as in MPS6;, features a modification of the amino acid from L to R at position 82.
+The protein's natural variant, known as in MPS6; mild form;, features a modification of the amino acid from T to M at position 92.
+The protein's natural variant, known as in MPS6; mild/severe form;, features a modification of the amino acid from R to Q at position 95.
+The protein's natural variant, known as in MPS6; severe form;, features a modification of the amino acid from P to H at position 116.
+The protein's natural variant, known as in MPS6; severe form;, features a modification of the amino acid from C to R at position 117.
+The protein's natural variant, known as in MPS6; intermediate form;, features a modification of the amino acid from G to V at position 137.
+The protein's natural variant, known as in MPS6;, features a modification of the amino acid from M to I at position 142.
+The protein's natural variant, known as in MPS6; severe form; severe reduction of activity;, features a modification of the amino acid from G to R at position 144.
+The protein's natural variant, known as in MPS6;, features a modification of the amino acid from W to L at position 146.
+The protein's natural variant, known as in MPS6;, features a modification of the amino acid from W to R at position 146.
+The protein's natural variant, known as in MPS6;, features a modification of the amino acid from W to S at position 146.
+The protein's natural variant, known as in MPS6; intermediate form;, features a modification of the amino acid from R to W at position 152.
+The protein's natural variant, known as in MPS6; intermediate form;, features a modification of the amino acid from R to Q at position 160.
+The protein's natural variant, known as in MPS6; mild form; severe reduction of activity;, features a modification of the amino acid from C to R at position 192.
+The protein's natural variant, known as in MPS6; mild/intermediate;, features a modification of the amino acid from Y to C at position 210.
+The protein's natural variant, known as in MPS6; mild form;, features a modification of the amino acid from L to P at position 236.
+The protein's natural variant, known as in MPS6;, features a modification of the amino acid from Q to R at position 239.
+The protein's natural variant, known as in MPS6; severe form;, features a modification of the amino acid from G to R at position 302.
+The protein's natural variant, known as in MPS6; severe form; loss of activity;, features a modification of the amino acid from W to C at position 312.
+The protein's natural variant, known as in MPS6; intermediate form;, features a modification of the amino acid from R to Q at position 315.
+The protein's natural variant, known as in MPS6; intermediate form; severe reduction of activity;, features a modification of the amino acid from L to P at position 321.
+The protein's natural variant, known as in MPS6; mild/severe form;, features a modification of the amino acid from H to P at position 393.
+The protein's natural variant, known as in MPS6;, features a modification of the amino acid from F to L at position 399.
+The protein's natural variant, known as in MPS6; mild form;, features a modification of the amino acid from C to Y at position 405.
+The protein's natural variant, known as in MPS6;, features a modification of the amino acid from R to G at position 484.
+The protein's natural variant, known as in MPS6; mild/severe form;, features a modification of the amino acid from L to P at position 498.
+The protein's natural variant, known as in MPS6; severe form; severe reduction of activity;, features a modification of the amino acid from C to Y at position 521.
+The protein's natural variant, known as in MPS6; mild form;, features a modification of the amino acid from P to R at position 531.
+The protein's natural variant, known as in HMN2D; unable to promote activation of KLF7 target genes including CDKN1A and L1CAM in both cultured cells and patient-derived cells;, features a modification of the amino acid from C to R at position 206.
+The protein's natural variant, known as in HFTC3; impairs the ability to form a ternary complex with FGF23 and FGFR1c; impairs KL-dependent FGF23 signaling;, features a modification of the amino acid from H to R at position 193.
+The protein's natural variant, known as in allele KL-VS; associated with S-370;, features a modification of the amino acid from F to V at position 352.
+The protein's natural variant, known as in allele KL-VS; associated with V-352;, features a modification of the amino acid from C to S at position 370.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from P to L at position 954.
+The protein's natural variant, known as in strain: R3-6, R3-105 and R3-107, features a modification of the amino acid from A to S at position 21.
+The natural variant of this protein is characterized by an amino acid alteration from P to S at position 292.
+The protein's natural variant, known as in COGIS, features a modification of the amino acid from N to S at position 194.
+The protein's natural variant, known as in COGIS, features a modification of the amino acid from R to G at position 236.
+The protein's natural variant, known as in COGIS; decreased trimethylation of 'Lys-27' of histone H3; no effect on interaction with EZH2;, features a modification of the amino acid from R to T at position 236.
+The protein's natural variant, known as in COGIS;, features a modification of the amino acid from H to Y at position 258.
+The protein's natural variant, known as in COGIS;, features a modification of the amino acid from R to G at position 302.
+The protein's natural variant, known as in COGIS; decreased trimethylation of 'Lys-27' of histone H3;, features a modification of the amino acid from R to S at position 302.
+The protein's natural variant, known as affects the interaction with LMNA;, features a modification of the amino acid from R to C at position 690.
+The protein's natural variant, known as found in a patient with severe dystrophia myotonica 2 (DM2) carrying a pathogenic CCTG repeat expansion in CNBP; unknown pathological significance; may act as a disease modifier; changes the voltage-gated sodium channel activity; increases membrane hyperexcitability; decreases channel fast inactivation;, features a modification of the amino acid from P to L at position 72.
+The protein's natural variant, known as probable disease-associated variant found in patients with severe fetal hypokinesia or congenital myopathy; complete loss of sodium channel function;, features a modification of the amino acid from R to H at position 104.
+The natural variant of this protein is characterized by an amino acid alteration from M to V at position 135.
+The protein's natural variant, known as in MYOSCN4A; causes a hyperpolarizing shift of the activation curve; enhances channel slow inactivation;, features a modification of the amino acid from I to V at position 141.
+The protein's natural variant, known as probable disease-associated variant found in patients with severe fetal hypokinesia or congenital myopathy; impaired sodium channel function;, features a modification of the amino acid from M to K at position 203.
+The protein's natural variant, known as in HOKPP2;, features a modification of the amino acid from R to W at position 222.
+The protein's natural variant, known as in MYOSCN4A; also found in patients with severe fetal hypokinesia or congenital myopathy; impaired sodium channel function;, features a modification of the amino acid from R to W at position 225.
+The protein's natural variant, known as no significant effect on channel activity;, features a modification of the amino acid from S to L at position 246.
+The protein's natural variant, known as in PMC;, features a modification of the amino acid from Q to K at position 270.
+The protein's natural variant, known as probable disease-associated variant found in patients with severe fetal hypokinesia or congenital myopathy; complete loss of sodium channel function, features a modification of the amino acid from P to T at position 382.
+The protein's natural variant, known as in MYOSCN4A;, features a modification of the amino acid from V to M at position 445.
+The protein's natural variant, known as in MYOSCN4A; variable phenotype ranging from mild to severe myotonia;, features a modification of the amino acid from E to K at position 452.
+The protein's natural variant, known as in HOKPP2;, features a modification of the amino acid from R to H at position 669.
+The protein's natural variant, known as in MYOSCN4A, features a modification of the amino acid from F to S at position 671.
+The protein's natural variant, known as in HOKPP2;, features a modification of the amino acid from R to C at position 672.
+The protein's natural variant, known as in HOKPP2;, features a modification of the amino acid from R to G at position 672.
+The protein's natural variant, known as in HOKPP2;, features a modification of the amino acid from R to H at position 672.
+The protein's natural variant, known as in HOKPP2;, features a modification of the amino acid from R to S at position 672.
+The protein's natural variant, known as in NKPP;, features a modification of the amino acid from R to G at position 675.
+The protein's natural variant, known as in NKPP;, features a modification of the amino acid from R to Q at position 675.
+The protein's natural variant, known as in NKPP;, features a modification of the amino acid from R to W at position 675.
+The protein's natural variant, known as in PMC;, features a modification of the amino acid from I to T at position 693.
+The protein's natural variant, known as in HYPP and PMC;, features a modification of the amino acid from T to M at position 704.
+The protein's natural variant, known as in MYOSCN4A;, features a modification of the amino acid from A to T at position 715.
+The protein's natural variant, known as voltage-gated sodium channel activity is not affected and channel activation as well as fast and slow inactivation curves are normal;, features a modification of the amino acid from V to I at position 781.
+The protein's natural variant, known as in PMC;, features a modification of the amino acid from S to F at position 804.
+The protein's natural variant, known as in MYOSCN4A, features a modification of the amino acid from S to N at position 804.
+The natural variant of this protein is characterized by an amino acid alteration from A to D at position 861.
+The protein's natural variant, known as probable disease-associated variant found in patients with severe fetal hypokinesia or congenital myopathy; impaired sodium channel function;, features a modification of the amino acid from D to N at position 1069.
+The protein's natural variant, known as in NKPP and HOKPP2; detected in a family where three affected members manifested hypokalemic periodic paralysis whereas five other patients had normokalemic periodic paralysis;, features a modification of the amino acid from R to Q at position 1129.
+The protein's natural variant, known as in HOKPP2; changes the voltage-gated sodium channel activity; increases membrane hypoexcitability; increases channel activation and both fast and slow channel inactivation;, features a modification of the amino acid from R to Q at position 1132.
+The protein's natural variant, known as in HOKPP2; also found in patients with severe fetal hypokinesia or congenital myopathy; increased depolarization tendency at normal and reduced extracellular potassium and reduced amplitude and rise time of action potentials;, features a modification of the amino acid from R to C at position 1135.
+The protein's natural variant, known as in HOKPP2; increased depolarization tendency at normal and reduced extracellular potassium and reduced amplitude and rise time of action potentials;, features a modification of the amino acid from R to H at position 1135.
+The protein's natural variant, known as in PMC, features a modification of the amino acid from A to D at position 1152.
+The protein's natural variant, known as in PMC, MYOSCN4A and HYPP;, features a modification of the amino acid from A to T at position 1156.
+The protein's natural variant, known as in HOKPP2; atypical phenotype with heat-induced myotonia and cold-induced paralysis with hypokalemia; changes the voltage-gated sodium channel activity; increases channel activation and slow inactivation at low temperature;, features a modification of the amino acid from P to S at position 1158.
+The protein's natural variant, known as in MYOSCN4A; acetazolamide-responsive myotonia;, features a modification of the amino acid from I to V at position 1160.
+The protein's natural variant, known as probable disease-associated variant found in patients with severe fetal hypokinesia or congenital myopathy; complete loss of sodium channel function, features a modification of the amino acid from C to F at position 1209.
+The protein's natural variant, known as in MYOSCN4A; enhances voltage-gated sodium channel activation inducing membrane hyperexcitability, features a modification of the amino acid from F to L at position 1290.
+The protein's natural variant, known as in PMC; without cold paralysis;, features a modification of the amino acid from V to I at position 1293.
+The protein's natural variant, known as in MYOSCN4A; unusually severe and lethal phenotype with neonatal onset;, features a modification of the amino acid from N to K at position 1297.
+The protein's natural variant, known as in PMC;, features a modification of the amino acid from G to A at position 1306.
+The protein's natural variant, known as in MYOSCN4A and PMC; severe;, features a modification of the amino acid from G to E at position 1306.
+The protein's natural variant, known as in MYOSCN4A and PMC;, features a modification of the amino acid from G to V at position 1306.
+The protein's natural variant, known as in MYOSCN4A;, features a modification of the amino acid from I to N at position 1310.
+The protein's natural variant, known as in PMC; changes the voltage-gated sodium channel activity; increases membrane hyperexcitability at low temperature; decreases channel activation, deactivation, fast inactivation and recovery delay from fast inactivation;, features a modification of the amino acid from T to M at position 1313.
+The protein's natural variant, known as in PMC and HYPP;, features a modification of the amino acid from L to R at position 1433.
+The protein's natural variant, known as in PMC;, features a modification of the amino acid from L to P at position 1436.
+The protein's natural variant, known as in CMS16; leads to fast inactivation;, features a modification of the amino acid from V to E at position 1442.
+The protein's natural variant, known as in PMC; changes the voltage-gated sodium channel activity; increases membrane hyperexcitability at low temperature; decreases channel activation, deactivation, fast inactivation and recovery delay from fast inactivation;, features a modification of the amino acid from R to C at position 1448.
+The protein's natural variant, known as in PMC;, features a modification of the amino acid from R to H at position 1448.
+The protein's natural variant, known as in PMC;, features a modification of the amino acid from R to L at position 1448.
+The protein's natural variant, known as in CMS16; leads to hyperpolarization of the steady-state fast inactivation, slow recovery from inactivation and reduces the channel ability to activate in response to repetitive stimulating pulses;, features a modification of the amino acid from R to W at position 1454.
+The protein's natural variant, known as in PMC;, features a modification of the amino acid from G to E at position 1456.
+The protein's natural variant, known as in CMS16; enhanced fast inactivation and slowed recovery from fast inactivation;, features a modification of the amino acid from R to H at position 1457.
+The protein's natural variant, known as in PMC; accelerates deactivation from the inactivated state and enhances the remobilization of gating charge, features a modification of the amino acid from F to S at position 1473.
+The protein's natural variant, known as in MYOSCN4A; highly variable severity;, features a modification of the amino acid from M to I at position 1476.
+The protein's natural variant, known as in MYOSCN4A; fluctuating cold-induced and exercise-induced stiffness;, features a modification of the amino acid from A to D at position 1481.
+The protein's natural variant, known as in PMC;, features a modification of the amino acid from V to M at position 1589.
+The protein's natural variant, known as in HYPP and NKPP;, features a modification of the amino acid from M to V at position 1592.
+The protein's natural variant, known as in MYOSCN4A; changes the voltage-gated sodium channel activity; increases membrane hyperexcitability; decreases channel fast inactivation, features a modification of the amino acid from Q to E at position 1633.
+The protein's natural variant, known as in PMC; increases the extent of charge immobilization in response to strong depolarization;, features a modification of the amino acid from F to I at position 1705.
+The protein's natural variant, known as in KINS, features a modification of the amino acid from P to A at position 231.
+The protein's natural variant, known as in KINS, features a modification of the amino acid from P to L at position 231.
+The protein's natural variant, known as in KINS, features a modification of the amino acid from A to S at position 233.
+The protein's natural variant, known as in KINS, features a modification of the amino acid from A to T at position 233.
+The protein's natural variant, known as in KINS, features a modification of the amino acid from A to V at position 233.
+The protein's natural variant, known as in KINS, features a modification of the amino acid from V to G at position 235.
+The protein's natural variant, known as found in a consanguineous family with intellectual disability; unknown pathological significance, features a modification of the amino acid from G to V at position 1215.
+The protein's natural variant, known as in 50% of the molecules, features a modification of the amino acid from A to S at position 112.
+The protein's natural variant, known as in strain: BG1, features a modification of the amino acid from V to I at position 137.
+The protein's natural variant, known as in LATHOS;, features a modification of the amino acid from R to Q at position 29.
+The protein's natural variant, known as in LATHOS;, features a modification of the amino acid from Y to S at position 46.
+The protein's natural variant, known as in LATHOS;, features a modification of the amino acid from G to D at position 211.
+The protein's natural variant, known as in SEMDJL2;, features a modification of the amino acid from P to L at position 148.
+The protein's natural variant, known as in SEMDJL2;, features a modification of the amino acid from P to S at position 148.
+The protein's natural variant, known as in SEMDJL2;, features a modification of the amino acid from R to L at position 149.
+The protein's natural variant, known as in SEMDJL2;, features a modification of the amino acid from R to Q at position 149.
+The protein's natural variant, known as in D2L2AD; unknown pathological significance; very mild decrease of citrate transport rates, features a modification of the amino acid from A to T at position 28.
+The protein's natural variant, known as in D2L2AD; reduced rates of citrate transport, features a modification of the amino acid from I to N at position 40.
+The protein's natural variant, known as in D2L2AD; severely reduced rates of citrate transport, features a modification of the amino acid from P to L at position 45.
+The protein's natural variant, known as in D2L2AD; severely reduced rates of citrate transport;, features a modification of the amino acid from E to K at position 47.
+The protein's natural variant, known as in D2L2AD; severely reduced rates of citrate transport, features a modification of the amino acid from G to D at position 93.
+The protein's natural variant, known as in D2L2AD; severely reduced rates of citrate transport;, features a modification of the amino acid from G to D at position 130.
+The protein's natural variant, known as in D2L2AD; abolishes citrate transport, features a modification of the amino acid from E to Q at position 144.
+The protein's natural variant, known as in D2L2AD, features a modification of the amino acid from G to R at position 167.
+The protein's natural variant, known as in D2L2AD; reduced rates of citrate transport;, features a modification of the amino acid from S to W at position 193.
+The protein's natural variant, known as in D2L2AD; severely reduced rates of citrate transport;, features a modification of the amino acid from R to H at position 198.
+The protein's natural variant, known as in D2L2AD; reduced rates of citrate transport;, features a modification of the amino acid from M to T at position 202.
+The protein's natural variant, known as in D2L2AD; disease phenotype may include decreased activity of mitochondrial respiratory chain complex V, features a modification of the amino acid from N to S at position 238.
+The protein's natural variant, known as in CMS23; reduced rates of citrate transport;, features a modification of the amino acid from R to Q at position 247.
+The protein's natural variant, known as in D2L2AD; reduced rates of citrate transport, features a modification of the amino acid from C to R at position 262.
+The protein's natural variant, known as in D2L2AD; abolishes citrate transport;, features a modification of the amino acid from R to C at position 282.
+The protein's natural variant, known as in D2L2AD; abolishes citrate transport;, features a modification of the amino acid from R to G at position 282.
+The protein's natural variant, known as in D2L2AD; abolishes citrate transport;, features a modification of the amino acid from R to H at position 282.
+The protein's natural variant, known as in D2L2AD; reduced rates of citrate transport, features a modification of the amino acid from Y to C at position 297.
+The protein's natural variant, known as in SLEB17; increased NFKB1 activation after stimulation with guanosine and ssRNA, features a modification of the amino acid from R to G at position 28.
+The protein's natural variant, known as in SLEB17; increased NFKB1 activation after stimulation with cGMP, features a modification of the amino acid from Y to H at position 264.
+The protein's natural variant, known as in SLEB17; increased NFKB1 activation after stimulation with cGMP, features a modification of the amino acid from F to L at position 507.
+The protein's natural variant, known as in IMD74; no enhanced expression after stimulation by imiquimod; defective up-regulation of type IIFN-related genes; decreased expression of IFNG;, features a modification of the amino acid from V to F at position 795.
+The natural variant of this protein is characterized by an amino acid alteration from Y to H at position 357.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from S to R at position 4.
+The protein's natural variant, known as found in a renal cell carcinoma sample; somatic mutation, features a modification of the amino acid from G to C at position 214.
+The protein's natural variant, known as in strain: CCUG 37602, features a modification of the amino acid from A to T at position 203.
+The protein's natural variant, known as in strain: CCUG 37602, features a modification of the amino acid from L to F at position 428.
+The protein's natural variant, known as in strain: CCUG 37602, features a modification of the amino acid from R to A at position 461.
+The protein's natural variant, known as in strain: CCUG 37602, features a modification of the amino acid from I to V at position 475.
+The protein's natural variant, known as in strain: CCUG 37602, features a modification of the amino acid from T to P at position 607.
+The protein's natural variant, known as in a lung neuroendocrine carcinoma sample; somatic mutation;, features a modification of the amino acid from G to D at position 962.
+The protein's natural variant, known as in minor component, features a modification of the amino acid from Y to C at position 23.
+The protein's natural variant, known as decreased nucleoside and nucleobase transport;, features a modification of the amino acid from D to Y at position 5.
+The protein's natural variant, known as no change in nucleoside and nucleobase transport;, features a modification of the amino acid from N to K at position 68.
+The protein's natural variant, known as no change in nucleoside and nucleobase transport;, features a modification of the amino acid from P to L at position 94.
+The protein's natural variant, known as decreased inosine and guanosine transport; no change in uridine and hypoxanthine transport, features a modification of the amino acid from SGV to M at position 186.
+The protein's natural variant, known as in AAT12; unknown pathological significance; results in impaired assembly of FBN1-containing microfibrils, features a modification of the amino acid from Y to N at position 321.
+The protein's natural variant, known as in AAT12; unknown pathological significance; has no effect on assembly of FBN1-containing microfibrils, features a modification of the amino acid from G to D at position 753.
+The protein's natural variant, known as in AAT12; unknown pathological significance; results in impaired assembly of FBN1-containing microfibrils, features a modification of the amino acid from R to W at position 781.
+The protein's natural variant, known as in CNM1; may act as a phenotype modifier; drastically reduced enzymatic activity;, features a modification of the amino acid from R to Q at position 336.
+The protein's natural variant, known as in CNM1; may act as a disease modifier; mutation found in a patient also carrying mutation Lys-368 in DNM2; reduced enzymatic activity;, features a modification of the amino acid from Y to C at position 462.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from S to L at position 184.
+The protein's natural variant, known as in IMGT allele IGLC3*04, features a modification of the amino acid from K to R at position 83.
+The protein's natural variant, known as in SPGF73, features a modification of the amino acid from S to I at position 816.
+The protein's natural variant, known as in SPGF73; unknown pathological significance, features a modification of the amino acid from G to R at position 848.
+The protein's natural variant, known as in LY-A cell line; destroys the phosphatidylinositol 4-phosphate-binding activity, abolishes localization to the Golgi apparatus, features a modification of the amino acid from G to E at position 67.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to H at position 594.
+The protein's natural variant, known as found in restrictive cardiomyopathy; unknown pathological significance;, features a modification of the amino acid from N to D at position 456.
+The protein's natural variant, known as found in a patient with neurodevelopmental anomalies; unknown pathological significance, features a modification of the amino acid from D to E at position 261.
+The protein's natural variant, known as found in a patient with epilepsy but without evidence of neurodevelopmental impairment; unknown pathological significance; affects channel properties resulting in slower channel deactivation, features a modification of the amino acid from V to F at position 447.
+The protein's natural variant, known as found in a patient with epilepsy and neurodevelopmental anomalies; unknown pathological significance; affects channel properties resulting in slower channel deactivation, features a modification of the amino acid from T to I at position 449.
+The protein's natural variant, known as found in a patient with epilepsy and neurodevelopmental anomalies; unknown pathological significance; affects channel properties resulting in slower channel deactivation, features a modification of the amino acid from V to L at position 456.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from I to V at position 36.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from H to Y at position 56.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from H to P at position 173.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from V to L at position 239.
+The natural variant of this protein is characterized by an amino acid alteration from F to Y at position 114.
+The natural variant of this protein is characterized by an amino acid alteration from A to V at position 296.
+The protein's natural variant, known as found in a patient with unilateral microphthalmia, optic disk and chorioretinal coloboma, mild learning difficulties;, features a modification of the amino acid from L to P at position 198.
+The protein's natural variant, known as in COXPD48; unknown pathological significance;, features a modification of the amino acid from A to P at position 141.
+The protein's natural variant, known as in COXPD48; unknown pathological significance;, features a modification of the amino acid from C to S at position 152.
+The protein's natural variant, known as in SPGF35; unknown pathological significance, features a modification of the amino acid from V to E at position 569.
+The protein's natural variant, known as in SPGF35; unknown pathological significance, features a modification of the amino acid from Q to K at position 1105.
+The protein's natural variant, known as in SPGF35; unknown pathological significance;, features a modification of the amino acid from G to E at position 1112.
+The protein's natural variant, known as in SPGF35; unknown pathological significance;, features a modification of the amino acid from M to V at position 1347.
+The protein's natural variant, known as in SPGF35; unknown pathological significance;, features a modification of the amino acid from R to H at position 1494.
+The protein's natural variant, known as in HPE4;, features a modification of the amino acid from S to C at position 157.
+The protein's natural variant, known as in HPE4;, features a modification of the amino acid from P to R at position 192.
+The protein's natural variant, known as in HPE4;, features a modification of the amino acid from Q to L at position 236.
+The protein's natural variant, known as in HPE4;, features a modification of the amino acid from T to A at position 280.
+The protein's natural variant, known as in HPE4;, features a modification of the amino acid from S to F at position 291.
+The protein's natural variant, known as in strain: NCTC 11638, features a modification of the amino acid from L to R at position 2.
+The protein's natural variant, known as in strain: NCTC 11638, features a modification of the amino acid from L to F at position 24.
+The protein's natural variant, known as in strain: NCTC 11638, features a modification of the amino acid from Q to K at position 41.
+The protein's natural variant, known as in strain: NCTC 11638, features a modification of the amino acid from S to F at position 49.
+The protein's natural variant, known as in strain: NCTC 11638, features a modification of the amino acid from K to E at position 51.
+The protein's natural variant, known as in strain: NCTC 11638, features a modification of the amino acid from LL to IP at position 61.
+The protein's natural variant, known as in strain: NCTC 11638, features a modification of the amino acid from I to M at position 67.
+The protein's natural variant, known as in strain: NCTC 11638, features a modification of the amino acid from E to K at position 74.
+The protein's natural variant, known as in strain: NCTC 11638, features a modification of the amino acid from S to F at position 81.
+The protein's natural variant, known as in a non-small cell lung cancer cell line, features a modification of the amino acid from R to C at position 348.
+The protein's natural variant, known as in a non-small cell lung cancer cell line, features a modification of the amino acid from D to H at position 397.
+The protein's natural variant, known as in a non-small cell lung cancer cell line;, features a modification of the amino acid from T to I at position 415.
+The protein's natural variant, known as in strain: Kisumu2 and YAO, features a modification of the amino acid from V to A at position 127.
+The protein's natural variant, known as in strain: YAO; confers resistance to insecticides, features a modification of the amino acid from G to S at position 280.
+The protein's natural variant, known as found in a renal cell carcinoma case; somatic mutation, features a modification of the amino acid from H to L at position 373.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from S to R at position 789.
+The protein's natural variant, known as lower Vmax for MPP(+) transport; no change in transport efficiency (Vmax/Km) and clearance of cyclo(his-pro) and salsolinol;, features a modification of the amino acid from M to I at position 165.
+The protein's natural variant, known as decreased Ki value for TBA inhibition of MPP(+); no change in transport efficiency (Vmax/Km) and clearance of cyclo(his-pro) and salsolinol;, features a modification of the amino acid from S to A at position 270.
+The protein's natural variant, known as lower Vmax and reduced Ki value for TBA inhibition of MPP(+); lower transport efficiency (Vmax/Km) and clearance of cyclo(his-pro); no change in transport efficiency (Vmax/Km) and clearance of salsolinol;, features a modification of the amino acid from R to C at position 400.
+The protein's natural variant, known as lower Km value for MPP(+) and reduced Ki value for TBA inhibition of MPP; no change in transport efficiency (Vmax/Km) and clearance of cyclo(his-pro) and salsolinol;, features a modification of the amino acid from K to Q at position 432.
+The protein's natural variant, known as in strain: Isolate 2, features a modification of the amino acid from V to I at position 102.
+The protein's natural variant, known as in strain: Isolate 2, features a modification of the amino acid from V to I at position 117.
+The protein's natural variant, known as transport properties comparable to wild-type;, features a modification of the amino acid from G to W at position 187.
+The protein's natural variant, known as transport properties comparable to wild-type;, features a modification of the amino acid from K to N at position 304.
+The protein's natural variant, known as transport properties comparable to wild-type;, features a modification of the amino acid from G to E at position 487.
+The protein's natural variant, known as 40% reduced expression level compared to wild-type; higher transport of 9-(2-phosphonyl-methoxyethyl) adenine than wild-type;, features a modification of the amino acid from Y to C at position 556.
+The protein's natural variant, known as 10% reduced expression level compared to wild-type; transport properties comparable to wild-type;, features a modification of the amino acid from E to K at position 757.
+The protein's natural variant, known as 20% reduced expression level compared to wild-type; significant lower activity in 6-mercaptopurine transport than wild-type;, features a modification of the amino acid from V to I at position 776.
+The protein's natural variant, known as transport properties comparable to wild-type;, features a modification of the amino acid from R to I at position 820.
+The protein's natural variant, known as transport properties comparable to wild-type;, features a modification of the amino acid from V to F at position 854.
+The protein's natural variant, known as transport properties comparable to wild-type;, features a modification of the amino acid from I to V at position 866.
+The protein's natural variant, known as 10% reduced expression level compared to wild-type; transport properties comparable to wild-type;, features a modification of the amino acid from T to M at position 1142.
+The protein's natural variant, known as may be a real difference between the Philippine and Japanese populations, features a modification of the amino acid from V to R at position 80.
+The natural variant of this protein is characterized by an amino acid alteration from L to V at position 11.
+The natural variant of this protein is characterized by an amino acid alteration from L to S at position 65.
+The protein's natural variant, known as in LADCI; severe, but incomplete loss of activation of RGS9 GTPase activator activity, affecting the deactivation of D(2) dopamine receptor-mediated signaling; decreased stability; decreased RGS9 stabilization;, features a modification of the amino acid from S to L at position 123.
+The protein's natural variant, known as in ECTD10B;, features a modification of the amino acid from C to Y at position 47.
+The protein's natural variant, known as in ECTD10B;, features a modification of the amino acid from C to R at position 87.
+The protein's natural variant, known as in ECTD10B;, features a modification of the amino acid from R to H at position 89.
+The protein's natural variant, known as in ECTD10B;, features a modification of the amino acid from R to Q at position 98.
+The protein's natural variant, known as in ECTD10B;, features a modification of the amino acid from D to A at position 110.
+The protein's natural variant, known as in ECTD10B, features a modification of the amino acid from C to R at position 148.
+The protein's natural variant, known as in ECTD10B;, features a modification of the amino acid from R to Q at position 358.
+The protein's natural variant, known as associated with increase in hair thickness; results in decreased downstream activity of NFKB1 48 hours after transfection into cells;, features a modification of the amino acid from V to A at position 370.
+The protein's natural variant, known as in ECTD10B; the mutant protein does not interact with EDARADD and is functionally inactive;, features a modification of the amino acid from R to H at position 375.
+The protein's natural variant, known as in ECTD10B, features a modification of the amino acid from L to F at position 377.
+The protein's natural variant, known as in ECTD10B;, features a modification of the amino acid from G to S at position 382.
+The protein's natural variant, known as in ECTD10B, features a modification of the amino acid from Q to QQ at position 396.
+The protein's natural variant, known as in ECTD10B;, features a modification of the amino acid from T to M at position 403.
+The protein's natural variant, known as in ECTD10B, features a modification of the amino acid from I to F at position 408.
+The protein's natural variant, known as in ECTD10B, features a modification of the amino acid from T to P at position 413.
+The protein's natural variant, known as in ECTD10B, features a modification of the amino acid from I to T at position 418.
+The protein's natural variant, known as in ECTD10A and ECTD10B; abolishes NF-kappa-B activation and reduces JNK activation;, features a modification of the amino acid from R to Q at position 420.
+The protein's natural variant, known as in ECTD10B;, features a modification of the amino acid from W to C at position 434.
+The protein's natural variant, known as in ECTD10B;, features a modification of the amino acid from W to R at position 434.
+The protein's natural variant, known as in COXPD42; decreased protein abundance;, features a modification of the amino acid from M to R at position 78.
+The protein's natural variant, known as in RP96, features a modification of the amino acid from C to F at position 147.
+The protein's natural variant, known as in a patient with atrioventricular septal defects;, features a modification of the amino acid from T to A at position 96.
+The protein's natural variant, known as in a patient with atrioventricular septal defects, features a modification of the amino acid from D to A at position 98.
+The protein's natural variant, known as in a patient with atrioventricular septal defects, features a modification of the amino acid from L to S at position 100.
+The protein's natural variant, known as in EA5; associated with susceptibility to EIG9;, features a modification of the amino acid from C to F at position 104.
+The protein's natural variant, known as in Redhill/Malmo-I/Tradate; associated with T-344 in Redhill;, features a modification of the amino acid from R to C at position 23.
+The protein's natural variant, known as in Fukuoka-2/Lille/Taipei/Varese/Komagome-3;, features a modification of the amino acid from R to H at position 23.
+The protein's natural variant, known as in Jaffna;, features a modification of the amino acid from R to L at position 24.
+The protein's natural variant, known as in Takefu/Honolulu-1;, features a modification of the amino acid from R to P at position 24.
+The protein's natural variant, known as in Christchurch/Honolulu-2;, features a modification of the amino acid from R to Q at position 24.
+The protein's natural variant, known as in Bleinheim/Iowa city-2;, features a modification of the amino acid from D to V at position 25.
+The protein's natural variant, known as in Nagasaki-3;, features a modification of the amino acid from H to Q at position 27.
+The protein's natural variant, known as in Larino;, features a modification of the amino acid from H to Y at position 27.
+The natural variant of this protein is characterized by an amino acid alteration from F to Y at position 73.
+The protein's natural variant, known as in Torino;, features a modification of the amino acid from E to K at position 84.
+The protein's natural variant, known as in Malmo-95/Dalakarlia;, features a modification of the amino acid from D to N at position 87.
+The protein's natural variant, known as in FDAH;, features a modification of the amino acid from L to P at position 90.
+The protein's natural variant, known as in Vibo Valentia;, features a modification of the amino acid from E to K at position 106.
+The natural variant of this protein is characterized by an amino acid alteration from E to G at position 121.
+The protein's natural variant, known as in Yanomama-2;, features a modification of the amino acid from R to G at position 138.
+The protein's natural variant, known as in Nagoya;, features a modification of the amino acid from E to K at position 143.
+The protein's natural variant, known as in Tregasio;, features a modification of the amino acid from V to E at position 146.
+The protein's natural variant, known as in Komagome-2;, features a modification of the amino acid from H to R at position 152.
+The protein's natural variant, known as in Hawkes bay;, features a modification of the amino acid from C to F at position 201.
+The protein's natural variant, known as in FDAH;, features a modification of the amino acid from R to H at position 242.
+The protein's natural variant, known as in FDAH;, features a modification of the amino acid from R to P at position 242.
+The protein's natural variant, known as in Tradate-2;, features a modification of the amino acid from K to Q at position 249.
+The protein's natural variant, known as in Herborn;, features a modification of the amino acid from K to E at position 264.
+The protein's natural variant, known as in Malmo-10;, features a modification of the amino acid from Q to R at position 292.
+The protein's natural variant, known as in Nagasaki-1;, features a modification of the amino acid from D to G at position 293.
+The protein's natural variant, known as in Caserta;, features a modification of the amino acid from K to N at position 300.
+The protein's natural variant, known as in Canterbury/New Guinea/Tagliacozzo/Cuneo/Cooperstown;, features a modification of the amino acid from K to N at position 337.
+The protein's natural variant, known as in Bergamo;, features a modification of the amino acid from D to G at position 338.
+The protein's natural variant, known as in Brest;, features a modification of the amino acid from D to V at position 338.
+The protein's natural variant, known as in Malmo-47;, features a modification of the amino acid from N to K at position 342.
+The protein's natural variant, known as in Redhill; associated with C-23;, features a modification of the amino acid from A to T at position 344.
+The protein's natural variant, known as in Roma;, features a modification of the amino acid from E to K at position 345.
+The protein's natural variant, known as in Sondrio;, features a modification of the amino acid from E to K at position 357.
+The protein's natural variant, known as in Hiroshima-1;, features a modification of the amino acid from E to K at position 378.
+The protein's natural variant, known as in Coari I/Porto Alegre;, features a modification of the amino acid from E to K at position 382.
+The protein's natural variant, known as in Trieste;, features a modification of the amino acid from K to N at position 383.
+The protein's natural variant, known as in Parklands;, features a modification of the amino acid from D to H at position 389.
+The protein's natural variant, known as in Iowa city-1;, features a modification of the amino acid from D to V at position 389.
+The protein's natural variant, known as in Naskapi/Mersin/Komagome-1;, features a modification of the amino acid from K to E at position 396.
+The protein's natural variant, known as in Nagasaki-2;, features a modification of the amino acid from D to N at position 399.
+The protein's natural variant, known as in Tochigi;, features a modification of the amino acid from E to K at position 400.
+The protein's natural variant, known as in Malmo-5;, features a modification of the amino acid from E to Q at position 400.
+The protein's natural variant, known as in Hiroshima-2;, features a modification of the amino acid from E to K at position 406.
+The natural variant of this protein is characterized by an amino acid alteration from E to K at position 420.
+The protein's natural variant, known as in Liprizzi;, features a modification of the amino acid from R to C at position 434.
+The protein's natural variant, known as in Dublin;, features a modification of the amino acid from E to K at position 503.
+The protein's natural variant, known as in Casebrook;, features a modification of the amino acid from D to N at position 518.
+The protein's natural variant, known as in Manaus-1/Adana/Lambadi/Vancouver;, features a modification of the amino acid from E to K at position 525.
+The protein's natural variant, known as in Ortonovo;, features a modification of the amino acid from E to K at position 529.
+The protein's natural variant, known as in Maddaloni;, features a modification of the amino acid from V to M at position 557.
+The protein's natural variant, known as in Castel di Sangro;, features a modification of the amino acid from K to E at position 560.
+The protein's natural variant, known as in Maku;, features a modification of the amino acid from K to E at position 565.
+The protein's natural variant, known as in Malmo-61;, features a modification of the amino acid from D to A at position 574.
+The protein's natural variant, known as in Mexico;, features a modification of the amino acid from D to G at position 574.
+The protein's natural variant, known as in Church bay;, features a modification of the amino acid from K to E at position 584.
+The protein's natural variant, known as in Fukuoka-1/Paris-2;, features a modification of the amino acid from D to N at position 587.
+The protein's natural variant, known as in Osaka-1;, features a modification of the amino acid from E to K at position 589.
+The protein's natural variant, known as in Osaka-2/Phnom Phen/albumin B/Verona;, features a modification of the amino acid from E to K at position 594.
+The protein's natural variant, known as in Venezia, features a modification of the amino acid from GKKLVAASQAALGL to PTMRIRERK at position 609.
+The protein's natural variant, known as in Gent/Milano Fast;, features a modification of the amino acid from K to E at position 597.
+The protein's natural variant, known as in Vanves;, features a modification of the amino acid from K to N at position 598.
+The protein's natural variant, known as in Kenitra, features a modification of the amino acid from LVAASQAALGL to TCCCKSSCLRLITSHLKASQPTMRIRERK at position 609.
+The protein's natural variant, known as in TYRSN2;, features a modification of the amino acid from G to V at position 362.
+The protein's natural variant, known as in a lung large cell carcinoma sample; somatic mutation, features a modification of the amino acid from M to I at position 112.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from A to T at position 130.
+The natural variant of this protein is characterized by an amino acid alteration from E to Q at position 34.
+The protein's natural variant, known as in SENS;, features a modification of the amino acid from A to E at position 30.
+The protein's natural variant, known as in SENS;, features a modification of the amino acid from P to L at position 31.
+The protein's natural variant, known as in SENS;, features a modification of the amino acid from P to R at position 31.
+The protein's natural variant, known as in SENS, features a modification of the amino acid from P to S at position 31.
+The protein's natural variant, known as in SENS;, features a modification of the amino acid from H to P at position 33.
+The protein's natural variant, known as in SENS;, features a modification of the amino acid from H to Q at position 33.
+The protein's natural variant, known as in SENS;, features a modification of the amino acid from G to D at position 62.
+The protein's natural variant, known as in SENS;, features a modification of the amino acid from H to P at position 74.
+The protein's natural variant, known as in MRXSSB; loss-of-function mutation affecting regulation of Wnt signaling, features a modification of the amino acid from I to T at position 214.
+The protein's natural variant, known as in MRXSSB;, features a modification of the amino acid from A to V at position 233.
+The protein's natural variant, known as in MRXSSB;, features a modification of the amino acid from L to P at position 235.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from R to T at position 294.
+The protein's natural variant, known as in MRXSSB, features a modification of the amino acid from V to F at position 300.
+The protein's natural variant, known as in MRXSSB; loss-of-function mutation affecting regulation of Wnt signaling;, features a modification of the amino acid from R to H at position 326.
+The protein's natural variant, known as in MRXSSB;, features a modification of the amino acid from R to Q at position 351.
+The protein's natural variant, known as in MRXSSB;, features a modification of the amino acid from R to C at position 362.
+The protein's natural variant, known as in MRXSSB; also found as a somatic mutation in medulloblastoma; loss of ATPase activity; increased interaction with CSNK1E in the absence of dsRNA; contrary to wild-type protein, strongly interacts with CSNK1A1 and CSNK1D in vivo; strongly increased ability to activate CSNK1E kinase activity, leading to increased DVL phosphorylation, thereby activating Wnt/beta-catenin signaling; increased RNA-binding; no effect on subcellular location;, features a modification of the amino acid from R to C at position 376.
+The protein's natural variant, known as in MRXSSB;, features a modification of the amino acid from L to P at position 392.
+The protein's natural variant, known as in MRXSSB;, features a modification of the amino acid from Q to P at position 417.
+The protein's natural variant, known as in MRXSSB;, features a modification of the amino acid from R to G at position 475.
+The protein's natural variant, known as in MRXSSB, features a modification of the amino acid from R to S at position 480.
+The protein's natural variant, known as in MRXSSB;, features a modification of the amino acid from R to H at position 488.
+The protein's natural variant, known as in MRXSSB; loss-of-function mutation affecting regulation of Wnt signaling;, features a modification of the amino acid from I to T at position 507.
+The protein's natural variant, known as in MRXSSB, features a modification of the amino acid from N to I at position 509.
+The protein's natural variant, known as in MRXSSB;, features a modification of the amino acid from I to T at position 514.
+The protein's natural variant, known as in medulloblastoma; somatic mutation; loss of ATPase activity; interacts with CSNK1E, even in the presence of dsRNA; contrary to wild-type protein, strongly interacts with CSNK1A1 and CSNK1D in vivo; strongly increased ability to activate CSNK1E kinase activity, leading to increased DVL phosphorylation, thereby activating Wnt/beta-catenin signaling; no effect on RNA-binding, nor on subcellular location, features a modification of the amino acid from R to H at position 528.
+The protein's natural variant, known as in MRXSSB; loss-of-function mutation affecting regulation of Wnt signaling, features a modification of the amino acid from R to H at position 534.
+The protein's natural variant, known as in MRXSSB;, features a modification of the amino acid from P to L at position 568.
+The protein's natural variant, known as in VUR3, features a modification of the amino acid from Q to QTQ at position 17.
+The protein's natural variant, known as in VUR3;, features a modification of the amino acid from G to C at position 178.
+The protein's natural variant, known as in VUR3; increased levels of the mutant protein that is associated with increased suppression of CTNNB1 signaling of the Wnt pathway compared to wild-type;, features a modification of the amino acid from Y to N at position 259.
+The protein's natural variant, known as in patients affected by schizophrenia;, features a modification of the amino acid from S to N at position 470.
+The protein's natural variant, known as in plasmid pCHL1 and plasmid pCTT1, features a modification of the amino acid from N to D at position 9.
+The protein's natural variant, known as in plasmid pCHL1 and plasmid pCTT1, features a modification of the amino acid from Q to R at position 47.
+The protein's natural variant, known as in plasmid pCTT1, features a modification of the amino acid from VLDQ to CWIE at position 186.
+The protein's natural variant, known as in plasmid pCTT1, features a modification of the amino acid from K to T at position 194.
+The protein's natural variant, known as in plasmid pCTT1, features a modification of the amino acid from S to L at position 205.
+The protein's natural variant, known as in plasmid pCTT1, features a modification of the amino acid from M to I at position 222.
+The protein's natural variant, known as in alpha-D', features a modification of the amino acid from C to N at position 104.
+The protein's natural variant, known as in MECD2;, features a modification of the amino acid from R to P at position 503.
+The protein's natural variant, known as in MECD2;, features a modification of the amino acid from E to K at position 509.
+The natural variant of this protein is characterized by an amino acid alteration from S to N at position 80.
+The natural variant of this protein is characterized by an amino acid alteration from M to V at position 34.
+The protein's natural variant, known as in strain: cv. Fidel, features a modification of the amino acid from T to S at position 171.
+The protein's natural variant, known as in strain: cv. Fidel, features a modification of the amino acid from D to E at position 195.
+The protein's natural variant, known as in strain: cv. Fidel, features a modification of the amino acid from G to R at position 226.
+The protein's natural variant, known as in XIGIS; unknown pathological significance, features a modification of the amino acid from P to S at position 47.
+The protein's natural variant, known as in XIGIS; unknown pathological significance, features a modification of the amino acid from R to W at position 487.
+The protein's natural variant, known as in XIGIS, features a modification of the amino acid from G to D at position 537.
+The protein's natural variant, known as in XIGIS; unknown pathological significance, features a modification of the amino acid from G to S at position 548.
+The protein's natural variant, known as in XIGIS; unknown pathological significance, features a modification of the amino acid from R to H at position 549.
+The protein's natural variant, known as in XIGIS; unknown pathological significance; does not affect nuclear localization, features a modification of the amino acid from D to N at position 607.
+The protein's natural variant, known as in XIGIS; unknown pathological significance; does not affect nuclear localization, features a modification of the amino acid from G to R at position 792.
+The protein's natural variant, known as in XIGIS, features a modification of the amino acid from S to P at position 1348.
+The protein's natural variant, known as in XIGIS, features a modification of the amino acid from D to G at position 1457.
+The protein's natural variant, known as in XIGIS; unknown pathological significance, features a modification of the amino acid from P to S at position 1478.
+The protein's natural variant, known as in XLA;, features a modification of the amino acid from L to P at position 11.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from K to R at position 12.
+The protein's natural variant, known as in XLA;, features a modification of the amino acid from S to F at position 14.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from K to E at position 19.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from F to S at position 25.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from K to R at position 27.
+The protein's natural variant, known as in XLA; no effect on phosphorylation of GTF2I, features a modification of the amino acid from R to C at position 28.
+The protein's natural variant, known as in XLA; moderate;, features a modification of the amino acid from R to H at position 28.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from R to P at position 28.
+The protein's natural variant, known as in XLA; severe;, features a modification of the amino acid from T to P at position 33.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from Y to S at position 39.
+The protein's natural variant, known as in XLA;, features a modification of the amino acid from Y to C at position 40.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from Y to N at position 40.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from I to N at position 61.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from V to D at position 64.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from V to F at position 64.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from Q to QSVFSSTR at position 103.
+The protein's natural variant, known as in XLA;, features a modification of the amino acid from V to D at position 113.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from S to F at position 115.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from T to P at position 117.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from Q to H at position 127.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from C to S at position 154.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from C to G at position 155.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from C to R at position 155.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from T to P at position 184.
+The protein's natural variant, known as in a lung large cell carcinoma sample; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from P to K at position 190.
+The protein's natural variant, known as in XLA;, features a modification of the amino acid from R to Q at position 288.
+The protein's natural variant, known as in XLA;, features a modification of the amino acid from R to W at position 288.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from L to P at position 295.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from G to E at position 302.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from G to R at position 302.
+The protein's natural variant, known as in XLA; loss of activity;, features a modification of the amino acid from R to G at position 307.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from R to T at position 307.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from D to E at position 308.
+The protein's natural variant, known as in XLA; moderate, features a modification of the amino acid from V to A at position 319.
+The protein's natural variant, known as in XLA;, features a modification of the amino acid from Y to S at position 334.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from L to F at position 358.
+The protein's natural variant, known as in XLA; mild;, features a modification of the amino acid from Y to C at position 361.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from H to Q at position 362.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from H to P at position 364.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from N to Y at position 365.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from S to F at position 366.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from L to F at position 369.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from I to M at position 370.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from R to G at position 372.
+The protein's natural variant, known as in XLA; moderate;, features a modification of the amino acid from L to P at position 408.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from G to R at position 414.
+The protein's natural variant, known as in XLA;, features a modification of the amino acid from Y to H at position 418.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from I to N at position 429.
+The protein's natural variant, known as in XLA; loss of phosphorylation of GTF2I;, features a modification of the amino acid from K to E at position 430.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from K to R at position 430.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from E to D at position 445.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from G to D at position 462.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from G to V at position 462.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from Y to D at position 476.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from M to R at position 477.
+The protein's natural variant, known as found in patients with chronic lymphocytic leukemia; unknown pathological significance; results in resistance to ibrutinib therapy; results in a protein that is reversibly inhibited by ibrutinib; disrupts the covalent binding between the enzyme and ibrutinib;, features a modification of the amino acid from C to S at position 481.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from C to F at position 502.
+The protein's natural variant, known as in XLA;, features a modification of the amino acid from C to W at position 502.
+The protein's natural variant, known as in XLA;, features a modification of the amino acid from C to R at position 506.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from C to Y at position 506.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from A to D at position 508.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from M to I at position 509.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from M to V at position 509.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from L to P at position 512.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from L to Q at position 512.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from L to R at position 518.
+The protein's natural variant, known as in XLA; severe; prevents activation due to absence of contact between the catalytic loop and the regulatory phosphorylated residue;, features a modification of the amino acid from R to Q at position 520.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from D to G at position 521.
+The protein's natural variant, known as in XLA; severe, features a modification of the amino acid from D to H at position 521.
+The protein's natural variant, known as in XLA; severe, features a modification of the amino acid from D to N at position 521.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from A to E at position 523.
+The protein's natural variant, known as in XLA;, features a modification of the amino acid from R to G at position 525.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from R to P at position 525.
+The protein's natural variant, known as in XLA; severe; disturbs ATP-binding;, features a modification of the amino acid from R to Q at position 525.
+The protein's natural variant, known as in XLA;, features a modification of the amino acid from N to K at position 526.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from V to F at position 535.
+The protein's natural variant, known as in XLA; growth hormone deficiency;, features a modification of the amino acid from L to P at position 542.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from R to G at position 544.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from R to K at position 544.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from F to S at position 559.
+The protein's natural variant, known as in XLA;, features a modification of the amino acid from R to P at position 562.
+The protein's natural variant, known as in XLA;, features a modification of the amino acid from R to W at position 562.
+The protein's natural variant, known as in XLA;, features a modification of the amino acid from W to L at position 563.
+The protein's natural variant, known as in XLA; severe, features a modification of the amino acid from E to K at position 567.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from S to Y at position 578.
+The protein's natural variant, known as in XLA;, features a modification of the amino acid from W to R at position 581.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from A to V at position 582.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from F to S at position 583.
+The protein's natural variant, known as in XLA; mild;, features a modification of the amino acid from M to L at position 587.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from E to D at position 589.
+The protein's natural variant, known as in XLA; moderate; interferes with substrate binding;, features a modification of the amino acid from E to G at position 589.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from E to K at position 589.
+The protein's natural variant, known as in XLA;, features a modification of the amino acid from S to P at position 592.
+The protein's natural variant, known as in XLA; mild; interferes with substrate binding, features a modification of the amino acid from G to E at position 594.
+The protein's natural variant, known as in XLA;, features a modification of the amino acid from G to R at position 594.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from Y to C at position 598.
+The protein's natural variant, known as in XLA; mild;, features a modification of the amino acid from A to D at position 607.
+The protein's natural variant, known as in XLA; mild; interferes with substrate binding and/or domain interactions;, features a modification of the amino acid from G to D at position 613.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from P to A at position 619.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from P to S at position 619.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from P to T at position 619.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from A to P at position 622.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from V to G at position 626.
+The natural variant of this protein is characterized by an amino acid alteration from M to I at position 630.
+The protein's natural variant, known as in XLA;, features a modification of the amino acid from M to K at position 630.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from M to T at position 630.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from C to Y at position 633.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from R to C at position 641.
+The protein's natural variant, known as in XLA; severe, features a modification of the amino acid from R to H at position 641.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from F to L at position 644.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from F to S at position 644.
+The protein's natural variant, known as in XLA, features a modification of the amino acid from L to P at position 647.
+The protein's natural variant, known as in XLA;, features a modification of the amino acid from L to P at position 652.
+The protein's natural variant, known as in strain: Sgu52E and Sgu52F, features a modification of the amino acid from G to E at position 110.
+The protein's natural variant, known as in strain: MMW1-15h2, MMW1-2h2, Sgu52E and Sgu52F, features a modification of the amino acid from N to D at position 120.
+The protein's natural variant, known as in strain: MMW1-15h2, MMW1-2h2, Sgu52E and Sgu52F, features a modification of the amino acid from V to I at position 228.
+The protein's natural variant, known as in strain: MMW1-15h2 and MMW1-2h2, features a modification of the amino acid from D to N at position 238.
+The protein's natural variant, known as in NBIA8; unknown pathological significance; loss of expression at the protein level and drastic decrease in beta-oxidation of palmitate in homozygous patient's primary fibroblasts as compared to wild-type cells; primary fibroblasts from a homozygous patient show much higher intracellular iron content than fibroblasts from control individuals and abnormally elevated levels of transferrin receptor 1/TFRC at the cell surface;, features a modification of the amino acid from R to H at position 321.
+The natural variant of this protein is characterized by an amino acid alteration from D to N at position 159.
+The natural variant of this protein is characterized by an amino acid alteration from R to H at position 359.
+The natural variant of this protein is characterized by an amino acid alteration from H to Y at position 418.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 448.
+The natural variant of this protein is characterized by an amino acid alteration from K to T at position 255.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from P to A at position 591.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to L at position 652.
+The protein's natural variant, known as in CSB;, features a modification of the amino acid from R to W at position 670.
+The protein's natural variant, known as in CSB;, features a modification of the amino acid from N to D at position 680.
+The protein's natural variant, known as in CSB;, features a modification of the amino acid from W to C at position 686.
+The protein's natural variant, known as in CSB;, features a modification of the amino acid from S to L at position 687.
+The protein's natural variant, known as in CSB; DNA-dependent ATPase-dead mutant; loss of chromatin remodeling activity; loss of its ability to inhibit non-homologous end joining-mediated repair and promote homologous recombination-mediated repair of DNA double-strand breaks; loss of its ability to suppress premature exit from G2/M checkpoint; abrogation of its UV-induced chromatin association;, features a modification of the amino acid from W to R at position 851.
+The protein's natural variant, known as in COFS1, features a modification of the amino acid from L to P at position 871.
+The protein's natural variant, known as in CSB, features a modification of the amino acid from V to G at position 957.
+The protein's natural variant, known as in COFS1;, features a modification of the amino acid from L to P at position 987.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from R to T at position 1038.
+The protein's natural variant, known as in CSB, features a modification of the amino acid from P to L at position 1042.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from E to Q at position 1119.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from E to V at position 1119.
+The protein's natural variant, known as found in CVM; Holstein cattle. Does not rescue defective transport of UDP-N-acetylglucosamine into Golgi lumen in SLC35A3-deficient cells, features a modification of the amino acid from V to F at position 180.
+The protein's natural variant, known as in IMD11B; no effect on protein abundance; decreased interaction with BCL10; dominant negative effect on NF-kappa-B signaling; dominant negative effect on TORC1 signaling, features a modification of the amino acid from E to D at position 57.
+The protein's natural variant, known as in BENTA; results in protein aggregation; constitutive activation of NF-kappa-B signaling;, features a modification of the amino acid from G to S at position 123.
+The protein's natural variant, known as in BENTA; results in protein aggregation; constitutive activation of NF-kappa-B signaling;, features a modification of the amino acid from E to G at position 134.
+The protein's natural variant, known as in IMD11B; no effect on protein abundance; decreased interaction with BCL10; dominant negative effect on NF-kappa-B signaling; dominant negative effect on TORC1 signaling, features a modification of the amino acid from L to P at position 194.
+The protein's natural variant, known as in IMD11B; no effect on protein abundance; dominant negative effect on NF-kappaB signaling; dominant negative effect on TORC1 signaling;, features a modification of the amino acid from R to W at position 975.
+The protein's natural variant, known as found in a consanguineous family with intellectual disability; unknown pathological significance, features a modification of the amino acid from K to N at position 2056.
+The protein's natural variant, known as in FCHL3; associated with disease susceptibility; has approximately 80% of the specific activity of wild-type enzyme;, features a modification of the amino acid from D to N at position 36.
+The protein's natural variant, known as in HLPP1; produces an inactive protein which is not secreted into the media, features a modification of the amino acid from N to S at position 70.
+The protein's natural variant, known as in HLPP1; gives rise to a 80% decrease in specific catalytic activity;, features a modification of the amino acid from V to L at position 96.
+The protein's natural variant, known as in HLPP1; decreases the specific activity of the enzyme; reduces the secretion of the mutant protein significantly; the total LPL mass is reduced compared to that of the wild-type construct;, features a modification of the amino acid from A to T at position 98.
+The protein's natural variant, known as in HLPP1;, features a modification of the amino acid from R to S at position 102.
+The protein's natural variant, known as in HLPP1, features a modification of the amino acid from W to G at position 113.
+The protein's natural variant, known as in HLPP1;, features a modification of the amino acid from W to R at position 113.
+The protein's natural variant, known as in HLPP1, features a modification of the amino acid from T to A at position 128.
+The protein's natural variant, known as in HLPP1; synthesized as a catalytically inactive form, features a modification of the amino acid from G to R at position 132.
+The protein's natural variant, known as in HLPP1, features a modification of the amino acid from H to R at position 163.
+The protein's natural variant, known as in HLPP1; loss of activity;, features a modification of the amino acid from G to E at position 169.
+The protein's natural variant, known as in HLPP1, features a modification of the amino acid from G to S at position 181.
+The protein's natural variant, known as in HLPP1; synthesized as a catalytically inactive form, features a modification of the amino acid from G to V at position 181.
+The protein's natural variant, known as in HLPP1; lacks both triolein and tributyrin esterase activities;, features a modification of the amino acid from D to G at position 183.
+The protein's natural variant, known as in HLPP1;, features a modification of the amino acid from D to H at position 183.
+The protein's natural variant, known as in HLPP1; lacks both triolein and tributyrin esterase activities;, features a modification of the amino acid from D to N at position 183.
+The protein's natural variant, known as in HLPP1; Nijmegen; loss of activity, features a modification of the amino acid from P to R at position 184.
+The protein's natural variant, known as in HLPP1; 3.2% of activity;, features a modification of the amino acid from A to T at position 185.
+The protein's natural variant, known as in HLPP1, features a modification of the amino acid from G to E at position 186.
+The protein's natural variant, known as in HLPP1, features a modification of the amino acid from E to G at position 190.
+The protein's natural variant, known as in HLPP1; mild hypertriglyceridemia; partial activity;, features a modification of the amino acid from S to C at position 199.
+The protein's natural variant, known as in HLPP1; almost complete loss of enzyme activity, features a modification of the amino acid from D to V at position 201.
+The protein's natural variant, known as in HLPP1; Bethesda; loss of activity and abnormal heparin binding;, features a modification of the amino acid from A to T at position 203.
+The protein's natural variant, known as in HLPP1;, features a modification of the amino acid from D to E at position 207.
+The protein's natural variant, known as in HLPP1; decreases the specific activity of the enzyme; has a mild effect on the secretion of the mutant enzyme; the total LPL mass is reduced compared to that of the wild-type construct;, features a modification of the amino acid from V to I at position 208.
+The protein's natural variant, known as in HLPP1; complete loss of enzyme activity, features a modification of the amino acid from H to D at position 210.
+The protein's natural variant, known as in HLPP1; loss of activity, features a modification of the amino acid from H to Q at position 210.
+The protein's natural variant, known as in HLPP1; loss of activity;, features a modification of the amino acid from G to E at position 215.
+The protein's natural variant, known as in HLPP1, features a modification of the amino acid from G to R at position 215.
+The protein's natural variant, known as in HLPP1; 2.0% of activity;, features a modification of the amino acid from S to R at position 220.
+The protein's natural variant, known as in HLPP1; loss of activity;, features a modification of the amino acid from I to T at position 221.
+The protein's natural variant, known as in HLPP1;, features a modification of the amino acid from G to E at position 222.
+The protein's natural variant, known as in HLPP1, features a modification of the amino acid from K to R at position 225.
+The protein's natural variant, known as in HLPP1;, features a modification of the amino acid from V to A at position 227.
+The protein's natural variant, known as in HLPP1; loss of activity;, features a modification of the amino acid from D to E at position 231.
+The protein's natural variant, known as in HLPP1; loss of activity;, features a modification of the amino acid from I to S at position 232.
+The protein's natural variant, known as in HLPP1; loss of activity;, features a modification of the amino acid from P to L at position 234.
+The protein's natural variant, known as in HLPP1; loss of activity, features a modification of the amino acid from C to S at position 243.
+The protein's natural variant, known as in HLPP1;, features a modification of the amino acid from I to T at position 252.
+The protein's natural variant, known as in HLPP1;, features a modification of the amino acid from C to W at position 266.
+The protein's natural variant, known as in HLPP1;, features a modification of the amino acid from R to C at position 270.
+The protein's natural variant, known as in HLPP1; loss of activity;, features a modification of the amino acid from R to H at position 270.
+The protein's natural variant, known as in HLPP1;, features a modification of the amino acid from S to T at position 271.
+The protein's natural variant, known as in HLPP1; 5% of full activity;, features a modification of the amino acid from D to N at position 277.
+The protein's natural variant, known as in HLPP1, features a modification of the amino acid from S to C at position 278.
+The protein's natural variant, known as in HLPP1; decreases the specific activity of the enzyme; the total LPL mass is reduced compared to that of the wild-type construct;, features a modification of the amino acid from L to R at position 279.
+The protein's natural variant, known as in HLPP1; decreases the specific activity of the enzyme; the total LPL mass is reduced compared to that of the wild-type construct;, features a modification of the amino acid from L to V at position 279.
+The protein's natural variant, known as in HLPP1, features a modification of the amino acid from S to G at position 286.
+The protein's natural variant, known as in HLPP1, features a modification of the amino acid from S to R at position 286.
+The protein's natural variant, known as in HLPP1; the LPL mass level is approximately 67% of the normal; the activity is 32% of the nornal;, features a modification of the amino acid from A to T at position 288.
+The protein's natural variant, known as in HLPP1; no enzyme activity;, features a modification of the amino acid from Y to H at position 289.
+The protein's natural variant, known as in HLPP1 and hyperlipidemia; synthesized as a catalytically inactive form; total amount is almost equal to that of the normal enzyme; non-releasable by heparin due to the abnormal structure of the mutant protein, features a modification of the amino acid from F to L at position 297.
+The protein's natural variant, known as in HLPP1; approximately 6% of normal LPL activity and 40% of LPL mass are detected in the patient's postheparin plasma; results in the production of a functionally inactive enzyme, features a modification of the amino acid from L to F at position 303.
+The protein's natural variant, known as in HLPP1;, features a modification of the amino acid from C to R at position 305.
+The protein's natural variant, known as in HLPP1; decreases the specific activity of the enzyme; reduces the secretion of the mutant protein significantly; the total LPL mass is reduced compared to that of the wild-type construct;, features a modification of the amino acid from C to Y at position 310.
+The protein's natural variant, known as in HLPP1, features a modification of the amino acid from L to P at position 313.
+The protein's natural variant, known as in FCHL3; associated with disease susceptibility; loss of activity; frequent mutation;, features a modification of the amino acid from N to S at position 318.
+The protein's natural variant, known as in HLPP1; has no effect on the specific activity of the enzyme; has a mild effect on the secretion of the mutant enzyme; the total LPL mass is reduced compared to that of the wild-type construct;, features a modification of the amino acid from S to R at position 325.
+The protein's natural variant, known as in HLPP1, features a modification of the amino acid from M to R at position 328.
+The protein's natural variant, known as in HLPP1;, features a modification of the amino acid from M to T at position 328.
+The protein's natural variant, known as in HLPP1, features a modification of the amino acid from L to F at position 330.
+The protein's natural variant, known as in HLPP1, features a modification of the amino acid from L to P at position 330.
+The protein's natural variant, known as in HLPP1;, features a modification of the amino acid from A to T at position 361.
+The protein's natural variant, known as in HLPP1; increases the specific activity of the enzyme; has a mild effect on the secretion of the mutant enzyme; the total LPL mass is reduced compared to that of the wild-type construct;, features a modification of the amino acid from S to F at position 365.
+The protein's natural variant, known as in HLPP1; loss of activity;, features a modification of the amino acid from L to V at position 392.
+The protein's natural variant, known as in HLPP1; decreased protein secretion; loss of interaction with GPIHBP1; decreased lipoprotein lipase activity, features a modification of the amino acid from M to R at position 404.
+The protein's natural variant, known as in HLPP1, features a modification of the amino acid from E to K at position 437.
+The protein's natural variant, known as in HLPP1, features a modification of the amino acid from E to V at position 437.
+The protein's natural variant, known as in HLPP1; has 48% of normal activity in vitro; decreased levels of activity account for by the lower protein mass levels of the mutants rather than by decreased enzymatic activities; loss of interaction with GPIHBP1;, features a modification of the amino acid from C to Y at position 445.
+The protein's natural variant, known as in HLPP1; results in a moderate reduction in catalytic activity;, features a modification of the amino acid from E to K at position 448.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from R to C at position 39.
+The protein's natural variant, known as in strain: cv. Wassilewskija-2, features a modification of the amino acid from S to Y at position 307.
+The protein's natural variant, known as in strain: Isolate 13, features a modification of the amino acid from F to L at position 24.
+The protein's natural variant, known as in strain: Isolate 13 and Isolate N2, features a modification of the amino acid from G to S at position 140.
+The protein's natural variant, known as in strain: Isolate 13 and Isolate N2, features a modification of the amino acid from D to G at position 177.
+The protein's natural variant, known as in strain: Isolate 13 and Isolate N2, features a modification of the amino acid from V to D at position 197.
+The protein's natural variant, known as in strain: Isolate 13 and Isolate N2, features a modification of the amino acid from S to P at position 284.
+The protein's natural variant, known as in strain: Isolate 13 and Isolate N2, features a modification of the amino acid from T to A at position 297.
+The protein's natural variant, known as in strain: Isolate 13, features a modification of the amino acid from T to A at position 333.
+The protein's natural variant, known as found in a patient with syndromic intellectual disability; probable disease-associated variant; does not affect interaction with DBN1, features a modification of the amino acid from G to E at position 230.
+The protein's natural variant, known as probable disease-associated variant found in a patient with syndromic intellectual disability; probable disease-associated variant; disrupts interaction with DBN1, features a modification of the amino acid from W to R at position 291.
+The protein's natural variant, known as found in a patient with syndromic intellectual disability; probable disease-associated variant; disrupts interaction with DBN1, features a modification of the amino acid from F to L at position 307.
+The protein's natural variant, known as found in a patient with syndromic intellectual disability; probable disease-associated variant; does not affect interaction with DBN1, features a modification of the amino acid from K to E at position 334.
+The protein's natural variant, known as found in a patient with syndromic intellectual disability; probable disease-associated variant, features a modification of the amino acid from E to K at position 980.
+The protein's natural variant, known as found in a patient with syndromic intellectual disability; probable disease-associated variant; disrupts interaction with GATAD2A, features a modification of the amino acid from C to S at position 1039.
+The protein's natural variant, known as found in a patient with syndromic intellectual disability; probable disease-associated variant; does not affect interaction with GATAD2A, features a modification of the amino acid from H to R at position 1054.
+The protein's natural variant, known as found in two patients with syndromic intellectual disability; probable disease-associated variant; disrupts interaction with GATAD2A, features a modification of the amino acid from W to R at position 1055.
+The protein's natural variant, known as in GAN2; interaction with DDB1 is decreased;, features a modification of the amino acid from R to C at position 317.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 84.
+The natural variant of this protein is characterized by an amino acid alteration from V to A at position 109.
+The natural variant of this protein is characterized by an amino acid alteration from L to S at position 346.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from V to M at position 484.
+The natural variant of this protein is characterized by an amino acid alteration from P to L at position 2348.
+The natural variant of this protein is characterized by an amino acid alteration from I to L at position 55.
+The natural variant of this protein is characterized by an amino acid alteration from L to V at position 145.
+The natural variant of this protein is characterized by an amino acid alteration from P to R at position 148.
+The natural variant of this protein is characterized by an amino acid alteration from L to M at position 171.
+The protein's natural variant, known as in IBD31; decreased stability; increased degradation; decreased localization to the nucleus; decreased localization to the extracellular space; decreased function in regulation of inflammatory response, features a modification of the amino acid from I to T at position 177.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from E to K at position 716.
+The natural variant of this protein is characterized by an amino acid alteration from A to P at position 314.
+The protein's natural variant, known as in strain: DBA/2J, features a modification of the amino acid from E to G at position 350.
+The protein's natural variant, known as in strain: DBA/2J, features a modification of the amino acid from P to R at position 352.
+The natural variant of this protein is characterized by an amino acid alteration from KL to NF at position 624.
+The protein's natural variant, known as in strain: PA103 and N-10, features a modification of the amino acid from Y to T at position 75.
+The protein's natural variant, known as in strain: PA103 and N-10, features a modification of the amino acid from Q to R at position 102.
+The protein's natural variant, known as in strain: PA103 and N-10, features a modification of the amino acid from T to Y at position 185.
+The protein's natural variant, known as in strain: 569B, features a modification of the amino acid from K to I at position 211.
+The protein's natural variant, known as in strain: PA103 and N-10, features a modification of the amino acid from S to G at position 241.
+The protein's natural variant, known as in strain: PA103 and N-10, features a modification of the amino acid from K to D at position 282.
+The protein's natural variant, known as in strain: IFO 3455, features a modification of the amino acid from M to V at position 325.
+The protein's natural variant, known as in strain: PA103, features a modification of the amino acid from R to S at position 471.
+The protein's natural variant, known as in K version, features a modification of the amino acid from A to S at position 21.
+The protein's natural variant, known as in S version, features a modification of the amino acid from A to S at position 311.
+The protein's natural variant, known as in S version, features a modification of the amino acid from D to E at position 456.
+The protein's natural variant, known as in MC3DN5;, features a modification of the amino acid from R to W at position 183.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from F to Y at position 208.
+The protein's natural variant, known as in MODY2, features a modification of the amino acid from V to E at position 16.
+The protein's natural variant, known as in MODY2, features a modification of the amino acid from I to N at position 19.
+The protein's natural variant, known as in MODY2, features a modification of the amino acid from L to P at position 20.
+The protein's natural variant, known as in MODY2;, features a modification of the amino acid from R to W at position 36.
+The protein's natural variant, known as in PNDM1; decreased stability; decreased glucokinase activity; decreased affinity for glucose;, features a modification of the amino acid from E to K at position 40.
+The protein's natural variant, known as in PNDM1; decreased stability; decreased glucokinase activity; no effect on affinity for glucose;, features a modification of the amino acid from R to C at position 43.
+The protein's natural variant, known as in MODY2; unknown pathological significance; no change in glucokinase activity;, features a modification of the amino acid from R to H at position 43.
+The protein's natural variant, known as in MODY2;, features a modification of the amino acid from R to S at position 43.
+The protein's natural variant, known as in MODY2;, features a modification of the amino acid from G to S at position 44.
+The protein's natural variant, known as in PNDM1; loss of stability; loss of glucokinase activity; decreased affinity for glucose, features a modification of the amino acid from H to D at position 50.
+The protein's natural variant, known as in MODY2, features a modification of the amino acid from A to S at position 53.
+The protein's natural variant, known as in MODY2; decreased glucokinase activity; decreased affinity for glucose; increased affinity for ATP, features a modification of the amino acid from Y to S at position 61.
+The protein's natural variant, known as in HHF3; increased glucokinase activity based on measure of catalytic efficiency; increased affinity for glucose; loss of inhibition by GCKR; unchanged affinity for ATP, features a modification of the amino acid from T to I at position 65.
+The protein's natural variant, known as in MODY2; unknown pathological significance; mildly increases glucokinase activity;, features a modification of the amino acid from G to D at position 68.
+The protein's natural variant, known as in MODY2; decreased affinity for glucose, features a modification of the amino acid from E to K at position 70.
+The protein's natural variant, known as in MODY2 and PNDM1; decreased stability; no effect on glucokinase activity; no effect on affinity for glucose;, features a modification of the amino acid from G to R at position 72.
+The protein's natural variant, known as in MODY2;, features a modification of the amino acid from L to P at position 77.
+The protein's natural variant, known as in MODY2, features a modification of the amino acid from D to E at position 78.
+The protein's natural variant, known as in MODY2, features a modification of the amino acid from G to A at position 80.
+The protein's natural variant, known as in MODY2, features a modification of the amino acid from G to D at position 80.
+The protein's natural variant, known as in MODY2;, features a modification of the amino acid from G to S at position 80.
+The protein's natural variant, known as in MODY2, features a modification of the amino acid from T to I at position 82.
+The protein's natural variant, known as in HHF3; increased glucokinase activity; increased affinity for glucose, features a modification of the amino acid from V to L at position 91.
+The protein's natural variant, known as in HHF3; increased glucokinase activity; increased affinity for glucose; increased affinity for ATP, features a modification of the amino acid from W to C at position 99.
+The natural variant of this protein is characterized by an amino acid alteration from M to T at position 107.
+The protein's natural variant, known as in MODY2;, features a modification of the amino acid from Y to H at position 108.
+The protein's natural variant, known as in MODY2;, features a modification of the amino acid from I to T at position 110.
+The protein's natural variant, known as in MODY2, features a modification of the amino acid from T to P at position 116.
+The protein's natural variant, known as in MODY2;, features a modification of the amino acid from A to D at position 119.
+The protein's natural variant, known as in MODY2, features a modification of the amino acid from C to Y at position 129.
+The protein's natural variant, known as in MODY2; decreased affinity for glucose;, features a modification of the amino acid from S to P at position 131.
+The protein's natural variant, known as in MODY2, features a modification of the amino acid from H to R at position 137.
+The protein's natural variant, known as in MODY2;, features a modification of the amino acid from F to S at position 150.
+The protein's natural variant, known as in PNDM1, features a modification of the amino acid from S to T at position 151.
+The protein's natural variant, known as in MODY2; unknown pathological significance;, features a modification of the amino acid from F to L at position 152.
+The protein's natural variant, known as in MODY2; decreased glucokinase activity; decreased affinity for glucose;, features a modification of the amino acid from D to N at position 160.
+The protein's natural variant, known as in MODY2 and PNDM1;, features a modification of the amino acid from L to P at position 164.
+The protein's natural variant, known as in PNDM1; decreased glucokinase activity; decreased affinity for glucose, features a modification of the amino acid from T to A at position 168.
+The protein's natural variant, known as in MODY2, features a modification of the amino acid from T to P at position 168.
+The protein's natural variant, known as in PNDM1, features a modification of the amino acid from K to R at position 169.
+The protein's natural variant, known as in MODY2;, features a modification of the amino acid from G to R at position 175.
+The protein's natural variant, known as in MODY2; decreased glucokinase activity; decreased affinity for glucose; increased affinity for ATP, features a modification of the amino acid from V to L at position 182.
+The protein's natural variant, known as in MODY2;, features a modification of the amino acid from V to M at position 182.
+The protein's natural variant, known as in MODY2, features a modification of the amino acid from D to Y at position 187.
+The protein's natural variant, known as in MODY2; decreased affinity for glucose;, features a modification of the amino acid from A to T at position 188.
+The protein's natural variant, known as in MODY2;, features a modification of the amino acid from A to V at position 188.
+The protein's natural variant, known as in MODY2;, features a modification of the amino acid from R to W at position 191.
+The protein's natural variant, known as in MODY2, features a modification of the amino acid from V to L at position 200.
+The protein's natural variant, known as in MODY2, features a modification of the amino acid from M to R at position 202.
+The protein's natural variant, known as in MODY2;, features a modification of the amino acid from M to T at position 202.
+The protein's natural variant, known as in MODY2;, features a modification of the amino acid from V to A at position 203.
+The protein's natural variant, known as in MODY2;, features a modification of the amino acid from T to M at position 206.
+The protein's natural variant, known as in MODY2;, features a modification of the amino acid from T to M at position 209.
+The protein's natural variant, known as in MODY2 and PNDM1;, features a modification of the amino acid from M to K at position 210.
+The protein's natural variant, known as in MODY2;, features a modification of the amino acid from M to T at position 210.
+The protein's natural variant, known as in MODY2, features a modification of the amino acid from C to R at position 213.
+The protein's natural variant, known as in HHF3; increased glucokinase activity based on measure of catalytic efficiency; increased affinity for glucose; decreased inhibition by GCKR;, features a modification of the amino acid from Y to C at position 214.
+The protein's natural variant, known as in MODY2; associated in cis with R-261 in some patients; mildly increased glucokinase activity; loss of glucokinase activity when associated with R-261;, features a modification of the amino acid from D to N at position 217.
+The protein's natural variant, known as in MODY2;, features a modification of the amino acid from E to K at position 221.
+The protein's natural variant, known as in MODY2;, features a modification of the amino acid from G to S at position 223.
+The protein's natural variant, known as in MODY2, features a modification of the amino acid from M to R at position 224.
+The protein's natural variant, known as in MODY2; associated in cis with K-248; highly decreased glucokinase activity; loss of glucokinase activity when associated with K-248;, features a modification of the amino acid from I to M at position 225.
+The protein's natural variant, known as in MODY2; no effect on stability; decreased glucokinase activity; decreased affinity for glucose;, features a modification of the amino acid from V to M at position 226.
+The protein's natural variant, known as in MODY2, features a modification of the amino acid from G to C at position 227.
+The protein's natural variant, known as in MODY2, features a modification of the amino acid from G to S at position 227.
+The protein's natural variant, known as in MODY2 and PNDM1;, features a modification of the amino acid from T to M at position 228.
+The protein's natural variant, known as in MODY2; unknown pathological significance, features a modification of the amino acid from N to H at position 231.
+The protein's natural variant, known as in MODY2; loss of glucokinase activity; loss of affinity for glucose; loss of affinity for ATP, features a modification of the amino acid from C to R at position 233.
+The protein's natural variant, known as in MODY2; associated in cis with M-225; highly decreased glucokinase activity; loss of glucokinase activity when associated with M-225;, features a modification of the amino acid from E to K at position 248.
+The protein's natural variant, known as in MODY2, features a modification of the amino acid from C to G at position 252.
+The protein's natural variant, known as in MODY2, features a modification of the amino acid from T to A at position 255.
+The protein's natural variant, known as in MODY2;, features a modification of the amino acid from E to K at position 256.
+The protein's natural variant, known as in MODY2; almost complete loss of glucokinase activity;, features a modification of the amino acid from W to R at position 257.
+The protein's natural variant, known as in MODY2;, features a modification of the amino acid from A to T at position 259.
+The protein's natural variant, known as in MODY2, features a modification of the amino acid from G to E at position 261.
+The protein's natural variant, known as in MODY2 and PNDM1; associated in cis with N-217 in some patients; highly decreased glucokinase activity; loss of glucokinase activity when associated with N-217; decreased affinity for glucose;, features a modification of the amino acid from G to R at position 261.
+The protein's natural variant, known as in MODY2; decreased glucokinase activity; decreased affinity for glucose; no effect on affinity for ATP;, features a modification of the amino acid from E to K at position 265.
+The protein's natural variant, known as in MODY2;, features a modification of the amino acid from E to Q at position 279.
+The protein's natural variant, known as in MODY2, features a modification of the amino acid from M to K at position 298.
+The protein's natural variant, known as in MODY2;, features a modification of the amino acid from G to R at position 299.
+The protein's natural variant, known as in MODY2;, features a modification of the amino acid from E to K at position 300.
+The protein's natural variant, known as in MODY2, features a modification of the amino acid from E to Q at position 300.
+The protein's natural variant, known as in MODY2, features a modification of the amino acid from R to W at position 308.
+The protein's natural variant, known as in MODY2, features a modification of the amino acid from L to P at position 309.
+The protein's natural variant, known as in MODY2; unknown pathological significance;, features a modification of the amino acid from L to F at position 315.
+The protein's natural variant, known as in MODY2, features a modification of the amino acid from S to L at position 336.
+The protein's natural variant, known as in MODY2;, features a modification of the amino acid from V to M at position 367.
+The protein's natural variant, known as in MODY2;, features a modification of the amino acid from R to H at position 377.
+The protein's natural variant, known as in MODY2;, features a modification of the amino acid from A to T at position 378.
+The protein's natural variant, known as in MODY2; decreased glucokinase activity; decreased affinity for glucose; decreased affinity for ATP;, features a modification of the amino acid from A to V at position 379.
+The protein's natural variant, known as in MODY2, features a modification of the amino acid from C to Y at position 382.
+The protein's natural variant, known as in MODY2;, features a modification of the amino acid from S to L at position 383.
+The protein's natural variant, known as in MODY2;, features a modification of the amino acid from A to T at position 384.
+The protein's natural variant, known as in MODY2, features a modification of the amino acid from G to V at position 385.
+The protein's natural variant, known as in MODY2;, features a modification of the amino acid from R to C at position 392.
+The protein's natural variant, known as in PNDM1; decreased stability; increased glucokinase activity; no effect on affinity for glucose;, features a modification of the amino acid from M to T at position 393.
+The protein's natural variant, known as in PNDM1; decreased stability; increased glucokinase activity; no effect on affinity for glucose;, features a modification of the amino acid from R to L at position 397.
+The protein's natural variant, known as in MODY2, features a modification of the amino acid from S to F at position 411.
+The protein's natural variant, known as in MODY2; decreased affinity for glucose;, features a modification of the amino acid from K to E at position 414.
+The protein's natural variant, known as in MODY2;, features a modification of the amino acid from H to P at position 416.
+The protein's natural variant, known as in MODY2; no effect on glucokinase activity; decreased affinity for glucose; no effect on affinity for ATP, features a modification of the amino acid from K to E at position 420.
+The protein's natural variant, known as in MODY2; unknown pathological significance, features a modification of the amino acid from C to F at position 434.
+The protein's natural variant, known as in PNDM1; decreased stability; decreased glucokinase activity; no effect on affinity for glucose;, features a modification of the amino acid from S to L at position 441.
+The protein's natural variant, known as in MODY2; decreased affinity for glucose, features a modification of the amino acid from S to W at position 441.
+The protein's natural variant, known as in HHF3; increased affinity for glucose;, features a modification of the amino acid from E to K at position 442.
+The protein's natural variant, known as in MODY2;, features a modification of the amino acid from R to Q at position 447.
+The protein's natural variant, known as in PNDM1; decreased stability; increased glucokinase activity; increased affinity for glucose;, features a modification of the amino acid from A to T at position 449.
+The protein's natural variant, known as in HHF3; increased glucokinase activity based on measure of catalytic efficiency; increased affinity for glucose; decreased inhibition by GCKR; no effect on affinity for ATP;, features a modification of the amino acid from V to M at position 455.
+The protein's natural variant, known as in HHF3; increased glucokinase activity based on measure of catalytic efficiency; increased affinity for glucose; loss of inhibition by GCKR; no effect on affinity for ATP;, features a modification of the amino acid from A to V at position 456.
+The protein's natural variant, known as in strain: ZIM5C, ZIM10C, ZIM16C, ZIM18C, ZIM28C, ZIM30C, ZIM34C and ZIM53C, features a modification of the amino acid from Q to H at position 22.
+The protein's natural variant, known as in strain: ZIM7C and ZIM12C, features a modification of the amino acid from Q to P at position 22.
+The protein's natural variant, known as in strain: ZIM28C, features a modification of the amino acid from EVVDDI to GKRNTR at position 337.
+The protein's natural variant, known as in strain: Canton-S and ZIM34C, features a modification of the amino acid from D to N at position 338.
+The protein's natural variant, known as in strain: Canton-S, ZIM12C and ZIM16C, features a modification of the amino acid from I to V at position 359.
+The protein's natural variant, known as in strain: ZIM5C and ZIM16C, features a modification of the amino acid from K to M at position 381.
+The protein's natural variant, known as in DM1; unknown pathological significance;, features a modification of the amino acid from T to M at position 32.
+The protein's natural variant, known as in DM1; unknown pathological significance, features a modification of the amino acid from P to S at position 338.
+The protein's natural variant, known as found in a patient with multiple congenital anomalies; does not affect CREB1 phosphorylation at S-119; fails to interact with CREBBP;, features a modification of the amino acid from D to G at position 102.
+The protein's natural variant, known as in MCVD; loss of function;, features a modification of the amino acid from G to V at position 508.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from D to N at position 613.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from T to I at position 3.
+The protein's natural variant, known as in PFD; type II; inhibits secretion and oligomerization, features a modification of the amino acid from C to Y at position 32.
+The protein's natural variant, known as in PFD; type II;, features a modification of the amino acid from R to W at position 100.
+The protein's natural variant, known as in PFD; type II; decreases expression, inhibits oligomerization and fails to stimulate bacteriolysis; does not affect binding to Complement C3 beta chain, features a modification of the amino acid from E to K at position 244.
+The protein's natural variant, known as in PFD; type I;, features a modification of the amino acid from G to V at position 298.
+The protein's natural variant, known as in PFD; type II; significantly decreases Complement C3 beta chain binding, features a modification of the amino acid from Q to R at position 343.
+The protein's natural variant, known as in PFD; type III; significantly decreases Complement C3 beta chain binding;, features a modification of the amino acid from Y to D at position 414.
+The protein's natural variant, known as in strain: Wpg6, Wpg8 and Wpg12, features a modification of the amino acid from C to S at position 45.
+The protein's natural variant, known as in strain: Zim10, features a modification of the amino acid from G to D at position 54.
+The protein's natural variant, known as in strain: fs(3)Neo61, Wpg1, Wpg10, Wpg16, Wpg2, Wpg3, Zim10, Zim18, Zim32 and Zim35, features a modification of the amino acid from A to S at position 239.
+The protein's natural variant, known as in strain: Wpg4, features a modification of the amino acid from F to Y at position 243.
+The protein's natural variant, known as in strain: Zim10, features a modification of the amino acid from P to R at position 394.
+The protein's natural variant, known as in DEE36; disease features include abnormal isoelectric focusing of serum transferrin consistent with a glycosylation defect; enzyme activity at about 17% of wild-type;, features a modification of the amino acid from K to E at position 94.
+The protein's natural variant, known as in DEE36; de novo mutation detected in unrelated patients;, features a modification of the amino acid from N to S at position 107.
+The protein's natural variant, known as in CSNB2A, features a modification of the amino acid from C to R at position 74.
+The protein's natural variant, known as in CSNB2A, features a modification of the amino acid from G to R at position 150.
+The protein's natural variant, known as in CSNB2A, features a modification of the amino acid from S to P at position 229.
+The protein's natural variant, known as in CSNB2A, features a modification of the amino acid from G to R at position 261.
+The protein's natural variant, known as in CSNB2A;, features a modification of the amino acid from G to D at position 369.
+The protein's natural variant, known as in CSNB2A;, features a modification of the amino acid from R to Q at position 519.
+The protein's natural variant, known as in AIED and CSNB2A;, features a modification of the amino acid from G to R at position 603.
+The protein's natural variant, known as in CSNB2A; unknown pathological significance;, features a modification of the amino acid from V to I at position 635.
+The protein's natural variant, known as in CSNB2A, features a modification of the amino acid from G to D at position 674.
+The protein's natural variant, known as in CSNB2A;, features a modification of the amino acid from F to C at position 753.
+The protein's natural variant, known as in CSNB2A; increases the number of mutant channels open at physiologic membrane potential and allows for persistent Ca(2+) entry due to reduced channel inactivation resulting in a gain-of-function defect;, features a modification of the amino acid from I to T at position 756.
+The protein's natural variant, known as in CSNB2A, features a modification of the amino acid from L to P at position 860.
+The protein's natural variant, known as in CSNB2A, features a modification of the amino acid from A to D at position 928.
+The protein's natural variant, known as in CSNB2A;, features a modification of the amino acid from G to R at position 1018.
+The protein's natural variant, known as in CSNB2A, features a modification of the amino acid from R to W at position 1060.
+The protein's natural variant, known as in CSNB2A, features a modification of the amino acid from L to P at position 1079.
+The protein's natural variant, known as in CSNB2A, features a modification of the amino acid from L to H at position 1375.
+The protein's natural variant, known as in CSNB2A, features a modification of the amino acid from C to R at position 1499.
+The protein's natural variant, known as in CSNB2A, features a modification of the amino acid from P to R at position 1500.
+The protein's natural variant, known as in CSNB2A;, features a modification of the amino acid from L to P at position 1508.
+The protein's natural variant, known as in FANCC;, features a modification of the amino acid from D to V at position 195.
+The protein's natural variant, known as in FANCC;, features a modification of the amino acid from L to R at position 496.
+The protein's natural variant, known as in FANCC; loss of activity; loss of CDK1-binding and IFNG-induced STAT1-binding; abnormal EIF2AK2 activation and augmented cell death;, features a modification of the amino acid from L to P at position 554.
+The natural variant of this protein is characterized by an amino acid alteration from VQ to IE at position 288.
+The natural variant of this protein is characterized by an amino acid alteration from A to R at position 302.
+The protein's natural variant, known as in BnSP-6 and Bn-IV, features a modification of the amino acid from Q to G at position 35.
+The protein's natural variant, known as in Bn-IV, features a modification of the amino acid from L to I at position 54.
+The natural variant of this protein is characterized by an amino acid alteration from K to R at position 212.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from R to H at position 82.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from V to E at position 140.
+The protein's natural variant, known as associated with lower plasma levels of triglyceride and higher levels of HDL cholesterol; strongly reduced inactivation of lipoprotein lipase LPL; no effect on protein secretion and stability of monomers; abolishes accumulation of oligomers;, features a modification of the amino acid from E to K at position 40.
+The natural variant of this protein is characterized by an amino acid alteration from G to R at position 233.
+The natural variant of this protein is characterized by an amino acid alteration from E to V at position 296.
+The protein's natural variant, known as no effect on protein folding;, features a modification of the amino acid from R to C at position 336.
+The protein's natural variant, known as impaired protein folding;, features a modification of the amino acid from W to C at position 349.
+The protein's natural variant, known as impaired protein folding;, features a modification of the amino acid from G to S at position 361.
+The protein's natural variant, known as impaired protein folding;, features a modification of the amino acid from R to W at position 384.
+The protein's natural variant, known as in strain: 253.27 and closs19, features a modification of the amino acid from A to T at position 641.
+The protein's natural variant, known as in strain: 253.27 and closs19, features a modification of the amino acid from T to S at position 697.
+The natural variant of this protein is characterized by an amino acid alteration from D to E at position 113.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from P to S at position 104.
+The protein's natural variant, known as in strain: UM23-1, features a modification of the amino acid from L to LL at position 75.
+The protein's natural variant, known as in strain: UM23-1, features a modification of the amino acid from F to Y at position 387.
+The protein's natural variant, known as in NKH;, features a modification of the amino acid from H to R at position 42.
+The protein's natural variant, known as in NKH;, features a modification of the amino acid from G to R at position 47.
+The protein's natural variant, known as in NKH;, features a modification of the amino acid from R to W at position 94.
+The protein's natural variant, known as in NKH; loss of aminomethyltransferase activity;, features a modification of the amino acid from N to I at position 145.
+The protein's natural variant, known as in NKH;, features a modification of the amino acid from E to K at position 211.
+The protein's natural variant, known as in NKH;, features a modification of the amino acid from R to C at position 222.
+The protein's natural variant, known as in NKH;, features a modification of the amino acid from R to C at position 265.
+The protein's natural variant, known as in NKH; decreased aminomethyltransferase activity;, features a modification of the amino acid from G to D at position 269.
+The protein's natural variant, known as in NKH;, features a modification of the amino acid from D to H at position 276.
+The protein's natural variant, known as in NKH;, features a modification of the amino acid from R to C at position 296.
+The protein's natural variant, known as in NKH; loss of aminomethyltransferase activity;, features a modification of the amino acid from R to H at position 320.
+The protein's natural variant, known as high frequency in individuals with diabetes mellitus type 2; increased repression activity; increased binding to SIN3A; impairs activation of insulin promoter;, features a modification of the amino acid from Q to R at position 62.
+The protein's natural variant, known as in MODY7; absent in one family member with diabetes; increased repression activity; no alteration in binding affinity to SIN3A;, features a modification of the amino acid from T to M at position 220.
+The protein's natural variant, known as in MODY7; increased repression activity; no alteration in binding affinity to SIN3A;, features a modification of the amino acid from A to S at position 347.
+The protein's natural variant, known as in ADMIO1; increases transcriptional activity; increases binding to ISL1 promoter region; decreases glucose stimulated insulin secretion, features a modification of the amino acid from P to S at position 330.
+The protein's natural variant, known as in HIES1;, features a modification of the amino acid from R to L at position 382.
+The protein's natural variant, known as in HIES1; loss of function;, features a modification of the amino acid from R to Q at position 382.
+The protein's natural variant, known as in HIES1; loss of function; reduced DNA-binding ability;, features a modification of the amino acid from R to W at position 382.
+The protein's natural variant, known as in HIES1, features a modification of the amino acid from F to L at position 384.
+The protein's natural variant, known as in HIES1, features a modification of the amino acid from F to S at position 384.
+The protein's natural variant, known as in HIES1; loss of function;, features a modification of the amino acid from T to I at position 389.
+The protein's natural variant, known as in ADMIO1;, features a modification of the amino acid from K to R at position 392.
+The protein's natural variant, known as in HIES1; unknown pathological significance; reduced DNA-binding ability, features a modification of the amino acid from N to Y at position 395.
+The protein's natural variant, known as in HIES1;, features a modification of the amino acid from R to Q at position 423.
+The protein's natural variant, known as in HIES1; unknown pathological significance; reduced DNA-binding ability, features a modification of the amino acid from N to Y at position 425.
+The protein's natural variant, known as in HIES1; loss of function, features a modification of the amino acid from H to Y at position 437.
+The protein's natural variant, known as in HIES1, features a modification of the amino acid from S to N at position 611.
+The protein's natural variant, known as in HIES1, features a modification of the amino acid from F to V at position 621.
+The protein's natural variant, known as in HIES1, features a modification of the amino acid from T to I at position 622.
+The protein's natural variant, known as in HIES1, features a modification of the amino acid from V to L at position 637.
+The protein's natural variant, known as in HIES1; reduced DNA-binding ability;, features a modification of the amino acid from V to M at position 637.
+The protein's natural variant, known as in ADMIO1;, features a modification of the amino acid from N to K at position 646.
+The protein's natural variant, known as in HIES1; reduced DNA-binding ability;, features a modification of the amino acid from Y to C at position 657.
+The protein's natural variant, known as in ADMIO1;, features a modification of the amino acid from K to N at position 658.
+The protein's natural variant, known as in ADMIO1;, features a modification of the amino acid from T to M at position 716.
+The protein's natural variant, known as in strain: WFB, features a modification of the amino acid from N to D at position 16.
+The protein's natural variant, known as in strain: WFB, features a modification of the amino acid from S to A at position 143.
+The protein's natural variant, known as in strain: WFB, features a modification of the amino acid from L to P at position 164.
+The protein's natural variant, known as in strain: WFB, features a modification of the amino acid from N to S at position 183.
+The protein's natural variant, known as in strain: WFB, features a modification of the amino acid from P to S at position 225.
+The protein's natural variant, known as in strain: WFB, features a modification of the amino acid from E to V at position 256.
+The protein's natural variant, known as in PPH2; affects SMAD-mediated signaling;, features a modification of the amino acid from K to E at position 43.
+The protein's natural variant, known as influences susceptibility to SLE;, features a modification of the amino acid from R to H at position 77.
+The protein's natural variant, known as in EDSS1;, features a modification of the amino acid from T to M at position 185.
+The protein's natural variant, known as found in patients with Charcot-Marie-Tooth disease; unknown pathological significance;, features a modification of the amino acid from Y to H at position 223.
+The protein's natural variant, known as frequency not significantly different between lithium-treated bipolar patients and healthy controls;, features a modification of the amino acid from T to A at position 228.
+The natural variant of this protein is characterized by an amino acid alteration from L to M at position 4.
+The protein's natural variant, known as in a breast pleomorphic lobular carcinoma sample; somatic mutation, features a modification of the amino acid from E to K at position 409.
+The protein's natural variant, known as in IBS, features a modification of the amino acid from T to P at position 500.
+The natural variant of this protein is characterized by an amino acid alteration from I to T at position 113.
+The protein's natural variant, known as in AH4; classic; highly decreases steroid 11-beta-hydroxylase activity;, features a modification of the amino acid from P to L at position 42.
+The protein's natural variant, known as in AH4; non-classic; highly decreases steroid 11-beta-hydroxylase activity;, features a modification of the amino acid from P to S at position 42.
+The protein's natural variant, known as in AH4; decreases steroid 11-beta-hydroxylase activity;, features a modification of the amino acid from R to Q at position 43.
+The protein's natural variant, known as in AH4; non-classic; highly decreases steroid 11-beta-hydroxylase activity;, features a modification of the amino acid from F to I at position 79.
+The protein's natural variant, known as in AH4; highly decreases steroid 11-beta-hydroxylase activity, features a modification of the amino acid from L to S at position 83.
+The protein's natural variant, known as in AH4; slightly decreases steroid 11-beta-hydroxylase activity;, features a modification of the amino acid from M to I at position 88.
+The protein's natural variant, known as in AH4; almost abolishes steroid 11-beta-hydroxylase activity;, features a modification of the amino acid from P to L at position 94.
+The protein's natural variant, known as in AH4; almost abolishes steroid 11-beta-hydroxylase activity;, features a modification of the amino acid from W to C at position 116.
+The protein's natural variant, known as in AH4; abolishes steroid 11-beta-hydroxylase activity;, features a modification of the amino acid from W to G at position 116.
+The protein's natural variant, known as in AH4; slightly decreases steroid 11-beta-hydroxylase activity;, features a modification of the amino acid from H to R at position 125.
+The protein's natural variant, known as in AH4; abolishes steroid 11-beta-hydroxylase activity;, features a modification of the amino acid from V to M at position 129.
+The protein's natural variant, known as in AH4; non-classic; highly decreases steroid 11-beta-hydroxylase activity;, features a modification of the amino acid from N to H at position 133.
+The protein's natural variant, known as in AH4; highly decreases steroid 11-beta-hydroxylase activity, features a modification of the amino acid from P to S at position 135.
+The protein's natural variant, known as in AH4; decreases steroid 11-beta-hydroxylase activity, features a modification of the amino acid from F to L at position 139.
+The protein's natural variant, known as in AH4; unknown pathological significance;, features a modification of the amino acid from R to Q at position 141.
+The protein's natural variant, known as in AH4; non-classic; highly decreases steroid 11-beta-hydroxylase activity;, features a modification of the amino acid from R to W at position 143.
+The protein's natural variant, known as in AH4; non-classic; highly decreases steroid 11-beta-hydroxylase activity;, features a modification of the amino acid from S to L at position 150.
+The protein's natural variant, known as in AH4; highly decreases steroid 11-beta-hydroxylase activity;, features a modification of the amino acid from L to P at position 158.
+The protein's natural variant, known as in AH4; decreases steroid 11-beta-hydroxylase activity;, features a modification of the amino acid from P to L at position 159.
+The protein's natural variant, known as in AH4; almost abolishes steroid 11-beta-hydroxylase activity;, features a modification of the amino acid from A to D at position 165.
+The protein's natural variant, known as in AH4; decreases steroid 11-beta-hydroxylase activity, features a modification of the amino acid from T to A at position 196.
+The protein's natural variant, known as in AH4, features a modification of the amino acid from G to D at position 267.
+The protein's natural variant, known as in AH4; non-classic; almost abolishes steroid 11-beta-hydroxylase activity;, features a modification of the amino acid from L to P at position 299.
+The protein's natural variant, known as in AH4; non-classic; almost abolishes steroid 11-beta-hydroxylase activity;, features a modification of the amino acid from A to V at position 306.
+The protein's natural variant, known as in AH4; abolishes steroid 11-beta-hydroxylase activity;, features a modification of the amino acid from E to K at position 310.
+The protein's natural variant, known as in AH4; abolishes steroid 11-beta-hydroxylase activity;, features a modification of the amino acid from G to R at position 314.
+The protein's natural variant, known as in AH4; abolishes steroid 11-beta-hydroxylase activity;, features a modification of the amino acid from T to M at position 318.
+The protein's natural variant, known as in AH4;, features a modification of the amino acid from T to P at position 318.
+The protein's natural variant, known as in AH4;, features a modification of the amino acid from T to R at position 318.
+The protein's natural variant, known as in AH4; non-classic; decreases steroid 11-beta-hydroxylase activity;, features a modification of the amino acid from T to M at position 319.
+The protein's natural variant, known as in AH4;, features a modification of the amino acid from F to V at position 321.
+The protein's natural variant, known as in AH4; abolishes steroid 11-beta-hydroxylase activity;, features a modification of the amino acid from A to V at position 331.
+The protein's natural variant, known as in AH4; high reduction of steroid 11-beta-monooxygenase activity, features a modification of the amino acid from R to G at position 332.
+The protein's natural variant, known as in AH4; non-classic; highly decreases steroid 11-beta-hydroxylase activity;, features a modification of the amino acid from R to Q at position 332.
+The protein's natural variant, known as in AH4;, features a modification of the amino acid from R to S at position 341.
+The protein's natural variant, known as in AH4; decreases steroid 11-beta-hydroxylase activity;, features a modification of the amino acid from R to C at position 366.
+The protein's natural variant, known as in AH4; abolishes steroid 11-beta-hydroxylase activity;, features a modification of the amino acid from A to D at position 368.
+The protein's natural variant, known as in AH4; abolishes steroid 11-beta-hydroxylase activity;, features a modification of the amino acid from E to G at position 371.
+The protein's natural variant, known as in AH4; abolishes steroid 11-beta-hydroxylase activity;, features a modification of the amino acid from R to Q at position 374.
+The protein's natural variant, known as in AH4;, features a modification of the amino acid from G to V at position 379.
+The protein's natural variant, known as in AH4, features a modification of the amino acid from R to G at position 384.
+The protein's natural variant, known as in AH4; abolishes steroid 11-beta-hydroxylase activity;, features a modification of the amino acid from R to Q at position 384.
+The protein's natural variant, known as in AH4; decreases steroid 11-beta-hydroxylase activity;, features a modification of the amino acid from T to A at position 401.
+The protein's natural variant, known as in AH4;, features a modification of the amino acid from R to H at position 427.
+The protein's natural variant, known as in AH4; abolishes steroid 11-beta-hydroxylase activity;, features a modification of the amino acid from V to G at position 441.
+The protein's natural variant, known as in AH4;, features a modification of the amino acid from G to D at position 444.
+The protein's natural variant, known as in AH4; abolishes steroid 11-beta-hydroxylase activity;, features a modification of the amino acid from R to C at position 448.
+The protein's natural variant, known as in AH4; abolishes steroid 11-beta-hydroxylase activity;, features a modification of the amino acid from R to H at position 448.
+The protein's natural variant, known as in AH4; abolishes steroid 11-beta-hydroxylase activity;, features a modification of the amino acid from R to Q at position 453.
+The protein's natural variant, known as in AH4;, features a modification of the amino acid from R to C at position 454.
+The protein's natural variant, known as in AH4; classic; abolishes steroid 11-beta-hydroxylase activity, features a modification of the amino acid from L to LL at position 463.
+The protein's natural variant, known as in AH4;, features a modification of the amino acid from L to S at position 489.
+The natural variant of this protein is characterized by an amino acid alteration from F to C at position 494.
+The protein's natural variant, known as in TAP2L, features a modification of the amino acid from V to F at position 352.
+The protein's natural variant, known as in TAP2L, features a modification of the amino acid from K to R at position 603.
+The protein's natural variant, known as in ALS26; unknown pathological significance;, features a modification of the amino acid from V to M at position 294.
+The protein's natural variant, known as in ALS26; unknown pathological significance;, features a modification of the amino acid from M to I at position 334.
+The protein's natural variant, known as in ALS26; unknown pathological significance;, features a modification of the amino acid from G to R at position 355.
+The protein's natural variant, known as in ALS26; unknown pathological significance;, features a modification of the amino acid from V to M at position 360.
+The protein's natural variant, known as in ALS26; accelerated formation of TIA1 amyloid-like fibrils; impaired stress granule disassembly; accumulation of insoluble TARDBP/TDP43-positive stress granules;, features a modification of the amino acid from P to L at position 362.
+The protein's natural variant, known as in ALS26; unknown pathological significance;, features a modification of the amino acid from A to T at position 381.
+The protein's natural variant, known as in WDM; results in a mild increase of stress granule numbers compared to controls; impaired stress granule disassembly;, features a modification of the amino acid from E to K at position 384.
+The protein's natural variant, known as in DEE87;, features a modification of the amino acid from G to A at position 28.
+The protein's natural variant, known as in DEE87; decreased protein kinase activity, features a modification of the amino acid from G to R at position 28.
+The protein's natural variant, known as in DEE87;, features a modification of the amino acid from Y to C at position 32.
+The protein's natural variant, known as in DEE87; fails to rescue neurologic phenotypes in a Drosophila model system; increased protein kinase activity;, features a modification of the amino acid from Y to H at position 32.
+The protein's natural variant, known as in DEE87; fails to rescue neurologic phenotypes in a Drosophila model system;, features a modification of the amino acid from T to A at position 196.
+The protein's natural variant, known as in DEE87;, features a modification of the amino acid from F to L at position 197.
+The protein's natural variant, known as in DEE87;, features a modification of the amino acid from W to C at position 198.
+The protein's natural variant, known as in DEE87;, features a modification of the amino acid from R to W at position 200.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 316.
+The natural variant of this protein is characterized by an amino acid alteration from S to L at position 586.
+The protein's natural variant, known as in BBS17;, features a modification of the amino acid from L to P at position 87.
+The protein's natural variant, known as in cot-3 mutation; abnormal hypha elongation, features a modification of the amino acid from I to N at position 278.
+The natural variant of this protein is characterized by an amino acid alteration from G to GGDFGG at position 24.
+The protein's natural variant, known as in OI18; unknown pathological significance;, features a modification of the amino acid from H to R at position 127.
+The protein's natural variant, known as in OI18; unknown pathological significance;, features a modification of the amino acid from D to G at position 231.
+The natural variant of this protein is characterized by an amino acid alteration from T to A at position 313.
+The protein's natural variant, known as in DEE110; does not promote calcium currents in transfected cells indicating loss of function in the positive regulation of voltage-gated calcium channel activity; severely decreased localization at the cell membrane; undergoes limited proteolytic cleavage, features a modification of the amino acid from G to D at position 209.
+The protein's natural variant, known as in ICPPS;, features a modification of the amino acid from G to V at position 248.
+The natural variant of this protein is characterized by an amino acid alteration from P to T at position 282.
+The protein's natural variant, known as in ICPPS;, features a modification of the amino acid from Q to R at position 531.
+The protein's natural variant, known as in L41P1A, features a modification of the amino acid from S to T at position 21.
+The natural variant of this protein is characterized by an amino acid alteration from R to G at position 313.
+The protein's natural variant, known as in FIGLU-URIA; mild phenotype; decreased glutamate formimidoyltransferase activity; 61% of wild-type activity;, features a modification of the amino acid from R to C at position 135.
+The protein's natural variant, known as in FIGLU-URIA; mild phenotype; decreased glutamate formimidoyltransferase activity; 57% wild-type activity;, features a modification of the amino acid from R to P at position 299.
+The natural variant of this protein is characterized by an amino acid alteration from A to E at position 438.
+The protein's natural variant, known as in strain: Chil, features a modification of the amino acid from T to M at position 32.
+The protein's natural variant, known as in HFM; loss-of-function mutation; targeted to the plasma membrane but has significantly impaired folate transport activity;, features a modification of the amino acid from R to C at position 113.
+The protein's natural variant, known as in HFM; abolishes folate uptake;, features a modification of the amino acid from R to S at position 113.
+The protein's natural variant, known as in HFM; reduces folate uptake to 13% of normal levels;, features a modification of the amino acid from G to R at position 147.
+The protein's natural variant, known as in HFM; loss of function measured as methotrexate uptake;, features a modification of the amino acid from D to Y at position 156.
+The protein's natural variant, known as in HFM; decreased folate uptake, features a modification of the amino acid from G to V at position 189.
+The protein's natural variant, known as in HFM; abolishes folate uptake;, features a modification of the amino acid from S to R at position 318.
+The protein's natural variant, known as in HFM; loss of function measured as methotrexate uptake;, features a modification of the amino acid from A to D at position 335.
+The protein's natural variant, known as in HFM; loss of function measured as methotrexate uptake;, features a modification of the amino acid from G to R at position 338.
+The protein's natural variant, known as in HFM; abolishes folate uptake;, features a modification of the amino acid from R to Q at position 376.
+The protein's natural variant, known as in HFM; abolishes folate uptake;, features a modification of the amino acid from R to W at position 376.
+The protein's natural variant, known as in HFM; locks the protein into an inward-open conformation, leading to decreased folate uptake; does not affect localization to the cell membrane, features a modification of the amino acid from F to V at position 392.
+The protein's natural variant, known as in HFM; decreased folate uptake, features a modification of the amino acid from N to K at position 411.
+The protein's natural variant, known as in HFM; strongly decreased folate and methotrexate uptake;, features a modification of the amino acid from P to R at position 425.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from E to Q at position 142.
+The protein's natural variant, known as in HAP3; exhibits impaired swimming only when in contact with a solid surface or a semisolid matrix, features a modification of the amino acid from R to C at position 168.
+The protein's natural variant, known as in RRP4-1; temperature-sensitive(ts) lethal mutation, features a modification of the amino acid from L to P at position 136.
+The protein's natural variant, known as in strain: B-3501, features a modification of the amino acid from G to S at position 114.
+The protein's natural variant, known as in strain: B-3501, features a modification of the amino acid from A to T at position 157.
+The protein's natural variant, known as in COXPD35; unknown pathological significance;, features a modification of the amino acid from I to S at position 283.
+The protein's natural variant, known as in COXPD35; unknown pathological significance;, features a modification of the amino acid from K to E at position 286.
+The protein's natural variant, known as in COXPD35; reduced tRNA dimethylallyltransferase activity;, features a modification of the amino acid from R to Q at position 323.
+The protein's natural variant, known as in COXPD35; unknown pathological significance;, features a modification of the amino acid from E to K at position 409.
+The protein's natural variant, known as in COXPD35; unknown pathological significance;, features a modification of the amino acid from H to P at position 419.
+The protein's natural variant, known as in BWS; unknown pathological significance;, features a modification of the amino acid from M to L at position 12.
+The protein's natural variant, known as in BWS;, features a modification of the amino acid from L to P at position 53.
+The protein's natural variant, known as in BWS;, features a modification of the amino acid from P to L at position 70.
+The protein's natural variant, known as in BWS; unknown pathological significance;, features a modification of the amino acid from P to A at position 158.
+The protein's natural variant, known as in BWS;, features a modification of the amino acid from A to APA at position 215.
+The protein's natural variant, known as in IMAGE;, features a modification of the amino acid from D to N at position 274.
+The protein's natural variant, known as in IMAGE; PCNA binding is disrupted;, features a modification of the amino acid from F to S at position 276.
+The protein's natural variant, known as in IMAGE;, features a modification of the amino acid from F to V at position 276.
+The protein's natural variant, known as in IMAGE; PCNA binding is disrupted;, features a modification of the amino acid from K to E at position 278.
+The protein's natural variant, known as in IMAGE;, features a modification of the amino acid from R to P at position 279.
+The protein's natural variant, known as in EPP2; results in decreased ATP hydrolysis; cells with the mutant protein show increased ALA levels and accumulation of the heme biosynthesis intermediate protoporphyrin IX, features a modification of the amino acid from G to D at position 298.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from I to T at position 206.
+The protein's natural variant, known as in VHO; loss of proteolytic cleavage of N-terminal propeptide; markedly reduced function in the activation of SMAD protein signal transduction;, features a modification of the amino acid from R to Q at position 298.
+The protein's natural variant, known as in strain: DBA/2J and SJL/J, features a modification of the amino acid from N to T at position 36.
+The protein's natural variant, known as in strain: DBA/2J and SJL/J, features a modification of the amino acid from V to I at position 64.
+The protein's natural variant, known as in strain: DBA/2J and SJL/J, features a modification of the amino acid from N to K at position 68.
+The protein's natural variant, known as in strain: DBA/2J and SJL/J, features a modification of the amino acid from G to D at position 70.
+The protein's natural variant, known as in allele ACP1*A;, features a modification of the amino acid from Q to R at position 106.
+The protein's natural variant, known as in CTHM; impairs transcriptional activation;, features a modification of the amino acid from F to L at position 151.
+The protein's natural variant, known as in CTHM, features a modification of the amino acid from K to Q at position 152.
+The protein's natural variant, known as in CTHM, features a modification of the amino acid from V to A at position 176.
+The protein's natural variant, known as in HNSCC, features a modification of the amino acid from D to G at position 20.
+The natural variant of this protein is characterized by an amino acid alteration from M to V at position 239.
+The natural variant of this protein is characterized by an amino acid alteration from K to R at position 457.
+The protein's natural variant, known as in MCTO;, features a modification of the amino acid from S to L at position 54.
+The protein's natural variant, known as in MCTO, features a modification of the amino acid from P to L at position 59.
+The protein's natural variant, known as in MCTO;, features a modification of the amino acid from T to P at position 62.
+The protein's natural variant, known as in MCTO, features a modification of the amino acid from P to R at position 63.
+The protein's natural variant, known as in MCTO, features a modification of the amino acid from S to C at position 66.
+The protein's natural variant, known as in MCTO;, features a modification of the amino acid from S to L at position 69.
+The protein's natural variant, known as in MCTO;, features a modification of the amino acid from S to A at position 70.
+The protein's natural variant, known as in MCTO;, features a modification of the amino acid from S to L at position 70.
+The protein's natural variant, known as in MCTO;, features a modification of the amino acid from P to L at position 71.
+The protein's natural variant, known as in MCTO;, features a modification of the amino acid from P to S at position 71.
+The protein's natural variant, known as in BC; early onset; loss of ATPase and helicase activities;, features a modification of the amino acid from P to A at position 47.
+The protein's natural variant, known as in FANCJ, features a modification of the amino acid from Q to H at position 255.
+The protein's natural variant, known as in BC; early onset; reduces helicase efficiency on longer substrates;, features a modification of the amino acid from M to I at position 299.
+The protein's natural variant, known as in FANCJ; destabilizes iron-sulfur-binding and abolishes helicase activity;, features a modification of the amino acid from A to P at position 349.
+The protein's natural variant, known as in FANCJ; associated with C-707;, features a modification of the amino acid from W to C at position 647.
+The protein's natural variant, known as in FANCJ; associated with C-647;, features a modification of the amino acid from R to C at position 707.
+The protein's natural variant, known as in a patient with ovarian cancer; unknown pathological significance;, features a modification of the amino acid from P to L at position 1034.
+The natural variant of this protein is characterized by an amino acid alteration from T to K at position 200.
+The protein's natural variant, known as in strain: HO-62, features a modification of the amino acid from Q to E at position 102.
+The protein's natural variant, known as in strain: HO-62, features a modification of the amino acid from E to A at position 106.
+The protein's natural variant, known as in FKR1-1; FK506-resistant, features a modification of the amino acid from K to KVQ at position 128.
+The protein's natural variant, known as in DEE33;, features a modification of the amino acid from G to S at position 70.
+The protein's natural variant, known as found in a patient with Rett syndrome-like phenotype; unknown pathological significance;, features a modification of the amino acid from A to T at position 92.
+The protein's natural variant, known as in MRD38;, features a modification of the amino acid from E to K at position 122.
+The protein's natural variant, known as in MRD38;, features a modification of the amino acid from D to H at position 252.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from G to S at position 239.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from P to A at position 484.
+The protein's natural variant, known as in strain: 10, features a modification of the amino acid from E to G at position 13.
+The protein's natural variant, known as in strain: 10, features a modification of the amino acid from L to I at position 15.
+The protein's natural variant, known as in AAS, features a modification of the amino acid from S to I at position 205.
+The protein's natural variant, known as in AAS, features a modification of the amino acid from E to A at position 380.
+The protein's natural variant, known as in AAS;, features a modification of the amino acid from R to H at position 443.
+The protein's natural variant, known as in AAS;, features a modification of the amino acid from R to H at position 522.
+The protein's natural variant, known as in AAS;, features a modification of the amino acid from R to Q at position 610.
+The protein's natural variant, known as in allele NAT2*14A, allele NAT2*14B, allele NAT2*14C, allele NAT2*14D, allele NAT2*14E, allele NAT2*14F and allele NAT2*14G; a slow acetylator;, features a modification of the amino acid from R to Q at position 64.
+The protein's natural variant, known as in allele NAT2*19;, features a modification of the amino acid from R to W at position 64.
+The protein's natural variant, known as in allele NAT2*5A, allele NAT2*5B, allele NAT2*5C, allele NAT2*5D, allele NAT2*5E, allele NAT2*5F, allele NAT2*14B and allele NAT2*14E; a slow acetylator;, features a modification of the amino acid from I to T at position 114.
+The protein's natural variant, known as in allele NAT2*17;, features a modification of the amino acid from Q to P at position 145.
+The protein's natural variant, known as in allele NAT2*5E, allele NAT2*6A, allele NAT2*6B, allele NAT2*6C, allele NAT2*6D and allele NAT2*14D; a slow acetylator;, features a modification of the amino acid from R to Q at position 197.
+The protein's natural variant, known as in allele NAT2*5A, allele NAT2*5D, allele NAT2*5E, allele NAT2*6A, allele NAT2*6B, allele NAT2*6D, allele NAT2*7A, allele NAT2*7B, NAT2*14A, allele NAT2*14B, allele NAT2*14D, allele NAT2*17, allele NAT2*18, allele NAT2*19;, features a modification of the amino acid from R to K at position 268.
+The protein's natural variant, known as in allele NAT2*18;, features a modification of the amino acid from K to T at position 282.
+The protein's natural variant, known as in allele NAT2*7A and allele NAT2*7B; a slow acetylator;, features a modification of the amino acid from G to E at position 286.
+The protein's natural variant, known as in SCC; impaired chromatid cohesion;, features a modification of the amino acid from S to F at position 24.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from L to P at position 215.
+The protein's natural variant, known as seems to be associated with hyperandrogenism, polycystic ovary syndrome (PCOS) and systemic lupus erythematosus;, features a modification of the amino acid from M to R at position 196.
+The protein's natural variant, known as in allele KAP1.6, features a modification of the amino acid from PSCSTSGTCGSSCCQPSCCETSSCQPRCCETSCCQPSCCQTSFCGFP to R at position 58.
+The protein's natural variant, known as in strain: cv Landsberg erecta, features a modification of the amino acid from E to K at position 310.
+The protein's natural variant, known as in HYPT1; dominant-negative mutant that perturbs the translational processing from the endoplasmic reticulum to the plasma membrane;, features a modification of the amino acid from L to R at position 9.
+The protein's natural variant, known as in HCC; patient BX-01, features a modification of the amino acid from W to R at position 31.
+The protein's natural variant, known as in HCC; patient T9, features a modification of the amino acid from F to L at position 78.
+The protein's natural variant, known as in HCC; patient BX-01, features a modification of the amino acid from C to Y at position 79.
+The protein's natural variant, known as in HCC; patient BX-10;, features a modification of the amino acid from N to K at position 91.
+The protein's natural variant, known as in HCC; patient NT1, features a modification of the amino acid from D to V at position 94.
+The protein's natural variant, known as in HCC; patient BX-05, features a modification of the amino acid from L to F at position 95.
+The protein's natural variant, known as in HCC; patient T9;, features a modification of the amino acid from I to V at position 108.
+The protein's natural variant, known as in HCC; patient NT4, features a modification of the amino acid from N to S at position 187.
+The protein's natural variant, known as in HCC; patient NT4, features a modification of the amino acid from K to I at position 195.
+The protein's natural variant, known as in MPS10; no effect on protein abundance; decreased glucuronate-2-sulfatase activity, features a modification of the amino acid from R to C at position 84.
+The protein's natural variant, known as in a lung squamous cell carcinoma sample; somatic mutation, features a modification of the amino acid from A to P at position 1488.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation, features a modification of the amino acid from A to G at position 2002.
+The protein's natural variant, known as in FCTCS;, features a modification of the amino acid from Q to R at position 2144.
+The protein's natural variant, known as in a lung large cell carcinoma sample; somatic mutation, features a modification of the amino acid from S to I at position 2233.
+The protein's natural variant, known as in a breast pleomorphic lobular carcinoma sample; somatic mutation, features a modification of the amino acid from E to K at position 2438.
+The protein's natural variant, known as in a breast infiltrating ductal carcinoma sample; somatic mutation, features a modification of the amino acid from E to Q at position 2537.
+The protein's natural variant, known as in AaV-SP-II, features a modification of the amino acid from D to N at position 70.
+The natural variant of this protein is characterized by an amino acid alteration from T to I at position 238.
+The natural variant of this protein is characterized by an amino acid alteration from T to V at position 238.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 304.
+The protein's natural variant, known as found in a patient with bilateral congenital cataracts; unknown pathological significance; lack of normal basal actin stress fiber formation; absence of SIPA1L3 and F-actin colocalization;, features a modification of the amino acid from D to Y at position 148.
+The protein's natural variant, known as in NEDSPM; loss of function mutation;, features a modification of the amino acid from S to R at position 153.
+The natural variant of this protein is characterized by an amino acid alteration from L to LC at position 180.
+The natural variant of this protein is characterized by an amino acid alteration from L to LL at position 20.
+The protein's natural variant, known as in strain: 4091-5-8, features a modification of the amino acid from A to R at position 77.
+The protein's natural variant, known as in KMIN; partially complement cell survival upon exposure to mitomycin C, features a modification of the amino acid from C to R at position 871.
+The protein's natural variant, known as in KMIN, features a modification of the amino acid from Q to P at position 929.
+The protein's natural variant, known as in KMIN;, features a modification of the amino acid from G to D at position 937.
+The protein's natural variant, known as in KMIN;, features a modification of the amino acid from D to N at position 960.
+The protein's natural variant, known as in DFNA4B;, features a modification of the amino acid from T to P at position 140.
+The protein's natural variant, known as in DFNA4B; impairs homooligomerization of the protein; decreases secretion of the protein;, features a modification of the amino acid from G to R at position 169.
+The protein's natural variant, known as associated with higher circulating levels of alanine transaminase with lower levels of low-density lipoprotein-cholesterol (LDL-C), triglycerides and alkaline phosphatase in 3 independent populations; reduces protein expression by 46%;, features a modification of the amino acid from E to K at position 167.
+The protein's natural variant, known as in cd; in a German Shorthaired Pointer, features a modification of the amino acid from D to N at position 262.
+The protein's natural variant, known as in strain: C57BL/6J, A/HeJ and SPRET/Ei, features a modification of the amino acid from E to EE at position 66.
+The protein's natural variant, known as in strain: SWR/J, AKR/J, RBF/DNJ and P/J, features a modification of the amino acid from E to EEE at position 66.
+The protein's natural variant, known as in strain: C57BL/6J, features a modification of the amino acid from H to Q at position 522.
+The protein's natural variant, known as in strain: vr1; rifampicin-resistant, features a modification of the amino acid from V to A at position 423.
+The protein's natural variant, known as in strain: vr2; rifampicin-resistant, features a modification of the amino acid from L to P at position 436.
+The protein's natural variant, known as in strain: vr3; rifampicin-resistant, features a modification of the amino acid from S to T at position 437.
+The protein's natural variant, known as in strain: RJ49; rifampicin-resistant, features a modification of the amino acid from QFMD to H at position 441.
+The protein's natural variant, known as in strain: vr4; rifampicin-resistant, features a modification of the amino acid from Q to L at position 438.
+The protein's natural variant, known as in strain: RJ37; rifampicin-resistant, features a modification of the amino acid from F to V at position 439.
+The protein's natural variant, known as in strain: vr3; rifampicin-resistant, features a modification of the amino acid from D to V at position 441.
+The protein's natural variant, known as in strain: RJ48; rifampicin-resistant, features a modification of the amino acid from LTHK to WPQ at position 452.
+The protein's natural variant, known as in strain: vr5; rifampicin-resistant, features a modification of the amino acid from H to D at position 451.
+The protein's natural variant, known as in strain: SP28; rifampicin-resistant, features a modification of the amino acid from H to L at position 451.
+The protein's natural variant, known as in strain: vr6; rifampicin-resistant, features a modification of the amino acid from H to N at position 451.
+The protein's natural variant, known as in strain: vr8; rifampicin-resistant, features a modification of the amino acid from H to P at position 451.
+The protein's natural variant, known as in strain: vr1; rifampicin-resistant, features a modification of the amino acid from H to Q at position 451.
+The protein's natural variant, known as in strain: vr7; rifampicin-resistant, features a modification of the amino acid from H to R at position 451.
+The protein's natural variant, known as in strain: vr11 and RJ37; rifampicin-resistant, features a modification of the amino acid from S to L at position 456.
+The protein's natural variant, known as in strain: vr9; rifampicin-resistant, features a modification of the amino acid from S to Q at position 456.
+The protein's natural variant, known as in strain: vr10; rifampicin-resistant, features a modification of the amino acid from S to W at position 456.
+The protein's natural variant, known as in strain: vr12 and SP22; rifampicin-resistant, features a modification of the amino acid from L to P at position 458.
+The protein's natural variant, known as in STHAG1;, features a modification of the amino acid from M to K at position 67.
+The protein's natural variant, known as in OFC5; cleft palate only;, features a modification of the amino acid from E to V at position 84.
+The protein's natural variant, known as in OFC5; cleft palate only, features a modification of the amino acid from G to D at position 97.
+The protein's natural variant, known as in OFC5; cleft palate only;, features a modification of the amino acid from V to G at position 120.
+The protein's natural variant, known as in OFC5; bilateral cleft palate;, features a modification of the amino acid from G to E at position 122.
+The protein's natural variant, known as in OFC5; unilateral cleft palate;, features a modification of the amino acid from R to S at position 157.
+The protein's natural variant, known as in STHAG1;, features a modification of the amino acid from R to P at position 202.
+The protein's natural variant, known as in strain: Clinical isolate 149 and O2:K1:H+ / MT78, features a modification of the amino acid from M to V at position 29.
+The protein's natural variant, known as in strain: Clinical isolate 149 and O2:K1:H+ / MT78, features a modification of the amino acid from E to V at position 54.
+The protein's natural variant, known as in strain: Clinical isolate 149 and O2:K1:H+ / MT78, features a modification of the amino acid from T to A at position 210.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from A to T at position 94.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from E to K at position 475.
+The protein's natural variant, known as found in a patient with global developmental delay; unknown pathological significance, features a modification of the amino acid from V to L at position 151.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to H at position 376.
+The protein's natural variant, known as in FAME2; gain of function; decreases interaction with PPP1R9B upon activation by neurotransmitter, features a modification of the amino acid from HGGAL to QFGR at position 229.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from E to Q at position 667.
+The natural variant of this protein is characterized by an amino acid alteration from H to R at position 122.
+The natural variant of this protein is characterized by an amino acid alteration from F to I at position 534.
+The protein's natural variant, known as in NBIA6; unknown pathological significance, features a modification of the amino acid from A to V at position 214.
+The protein's natural variant, known as in NBIA6; reduced protein abundance; loss of dephospho-CoA kinase activity;, features a modification of the amino acid from R to C at position 499.
+The protein's natural variant, known as in BLS2, features a modification of the amino acid from K to IE at position 120.
+The protein's natural variant, known as in BLS2; mild immunodeficiency; has residual MHC class II trans activation activity, features a modification of the amino acid from L to P at position 469.
+The protein's natural variant, known as in BLS2, features a modification of the amino acid from F to S at position 962.
+The protein's natural variant, known as common variant in the Beijing-W clade/SCG-2 phylogenetic group, features a modification of the amino acid from D to A at position 64.
+The protein's natural variant, known as reduces TLR2-mediated NF-kappa-B activation;, features a modification of the amino acid from T to I at position 411.
+The protein's natural variant, known as reduces TLR2-mediated NF-kappa-B activation;, features a modification of the amino acid from P to H at position 631.
+The protein's natural variant, known as reduces TLR2-mediated NF-kappa-B activation;, features a modification of the amino acid from R to Q at position 753.
+The protein's natural variant, known as in allotype C4B-long;, features a modification of the amino acid from S to Y at position 347.
+The protein's natural variant, known as in allotype C4B1-hi, features a modification of the amino acid from P to L at position 478.
+The protein's natural variant, known as in allotype C4B-long and allotype C4B2;, features a modification of the amino acid from T to A at position 907.
+The protein's natural variant, known as in allotype C4B2 and allotype C4B5-Rg1;, features a modification of the amino acid from G to D at position 1073.
+The protein's natural variant, known as in allotype C4B1a;, features a modification of the amino acid from S to N at position 1176.
+The protein's natural variant, known as in allotype C4B5-Rg1;, features a modification of the amino acid from A to V at position 1207.
+The protein's natural variant, known as in allotype C4B5-Rg1;, features a modification of the amino acid from R to L at position 1210.
+The protein's natural variant, known as in allotype C4B1-SC01;, features a modification of the amino acid from I to F at position 1317.
+The protein's natural variant, known as in strain: E/UW-5/Cx, features a modification of the amino acid from P to S at position 80.
+The protein's natural variant, known as in strain: E/UW-5/Cx, features a modification of the amino acid from S to G at position 185.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to Q at position 37.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from V to I at position 114.
+The protein's natural variant, known as in TPBS;, features a modification of the amino acid from P to R at position 539.
+The protein's natural variant, known as in UV-induced tumor 6132A antigen, features a modification of the amino acid from L to H at position 47.
+The protein's natural variant, known as in MCOPS2;, features a modification of the amino acid from P to L at position 85.
+The protein's natural variant, known as in one form, features a modification of the amino acid from P to T at position 652.
+The protein's natural variant, known as in PFIC7, features a modification of the amino acid from R to S at position 99.
+The protein's natural variant, known as in PFIC7, features a modification of the amino acid from H to R at position 132.
+The protein's natural variant, known as in PFIC7; unknown pathological significance, features a modification of the amino acid from P to L at position 242.
+The protein's natural variant, known as in PFIC7, features a modification of the amino acid from G to V at position 293.
+The protein's natural variant, known as probable disease-associated variant found in a family with symmetrical acral keratoderma, features a modification of the amino acid from P to T at position 29.
+The protein's natural variant, known as in PTHS; also expressed in the nucleus with a pattern indistinguishable from the wild-type; does not have a major impact on homodimer formation; affects transcriptional activity in a context-dependent manner, features a modification of the amino acid from G to V at position 358.
+The protein's natural variant, known as in PTHS; loss of function; also expressed in the nucleus with a pattern indistinguishable from the wild-type; does not have a major impact on homodimer formation; affects transcriptional activity in a context-dependent manner, features a modification of the amino acid from D to G at position 535.
+The protein's natural variant, known as in PTHS, features a modification of the amino acid from R to W at position 565.
+The protein's natural variant, known as in PTHS; loss of function, features a modification of the amino acid from R to G at position 572.
+The protein's natural variant, known as in PTHS;, features a modification of the amino acid from R to Q at position 572.
+The protein's natural variant, known as in PTHS;, features a modification of the amino acid from R to H at position 574.
+The protein's natural variant, known as in PTHS; mislocalized to small spherical punctae that are dispersed throughout the nucleus; can attenuate homo- and heterodimer formation; affects transcriptional activity in a context-dependent manner;, features a modification of the amino acid from R to P at position 574.
+The protein's natural variant, known as in PTHS; loss of function;, features a modification of the amino acid from R to Q at position 576.
+The protein's natural variant, known as in PTHS; mislocalized to small spherical punctae that are dispersed throughout the nucleus; can attenuate homo- and heterodimer formation; affects transcriptional activity in a context-dependent manner;, features a modification of the amino acid from R to W at position 576.
+The protein's natural variant, known as in PTHS, features a modification of the amino acid from R to H at position 578.
+The protein's natural variant, known as in PTHS, features a modification of the amino acid from R to P at position 578.
+The protein's natural variant, known as in PTHS, features a modification of the amino acid from A to P at position 583.
+The protein's natural variant, known as in PTHS; loss of function; mislocalized to small spherical punctae that are dispersed throughout the nucleus; can attenuate homo- and heterodimer formation; affects transcriptional activity in a context-dependent manner, features a modification of the amino acid from A to V at position 610.
+The protein's natural variant, known as in a lung large cell carcinoma sample; somatic mutation, features a modification of the amino acid from R to S at position 105.
+The protein's natural variant, known as in SEMD-SL; abolishes collagen binding;, features a modification of the amino acid from E to K at position 113.
+The protein's natural variant, known as in SEMD-SL, features a modification of the amino acid from R to W at position 124.
+The protein's natural variant, known as in WRCN; increased autophosphorylation in patient fibroblasts, features a modification of the amino acid from L to P at position 610.
+The protein's natural variant, known as in SEMD-SL; causes retention in an intracellular compartment and thereby abolishes signaling in response collagen binding;, features a modification of the amino acid from T to I at position 713.
+The protein's natural variant, known as in SEMD-SL; causes retention in an intracellular compartment and thereby abolishes signaling in response collagen binding;, features a modification of the amino acid from I to R at position 726.
+The protein's natural variant, known as in WRCN; increased autophosphorylation in patient fibroblasts, features a modification of the amino acid from Y to C at position 740.
+The protein's natural variant, known as in SEMD-SL; causes retention in an intracellular compartment and thereby abolishes signaling in response collagen binding;, features a modification of the amino acid from R to C at position 752.
+The protein's natural variant, known as in strain: 399A, 774A, 852A, 859A, Congo13, Congo194 and Congo346, features a modification of the amino acid from A to T at position 184.
+The protein's natural variant, known as in strain: 799A, features a modification of the amino acid from K to M at position 220.
+The protein's natural variant, known as in strain: 399A, features a modification of the amino acid from V to A at position 232.
+The protein's natural variant, known as in strain: 859A, features a modification of the amino acid from S to N at position 265.
+The protein's natural variant, known as in strain: 820A, features a modification of the amino acid from E to K at position 310.
+The protein's natural variant, known as in strain: 639A, features a modification of the amino acid from S to G at position 325.
+The protein's natural variant, known as in strain: 5, 7, 399A, 591A, 799A, 852A, 859A, Amherst, Congo13, Congo194, Congo216 and Congo346, features a modification of the amino acid from V to G at position 352.
+The protein's natural variant, known as in strain: 639A, features a modification of the amino acid from Y to H at position 405.
+The protein's natural variant, known as in strain: 732A, features a modification of the amino acid from R to C at position 412.
+The protein's natural variant, known as in strain: 639A, features a modification of the amino acid from P to S at position 430.
+The protein's natural variant, known as in strain: 820A, features a modification of the amino acid from L to P at position 465.
+The protein's natural variant, known as in strain: Congo194, features a modification of the amino acid from L to V at position 503.
+The protein's natural variant, known as in TKS;, features a modification of the amino acid from Y to C at position 64.
+The protein's natural variant, known as in strain: Tunisia, features a modification of the amino acid from FKM to KHK at position 12.
+The protein's natural variant, known as in strain: Tunisia, features a modification of the amino acid from PIF to ALL at position 19.
+The protein's natural variant, known as in strain: Tunisia, features a modification of the amino acid from GD to SA at position 23.
+The protein's natural variant, known as increased lysosomal pH; increased lipid droplets accumulation;, features a modification of the amino acid from I to L at position 231.
+The protein's natural variant, known as in strain: Landrace; loss of function, features a modification of the amino acid from RRLAKFPG to QVPRLNRTLQAARGLQGTSPGNEDQPPSLTD at position 663.
+The protein's natural variant, known as in strain: Montrache, features a modification of the amino acid from N to S at position 40.
+The protein's natural variant, known as in strain: Montrache, features a modification of the amino acid from K to M at position 61.
+The protein's natural variant, known as in strain: Montrache, features a modification of the amino acid from N to S at position 63.
+The protein's natural variant, known as in strain: Montrache, features a modification of the amino acid from I to V at position 308.
+The natural variant of this protein is characterized by an amino acid alteration from S to T at position 115.
+The protein's natural variant, known as in strain: cv. Miranda, features a modification of the amino acid from M to S at position 313.
+The protein's natural variant, known as in strain: cv. Miranda, features a modification of the amino acid from F to L at position 452.
+The protein's natural variant, known as in strain: cv. Miranda, features a modification of the amino acid from V to E at position 631.
+The natural variant of this protein is characterized by an amino acid alteration from P to T at position 35.
+The protein's natural variant, known as in NDI2;, features a modification of the amino acid from L to V at position 22.
+The protein's natural variant, known as in NDI2, features a modification of the amino acid from L to P at position 28.
+The protein's natural variant, known as in NDI2;, features a modification of the amino acid from A to V at position 47.
+The protein's natural variant, known as in NDI2;, features a modification of the amino acid from Q to P at position 57.
+The protein's natural variant, known as in NDI2; loss of water channel activity;, features a modification of the amino acid from G to R at position 64.
+The protein's natural variant, known as in NDI2;, features a modification of the amino acid from N to S at position 68.
+The protein's natural variant, known as in NDI2, features a modification of the amino acid from A to D at position 70.
+The protein's natural variant, known as in NDI2;, features a modification of the amino acid from V to M at position 71.
+The protein's natural variant, known as in NDI2;, features a modification of the amino acid from G to R at position 100.
+The protein's natural variant, known as in NDI2;, features a modification of the amino acid from G to V at position 100.
+The protein's natural variant, known as in NDI2;, features a modification of the amino acid from T to M at position 108.
+The protein's natural variant, known as in NDI2;, features a modification of the amino acid from T to M at position 125.
+The protein's natural variant, known as in NDI2;, features a modification of the amino acid from T to M at position 126.
+The protein's natural variant, known as in NDI2;, features a modification of the amino acid from A to T at position 147.
+The protein's natural variant, known as in NDI2;, features a modification of the amino acid from V to M at position 168.
+The protein's natural variant, known as in NDI2;, features a modification of the amino acid from G to R at position 175.
+The protein's natural variant, known as in NDI2;, features a modification of the amino acid from G to S at position 180.
+The protein's natural variant, known as in NDI2;, features a modification of the amino acid from C to W at position 181.
+The protein's natural variant, known as in NDI2;, features a modification of the amino acid from P to A at position 185.
+The protein's natural variant, known as in NDI2; loss of water channel activity; mutant protein does not fold properly;, features a modification of the amino acid from R to C at position 187.
+The protein's natural variant, known as in NDI2;, features a modification of the amino acid from R to H at position 187.
+The protein's natural variant, known as in NDI2; mutant protein does not fold properly and is not functional;, features a modification of the amino acid from A to T at position 190.
+The protein's natural variant, known as in NDI2, features a modification of the amino acid from W to C at position 202.
+The protein's natural variant, known as in NDI2; loss of water channel activity;, features a modification of the amino acid from S to P at position 216.
+The protein's natural variant, known as in NDI2; results in the loss of arginine vasopressin-mediated phosphorylation at S-256, features a modification of the amino acid from R to L at position 254.
+The protein's natural variant, known as in NDI2; exerts a dominant-negative effect on wild-type-AQP2 in that it interferes with its trafficking to the apical membrane; is a loss of function instead of a gain of function mutation on dominant nephrogenic diabetes insipidus, features a modification of the amino acid from R to Q at position 254.
+The protein's natural variant, known as in NDI2; retained in the Golgi compartment;, features a modification of the amino acid from E to K at position 258.
+The protein's natural variant, known as in NDI2; mutant protein folds properly and is functional but is retained in intracellular vesicles; able to assemble into tetramers with wild-type AQP2 that properly localize to the apical membrane;, features a modification of the amino acid from P to L at position 262.
+The natural variant of this protein is characterized by an amino acid alteration from H to Q at position 67.
+The protein's natural variant, known as found in a patient with intellectual disability; unknown pathological significance, features a modification of the amino acid from E to K at position 275.
+The protein's natural variant, known as in strain: LBV2, features a modification of the amino acid from A to G at position 57.
+The protein's natural variant, known as in strain: LBV2, SA3 and SA4, features a modification of the amino acid from S to A at position 70.
+The protein's natural variant, known as in strain: LO4, LBV2, SA3 and SA4, features a modification of the amino acid from S to T at position 148.
+The protein's natural variant, known as in strain: LO4, LBV2, SA3 and SA4, features a modification of the amino acid from P to L at position 189.
+The protein's natural variant, known as in strain: LBV2, SA3 and SA4, features a modification of the amino acid from E to D at position 198.
+The protein's natural variant, known as in strain: LO4, LBV2, SA3 and SA4, features a modification of the amino acid from A to E at position 360.
+The protein's natural variant, known as in strain: LBV2, SA3 and SA4, features a modification of the amino acid from I to V at position 365.
+The protein's natural variant, known as in strain: SA3, features a modification of the amino acid from T to A at position 401.
+The protein's natural variant, known as in strain: LO4, features a modification of the amino acid from T to M at position 401.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to W at position 562.
+The protein's natural variant, known as in strain: ATCC 15742 / P1059, features a modification of the amino acid from M to T at position 25.
+The protein's natural variant, known as in strain: 825, features a modification of the amino acid from A to S at position 27.
+The protein's natural variant, known as in strain: 849, features a modification of the amino acid from I to L at position 42.
+The protein's natural variant, known as in strain: 854, features a modification of the amino acid from L to F at position 91.
+The protein's natural variant, known as in strain: KU5, features a modification of the amino acid from V to A at position 103.
+The protein's natural variant, known as in strain: 6407, 825, 849, BA 70/12 and KU5, features a modification of the amino acid from L to P at position 104.
+The protein's natural variant, known as in strain: 6407 and 825, features a modification of the amino acid from T to M at position 110.
+The protein's natural variant, known as in strain: 849 and BA 70/12, features a modification of the amino acid from A to V at position 116.
+The protein's natural variant, known as in strain: 836, features a modification of the amino acid from S to N at position 154.
+The protein's natural variant, known as in strain: KU5, features a modification of the amino acid from K to G at position 171.
+The protein's natural variant, known as in strain: NRRLB-4449 and IO-1, features a modification of the amino acid from R to M at position 202.
+The protein's natural variant, known as in strain: 210, features a modification of the amino acid from D to Y at position 218.
+The protein's natural variant, known as in strain: NRRLB-4449 and IO-1, features a modification of the amino acid from A to S at position 247.
+The protein's natural variant, known as in strain: NRRLB-4449 and IO-1, features a modification of the amino acid from V to A at position 275.
+The protein's natural variant, known as in strain: NRRLB-4449 and IO-1, features a modification of the amino acid from T to S at position 388.
+The protein's natural variant, known as in strain: IO-1, features a modification of the amino acid from E to K at position 407.
+The protein's natural variant, known as in strain: NRRLB-4449, features a modification of the amino acid from H to Y at position 416.
+The protein's natural variant, known as in form 1, form 2 and Mr30-1, features a modification of the amino acid from V to A at position 19.
+The protein's natural variant, known as in form 1, form 2 and Mr30-1, features a modification of the amino acid from E to D at position 33.
+The protein's natural variant, known as in form 1, features a modification of the amino acid from V to M at position 49.
+The protein's natural variant, known as in Mr30-1, features a modification of the amino acid from K to E at position 186.
+The protein's natural variant, known as in AH5; 38% 17alpha-hydroxylase activity and 33% 17,20-lyase activity, features a modification of the amino acid from P to L at position 35.
+The protein's natural variant, known as in AH5;, features a modification of the amino acid from Y to S at position 64.
+The protein's natural variant, known as in AH5;, features a modification of the amino acid from F to C at position 93.
+The protein's natural variant, known as in AH5;, features a modification of the amino acid from R to Q at position 96.
+The protein's natural variant, known as in AH5; 25% of both 17alpha-hydroxylase and 17,20-lyase activities;, features a modification of the amino acid from R to W at position 96.
+The protein's natural variant, known as in AH5;, features a modification of the amino acid from S to P at position 106.
+The protein's natural variant, known as in AH5, features a modification of the amino acid from I to II at position 112.
+The protein's natural variant, known as in AH5;, features a modification of the amino acid from F to V at position 114.
+The protein's natural variant, known as in AH5;, features a modification of the amino acid from D to V at position 116.
+The protein's natural variant, known as in AH5; partial loss of activity, features a modification of the amino acid from W to R at position 121.
+The protein's natural variant, known as in AH5, features a modification of the amino acid from A to E at position 174.
+The protein's natural variant, known as in AH5; 10% 17alpha-hydroxylase and 17,20-lyase activities, features a modification of the amino acid from N to D at position 177.
+The protein's natural variant, known as in AH5;, features a modification of the amino acid from Y to D at position 329.
+The protein's natural variant, known as in AH5;, features a modification of the amino acid from P to T at position 342.
+The protein's natural variant, known as in AH5;, features a modification of the amino acid from R to C at position 347.
+The protein's natural variant, known as in AH5; selectively ablates 17,20-lyase activity, while preserving most 17alpha-hydroxylase activity;, features a modification of the amino acid from R to H at position 347.
+The protein's natural variant, known as in AH5; selectively ablates 17,20-lyase activity, while preserving most 17alpha-hydroxylase activity;, features a modification of the amino acid from R to Q at position 358.
+The protein's natural variant, known as in AH5;, features a modification of the amino acid from R to C at position 362.
+The protein's natural variant, known as in AH5;, features a modification of the amino acid from H to L at position 373.
+The protein's natural variant, known as in AH5;, features a modification of the amino acid from H to N at position 373.
+The protein's natural variant, known as in AH5; complete loss of both 17alpha-hydroxylase and 17,20-lyase activities, features a modification of the amino acid from W to L at position 406.
+The protein's natural variant, known as in AH5;, features a modification of the amino acid from W to R at position 406.
+The protein's natural variant, known as in AH5; ablates both 17,20-lyase activity and 17alpha-hydroxylase activity; loss of heme-binding and loss of phosphorylation;, features a modification of the amino acid from F to C at position 417.
+The protein's natural variant, known as in AH5;, features a modification of the amino acid from P to L at position 428.
+The protein's natural variant, known as in AH5;, features a modification of the amino acid from R to H at position 440.
+The protein's natural variant, known as in AH5;, features a modification of the amino acid from R to C at position 496.
+The protein's natural variant, known as in AH5; 30% 17alpha-hydroxylase activity and 29% 17,20-lyase activity;, features a modification of the amino acid from R to H at position 496.
+The natural variant of this protein is characterized by an amino acid alteration from V to D at position 23.
+The protein's natural variant, known as in DFNX6;, features a modification of the amino acid from G to S at position 591.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from G to E at position 1130.
+The protein's natural variant, known as in USH1G; reduced interaction with IFT52 and IFT57;, features a modification of the amino acid from L to P at position 48.
+The protein's natural variant, known as probable disease-associated variant found in patients with non-syndromic sensorineural hearing loss; reduced interaction with IFT52 and IFT57; failure to rescue the USH1C splicing defect seen in USH1G-depleted cells;, features a modification of the amino acid from M to V at position 104.
+The protein's natural variant, known as in USH1G; atypical form with mild retinitis pigmentosa and normal vestibular function; also found in patients with autosomal recessive non-syndromic deafness; strongly reduced affinity for USH1C;, features a modification of the amino acid from D to V at position 458.
+The protein's natural variant, known as increases resistance to BM212 with 4-fold increase in minimal inhibitory concentration (MIC) to BM212 in liquid and solid media, features a modification of the amino acid from V to M at position 197.
+The protein's natural variant, known as growth defect in both liquid and solid media; confers resistance to SQ109 and AU1235 with 2-fold and 4-fold increased resistance, respectively; disrupted membrane potential; increased cell wall hydrophobicity; more sensitive to ampicillin and the hydrophobic antibiotics, rifampicin and erythromycin, but no change in sensitivity to chloramphenicol or kanamycin, compared to wild-type, features a modification of the amino acid from Y to C at position 257.
+The protein's natural variant, known as growth defect in both liquid and solid media; confers resistance to SQ109 and AU1235 with 4-fold and 33-fold increased resistance, respectively; disrupted membrane potential; no significant difference in cell wall hydrophobicity; more sensitive to ampicillin and the hydrophobic antibiotics, rifampicin and erythromycin, but no change in sensitivity to chloramphenicol or kanamycin, compared to wild-type, features a modification of the amino acid from S to A at position 293.
+The protein's natural variant, known as grows as wild-type in liquid media; weak binding to both SQ109 and ICA38 while the dissociation constant (Kd) value for AU1235 increases 6.6-fold compared with wild-type; 8-fold and 4-fold increased resistance to AU1235 and SQ109, respectively; disrupted membrane potential; increased cell wall hydrophobicity; more sensitive to ampicillin and the hydrophobic antibiotics, rifampicin and erythromycin, but no change in sensitivity to chloramphenicol or kanamycin, compared to wild-type, features a modification of the amino acid from S to T at position 293.
+The protein's natural variant, known as growth defect in certain liquid medium; severely reduced binding to SQ109 and AU1235; no change in resistance and 4-fold increased resistance to SQ109 and AU1235, respectively; disrupted membrane potential; increased cell wall hydrophobicity; more sensitive to ampicillin and the hydrophobic antibiotics, rifampicin and erythromycin, but no change in sensitivity to chloramphenicol or kanamycin, compared to wild-type, features a modification of the amino acid from I to F at position 297.
+The protein's natural variant, known as increases resistance to BM212 with 4-fold increase in minimal inhibitory concentration (MIC) to BM212 in liquid and solid media, features a modification of the amino acid from A to T at position 326.
+The protein's natural variant, known as rescues the growth defect of A-293 variant by partially restoring the membrane potential, features a modification of the amino acid from G to D at position 750.
+The natural variant of this protein is characterized by an amino acid alteration from R to T at position 566.
+The protein's natural variant, known as in variant D, features a modification of the amino acid from A to T at position 68.
+The protein's natural variant, known as in variant C, features a modification of the amino acid from E to G at position 207.
+The natural variant of this protein is characterized by an amino acid alteration from R to M at position 279.
+The natural variant of this protein is characterized by an amino acid alteration from M to V at position 405.
+The natural variant of this protein is characterized by an amino acid alteration from D to E at position 155.
+The protein's natural variant, known as in strain: herbicide resistance, features a modification of the amino acid from S to G at position 264.
+The protein's natural variant, known as in strain: SR; confers resistance to insecticides, features a modification of the amino acid from G to S at position 247.
+The protein's natural variant, known as does not affect serine/threonine-protein kinase kinase activity;, features a modification of the amino acid from L to F at position 378.
+The protein's natural variant, known as in strain: Isolate Eweb652, features a modification of the amino acid from I to V at position 39.
+The protein's natural variant, known as in strain: Isolate Eweb652, features a modification of the amino acid from S to T at position 203.
+The protein's natural variant, known as in strain: Isolate Eweb652, features a modification of the amino acid from L to F at position 236.
+The protein's natural variant, known as in strain: Isolate Eweb652, features a modification of the amino acid from L to F at position 249.
+The protein's natural variant, known as in strain: Isolate Eweb652, features a modification of the amino acid from T to A at position 334.
+The protein's natural variant, known as induces thermal instability;, features a modification of the amino acid from I to M at position 58.
+The protein's natural variant, known as requires 2 nucleotide substitutions, features a modification of the amino acid from A to R at position 129.
+The protein's natural variant, known as in esophagus cancer samples;, features a modification of the amino acid from S to R at position 8.
+The protein's natural variant, known as in esophagus cancer sample; impairs homodimerization and reduces ubiquitin ligase activity, features a modification of the amino acid from S to L at position 12.
+The protein's natural variant, known as in esophagus cancer sample, features a modification of the amino acid from P to S at position 13.
+The protein's natural variant, known as in esophagus cancer samples, features a modification of the amino acid from L to Q at position 23.
+The protein's natural variant, known as in esophagus cancer samples; impairs interaction with SKP1, features a modification of the amino acid from P to T at position 76.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from S to F at position 8.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from A to T at position 13.
+The protein's natural variant, known as riboflavin transport is unaffected;, features a modification of the amino acid from Q to R at position 70.
+The protein's natural variant, known as riboflavin transport is unaffected;, features a modification of the amino acid from V to M at position 296.
+The protein's natural variant, known as found in a patient with early-onset Parkinson disease; unknown pathological significance;, features a modification of the amino acid from N to S at position 105.
+The protein's natural variant, known as found in patients with early-onset Parkinson disease; unknown pathological significance; impaired ATPase flippase activity;, features a modification of the amino acid from T to N at position 161.
+The protein's natural variant, known as found in a family with Parkinson disease; unknown pathological significance;, features a modification of the amino acid from V to M at position 219.
+The protein's natural variant, known as impaired ATPase flippase activity;, features a modification of the amino acid from G to W at position 393.
+The protein's natural variant, known as found in a family with Parkinson disease; unknown pathological significance;, features a modification of the amino acid from I to T at position 540.
+The protein's natural variant, known as found in a patient with early-onset Parkinson disease; unknown pathological significance;, features a modification of the amino acid from A to V at position 558.
+The protein's natural variant, known as found in patients with early-onset Parkinson disease; unknown pathological significance; impaired ATPase flippase activity;, features a modification of the amino acid from G to R at position 648.
+The protein's natural variant, known as found in patients with early-onset Parkinson disease; unknown pathological significance; impaired ATPase flippase activity;, features a modification of the amino acid from G to R at position 671.
+The protein's natural variant, known as found in a patient with early-onset Parkinson disease; unknown pathological significance; impaired ATPase flippase activity;, features a modification of the amino acid from V to L at position 748.
+The protein's natural variant, known as found in patients with early-onset Parkinson disease; unknown pathological significance; impaired ATPase flippase activity;, features a modification of the amino acid from N to K at position 865.
+The protein's natural variant, known as found in a patient with early-onset Parkinson disease; unknown pathological significance; impaired ATPase flippase activity;, features a modification of the amino acid from E to A at position 993.
+The protein's natural variant, known as found in a patient with early-onset Parkinson disease; unknown pathological significance; impaired ATPase flippase activity, features a modification of the amino acid from I to T at position 1038.
+The protein's natural variant, known as found in a patient with early-onset Parkinson disease; unknown pathological significance; has no effect on ATPase flippase activity;, features a modification of the amino acid from I to T at position 1222.
+The protein's natural variant, known as found in patients with Parkinson disease; unknown pathological significance;, features a modification of the amino acid from L to F at position 1421.
+The protein's natural variant, known as lowers activity by approximately 30%;, features a modification of the amino acid from R to W at position 54.
+The protein's natural variant, known as in IMD12;, features a modification of the amino acid from S to I at position 89.
+The protein's natural variant, known as in PFHB1B; attenuated desumoylation of TRPM4 resulting in constitutive sumoylation of the channel leading to impaired endocytosis and elevated channel density at the cell surface;, features a modification of the amino acid from E to K at position 7.
+The protein's natural variant, known as in PFHB1B; incomplete right bundle-branch block;, features a modification of the amino acid from Q to H at position 131.
+The protein's natural variant, known as in PFHB1B;, features a modification of the amino acid from R to W at position 164.
+The protein's natural variant, known as in PFHB1B; right bundle-branch block;, features a modification of the amino acid from Q to R at position 293.
+The protein's natural variant, known as in PFHB1B; atrioventricular block;, features a modification of the amino acid from A to T at position 432.
+The protein's natural variant, known as in PFHB1B; atrioventricular block;, features a modification of the amino acid from G to S at position 582.
+The protein's natural variant, known as in PFHB1B; atrioventricular block;, features a modification of the amino acid from Y to H at position 790.
+The protein's natural variant, known as in PFHB1B; right bundle-branch block;, features a modification of the amino acid from G to D at position 844.
+The protein's natural variant, known as in PFHB1B; atrioventricular block;, features a modification of the amino acid from K to R at position 914.
+The protein's natural variant, known as in PFHB1B; incomplete right bundle-branch block;, features a modification of the amino acid from P to S at position 970.
+The protein's natural variant, known as in EKVP6; increased calcium activated cation channel activity; increased keratinocytes proliferation and differentiation; no effect on localization at cell membrane;, features a modification of the amino acid from I to M at position 1033.
+The protein's natural variant, known as in EKVP6; increased calcium activated cation channel activity; increased keratinocytes proliferation and differentiation; no effect on localization at cell membrane;, features a modification of the amino acid from I to T at position 1040.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from G to R at position 120.
+The protein's natural variant, known as no effect on basal enzyme activity, but increased enzyme activity upon activation via G-proteins or forskolin;, features a modification of the amino acid from A to S at position 674.
+The protein's natural variant, known as in LCCS8;, features a modification of the amino acid from R to C at position 1116.
+The natural variant of this protein is characterized by an amino acid alteration from K to R at position 227.
+The natural variant of this protein is characterized by an amino acid alteration from D to N at position 296.
+The protein's natural variant, known as in strain: SAW 142, features a modification of the amino acid from I to T at position 94.
+The protein's natural variant, known as in strain: SAW 142, features a modification of the amino acid from V to I at position 142.
+The protein's natural variant, known as in arFMF;, features a modification of the amino acid from R to W at position 42.
+The protein's natural variant, known as in arFMF;, features a modification of the amino acid from S to R at position 108.
+The protein's natural variant, known as in arFMF;, features a modification of the amino acid from L to P at position 110.
+The protein's natural variant, known as in arFMF and adFMF; likely benign variant; associated with S-369 and Q-408 in cis; associated with I-694 in some patients;, features a modification of the amino acid from E to Q at position 148.
+The protein's natural variant, known as in arFMF;, features a modification of the amino acid from E to V at position 148.
+The protein's natural variant, known as in arFMF;, features a modification of the amino acid from E to A at position 163.
+The protein's natural variant, known as in arFMF;, features a modification of the amino acid from E to D at position 167.
+The protein's natural variant, known as in arFMF;, features a modification of the amino acid from T to I at position 177.
+The protein's natural variant, known as in arFMF; unknown pathological significance;, features a modification of the amino acid from G to W at position 196.
+The protein's natural variant, known as benign variant; no effect on PYCARD/ASC inflammasome formation;, features a modification of the amino acid from R to Q at position 202.
+The protein's natural variant, known as in arFMF;, features a modification of the amino acid from E to K at position 230.
+The protein's natural variant, known as in PAAND; results in constitutive inflammasome activation; increased PYCARD/ASC specks formation; increased caspase-1 activation and IL1B production; loss of S-242 phosphorylation; loss of interaction with 14-3-3 proteins;, features a modification of the amino acid from S to R at position 242.
+The protein's natural variant, known as in PAAND; results in constitutive inflammasome activation; increased PYCARD/ASC specks formation; increased caspase-1 activation and IL1B and IL18 production; decreased interaction with 14-3-3 proteins; no effect on interaction with PSTPIP1, features a modification of the amino acid from E to K at position 244.
+The protein's natural variant, known as in arFMF; unknown pathological significance;, features a modification of the amino acid from I to V at position 247.
+The protein's natural variant, known as in arFMF;, features a modification of the amino acid from T to I at position 267.
+The protein's natural variant, known as in arFMF; unknown pathological significance;, features a modification of the amino acid from P to L at position 283.
+The protein's natural variant, known as in arFMF; unknown pathological significance; no effect on PYCARD/ASC inflammasome formation;, features a modification of the amino acid from G to R at position 304.
+The protein's natural variant, known as in arFMF;, features a modification of the amino acid from E to K at position 319.
+The protein's natural variant, known as in arFMF; unknown pathological significance; associated with Q-148 and Q-408 in cis;, features a modification of the amino acid from P to S at position 369.
+The protein's natural variant, known as in arFMF; associated with Q-148 and S-369 in cis;, features a modification of the amino acid from R to Q at position 408.
+The protein's natural variant, known as in arFMF;, features a modification of the amino acid from E to K at position 474.
+The protein's natural variant, known as in adFMF; severe;, features a modification of the amino acid from H to Y at position 478.
+The protein's natural variant, known as in arFMF;, features a modification of the amino acid from F to L at position 479.
+The protein's natural variant, known as probable disease-associated variant found in an autosomal dominant autoinflammatory disease with some similarities to familial Mediterranean fever, features a modification of the amino acid from T to A at position 577.
+The protein's natural variant, known as probable disease-associated variant found in an autosomal dominant autoinflammatory disease with some similarities to familial Mediterranean fever;, features a modification of the amino acid from T to N at position 577.
+The protein's natural variant, known as probable disease-associated variant found in an autosomal dominant autoinflammatory disease with some similarities to familial Mediterranean fever;, features a modification of the amino acid from T to S at position 577.
+The protein's natural variant, known as in arFMF; unknown pathological significance;, features a modification of the amino acid from I to T at position 591.
+The protein's natural variant, known as in arFMF; unknown pathological significance;, features a modification of the amino acid from G to A at position 632.
+The protein's natural variant, known as in arFMF;, features a modification of the amino acid from G to S at position 632.
+The protein's natural variant, known as in arFMF;, features a modification of the amino acid from I to M at position 640.
+The protein's natural variant, known as in arFMF;, features a modification of the amino acid from I to F at position 641.
+The protein's natural variant, known as in arFMF;, features a modification of the amino acid from P to L at position 646.
+The protein's natural variant, known as in arFMF;, features a modification of the amino acid from L to P at position 649.
+The protein's natural variant, known as in arFMF;, features a modification of the amino acid from R to H at position 653.
+The protein's natural variant, known as in arFMF;, features a modification of the amino acid from E to A at position 656.
+The protein's natural variant, known as in arFMF;, features a modification of the amino acid from D to N at position 661.
+The protein's natural variant, known as in arFMF;, features a modification of the amino acid from S to N at position 675.
+The protein's natural variant, known as in arFMF;, features a modification of the amino acid from G to E at position 678.
+The protein's natural variant, known as in arFMF and adFMF; reduced CASP1 interaction; decreased interaction with ULK1 and diminished NLRP3 degradation after induction of autophagy by starvation; when associated with V-694 (PubMed:26347139); no effect on PYCARD/ASC inflammasome formation; no effect on interaction with 14-3-3 proteins;, features a modification of the amino acid from M to I at position 680.
+The protein's natural variant, known as in arFMF;, features a modification of the amino acid from M to L at position 680.
+The protein's natural variant, known as in arFMF;, features a modification of the amino acid from T to I at position 681.
+The protein's natural variant, known as in arFMF;, features a modification of the amino acid from Y to C at position 688.
+The protein's natural variant, known as in arFMF and adFMF; associated with Q-148 in some patients; no effect on PYCARD/ASC inflammasome formation; no effect on interaction with 14-3-3 proteins;, features a modification of the amino acid from M to I at position 694.
+The protein's natural variant, known as in arFMF;, features a modification of the amino acid from M to K at position 694.
+The protein's natural variant, known as in arFMF;, features a modification of the amino acid from M to L at position 694.
+The protein's natural variant, known as in arFMF and adFMF; very common mutation particularly in North African Jews; can be associated with amyloidosis development; reduced interaction with CASP1 and with ULK1 and diminished NLRP3 degradation after induction of autophagy by starvation (PubMed:16785446) (PubMed:26347139); effect on autophagic NLRP3 degradation is increased; when associated with I-680; no effect on interaction with CASP1, CASP5, NLRP1, NLRP2 or NLRP3 (PubMed:17431422);, features a modification of the amino acid from M to V at position 694.
+The protein's natural variant, known as in arFMF;, features a modification of the amino acid from K to M at position 695.
+The protein's natural variant, known as in arFMF; reduced penetrance among Ashkenazi Jews;, features a modification of the amino acid from K to R at position 695.
+The protein's natural variant, known as in one patient with familial Mediterranean fever;, features a modification of the amino acid from S to C at position 702.
+The protein's natural variant, known as in arFMF;, features a modification of the amino acid from V to I at position 704.
+The protein's natural variant, known as in arFMF;, features a modification of the amino acid from P to S at position 705.
+The protein's natural variant, known as in arFMF;, features a modification of the amino acid from I to M at position 720.
+The protein's natural variant, known as in arFMF; common mutation; in Iraqi and Ashkenazi Jews, Druze, Armenians; reduced interaction with CASP1 and ULK1 and diminished NLRP3 degradation after induction of autophagy by starvation; when associated with I-680 and V-694; no effect on CASP1 activation; no effect on interaction with 14-3-3 proteins;, features a modification of the amino acid from V to A at position 726.
+The protein's natural variant, known as in arFMF;, features a modification of the amino acid from F to L at position 743.
+The protein's natural variant, known as in arFMF; uncertain pathological significance;, features a modification of the amino acid from A to S at position 744.
+The protein's natural variant, known as in arFMF;, features a modification of the amino acid from P to S at position 758.
+The protein's natural variant, known as in arFMF;, features a modification of the amino acid from R to H at position 761.
+The protein's natural variant, known as in arFMF;, features a modification of the amino acid from P to T at position 780.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 769.
+The protein's natural variant, known as in COXPD55; results in mild reduction of transcription of mitochondrial DNA in an in vitro assay;, features a modification of the amino acid from H to D at position 250.
+The protein's natural variant, known as in COXPD55; when associated in cis with F-1193;, features a modification of the amino acid from P to S at position 566.
+The protein's natural variant, known as in COXPD55; results in decreased transcription of mitochondrial DNA in vitro; reduced DNA primase activity, features a modification of the amino acid from S to F at position 611.
+The protein's natural variant, known as in COXPD55; results in mild reduction of transcription of mitochondrial DNA in vitro; reduced DNA primase activity, features a modification of the amino acid from F to L at position 641.
+The protein's natural variant, known as in COXPD55; unknown pathological significance; results in decreased transcription of mitochondrial DNA in vitro, features a modification of the amino acid from P to S at position 810.
+The protein's natural variant, known as in COXPD55; unknown pathological significance; results in decreased transcription of mitochondrial DNA in vitro, features a modification of the amino acid from D to N at position 870.
+The protein's natural variant, known as in COXPD55; results in decreased transcription of mitochondrial DNA in vitro, features a modification of the amino acid from R to C at position 1013.
+The protein's natural variant, known as in COXPD55; when associated in cis with S-566;, features a modification of the amino acid from S to F at position 1193.
+The protein's natural variant, known as in strain: fluconazole-resistant isolates, features a modification of the amino acid from F to L at position 105.
+The protein's natural variant, known as in strain: azole-resistant isolates, features a modification of the amino acid from G to A at position 129.
+The protein's natural variant, known as in strain: azole-resistant isolates, features a modification of the amino acid from Y to H at position 132.
+The protein's natural variant, known as in strain: fluconazole-resistant isolates, features a modification of the amino acid from F to L at position 145.
+The protein's natural variant, known as in strain: fluconazole-resistant isolates, features a modification of the amino acid from A to V at position 149.
+The protein's natural variant, known as in strain: fluconazole-resistant isolates, features a modification of the amino acid from D to E at position 153.
+The protein's natural variant, known as in strain: fluconazole-resistant isolates, features a modification of the amino acid from E to Y at position 165.
+The protein's natural variant, known as in strain: fluconazole-resistant isolates, features a modification of the amino acid from E to D at position 266.
+The protein's natural variant, known as in strain: fluconazole-resistant isolates, features a modification of the amino acid from S to F at position 279.
+The protein's natural variant, known as in strain: fluconazole-resistant isolates, features a modification of the amino acid from K to R at position 287.
+The protein's natural variant, known as in strain: azole-resistant isolates, features a modification of the amino acid from S to F at position 405.
+The protein's natural variant, known as in strain: fluconazole-resistant isolates, features a modification of the amino acid from G to E at position 448.
+The protein's natural variant, known as in strain: fluconazole-resistant isolates, features a modification of the amino acid from G to E at position 450.
+The protein's natural variant, known as in strain: fluconazole-resistant isolates, features a modification of the amino acid from V to A at position 452.
+The protein's natural variant, known as in strain: fluconazole-resistant isolates, features a modification of the amino acid from G to S at position 464.
+The protein's natural variant, known as in strain: fluconazole-resistant isolates, features a modification of the amino acid from G to S at position 465.
+The protein's natural variant, known as in strain: Isolate 13; azole-resistant, features a modification of the amino acid from R to K at position 467.
+The protein's natural variant, known as in strain: fluconazole-resistant isolates, features a modification of the amino acid from V to I at position 488.
+The protein's natural variant, known as in cell line CHO-glyB; loss of folate transport into mitochondria; no effect on its mitochondrial localization, features a modification of the amino acid from G to E at position 192.
+The natural variant of this protein is characterized by an amino acid alteration from A to V at position 1450.
+The protein's natural variant, known as in EDM5;, features a modification of the amino acid from R to H at position 70.
+The protein's natural variant, known as in EDM5, features a modification of the amino acid from F to S at position 105.
+The protein's natural variant, known as in EDM5; retained and accumulates within the cell;, features a modification of the amino acid from T to M at position 120.
+The protein's natural variant, known as in EDM5; retained and accumulates within the cell;, features a modification of the amino acid from R to W at position 121.
+The protein's natural variant, known as in EDM5; bilateral hereditary microepiphyseal dysplasia;, features a modification of the amino acid from A to P at position 128.
+The protein's natural variant, known as in EDM5; retained and accumulates within the cell, features a modification of the amino acid from E to K at position 134.
+The protein's natural variant, known as in EDM5;, features a modification of the amino acid from A to D at position 173.
+The protein's natural variant, known as in EDM5; retained and accumulates within the cell, features a modification of the amino acid from I to N at position 192.
+The protein's natural variant, known as in EDM5; retained and accumulates within the cell;, features a modification of the amino acid from V to D at position 194.
+The protein's natural variant, known as in EDM5, features a modification of the amino acid from T to K at position 195.
+The protein's natural variant, known as in EDM5;, features a modification of the amino acid from R to P at position 209.
+The protein's natural variant, known as in EDM5, features a modification of the amino acid from Y to N at position 218.
+The protein's natural variant, known as in EDM5; retained and accumulates within the cell;, features a modification of the amino acid from A to D at position 219.
+The protein's natural variant, known as in EDM5;, features a modification of the amino acid from K to N at position 231.
+The protein's natural variant, known as in EDM5;, features a modification of the amino acid from V to M at position 245.
+The protein's natural variant, known as secreted normally as the wild-type;, features a modification of the amino acid from E to K at position 252.
+The protein's natural variant, known as in SEMDBCD;, features a modification of the amino acid from C to S at position 304.
+The natural variant of this protein is characterized by an amino acid alteration from M to V at position 494.
+The natural variant of this protein is characterized by an amino acid alteration from V to M at position 593.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from Q to E at position 280.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from L to F at position 576.
+The protein's natural variant, known as in NDPLHS; increased basal signaling activity and only weak stimulation by GABA agonist; when injected into Xenopus tadpoles, causes abnormal swimming patterns and increased frequencies of seizure-like behavior compared to wild-type-injected animals; no effect on cell surface expression;, features a modification of the amino acid from A to T at position 567.
+The natural variant of this protein is characterized by an amino acid alteration from Y to F at position 628.
+The protein's natural variant, known as in DEE59; unknown pathological significance;, features a modification of the amino acid from G to W at position 693.
+The protein's natural variant, known as in DEE59; full signaling activity in the absence of GABA agonist; when injected into Xenopus tadpoles, causes abnormal swimming patterns and increased frequencies of seizure-like behavior compared to wild-type-injected animals; no effect on cell surface expression;, features a modification of the amino acid from S to I at position 695.
+The protein's natural variant, known as in DEE59; increased basal signaling activity and no stimulation by GABA agonist; when injected into Xenopus tadpoles, causes abnormal swimming patterns and increased frequencies of seizure-like behavior compared to wild-type-injected animals; no effect on cell surface expression;, features a modification of the amino acid from I to N at position 705.
+The protein's natural variant, known as in NDPLHS; increased basal signaling activity and only weak stimulation by GABA agonist; no effect on cell surface expression;, features a modification of the amino acid from A to T at position 707.
+The natural variant of this protein is characterized by an amino acid alteration from C to Y at position 67.
+The natural variant of this protein is characterized by an amino acid alteration from I to M at position 77.
+The natural variant of this protein is characterized by an amino acid alteration from I to T at position 88.
+The natural variant of this protein is characterized by an amino acid alteration from G to N at position 150.
+The natural variant of this protein is characterized by an amino acid alteration from L to F at position 222.
+The natural variant of this protein is characterized by an amino acid alteration from T to A at position 225.
+The natural variant of this protein is characterized by an amino acid alteration from L to F at position 228.
+The natural variant of this protein is characterized by an amino acid alteration from S to T at position 341.
+The protein's natural variant, known as decreased transcription factor activity due to impaired localization to the nucleus;, features a modification of the amino acid from R to W at position 46.
+The protein's natural variant, known as decreased transcription factor activity;, features a modification of the amino acid from R to H at position 107.
+The protein's natural variant, known as does not affect the transcription factor activity;, features a modification of the amino acid from R to Q at position 402.
+The protein's natural variant, known as does not affect the transcription factor activity;, features a modification of the amino acid from W to R at position 410.
+The protein's natural variant, known as in HH18; results in decreased expression at the cell surface and reduced activity;, features a modification of the amino acid from K to T at position 131.
+The protein's natural variant, known as in HH18; results in decreased expression at the cell surface, features a modification of the amino acid from K to R at position 162.
+The protein's natural variant, known as in HH18; reduced activity, features a modification of the amino acid from P to S at position 306.
+The protein's natural variant, known as in HH18; rare variant associated with susceptibility to disease; some patients have a second mutation in the HH-associated gene FGFR1; reduced activity;, features a modification of the amino acid from Y to C at position 379.
+The protein's natural variant, known as in HH18; reduced activity;, features a modification of the amino acid from S to L at position 468.
+The protein's natural variant, known as in HH18; reduced activity;, features a modification of the amino acid from P to Q at position 577.
+The protein's natural variant, known as in HH18; rare variant associated with susceptibility to disease; the patient carries a second mutation in the HH-associated gene KISS1R; results in decreased expression at the cell surface;, features a modification of the amino acid from A to V at position 735.
+The protein's natural variant, known as in strain: A68, NCTC 11638 and NCTC 11639, features a modification of the amino acid from A to V at position 3.
+The protein's natural variant, known as in strain: NCTC 11638, features a modification of the amino acid from N to D at position 13.
+The protein's natural variant, known as in strain: NCTC 11639, features a modification of the amino acid from N to S at position 13.
+The protein's natural variant, known as in strain: A68, NCTC 11638 and NCTC 11639, features a modification of the amino acid from V to A at position 34.
+The protein's natural variant, known as in strain: NCTC 11639, features a modification of the amino acid from S to N at position 35.
+The protein's natural variant, known as in strain: A68, NCTC 11638 and NCTC 11639, features a modification of the amino acid from V to I at position 66.
+The protein's natural variant, known as associated with non-Hodgkin's lymphoma and breast cancer risk;, features a modification of the amino acid from T to A at position 394.
+The protein's natural variant, known as susceptibility to seasonal affective disorder (SAD) and diurnal preference;, features a modification of the amino acid from S to L at position 471.
+The natural variant of this protein is characterized by an amino acid alteration from M to T at position 14.
+The protein's natural variant, known as in EKD1;, features a modification of the amino acid from R to W at position 266.
+The protein's natural variant, known as in EKD1, features a modification of the amino acid from W to R at position 281.
+The protein's natural variant, known as in EKD1; may affect subcellular location, becoming predominantly cytoplasmic; impairs interaction with GRIA1 and SNAP25, features a modification of the amino acid from A to T at position 287.
+The protein's natural variant, known as in EKD1;, features a modification of the amino acid from G to R at position 305.
+The protein's natural variant, known as in EKD1; no effect on location at the plasma membrane;, features a modification of the amino acid from R to C at position 308.
+The protein's natural variant, known as in ICCA;, features a modification of the amino acid from S to N at position 317.
+The protein's natural variant, known as in BFIS2, features a modification of the amino acid from G to E at position 323.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from M to I at position 361.
+The protein's natural variant, known as in strain: CCUG 17874 / NCTC 11638, features a modification of the amino acid from VI to AV at position 74.
+The protein's natural variant, known as in strain: CCUG 17874 / NCTC 11638, features a modification of the amino acid from V to I at position 363.
+The natural variant of this protein is characterized by an amino acid alteration from G to R at position 4.
+The natural variant of this protein is characterized by an amino acid alteration from D to G at position 292.
+The natural variant of this protein is characterized by an amino acid alteration from S to P at position 345.
+The protein's natural variant, known as in ARVD13;, features a modification of the amino acid from V to D at position 94.
+The natural variant of this protein is characterized by an amino acid alteration from F to C at position 16.
+The protein's natural variant, known as in GA2C; unknown pathological significance, features a modification of the amino acid from Y to C at position 49.
+The protein's natural variant, known as in GA2C;, features a modification of the amino acid from S to F at position 82.
+The protein's natural variant, known as in GA2C, features a modification of the amino acid from S to P at position 82.
+The protein's natural variant, known as in GA2C;, features a modification of the amino acid from A to T at position 84.
+The protein's natural variant, known as in GA2C, features a modification of the amino acid from H to Y at position 112.
+The protein's natural variant, known as in GA2C;, features a modification of the amino acid from L to H at position 127.
+The protein's natural variant, known as in GA2C; unknown pathological significance;, features a modification of the amino acid from L to R at position 138.
+The protein's natural variant, known as in GA2C;, features a modification of the amino acid from R to H at position 175.
+The protein's natural variant, known as in GA2C;, features a modification of the amino acid from R to L at position 175.
+The protein's natural variant, known as in GA2C; unknown pathological significance;, features a modification of the amino acid from D to N at position 218.
+The protein's natural variant, known as in GA2C; unknown pathological significance;, features a modification of the amino acid from Q to P at position 222.
+The protein's natural variant, known as in GA2C; unknown pathological significance, features a modification of the amino acid from L to F at position 262.
+The protein's natural variant, known as in GA2C; unknown pathological significance;, features a modification of the amino acid from L to P at position 334.
+The protein's natural variant, known as in GA2C; unknown pathological significance;, features a modification of the amino acid from H to R at position 346.
+The protein's natural variant, known as in GA2C; unknown pathological significance;, features a modification of the amino acid from L to P at position 377.
+The protein's natural variant, known as in GA2C; unknown pathological significance, features a modification of the amino acid from R to K at position 452.
+The protein's natural variant, known as in GA2C;, features a modification of the amino acid from P to L at position 456.
+The protein's natural variant, known as in GA2C, features a modification of the amino acid from P to T at position 456.
+The protein's natural variant, known as in GA2C; unknown pathological significance;, features a modification of the amino acid from P to L at position 483.
+The protein's natural variant, known as in GA2C;, features a modification of the amino acid from P to L at position 562.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from V to L at position 565.
+The protein's natural variant, known as in GA2C, features a modification of the amino acid from K to E at position 590.
+The protein's natural variant, known as in GA2C;, features a modification of the amino acid from G to E at position 611.
+The protein's natural variant, known as in DYT1; increased identical protein binding; decreased ATP-dependent chaperone mediated protein folding; changed nuclear membrane organization; decreased neuron projection development;, features a modification of the amino acid from F to I at position 205.
+The natural variant of this protein is characterized by an amino acid alteration from D to H at position 264.
+The protein's natural variant, known as in DYT1; increased identical protein binding; decreased ATP-dependent chaperone mediated protein folding; changed nuclear membrane organization;, features a modification of the amino acid from R to Q at position 288.
+The protein's natural variant, known as in AMC5; increased localization to the nuclear membrane; induces the formation of spheroid bodies in cells;, features a modification of the amino acid from G to S at position 318.
+The protein's natural variant, known as in LOAM; acts as a modifier allele increasing the penetrance and expressivity of LHON-associated mtDNA mutations; reduced protein levels; does not affect localization to mitochondria; results in altered complex V stability and activity, features a modification of the amino acid from R to W at position 53.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from E to D at position 558.
+The protein's natural variant, known as cosegregates with obesity phenotype in a large family;, features a modification of the amino acid from L to F at position 61.
+The protein's natural variant, known as in strain: Isolate JP52, features a modification of the amino acid from T to I at position 12.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from G to E at position 754.
+The protein's natural variant, known as confers streptomycin independence on the streptomycin-dependent mutant L-90, features a modification of the amino acid from K to R at position 43.
+The protein's natural variant, known as in temperature-sensitive allele, features a modification of the amino acid from G to S at position 4.
+The protein's natural variant, known as in temperature-sensitive allele, features a modification of the amino acid from A to V at position 19.
+The protein's natural variant, known as in temperature-sensitive allele, features a modification of the amino acid from L to V at position 78.
+The protein's natural variant, known as in strain: Angus, Charolais, Holstein and Limousin, features a modification of the amino acid from D to N at position 214.
+The protein's natural variant, known as in MRD60; reduced clathrin-mediated endocytosis; no effect on clathrin-coated pit location; no effect on protein stability and membrane recruitment;, features a modification of the amino acid from R to W at position 170.
+The protein's natural variant, known as in XLID97; unknown pathological significance;, features a modification of the amino acid from G to E at position 139.
+The protein's natural variant, known as in XLID97;, features a modification of the amino acid from I to T at position 244.
+The protein's natural variant, known as in XLID97; unknown pathological significance;, features a modification of the amino acid from H to R at position 274.
+The protein's natural variant, known as in XLID97; unknown pathological significance;, features a modification of the amino acid from N to S at position 601.
+The protein's natural variant, known as in XLID97; unknown pathological significance, features a modification of the amino acid from E to D at position 622.
+The protein's natural variant, known as in strain: cv. 164 and cv. Snowman, features a modification of the amino acid from V to I at position 5.
+The protein's natural variant, known as in strain: cv. Snowman, features a modification of the amino acid from K to Q at position 28.
+The protein's natural variant, known as in strain: cv. 164 and cv. Snowman, features a modification of the amino acid from S to A at position 35.
+The protein's natural variant, known as in metJ193, features a modification of the amino acid from L to Q at position 57.
+The protein's natural variant, known as hinders dimerization, features a modification of the amino acid from A to T at position 61.
+The protein's natural variant, known as in an ovarian Endometrioid carcinoma sample; somatic mutation, features a modification of the amino acid from E to Q at position 404.
+The protein's natural variant, known as in a lung small cell carcinoma sample; somatic mutation, features a modification of the amino acid from W to C at position 460.
+The protein's natural variant, known as found in individuals with delayed sleep phase syndrome; has higher frequency in affected individuals than in healthy controls; unknown pathological significance;, features a modification of the amino acid from A to T at position 129.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from D to Y at position 87.
+The protein's natural variant, known as in BofC1, features a modification of the amino acid from S to F at position 96.
+The protein's natural variant, known as in FA11D, features a modification of the amino acid from F to S at position 30.
+The protein's natural variant, known as in FA11D;, features a modification of the amino acid from G to R at position 32.
+The protein's natural variant, known as in FA11D;, features a modification of the amino acid from D to H at position 34.
+The protein's natural variant, known as in FA11D; dominant-negative mutation that results in severely decreased protein secretion;, features a modification of the amino acid from A to T at position 43.
+The protein's natural variant, known as in FA11D;, features a modification of the amino acid from C to F at position 46.
+The protein's natural variant, known as in FA11D;, features a modification of the amino acid from T to I at position 51.
+The protein's natural variant, known as in FA11D;, features a modification of the amino acid from T to P at position 51.
+The protein's natural variant, known as in FA11D;, features a modification of the amino acid from H to Q at position 53.
+The protein's natural variant, known as in FA11D; secretion of the mutant protein is impaired;, features a modification of the amino acid from C to R at position 56.
+The protein's natural variant, known as in FA11D;, features a modification of the amino acid from A to V at position 63.
+The protein's natural variant, known as in FA11D;, features a modification of the amino acid from K to R at position 101.
+The protein's natural variant, known as in FA11D;, features a modification of the amino acid from A to T at position 109.
+The protein's natural variant, known as in FA11D;, features a modification of the amino acid from C to Y at position 140.
+The protein's natural variant, known as in FA11D;, features a modification of the amino acid from Y to C at position 151.
+The protein's natural variant, known as in FA11D, features a modification of the amino acid from D to N at position 216.
+The protein's natural variant, known as in FA11D;, features a modification of the amino acid from D to Y at position 222.
+The protein's natural variant, known as in FA11D;, features a modification of the amino acid from R to Q at position 228.
+The protein's natural variant, known as in FA11D; dominant-negative mutation that results in severely decreased protein secretion;, features a modification of the amino acid from F to L at position 241.
+The protein's natural variant, known as found in a patient with factor XI deficiency that also carries mutation N-266;, features a modification of the amino acid from Q to R at position 244.
+The protein's natural variant, known as in FA11D;, features a modification of the amino acid from W to C at position 246.
+The protein's natural variant, known as in FA11D;, features a modification of the amino acid from R to T at position 252.
+The protein's natural variant, known as in FA11D; secretion of the mutant protein is impaired;, features a modification of the amino acid from C to Y at position 255.
+The protein's natural variant, known as in FA11D;, features a modification of the amino acid from G to E at position 263.
+The protein's natural variant, known as in FA11D;, features a modification of the amino acid from S to N at position 266.
+The protein's natural variant, known as in FA11D; although the mutant protein is synthesized the secretion is reduced;, features a modification of the amino acid from K to I at position 270.
+The protein's natural variant, known as in FA11D;, features a modification of the amino acid from S to C at position 276.
+The protein's natural variant, known as in FA11D;, features a modification of the amino acid from G to D at position 277.
+The protein's natural variant, known as in FA11D;, features a modification of the amino acid from F to L at position 301.
+The protein's natural variant, known as in FA11D;, features a modification of the amino acid from E to K at position 315.
+The protein's natural variant, known as in FA11D;, features a modification of the amino acid from L to P at position 320.
+The protein's natural variant, known as in FA11D;, features a modification of the amino acid from T to I at position 322.
+The protein's natural variant, known as in FA11D;, features a modification of the amino acid from R to C at position 326.
+The protein's natural variant, known as in FA11D;, features a modification of the amino acid from T to I at position 331.
+The protein's natural variant, known as in FA11D;, features a modification of the amino acid from E to K at position 341.
+The protein's natural variant, known as in FA11D;, features a modification of the amino acid from L to P at position 360.
+The protein's natural variant, known as in FA11D;, features a modification of the amino acid from W to R at position 401.
+The protein's natural variant, known as in FA11D; dominant-negative mutation that results in severely decreased protein secretion;, features a modification of the amino acid from V to M at position 403.
+The protein's natural variant, known as in FA11D;, features a modification of the amino acid from T to N at position 404.
+The protein's natural variant, known as in FA11D; mutant is not secreted by transfected fibroblasts; dominant-negative effect;, features a modification of the amino acid from G to V at position 418.
+The protein's natural variant, known as in FA11D;, features a modification of the amino acid from A to V at position 430.
+The protein's natural variant, known as in FA11D;, features a modification of the amino acid from I to K at position 454.
+The protein's natural variant, known as in FA11D;, features a modification of the amino acid from F to V at position 460.
+The protein's natural variant, known as in FA11D;, features a modification of the amino acid from I to S at position 481.
+The protein's natural variant, known as in FA11D;, features a modification of the amino acid from T to I at position 493.
+The protein's natural variant, known as in FA11D;, features a modification of the amino acid from S to P at position 503.
+The protein's natural variant, known as in FA11D; mild phenotype;, features a modification of the amino acid from D to G at position 506.
+The protein's natural variant, known as in FA11D; transfected cells contain reduced amount of mutant protein and display decreased secretion;, features a modification of the amino acid from Y to H at position 511.
+The protein's natural variant, known as in FA11D;, features a modification of the amino acid from C to F at position 514.
+The protein's natural variant, known as in FA11D;, features a modification of the amino acid from D to E at position 526.
+The protein's natural variant, known as in FA11D;, features a modification of the amino acid from P to L at position 538.
+The protein's natural variant, known as in FA11D;, features a modification of the amino acid from E to K at position 543.
+The protein's natural variant, known as in FA11D;, features a modification of the amino acid from H to R at position 552.
+The protein's natural variant, known as in FA11D;, features a modification of the amino acid from E to K at position 565.
+The protein's natural variant, known as in FA11D;, features a modification of the amino acid from S to L at position 575.
+The protein's natural variant, known as in FA11D; mutant is not secreted by transfected fibroblasts; dominant-negative effect;, features a modification of the amino acid from W to S at position 587.
+The protein's natural variant, known as in FA11D;, features a modification of the amino acid from S to R at position 594.
+The protein's natural variant, known as in FA11D;, features a modification of the amino acid from E to K at position 597.
+The protein's natural variant, known as in FA11D;, features a modification of the amino acid from Y to H at position 608.
+The protein's natural variant, known as in FA11D;, features a modification of the amino acid from I to S at position 618.
+The protein's natural variant, known as in RP61; the mutant protein is retained in the endoplasmic reticulum;, features a modification of the amino acid from P to L at position 31.
+The protein's natural variant, known as in USH3A;, features a modification of the amino acid from C to G at position 40.
+The protein's natural variant, known as in USH3A;, features a modification of the amino acid from N to K at position 48.
+The protein's natural variant, known as in USH3A, features a modification of the amino acid from S to P at position 105.
+The protein's natural variant, known as in USH3A;, features a modification of the amino acid from M to K at position 120.
+The protein's natural variant, known as in USH3A;, features a modification of the amino acid from L to P at position 150.
+The protein's natural variant, known as in USH3A, features a modification of the amino acid from IL to M at position 154.
+The protein's natural variant, known as in RP61; the mutant protein is retained in the endoplasmic reticulum;, features a modification of the amino acid from L to W at position 154.
+The protein's natural variant, known as in USH3A, features a modification of the amino acid from I to N at position 168.
+The protein's natural variant, known as in a colorectal cancer cell line;, features a modification of the amino acid from M to T at position 15.
+The protein's natural variant, known as in PCS;, features a modification of the amino acid from R to Q at position 36.
+The protein's natural variant, known as in MVA1; heterozygous compound with nonsense mutation;, features a modification of the amino acid from R to Q at position 550.
+The protein's natural variant, known as in MVA1; heterozygous compound with nonsense mutation;, features a modification of the amino acid from R to H at position 814.
+The protein's natural variant, known as in MVA1; associated with H-921; heterozygous compound with nonsense mutation;, features a modification of the amino acid from L to F at position 844.
+The protein's natural variant, known as in MVA1; heterozygous compound with nonsense mutation;, features a modification of the amino acid from I to T at position 909.
+The protein's natural variant, known as in MVA1; associated with F-844; heterozygous compound with nonsense mutation;, features a modification of the amino acid from Q to H at position 921.
+The protein's natural variant, known as in MVA1; heterozygous compound with nonsense mutation;, features a modification of the amino acid from L to P at position 1012.
+The protein's natural variant, known as in NBIA5; unknown pathological significance, features a modification of the amino acid from A to D at position 208.
+The protein's natural variant, known as found in a patient with MRT52; unknown pathological significance;, features a modification of the amino acid from T to A at position 352.
+The protein's natural variant, known as in NEDHAHM; impaired vesicle fusion;, features a modification of the amino acid from S to P at position 75.
+The protein's natural variant, known as in NEDHAHM;, features a modification of the amino acid from F to S at position 77.
+The protein's natural variant, known as in NEDHAHM; no effect on vesicle fusion;, features a modification of the amino acid from E to A at position 78.
+The protein's natural variant, known as found in patients with tumors; dominant mutation; reduced nucleotidyltransferase activity, features a modification of the amino acid from G to E at position 303.
+The protein's natural variant, known as found in patients with uterine endometrioid carcinoma, reduced nucleotidyltransferase activity, features a modification of the amino acid from K to T at position 432.
+The protein's natural variant, known as in ARGINSA; 18-fold reduction in catalytic efficiency toward argininosuccinate;, features a modification of the amino acid from R to Q at position 12.
+The protein's natural variant, known as in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression;, features a modification of the amino acid from D to N at position 31.
+The protein's natural variant, known as in ARGINSA;, features a modification of the amino acid from V to A at position 70.
+The protein's natural variant, known as in ARGINSA; complete loss of argininosuccinate lyase activity; abolishes protein expression, features a modification of the amino acid from E to K at position 73.
+The protein's natural variant, known as in ARGINSA; loss of argininosuccinate lyase activity;, features a modification of the amino acid from D to G at position 87.
+The protein's natural variant, known as in ARGINSA; severe;, features a modification of the amino acid from R to C at position 94.
+The protein's natural variant, known as in ARGINSA;, features a modification of the amino acid from R to H at position 94.
+The protein's natural variant, known as in ARGINSA; loss of argininosuccinate lyase activity;, features a modification of the amino acid from R to C at position 95.
+The protein's natural variant, known as in ARGINSA;, features a modification of the amino acid from R to H at position 95.
+The protein's natural variant, known as in ARGINSA, features a modification of the amino acid from A to V at position 104.
+The protein's natural variant, known as in ARGINSA;, features a modification of the amino acid from R to W at position 111.
+The protein's natural variant, known as in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on nitric oxide production;, features a modification of the amino acid from R to Q at position 113.
+The protein's natural variant, known as in ARGINSA; severe, features a modification of the amino acid from D to E at position 120.
+The protein's natural variant, known as in ARGINSA, features a modification of the amino acid from L to H at position 121.
+The protein's natural variant, known as in ARGINSA;, features a modification of the amino acid from R to W at position 126.
+The protein's natural variant, known as in ARGINSA;, features a modification of the amino acid from R to W at position 146.
+The protein's natural variant, known as in ARGINSA;, features a modification of the amino acid from P to R at position 156.
+The protein's natural variant, known as in ARGINSA, features a modification of the amino acid from H to N at position 160.
+The protein's natural variant, known as in ARGINSA, features a modification of the amino acid from P to H at position 166.
+The protein's natural variant, known as in ARGINSA;, features a modification of the amino acid from R to H at position 168.
+The protein's natural variant, known as in ARGINSA;, features a modification of the amino acid from S to N at position 170.
+The protein's natural variant, known as in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression;, features a modification of the amino acid from V to M at position 178.
+The protein's natural variant, known as in ARGINSA;, features a modification of the amino acid from L to R at position 180.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from T to S at position 181.
+The protein's natural variant, known as in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression;, features a modification of the amino acid from R to Q at position 182.
+The protein's natural variant, known as in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression;, features a modification of the amino acid from R to Q at position 186.
+The protein's natural variant, known as in ARGINSA;, features a modification of the amino acid from R to W at position 191.
+The protein's natural variant, known as in ARGINSA;, features a modification of the amino acid from R to Q at position 193.
+The protein's natural variant, known as in ARGINSA;, features a modification of the amino acid from R to W at position 193.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from G to V at position 200.
+The protein's natural variant, known as in ARGINSA;, features a modification of the amino acid from A to V at position 205.
+The protein's natural variant, known as in ARGINSA;, features a modification of the amino acid from R to Q at position 213.
+The protein's natural variant, known as in ARGINSA, features a modification of the amino acid from L to P at position 227.
+The protein's natural variant, known as in ARGINSA, features a modification of the amino acid from S to R at position 229.
+The protein's natural variant, known as in ARGINSA;, features a modification of the amino acid from S to T at position 229.
+The protein's natural variant, known as in ARGINSA, features a modification of the amino acid from D to E at position 231.
+The protein's natural variant, known as in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on NOS complex formation;, features a modification of the amino acid from R to W at position 236.
+The protein's natural variant, known as in ARGINSA; severe;, features a modification of the amino acid from D to N at position 237.
+The protein's natural variant, known as in ARGINSA;, features a modification of the amino acid from M to T at position 256.
+The protein's natural variant, known as in ARGINSA;, features a modification of the amino acid from L to P at position 262.
+The protein's natural variant, known as in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression;, features a modification of the amino acid from Q to R at position 286.
+The protein's natural variant, known as in ARGINSA;, features a modification of the amino acid from L to P at position 295.
+The protein's natural variant, known as in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression;, features a modification of the amino acid from R to Q at position 297.
+The protein's natural variant, known as in ARGINSA;, features a modification of the amino acid from G to R at position 301.
+The protein's natural variant, known as in ARGINSA; severe;, features a modification of the amino acid from R to W at position 306.
+The protein's natural variant, known as in ARGINSA, features a modification of the amino acid from D to A at position 324.
+The protein's natural variant, known as in ARGINSA; severe, features a modification of the amino acid from Q to L at position 326.
+The protein's natural variant, known as in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression, features a modification of the amino acid from V to L at position 335.
+The protein's natural variant, known as in ARGINSA, features a modification of the amino acid from L to F at position 343.
+The protein's natural variant, known as in ARGINSA, features a modification of the amino acid from L to P at position 343.
+The protein's natural variant, known as in ARGINSA; loss of argininosuccinate lyase activity; may cause protein misfolding;, features a modification of the amino acid from M to T at position 360.
+The protein's natural variant, known as in ARGINSA;, features a modification of the amino acid from M to V at position 368.
+The protein's natural variant, known as in ARGINSA;, features a modification of the amino acid from R to C at position 379.
+The protein's natural variant, known as in ARGINSA, features a modification of the amino acid from K to E at position 380.
+The protein's natural variant, known as in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression, features a modification of the amino acid from M to R at position 382.
+The protein's natural variant, known as in ARGINSA;, features a modification of the amino acid from R to C at position 385.
+The protein's natural variant, known as in ARGINSA;, features a modification of the amino acid from R to H at position 385.
+The protein's natural variant, known as in ARGINSA; severe, features a modification of the amino acid from R to L at position 385.
+The protein's natural variant, known as in ARGINSA; severe, features a modification of the amino acid from H to Q at position 388.
+The protein's natural variant, known as in ARGINSA; impairs tetramer formation likely due to protein misfolding; loss of argininosuccinate lyase activity, features a modification of the amino acid from A to D at position 398.
+The protein's natural variant, known as in ARGINSA;, features a modification of the amino acid from S to R at position 433.
+The protein's natural variant, known as in ARGINSA;, features a modification of the amino acid from V to L at position 434.
+The protein's natural variant, known as in ARGINSA;, features a modification of the amino acid from S to N at position 447.
+The protein's natural variant, known as in ARGINSA;, features a modification of the amino acid from R to Q at position 456.
+The protein's natural variant, known as in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression;, features a modification of the amino acid from R to W at position 456.
+The protein's natural variant, known as in MNDLFH; unknown pathological significance, features a modification of the amino acid from S to I at position 56.
+The protein's natural variant, known as in MNDLFH, features a modification of the amino acid from C to W at position 384.
+The protein's natural variant, known as in MNDLFH, features a modification of the amino acid from T to K at position 405.
+The protein's natural variant, known as in MNDLFH; unknown pathological significance, features a modification of the amino acid from D to N at position 452.
+The protein's natural variant, known as in OI; loss of function;, features a modification of the amino acid from A to P at position 457.
+The natural variant of this protein is characterized by an amino acid alteration from A to V at position 49.
+The natural variant of this protein is characterized by an amino acid alteration from Y to F at position 71.
+The natural variant of this protein is characterized by an amino acid alteration from Y to S at position 71.
+The protein's natural variant, known as in strain: Mae/Stm, features a modification of the amino acid from I to V at position 263.
+The protein's natural variant, known as in strain: BALB/c, features a modification of the amino acid from L to V at position 468.
+The protein's natural variant, known as in strain: Mae/Stm, features a modification of the amino acid from R to Q at position 469.
+The protein's natural variant, known as in strain: BALB/c; requires 2 nucleotide substitutions, features a modification of the amino acid from E to R at position 477.
+The protein's natural variant, known as in strain: BALB/c, features a modification of the amino acid from GTPCLGRNLQTQAC to DQHGGDF at position 587.
+The natural variant of this protein is characterized by an amino acid alteration from N to D at position 68.
+The natural variant of this protein is characterized by an amino acid alteration from A to G at position 177.
+The natural variant of this protein is characterized by an amino acid alteration from I to T at position 210.
+The natural variant of this protein is characterized by an amino acid alteration from F to V at position 246.
+The protein's natural variant, known as in CHN1; loss of large and small myelinated nerve fibers;, features a modification of the amino acid from I to N at position 268.
+The protein's natural variant, known as in CMT1D;, features a modification of the amino acid from D to V at position 355.
+The protein's natural variant, known as in DSS and CMT1D; associated with A-136 in the GJB1 gene in a DSSKorean girl; loss of DNA binding and loss of transactivation activity; loss of small and large myelinated nerve fibers; residual fibers with thin myelin sheaths;, features a modification of the amino acid from R to W at position 359.
+The protein's natural variant, known as in CMT1D;, features a modification of the amino acid from R to C at position 381.
+The protein's natural variant, known as in CMT1D;, features a modification of the amino acid from R to H at position 381.
+The protein's natural variant, known as in CHN1, features a modification of the amino acid from SD to RY at position 383.
+The protein's natural variant, known as in CMT1D;, features a modification of the amino acid from D to Y at position 383.
+The protein's natural variant, known as in CMT1D; unknown pathological significance;, features a modification of the amino acid from T to N at position 387.
+The protein's natural variant, known as in CMT1D;, features a modification of the amino acid from R to W at position 409.
+The protein's natural variant, known as in DSS, features a modification of the amino acid from D to G at position 411.
+The protein's natural variant, known as in CMT1D; loss of myelinated and unmyelinated nerve fibers;, features a modification of the amino acid from E to G at position 412.
+The protein's natural variant, known as in DSS; loss of DNA binding and loss of transactivation activity;, features a modification of the amino acid from E to K at position 412.
+The protein's natural variant, known as no effect on 17beta-HSD activity;, features a modification of the amino acid from M to I at position 175.
+The protein's natural variant, known as in MANSA; results in less than 20% of wild-type enzyme activity;, features a modification of the amino acid from C to F at position 55.
+The protein's natural variant, known as in MANSA; type II;, features a modification of the amino acid from H to L at position 72.
+The protein's natural variant, known as in MANSA; results in less than 20% of wild-type enzyme activity;, features a modification of the amino acid from D to E at position 74.
+The protein's natural variant, known as in MANSA; results in less than 20% of wild-type enzyme activity;, features a modification of the amino acid from A to P at position 95.
+The protein's natural variant, known as in MANSA; results in less than 20% of wild-type enzyme activity;, features a modification of the amino acid from Y to H at position 99.
+The protein's natural variant, known as in MANSA; results in less than 20% of wild-type enzyme activity;, features a modification of the amino acid from D to N at position 159.
+The protein's natural variant, known as in MANSA; results in less than 20% of wild-type enzyme activity;, features a modification of the amino acid from P to R at position 197.
+The protein's natural variant, known as in MANSA; no residual enzyme activity;, features a modification of the amino acid from H to L at position 200.
+The protein's natural variant, known as in MANSA; reduced enzyme activity;, features a modification of the amino acid from H to N at position 200.
+The protein's natural variant, known as in MANSA; reduced enzyme activity;, features a modification of the amino acid from R to P at position 202.
+The protein's natural variant, known as in MANSA; reduced enzyme activity;, features a modification of the amino acid from R to W at position 229.
+The protein's natural variant, known as in MANSA; results in less than 20% of wild-type enzyme activity;, features a modification of the amino acid from P to L at position 263.
+The protein's natural variant, known as in MANSA; reduced enzyme activity;, features a modification of the amino acid from S to L at position 318.
+The protein's natural variant, known as in MANSA; results in less than 20% of wild-type enzyme activity;, features a modification of the amino acid from L to P at position 352.
+The protein's natural variant, known as in MANSA;, features a modification of the amino acid from T to P at position 355.
+The protein's natural variant, known as in MANSA; type I;, features a modification of the amino acid from P to R at position 356.
+The protein's natural variant, known as in MANSA; reduced enzyme activity;, features a modification of the amino acid from P to L at position 379.
+The protein's natural variant, known as in MANSA; results in less than 20% of wild-type enzyme activity;, features a modification of the amino acid from G to C at position 390.
+The protein's natural variant, known as in MANSA; unknown pathological significance;, features a modification of the amino acid from E to K at position 402.
+The protein's natural variant, known as in MANSA; results in less than 20% of wild-type enzyme activity;, features a modification of the amino acid from G to V at position 420.
+The protein's natural variant, known as in MANSA; results in less than 20% of wild-type enzyme activity;, features a modification of the amino acid from H to Y at position 445.
+The protein's natural variant, known as in MANSA; reduced enzyme activity;, features a modification of the amino acid from G to C at position 451.
+The protein's natural variant, known as in MANSA; reduced enzyme activity;, features a modification of the amino acid from S to F at position 453.
+The protein's natural variant, known as in MANSA;, features a modification of the amino acid from S to Y at position 453.
+The protein's natural variant, known as in MANSA; reduced enzyme activity;, features a modification of the amino acid from V to E at position 457.
+The protein's natural variant, known as in MANSA; reduced enzyme activity;, features a modification of the amino acid from C to S at position 501.
+The protein's natural variant, known as in MANSA; results in less than 20% of wild-type enzyme activity;, features a modification of the amino acid from L to P at position 565.
+The protein's natural variant, known as in MANSA;, features a modification of the amino acid from W to R at position 714.
+The protein's natural variant, known as in MANSA; results in less than 20% of wild-type enzyme activity;, features a modification of the amino acid from T to R at position 745.
+The protein's natural variant, known as in MANSA; type II;, features a modification of the amino acid from R to W at position 750.
+The protein's natural variant, known as in MANSA; results in less than 20% of wild-type enzyme activity;, features a modification of the amino acid from G to R at position 800.
+The protein's natural variant, known as in MANSA; results in less than 20% of wild-type enzyme activity;, features a modification of the amino acid from G to W at position 800.
+The protein's natural variant, known as in MANSA; no residual enzyme activity;, features a modification of the amino acid from G to D at position 801.
+The protein's natural variant, known as in MANSA;, features a modification of the amino acid from L to P at position 809.
+The protein's natural variant, known as in MANSA; results in less than 20% of wild-type enzyme activity, features a modification of the amino acid from R to RHR at position 815.
+The protein's natural variant, known as in MANSA; results in less than 20% of wild-type enzyme activity;, features a modification of the amino acid from G to R at position 891.
+The protein's natural variant, known as in MANSA; results in less than 20% of wild-type enzyme activity;, features a modification of the amino acid from L to P at position 892.
+The protein's natural variant, known as in MANSA; results in less than 20% of wild-type enzyme activity;, features a modification of the amino acid from R to C at position 916.
+The protein's natural variant, known as in MANSA; results in less than 20% of wild-type enzyme activity;, features a modification of the amino acid from R to H at position 916.
+The protein's natural variant, known as in MANSA; results in less than 20% of wild-type enzyme activity;, features a modification of the amino acid from R to P at position 950.
+The protein's natural variant, known as in MANSA; results in less than 20% of wild-type enzyme activity;, features a modification of the amino acid from L to R at position 956.
+The protein's natural variant, known as in MANSA; results in less than 20% of wild-type enzyme activity;, features a modification of the amino acid from F to S at position 1000.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to C at position 179.
+The natural variant of this protein is characterized by an amino acid alteration from E to K at position 68.
+The protein's natural variant, known as found in a patient with hereditary motor and sensory neuropathy; unknown pathological significance;, features a modification of the amino acid from N to H at position 227.
+The protein's natural variant, known as in SNCV;, features a modification of the amino acid from T to I at position 357.
+The protein's natural variant, known as in FPF;, features a modification of the amino acid from H to Q at position 51.
+The protein's natural variant, known as in FPF;, features a modification of the amino acid from C to R at position 59.
+The protein's natural variant, known as in FPF;, features a modification of the amino acid from C to S at position 59.
+The protein's natural variant, known as in FPF;, features a modification of the amino acid from C to G at position 62.
+The protein's natural variant, known as in FPF;, features a modification of the amino acid from C to Y at position 62.
+The protein's natural variant, known as in FPF; benign variant;, features a modification of the amino acid from P to L at position 75.
+The protein's natural variant, known as in FPF;, features a modification of the amino acid from T to M at position 79.
+The protein's natural variant, known as in FPF;, features a modification of the amino acid from C to F at position 81.
+The protein's natural variant, known as in FPF;, features a modification of the amino acid from C to S at position 99.
+The protein's natural variant, known as in FPF, features a modification of the amino acid from S to G at position 115.
+The protein's natural variant, known as in FPF;, features a modification of the amino acid from C to R at position 117.
+The protein's natural variant, known as in FPF;, features a modification of the amino acid from C to Y at position 117.
+The protein's natural variant, known as in FPF;, features a modification of the amino acid from R to P at position 121.
+The protein's natural variant, known as in FPF; unknown pathological significance;, features a modification of the amino acid from R to Q at position 121.
+The protein's natural variant, known as in DFNA81; perturbed subcellular location with loss of colocalization with F-actin in the cytoplasm and concentration in the nucleus; may also have a shorter half-life than the wild-type protein, features a modification of the amino acid from H to R at position 171.
+The protein's natural variant, known as in DFNB88; perturbed subcellular location with loss of targeting to stereocilia and concentration in the nucleus; loss of ARL2 GAP activity;, features a modification of the amino acid from L to S at position 265.
+The protein's natural variant, known as in strain: isolate ANT5.10, features a modification of the amino acid from L to I at position 54.
+The protein's natural variant, known as in strain: isolate ANT5.10, features a modification of the amino acid from L to H at position 231.
+The protein's natural variant, known as in DEE47; increased function in positive regulation of SCN8A voltage-dependent sodium channel activity;, features a modification of the amino acid from R to H at position 114.
+The natural variant of this protein is characterized by an amino acid alteration from G to S at position 9.
+The protein's natural variant, known as in 50% of the molecules, features a modification of the amino acid from G to S at position 28.
+The protein's natural variant, known as found in patients with autosomal dominant nocturnal frontal lobe epilepsy; unknown pathological significance; results in decreased protein levels; decreased protein secretion;, features a modification of the amino acid from P to R at position 30.
+The protein's natural variant, known as increased protection from polycythemia at high altitude; when associated with S-127;, features a modification of the amino acid from D to E at position 4.
+The protein's natural variant, known as increased protection from polycythemia at high altitude; when associated with E-4;, features a modification of the amino acid from C to S at position 127.
+The protein's natural variant, known as in ECYT3; marked decrease in enzyme activity;, features a modification of the amino acid from P to R at position 317.
+The protein's natural variant, known as in ECYT3; decreased interaction with HIF1A and EPAS1 and decreased enzyme activity;, features a modification of the amino acid from R to H at position 371.
+The protein's natural variant, known as results in decreased zinc efflux;, features a modification of the amino acid from S to R at position 61.
+The protein's natural variant, known as in HLD25; does not rescue developmental defects and myelin deficit in zebrafish morphants but results in a more severe phenotype; affects cell development and survival when expressed in oligodendroglial cells, features a modification of the amino acid from L to P at position 76.
+The protein's natural variant, known as in HLD25; severely decreased function in zinc transport; does not rescue developmental defects and myelin deficit in zebrafish morphants but results in a more severe phenotype, features a modification of the amino acid from L to R at position 76.
+The protein's natural variant, known as results in decreased zinc efflux;, features a modification of the amino acid from S to C at position 95.
+The protein's natural variant, known as in HLD25; results in decreased function in zinc transport; affects cell development and survival when expressed in oligodendroglial cells, features a modification of the amino acid from R to C at position 138.
+The protein's natural variant, known as in HLD25; unknown pathological significance; results in decreased function in zinc transport; affects cell development and survival when expressed in oligodendroglial cells, features a modification of the amino acid from H to R at position 146.
+The protein's natural variant, known as results in decreased zinc efflux;, features a modification of the amino acid from S to P at position 193.
+The protein's natural variant, known as results in decreased zinc efflux;, features a modification of the amino acid from E to K at position 286.
+The protein's natural variant, known as in PC1;, features a modification of the amino acid from M to T at position 121.
+The protein's natural variant, known as in PC1;, features a modification of the amino acid from Q to P at position 122.
+The protein's natural variant, known as in PC1;, features a modification of the amino acid from L to H at position 124.
+The protein's natural variant, known as in PC1;, features a modification of the amino acid from L to P at position 124.
+The protein's natural variant, known as in PC1;, features a modification of the amino acid from L to R at position 124.
+The protein's natural variant, known as in PC1;, features a modification of the amino acid from N to D at position 125.
+The protein's natural variant, known as in PC1; requires 2 nucleotide substitutions;, features a modification of the amino acid from N to G at position 125.
+The protein's natural variant, known as in FNEPPK1 and PC1;, features a modification of the amino acid from N to S at position 125.
+The protein's natural variant, known as in FNEPPK1 and PC1;, features a modification of the amino acid from R to C at position 127.
+The protein's natural variant, known as in PC1;, features a modification of the amino acid from R to P at position 127.
+The protein's natural variant, known as in PC1;, features a modification of the amino acid from L to Q at position 128.
+The protein's natural variant, known as in PC1;, features a modification of the amino acid from L to P at position 132.
+The protein's natural variant, known as in PC1; late onset;, features a modification of the amino acid from K to N at position 354.
+The protein's natural variant, known as in PC1, features a modification of the amino acid from L to P at position 421.
+The protein's natural variant, known as in AGM9; decreased zinc ion transporter activity; does not affect localization to endoplasmic reticulum, features a modification of the amino acid from P to A at position 190.
+The protein's natural variant, known as in AGM9, features a modification of the amino acid from L to P at position 217.
+The protein's natural variant, known as in AGM9; decreased zinc ion transporter activity; does not affect localization to endoplasmic reticulum, features a modification of the amino acid from E to K at position 363.
+The protein's natural variant, known as in AGM9; unknown pathological significance, features a modification of the amino acid from T to I at position 395.
+The protein's natural variant, known as in AGM9; unknown pathological significance, features a modification of the amino acid from G to A at position 458.
+The protein's natural variant, known as in To3, features a modification of the amino acid from G to V at position 15.
+The protein's natural variant, known as in RTSC4; reduced inhibition of dendrite development in transfected primary neurons; decreased interaction with MAP2; decreased interaction with TUBB3, features a modification of the amino acid from E to K at position 41.
+The protein's natural variant, known as in RTSC4; reduced inhibition of dendrite development in transfected primary neurons; decreased interaction with MAP2; decreased interaction with TUBB3, features a modification of the amino acid from G to R at position 47.
+The protein's natural variant, known as in allelic variant, features a modification of the amino acid from G to E at position 6.
+The protein's natural variant, known as in allelic variant, features a modification of the amino acid from S to A at position 139.
+The protein's natural variant, known as in MRT39; impaired TTT complex formation;, features a modification of the amino acid from I to N at position 436.
+The protein's natural variant, known as in strain: GMMK6, features a modification of the amino acid from M to T at position 32.
+The protein's natural variant, known as in strain: Muheza, features a modification of the amino acid from L to S at position 116.
+The protein's natural variant, known as in haplotype 25, features a modification of the amino acid from I to V at position 181.
+The protein's natural variant, known as in haplotype 38, features a modification of the amino acid from V to F at position 190.
+The protein's natural variant, known as in haplotype 39, features a modification of the amino acid from D to N at position 239.
+The protein's natural variant, known as in haplotype 24, features a modification of the amino acid from V to M at position 377.
+The protein's natural variant, known as in haplotype 24, haplotype 25 and haplotype 27, features a modification of the amino acid from N to K at position 378.
+The natural variant of this protein is characterized by an amino acid alteration from G to D at position 412.
+The protein's natural variant, known as in MULLAPL; unable to suppress steroidogenesis in an ovarian adenocarcinoma cell line resulting in increased androgen production;, features a modification of the amino acid from L to P at position 12.
+The protein's natural variant, known as in MULLAPL; with androgen excess, normal kidney size and location; unable to suppress expression of steroidogenic enzymes in ovarian; impairs protein secretion, features a modification of the amino acid from R to C at position 83.
+The protein's natural variant, known as in SERKAL; reduced transcript levels;, features a modification of the amino acid from A to V at position 114.
+The protein's natural variant, known as in MULLAPL; unable to suppress expression of steroidogenic enzymes in ovarian and adrenal cell lines;, features a modification of the amino acid from E to G at position 216.
+The protein's natural variant, known as in strain: cv. Jikkoku; semidwarfing, features a modification of the amino acid from G to V at position 94.
+The protein's natural variant, known as in strain: cv. Calrose76; semidwarfing, features a modification of the amino acid from L to F at position 266.
+The protein's natural variant, known as in strain: cv. Reimei; semidwarfing, features a modification of the amino acid from D to H at position 349.
+The protein's natural variant, known as in IDDSDF; loss of DNA-binding transcription factor activity;, features a modification of the amino acid from I to S at position 59.
+The protein's natural variant, known as in IDDSDF; loss of DNA-binding transcription factor activity;, features a modification of the amino acid from F to L at position 66.
+The protein's natural variant, known as in IDDSDF; loss of DNA-binding transcription factor activity;, features a modification of the amino acid from K to N at position 105.
+The protein's natural variant, known as in IDDSDF; loss DNA-binding transcription factor activity;, features a modification of the amino acid from A to P at position 112.
+The protein's natural variant, known as in TPID;, features a modification of the amino acid from C to Y at position 42.
+The protein's natural variant, known as in TPID, features a modification of the amino acid from G to A at position 73.
+The protein's natural variant, known as in TPID; no effect on triose-phosphate isomerase activity; changed protein homodimerization activity; the homodimer stability is temperature-dependent and affects the triose-phosphate isomerase activity;, features a modification of the amino acid from E to D at position 105.
+The protein's natural variant, known as in Manchester; thermolabile;, features a modification of the amino acid from G to R at position 123.
+The protein's natural variant, known as in TPID;, features a modification of the amino acid from V to M at position 155.
+The protein's natural variant, known as in TPID;, features a modification of the amino acid from I to V at position 171.
+The protein's natural variant, known as in TPID;, features a modification of the amino acid from V to M at position 232.
+The protein's natural variant, known as in TPID; Hungary; thermolabile;, features a modification of the amino acid from F to L at position 241.
+The protein's natural variant, known as in a gastric adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from Y to H at position 419.
+The protein's natural variant, known as in a lung large cell carcinoma sample; somatic mutation, features a modification of the amino acid from Q to H at position 865.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation, features a modification of the amino acid from K to R at position 2003.
+The protein's natural variant, known as in a gastric adenocarcinoma sample; somatic mutation, features a modification of the amino acid from F to S at position 2138.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from S to L at position 247.
+The protein's natural variant, known as in allele ESD*2;, features a modification of the amino acid from G to E at position 190.
+The protein's natural variant, known as in MSCCA; results in reduced glutaminyl-tRNA aminoacylation activity; does not affect interaction with RARS1;, features a modification of the amino acid from G to V at position 45.
+The protein's natural variant, known as in MSCCA; results in reduced glutaminyl-tRNA aminoacylation activity; does not affect interaction with RARS1;, features a modification of the amino acid from Y to H at position 57.
+The protein's natural variant, known as in MSCCA; results in loss of glutaminyl-tRNA aminoacylation activity; impairs protein folding; does not interact with RARS1; results in reduced protein solubility;, features a modification of the amino acid from R to W at position 403.
+The protein's natural variant, known as in MSCCA; results in loss of glutaminyl-tRNA aminoacylation activity; impairs protein folding; results in reduced protein solubility;, features a modification of the amino acid from R to W at position 515.
+The protein's natural variant, known as in GSD10;, features a modification of the amino acid from E to A at position 89.
+The protein's natural variant, known as in GSD10;, features a modification of the amino acid from R to W at position 90.
+The protein's natural variant, known as in GSD10;, features a modification of the amino acid from G to D at position 97.
+The protein's natural variant, known as in strain: ZW141, features a modification of the amino acid from A to V at position 15.
+The protein's natural variant, known as in strain: Loua, features a modification of the amino acid from T to A at position 51.
+The protein's natural variant, known as in strain: ZW141, features a modification of the amino acid from L to S at position 62.
+The protein's natural variant, known as in strain: Draveil, Loua, Monty5, P.bourg, Tahiti, Texas and ZW141, features a modification of the amino acid from V to L at position 152.
+The protein's natural variant, known as in fusion protein; decreases DNA-binding activity, features a modification of the amino acid from I to F at position 253.
+The protein's natural variant, known as in strain: 16, 17, 25, 7, Black Minorca, Fayoumi GSP, WL-F and WL-N, features a modification of the amino acid from W to R at position 5.
+The protein's natural variant, known as in strain: Black-bone, features a modification of the amino acid from F to S at position 8.
+The protein's natural variant, known as in strain: 25, Black Minorca, Fayoumi GSP and WL-F, features a modification of the amino acid from Q to R at position 21.
+The protein's natural variant, known as in strain: 16, 17, 25, Black Minorca, Fayoumi GSP and WL-F, features a modification of the amino acid from R to P at position 41.
+The protein's natural variant, known as in strain: 16, 17, 25, Black Minorca, Fayoumi GSP and WL-F, features a modification of the amino acid from S to L at position 42.
+The protein's natural variant, known as in strain: WL-N, features a modification of the amino acid from D to N at position 72.
+The protein's natural variant, known as in strain: WL-N, features a modification of the amino acid from S to N at position 84.
+The protein's natural variant, known as in strain: 16, 17, 25, 7, Black-bone, Black Minorca, Fayoumi GSP, WL-F and WL-N, features a modification of the amino acid from Q to R at position 94.
+The protein's natural variant, known as in strain: WL-F, features a modification of the amino acid from K to E at position 143.
+The protein's natural variant, known as in strain: WL-F, features a modification of the amino acid from E to K at position 152.
+The protein's natural variant, known as in strain: WL-N, features a modification of the amino acid from M to V at position 158.
+The protein's natural variant, known as in strain: 16, 17, features a modification of the amino acid from S to T at position 202.
+The protein's natural variant, known as in strain: 25, 7, Black-bone, Black Minorca, Fayoumi GSP, WL-F and WL-N, features a modification of the amino acid from I to V at position 308.
+The protein's natural variant, known as in strain: WL-F, features a modification of the amino acid from K to E at position 317.
+The protein's natural variant, known as in strain: 25, 7, Black-bone, Black Minorca, Fayoumi GSP, WL-F and WL-N, features a modification of the amino acid from A to T at position 339.
+The protein's natural variant, known as in strain: WL-N, features a modification of the amino acid from H to R at position 352.
+The protein's natural variant, known as in strain: Black-bone, features a modification of the amino acid from G to E at position 377.
+The protein's natural variant, known as in strain: Black Minorca and Fayoumi GSP, features a modification of the amino acid from Q to R at position 505.
+The protein's natural variant, known as in strain: Black-bone, features a modification of the amino acid from Q to R at position 530.
+The protein's natural variant, known as in strain: 25, WL-F and WL-N, features a modification of the amino acid from A to V at position 548.
+The protein's natural variant, known as in strain: 16, 17, 25, 7, Black-bone, Black Minorca, Fayoumi GSP, WL-F and WL-N, features a modification of the amino acid from A to T at position 583.
+The protein's natural variant, known as in strain: 25, Black-bone, WL-F and WL-N, features a modification of the amino acid from S to N at position 631.
+The protein's natural variant, known as in temperature sensitive mutant, features a modification of the amino acid from G to R at position 493.
+The protein's natural variant, known as in ENFL3;, features a modification of the amino acid from V to L at position 287.
+The protein's natural variant, known as in ENFL3; approximately 10-fold increase in acetylcholine sensitivity;, features a modification of the amino acid from V to M at position 287.
+The protein's natural variant, known as slightly decreased phosphodiesterase activity;, features a modification of the amino acid from I to V at position 307.
+The protein's natural variant, known as in CMS5; abrogates binding to T subunit, features a modification of the amino acid from P to Q at position 59.
+The protein's natural variant, known as in CMS5;, features a modification of the amino acid from I to T at position 337.
+The protein's natural variant, known as in CMS5; impairs anchoring to the basal lamina;, features a modification of the amino acid from D to E at position 342.
+The protein's natural variant, known as in CMS5;, features a modification of the amino acid from R to Q at position 410.
+The protein's natural variant, known as in CMS5;, features a modification of the amino acid from Y to S at position 430.
+The protein's natural variant, known as in CMS5, features a modification of the amino acid from C to Y at position 444.
+The protein's natural variant, known as in CMD2B;, features a modification of the amino acid from S to P at position 102.
+The protein's natural variant, known as in strain: FSLc2011, features a modification of the amino acid from A to T at position 22.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from A to V at position 123.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from T to M at position 291.
+The natural variant of this protein is characterized by an amino acid alteration from D to H at position 609.
+The protein's natural variant, known as in strain: 2137 and CC-503, features a modification of the amino acid from R to A at position 25.
+The protein's natural variant, known as in GLC1E;, features a modification of the amino acid from H to D at position 26.
+The protein's natural variant, known as in GLC1E; selectively promotes cell death of retinal ganglion cells probably by inducing TBC1D17-mediated inhibition of autophagy; affects Rab8-mediated endocytic trafficking; no effect on interaction with TBC1D17; increases colocalization with TBC1D17 and Rab8; increases interaction with TFRC and impairs its endocytic recycling; increases interactions with TBK1; decreases self-association; disturbs transition from the ER to Golgi; no effect on ubiquitin-binding; increases interaction with RAB8A as shown by immunoprecipitation in transfected HeLa cells, although other assays in yeast and mice show loss of direct interaction, it has been proposed that the variant might abolish direct interaction with Rab8 and enhance indirect interaction, hence altering the functional positioning of the molecules in the complex in such a way that it leads to constitutive or increased inactivation of Rab8 by TBC1D17;, features a modification of the amino acid from E to K at position 50.
+The protein's natural variant, known as may modify intraocular pressure and increase risk of GLC1E and NPG; induces TFRC degradation leading to autophagic death in retinal ganglion cells;, features a modification of the amino acid from M to K at position 98.
+The protein's natural variant, known as in GLC1E;, features a modification of the amino acid from E to D at position 103.
+The natural variant of this protein is characterized by an amino acid alteration from P to S at position 201.
+The protein's natural variant, known as requires 2 nucleotide substitutions, features a modification of the amino acid from K to H at position 213.
+The protein's natural variant, known as in ALS12; no effect on Golgi subcellular location; no effect on protein expression level; increased Golgi fragmentation; decreased Golgi ribbon formation; increased susceptibility to endoplasmic reticulum (ER) stress;, features a modification of the amino acid from V to F at position 295.
+The natural variant of this protein is characterized by an amino acid alteration from T to P at position 357.
+The protein's natural variant, known as in ALS12;, features a modification of the amino acid from E to G at position 478.
+The protein's natural variant, known as in GLC1E; juvenile onset;, features a modification of the amino acid from H to R at position 486.
+The protein's natural variant, known as in GLC1E; unknown pathological significance;, features a modification of the amino acid from R to Q at position 545.
+The protein's natural variant, known as found in a patient with nephrotic syndrome; unknown pathological significance; no effect on protein localization;, features a modification of the amino acid from Y to H at position 801.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from L to H at position 12.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from L to P at position 13.
+The protein's natural variant, known as in XLRS1; loss of octamerization; no effect on secretion;, features a modification of the amino acid from C to S at position 59.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from Y to C at position 65.
+The protein's natural variant, known as in XLRS1, features a modification of the amino acid from G to A at position 70.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from G to S at position 70.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from E to D at position 72.
+The protein's natural variant, known as in XLRS1, features a modification of the amino acid from E to G at position 72.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from E to K at position 72.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from S to P at position 73.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from G to V at position 74.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from Y to C at position 89.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from W to R at position 96.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from A to E at position 98.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from R to Q at position 102.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from R to W at position 102.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from L to R at position 103.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from F to C at position 108.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from G to E at position 109.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from G to R at position 109.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from G to W at position 109.
+The protein's natural variant, known as in XLRS1; loss of secretion into the extracellular space; may impair protein folding;, features a modification of the amino acid from C to Y at position 110.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from W to C at position 112.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from L to F at position 113.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from L to P at position 127.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from G to V at position 135.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from I to T at position 136.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from T to A at position 138.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from G to E at position 140.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from G to R at position 140.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from R to C at position 141.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from R to G at position 141.
+The protein's natural variant, known as in XLRS1; no effect on oligomerization; no effect on protein stability;, features a modification of the amino acid from R to H at position 141.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from C to W at position 142.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from D to V at position 143.
+The protein's natural variant, known as in XLRS1, features a modification of the amino acid from D to H at position 145.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from E to D at position 146.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from E to K at position 146.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from Y to C at position 155.
+The protein's natural variant, known as in XLRS1, features a modification of the amino acid from R to G at position 156.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from W to C at position 163.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from G to D at position 178.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from R to C at position 182.
+The protein's natural variant, known as in XLRS1, features a modification of the amino acid from P to L at position 192.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from P to R at position 192.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from P to S at position 192.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from P to L at position 193.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from P to S at position 193.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from R to C at position 197.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from R to H at position 197.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from I to T at position 199.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from R to C at position 200.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from R to H at position 200.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from P to L at position 203.
+The protein's natural variant, known as in XLRS1, features a modification of the amino acid from W to C at position 206.
+The protein's natural variant, known as in XLRS1; decreases protein stability; does not abrogate oligomerization or secretion;, features a modification of the amino acid from H to Q at position 207.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from R to C at position 209.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from R to H at position 209.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from R to Q at position 213.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from R to W at position 213.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from E to K at position 215.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from E to Q at position 215.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from L to P at position 216.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from C to G at position 219.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from C to R at position 219.
+The protein's natural variant, known as in XLRS1;, features a modification of the amino acid from C to R at position 223.
+The protein's natural variant, known as in EKVP4; loss of 3-dehydrosphinganine reductase activity, features a modification of the amino acid from QG to R at position 56.
+The protein's natural variant, known as in EKVP4;, features a modification of the amino acid from Y to F at position 186.
+The natural variant of this protein is characterized by an amino acid alteration from A to V at position 224.
+The protein's natural variant, known as in MC1DN6;, features a modification of the amino acid from R to Q at position 228.
+The protein's natural variant, known as in MC1DN6;, features a modification of the amino acid from P to Q at position 229.
+The protein's natural variant, known as in MC1DN6;, features a modification of the amino acid from S to P at position 413.
+The protein's natural variant, known as in MC1DN6; loss of catalytic activity; no change in Km value for ubiquinone-1, features a modification of the amino acid from D to N at position 446.
+The protein's natural variant, known as in strain: TN106, features a modification of the amino acid from YG to FS at position 119.
+The protein's natural variant, known as in strain: TN106, features a modification of the amino acid from D to E at position 121.
+The protein's natural variant, known as in strain: TN106, features a modification of the amino acid from GA to SS at position 125.
+The protein's natural variant, known as in strain: TN106, features a modification of the amino acid from S to P at position 128.
+The protein's natural variant, known as in strain: TN106, features a modification of the amino acid from A to S at position 151.
+The protein's natural variant, known as in NTD; unknown pathological significance;, features a modification of the amino acid from G to C at position 156.
+The protein's natural variant, known as in SAVA; reduced DNA binding activity; increased cell growth; altered expression of genes involved in ossification and notochord maintenance;, features a modification of the amino acid from H to R at position 171.
+The protein's natural variant, known as in Sinnai, features a modification of the amino acid from V to L at position 12.
+The protein's natural variant, known as in NSHA; Gahoe; class III; frequent in Chinese;, features a modification of the amino acid from H to R at position 32.
+The protein's natural variant, known as in NSHA; Orissa; class III; frequent in Indian tribal populations;, features a modification of the amino acid from A to G at position 44.
+The protein's natural variant, known as in NSHA; Aures; class II;, features a modification of the amino acid from I to T at position 48.
+The protein's natural variant, known as in NSHA; Metaponto; class III;, features a modification of the amino acid from D to N at position 58.
+The protein's natural variant, known as in NSHA; A(-) type I; class III; frequent in African population;, features a modification of the amino acid from V to M at position 68.
+The protein's natural variant, known as in NSHA; Namoru; 4% activity;, features a modification of the amino acid from Y to H at position 70.
+The protein's natural variant, known as in NSHA; Swansea; class I, features a modification of the amino acid from L to P at position 75.
+The protein's natural variant, known as in NSHA; Konan/Ube; class III;, features a modification of the amino acid from R to C at position 81.
+The protein's natural variant, known as in NSHA; Lagosanto; class III;, features a modification of the amino acid from R to H at position 81.
+The protein's natural variant, known as in NSHA; Vancouver; class I;, features a modification of the amino acid from S to C at position 106.
+The protein's natural variant, known as found in Santa Maria and Mount Sinai; associated with C-387 in Mount Sinai; class IV and class I;, features a modification of the amino acid from N to D at position 126.
+The protein's natural variant, known as in NSHA; Vanua Lava; 4% activity;, features a modification of the amino acid from L to P at position 128.
+The protein's natural variant, known as in Chinese-4;, features a modification of the amino acid from G to V at position 131.
+The protein's natural variant, known as in NSHA; Ilesha; class III;, features a modification of the amino acid from E to K at position 156.
+The protein's natural variant, known as in NSHA; Plymouth; class I, features a modification of the amino acid from G to D at position 163.
+The protein's natural variant, known as in NSHA; Mahidol; class III; associated with reduced density of Plasmodium vivax but not Plasmodium falciparum in Southeast Asians; reduced activity;, features a modification of the amino acid from G to S at position 163.
+The protein's natural variant, known as in NSHA; Chinese-3; class II;, features a modification of the amino acid from N to D at position 165.
+The protein's natural variant, known as in NSHA; Naone; 1% activity, features a modification of the amino acid from R to H at position 166.
+The protein's natural variant, known as in NSHA; Shinshu; class I, features a modification of the amino acid from D to G at position 176.
+The protein's natural variant, known as in NSHA; Santa Maria; class I;, features a modification of the amino acid from D to V at position 181.
+The protein's natural variant, known as in NSHA; Vancouver; class I;, features a modification of the amino acid from R to W at position 182.
+The protein's natural variant, known as in Dindori; class II; 5% of activity;, features a modification of the amino acid from S to F at position 184.
+The protein's natural variant, known as in NSHA; Sassari/Cagliari; class II; frequent in the Mediterranean;, features a modification of the amino acid from S to F at position 188.
+The protein's natural variant, known as in Coimbra; class II;, features a modification of the amino acid from R to C at position 198.
+The protein's natural variant, known as in Nilgiris; class II;, features a modification of the amino acid from R to H at position 198.
+The protein's natural variant, known as in NSHA; Santiago; class I;, features a modification of the amino acid from R to P at position 198.
+The protein's natural variant, known as in NSHA; Herlev; loss of glucose-6-phosphate dehydrogenase activity, features a modification of the amino acid from R to S at position 198.
+The protein's natural variant, known as in NSHA; Sibari; class III;, features a modification of the amino acid from M to V at position 212.
+The protein's natural variant, known as in NSHA; Minnesota; class I;, features a modification of the amino acid from V to L at position 213.
+The protein's natural variant, known as in NSHA; Harilaou; class I;, features a modification of the amino acid from F to L at position 216.
+The protein's natural variant, known as in NSHA; A- type 2; class III;, features a modification of the amino acid from R to L at position 227.
+The protein's natural variant, known as in Mexico City; class III;, features a modification of the amino acid from R to Q at position 227.
+The protein's natural variant, known as in NSHA; Wayne; class I, features a modification of the amino acid from R to G at position 257.
+The protein's natural variant, known as in NSHA; Corum; class I, features a modification of the amino acid from E to K at position 274.
+The protein's natural variant, known as in NSHA; Wexham; class I, features a modification of the amino acid from S to F at position 278.
+The protein's natural variant, known as in NSHA; Chinese-1; class II, features a modification of the amino acid from T to S at position 279.
+The protein's natural variant, known as in NSHA; Seattle; class III;, features a modification of the amino acid from D to H at position 282.
+The protein's natural variant, known as in NSHA; Montalbano; class III;, features a modification of the amino acid from R to H at position 285.
+The protein's natural variant, known as in NSHA; Viangchan/Jammu; class II;, features a modification of the amino acid from V to M at position 291.
+The protein's natural variant, known as in NSHA; Kalyan/Kerala; class III;, features a modification of the amino acid from E to K at position 317.
+The protein's natural variant, known as in NSHA; Bhavnagar; decreased enzyme stability, features a modification of the amino acid from G to V at position 321.
+The protein's natural variant, known as in Rehovot;, features a modification of the amino acid from Y to H at position 322.
+The protein's natural variant, known as in NSHA; A- type 3; class III;, features a modification of the amino acid from L to P at position 323.
+The protein's natural variant, known as in NSHA; Chatham; class III;, features a modification of the amino acid from A to T at position 335.
+The protein's natural variant, known as in Chinese-5;, features a modification of the amino acid from L to F at position 342.
+The protein's natural variant, known as in Ierapetra; class II;, features a modification of the amino acid from P to S at position 353.
+The protein's natural variant, known as in NSHA; Loma Linda; class I;, features a modification of the amino acid from N to K at position 363.
+The protein's natural variant, known as in NSHA; Tomah; class I;, features a modification of the amino acid from C to R at position 385.
+The protein's natural variant, known as in NSHA; Iowa; class I;, features a modification of the amino acid from K to E at position 386.
+The protein's natural variant, known as in NSHA; Guadajalara and Mount Sinai; class I;, features a modification of the amino acid from R to C at position 387.
+The protein's natural variant, known as in NSHA; Beverly Hills; class I;, features a modification of the amino acid from R to H at position 387.
+The protein's natural variant, known as in NSHA; Nashville/Anaheim; class I;, features a modification of the amino acid from R to H at position 393.
+The protein's natural variant, known as in NSHA; Alhambra; class I;, features a modification of the amino acid from V to L at position 394.
+The protein's natural variant, known as in NSHA; Bari; class I;, features a modification of the amino acid from P to L at position 396.
+The protein's natural variant, known as in NSHA; Puerto Limon; class I;, features a modification of the amino acid from E to K at position 398.
+The protein's natural variant, known as in NSHA; Riverside; class I;, features a modification of the amino acid from G to C at position 410.
+The protein's natural variant, known as in NSHA; Japan; class I;, features a modification of the amino acid from G to D at position 410.
+The protein's natural variant, known as in NSHA; Tokyo; class I, features a modification of the amino acid from E to K at position 416.
+The protein's natural variant, known as in NSHA; Pawnee; class I;, features a modification of the amino acid from R to P at position 439.
+The protein's natural variant, known as in NSHA; Telti/Kobe; class I;, features a modification of the amino acid from L to F at position 440.
+The protein's natural variant, known as in NSHA; Santiago de Cuba; class I;, features a modification of the amino acid from G to R at position 447.
+The protein's natural variant, known as in NSHA; Cassano; class II, features a modification of the amino acid from Q to H at position 449.
+The protein's natural variant, known as in NSHA; Chinese-II/Maewo/Union; class II; <1% activity;, features a modification of the amino acid from R to C at position 454.
+The protein's natural variant, known as in NSHA; Andalus; class I;, features a modification of the amino acid from R to H at position 454.
+The protein's natural variant, known as in NSHA; Canton; class II; frequent in China;, features a modification of the amino acid from R to L at position 459.
+The protein's natural variant, known as in NSHA; Cosenza; class II;, features a modification of the amino acid from R to P at position 459.
+The protein's natural variant, known as in Kaiping; class II;, features a modification of the amino acid from R to H at position 463.
+The protein's natural variant, known as in NSHA; Campinas; class I, features a modification of the amino acid from G to V at position 488.
+The protein's natural variant, known as no effect on substrate affinity;, features a modification of the amino acid from I to V at position 2458.
+The protein's natural variant, known as in AOS6;, features a modification of the amino acid from A to P at position 121.
+The protein's natural variant, known as in AOS6;, features a modification of the amino acid from R to C at position 186.
+The protein's natural variant, known as in AOS6;, features a modification of the amino acid from F to L at position 195.
+The protein's natural variant, known as in AOS6;, features a modification of the amino acid from P to T at position 267.
+The protein's natural variant, known as in AOS6;, features a modification of the amino acid from C to R at position 390.
+The protein's natural variant, known as in AOS6;, features a modification of the amino acid from C to Y at position 390.
+The protein's natural variant, known as in AOS6;, features a modification of the amino acid from C to W at position 455.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from R to C at position 418.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from A to V at position 26.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from V to M at position 39.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from V to I at position 59.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from Y to H at position 115.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from T to I at position 124.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from R to G at position 143.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from R to Q at position 143.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from R to W at position 143.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from K to N at position 146.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from S to I at position 148.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from Y to C at position 162.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from V to L at position 186.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from N to K at position 187.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from T to N at position 188.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from R to T at position 190.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from A to T at position 196.
+The protein's natural variant, known as in CMD1S;, features a modification of the amino acid from I to T at position 201.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from R to H at position 204.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from K to Q at position 207.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from P to L at position 211.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from Q to K at position 222.
+The protein's natural variant, known as in CMD1S;, features a modification of the amino acid from A to T at position 223.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from L to V at position 227.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from N to S at position 232.
+The protein's natural variant, known as in CMH1 and LVNC5;, features a modification of the amino acid from R to H at position 243.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from F to L at position 244.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from R to Q at position 249.
+The protein's natural variant, known as in LVNC5, features a modification of the amino acid from F to L at position 252.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from G to E at position 256.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from I to M at position 263.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from I to T at position 263.
+The protein's natural variant, known as in CMD1S;, features a modification of the amino acid from Y to D at position 283.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from F to C at position 312.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from V to M at position 320.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from E to G at position 328.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from M to T at position 349.
+The protein's natural variant, known as in CMD1S, features a modification of the amino acid from Y to N at position 350.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from K to E at position 351.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from A to T at position 355.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from K to N at position 383.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from A to V at position 385.
+The protein's natural variant, known as in CMD1S, features a modification of the amino acid from L to P at position 390.
+The protein's natural variant, known as in CMH1, features a modification of the amino acid from L to V at position 390.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from R to L at position 403.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from R to Q at position 403.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from R to W at position 403.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from V to L at position 404.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from V to M at position 404.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from V to M at position 406.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from G to V at position 407.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from V to I at position 411.
+The protein's natural variant, known as in CMD1S;, features a modification of the amino acid from T to N at position 412.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from G to R at position 425.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from A to V at position 428.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from A to E at position 430.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from M to T at position 435.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from V to M at position 440.
+The protein's natural variant, known as in MPD1;, features a modification of the amino acid from T to M at position 441.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from I to T at position 443.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from K to E at position 450.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from K to T at position 450.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from R to C at position 453.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from R to H at position 453.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from R to S at position 453.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from N to S at position 479.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from E to K at position 483.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from E to D at position 497.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from E to K at position 499.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from E to A at position 500.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from Y to C at position 501.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from I to F at position 511.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from I to T at position 511.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from F to C at position 513.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from M to R at position 515.
+The protein's natural variant, known as in CMH1; infrequent, features a modification of the amino acid from M to V at position 515.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from L to M at position 517.
+The protein's natural variant, known as in CMD1S;, features a modification of the amino acid from S to P at position 532.
+The protein's natural variant, known as in CMD1S;, features a modification of the amino acid from A to V at position 550.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from G to R at position 571.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from H to R at position 576.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from G to R at position 584.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from G to S at position 584.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from D to V at position 587.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from Q to R at position 595.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from L to V at position 601.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from N to S at position 602.
+The protein's natural variant, known as in CMH1; in cis with V-728 gives a more severe phenotype;, features a modification of the amino acid from V to M at position 606.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from K to N at position 615.
+The protein's natural variant, known as in CMH1, features a modification of the amino acid from K to Q at position 615.
+The protein's natural variant, known as in CMD1S;, features a modification of the amino acid from S to L at position 642.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from M to I at position 659.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from R to C at position 663.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from R to H at position 663.
+The protein's natural variant, known as in CMH1, features a modification of the amino acid from R to S at position 663.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from R to C at position 671.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from R to C at position 694.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from R to H at position 694.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from N to S at position 696.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from V to A at position 698.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from R to L at position 712.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from G to R at position 716.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from R to Q at position 719.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from R to W at position 719.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from R to C at position 723.
+The protein's natural variant, known as in CMH1; malignant phenotype;, features a modification of the amino acid from R to G at position 723.
+The protein's natural variant, known as in CMH1; in cis with M-606 gives a more severe phenotype;, features a modification of the amino acid from A to V at position 728.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from P to L at position 731.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from G to E at position 733.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from Q to E at position 734.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from Q to P at position 734.
+The protein's natural variant, known as in CMH1, features a modification of the amino acid from I to M at position 736.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from I to T at position 736.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from G to R at position 741.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from G to W at position 741.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from A to E at position 742.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from E to D at position 743.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from V to G at position 763.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from V to M at position 763.
+The protein's natural variant, known as in CMD1S;, features a modification of the amino acid from F to L at position 764.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from G to R at position 768.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from E to V at position 774.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from D to E at position 778.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from D to G at position 778.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from D to V at position 778.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from S to N at position 782.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from R to C at position 787.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from R to H at position 787.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from L to F at position 796.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from A to T at position 797.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from M to L at position 822.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from M to T at position 822.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from G to E at position 823.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from V to I at position 824.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from E to Q at position 846.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from M to T at position 852.
+The protein's natural variant, known as in CMH1; infrequent;, features a modification of the amino acid from R to C at position 858.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from R to H at position 858.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from R to C at position 869.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from R to G at position 869.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from R to H at position 869.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from R to C at position 870.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from R to H at position 870.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from M to K at position 877.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from Q to E at position 882.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from E to G at position 894.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from A to G at position 901.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from C to F at position 905.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from D to G at position 906.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from L to V at position 908.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from E to K at position 921.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from E to K at position 924.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from E to Q at position 924.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from E to K at position 927.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from D to N at position 928.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from E to K at position 930.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from E to K at position 931.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from E to K at position 935.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from E to K at position 949.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from D to H at position 953.
+The protein's natural variant, known as in CMD1S;, features a modification of the amino acid from T to N at position 1019.
+The protein's natural variant, known as in CMD1S, features a modification of the amino acid from V to A at position 1044.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from G to D at position 1057.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from G to S at position 1057.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from L to R at position 1135.
+The protein's natural variant, known as in CMD1S;, features a modification of the amino acid from R to S at position 1193.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from E to Q at position 1218.
+The protein's natural variant, known as in CMD1S;, features a modification of the amino acid from A to E at position 1263.
+The protein's natural variant, known as in CMD1S, features a modification of the amino acid from L to V at position 1297.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from N to K at position 1327.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from E to K at position 1356.
+The protein's natural variant, known as in LVNC5; unknown pathological significance;, features a modification of the amino acid from R to C at position 1359.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from T to M at position 1377.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from A to T at position 1379.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from R to W at position 1382.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from L to M at position 1414.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from R to W at position 1420.
+The protein's natural variant, known as in CMD1S;, features a modification of the amino acid from E to K at position 1426.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from A to T at position 1454.
+The protein's natural variant, known as in CMH1 and CMD1S;, features a modification of the amino acid from K to N at position 1459.
+The protein's natural variant, known as in MPD1;, features a modification of the amino acid from R to P at position 1500.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from T to S at position 1513.
+The natural variant of this protein is characterized by an amino acid alteration from S to C at position 1519.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from E to K at position 1555.
+The protein's natural variant, known as in CMD1S; unknown pathological significance;, features a modification of the amino acid from E to K at position 1573.
+The protein's natural variant, known as in CMD1S; unknown pathological significance;, features a modification of the amino acid from R to C at position 1634.
+The protein's natural variant, known as in MPD1;, features a modification of the amino acid from A to P at position 1663.
+The protein's natural variant, known as in CMH1; unknown pathological significance, features a modification of the amino acid from V to M at position 1692.
+The protein's natural variant, known as in MPD1;, features a modification of the amino acid from L to P at position 1706.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from R to W at position 1712.
+The protein's natural variant, known as in CMH1; associated with phenotype variability;, features a modification of the amino acid from E to K at position 1752.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from E to K at position 1753.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from E to K at position 1768.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from S to G at position 1776.
+The protein's natural variant, known as in LVNC5, features a modification of the amino acid from S to T at position 1776.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from A to T at position 1777.
+The protein's natural variant, known as in MSMA;, features a modification of the amino acid from L to P at position 1793.
+The protein's natural variant, known as in MSMB;, features a modification of the amino acid from R to W at position 1820.
+The protein's natural variant, known as in MSMA and SPMM;, features a modification of the amino acid from R to W at position 1845.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from T to M at position 1854.
+The protein's natural variant, known as in CMH1;, features a modification of the amino acid from E to K at position 1883.
+The protein's natural variant, known as in MSMA;, features a modification of the amino acid from H to L at position 1901.
+The protein's natural variant, known as in CMD1S, features a modification of the amino acid from N to K at position 1918.
+The protein's natural variant, known as in CMH1; unknown pathological significance;, features a modification of the amino acid from T to M at position 1929.
+The protein's natural variant, known as in ingls; loss of interaction with Pikfyve but not with Fig4, features a modification of the amino acid from L to R at position 156.
+The protein's natural variant, known as in patients with PROC deficiency, features a modification of the amino acid from W to G at position 14.
+The protein's natural variant, known as in THPH3, features a modification of the amino acid from R to C at position 32.
+The protein's natural variant, known as in patients with PROC deficiency;, features a modification of the amino acid from R to W at position 38.
+The protein's natural variant, known as in patients with PROC deficiency;, features a modification of the amino acid from R to C at position 42.
+The protein's natural variant, known as in Malakoff; low anticoagulant activity;, features a modification of the amino acid from R to H at position 42.
+The protein's natural variant, known as in THPH3; type II; Osaka-10; alters proteolytic processing so that S-42 is the N-terminus of the mature protein;, features a modification of the amino acid from R to S at position 42.
+The protein's natural variant, known as in patients with PROC deficiency, features a modification of the amino acid from E to D at position 49.
+The protein's natural variant, known as in patients with PROC deficiency;, features a modification of the amino acid from R to C at position 51.
+The protein's natural variant, known as in Yonago; defective anticoagulant activity, features a modification of the amino acid from R to G at position 57.
+The protein's natural variant, known as in patients with PROC deficiency;, features a modification of the amino acid from R to Q at position 57.
+The protein's natural variant, known as in THPH3;, features a modification of the amino acid from R to W at position 57.
+The protein's natural variant, known as in THPH3; Vermont-1;, features a modification of the amino acid from E to A at position 62.
+The protein's natural variant, known as in patients with PROC deficiency;, features a modification of the amino acid from K to E at position 70.
+The protein's natural variant, known as in THPH3; Vermont-1;, features a modification of the amino acid from V to M at position 76.
+The protein's natural variant, known as in THPH4; no effect on secretion; no effect on catalytic activity in vitro, features a modification of the amino acid from D to G at position 77.
+The protein's natural variant, known as in patients with PROC deficiency, features a modification of the amino acid from G to C at position 89.
+The protein's natural variant, known as in patients with PROC deficiency;, features a modification of the amino acid from C to G at position 106.
+The protein's natural variant, known as in patients with PROC deficiency; La Jolla-1;, features a modification of the amino acid from H to N at position 108.
+The protein's natural variant, known as in patients with PROC deficiency, features a modification of the amino acid from G to R at position 109.
+The protein's natural variant, known as in THPH3;, features a modification of the amino acid from G to R at position 114.
+The protein's natural variant, known as in patients with PROC deficiency; requires 2 nucleotide substitutions, features a modification of the amino acid from F to A at position 118.
+The protein's natural variant, known as in patients with PROC deficiency;, features a modification of the amino acid from F to L at position 118.
+The protein's natural variant, known as in THPH4; neonatal purpura fulminans, features a modification of the amino acid from NG to K at position 145.
+The protein's natural variant, known as in THPH3;, features a modification of the amino acid from G to R at position 145.
+The protein's natural variant, known as in patients with PROC deficiency;, features a modification of the amino acid from C to Y at position 147.
+The protein's natural variant, known as in patients with PROC deficiency;, features a modification of the amino acid from H to P at position 149.
+The protein's natural variant, known as in patients with PROC deficiency;, features a modification of the amino acid from S to R at position 161.
+The protein's natural variant, known as in THPH4; drastically reduced secretion; colocalizes with 26S proteasome, features a modification of the amino acid from A to E at position 163.
+The protein's natural variant, known as in THPH3; drastically reduced secretion; colocalizes with 26S proteasome, features a modification of the amino acid from A to V at position 163.
+The protein's natural variant, known as in patients with PROC deficiency;, features a modification of the amino acid from C to Y at position 175.
+The protein's natural variant, known as in THPH4; Clamart;, features a modification of the amino acid from A to P at position 178.
+The protein's natural variant, known as in patients with PROC deficiency;, features a modification of the amino acid from F to V at position 181.
+The protein's natural variant, known as in patients with PROC deficiency;, features a modification of the amino acid from C to R at position 183.
+The protein's natural variant, known as in patients with PROC deficiency; La Jolla-3;, features a modification of the amino acid from R to W at position 189.
+The protein's natural variant, known as in patients with PROC deficiency;, features a modification of the amino acid from R to C at position 194.
+The protein's natural variant, known as in THPH3;, features a modification of the amino acid from P to L at position 210.
+The protein's natural variant, known as in patients with PROC deficiency;, features a modification of the amino acid from R to Q at position 211.
+The protein's natural variant, known as in THPH3; London-1/Tochigi;, features a modification of the amino acid from R to W at position 211.
+The protein's natural variant, known as in patients with PROC deficiency, features a modification of the amino acid from R to P at position 220.
+The protein's natural variant, known as in THPH3; Vermont-3;, features a modification of the amino acid from R to Q at position 220.
+The protein's natural variant, known as in THPH3;, features a modification of the amino acid from R to W at position 220.
+The protein's natural variant, known as in patients with PROC deficiency;, features a modification of the amino acid from S to R at position 223.
+The protein's natural variant, known as in patients with PROC deficiency;, features a modification of the amino acid from Q to H at position 226.
+The protein's natural variant, known as in patients with PROC deficiency, features a modification of the amino acid from A to G at position 240.
+The protein's natural variant, known as in THPH3;, features a modification of the amino acid from I to T at position 243.
+The protein's natural variant, known as in patients with PROC deficiency;, features a modification of the amino acid from H to Y at position 244.
+The protein's natural variant, known as in patients with PROC deficiency;, features a modification of the amino acid from H to Q at position 253.
+The protein's natural variant, known as in patients with PROC deficiency;, features a modification of the amino acid from L to F at position 265.
+The protein's natural variant, known as in Marseille; low anticoagulant activity;, features a modification of the amino acid from R to Q at position 271.
+The protein's natural variant, known as in patients with PROC deficiency;, features a modification of the amino acid from R to W at position 271.
+The protein's natural variant, known as in THPH3;, features a modification of the amino acid from R to C at position 272.
+The protein's natural variant, known as in patients with PROC deficiency, features a modification of the amino acid from D to DLD at position 281.
+The protein's natural variant, known as in THPH4;, features a modification of the amino acid from P to L at position 289.
+The protein's natural variant, known as in Paris; low anticoagulant activity;, features a modification of the amino acid from S to N at position 294.
+The protein's natural variant, known as in THPH3; also found in patients with PROC deficiency; decrease in vitamin-K dependent serine protease activity; decreased Golgi localization;, features a modification of the amino acid from D to H at position 297.
+The protein's natural variant, known as in patients with PROC deficiency, features a modification of the amino acid from N to D at position 298.
+The protein's natural variant, known as in patients with PROC deficiency;, features a modification of the amino acid from A to T at position 301.
+The protein's natural variant, known as in patients with PROC deficiency;, features a modification of the amino acid from A to V at position 301.
+The protein's natural variant, known as in patients with PROC deficiency;, features a modification of the amino acid from A to T at position 309.
+The protein's natural variant, known as in patients with PROC deficiency;, features a modification of the amino acid from S to L at position 312.
+The protein's natural variant, known as in a patient with PROC deficiency; sporadic case, features a modification of the amino acid from S to P at position 312.
+The protein's natural variant, known as in patients with PROC deficiency; abolishes Golgi localization, features a modification of the amino acid from P to S at position 317.
+The protein's natural variant, known as in THPH3;, features a modification of the amino acid from P to L at position 321.
+The protein's natural variant, known as in THPH3, features a modification of the amino acid from G to R at position 324.
+The protein's natural variant, known as in patients with PROC deficiency;, features a modification of the amino acid from E to V at position 327.
+The protein's natural variant, known as in THPH3;, features a modification of the amino acid from R to C at position 328.
+The protein's natural variant, known as in THPH4; Muenchen, features a modification of the amino acid from R to H at position 328.
+The protein's natural variant, known as in THPH4;, features a modification of the amino acid from G to S at position 334.
+The protein's natural variant, known as in THPH3; Vermont-2;, features a modification of the amino acid from T to M at position 340.
+The protein's natural variant, known as in patients with PROC deficiency, features a modification of the amino acid from G to D at position 343.
+The protein's natural variant, known as gain of function mutation; abolishes glycosylation at N-313; decreases its catalytic activity; significant loss of its protective effect on endothelial barrier function; increased activation by thrombin, features a modification of the amino acid from T to A at position 357.
+The protein's natural variant, known as in THPH4; neonatal purpura fulminans;, features a modification of the amino acid from V to A at position 367.
+The protein's natural variant, known as in THPH3; Osaka-6;, features a modification of the amino acid from P to L at position 369.
+The protein's natural variant, known as in patients with PROC deficiency, features a modification of the amino acid from M to I at position 385.
+The protein's natural variant, known as in patients with PROC deficiency, features a modification of the amino acid from A to T at position 388.
+The protein's natural variant, known as in patients with PROC deficiency;, features a modification of the amino acid from A to V at position 388.
+The protein's natural variant, known as in THPH3; Osaka-9;, features a modification of the amino acid from G to R at position 392.
+The protein's natural variant, known as in patients with PROC deficiency;, features a modification of the amino acid from R to W at position 394.
+The protein's natural variant, known as in THPH3; La Jolla-2/Osaka-7 and -8;, features a modification of the amino acid from D to N at position 401.
+The protein's natural variant, known as in THPH4; Hong Kong-2, features a modification of the amino acid from G to D at position 418.
+The protein's natural variant, known as in THPH3; also found in patients with PROC deficiency; decrease in vitamin-K dependent serine protease activity;, features a modification of the amino acid from V to L at position 420.
+The protein's natural variant, known as in THPH3, features a modification of the amino acid from G to S at position 423.
+The protein's natural variant, known as in THPH3, features a modification of the amino acid from C to Y at position 426.
+The protein's natural variant, known as in patients with PROC deficiency; Purmerend;, features a modification of the amino acid from G to S at position 433.
+The protein's natural variant, known as in THPH3, features a modification of the amino acid from T to N at position 436.
+The protein's natural variant, known as in THPH3; Osaka-4;, features a modification of the amino acid from Y to H at position 441.
+The protein's natural variant, known as in THPH3;, features a modification of the amino acid from W to C at position 444.
+The protein's natural variant, known as in patients with PROC deficiency;, features a modification of the amino acid from I to M at position 445.
+The protein's natural variant, known as in allele B*13:02, allele B*15:01, allele B*18:01, allele B*27:01, allele B*27:05, allele B*35:01, allele B*37:01, allele B*40:01, allele B*40:02, allele B*41:01, allele B*44:02, allele B*45:01, allele B*46:01, allele B*47:01, allele B*49:01, allele B*50:01, allele B*51:01, allele B*52:01, allele B*53:01, allele B*54:01, allele B*55:01, allele B*56:01, allele B*57:01, allele B*58:01, allele B*59:01, allele B*78:01 and allele B*82:01;, features a modification of the amino acid from L to R at position 2.
+The protein's natural variant, known as in allele B*13:02, allele B*15:01, allele B*18:01, allele B*27:01, allele B*27:05, allele B*35:01, allele B*37:01, allele B*40:01, allele B*40:02, allele B*41:01, allele B*44:02, allele B*45:01, allele B*46:01, allele B*47:01, allele B*49:01, allele B*50:01, allele B*51:01, allele B*52:01, allele B*53:01, allele B*54:01, allele B*55:01, allele B*56:01, allele B*57:01, allele B*58:01, allele B*59:01, allele B*78:01 and allele B*82:01;, features a modification of the amino acid from M to T at position 4.
+The protein's natural variant, known as in allele B*13:02, allele B*18:01, allele B*27:01, allele B*27:05, allele B*37:01, allele B*40:02, allele B*44:02, allele B*47:01, allele B*54:01, allele B*55:01, allele B*56:01, allele B*59:01 and allele B*82:01;, features a modification of the amino acid from V to L at position 9.
+The protein's natural variant, known as in allele B*13:02, allele B*18:01, allele B*27:01, allele B*27:05, allele B*35:01, allele B*37:01, allele B*40:02, allele B*44:02, allele B*47:01, allele B*51:01, allele B*52:01, allele B*53:01, allele B*54:01, allele B*55:01, allele B*56:01, allele B*57:01, allele B*58:01, allele B*59:01, allele B*78:01, allele B*81:01 and allele B*82:01;, features a modification of the amino acid from S to W at position 14.
+The protein's natural variant, known as in allele B*13:02, allele B*15:01, allele B*18:01, allele B*27:01, allele B*27:05, allele B*35:01, allele B*37:01, allele B*40:02, allele B*44:02, allele B*46:01, allele B*47:01, allele B*51:01, allele B*52:01, allele B*53:01, allele B*54:01, allele B*55:01, allele B*56:01, allele B*57:01, allele B*58:01, allele B*59:01, allele B*78:01, allele B*81:01 and allele B*82:01;, features a modification of the amino acid from A to G at position 15.
+The protein's natural variant, known as in allele B*13:02, allele B*18:01, allele B*27:01, allele B*27:05, allele B*35:01, allele B*37:01, allele B*40:02, allele B*44:02, allele B*47:01, allele B*51:01, allele B*52:01, allele B*53:01, allele B*57:01, allele B*58:01, allele B*78:01 and allele B*81:01;, features a modification of the amino acid from L to V at position 17.
+The protein's natural variant, known as in allele B*08:01; associated with increased risk for rheumatoid arthritis;, features a modification of the amino acid from Y to D at position 33.
+The protein's natural variant, known as in allele B*18:01, allele B*27:01, allele B*27:05, allele B*37:01, allele B*40:01, allele B*40:02, allele B*41:01, allele B*45:01, allele B*49:01, allele B*50:01 and allele B*73:01;, features a modification of the amino acid from Y to H at position 33.
+The protein's natural variant, known as in allele B*08:01, allele B*13:02, allele B*15:01, allele B*35:01, allele B*40:01, allele B*41:01, allele B*44:02, allele B*45:01, allele B*46:01, allele B*47:01, allele B*49:01, allele B*50:01, allele B*51:01, allele B*52:01, allele B*53:01, allele B*54:01, allele B*55:01, allele B*56:01, allele B*57:01, allele B*58:01, allele B*59:01, allele B*78:01 and allele B*82:01;, features a modification of the amino acid from S to A at position 35.
+The protein's natural variant, known as in allele B*08:01, allele B*13:02, allele B*15:01, allele B*35:01, allele B*40:01, allele B*41:01, allele B*44:02, allele B*45:01, allele B*46:01, allele B*47:01, allele B*49:01, allele B*50:01, allele B*51:01, allele B*52:01, allele B*53:01, allele B*54:01, allele B*55:01, allele B*56:01, allele B*57:01, allele B*58:01, allele B*59:01, allele B*78:01 and allele B*82:01;, features a modification of the amino acid from V to M at position 36.
+The protein's natural variant, known as in allele B*15:01, allele B*35:01, allele B*46:01, allele B*51:01, allele B*52:01, allele B*53:01, allele B*54:01, allele B*55:01, allele B*56:01, allele B*57:01, allele B*58:01, allele B*59:01 and allele B*78:01;, features a modification of the amino acid from S to A at position 48.
+The protein's natural variant, known as in allele B*13:02, allele B*27:01, allele B*27:05, allele B*40:01, allele B*40:02, allele B*41:01, allele B*44:02, allele B*45:01, allele B*47:01, allele B*49:01, allele B*50:01 and allele B*73:01;, features a modification of the amino acid from S to T at position 48.
+The protein's natural variant, known as in allele B*18:01;, features a modification of the amino acid from D to G at position 54.
+The protein's natural variant, known as in allele B*27:01, allele B*27:05, allele B*40:01, allele B*40:02, allele B*41:01, allele B*44:02, allele B*45:01, allele B*47:01, allele B*49:01 and allele B*50:01;, features a modification of the amino acid from Q to L at position 56.
+The protein's natural variant, known as in allele B*13:02, allele B*40:01, allele B*40:02, allele B*41:01, allele B*44:02, allele B*45:01, allele B*47:01, allele B*49:01 and allele B*50:01;, features a modification of the amino acid from A to T at position 65.
+The protein's natural variant, known as in allele B*54:01;, features a modification of the amino acid from E to G at position 69.
+The protein's natural variant, known as in allele B*40:01, allele B*40:02, allele B*41:01, allele B*44:02, allele B*45:01, allele B*47:01, allele B*49:01 and allele B*50:01;, features a modification of the amino acid from E to K at position 69.
+The protein's natural variant, known as in allele B*13:02, allele B*15:01, allele B*46:01 and allele B*57:01; requires 2 nucleotide substitutions, features a modification of the amino acid from E to M at position 69.
+The protein's natural variant, known as in allele B*18:01, allele B*35:01, allele B*37:01, allele B*51:01, allele B*52:01, allele B*53:01, allele B*58:01 and allele B*78:01; requires 2 nucleotide substitutions, features a modification of the amino acid from E to T at position 69.
+The protein's natural variant, known as in allele B*13:02, allele B*15:01, allele B*46:01 and allele B*57:01;, features a modification of the amino acid from E to A at position 70.
+The protein's natural variant, known as in allele B*54:01;, features a modification of the amino acid from I to V at position 76.
+The protein's natural variant, known as in allele B*57:01 and allele B*58:01;, features a modification of the amino acid from R to G at position 86.
+The protein's natural variant, known as in allele B*13:02, allele B*15:01, allele B*27:01, allele B*27:05, allele B*37:01, allele B*39:02, allele B*40:01, allele B*40:02, allele B*41:01, allele B*44:02, allele B*45:01, allele B*46:01, allele B*47:01, allele B*48:01, allele B*49:01, allele B*50:01, allele B*52:01, allele B*57:01 and allele B*58:01; requires 2 nucleotide substitutions, features a modification of the amino acid from N to E at position 87.
+The protein's natural variant, known as in allele B*57:01 and allele B*58:01;, features a modification of the amino acid from Q to R at position 89.
+The protein's natural variant, known as in allele B*46:01, features a modification of the amino acid from I to K at position 90.
+The protein's natural variant, known as in allele B*57:01 and allele B*58:01;, features a modification of the amino acid from I to N at position 90.
+The protein's natural variant, known as in allele B*14:01, allele B*27:01, allele B*27:05, allele B*38:01 and allele B*73:01;, features a modification of the amino acid from Y to C at position 91.
+The protein's natural variant, known as in allele B*08:01, allele B*35:01, allele B*51:01, allele B*53:01, allele B*59:01 and allele B*78:01;, features a modification of the amino acid from Y to F at position 91.
+The protein's natural variant, known as in allele B*57:01 and allele B*58:01; requires 2 nucleotide substitutions, features a modification of the amino acid from Y to M at position 91.
+The protein's natural variant, known as in allele B*13:02, allele B*15:01, allele B*18:01, allele B*37:01, allele B*39:02, allele B*40:01, allele B*40:02, allele B*41:01, allele B*44:02, allele B*45:01, allele B*47:01, allele B*48:01, allele B*49:01, allele B*50:01 and allele B*52:01;, features a modification of the amino acid from Y to S at position 91.
+The protein's natural variant, known as in allele B*46:01; requires 2 nucleotide substitutions, features a modification of the amino acid from A to R at position 93.
+The protein's natural variant, known as in allele B*08:01, allele B*13:02, allele B*14:01, allele B*15:01, allele B*18:01, allele B*35:01, allele B*37:01, allele B*38:01, allele B*39:02, allele B*40:01, allele B*40:02, allele B*41:01, allele B*44:02, allele B*45:01, allele B*47:01, allele B*48:01, allele B*49:01, allele B*50:01, allele B*51:01, allele B*52:01, allele B*53:01, allele B*59:01 and allele B*78:01;, features a modification of the amino acid from A to T at position 93.
+The protein's natural variant, known as in allele B*27:01, allele B*27:05 and allele B*73:01;, features a modification of the amino acid from Q to K at position 94.
+The protein's natural variant, known as in allele B*08:01, allele B*13:02, allele B*14:01, allele B*15:01, allele B*18:01, allele B*35:01, allele B*37:01, allele B*38:01, allele B*39:02, allele B*40:01, allele B*40:02, allele B*41:01, allele B*44:02, allele B*45:01, allele B*47:01, allele B*48:01, allele B*49:01, allele B*50:01, allele B*51:01, allele B*52:01, allele B*53:01, allele B*59:01 and allele B*78:01; requires 2 nucleotide substitutions, features a modification of the amino acid from Q to N at position 94.
+The protein's natural variant, known as in allele B*57:01 and allele B*58:01; requires 2 nucleotide substitutions, features a modification of the amino acid from Q to S at position 94.
+The protein's natural variant, known as in allele B*08:01, allele B*13:02, allele B*14:01, allele B*15:01, allele B*18:01, allele B*35:01, allele B*37:01, allele B*38:01, allele B*39:02, allele B*40:01, allele B*40:02, allele B*41:01, allele B*44:02, allele B*45:01, allele B*47:01, allele B*48:01, allele B*49:01, allele B*50:01, allele B*51:01, allele B*52:01, allele B*53:01, allele B*59:01 and allele B*78:01;, features a modification of the amino acid from A to T at position 95.
+The protein's natural variant, known as in allele B*13:02, allele B*15:01, allele B*18:01, allele B*27:01, allele B*35:01, allele B*37:01, allele B*38:01, allele B*40:01, allele B*40:02, allele B*41:01, allele B*44:02, allele B*45:01, allele B*47:01, allele B*48:01, allele B*49:01, allele B*50:01, allele B*51:01, allele B*52:01, allele B*53:01, allele B*57:01, allele B*58:01 and allele B*59:01;, features a modification of the amino acid from D to Y at position 98.
+The protein's natural variant, known as in allele B*46:01 and allele B*73:01;, features a modification of the amino acid from E to V at position 100.
+The protein's natural variant, known as in allele B*27:05, allele B*37:01 and allele B*47:01; requires 2 nucleotide substitutions, features a modification of the amino acid from S to D at position 101.
+The protein's natural variant, known as in allele B*73:01;, features a modification of the amino acid from S to G at position 101.
+The protein's natural variant, known as in allele B*13:02, allele B*27:01, allele B*38:01, allele B*44:02, allele B*49:01, allele B*51:01, allele B*52:01, allele B*53:01, allele B*57:01, allele B*58:01 and allele B*59:01;, features a modification of the amino acid from S to N at position 101.
+The protein's natural variant, known as in allele B*38:01, allele B*49:01, allele B*51:01, allele B*52:01, allele B*53:01, allele B*57:01 and allele B*59:01; part of Bw4 motif involved in the recognition of KIR3DL1;, features a modification of the amino acid from N to I at position 104.
+The protein's natural variant, known as in allele B*13:02, allele B*27:01, allele B*27:05, allele B*37:01, allele B*44:02 and allele B*47:01;, features a modification of the amino acid from N to T at position 104.
+The protein's natural variant, known as in allele B*13:02, allele B*27:01, allele B*38:01, allele B*44:02, allele B*49:01, allele B*51:01, allele B*52:01, allele B*53:01, allele B*57:01, allele B*58:01 and allele B*59:01; requires 2 nucleotide substitutions, features a modification of the amino acid from L to A at position 105.
+The protein's natural variant, known as in allele B*13:02, allele B*27:01, allele B*27:05, allele B*37:01, allele B*38:01, allele B*44:02, allele B*49:01, allele B*51:01, allele B*52:01, allele B*53:01, allele B*57:01, allele B*58:01 and allele B*59:01;, features a modification of the amino acid from R to L at position 106.
+The protein's natural variant, known as in allele B*13:02, allele B*27:01, allele B*27:05, allele B*37:01, allele B*38:01, allele B*44:02, allele B*47:01, allele B*49:01, allele B*51:01, allele B*52:01, allele B*53:01, allele B*57:01, allele B*58:01 and allele B*59:01; part of Bw4 motif involved in the recognition of KIR3DL1;, features a modification of the amino acid from G to R at position 107.
+The protein's natural variant, known as in allele B*73:01;, features a modification of the amino acid from A to D at position 114.
+The protein's natural variant, known as in allele B*35:01, allele B*44:02, allele B*53:01, allele B*57:01 and allele B*58:01;, features a modification of the amino acid from T to I at position 118.
+The protein's natural variant, known as in allele B*35:01, allele B*37:01, allele B*44:02, allele B*53:01, allele B*57:01 and allele B*58:01;, features a modification of the amino acid from L to I at position 119.
+The protein's natural variant, known as in allele B*13:02, allele B*41:01, allele B*45:01, allele B*49:01, allele B*50:01, allele B*51:01, allele B*52:01, allele B*54:01, allele B*55:01, allele B*56:01, allele B*59:01, allele B*73:01 and allele B*78:01, features a modification of the amino acid from L to W at position 119.
+The protein's natural variant, known as in allele B*27:01 and allele B*27:05;, features a modification of the amino acid from S to N at position 121.
+The protein's natural variant, known as in allele B*15:01, allele B*18:01, allele B*35:01, allele B*37:01, allele B*38:01, allele B*39:02, allele B*40:01, allele B*41:01, allele B*44:02, allele B*45:01, allele B*46:01, allele B*47:01, allele B*49:01, allele B*50:01, allele B*53:01, allele B*58:01, allele B*67:01 and allele B*82:01;, features a modification of the amino acid from S to R at position 121.
+The protein's natural variant, known as in allele B*13:02, allele B*51:01, allele B*52:01, allele B*54:01, allele B*55:01, allele B*56:01, allele B*59:01, allele B*73:01 and allele B*78:01;, features a modification of the amino acid from S to T at position 121.
+The protein's natural variant, known as in allele B*57:01; requires 2 nucleotide substitutions, features a modification of the amino acid from S to V at position 121.
+The protein's natural variant, known as in allele B*14:01, features a modification of the amino acid from S to W at position 121.
+The protein's natural variant, known as in allele B*47:01 and allele B*82:01;, features a modification of the amino acid from Y to F at position 123.
+The protein's natural variant, known as in allele B*37:01;, features a modification of the amino acid from Y to S at position 123.
+The protein's natural variant, known as in allele B*13:02, allele B*35:01, allele B*45:01, allele B*49:01, allele B*50:01, allele B*53:01, allele B*54:01, allele B*55:01, allele B*56:01, allele B*58:01, allele B*59:01 and allele B*82:01;, features a modification of the amino acid from V to L at position 127.
+The protein's natural variant, known as in allele B*73:01;, features a modification of the amino acid from V to M at position 127.
+The protein's natural variant, known as in allele B*14:01, allele B*27:01, allele B*27:05, allele B*37:01, allele B*44:02, allele B*45:01, allele B*47:01, allele B*49:01, allele B*50:01 and allele B*73:01;, features a modification of the amino acid from H to Y at position 137.
+The protein's natural variant, known as in allele B*27:01, allele B*27:05 and allele B*47:01;, features a modification of the amino acid from D to H at position 138.
+The protein's natural variant, known as in allele B*08:01, allele B*13:02, allele B*14:01, allele B*37:01, allele B*38:01, allele B*39:02, allele B*40:01, allele B*40:02, allele B*41:01, allele B*42:01, allele B*45:01, allele B*48:01, allele B*49:01, allele B*50:01, allele B*51:01, allele B*52:01, allele B*54:01, allele B*55:01, allele B*56:01, allele B*59:01, allele B*67:01, allele B*73:01, allele B*78:01, allele B*81:01 and allele B*82:01;, features a modification of the amino acid from D to N at position 138.
+The protein's natural variant, known as in allele B*27:01, allele B*27:05, allele B*44:02 and allele B*47:01;, features a modification of the amino acid from Y to D at position 140.
+The protein's natural variant, known as in allele B*14:01, allele B*37:01, allele B*38:01, allele B*39:02, allele B*67:01 and allele B*73:01;, features a modification of the amino acid from Y to F at position 140.
+The protein's natural variant, known as in allele B*13:02, allele B*45:01, allele B*49:01, allele B*50:01, allele B*54:01, allele B*55:01, allele B*56:01, allele B*59:01 and allele B*82:01; requires 2 nucleotide substitutions;, features a modification of the amino acid from Y to L at position 140.
+The protein's natural variant, known as in allele B*15:01, allele B*18:01, allele B*35:01, allele B*46:01, allele B*53:01, allele B*57:01 and allele B*58:01;, features a modification of the amino acid from Y to S at position 140.
+The protein's natural variant, known as in allele B*13:02, allele B*14:01, allele B*15:01, allele B*18:01, allele B*27:01, allele B*27:05, allele B*35:01, allele B*37:01, allele B*38:01, allele B*39:02, allele B*44:02, allele B*45:01, allele B*46:01, allele B*47:01, allele B*49:01, allele B*50:01, allele B*51:01, allele B*52:01, allele B*53:01, allele B*54:01, allele B*55:01, allele B*56:01, allele B*57:01, allele B*58:01, allele B*59:01, allele B*67:01, allele B*78:01 and allele B*82:01;, features a modification of the amino acid from R to S at position 155.
+The protein's natural variant, known as in allele B*40:01, allele B*48:01 and allele B*81:01;, features a modification of the amino acid from T to S at position 167.
+The protein's natural variant, known as in allele B*13:02;, features a modification of the amino acid from R to L at position 169.
+The protein's natural variant, known as in allele B*40:01, allele B*48:01 and allele B*81:01;, features a modification of the amino acid from W to L at position 171.
+The protein's natural variant, known as in allele B*08:01, allele B*13:02, allele B*18:01, allele B*27:01, allele B*27:05, allele B*35:01, allele B*37:01, allele B*38:01, allele B*39:02, allele B*40:01, allele B*40:02, allele B*41:01, allele B*42:01, allele B*44:02, allele B*45:01, allele B*47:01, allele B*48:01, allele B*53:01, allele B*54:01, allele B*56:01, allele B*57:01, allele B*58:01, allele B*59:01, allele B*67:01, allele B*73:01, allele B*81:01 and allele B*82:01;, features a modification of the amino acid from E to V at position 176.
+The protein's natural variant, known as in allele B*08:01, allele B*37:01, allele B*41:01, allele B*42:01, allele B*44:02, allele B*45:01 and allele B*82:01; requires 2 nucleotide substitutions;, features a modification of the amino acid from R to D at position 180.
+The protein's natural variant, known as in allele B*13:02, allele B*14:01, allele B*18:01, allele B*27:01, allele B*27:05, allele B*35:01, allele B*38:01, allele B*39:02, allele B*40:01, allele B*40:02, allele B*47:01, allele B*48:01, allele B*49:01, allele B*50:01, allele B*51:01, allele B*52:01, allele B*53:01, allele B*54:01, allele B*55:01, allele B*56:01, allele B*57:01, allele B*58:01, allele B*59:01, allele B*67:01, allele B*73:01, allele B*78:01 and allele B*81:01;, features a modification of the amino acid from R to L at position 180.
+The protein's natural variant, known as in allele B*15:01 and allele B*46:01;, features a modification of the amino acid from R to W at position 180.
+The protein's natural variant, known as in allele B*38:01, allele B*39:02 and allele B*67:01;, features a modification of the amino acid from A to T at position 182.
+The protein's natural variant, known as in allele B*82:01;, features a modification of the amino acid from G to D at position 186.
+The protein's natural variant, known as in allele B*15:01, allele B*35:01, allele B*44:02, allele B*45:01, allele B*46:01, allele B*49:01, allele B*50:01, allele B*51:01, allele B*52:01, allele B*53:01, allele B*56:01, allele B*57:01, allele B*58:01, allele B*78:01 and allele B*82:01; requires 2 nucleotide substitutions;, features a modification of the amino acid from E to L at position 187.
+The protein's natural variant, known as in allele B*08:01, allele B*14:01, allele B*18:01, allele B*37:01, allele B*38:01, allele B*39:02, allele B*41:01, allele B*42:01, allele B*54:01, allele B*55:01, allele B*59:01 and allele B*67:01; requires 2 nucleotide substitutions;, features a modification of the amino acid from E to T at position 187.
+The protein's natural variant, known as in allele B*44:02, allele B*45:01 and allele B*82:01;, features a modification of the amino acid from W to S at position 191.
+The protein's natural variant, known as in allele B*14:01, allele B*18:01, allele B*51:01, allele B*52:01, allele B*73:01 and allele B*78:01;, features a modification of the amino acid from Y to H at position 195.
+The protein's natural variant, known as in allele B*13:02, allele B*14:01, allele B*15:01, allele B*18:01, allele B*27:01, allele B*27:05, allele B*35:01, allele B*37:01, allele B*38:01, allele B*39:02, allele B*40:02, allele B*44:02, allele B*45:01, allele B*46:01, allele B*47:01, allele B*49:01, allele B*50:01, allele B*51:01, allele B*52:01, allele B*53:01, allele B*54:01, allele B*55:01, allele B*56:01, allele B*57:01, allele B*58:01, allele B*59:01, allele B*67:01, allele B*73:01, allele B*78:01 and allele B*82:01;, features a modification of the amino acid from D to E at position 201.
+The protein's natural variant, known as in allele B*08:01, allele B*13:02, allele B*14:01, allele B*15:01, allele B*18:01, allele B*27:01, allele B*27:05, allele B*35:01, allele B*37:01, allele B*38:01 allele B*39:02, allele B*40:02, allele B*41:01, allele B*42:01, allele B*44:02, allele B*45:01, allele B*46:01, allele B*47:01, allele B*49:01, allele B*50:01, allele B*51:01, allele B*52:01, allele B*53:01, allele B*54:01, allele B*55:01, allele B*56:01, allele B*57:01, allele B*58:01, allele B*59:01, allele B*67:01, allele B*73:01, allele B*78:01 and allele B*82:01;, features a modification of the amino acid from K to T at position 202.
+The protein's natural variant, known as in allele B*13:02, allele B*14:01, allele B*15:01, allele B*18:01, allele B*27:01, allele B*27:05, allele B*35:01, allele B*37:01, allele B*38:01, allele B*39:02, allele B*40:02, allele B*44:02, allele B*45:01, allele B*46:01, allele B*47:01, allele B*49:01, allele B*50:01, allele B*51:01, allele B*52:01, allele B*53:01, allele B*54:01, allele B*55:01, allele B*56:01, allele B*57:01, allele B*58:01, allele B*59:01, allele B*67:01, allele B*73:01, allele B*78:01 and allele B*82:01;, features a modification of the amino acid from E to Q at position 204.
+The protein's natural variant, known as in allele B*35:01, allele B*51:01, allele B*52:01, allele B*53:01, allele B*58:01 and allele B*78:01;, features a modification of the amino acid from I to V at position 218.
+The protein's natural variant, known as in allele B*44:02;, features a modification of the amino acid from A to V at position 223.
+The protein's natural variant, known as in allele B*73:01;, features a modification of the amino acid from R to G at position 263.
+The protein's natural variant, known as in allele B*48:01, allele B*81:01;, features a modification of the amino acid from A to T at position 269.
+The protein's natural variant, known as in allele B*73:01;, features a modification of the amino acid from E to Q at position 277.
+The protein's natural variant, known as in allele B*73:01;, features a modification of the amino acid from P to Q at position 291.
+The protein's natural variant, known as in allele B*73:01;, features a modification of the amino acid from K to E at position 292.
+The protein's natural variant, known as in allele B*73:01; requires 2 nucleotide substitutions, features a modification of the amino acid from L to C at position 294.
+The protein's natural variant, known as in allele B*73:01;, features a modification of the amino acid from E to K at position 299.
+The protein's natural variant, known as in allele B*15:01, allele B*18:01, allele B*35:01, allele B*37:01, allele B*45:01, allele B*46:01, allele B*49:01, allele B*50:01, allele B*51:01, allele B*52:01, allele B*53:01, allele B*54:01, allele B*55:01, allele B*56:01, allele B*58:01, allele B*59:01, allele B*73:01, allele B*78:01 and allele B*82:01;, features a modification of the amino acid from V to I at position 306.
+The protein's natural variant, known as in allele B*73:01, features a modification of the amino acid from AVVVIG to VVTVAVV at position 324.
+The protein's natural variant, known as in allele B*15:01, allele B*18:01, allele B*35:01, allele B*37:01, allele B*45:01, allele B*46:01, allele B*49:01, allele B*50:01, allele B*51:01, allele B*52:01, allele B*53:01, allele B*54:01, allele B*55:01, allele B*56:01, allele B*58:01, allele B*59:01, allele B*78:01 and allele B*82:01;, features a modification of the amino acid from A to T at position 329.
+The protein's natural variant, known as in allele B*47:01;, features a modification of the amino acid from M to V at position 331.
+The protein's natural variant, known as in allele B*14:01, allele B*15:01, allele B*18:01, allele B*35:01, allele B*37:01, allele B*38:01, allele B*39:02, allele B*45:01, allele B*46:01, allele B*49:01, allele B*50:01, allele B*51:01, allele B*52:01, allele B*53:01, allele B*54:01, allele B*55:01, allele B*56:01, allele B*58:01, allele B*59:01, allele B*67:01, allele B*73:01, allele B*78:01 and allele B*82:01;, features a modification of the amino acid from C to S at position 349.
+The natural variant of this protein is characterized by an amino acid alteration from T to I at position 389.
+The natural variant of this protein is characterized by an amino acid alteration from F to S at position 518.
+The protein's natural variant, known as associated with poor response to eculizumab in PNH patients;, features a modification of the amino acid from R to C at position 885.
+The protein's natural variant, known as associated with poor response to eculizumab in PNH patients;, features a modification of the amino acid from R to H at position 885.
+The protein's natural variant, known as confirmed at protein level;, features a modification of the amino acid from D to Y at position 966.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from I to V at position 156.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from N to S at position 158.
+The protein's natural variant, known as in RNA edited version;, features a modification of the amino acid from I to V at position 160.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from Y to F at position 640.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from T to N at position 664.
+The protein's natural variant, known as in MLASA1; unknown pathological significance;, features a modification of the amino acid from Q to R at position 101.
+The protein's natural variant, known as in MLASA1;, features a modification of the amino acid from R to W at position 144.
+The protein's natural variant, known as in MLASA1; unknown pathological significance; mild phenotype;, features a modification of the amino acid from R to Q at position 295.
+The protein's natural variant, known as in MLASA1; unknown pathological significance; mild phenotype;, features a modification of the amino acid from R to W at position 295.
+The protein's natural variant, known as in MFAB; confers constitutive activity;, features a modification of the amino acid from I to L at position 170.
+The protein's natural variant, known as in HPRL; loss of function;, features a modification of the amino acid from H to R at position 212.
+The protein's natural variant, known as in MCPH19; unknown pathological significance;, features a modification of the amino acid from R to C at position 254.
+The protein's natural variant, known as in CHUJANS; unknown pathological significance;, features a modification of the amino acid from F to S at position 17.
+The protein's natural variant, known as in CHUJANS; unknown pathological significance;, features a modification of the amino acid from R to C at position 110.
+The protein's natural variant, known as in CHUJANS; unknown pathological significance;, features a modification of the amino acid from R to S at position 110.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from V to I at position 469.
+The protein's natural variant, known as in CHUJANS; unknown pathological significance; found in a patient who also carries a de novo missense variant in TBC1D8B, features a modification of the amino acid from Q to E at position 1263.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from R to I at position 1767.
+The protein's natural variant, known as found in patient with severe intellectual disability; unknown pathological significance, features a modification of the amino acid from A to D at position 112.
+The protein's natural variant, known as in strain: cv. Nd-1, features a modification of the amino acid from D to N at position 838.
+The protein's natural variant, known as in strain: Isolate South Africa, features a modification of the amino acid from P to S at position 25.
+The protein's natural variant, known as in strain: Isolate South Africa, features a modification of the amino acid from I to V at position 188.
+The protein's natural variant, known as in strain: Isolate South Africa, features a modification of the amino acid from D to N at position 252.
+The protein's natural variant, known as in strain: Isolate South Africa, features a modification of the amino acid from T to I at position 257.
+The protein's natural variant, known as in alloantigen HPA-1B;, features a modification of the amino acid from L to P at position 59.
+The protein's natural variant, known as in GT2; severe type 1 phenotype; the mutation prevents normal ITGA2B/ITGB3 complex expression;, features a modification of the amino acid from C to Y at position 64.
+The protein's natural variant, known as in GT2;, features a modification of the amino acid from R to W at position 119.
+The protein's natural variant, known as in GT2, features a modification of the amino acid from Y to C at position 141.
+The protein's natural variant, known as in GT2;, features a modification of the amino acid from L to W at position 143.
+The protein's natural variant, known as in GT2; severe type 1 phenotype; the mutation prevented normal ITGA2B/ITGB3 complex expression on the cell surface;, features a modification of the amino acid from M to R at position 144.
+The protein's natural variant, known as in GT2;, features a modification of the amino acid from D to N at position 145.
+The protein's natural variant, known as in GT2; type B;, features a modification of the amino acid from D to Y at position 145.
+The protein's natural variant, known as in GT2; may confer constitutive activity to the alpha-IIb/(mutated)beta-3 receptor;, features a modification of the amino acid from M to V at position 150.
+The protein's natural variant, known as associated with neonatal thrombocytopenia; alloantigen Duv(a+); does not affect significantly the integrin function;, features a modification of the amino acid from T to I at position 166.
+The protein's natural variant, known as in alloantigen HPA-4B;, features a modification of the amino acid from R to Q at position 169.
+The protein's natural variant, known as in GT2; type II;, features a modification of the amino acid from S to L at position 188.
+The protein's natural variant, known as in GT2; variant form;, features a modification of the amino acid from L to P at position 222.
+The protein's natural variant, known as in GT2; type B;, features a modification of the amino acid from R to Q at position 240.
+The protein's natural variant, known as in GT2; variant Strasbourg-1;, features a modification of the amino acid from R to W at position 240.
+The protein's natural variant, known as in GT2;, features a modification of the amino acid from R to Q at position 242.
+The protein's natural variant, known as in GT2, features a modification of the amino acid from D to V at position 243.
+The protein's natural variant, known as in GT2; severe type 1 phenotype; the mutation prevents normal ITGA2B/ITGB3 complex expression on the cell surface; the mutation may interfere with correct folding of the protein;, features a modification of the amino acid from G to D at position 247.
+The protein's natural variant, known as in GT2; severe type 1 phenotype; the mutation prevents normal ITGA2B/ITGB3 complex expression on the cell surface; the mutation interupts the interaction of the ITGA2B/ITGB3 complex;, features a modification of the amino acid from K to M at position 279.
+The protein's natural variant, known as in GT2, features a modification of the amino acid from L to P at position 288.
+The protein's natural variant, known as in GT2;, features a modification of the amino acid from H to P at position 306.
+The protein's natural variant, known as in GT2, features a modification of the amino acid from M to L at position 321.
+The protein's natural variant, known as in GT2; not expressed on the surface and absent inside the transfected cells, features a modification of the amino acid from I to N at position 330.
+The protein's natural variant, known as in GT2;, features a modification of the amino acid from C to Y at position 400.
+The protein's natural variant, known as in alloantigen MO(+); in a case of neonatal alloimmune thrombocytopenia;, features a modification of the amino acid from P to A at position 433.
+The protein's natural variant, known as in alloantigen CA(+)/TU(+);, features a modification of the amino acid from R to Q at position 515.
+The protein's natural variant, known as in GT2;, features a modification of the amino acid from C to Y at position 532.
+The protein's natural variant, known as in GT2; type I;, features a modification of the amino acid from C to R at position 568.
+The protein's natural variant, known as in GT2, features a modification of the amino acid from C to F at position 586.
+The protein's natural variant, known as in GT2; gain-of-function mutation; constitutively binds ligand-induced binding sites antibodies and the fibrinogen-mimetic antibody PAC-1, features a modification of the amino acid from C to R at position 586.
+The protein's natural variant, known as in GT2, features a modification of the amino acid from G to S at position 598.
+The protein's natural variant, known as in GT2;, features a modification of the amino acid from C to R at position 601.
+The protein's natural variant, known as in GT2; type II;, features a modification of the amino acid from G to S at position 605.
+The protein's natural variant, known as in alloantigen SR(A);, features a modification of the amino acid from R to C at position 662.
+The protein's natural variant, known as in BDPLT24; the mutant protein is constitutively active; spontaneous FAK phosphosphorylation; abnormal cell shape;, features a modification of the amino acid from D to H at position 749.
+The protein's natural variant, known as in GT2; variant Strasbourg-1;, features a modification of the amino acid from S to P at position 778.
+The natural variant of this protein is characterized by an amino acid alteration from M to T at position 573.
+The protein's natural variant, known as found in a patient with schizophrenia; unknown pathological significance;, features a modification of the amino acid from R to C at position 679.
+The protein's natural variant, known as found in a patient with autism spectrum disorder; unknown pathological significance;, features a modification of the amino acid from I to T at position 863.
+The protein's natural variant, known as found in a patient with schizophrenia; unknown pathological significance;, features a modification of the amino acid from S to P at position 989.
+The protein's natural variant, known as found in a patient with schizophrenia; unknown pathological significance, features a modification of the amino acid from S to L at position 995.
+The protein's natural variant, known as in POF9;, features a modification of the amino acid from G to S at position 736.
+The protein's natural variant, known as in POF9;, features a modification of the amino acid from I to S at position 884.
+The protein's natural variant, known as in patients with macular dysfunction; macular dysfunction severity is influenced by the presence of a W-172 mutation in PRPH2.;, features a modification of the amino acid from R to H at position 229.
+The natural variant of this protein is characterized by an amino acid alteration from R to G at position 87.
+The protein's natural variant, known as in PW095; partially suppresses a rimM deletion, features a modification of the amino acid from N to H at position 105.
+The protein's natural variant, known as in PW097; partially suppresses a rimM deletion, features a modification of the amino acid from N to K at position 105.
+The protein's natural variant, known as in strain: 2.3.1, features a modification of the amino acid from L to T at position 108.
+The protein's natural variant, known as in strain: 2.3.1, features a modification of the amino acid from T to S at position 115.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from Y to N at position 60.
+The protein's natural variant, known as in allele DRB3*01:04, features a modification of the amino acid from L to S at position 37.
+The protein's natural variant, known as in allele DRB3*02:12;, features a modification of the amino acid from E to Q at position 38.
+The protein's natural variant, known as in allele DRB3*01:14; requires 2 nucleotide substitutions, features a modification of the amino acid from L to Y at position 39.
+The protein's natural variant, known as in allele DRB3*01:02, features a modification of the amino acid from R to C at position 40.
+The protein's natural variant, known as in allele DRB3*02:01, allele DRB3*02:02, allele DRB3*02:03, allele DRB3*02:04, allele DRB3*02:05, allele DRB3*02:06, allele DRB3*02:07, allele DRB3*02:08, allele DRB3*02:09, allele DRB3*02:10, allele DRB3*02:11, allele DRB3*02:12, allele DRB3*02:13, allele DRB3*02:14, allele DRB3*02:15, allele DRB3*02:16, allele DRB3*02:17, allele DRB3*02:18, allele DRB3*02:19, allele DRB3*02:20, allele DRB3*02:21, allele DRB3*02:22, allele DRB3*02:23, allele DRB3*02:24, allele DRB3*02:25, allele DRB3*03:01, allele DRB3*03:02 and allele DRB3*03:03;, features a modification of the amino acid from R to L at position 40.
+The protein's natural variant, known as in allele DRB3*01:14;, features a modification of the amino acid from R to S at position 40.
+The protein's natural variant, known as in allele DRB3*01:14;, features a modification of the amino acid from K to T at position 41.
+The protein's natural variant, known as in allele DRB3*01:09, allele DRB3*02:01, allele DRB3*02:02, allele DRB3*02:03, allele DRB3*02:04, allele DRB3*02:05, allele DRB3*02:06, allele DRB3*02:07, allele DRB3*02:08, allele DRB3*02:09, allele DRB3*02:10, allele DRB3*02:11, allele DRB3*02:12, allele DRB3*02:14, allele DRB3*02:15, allele DRB3*02:16, allele DRB3*02:17, allele DRB3*02:18, allele DRB3*02:19, allele DRB3*02:20, allele DRB3*02:21, allele DRB3*02:22, allele DRB3*02:23, allele DRB3*02:24, allele DRB3*02:25, allele DRB3*03:01, allele DRB3*03:02 and allele DRB3*03:03;, features a modification of the amino acid from Y to F at position 55.
+The protein's natural variant, known as in allele DRB3*02:13; requires 2 nucleotide substitutions, features a modification of the amino acid from Y to L at position 55.
+The protein's natural variant, known as in allele DRB3*01:03, allele DRB3*01:09, allele DRB3*02:01, allele DRB3*02:02, allele DRB3*02:03, allele DRB3*02:04, allele DRB3*02:05, allele DRB3*02:06, allele DRB3*02:07, allele DRB3*02:08, allele DRB3*02:09, allele DRB3*02:10, allele DRB3*02:11, allele DRB3*02:12, allele DRB3*02:13, allele DRB3*02:14, allele DRB3*02:15, allele DRB3*02:16, allele DRB3*02:17, allele DRB3*02:18, allele DRB3*02:19, allele DRB3*02:20, allele DRB3*02:21, allele DRB3*02:22, allele DRB3*02:23, allele DRB3*02:24, allele DRB3*02:25, allele DRB3*03:01, allele DRB3*03:02 and allele DRB3*03:03;, features a modification of the amino acid from D to E at position 57.
+The protein's natural variant, known as in allele DRB3*01:05;, features a modification of the amino acid from D to N at position 57.
+The protein's natural variant, known as in allele DRB3*01:11;, features a modification of the amino acid from R to I at position 58.
+The protein's natural variant, known as in allele DRB3*01:09, allele DRB3*02:01, allele DRB3*02:02, allele DRB3*02:03, allele DRB3*02:04, allele DRB3*02:06, allele DRB3*02:07, allele DRB3*02:08, allele DRB3*02:09, allele DRB3*02:10, allele DRB3*02:11, allele DRB3*02:12, allele DRB3*02:13, allele DRB3*02:14, allele DRB3*02:15, allele DRB3*02:16, allele DRB3*02:17, allele DRB3*02:18, allele DRB3*02:19, allele DRB3*02:20, allele DRB3*02:21, allele DRB3*02:22, allele DRB3*02:23, allele DRB3*02:24, allele DRB3*02:25 and allele DRB3*03:02;, features a modification of the amino acid from Y to H at position 59.
+The protein's natural variant, known as in allele DRB3*01:13;, features a modification of the amino acid from F to L at position 66.
+The protein's natural variant, known as in allele DRB3*01:08, allele DRB3*02:06 and allele DRB3*02:20; requires 2 nucleotide substitutions, features a modification of the amino acid from F to N at position 66.
+The protein's natural variant, known as in allele DRB3*02:03;, features a modification of the amino acid from F to S at position 66.
+The protein's natural variant, known as in allele DRB3*01:07, allele DRB3*01:09, allele DRB3*02:01, allele DRB3*02:02, allele DRB3*02:04, allele DRB3*02:05, allele DRB3*02:07, allele DRB3*02:08, allele DRB3*02:09, allele DRB3*02:10, allele DRB3*02:11, allele DRB3*02:12, allele DRB3*02:13, allele DRB3*02:14, allele DRB3*02:15, allele DRB3*02:16, allele DRB3*02:17, allele DRB3*02:18, allele DRB3*02:19, allele DRB3*02:21, allele DRB3*02:22, allele DRB3*02:23, allele DRB3*02:24 and allele DRB3*02:25;, features a modification of the amino acid from F to Y at position 66.
+The protein's natural variant, known as in allele DRB3*01:07, allele DRB3*01:09, allele DRB3*02:01, allele DRB3*02:02, allele DRB3*02:04, allele DRB3*02:05, allele DRB3*02:06, allele DRB3*02:07, allele DRB3*02:08, allele DRB3*02:09, allele DRB3*02:10, allele DRB3*02:11, allele DRB3*02:12, allele DRB3*02:13, allele DRB3*02:14, allele DRB3*02:15, allele DRB3*02:16, allele DRB3*02:17, allele DRB3*02:18, allele DRB3*02:19, allele DRB3*02:21, allele DRB3*02:22, allele DRB3*02:23, allele DRB3*02:24 and allele DRB3*02:25; requires 2 nucleotide substitutions, features a modification of the amino acid from L to A at position 67.
+The protein's natural variant, known as in allele DRB3*01:06, allele DRB3*01:08, allele DRB3*02:03, allele DRB3*02:20, allele DRB3*03:01, allele DRB3*03:02 and allele DRB3*03:03;, features a modification of the amino acid from L to V at position 67.
+The protein's natural variant, known as in allele DRB3*01:10;, features a modification of the amino acid from R to S at position 68.
+The protein's natural variant, known as in allele DRB3*01:07, allele DRB3*02:01, allele DRB3*02:02, allele DRB3*02:03, allele DRB3*02:04, allele DRB3*02:05, allele DRB3*02:06, allele DRB3*02:07, allele DRB3*02:08, allele DRB3*02:11, allele DRB3*02:12, allele DRB3*02:13, allele DRB3*02:14, allele DRB3*02:15, allele DRB3*02:16, allele DRB3*02:17, allele DRB3*02:18, allele DRB3*02:19, allele DRB3*02:20, allele DRB3*02:21, allele DRB3*02:22, allele DRB3*02:23, allele DRB3*02:24 and allele DRB3*02:25;, features a modification of the amino acid from T to R at position 80.
+The protein's natural variant, known as in allele DRB3*02:23, features a modification of the amino acid from R to L at position 84.
+The protein's natural variant, known as in allele DRB3*02:16;, features a modification of the amino acid from V to A at position 86.
+The protein's natural variant, known as in allele DRB3*01:07, allele DRB3*02:01, allele DRB3*02:02, allele DRB3*02:03, allele DRB3*02:04, allele DRB3*02:05, allele DRB3*02:06, allele DRB3*02:10, allele DRB3*02:11, allele DRB3*02:12, allele DRB3*02:13, allele DRB3*02:14, allele DRB3*02:15, allele DRB3*02:17, allele DRB3*02:18, allele DRB3*02:19, allele DRB3*02:20, allele DRB3*02:22, allele DRB3*02:23, allele DRB3*02:24 and allele DRB3*02:25;, features a modification of the amino acid from V to D at position 86.
+The protein's natural variant, known as in allele DRB3*02:08; requires 2 nucleotide substitutions, features a modification of the amino acid from V to S at position 86.
+The protein's natural variant, known as in allele DRB3*02:18, features a modification of the amino acid from A to E at position 87.
+The protein's natural variant, known as in allele DRB3*02:16; requires 2 nucleotide substitutions, features a modification of the amino acid from S to H at position 89.
+The protein's natural variant, known as in allele DRB3*01:07, allele DRB3*02:01, allele DRB3*02:02, allele DRB3*02:03, allele DRB3*02:04, allele DRB3*02:05, allele DRB3*02:06, allele DRB3*02:07, allele DRB3*02:08, allele DRB3*02:10, allele DRB3*02:11, allele DRB3*02:12, allele DRB3*02:13, allele DRB3*02:14, allele DRB3*02:15, allele DRB3*02:17, allele DRB3*02:18, allele DRB3*02:20, allele DRB3*02:22, allele DRB3*02:23 and allele DRB3*02:24;, features a modification of the amino acid from S to Y at position 89.
+The protein's natural variant, known as in allele DRB3*02:17;, features a modification of the amino acid from L to F at position 96.
+The protein's natural variant, known as in allele DRB3*02:11;, features a modification of the amino acid from L to I at position 96.
+The protein's natural variant, known as in allele DRB3*01:07, allele DRB3*02:01, allele DRB3*02:02, allele DRB3*02:03, allele DRB3*02:05, allele DRB3*02:06, allele DRB3*02:07, allele DRB3*02:08, allele DRB3*02:09, allele DRB3*02:10, allele DRB3*02:11, allele DRB3*02:12, allele DRB3*02:13, allele DRB3*02:14, allele DRB3*02:15, allele DRB3*02:16, allele DRB3*02:17, allele DRB3*02:18, allele DRB3*02:20, allele DRB3*02:21, allele DRB3*02:23, allele DRB3*02:24, allele DRB3*02:25, allele DRB3*03:01 and allele DRB3*03:02;, features a modification of the amino acid from R to Q at position 103.
+The protein's natural variant, known as in allele DRB3*02:15;, features a modification of the amino acid from N to T at position 106.
+The protein's natural variant, known as in allele DRB3*01:12, features a modification of the amino acid from G to R at position 113.
+The protein's natural variant, known as in allele DRB3*02:14, features a modification of the amino acid from G to A at position 115.
+The protein's natural variant, known as in allele DRB3*02:01, allele DRB3*02:04, allele DRB3*02:24, allele DRB3*03:01 and allele DRB3*03:02;, features a modification of the amino acid from G to V at position 115.
+The protein's natural variant, known as in allele DRB3*03:01;, features a modification of the amino acid from A to T at position 169.
+The protein's natural variant, known as in allele DRB3*03:01;, features a modification of the amino acid from Q to H at position 178.
+The protein's natural variant, known as in allele DRB3*02:01, features a modification of the amino acid from V to F at position 193.
+The protein's natural variant, known as in allele DRB3*02:01, allele DRB3*02:02, allele DRB3*02:10, allele DRB3*02:11, allele DRB3*02:24 and allele DRB3*03:01;, features a modification of the amino acid from A to P at position 212.
+The protein's natural variant, known as in allele DRB3*02:01, allele DRB3*02:02, allele DRB3*02:10 and allele DRB3*02:11;, features a modification of the amino acid from R to S at position 218.
+The protein's natural variant, known as in XLID58;, features a modification of the amino acid from P to H at position 172.
+The natural variant of this protein is characterized by an amino acid alteration from F to L at position 19.
+The natural variant of this protein is characterized by an amino acid alteration from Y to H at position 37.
+The natural variant of this protein is characterized by an amino acid alteration from P to A at position 136.
+The protein's natural variant, known as in Hy1 and Hy2;, features a modification of the amino acid from G to V at position 108.
+The protein's natural variant, known as in Jo(a);, features a modification of the amino acid from T to I at position 117.
+The protein's natural variant, known as in Do(b), Hy1 and Hy2;, features a modification of the amino acid from N to D at position 265.
+The protein's natural variant, known as in Hy1;, features a modification of the amino acid from L to V at position 300.
+The protein's natural variant, known as in strain: C57BL/6, features a modification of the amino acid from LAKDISP to SS at position 209.
+The protein's natural variant, known as exhibits significantly reduced B(max) and slightly enhanced affinity;, features a modification of the amino acid from R to W at position 54.
+The protein's natural variant, known as similar binding characteristics compared to wild-type;, features a modification of the amino acid from A to V at position 157.
+The natural variant of this protein is characterized by an amino acid alteration from K to M at position 167.
+The protein's natural variant, known as in RP26;, features a modification of the amino acid from R to S at position 106.
+The protein's natural variant, known as in OPA5; changed localization to mitochondrion; impaired mitochondrial membrane fission;, features a modification of the amino acid from E to A at position 2.
+The protein's natural variant, known as in EMPF1; autosomal recessive; impaired mitochondrial membrane fission; hypomorphic mutation retaining partial activity in mitochondrial membrane fission;, features a modification of the amino acid from S to G at position 36.
+The protein's natural variant, known as in OPA5; changed localization to mitochondrion; impaired mitochondrial membrane fission;, features a modification of the amino acid from A to E at position 192.
+The protein's natural variant, known as in EMPF1; unknown pathological significance; unable to associate with MIEF2 into filaments forming the tubular structures that wrap around the scission site; presence of concentric cristae and/or increased dense granules in some mitochondria;, features a modification of the amino acid from G to D at position 362.
+The protein's natural variant, known as in EMPF1; the mutation acts in a dominant-negative manner; defects observed in mitochondrial fission; significant decrease in mitochondrial respiratory chain complex IV activity;, features a modification of the amino acid from G to S at position 362.
+The protein's natural variant, known as in EMPF1; the mutation acts in a dominant-negative manner; defects observed in both mitochondrial and peroxisomal fission; reduced oligomerization, decreased mitochondrial recruitment;, features a modification of the amino acid from A to D at position 395.
+The protein's natural variant, known as in EMPF1; the mutation acts in a dominant-negative manner; reduced oligomerization; decreased mitochondrial recruitment; defects observed in mitochondrial fission;, features a modification of the amino acid from R to C at position 403.
+The protein's natural variant, known as in EMPF1; impaired mitochondrial and peroxisomal membrane fission, features a modification of the amino acid from L to S at position 406.
+The protein's natural variant, known as in strain: Isolate New Jersey 121A, features a modification of the amino acid from T to P at position 10.
+The protein's natural variant, known as in strain: Isolate Georgia 2B, features a modification of the amino acid from L to P at position 45.
+The protein's natural variant, known as in strain: Isolate Nova Scotia 2B, features a modification of the amino acid from L to P at position 49.
+The protein's natural variant, known as in strain: Isolate New Jersey 137A, features a modification of the amino acid from Q to R at position 112.
+The protein's natural variant, known as in strain: Isolate New Jersey 137A, features a modification of the amino acid from N to S at position 114.
+The protein's natural variant, known as in strain: Isolate Maine 2A, Isolate New Jersey 121B, Isolate New Jersey 197B, Isolate Nova Scotia 1A, Isolate Nova Scotia 1B, Isolate Nova Scotia 2A and Isolate Nova Scotia 2B, features a modification of the amino acid from A to S at position 185.
+The protein's natural variant, known as in strain: Isolate Nova Scotia 1B and Isolate Nova Scotia 2B, features a modification of the amino acid from E to D at position 287.
+The protein's natural variant, known as in strain: Isolate New Jersey 197B, features a modification of the amino acid from V to L at position 301.
+The protein's natural variant, known as in strain: Isolate Maine 2A, Isolate New Jersey 137A, Isolate New Jersey 137B, Isolate New Jersey 197B, Isolate Nova Scotia 1A, Isolate Nova Scotia 1B, Isolate Nova Scotia 2A and Isolate Nova Scotia 2B, features a modification of the amino acid from D to A at position 311.
+The protein's natural variant, known as in NISBD2; loss of function; the mutant does not localize to the cell membrane; has diffuse cytoplasmic localization;, features a modification of the amino acid from G to D at position 428.
+The protein's natural variant, known as found in a lung cancer sample; more sensitive to gefitinib than wild-type;, features a modification of the amino acid from E to A at position 709.
+The protein's natural variant, known as found in a lung cancer sample; constitutively activated kinase with higher levels of basal autophosphorylation; more sensitive to gefitinib than wild-type;, features a modification of the amino acid from E to G at position 709.
+The protein's natural variant, known as found in a lung cancer sample;, features a modification of the amino acid from E to K at position 709.
+The protein's natural variant, known as found in a lung cancer sample;, features a modification of the amino acid from G to A at position 719.
+The protein's natural variant, known as found in a lung cancer sample;, features a modification of the amino acid from G to C at position 719.
+The protein's natural variant, known as found in a lung cancer sample;, features a modification of the amino acid from G to D at position 719.
+The protein's natural variant, known as found in a lung cancer sample; somatic mutation; strongly increased kinase activity; constitutively activated kinase with higher levels of basal autophosphorylation; more sensitive to gefitinib than wild-type;, features a modification of the amino acid from G to S at position 719.
+The protein's natural variant, known as found in a lung cancer sample;, features a modification of the amino acid from G to S at position 724.
+The protein's natural variant, known as found in a lung cancer sample;, features a modification of the amino acid from E to K at position 734.
+The protein's natural variant, known as found in a lung cancer sample, features a modification of the amino acid from ELREATS to D at position 752.
+The protein's natural variant, known as found in a lung cancer sample, features a modification of the amino acid from ELREAT to A at position 751.
+The protein's natural variant, known as found in a lung cancer sample, features a modification of the amino acid from L to F at position 747.
+The protein's natural variant, known as found in a lung cancer sample, features a modification of the amino acid from R to P at position 748.
+The protein's natural variant, known as found in a lung cancer sample; constitutively activated kinase with higher levels of basal autophosphorylation; more sensitive to gefitinib than wild-type;, features a modification of the amino acid from S to I at position 768.
+The protein's natural variant, known as found in a lung cancer sample;, features a modification of the amino acid from V to M at position 769.
+The protein's natural variant, known as found in a lung cancer sample, features a modification of the amino acid from Q to R at position 787.
+The protein's natural variant, known as found in a lung cancer sample; increased kinase activity;, features a modification of the amino acid from T to M at position 790.
+The protein's natural variant, known as found in a lung cancer sample; more sensitive to gefitinib than wild-type;, features a modification of the amino acid from L to V at position 833.
+The protein's natural variant, known as found in a lung cancer sample;, features a modification of the amino acid from V to L at position 834.
+The protein's natural variant, known as found in a lung cancer sample; more sensitive to gefitinib than wild-type;, features a modification of the amino acid from H to L at position 835.
+The protein's natural variant, known as found in a lung cancer sample; more sensitive to gefitinib than wild-type;, features a modification of the amino acid from L to V at position 838.
+The protein's natural variant, known as found in a lung cancer sample;, features a modification of the amino acid from L to M at position 858.
+The protein's natural variant, known as found in a lung cancer sample; somatic mutation; constitutively activated enzyme with strongly increased kinase activity; more sensitive to gefitinib than wild-type;, features a modification of the amino acid from L to R at position 858.
+The protein's natural variant, known as found in a lung cancer sample; constitutively activated kinase with higher levels of basal autophosphorylation; more sensitive to gefitinib than wild-type;, features a modification of the amino acid from L to Q at position 861.
+The protein's natural variant, known as found in a lung cancer sample, features a modification of the amino acid from G to E at position 873.
+The protein's natural variant, known as in CFEOM3A; affects heterodimers formation; results in increased stability and reduced dynamics of microtubules;, features a modification of the amino acid from R to Q at position 62.
+The protein's natural variant, known as in CDCBM1; can form tubulin heterodimers that are properly incorporated into microtubules; the microtubules are less stable than wild-type;, features a modification of the amino acid from T to M at position 178.
+The protein's natural variant, known as in CDCBM1; does not form tubulin heterodimers; patient fibroblasts show no major alterations in the microtubule network, but the microtubules are less stable than wild-type;, features a modification of the amino acid from E to K at position 205.
+The protein's natural variant, known as in CFEOM3A; affects heterodimers formation; affects microtubules polymerization and depolymerization rates;, features a modification of the amino acid from R to C at position 262.
+The protein's natural variant, known as in CFEOM3A; severe phenotype with congenital facial weakness, congenital wrist and finger contractures; affects microtubules polymerization and depolymerization rates;, features a modification of the amino acid from R to H at position 262.
+The protein's natural variant, known as in CFEOM3A; affects heterodimers formation; results in increased stability and reduced dynamics of microtubules;, features a modification of the amino acid from A to T at position 302.
+The protein's natural variant, known as in CDCBM1; does not form tubulin heterodimers;, features a modification of the amino acid from A to V at position 302.
+The protein's natural variant, known as in CDCBM1; reduced heterodimers formation;, features a modification of the amino acid from M to V at position 323.
+The protein's natural variant, known as in CFEOM3A; affects heterodimers formation; results in increased stability and reduced dynamics of microtubules;, features a modification of the amino acid from R to C at position 380.
+The protein's natural variant, known as in CFEOM3A; severe phenotype with congenital facial weakness; lower extremity weakness and sensory loss in the second to third decade of life in one patient; affects microtubules polymerization and depolymerization rates;, features a modification of the amino acid from E to K at position 410.
+The protein's natural variant, known as in CFEOM3A; severe phenotype with congenital facial weakness, congenital wrist and finger contractures;, features a modification of the amino acid from D to H at position 417.
+The protein's natural variant, known as in CFEOM3A; some patients with lower extremity weakness and sensory loss in the second to third decade of life; also found in patients without CFEOM3A who developed polyneuropathy;, features a modification of the amino acid from D to N at position 417.
+The protein's natural variant, known as in UHS1; forms large aggregates; decreases protein-arginine deiminase activity;, features a modification of the amino acid from L to H at position 112.
+The protein's natural variant, known as in UHS1; forms large aggregates; decreases protein-arginine deiminase activity;, features a modification of the amino acid from A to V at position 294.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from G to R at position 509.
+The protein's natural variant, known as in UHS1; forms large aggregates; decreases protein-arginine deiminase activity;, features a modification of the amino acid from P to T at position 605.
+The protein's natural variant, known as in PERRYS; mutation carriers either do not develop depression or they do develop it late in the disease course;, features a modification of the amino acid from F to L at position 52.
+The protein's natural variant, known as in HMN7B; reduced affinity for microtubules which has been suggested to impair axonal transport; the effect is identical to that of complete loss of the CAP-Gly domain; decreased interaction with MAPRE1; no effect on its interaction with TBCB;, features a modification of the amino acid from G to S at position 59.
+The protein's natural variant, known as in PERRYS;, features a modification of the amino acid from G to A at position 71.
+The protein's natural variant, known as in PERRYS;, features a modification of the amino acid from G to E at position 71.
+The protein's natural variant, known as in PERRYS; reduced microtubule binding; results in the accumulation of intracytoplasmic inclusions; loss of interaction with CLIP1; significant decrease in motility of dynein-dynactin complex along microtubules;, features a modification of the amino acid from G to R at position 71.
+The protein's natural variant, known as in PERRYS;, features a modification of the amino acid from T to P at position 72.
+The protein's natural variant, known as in PERRYS; diminishes microtubule binding and lead to intracytoplasmic inclusions; significant decrease in motility of dynein-dynactin complex along microtubules; defective in inhibiting microtubule catastrophe in neurons;, features a modification of the amino acid from Q to P at position 74.
+The protein's natural variant, known as in PERRYS; significantly reduced microtubule binding;, features a modification of the amino acid from Y to C at position 78.
+The natural variant of this protein is characterized by an amino acid alteration from A to P at position 163.
+The protein's natural variant, known as no effect of its interaction with TBCB; no loss of localization to microtubules;, features a modification of the amino acid from I to V at position 196.
+The protein's natural variant, known as in ALS; associated with disease susceptibility;, features a modification of the amino acid from M to T at position 571.
+The protein's natural variant, known as found in a patient with hereditary motor and sensory neuropathy; unknown pathological significance;, features a modification of the amino acid from Y to F at position 670.
+The protein's natural variant, known as in ALS; associated with disease susceptibility;, features a modification of the amino acid from R to W at position 785.
+The protein's natural variant, known as in ALS; associated with disease susceptibility;, features a modification of the amino acid from R to K at position 1101.
+The protein's natural variant, known as in ALS; unknown pathological significance;, features a modification of the amino acid from T to I at position 1249.
+The natural variant of this protein is characterized by an amino acid alteration from N to P at position 8.
+The natural variant of this protein is characterized by an amino acid alteration from H to Y at position 9.
+The natural variant of this protein is characterized by an amino acid alteration from W to G at position 20.
+The protein's natural variant, known as in SNDC;, features a modification of the amino acid from W to L at position 424.
+The protein's natural variant, known as in SNDC;, features a modification of the amino acid from A to S at position 582.
+The protein's natural variant, known as in SNDC;, features a modification of the amino acid from S to L at position 583.
+The protein's natural variant, known as in mutant PRSA1; alters the binding of divalent cations, especially magnesium. Little alteration in the affinity for ribose 5-phosphate and 27-fold decrease of the affinity for ATP. Absence of inhibition by AMP, features a modification of the amino acid from D to A at position 129.
+The protein's natural variant, known as in MDDGC15; unknown pathological significance;, features a modification of the amino acid from L to P at position 14.
+The protein's natural variant, known as in MDDGB15; unknown pathological significance;, features a modification of the amino acid from P to A at position 42.
+The protein's natural variant, known as in MDDGC15; when transfected into DPM3-deficient cells, only slightly restores dolichol-phosphate mannose synthase activity contrary to wild-type DPM3; reduced interaction with DPM1;, features a modification of the amino acid from L to S at position 85.
+The natural variant of this protein is characterized by an amino acid alteration from D to G at position 15.
+The protein's natural variant, known as associated with increased colorectal cancer risk;, features a modification of the amino acid from A to T at position 181.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from N to D at position 23.
+The protein's natural variant, known as in some childhood acute lymphoblastic leukemia patients; uncertain pathological significance; rare variant;, features a modification of the amino acid from S to L at position 93.
+The protein's natural variant, known as in some childhood acute lymphoblastic leukemia patients; uncertain pathological significance; rare variant;, features a modification of the amino acid from D to N at position 95.
+The protein's natural variant, known as in BC;, features a modification of the amino acid from L to F at position 150.
+The protein's natural variant, known as in some childhood acute lymphoblastic leukemia patients; uncertain pathological significance; rare variant; associated with aplastic anemia at homozygosity;, features a modification of the amino acid from I to V at position 171.
+The protein's natural variant, known as found in a renal cell carcinoma sample; somatic mutation, features a modification of the amino acid from Y to H at position 679.
+The protein's natural variant, known as in protamine-Z2, features a modification of the amino acid from V to A at position 22.
+The protein's natural variant, known as in MCOPS16; unknown pathological significance, features a modification of the amino acid from Y to H at position 160.
+The protein's natural variant, known as in MCOPS16; unknown pathological significance, features a modification of the amino acid from R to Q at position 187.
+The protein's natural variant, known as in MCOPS16; unknown pathological significance, features a modification of the amino acid from R to Q at position 188.
+The protein's natural variant, known as in MCOPS16; does not affect nuclear localization; reduces DNA binding activity;, features a modification of the amino acid from R to Q at position 192.
+The protein's natural variant, known as in strain: N282; confers erythromycin resistance. Ribosomes bind erythromycin poorly and have reduced peptidyltransferase activity. 50S subunits assemble normally, even in the presence of drug, but assembly is cold-sensitive at 20 degrees Celsius, features a modification of the amino acid from K to E at position 63.
+The protein's natural variant, known as in NPHP9; a full-length mouse NEK8 construct containing the mutation shows a defect in ciliary localization with no apparent effect on ciliation, mitosis or centriole number;, features a modification of the amino acid from L to F at position 330.
+The protein's natural variant, known as in NPHP9; a full-length mouse NEK8 construct containing the mutation shows a defect in ciliary localization with no apparent effect on ciliation, mitosis or centriole number;, features a modification of the amino acid from H to Y at position 425.
+The protein's natural variant, known as in NPHP9; a full-length mouse NEK8 construct containing the mutation shows a defect in ciliary localization with no apparent effect on ciliation, mitosis or centriole number;, features a modification of the amino acid from A to P at position 497.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from A to V at position 85.
+The protein's natural variant, known as in HBSL;, features a modification of the amino acid from M to L at position 256.
+The protein's natural variant, known as in HBSL;, features a modification of the amino acid from A to V at position 274.
+The protein's natural variant, known as in HBSL;, features a modification of the amino acid from D to Y at position 367.
+The protein's natural variant, known as in HBSL;, features a modification of the amino acid from R to H at position 460.
+The protein's natural variant, known as in HBSL;, features a modification of the amino acid from P to L at position 464.
+The protein's natural variant, known as in HBSL;, features a modification of the amino acid from R to C at position 487.
+The protein's natural variant, known as in HBSL;, features a modification of the amino acid from R to C at position 494.
+The protein's natural variant, known as in HBSL;, features a modification of the amino acid from R to G at position 494.
+The protein's natural variant, known as in CDGF1; drastic decrease of protein level in patient's fibroblasts and complete loss of total core fucosylated N-glycans in serum and fibroblasts compared to controls, features a modification of the amino acid from R to G at position 337.
+The protein's natural variant, known as in CYP82E4v2, features a modification of the amino acid from VF to LS at position 3.
+The protein's natural variant, known as in CYP82E4v11, features a modification of the amino acid from R to Q at position 61.
+The protein's natural variant, known as in CYP82E4v4, features a modification of the amino acid from F to L at position 74.
+The protein's natural variant, known as in CYP82E4v11, features a modification of the amino acid from N to D at position 99.
+The protein's natural variant, known as in CYP82E4v7, features a modification of the amino acid from I to V at position 191.
+The protein's natural variant, known as in CYP82E4v7, features a modification of the amino acid from K to E at position 217.
+The protein's natural variant, known as in CYP82E4v10, features a modification of the amino acid from A to S at position 231.
+The protein's natural variant, known as in CYP82E4v8, features a modification of the amino acid from T to A at position 252.
+The protein's natural variant, known as in CYP82E4v12, features a modification of the amino acid from K to E at position 309.
+The protein's natural variant, known as in CYP82E4v11, features a modification of the amino acid from S to G at position 314.
+The protein's natural variant, known as in CYP82E4v10, features a modification of the amino acid from I to M at position 335.
+The protein's natural variant, known as in CYP82E4v12, features a modification of the amino acid from G to C at position 353.
+The protein's natural variant, known as in CYP82E4v8, features a modification of the amino acid from A to V at position 410.
+The protein's natural variant, known as in CYP82E4v5, features a modification of the amino acid from M to V at position 413.
+The protein's natural variant, known as in CYP82E4v6, features a modification of the amino acid from Q to L at position 416.
+The protein's natural variant, known as in CYP82E4v6, features a modification of the amino acid from S to P at position 423.
+The protein's natural variant, known as in CYP82E4v10, features a modification of the amino acid from D to G at position 439.
+The protein's natural variant, known as in CYP82E4v12, features a modification of the amino acid from S to P at position 452.
+The protein's natural variant, known as in CYP82E4v11, features a modification of the amino acid from M to I at position 471.
+The protein's natural variant, known as in CYP82E4v3, features a modification of the amino acid from L to S at position 488.
+The protein's natural variant, known as in SRTD16;, features a modification of the amino acid from A to T at position 199.
+The protein's natural variant, known as in ZKS; results in decreased secretion of WNT3A and WNT5A; decreased activation of WNT signaling, features a modification of the amino acid from Y to C at position 392.
+The protein's natural variant, known as in ZKS; results in decreased secretion of WNT3A and WNT5A; decreased activation of WNT signaling;, features a modification of the amino acid from Y to C at position 478.
+The protein's natural variant, known as in ZKS; results in decreased secretion of WNT3A and WNT5A; decreased activation of WNT signaling, features a modification of the amino acid from I to T at position 531.
+The protein's natural variant, known as in ZKS; results in decreased secretion of WNT3A and WNT5A; decreased activation of WNT signaling, features a modification of the amino acid from R to C at position 536.
+The protein's natural variant, known as rare variant found in Diamond-Blackfan anemia patients; unknown pathological significance;, features a modification of the amino acid from I to T at position 99.
+The protein's natural variant, known as in EEMS;, features a modification of the amino acid from N to I at position 322.
+The protein's natural variant, known as in HJMD;, features a modification of the amino acid from R to H at position 503.
+The protein's natural variant, known as in plasmid pYVa127/90, features a modification of the amino acid from T to A at position 25.
+The protein's natural variant, known as in BRKS1;, features a modification of the amino acid from E to K at position 113.
+The protein's natural variant, known as in BRKS1;, features a modification of the amino acid from R to Q at position 115.
+The protein's natural variant, known as in BRKS1;, features a modification of the amino acid from P to L at position 136.
+The protein's natural variant, known as in CODASS, features a modification of the amino acid from E to A at position 476.
+The protein's natural variant, known as in CODASS;, features a modification of the amino acid from S to Y at position 631.
+The protein's natural variant, known as in CODASS;, features a modification of the amino acid from A to V at position 670.
+The protein's natural variant, known as in CODASS;, features a modification of the amino acid from R to C at position 672.
+The protein's natural variant, known as in CODASS;, features a modification of the amino acid from P to S at position 676.
+The protein's natural variant, known as in CODASS;, features a modification of the amino acid from R to H at position 679.
+The protein's natural variant, known as in CODASS;, features a modification of the amino acid from R to G at position 721.
+The protein's natural variant, known as in CODASS;, features a modification of the amino acid from A to V at position 724.
+The protein's natural variant, known as in CODASS, features a modification of the amino acid from P to S at position 749.
+The protein's natural variant, known as in CODASS;, features a modification of the amino acid from G to E at position 767.
+The protein's natural variant, known as resistance to EMB, features a modification of the amino acid from A to T at position 201.
+The protein's natural variant, known as resistance to EMB, features a modification of the amino acid from G to S at position 321.
+The protein's natural variant, known as resistance to EMB, features a modification of the amino acid from G to D at position 350.
+The protein's natural variant, known as resistance to EMB, features a modification of the amino acid from A to V at position 462.
+The protein's natural variant, known as resistance to EMB, features a modification of the amino acid from D to A at position 833.
+The protein's natural variant, known as resistance to EMB, features a modification of the amino acid from P to S at position 913.
+The protein's natural variant, known as in allele Ald3a1c, features a modification of the amino acid from I to N at position 154.
+The protein's natural variant, known as in allele Ald3a1c, features a modification of the amino acid from H to R at position 305.
+The protein's natural variant, known as in allele Ald3a1c, features a modification of the amino acid from I to V at position 352.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from A to V at position 43.
+The protein's natural variant, known as in KLEFS1, features a modification of the amino acid from C to Y at position 1075.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from Y to F at position 1173.
+The protein's natural variant, known as in strain: Port-Louis, features a modification of the amino acid from S to N at position 27.
+The protein's natural variant, known as in strain: 1631, features a modification of the amino acid from I to V at position 72.
+The protein's natural variant, known as in MMAB;, features a modification of the amino acid from I to T at position 96.
+The protein's natural variant, known as in MMAB;, features a modification of the amino acid from A to T at position 135.
+The protein's natural variant, known as in MMAB;, features a modification of the amino acid from R to W at position 186.
+The protein's natural variant, known as in MMAB;, features a modification of the amino acid from R to W at position 191.
+The protein's natural variant, known as in MMAB;, features a modification of the amino acid from E to K at position 193.
+The protein's natural variant, known as in T-haplotype, features a modification of the amino acid from Q to E at position 17.
+The protein's natural variant, known as in T-haplotype, features a modification of the amino acid from R to S at position 23.
+The protein's natural variant, known as in T-haplotype, features a modification of the amino acid from K to R at position 26.
+The protein's natural variant, known as in T-haplotype, features a modification of the amino acid from ERL to P at position 43.
+The protein's natural variant, known as in T-haplotype, features a modification of the amino acid from H to R at position 48.
+The protein's natural variant, known as in T-haplotype, features a modification of the amino acid from Y to F at position 52.
+The protein's natural variant, known as in T-haplotype, features a modification of the amino acid from S to A at position 60.
+The protein's natural variant, known as requires 2 nucleotide substitutions; in T-haplotype, features a modification of the amino acid from V to S at position 64.
+The protein's natural variant, known as in T-haplotype, features a modification of the amino acid from L to S at position 93.
+The protein's natural variant, known as in T-haplotype, features a modification of the amino acid from G to R at position 125.
+The protein's natural variant, known as in T-haplotype, features a modification of the amino acid from A to G at position 153.
+The protein's natural variant, known as in EDM3;, features a modification of the amino acid from G to D at position 35.
+The protein's natural variant, known as associated with an increased risk for intervertebral disk disease;, features a modification of the amino acid from R to W at position 103.
+The protein's natural variant, known as in HELIX; decreased function in regulation of paracellular ion transport as shown by reduced sodium permeability of cell layers expressing the mutant; affects self-interaction by inhibiting homodimerization in trans and promoting homodimerization in cis; no effect on localization to plasma membrane;, features a modification of the amino acid from N to K at position 48.
+The protein's natural variant, known as in HELIX; strongly reduced localization at the plasma membrane;, features a modification of the amino acid from S to L at position 131.
+The protein's natural variant, known as in CDG2N;, features a modification of the amino acid from V to M at position 33.
+The protein's natural variant, known as in CDG2N; loss of manganese ion transmembrane transport; loss of localization to the plasma membrane; retained in the endoplasmic reticulum; no effect on protein abundance;, features a modification of the amino acid from G to R at position 38.
+The protein's natural variant, known as probable disease-associated variant found in patients with Leigh-like syndrome; no effect on protein abundance; loss of localization to the plasma membrane; retained in the endoplasmic reticulum; loss of manganese ion transmembrane transport;, features a modification of the amino acid from C to S at position 113.
+The protein's natural variant, known as in CDG2N;, features a modification of the amino acid from G to C at position 204.
+The protein's natural variant, known as in CDG2N;, features a modification of the amino acid from S to T at position 335.
+The protein's natural variant, known as in CDG2N; no detectable serum or urinary manganese levels in an affected individual who also carries R-38 mutation;, features a modification of the amino acid from I to N at position 340.
+The protein's natural variant, known as no effect on protein abundance; decreased cadmium ion transmembrane transport; increased resistance to cadmium cytotoxicity; associated with decreased activity of manganese-dependent enzymes;, features a modification of the amino acid from A to T at position 391.
+The protein's natural variant, known as in SIDS;, features a modification of the amino acid from V to L at position 14.
+The protein's natural variant, known as in HYPCK, RMD2 and MPDT;, features a modification of the amino acid from R to Q at position 27.
+The protein's natural variant, known as in RMD2;, features a modification of the amino acid from D to E at position 28.
+The protein's natural variant, known as in HYPCK;, features a modification of the amino acid from P to L at position 29.
+The protein's natural variant, known as in RMD2 and MPDT;, features a modification of the amino acid from N to K at position 33.
+The protein's natural variant, known as in RMD2;, features a modification of the amino acid from V to E at position 44.
+The protein's natural variant, known as in RMD2; decreased surface expression of the CAV3 protein;, features a modification of the amino acid from A to T at position 46.
+The protein's natural variant, known as in RMD2;, features a modification of the amino acid from A to V at position 46.
+The protein's natural variant, known as in RMD2;, features a modification of the amino acid from S to G at position 53.
+The protein's natural variant, known as in HYPCK;, features a modification of the amino acid from V to M at position 57.
+The protein's natural variant, known as in a patient with mild proximal myopathy;, features a modification of the amino acid from S to R at position 61.
+The protein's natural variant, known as in RMD2;, features a modification of the amino acid from T to P at position 64.
+The protein's natural variant, known as in CMH;, features a modification of the amino acid from T to S at position 64.
+The protein's natural variant, known as in LQT9 and SIDS;, features a modification of the amino acid from T to M at position 78.
+The protein's natural variant, known as in LQT9 and SIDS;, features a modification of the amino acid from L to R at position 79.
+The protein's natural variant, known as in LQT9;, features a modification of the amino acid from A to T at position 85.
+The protein's natural variant, known as in RMD2;, features a modification of the amino acid from L to P at position 87.
+The protein's natural variant, known as in RMD2;, features a modification of the amino acid from A to T at position 93.
+The protein's natural variant, known as in LQT9; increase in late sodium current;, features a modification of the amino acid from F to C at position 97.
+The protein's natural variant, known as in RMD2;, features a modification of the amino acid from P to L at position 105.
+The protein's natural variant, known as in LQT9; increase in late sodium current;, features a modification of the amino acid from S to R at position 141.
+The protein's natural variant, known as in FANCA; benign variant;, features a modification of the amino acid from N to K at position 8.
+The protein's natural variant, known as in FANCA; benign variant;, features a modification of the amino acid from A to V at position 181.
+The protein's natural variant, known as in FANCA, features a modification of the amino acid from L to R at position 210.
+The protein's natural variant, known as in FANCA, features a modification of the amino acid from L to F at position 244.
+The protein's natural variant, known as in FANCA; benign variant;, features a modification of the amino acid from D to G at position 252.
+The protein's natural variant, known as in FANCA;, features a modification of the amino acid from R to C at position 435.
+The protein's natural variant, known as in FANCA;, features a modification of the amino acid from H to R at position 492.
+The protein's natural variant, known as in FANCA;, features a modification of the amino acid from D to N at position 598.
+The protein's natural variant, known as in FANCA;, features a modification of the amino acid from L to P at position 660.
+The protein's natural variant, known as in FANCA, features a modification of the amino acid from L to P at position 817.
+The protein's natural variant, known as in FANCA;, features a modification of the amino acid from Y to D at position 843.
+The protein's natural variant, known as in FANCA;, features a modification of the amino acid from L to P at position 845.
+The protein's natural variant, known as in FANCA;, features a modification of the amino acid from S to R at position 858.
+The protein's natural variant, known as in FANCA;, features a modification of the amino acid from Q to P at position 869.
+The protein's natural variant, known as in FANCA;, features a modification of the amino acid from R to L at position 1055.
+The protein's natural variant, known as in FANCA;, features a modification of the amino acid from R to W at position 1055.
+The protein's natural variant, known as in FANCA, features a modification of the amino acid from L to P at position 1082.
+The protein's natural variant, known as in FANCA;, features a modification of the amino acid from S to F at position 1088.
+The protein's natural variant, known as in FANCA; loss of function, features a modification of the amino acid from H to P at position 1110.
+The protein's natural variant, known as in FANCA;, features a modification of the amino acid from R to G at position 1117.
+The protein's natural variant, known as in FANCA;, features a modification of the amino acid from Q to E at position 1128.
+The protein's natural variant, known as in FANCA;, features a modification of the amino acid from T to A at position 1131.
+The protein's natural variant, known as in FANCA;, features a modification of the amino acid from L to P at position 1249.
+The protein's natural variant, known as in FANCA;, features a modification of the amino acid from F to L at position 1262.
+The protein's natural variant, known as in FANCA;, features a modification of the amino acid from W to R at position 1302.
+The protein's natural variant, known as in FANCA;, features a modification of the amino acid from P to L at position 1324.
+The protein's natural variant, known as in FANCA; likely benign variant;, features a modification of the amino acid from A to T at position 1346.
+The protein's natural variant, known as in FANCA;, features a modification of the amino acid from D to Y at position 1359.
+The protein's natural variant, known as in FANCA;, features a modification of the amino acid from M to I at position 1360.
+The protein's natural variant, known as in FANCA;, features a modification of the amino acid from R to H at position 1400.
+The protein's natural variant, known as in FANCA;, features a modification of the amino acid from H to D at position 1417.
+The natural variant of this protein is characterized by an amino acid alteration from F to L at position 58.
+The natural variant of this protein is characterized by an amino acid alteration from F to S at position 180.
+The natural variant of this protein is characterized by an amino acid alteration from S to N at position 323.
+The natural variant of this protein is characterized by an amino acid alteration from V to A at position 413.
+The natural variant of this protein is characterized by an amino acid alteration from I to T at position 476.
+The protein's natural variant, known as in Pinot Meunier L1 layer; induces the formation of influorescence instead of grapewine tendrils, features a modification of the amino acid from L to H at position 38.
+The protein's natural variant, known as in strain: IFO 16449, features a modification of the amino acid from KQ to TK at position 165.
+The protein's natural variant, known as in sxy-Long; causes a 100-fold to 1000-fold increase in spontaneous natural competence, features a modification of the amino acid from V to I at position 19.
+The protein's natural variant, known as in an ovarian mucinous carcinoma sample; somatic mutation;, features a modification of the amino acid from V to I at position 243.
+The protein's natural variant, known as in strain: ATCC 30957 / WB, features a modification of the amino acid from A to P at position 214.
+The protein's natural variant, known as in strain: ATCC 30957 / WB, features a modification of the amino acid from N to K at position 268.
+The protein's natural variant, known as in strain: MHN1, features a modification of the amino acid from R to I at position 3.
+The protein's natural variant, known as in strain: MHN1, features a modification of the amino acid from I to L at position 14.
+The protein's natural variant, known as in strain: MHN1, features a modification of the amino acid from T to A at position 21.
+The protein's natural variant, known as in strain: MHN1 and Q980R, features a modification of the amino acid from I to V at position 36.
+The protein's natural variant, known as in strain: MHN1, features a modification of the amino acid from P to S at position 58.
+The protein's natural variant, known as in strain: MHN1 and Q980R, features a modification of the amino acid from A to P at position 108.
+The protein's natural variant, known as in strain: Q980R, features a modification of the amino acid from L to V at position 152.
+The protein's natural variant, known as in strain: MHN1, features a modification of the amino acid from N to K at position 262.
+The protein's natural variant, known as in strain: Q980R, features a modification of the amino acid from A to V at position 319.
+The protein's natural variant, known as in strain: MHN1, features a modification of the amino acid from T to K at position 362.
+The protein's natural variant, known as in PDE; loss of alpha-AASA dehydrogenase activity;, features a modification of the amino acid from A to V at position 199.
+The protein's natural variant, known as in PDE, features a modification of the amino acid from G to V at position 202.
+The protein's natural variant, known as in PDE, features a modification of the amino acid from G to E at position 291.
+The protein's natural variant, known as in PDE;, features a modification of the amino acid from N to I at position 301.
+The protein's natural variant, known as in PDE;, features a modification of the amino acid from R to Q at position 335.
+The protein's natural variant, known as in PDE, features a modification of the amino acid from V to G at position 395.
+The protein's natural variant, known as in PDE; loss of alpha-AASA dehydrogenase activity;, features a modification of the amino acid from E to Q at position 427.
+The protein's natural variant, known as in PDE, features a modification of the amino acid from S to N at position 458.
+The protein's natural variant, known as associated with susceptibility to lung cancer;, features a modification of the amino acid from D to N at position 398.
+The protein's natural variant, known as in strain: Isolate CD11, features a modification of the amino acid from I to T at position 10.
+The protein's natural variant, known as in strain: Isolate CD11, features a modification of the amino acid from T to M at position 17.
+The protein's natural variant, known as in strain: Isolate CD11, features a modification of the amino acid from A to T at position 158.
+The protein's natural variant, known as in strain: Isolate CD11, features a modification of the amino acid from A to V at position 229.
+The protein's natural variant, known as in strain: Isolate CD11, features a modification of the amino acid from I to T at position 238.
+The protein's natural variant, known as in strain: Isolate CD11, features a modification of the amino acid from T to S at position 246.
+The protein's natural variant, known as in strain: Isolate CD11, features a modification of the amino acid from V to A at position 353.
+The protein's natural variant, known as in protamine-Y1, features a modification of the amino acid from Q to E at position 6.
+The protein's natural variant, known as in DEE97; unknown pathological significance; mislocalized to the cytoplasm, features a modification of the amino acid from R to G at position 493.
+The protein's natural variant, known as in DEE97; mislocalized to the cytoplasm, features a modification of the amino acid from P to S at position 507.
+The protein's natural variant, known as in strain: various strains, features a modification of the amino acid from E to G at position 135.
+The protein's natural variant, known as in strain: various strains, features a modification of the amino acid from A to S at position 224.
+The protein's natural variant, known as in MRXS35; increased the formation of actively translating ribosomes when expressed in a yeast heterologous system, features a modification of the amino acid from A to V at position 64.
+The protein's natural variant, known as in MRXS35; loss of function; fails to rescue embryonic brain development when expressed in a zebrafish heterologous system;, features a modification of the amino acid from K to E at position 78.
+The protein's natural variant, known as in MRXS35; unknown pathological significance;, features a modification of the amino acid from G to S at position 161.
+The protein's natural variant, known as rescues embryonic brain development when expressed in a zebrafish heterologous system;, features a modification of the amino acid from S to N at position 202.
+The protein's natural variant, known as in AUTSX5; associated with disease susceptibility; no effect on function; rescues embryonic brain development when expressed in a zebrafish heterologous system;, features a modification of the amino acid from L to M at position 206.
+The protein's natural variant, known as in AUTSX5; associated with disease susceptibility; no effect on function; rescues embryonic brain development when expressed in a zebrafish heterologous system;, features a modification of the amino acid from H to Q at position 213.
+The protein's natural variant, known as found as homozygous mutation in a patient with autosomal recessive cutis laxa also carrying a mutation in FBLN5; unknown pathological significance;, features a modification of the amino acid from P to S at position 211.
+The protein's natural variant, known as in CILD14; unknown pathological significance;, features a modification of the amino acid from T to I at position 594.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from P to S at position 1060.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from S to R at position 1191.
+The protein's natural variant, known as in GSD3; deficient in ability to bind glycogen; unstable due to enhanced ubiquitination; forms aggresomes upon proteasome impairment;, features a modification of the amino acid from G to R at position 1448.
+The protein's natural variant, known as in SCA14, features a modification of the amino acid from G to R at position 63.
+The protein's natural variant, known as in SCA14;, features a modification of the amino acid from G to V at position 63.
+The protein's natural variant, known as in SCA14;, features a modification of the amino acid from H to Y at position 101.
+The protein's natural variant, known as in SCA14;, features a modification of the amino acid from S to P at position 119.
+The protein's natural variant, known as in SCA14;, features a modification of the amino acid from G to D at position 128.
+The natural variant of this protein is characterized by an amino acid alteration from R to C at position 141.
+The natural variant of this protein is characterized by an amino acid alteration from H to Q at position 415.
+The natural variant of this protein is characterized by an amino acid alteration from A to D at position 523.
+The protein's natural variant, known as found in a patient with spastic paraplegia; unknown pathological significance;, features a modification of the amino acid from V to M at position 5.
+The protein's natural variant, known as in ILLD; when assayed in yeast, induces a slight growth retardation and reduction in methionine incorporation; may interfere with efficient substrate binding;, features a modification of the amino acid from Y to C at position 344.
+The protein's natural variant, known as in ILLD;, features a modification of the amino acid from F to L at position 370.
+The protein's natural variant, known as in ILLD; may act as a disease modifier aggravating the phenotype; found in patients that carried additional mutations C-344 and/or L-567; when assayed in yeast, does not exhibit any phenotype; when assayed in yeast in association with L-567, increases L-567-induced growth retardation and reduction in methionine incorporation;, features a modification of the amino acid from A to T at position 393.
+The protein's natural variant, known as in TTD9; unknown pathological significance; homozygous patient cells show decreased methionyl-tRNA aminoacylation; decreased protein abundance in homozygous patient cells;, features a modification of the amino acid from V to M at position 401.
+The protein's natural variant, known as in ILLD;, features a modification of the amino acid from I to T at position 523.
+The protein's natural variant, known as in ILLD; when assayed in yeast, reduces methionine incorporation; when assayed in yeast in association with T-393, induces growth retardation and strong reduction in methionine incorporation; may interfere with efficient substrate binding;, features a modification of the amino acid from S to L at position 567.
+The protein's natural variant, known as in ILLD; when assayed in yeast, induces a slight growth retardation and reduction in methionine incorporation; may interfere with efficient substrate binding;, features a modification of the amino acid from D to V at position 605.
+The protein's natural variant, known as in CMT2U; loss of function mutation;, features a modification of the amino acid from R to C at position 618.
+The protein's natural variant, known as found in a patient with spastic paraplegia; unknown pathological significance;, features a modification of the amino acid from R to W at position 702.
+The protein's natural variant, known as in CMT2U;, features a modification of the amino acid from P to T at position 800.
+The protein's natural variant, known as in allele FCGR3B*01;, features a modification of the amino acid from S to R at position 36.
+The protein's natural variant, known as in allele FCGR3B*01;, features a modification of the amino acid from S to N at position 65.
+The protein's natural variant, known as in allele SH;, features a modification of the amino acid from A to D at position 78.
+The protein's natural variant, known as in allele FCGR3B*01;, features a modification of the amino acid from N to D at position 82.
+The protein's natural variant, known as in allele FCGR3B*01;, features a modification of the amino acid from I to V at position 106.
+The natural variant of this protein is characterized by an amino acid alteration from A to AA at position 159.
+The natural variant of this protein is characterized by an amino acid alteration from A to AAA at position 159.
+The natural variant of this protein is characterized by an amino acid alteration from A to AAAA at position 159.
+The natural variant of this protein is characterized by an amino acid alteration from A to AAAAA at position 159.
+The natural variant of this protein is characterized by an amino acid alteration from A to AAAAAA at position 159.
+The natural variant of this protein is characterized by an amino acid alteration from A to AAAAAAAA at position 159.
+The protein's natural variant, known as in chesnut color, features a modification of the amino acid from S to F at position 83.
+The natural variant of this protein is characterized by an amino acid alteration from S to T at position 202.
+The protein's natural variant, known as in one EMPD primary tumor; somatic mutation, features a modification of the amino acid from Y to H at position 23.
+The protein's natural variant, known as in CMT1C;, features a modification of the amino acid from T to M at position 49.
+The protein's natural variant, known as in CMT1C; does not abolish interaction with NEDD4 and TSG101;, features a modification of the amino acid from G to S at position 112.
+The protein's natural variant, known as in CMT1C; does not abolish interaction with NEDD4 and TSG101;, features a modification of the amino acid from T to N at position 115.
+The protein's natural variant, known as in CMT1C; decreases protein stability and association with early endosome membranes; impaired function in targeting endocytosed proteins for lysosomal degradation; does not abolish interaction with NEDD4 and TSG101;, features a modification of the amino acid from W to G at position 116.
+The protein's natural variant, known as in CMT1C;, features a modification of the amino acid from L to V at position 122.
+The protein's natural variant, known as in strain: NTHi 2019, features a modification of the amino acid from A to S at position 29.
+The protein's natural variant, known as in strain: NTHi 7502, features a modification of the amino acid from I to M at position 133.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from Q to H at position 79.
+The protein's natural variant, known as de novo variant found in a patient with childhood apraxia of speech; unknown pathological significance;, features a modification of the amino acid from I to V at position 138.
+The protein's natural variant, known as in RP27; decreases phosphorylation; no effect on subcellular localization; increased transcriptional coactivator activity, features a modification of the amino acid from S to L at position 50.
+The protein's natural variant, known as in RP27; decreases phosphorylation; no effect on subcellular localization; increased transcriptional coactivator activity, features a modification of the amino acid from S to P at position 50.
+The protein's natural variant, known as in RP27; decreases phosphorylation; no effect on subcellular localization; increased transactivational activity; increased transcriptional coactivator activity;, features a modification of the amino acid from S to T at position 50.
+The protein's natural variant, known as in RP27; decreases phosphorylation; no effect on subcellular localization; increased transcriptional coactivator activity, features a modification of the amino acid from P to L at position 51.
+The protein's natural variant, known as in RP27; decreases phosphorylation; no effect on subcellular localization; increased transcriptional coactivator activity;, features a modification of the amino acid from P to S at position 51.
+The protein's natural variant, known as in RP27; autosomal dominant; decreases phosphorylation; no effect on subcellular localization; increased transcriptional coactivator activity, features a modification of the amino acid from P to T at position 51.
+The protein's natural variant, known as in RP27; no effect on phosphorylation; no effect on subcellular localization; no effect on transcriptional coactivator activity;, features a modification of the amino acid from P to S at position 67.
+The protein's natural variant, known as in RDCP; unknown pathological significance; alters phosphorylation; no effect on subcellular localization; no effect on transcriptional coactivator activity;, features a modification of the amino acid from A to V at position 76.
+The protein's natural variant, known as in RP27; increased transactivational activity;, features a modification of the amino acid from M to T at position 96.
+The protein's natural variant, known as in RP27; unknown pathological significance; alters phosphorylation; no effect on subcellular localization; no effect on transcriptional coactivator activity;, features a modification of the amino acid from G to E at position 122.
+The protein's natural variant, known as found in a patient with atypical retinitis pigmentosa and a patient with cone dysfunction; unknown pathological significance; no effect on phosphorylation; no effect on subcellular localization;, features a modification of the amino acid from H to Q at position 125.
+The protein's natural variant, known as in RDCP; alters phosphorylation; no effect on subcellular localization; loss of transcriptional coactivator activity;, features a modification of the amino acid from L to P at position 160.
+The protein's natural variant, known as in RP27;, features a modification of the amino acid from R to S at position 170.
+The protein's natural variant, known as in strain: NRRL 28065, features a modification of the amino acid from N to D at position 279.
+The protein's natural variant, known as in HH20; rare variant associated with susceptibility to disease; some patients have a second mutation in another HH-associated gene including FGFR1, HS6ST1 and FLRT3; the mutant has reduced ability to activate FGFR1;, features a modification of the amino acid from I to T at position 108.
+The protein's natural variant, known as in HH20; the mutant has reduced ability to activate FGFR1;, features a modification of the amino acid from R to H at position 177.
+The protein's natural variant, known as in HH20;, features a modification of the amino acid from N to S at position 187.
+The protein's natural variant, known as in FPVEPD; may affect microtubules stability;, features a modification of the amino acid from F to S at position 394.
+The natural variant of this protein is characterized by an amino acid alteration from S to N at position 22.
+The protein's natural variant, known as no effect on urate transport activity;, features a modification of the amino acid from G to R at position 25.
+The protein's natural variant, known as in RHUC2; reduced urate transport activity; decreased protein expression; decreased urate uptake; no effect on glucose transport;, features a modification of the amino acid from L to R at position 75.
+The protein's natural variant, known as in RHUC2; markedly reduced urate transport activity; decreased protein expression; decreased urate uptake; no effect on glucose transport;, features a modification of the amino acid from T to M at position 125.
+The protein's natural variant, known as no effect on urate transport activity;, features a modification of the amino acid from V to M at position 169.
+The protein's natural variant, known as in RHUC2; unknown pathological significance; according to PubMed:21810765 the variant results in markedly reduced urate uptake, however according to PubMed:29967582 urate transport activity is not affected; no effect on Vmax; no effect on Km for urate; decreased protein expression; no effect on glucose transport;, features a modification of the amino acid from R to C at position 171.
+The protein's natural variant, known as in RHUC2; markedly reduced urate transport activity; decreased Vmax; decreased urate uptake; no effect on protein expression; no effect on glucose transport;, features a modification of the amino acid from R to C at position 198.
+The protein's natural variant, known as in RHUC2; decreased protein expression; decreased urate uptake; no effect on glucose transport;, features a modification of the amino acid from G to R at position 216.
+The protein's natural variant, known as no effect on urate transport activity;, features a modification of the amino acid from T to M at position 275.
+The protein's natural variant, known as no effect on urate transport activity;, features a modification of the amino acid from D to H at position 281.
+The protein's natural variant, known as no effect on urate transport activity;, features a modification of the amino acid from V to I at position 282.
+The protein's natural variant, known as no effect on urate transport activity; no effect on protein expression; no effect on glucose transport;, features a modification of the amino acid from R to H at position 294.
+The protein's natural variant, known as in RHUC2; decreased urate uptake; increased Km for urate; no effect on protein expression; no effect on glucose transport;, features a modification of the amino acid from N to S at position 333.
+The protein's natural variant, known as no effect on urate transport activity; no effect on urate transport; no effect on protein expression; no effect on glucose;, features a modification of the amino acid from P to L at position 350.
+The protein's natural variant, known as in RHUC2; markedly reduced urate transport activity; decreased Vmax; no effect on protein expression; no effect on glucose transport;, features a modification of the amino acid from R to W at position 380.
+The protein's natural variant, known as in RHUC2; unknown pathological significance; according to PubMed:18701466 the variant results in decreased urate uptake, however according to PubMed:22132964 and PubMed:29967582 urate transport activity is not affected; no effect on Vmax for urate uptake; no effect on affinity for urate; no effect on protein expression; no effect on localization to plasma membrane; no effect on glucose transport;, features a modification of the amino acid from P to R at position 412.
+The protein's natural variant, known as decreased urate transport; decreased protein expression; no effect on glucose, features a modification of the amino acid from V to I at position 531.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from G to S at position 430.
+The protein's natural variant, known as in coagulogen-2, features a modification of the amino acid from T to I at position 102.
+The protein's natural variant, known as in coagulogen-2, features a modification of the amino acid from L to S at position 106.
+The protein's natural variant, known as in strain: s3041 / Serovar V and s3044 /Serovar V, features a modification of the amino acid from I to V at position 28.
+The protein's natural variant, known as in strain: s2995 / Serovar VI and s3057 /Serovar VI, features a modification of the amino acid from G to A at position 75.
+The protein's natural variant, known as high incidence in Japanese depressed subjects;, features a modification of the amino acid from Q to R at position 63.
+The protein's natural variant, known as found in a patient with primary ovarian failure associated with intellectual disability and sensorineural hearing loss; unknown pathological significance; no change in glycosylation pattern;, features a modification of the amino acid from R to H at position 217.
+The protein's natural variant, known as no change in glycosylation pattern;, features a modification of the amino acid from I to V at position 272.
+The protein's natural variant, known as in OOMD7; impaired glycosylation resulting in the absence of GLY2 and the accumulation of GLY1 forms; associated with increased hemi-channel activity;, features a modification of the amino acid from K to E at position 346.
+The protein's natural variant, known as in OOMD7; impaired glycosylation resulting in the absence of GLY2 and the accumulation of GLY1 forms; associated with increased hemichannel activity;, features a modification of the amino acid from C to S at position 347.
+The protein's natural variant, known as found in a renal cell carcinoma sample; somatic mutation;, features a modification of the amino acid from P to T at position 921.
+The protein's natural variant, known as in Smba9, features a modification of the amino acid from R to H at position 62.
+The protein's natural variant, known as in Smba2, features a modification of the amino acid from D to N at position 201.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from L to V at position 22.
+The protein's natural variant, known as in a primary colorectal cancer;, features a modification of the amino acid from E to V at position 186.
+The protein's natural variant, known as in a primary colorectal cancer, features a modification of the amino acid from K to I at position 191.
+The protein's natural variant, known as in a primary colorectal cancer, features a modification of the amino acid from K to N at position 191.
+The protein's natural variant, known as in a primary colorectal cancer, features a modification of the amino acid from YDSE to CDND at position 202.
+The protein's natural variant, known as in a primary colorectal cancer, features a modification of the amino acid from E to D at position 202.
+The protein's natural variant, known as in a primary colorectal cancer;, features a modification of the amino acid from R to K at position 218.
+The protein's natural variant, known as in VSVS; loss of DEAF1-promoter repression; loss of transcriptional activation of EIF4G3; loss of DNA binding; decreased interaction with XRCC6;, features a modification of the amino acid from R to W at position 224.
+The protein's natural variant, known as in VSVS; loss of DEAF1-promoter repression; loss of transcriptional activation of EIF4G3; loss of DNA binding; loss of interaction with XRCC6;, features a modification of the amino acid from I to S at position 228.
+The protein's natural variant, known as in VSVS; loss of DEAF1-promoter repression; gain of transcriptional activation of EIF4G3; a 9-fold reduction in DNA binding;, features a modification of the amino acid from R to S at position 254.
+The protein's natural variant, known as in VSVS; loss of DEAF1-promoter repression; loss of transcriptional activation of EIF4G3; loss of DNA binding; loss of interaction with XRCC6;, features a modification of the amino acid from Q to P at position 264.
+The protein's natural variant, known as in a primary colorectal cancer, features a modification of the amino acid from DRA to GQT at position 352.
+The protein's natural variant, known as in a primary colorectal cancer; requires 2 nucleotide substitutions, features a modification of the amino acid from E to H at position 356.
+The protein's natural variant, known as in a primary colorectal cancer, features a modification of the amino acid from S to N at position 364.
+The protein's natural variant, known as in a primary colorectal cancer, features a modification of the amino acid from Q to H at position 367.
+The protein's natural variant, known as in a primary colorectal cancer, features a modification of the amino acid from V to L at position 370.
+The protein's natural variant, known as in a primary colorectal cancer, features a modification of the amino acid from Y to F at position 397.
+The protein's natural variant, known as in a primary colorectal cancer, features a modification of the amino acid from V to A at position 442.
+The protein's natural variant, known as in a primary colorectal cancer, features a modification of the amino acid from E to K at position 449.
+The protein's natural variant, known as in a primary colorectal cancer, features a modification of the amino acid from RS to GI at position 452.
+The protein's natural variant, known as in a primary colorectal cancer, features a modification of the amino acid from Q to H at position 468.
+The protein's natural variant, known as in a primary colorectal cancer, features a modification of the amino acid from H to L at position 479.
+The protein's natural variant, known as in a primary colorectal cancer, features a modification of the amino acid from E to K at position 498.
+The protein's natural variant, known as in a primary colorectal cancer, features a modification of the amino acid from T to N at position 526.
+The protein's natural variant, known as in a primary colorectal cancer, features a modification of the amino acid from R to L at position 530.
+The protein's natural variant, known as in a primary colorectal cancer, features a modification of the amino acid from QH to HL at position 538.
+The protein's natural variant, known as in a primary colorectal cancer, features a modification of the amino acid from Q to H at position 542.
+The protein's natural variant, known as in a primary colorectal cancer;, features a modification of the amino acid from A to G at position 545.
+The protein's natural variant, known as in a primary colorectal cancer, features a modification of the amino acid from A to V at position 545.
+The protein's natural variant, known as in BRGDA2; unknown pathological significance; decreased enzymatic activity and significant reduction of sodium current when coexpressed with SCN5A in HEK cells;, features a modification of the amino acid from E to K at position 83.
+The protein's natural variant, known as in BRGDA2; unknown pathological significance; significant reduction of sodium current when coexpressed with SCN5A in HEK cells;, features a modification of the amino acid from I to V at position 124.
+The protein's natural variant, known as in BRGDA2; unknown pathological significance; significant reduction of sodium current when coexpressed with SCN5A in HEK cells;, features a modification of the amino acid from R to C at position 273.
+The protein's natural variant, known as in BRGDA2; unknown pathological significance; decreased enzymatic activity; affects SCN5A membrane expression; reduction of sodium current when coexpressed with SCN5A in HEK cells;, features a modification of the amino acid from A to V at position 280.
+The protein's natural variant, known as in a biliary tract tumor;, features a modification of the amino acid from D to E at position 14.
+The protein's natural variant, known as in a biliary tract tumor and a familial melanoma;, features a modification of the amino acid from L to P at position 16.
+The protein's natural variant, known as in CMM2; loss of CDK4 binding, features a modification of the amino acid from A to ATA at position 19.
+The protein's natural variant, known as in a lung tumor and melanoma;, features a modification of the amino acid from A to P at position 20.
+The protein's natural variant, known as in a biliary tract tumor;, features a modification of the amino acid from A to S at position 20.
+The protein's natural variant, known as in a pancreas tumor and a melanoma; loss of CDK4 binding;, features a modification of the amino acid from G to D at position 23.
+The protein's natural variant, known as in CMM2, features a modification of the amino acid from R to C at position 24.
+The protein's natural variant, known as in CMM2;, features a modification of the amino acid from R to P at position 24.
+The protein's natural variant, known as found in a patient with multiple primary melanoma; partial loss of CDK4 binding;, features a modification of the amino acid from R to Q at position 24.
+The protein's natural variant, known as in a biliary tract tumor, features a modification of the amino acid from E to D at position 26.
+The protein's natural variant, known as in CMM2;, features a modification of the amino acid from L to P at position 32.
+The protein's natural variant, known as in a biliary tract tumor, features a modification of the amino acid from E to D at position 33.
+The protein's natural variant, known as in CMM2; also found in a biliary tract tumor and a patient with uveal melanoma; partial loss of CDK4 binding;, features a modification of the amino acid from G to A at position 35.
+The protein's natural variant, known as in CMM2;, features a modification of the amino acid from G to E at position 35.
+The protein's natural variant, known as in CMM2; loss of CDK4 binding;, features a modification of the amino acid from G to V at position 35.
+The protein's natural variant, known as in CMM2; also found in head and neck tumor; somatic mutation, features a modification of the amino acid from P to L at position 48.
+The protein's natural variant, known as in a biliary tract tumor;, features a modification of the amino acid from I to S at position 49.
+The protein's natural variant, known as in CMM2;, features a modification of the amino acid from Q to R at position 50.
+The protein's natural variant, known as in CMM2;, features a modification of the amino acid from M to I at position 53.
+The protein's natural variant, known as in pancreas carcinoma; somatic mutation; partial loss of CDK4 binding;, features a modification of the amino acid from A to V at position 57.
+The protein's natural variant, known as in CMM2;, features a modification of the amino acid from V to G at position 59.
+The protein's natural variant, known as in melanoma; loss of CDK4 binding;, features a modification of the amino acid from A to V at position 60.
+The natural variant of this protein is characterized by an amino acid alteration from EL to DV at position 62.
+The protein's natural variant, known as in CMM2, features a modification of the amino acid from L to P at position 62.
+The protein's natural variant, known as in non-small cell lung carcinoma, features a modification of the amino acid from H to Y at position 66.
+The protein's natural variant, known as in CMM2; partial loss of CDK4 binding;, features a modification of the amino acid from G to R at position 67.
+The protein's natural variant, known as in CMM2; requires 2 nucleotide substitutions;, features a modification of the amino acid from A to L at position 68.
+The protein's natural variant, known as in an esophagus tumor, features a modification of the amino acid from A to T at position 68.
+The protein's natural variant, known as found in some patients with melanoma; partial loss of CDK4 binding;, features a modification of the amino acid from E to G at position 69.
+The protein's natural variant, known as in a bladder tumor, features a modification of the amino acid from E to K at position 69.
+The protein's natural variant, known as in a lung tumor, features a modification of the amino acid from E to V at position 69.
+The protein's natural variant, known as in CMM2, features a modification of the amino acid from N to K at position 71.
+The protein's natural variant, known as in an esophagus tumor, features a modification of the amino acid from C to G at position 72.
+The protein's natural variant, known as in a bladder tumor;, features a modification of the amino acid from D to N at position 74.
+The protein's natural variant, known as in a biliary tract tumor;, features a modification of the amino acid from D to V at position 74.
+The protein's natural variant, known as in CMM2; loss of CDK4 binding;, features a modification of the amino acid from D to Y at position 74.
+The protein's natural variant, known as in CMM2; loss of CDK4 binding, features a modification of the amino acid from T to P at position 77.
+The protein's natural variant, known as in a head and neck tumor, features a modification of the amino acid from R to L at position 80.
+The protein's natural variant, known as in CMM2; loss of CDK4 binding;, features a modification of the amino acid from R to P at position 80.
+The protein's natural variant, known as in some patients with melanoma; impairs the function;, features a modification of the amino acid from P to L at position 81.
+The protein's natural variant, known as in CMM2; loss of CDK4 binding;, features a modification of the amino acid from P to T at position 81.
+The protein's natural variant, known as in a lung tumor, features a modification of the amino acid from H to N at position 83.
+The protein's natural variant, known as in a pancreas tumor; also found in head and neck tumor;, features a modification of the amino acid from H to Y at position 83.
+The protein's natural variant, known as in a bladder tumor, features a modification of the amino acid from D to E at position 84.
+The protein's natural variant, known as in non-small cell lung carcinoma, features a modification of the amino acid from D to H at position 84.
+The protein's natural variant, known as in an esophagus tumor; also found in head and neck tumor; also found in a lung tumor;, features a modification of the amino acid from D to N at position 84.
+The protein's natural variant, known as in CMM2; also found in a lung tumor and a prostate tumor;, features a modification of the amino acid from D to Y at position 84.
+The protein's natural variant, known as in CMM2; impairs the function;, features a modification of the amino acid from R to P at position 87.
+The protein's natural variant, known as in CMM2; partial loss of CDK4 binding;, features a modification of the amino acid from R to W at position 87.
+The protein's natural variant, known as in a biliary tract tumor, features a modification of the amino acid from E to D at position 88.
+The protein's natural variant, known as in CMM2; somatic mutation;, features a modification of the amino acid from G to D at position 89.
+The protein's natural variant, known as in CMM2;, features a modification of the amino acid from G to S at position 89.
+The protein's natural variant, known as in non-small cell lung carcinoma, features a modification of the amino acid from T to A at position 93.
+The protein's natural variant, known as in CMM2;, features a modification of the amino acid from L to Q at position 94.
+The protein's natural variant, known as in non-small cell lung carcinoma, features a modification of the amino acid from V to A at position 95.
+The protein's natural variant, known as in CMM2; loss of CDK4 binding, features a modification of the amino acid from L to R at position 97.
+The protein's natural variant, known as in CMM2, features a modification of the amino acid from H to P at position 98.
+The protein's natural variant, known as in CMM2;, features a modification of the amino acid from H to Q at position 98.
+The protein's natural variant, known as in CMM2; loss of CDK4 binding;, features a modification of the amino acid from R to P at position 99.
+The protein's natural variant, known as in non-small cell lung carcinoma;, features a modification of the amino acid from R to Q at position 99.
+The protein's natural variant, known as in CMM2; requires 2 nucleotide substitutions, features a modification of the amino acid from A to L at position 100.
+The natural variant of this protein is characterized by an amino acid alteration from A to P at position 100.
+The protein's natural variant, known as in CMM2 and FAMMMPC; impairs the function;, features a modification of the amino acid from G to W at position 101.
+The protein's natural variant, known as found in seminoma and medulloblastoma tissues from Li-Fraumeni syndrome patients carrying a mutation in TP53; somatic mutation;, features a modification of the amino acid from A to E at position 102.
+The protein's natural variant, known as in CMM2;, features a modification of the amino acid from R to C at position 107.
+The protein's natural variant, known as in a bladder tumor, features a modification of the amino acid from D to H at position 108.
+The protein's natural variant, known as in a head and neck tumor;, features a modification of the amino acid from D to Y at position 108.
+The protein's natural variant, known as in CMM2, features a modification of the amino acid from R to RR at position 112.
+The protein's natural variant, known as in non-small cell lung carcinoma;, features a modification of the amino acid from P to L at position 114.
+The protein's natural variant, known as found in some patients with melanoma; loss of CDK4 binding;, features a modification of the amino acid from P to S at position 114.
+The protein's natural variant, known as in CMM2; somatic mutation, features a modification of the amino acid from L to M at position 117.
+The protein's natural variant, known as in CMM2;, features a modification of the amino acid from A to T at position 118.
+The protein's natural variant, known as in a biliary tract tumor, features a modification of the amino acid from E to Q at position 119.
+The protein's natural variant, known as in non-small cell lung carcinoma, features a modification of the amino acid from E to A at position 120.
+The protein's natural variant, known as in non-small cell lung carcinoma, features a modification of the amino acid from E to K at position 120.
+The protein's natural variant, known as in CMM2;, features a modification of the amino acid from G to R at position 122.
+The protein's natural variant, known as in a biliary tract tumor;, features a modification of the amino acid from G to S at position 122.
+The protein's natural variant, known as in leukemia;, features a modification of the amino acid from H to Q at position 123.
+The protein's natural variant, known as in an esophagus tumor;, features a modification of the amino acid from R to H at position 124.
+The protein's natural variant, known as in CMM2; impairs the function;, features a modification of the amino acid from V to D at position 126.
+The protein's natural variant, known as in squamous cell carcinoma;, features a modification of the amino acid from A to S at position 127.
+The protein's natural variant, known as in non-small cell lung carcinoma, features a modification of the amino acid from A to P at position 132.
+The protein's natural variant, known as in non-small cell lung carcinoma;, features a modification of the amino acid from A to V at position 134.
+The protein's natural variant, known as in non-small cell lung carcinoma;, features a modification of the amino acid from H to Y at position 142.
+The protein's natural variant, known as in squamous cell carcinoma;, features a modification of the amino acid from R to C at position 144.
+The protein's natural variant, known as in non-small cell lung carcinoma, features a modification of the amino acid from G to V at position 150.
+The protein's natural variant, known as in strain: cv. Cvi-1, features a modification of the amino acid from E to K at position 127.
+The protein's natural variant, known as in strain: cv. Cvi-1, features a modification of the amino acid from T to S at position 178.
+The protein's natural variant, known as in KTGS;, features a modification of the amino acid from G to S at position 515.
+The protein's natural variant, known as in AT3D; type-I, features a modification of the amino acid from Y to S at position 17.
+The protein's natural variant, known as in AT3D; type-I; does not undergo post-translational glycosylation;, features a modification of the amino acid from L to P at position 23.
+The protein's natural variant, known as in Dublin;, features a modification of the amino acid from V to E at position 30.
+The protein's natural variant, known as in AT3D; type-I, features a modification of the amino acid from C to R at position 32.
+The protein's natural variant, known as in AT3D; type-II; Rouen-3; lack of heparin-binding properties;, features a modification of the amino acid from I to N at position 39.
+The protein's natural variant, known as previously Whitechapel;, features a modification of the amino acid from M to T at position 52.
+The protein's natural variant, known as in AT3D, features a modification of the amino acid from C to F at position 53.
+The protein's natural variant, known as in AT3D; type-II; Rouen-4; lack of heparin-binding properties;, features a modification of the amino acid from R to C at position 56.
+The protein's natural variant, known as in AT3D; type-II; lacks heparin-binding ability;, features a modification of the amino acid from P to L at position 73.
+The protein's natural variant, known as in AT3D; Tours/Alger/Amiens/Toyama/Paris-1/Paris-2/Padua-2/Barcelona-2/Kumamoto/Omura/Sasebo; lacks heparin-binding ability;, features a modification of the amino acid from R to C at position 79.
+The protein's natural variant, known as in AT3D; type-II; Rouen-1/Padua-1/Bligny/Budapest-2; lack of heparin-binding properties;, features a modification of the amino acid from R to H at position 79.
+The protein's natural variant, known as in AT3D; type-II; Rouen-2; lack of heparin-binding properties;, features a modification of the amino acid from R to S at position 79.
+The protein's natural variant, known as in AT3D; type-I;, features a modification of the amino acid from R to C at position 89.
+The protein's natural variant, known as in AT3D; type-I; Budapest-6, features a modification of the amino acid from F to L at position 90.
+The protein's natural variant, known as in AT3D; type-I;, features a modification of the amino acid from Y to C at position 95.
+The protein's natural variant, known as in AT3D; type-I, features a modification of the amino acid from Y to S at position 95.
+The protein's natural variant, known as in AT3D; type-I, features a modification of the amino acid from L to P at position 98.
+The protein's natural variant, known as in AT3D; severely decreased antithrombin activity, features a modification of the amino acid from P to S at position 112.
+The protein's natural variant, known as in AT3D; type-I, features a modification of the amino acid from P to T at position 112.
+The protein's natural variant, known as in AT3D; type-I, features a modification of the amino acid from M to K at position 121.
+The protein's natural variant, known as in AT3D, features a modification of the amino acid from G to D at position 125.
+The protein's natural variant, known as in AT3D; type-I;, features a modification of the amino acid from C to R at position 127.
+The protein's natural variant, known as in AT3D; type-II; Budapest-3/Budapest-7;, features a modification of the amino acid from L to F at position 131.
+The protein's natural variant, known as in AT3D; type-II; Southport, features a modification of the amino acid from L to V at position 131.
+The protein's natural variant, known as in AT3D; type I;, features a modification of the amino acid from Q to K at position 133.
+The protein's natural variant, known as in AT3D; Dreux; complete loss af heparin binding;, features a modification of the amino acid from K to E at position 146.
+The protein's natural variant, known as in AT3D; type-II; Nagasaki; defective heparin binding associated with thrombosis;, features a modification of the amino acid from S to P at position 148.
+The protein's natural variant, known as in AT3D; type-II; Vienna;, features a modification of the amino acid from Q to P at position 150.
+The protein's natural variant, known as in AT3D; type-I, features a modification of the amino acid from H to Y at position 152.
+The protein's natural variant, known as in AT3D; type-I, features a modification of the amino acid from L to P at position 158.
+The protein's natural variant, known as in AT3D; type-I, features a modification of the amino acid from C to Y at position 160.
+The protein's natural variant, known as in AT3D; type-II; Geneva;, features a modification of the amino acid from R to Q at position 161.
+The protein's natural variant, known as in AT3D, features a modification of the amino acid from S to P at position 170.
+The protein's natural variant, known as in AT3D; type-I, features a modification of the amino acid from L to H at position 178.
+The protein's natural variant, known as in AT3D; type-I, features a modification of the amino acid from F to L at position 179.
+The protein's natural variant, known as variant of uncertain significance, features a modification of the amino acid from Y to C at position 190.
+The protein's natural variant, known as in AT3D; type-I and -II; Whitechapel;, features a modification of the amino acid from Y to C at position 198.
+The protein's natural variant, known as in AT3D; type-I;, features a modification of the amino acid from Y to H at position 198.
+The protein's natural variant, known as in AT3D; type-I, features a modification of the amino acid from S to F at position 214.
+The protein's natural variant, known as in AT3D; type-I;, features a modification of the amino acid from S to Y at position 214.
+The protein's natural variant, known as in AT3D, features a modification of the amino acid from I to N at position 218.
+The protein's natural variant, known as in AT3D; type-II; Rouen-6; increases affinity for heparin;, features a modification of the amino acid from N to D at position 219.
+The protein's natural variant, known as in AT3D; type-II; Glasgow-3, features a modification of the amino acid from N to K at position 219.
+The protein's natural variant, known as in AT3D; type-I;, features a modification of the amino acid from S to P at position 223.
+The protein's natural variant, known as in AT3D; severely decreased antithrombin activity; low affinity for heparin, features a modification of the amino acid from EL to VLVLVNTRTS at position 242.
+The protein's natural variant, known as in AT3D; type-I, features a modification of the amino acid from T to I at position 243.
+The protein's natural variant, known as in AT3D, features a modification of the amino acid from V to G at position 248.
+The protein's natural variant, known as in AT3D; type-I;, features a modification of the amino acid from I to T at position 251.
+The protein's natural variant, known as in AT3D; type-I, features a modification of the amino acid from W to R at position 257.
+The protein's natural variant, known as in AT3D, features a modification of the amino acid from F to L at position 261.
+The protein's natural variant, known as in AT3D; type-II; Truro; increases affinity for heparin;, features a modification of the amino acid from E to K at position 269.
+The protein's natural variant, known as in AT3D; type-II, features a modification of the amino acid from M to I at position 283.
+The protein's natural variant, known as in AT3D; type-II, features a modification of the amino acid from M to V at position 283.
+The protein's natural variant, known as in AT3D, features a modification of the amino acid from R to P at position 293.
+The protein's natural variant, known as in AT3D; type-I, features a modification of the amino acid from L to P at position 302.
+The protein's natural variant, known as in AT3D; type-II; Haslar/Whitechapel, features a modification of the amino acid from I to N at position 316.
+The protein's natural variant, known as in AT3D, features a modification of the amino acid from S to P at position 323.
+The protein's natural variant, known as in AT3D; type-II, features a modification of the amino acid from E to K at position 334.
+The protein's natural variant, known as in AT3D; type-I;, features a modification of the amino acid from S to P at position 381.
+The protein's natural variant, known as in AT3D, features a modification of the amino acid from P to PVFLP at position 384.
+The protein's natural variant, known as in AT3D; type-I, features a modification of the amino acid from S to P at position 397.
+The protein's natural variant, known as in AT3D; type-I, features a modification of the amino acid from D to H at position 398.
+The protein's natural variant, known as in AT3D, features a modification of the amino acid from H to R at position 401.
+The protein's natural variant, known as in AT3D; type-I, features a modification of the amino acid from S to R at position 412.
+The protein's natural variant, known as in AT3D; type-II; Hamilton/Glasgow-2; reduces interaction with thrombin by 90%;, features a modification of the amino acid from A to T at position 414.
+The protein's natural variant, known as in AT3D; type-II; Charleville/Sudbury/Vicenza/Cambridge-1;, features a modification of the amino acid from A to P at position 416.
+The protein's natural variant, known as in AT3D; type-II; Cambridge-2;, features a modification of the amino acid from A to S at position 416.
+The protein's natural variant, known as in AT3D; type-I;, features a modification of the amino acid from A to V at position 419.
+The protein's natural variant, known as in AT3D; type-II; Stockholm;, features a modification of the amino acid from G to D at position 424.
+The protein's natural variant, known as in AT3D; type-II;, features a modification of the amino acid from R to C at position 425.
+The protein's natural variant, known as in AT3D; type-II; Glasgow/Sheffield/Chicago/Avranches/Kumamoto-2; increases affinity for heparin; deprived of inhibitory activity;, features a modification of the amino acid from R to H at position 425.
+The protein's natural variant, known as in AT3D; type-II; Pescara; deprived of inhibitory of activity;, features a modification of the amino acid from R to P at position 425.
+The protein's natural variant, known as in AT3D; type-II; Denver/Milano-2; deprived of inhibitory activity;, features a modification of the amino acid from S to L at position 426.
+The protein's natural variant, known as in AT3D; type-II; Rosny;, features a modification of the amino acid from F to C at position 434.
+The protein's natural variant, known as in AT3D; type-II; Maisons-Laffite, features a modification of the amino acid from F to L at position 434.
+The protein's natural variant, known as in AT3D; type-II; Torino, features a modification of the amino acid from F to S at position 434.
+The protein's natural variant, known as in AT3D; type-II; Oslo/Paris-3;, features a modification of the amino acid from A to T at position 436.
+The protein's natural variant, known as in AT3D; type-II; La Rochelle;, features a modification of the amino acid from N to K at position 437.
+The protein's natural variant, known as in AT3D; type I and type-II, features a modification of the amino acid from R to G at position 438.
+The protein's natural variant, known as in AT3D; type-II; Kyoto, features a modification of the amino acid from R to M at position 438.
+The protein's natural variant, known as in AT3D, features a modification of the amino acid from P to A at position 439.
+The protein's natural variant, known as in AT3D; type-II; Utah; deprived of inhibitory activity;, features a modification of the amino acid from P to L at position 439.
+The protein's natural variant, known as in AT3D; type-II; Budapest-5;, features a modification of the amino acid from P to T at position 439.
+The protein's natural variant, known as in AT3D; type-II;, features a modification of the amino acid from L to P at position 441.
+The protein's natural variant, known as in AT3D; type-I, features a modification of the amino acid from I to T at position 453.
+The protein's natural variant, known as in AT3D; type-I; severely decreased antithrombin activity, features a modification of the amino acid from G to R at position 456.
+The protein's natural variant, known as in AT3D; type-II, features a modification of the amino acid from R to T at position 457.
+The protein's natural variant, known as in AT3D; type-I;, features a modification of the amino acid from A to D at position 459.
+The protein's natural variant, known as in AT3D; type-II; Budapest;, features a modification of the amino acid from P to L at position 461.
+The protein's natural variant, known as in AT3D; type-I, features a modification of the amino acid from C to F at position 462.
+The natural variant of this protein is characterized by an amino acid alteration from A to P at position 437.
+The natural variant of this protein is characterized by an amino acid alteration from V to M at position 649.
+The protein's natural variant, known as in IDDDFP; decreased histone H3-K23 acetylation; changed cytoplasmic localization; no effect on expression and assembly of the MOZ/MORF complex;, features a modification of the amino acid from P to S at position 370.
+The protein's natural variant, known as in IDDDFP;, features a modification of the amino acid from C to R at position 389.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from V to L at position 106.
+The protein's natural variant, known as in KURIS, features a modification of the amino acid from P to A at position 12.
+The protein's natural variant, known as in KURIS; loss-of-function variant; increased steady-state levels of ubiquitinated H2A are found in patient cells; unable to rescue impaired H2AK119ub deubiquitination when expressed in BAP1-deficient cells; does not affect localization to the nucleus, features a modification of the amino acid from P to T at position 12.
+The protein's natural variant, known as in KURIS; unknown pathological significance, features a modification of the amino acid from E to K at position 31.
+The protein's natural variant, known as found in a primary uveal melanoma; somatic mutation; induces cytoplasmic accumulation; loss of deubiquitinase activity; up-regulates heat shock response; induces formation of amyloid-beta aggregates, features a modification of the amino acid from I to F at position 47.
+The protein's natural variant, known as in KURIS; unknown pathological significance, features a modification of the amino acid from L to P at position 49.
+The protein's natural variant, known as found in a malignant pleural mesothelioma sample; somatic mutation;, features a modification of the amino acid from S to C at position 63.
+The protein's natural variant, known as found in a malignant pleural mesothelioma sample; somatic mutation; induces cytoplasmic accumulation; loss of deubiquitinase activity; up-regulates heat shock response; induces formation of amyloid-beta aggregates, features a modification of the amino acid from F to V at position 81.
+The protein's natural variant, known as in KURIS, features a modification of the amino acid from C to G at position 91.
+The protein's natural variant, known as in KURIS; loss-of-function variant; unable to rescue impaired H2AK119ub deubiquitination when expressed in BAP1-deficient cells; does not affect localization to the nucleus;, features a modification of the amino acid from C to R at position 91.
+The protein's natural variant, known as in KURIS; loss-of-function variant; increased steady-state level of ubiquitinated H2A are found in patient cells; unable to rescue impaired H2AK119ub deubiquitination when expressed in BAP1-deficient cells; abolishes deubiquitinase activity without affecting its ability to interfere with BRCA1 E3 ligase activity; does not affect localization to the nucleus; has a dominant negative effect on cell growth; does not affect interaction with FOXK1 and FOXK2, features a modification of the amino acid from C to S at position 91.
+The protein's natural variant, known as found in a malignant pleural mesothelioma sample, features a modification of the amino acid from C to W at position 91.
+The protein's natural variant, known as in TPDS1; significantly increased risk for renal cell carcinoma, features a modification of the amino acid from T to A at position 93.
+The protein's natural variant, known as in a lung cancer sample; also found in a malignant pleural mesothelioma cell line; induces cytoplasmic accumulation; loss of deubiquitinase activity; up-regulates heat shock response; induces formation of amyloid-beta aggregates, features a modification of the amino acid from A to D at position 95.
+The protein's natural variant, known as in KURIS; loss-of-function variant; unable to rescue impaired H2AK119ub deubiquitination when expressed in BAP1-deficient cells; does not affect localization to the nucleus, features a modification of the amino acid from H to R at position 169.
+The protein's natural variant, known as in a lung cancer sample; induces cytoplasmic accumulation; impairs deubiquitinase activity; up-regulates heat shock response; induces formation of beta-amyloid aggregates, features a modification of the amino acid from G to V at position 178.
+The protein's natural variant, known as found in a malignant pleural mesothelioma sample;, features a modification of the amino acid from E to A at position 315.
+The protein's natural variant, known as found in a malignant pleural mesothelioma cell line, features a modification of the amino acid from E to V at position 685.
+The protein's natural variant, known as in KURIS; unknown pathological significance; able to rescue impaired H2AK119ub deubiquitination when expressed in BAP1-deficient cells; does not affect localization to the nucleus;, features a modification of the amino acid from R to Q at position 718.
+The protein's natural variant, known as in strain: IT04, features a modification of the amino acid from P to A at position 40.
+The protein's natural variant, known as in strain: IT04, features a modification of the amino acid from E to G at position 196.
+The natural variant of this protein is characterized by an amino acid alteration from K to R at position 78.
+The protein's natural variant, known as in MECREN; loss-of-function variant unable to rescue motor deficiencies in zebrafish morphants;, features a modification of the amino acid from N to D at position 291.
+The protein's natural variant, known as in strain: ATCC 42163 / CBS 7823 / 68-5, features a modification of the amino acid from GAD to MRRN at position 375.
+The natural variant of this protein is characterized by an amino acid alteration from A to T at position 831.
+The protein's natural variant, known as in allele Y, features a modification of the amino acid from H to Y at position 90.
+The protein's natural variant, known as in allele S, features a modification of the amino acid from N to S at position 132.
+The protein's natural variant, known as in DHFRD;, features a modification of the amino acid from L to F at position 80.
+The protein's natural variant, known as in DHFRD;, features a modification of the amino acid from D to V at position 153.
+The natural variant of this protein is characterized by an amino acid alteration from P to Q at position 34.
+The natural variant of this protein is characterized by an amino acid alteration from D to V at position 53.
+The natural variant of this protein is characterized by an amino acid alteration from R to G at position 59.
+The natural variant of this protein is characterized by an amino acid alteration from S to N at position 66.
+The natural variant of this protein is characterized by an amino acid alteration from T to R at position 75.
+The natural variant of this protein is characterized by an amino acid alteration from P to R at position 80.
+The natural variant of this protein is characterized by an amino acid alteration from I to T at position 139.
+The protein's natural variant, known as in ALL3; confers susceptibility to ALL3; reduced transcription factor activity;, features a modification of the amino acid from G to S at position 183.
+The natural variant of this protein is characterized by an amino acid alteration from G to V at position 183.
+The natural variant of this protein is characterized by an amino acid alteration from G to V at position 338.
+The protein's natural variant, known as in XP-B; combined with features of Cockayne syndrome; mild;, features a modification of the amino acid from F to S at position 99.
+The protein's natural variant, known as in TTD2; mild;, features a modification of the amino acid from T to P at position 119.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from K to Q at position 418.
+The protein's natural variant, known as in SPG62;, features a modification of the amino acid from G to V at position 50.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from K to R at position 381.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from K to R at position 398.
+The natural variant of this protein is characterized by an amino acid alteration from A to G at position 198.
+The natural variant of this protein is characterized by an amino acid alteration from H to Q at position 216.
+The natural variant of this protein is characterized by an amino acid alteration from F to L at position 315.
+The protein's natural variant, known as in strain: S-23, features a modification of the amino acid from I to L at position 45.
+The protein's natural variant, known as in strain: S-23, features a modification of the amino acid from I to V at position 191.
+The protein's natural variant, known as in strain: S-23, features a modification of the amino acid from V to E at position 213.
+The protein's natural variant, known as in strain: S-23, features a modification of the amino acid from D to A at position 241.
+The protein's natural variant, known as in allelic sequence, features a modification of the amino acid from E to Q at position 121.
+The protein's natural variant, known as in Schlei; decreases cilium assembly; loss of protein localization to cilium, features a modification of the amino acid from E to G at position 125.
+The protein's natural variant, known as in strain: 2574, ATCC 24657 / D273-10B, ATCC 200060 / W303, Sigma 1278B, YJM 1129, YJM 270, YJM 627 and YJM 789, features a modification of the amino acid from D to G at position 30.
+The protein's natural variant, known as in strain: ATCC 24657 / D273-10B, ATCC 200060 / W303, Sigma 1278B, YJM 1129, YJM 270, YJM 627 and YJM 789, features a modification of the amino acid from K to R at position 453.
+The natural variant of this protein is characterized by an amino acid alteration from C to Y at position 13.
+The natural variant of this protein is characterized by an amino acid alteration from C to F at position 212.
+The protein's natural variant, known as may be associated with inflammatory bowel disease; results in reduced binding affinity to MST1R;, features a modification of the amino acid from R to C at position 689.
+The protein's natural variant, known as in CH2LV, features a modification of the amino acid from I to L at position 72.
+The protein's natural variant, known as in CH2SV, features a modification of the amino acid from I to V at position 72.
+The protein's natural variant, known as in CH2SV, features a modification of the amino acid from RV to KF at position 75.
+The protein's natural variant, known as in CH2LV, features a modification of the amino acid from M to T at position 91.
+The protein's natural variant, known as in CH2SV, features a modification of the amino acid from Q to E at position 96.
+The protein's natural variant, known as in CH2SV, features a modification of the amino acid from N to K at position 105.
+The protein's natural variant, known as in strain: W, features a modification of the amino acid from N to D at position 160.
+The protein's natural variant, known as may increase risk to develop PFB; the variant is disruptive at late stages of filament assembly compromising the aggregation of keratin molecules into intermediate filaments;, features a modification of the amino acid from A to T at position 161.
+The protein's natural variant, known as in LAHS;, features a modification of the amino acid from E to K at position 337.
+The natural variant of this protein is characterized by an amino acid alteration from K to L at position 106.
+The protein's natural variant, known as in strain: B316, features a modification of the amino acid from V to F at position 9.
+The protein's natural variant, known as in strain: B205, features a modification of the amino acid from N to S at position 34.
+The protein's natural variant, known as in strain: B316, features a modification of the amino acid from I to V at position 44.
+The protein's natural variant, known as in strain: Z22, features a modification of the amino acid from K to N at position 48.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from Q to E at position 228.
+The protein's natural variant, known as in HUMOP2, features a modification of the amino acid from L to P at position 335.
+The protein's natural variant, known as in strain: AB1, features a modification of the amino acid from W to G at position 11.
+The protein's natural variant, known as in strain: PB306, features a modification of the amino acid from L to W at position 20.
+The protein's natural variant, known as in strain: PB306, features a modification of the amino acid from S to G at position 26.
+The protein's natural variant, known as in strain: PB306, features a modification of the amino acid from F to C at position 30.
+The protein's natural variant, known as in strain: CB4856, features a modification of the amino acid from Y to C at position 45.
+The protein's natural variant, known as in strain: PB306, features a modification of the amino acid from I to S at position 51.
+The protein's natural variant, known as in strain: PB306, features a modification of the amino acid from I to S at position 61.
+The protein's natural variant, known as in strain: PB306, features a modification of the amino acid from S to G at position 64.
+The protein's natural variant, known as in strain: PB306, features a modification of the amino acid from L to V at position 70.
+The protein's natural variant, known as in strain: PB303, features a modification of the amino acid from G to S at position 317.
+The protein's natural variant, known as in strain: KR314, features a modification of the amino acid from SAPLVLMMYNVFWLSVFY to QHH at position 409.
+The protein's natural variant, known as broaden the specificity of inducer recognition, features a modification of the amino acid from D to E at position 190.
+The protein's natural variant, known as broaden the specificity of inducer recognition, features a modification of the amino acid from A to T at position 195.
+The protein's natural variant, known as broaden the specificity of inducer recognition, features a modification of the amino acid from F to C at position 196.
+The protein's natural variant, known as in GSD7; Ashkenazi;, features a modification of the amino acid from R to L at position 39.
+The protein's natural variant, known as in GSD7; Italian;, features a modification of the amino acid from R to P at position 39.
+The protein's natural variant, known as in GSD7; Italian, features a modification of the amino acid from G to V at position 57.
+The protein's natural variant, known as in GSD7; Italian, features a modification of the amino acid from S to C at position 180.
+The protein's natural variant, known as in GSD7; loss of activity shown by complementation assays in yeast;, features a modification of the amino acid from G to D at position 209.
+The protein's natural variant, known as in GSD7; Spanish; complete loss of enzyme activity;, features a modification of the amino acid from D to G at position 309.
+The protein's natural variant, known as in GSD7; Italian;, features a modification of the amino acid from D to A at position 543.
+The protein's natural variant, known as in GSD7; Italian, features a modification of the amino acid from D to A at position 591.
+The protein's natural variant, known as in GSD7; Japanese;, features a modification of the amino acid from W to C at position 686.
+The protein's natural variant, known as in strain: PAK, features a modification of the amino acid from R to K at position 136.
+The protein's natural variant, known as in strain: PAK, features a modification of the amino acid from Q to E at position 169.
+The protein's natural variant, known as in strain: PAK, features a modification of the amino acid from V to I at position 182.
+The protein's natural variant, known as in strain: PAK, features a modification of the amino acid from L to M at position 189.
+The protein's natural variant, known as in strain: PAK, features a modification of the amino acid from K to Q at position 215.
+The protein's natural variant, known as unknown pathological significance; no effect on its transcriptional activator activity or subcellular localization;, features a modification of the amino acid from G to C at position 17.
+The protein's natural variant, known as in VACTERLX, features a modification of the amino acid from A to AAA at position 46.
+The protein's natural variant, known as unknown pathological significance; no effect on its transcriptional activator activity or subcellular localization, features a modification of the amino acid from A to AA at position 53.
+The protein's natural variant, known as in CHTD1; does not affect its transcriptional activator activity; decrease in nuclear localization;, features a modification of the amino acid from S to C at position 109.
+The protein's natural variant, known as in HTX1 and CHTD1; lacks DNA-binding; does not inhibit transcriptional activation and interaction with GLI3; decrease in nuclear localization;, features a modification of the amino acid from P to A at position 217.
+The protein's natural variant, known as in HTX1; increases strongly its cytoplasmic localization; lacks DNA-binding; does not inhibit transcriptional activation and interaction with GLI3;, features a modification of the amino acid from C to S at position 253.
+The protein's natural variant, known as in HTX1; decreases protein expression and transcriptional activity and increases its cytoplasmic localization;, features a modification of the amino acid from W to G at position 255.
+The protein's natural variant, known as in HTX1; inreases weakly its cytoplasmic localization; lacks DNA-binding; does not inhibit transcriptional activation and interaction with GLI3, features a modification of the amino acid from H to R at position 286.
+The protein's natural variant, known as in VACTERLX; decrease in transcriptional activator activity; significant decrease in nuclear localization, features a modification of the amino acid from H to N at position 318.
+The protein's natural variant, known as in HTX1; lacks DNA-binding; does not inhibit transcriptional activation and interaction with GLI3;, features a modification of the amino acid from T to M at position 323.
+The protein's natural variant, known as in HTX1; lacks DNA-binding; does not inhibit transcriptional activation and interaction with GLI3;, features a modification of the amino acid from K to E at position 405.
+The protein's natural variant, known as in CHTD1; Increase in transcriptional activator activity; decrease in nuclear localization, features a modification of the amino acid from A to G at position 447.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to H at position 901.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from T to M at position 933.
+The protein's natural variant, known as in MGORS3;, features a modification of the amino acid from Y to S at position 232.
+The protein's natural variant, known as in strain: KZ2W, features a modification of the amino acid from M to I at position 4.
+The protein's natural variant, known as in ASAT;, features a modification of the amino acid from E to D at position 208.
+The natural variant of this protein is characterized by an amino acid alteration from R to G at position 315.
+The natural variant of this protein is characterized by an amino acid alteration from F to I at position 346.
+The protein's natural variant, known as in ASAT;, features a modification of the amino acid from I to M at position 400.
+The protein's natural variant, known as in ASAT;, features a modification of the amino acid from V to L at position 411.
+The protein's natural variant, known as in ASAT; impaired maturation of cytosolic Fe/S proteins, loss of the ability to couple MgATP binding with stimulation of ATPase activity at the nucleotide binding domain;; loss of [2Fe-2S]-(GS)4 cluster transport;, features a modification of the amino acid from E to K at position 433.
+The protein's natural variant, known as in HKPX4; unknown pathological significance; likely affects splicing due to removal of the splice donor site of intron 2;, features a modification of the amino acid from Q to H at position 54.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from V to I at position 107.
+The natural variant of this protein is characterized by an amino acid alteration from F to Y at position 10.
+The protein's natural variant, known as in MKS14; unknown pathological significance;, features a modification of the amino acid from L to P at position 212.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from S to P at position 248.
+The protein's natural variant, known as in strain: MEL20, ZBMEL131, ZBMEL186, ZBMEL384 and ZBMEL398, features a modification of the amino acid from L to V at position 2.
+The protein's natural variant, known as in strain: =MEL01, MEL02, MEL11, MEL12, MEL14, MEL15, MEL16, MEL17, MEL18, MEL19, MEL20, ZBMEL82, ZBMEL95, ZBMEL131, ZBMEL145, ZBMEL157, ZBMEL186, ZBMEL191, ZBMEL229, ZBMEL377, ZBMEL384 and ZBMEL398, features a modification of the amino acid from D to E at position 225.
+The protein's natural variant, known as in strain: ZBMEL191, ZBMEL229, ZBMEL377 and ZBMEL384, features a modification of the amino acid from L to V at position 252.
+The natural variant of this protein is characterized by an amino acid alteration from L to P at position 122.
+The natural variant of this protein is characterized by an amino acid alteration from K to E at position 190.
+The protein's natural variant, known as in ACADMD;, features a modification of the amino acid from R to C at position 53.
+The protein's natural variant, known as in ACADMD; mild;, features a modification of the amino acid from Y to H at position 67.
+The protein's natural variant, known as in ACADMD;, features a modification of the amino acid from I to T at position 78.
+The protein's natural variant, known as in ACADMD;, features a modification of the amino acid from C to Y at position 116.
+The protein's natural variant, known as in ACADMD;, features a modification of the amino acid from T to I at position 121.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from P to R at position 132.
+The protein's natural variant, known as in ACADMD;, features a modification of the amino acid from M to I at position 149.
+The protein's natural variant, known as in ACADMD; the thermostability is markedly decreased;, features a modification of the amino acid from T to A at position 193.
+The protein's natural variant, known as in ACADMD;, features a modification of the amino acid from G to R at position 195.
+The protein's natural variant, known as in ACADMD;, features a modification of the amino acid from R to L at position 206.
+The protein's natural variant, known as in ACADMD;, features a modification of the amino acid from C to R at position 244.
+The protein's natural variant, known as in ACADMD;, features a modification of the amino acid from S to L at position 245.
+The protein's natural variant, known as in ACADMD;, features a modification of the amino acid from G to R at position 267.
+The protein's natural variant, known as in ACADMD; mild or benign clinical phenotype;, features a modification of the amino acid from R to T at position 281.
+The protein's natural variant, known as in ACADMD;, features a modification of the amino acid from G to R at position 310.
+The protein's natural variant, known as in ACADMD;, features a modification of the amino acid from M to T at position 326.
+The protein's natural variant, known as in ACADMD; may alter splicing; decreased fatty acid beta-oxidation;, features a modification of the amino acid from K to E at position 329.
+The protein's natural variant, known as in ACADMD, features a modification of the amino acid from S to R at position 336.
+The protein's natural variant, known as in ACADMD;, features a modification of the amino acid from Y to C at position 352.
+The protein's natural variant, known as in ACADMD;, features a modification of the amino acid from I to T at position 375.
+The protein's natural variant, known as in AEZ; Loss of zinc transport activity. Decreases location at cell membrane; retained in the ER;, features a modification of the amino acid from R to C at position 95.
+The protein's natural variant, known as in AEZ; Loss of zinc transport activity. Decreases location at cell membrane; retained in the ER.;, features a modification of the amino acid from N to K at position 106.
+The protein's natural variant, known as in AEZ; Loss of zinc transport activity. Decreases location at cell membrane. Retained in the ER;, features a modification of the amino acid from P to L at position 200.
+The protein's natural variant, known as in AEZ; unknown pathological significance;, features a modification of the amino acid from R to W at position 251.
+The protein's natural variant, known as in AEZ; unknown pathological significance; Loss of zinc transport activity. Decreases location at cell membrane. Retained in the ER;, features a modification of the amino acid from Q to H at position 303.
+The protein's natural variant, known as in AEZ; Decreases location at cell membrane. Retained in the ER;, features a modification of the amino acid from C to Y at position 309.
+The protein's natural variant, known as in AEZ;, features a modification of the amino acid from G to D at position 330.
+The protein's natural variant, known as in AEZ; requires 2 nucleotide substitutions, features a modification of the amino acid from V to P at position 372.
+The protein's natural variant, known as in AEZ;, features a modification of the amino acid from G to R at position 374.
+The protein's natural variant, known as in AEZ; unknown pathological significance, features a modification of the amino acid from L to P at position 410.
+The protein's natural variant, known as in AEZ;, features a modification of the amino acid from G to R at position 526.
+The protein's natural variant, known as in AEZ, features a modification of the amino acid from G to R at position 630.
+The natural variant of this protein is characterized by an amino acid alteration from E to G at position 592.
+The protein's natural variant, known as in a gastric adenocarcinoma sample; somatic mutation, features a modification of the amino acid from G to W at position 36.
+The natural variant of this protein is characterized by an amino acid alteration from Y to H at position 363.
+The protein's natural variant, known as in HYC4;, features a modification of the amino acid from R to H at position 608.
+The protein's natural variant, known as in HYC4;, features a modification of the amino acid from R to H at position 796.
+The protein's natural variant, known as in Novikoff hepatoma cells, features a modification of the amino acid from R to H at position 273.
+The protein's natural variant, known as in cyt-12-12/cyc-1-1; characterized by slow growth and a deficiency of spectrophotometrically-detectable cytochromes aa3 and c, features a modification of the amino acid from G to D at position 11.
+The protein's natural variant, known as in COQ10D3;, features a modification of the amino acid from S to L at position 382.
+The protein's natural variant, known as in MCOP7; reduces the amount of active ligand secreted;, features a modification of the amino acid from R to Q at position 195.
+The protein's natural variant, known as in KFS3 and MCOPCB6; reduces the amount of active ligand secreted; reduced amout of mature protein in the cytosol;, features a modification of the amino acid from R to C at position 266.
+The protein's natural variant, known as in MCOPCB6;, features a modification of the amino acid from R to W at position 274.
+The protein's natural variant, known as in MCOP7; also detected in a patient with bilateral iris coloboma; reduces the amount of active ligand secreted;, features a modification of the amino acid from L to P at position 305.
+The protein's natural variant, known as in CHNG4, features a modification of the amino acid from T to P at position 73.
+The protein's natural variant, known as in strain: O15:H- / 83/39 /ETEC, features a modification of the amino acid from N to G at position 1358.
+The protein's natural variant, known as in strain: O15:H- / 83/39 / ETEC, features a modification of the amino acid from DGTPLPEFYSE to EGELPKFFSD at position 1402.
+The protein's natural variant, known as in strain: O15:H- / 83/39 / ETEC, features a modification of the amino acid from EVSNDK to DVGDKT at position 1428.
+The protein's natural variant, known as in strain: O15:H- / 83/39 /ETEC, features a modification of the amino acid from D to K at position 1498.
+The protein's natural variant, known as in strain: O15:H- / 83/39 /ETEC, features a modification of the amino acid from Q to K at position 1511.
+The protein's natural variant, known as in strain: O15:H- / 83/39 /ETEC, features a modification of the amino acid from A to V at position 1519.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from V to L at position 134.
+The protein's natural variant, known as in JALIS, features a modification of the amino acid from S to P at position 196.
+The protein's natural variant, known as in JALIS;, features a modification of the amino acid from S to Y at position 200.
+The protein's natural variant, known as in JALIS;, features a modification of the amino acid from R to Q at position 236.
+The protein's natural variant, known as in JALIS;, features a modification of the amino acid from L to P at position 324.
+The natural variant of this protein is characterized by an amino acid alteration from M to K at position 463.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from D to Y at position 202.
+The protein's natural variant, known as in strain: YE737 and 1209-79, features a modification of the amino acid from N to D at position 362.
+The protein's natural variant, known as in ACCES; loss of function; does not rescue the abnormal phenotype in a zebrafish disease model, features a modification of the amino acid from G to V at position 24.
+The protein's natural variant, known as in ACCES, features a modification of the amino acid from N to T at position 56.
+The protein's natural variant, known as in ACCES; loss of function; does not rescue the abnormal phenotype in a zebrafish disease model, features a modification of the amino acid from R to G at position 122.
+The protein's natural variant, known as in ACCES; loss of function; does not rescue the abnormal phenotype in a zebrafish disease model, features a modification of the amino acid from E to K at position 483.
+The protein's natural variant, known as in strain: mc(2)651; INH- and ETH-resistant, features a modification of the amino acid from S to A at position 94.
+The protein's natural variant, known as in CORD20; disrupts interaction with FAM161A; localization of the mutant is cytosolic without enrichment at specific subcellular sites;, features a modification of the amino acid from R to P at position 106.
+The protein's natural variant, known as in strain: Z5, features a modification of the amino acid from N to D at position 2.
+The protein's natural variant, known as in strain: Z24, features a modification of the amino acid from N to K at position 2.
+The protein's natural variant, known as in strain: M2, MJ1 and MJ3, features a modification of the amino acid from F to L at position 3.
+The protein's natural variant, known as in strain: B226, features a modification of the amino acid from F to L at position 7.
+The protein's natural variant, known as in strain: Z5, features a modification of the amino acid from V to G at position 8.
+The protein's natural variant, known as in strain: B115, M11 and M47, features a modification of the amino acid from A to T at position 11.
+The protein's natural variant, known as in strain: MJ2, features a modification of the amino acid from V to A at position 36.
+The protein's natural variant, known as in PA-1;, features a modification of the amino acid from A to P at position 75.
+The protein's natural variant, known as in PA-1; loss of function;, features a modification of the amino acid from R to W at position 77.
+The protein's natural variant, known as in PA-1; loss of function;, features a modification of the amino acid from A to T at position 138.
+The protein's natural variant, known as in PA-1; loss of function;, features a modification of the amino acid from I to T at position 164.
+The protein's natural variant, known as in PA-1, features a modification of the amino acid from G to E at position 197.
+The protein's natural variant, known as in PA-1;, features a modification of the amino acid from M to K at position 229.
+The protein's natural variant, known as in PA-1, features a modification of the amino acid from Q to R at position 297.
+The protein's natural variant, known as in PA-1, features a modification of the amino acid from D to G at position 368.
+The protein's natural variant, known as in PA-1; unstable protein; loss of function;, features a modification of the amino acid from M to K at position 373.
+The protein's natural variant, known as in PA-1;, features a modification of the amino acid from G to V at position 379.
+The protein's natural variant, known as in PA-1, features a modification of the amino acid from C to R at position 398.
+The protein's natural variant, known as in PA-1;, features a modification of the amino acid from R to Q at position 399.
+The protein's natural variant, known as in PA-1;, features a modification of the amino acid from P to L at position 423.
+The protein's natural variant, known as in PA-1;, features a modification of the amino acid from W to L at position 559.
+The protein's natural variant, known as in PA-1; loss of function;, features a modification of the amino acid from G to R at position 631.
+The protein's natural variant, known as in PA-1; loss of biotinylation;, features a modification of the amino acid from G to R at position 668.
+The protein's natural variant, known as in strain: cv. RLD, features a modification of the amino acid from RHQRHKDQILL to KASKTQRSNSSLTCLLLVIFGIVLMIVIIVLAV at position 255.
+The protein's natural variant, known as in PBAM1; abolishes taurocholate transport;, features a modification of the amino acid from L to P at position 243.
+The protein's natural variant, known as in PBAM1; abolishes taurocholate transport;, features a modification of the amino acid from T to M at position 262.
+The protein's natural variant, known as in a patient with Crohn disease; abolishes taurocholate transport;, features a modification of the amino acid from P to S at position 290.
+The protein's natural variant, known as in cell line tsBN7; confers temperature sensitivity, features a modification of the amino acid from G to R at position 38.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from A to T at position 865.
+The natural variant of this protein is characterized by an amino acid alteration from A to P at position 1628.
+The protein's natural variant, known as in an ovarian serous carcinoma sample; somatic mutation, features a modification of the amino acid from S to C at position 406.
+The protein's natural variant, known as in a breast infiltrating ductal carcinoma sample; somatic mutation;, features a modification of the amino acid from T to S at position 720.
+The protein's natural variant, known as in a gastric adenocarcinoma sample; somatic mutation, features a modification of the amino acid from M to V at position 830.
+The protein's natural variant, known as probable disease-associated variant found in a patient with hypomagnesemia and secondary hypocalcemia; de novo variant; causes severely reduced Mg(2+) uptake in transfected cells;, features a modification of the amino acid from G to D at position 1046.
+The protein's natural variant, known as mutant channels are functional but show increased susceptibility to inhibition by intracellular magnesium concentrations compared to wild-type channels;, features a modification of the amino acid from T to I at position 1482.
+The protein's natural variant, known as in KBGS; unknown pathological significance, features a modification of the amino acid from R to Q at position 2512.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 517.
+The protein's natural variant, known as in WHIKERS, features a modification of the amino acid from R to Q at position 188.
+The protein's natural variant, known as in WHIKERS, features a modification of the amino acid from R to W at position 188.
+The protein's natural variant, known as in WHIKERS, features a modification of the amino acid from E to K at position 213.
+The protein's natural variant, known as in WHIKERS, features a modification of the amino acid from F to V at position 429.
+The protein's natural variant, known as in CACOV and DA7;, features a modification of the amino acid from R to Q at position 674.
+The protein's natural variant, known as in a melanoma;, features a modification of the amino acid from R to G at position 129.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from T to M at position 283.
+The protein's natural variant, known as in ARS; results in a severe decrease of decapase activity;, features a modification of the amino acid from T to M at position 316.
+The protein's natural variant, known as in SPG53; found in patients with complex hereditary spastic paraparesis; hypomorphic mutation; does not affect interaction with TSG101 and VPS28;, features a modification of the amino acid from K to N at position 382.
+The protein's natural variant, known as in NEDSHBA; does not rescue axon outgrowth defects when expressed in an heterologous system; decreased protein abundance; increased proteasomal degradation; decreased homodimerization; decreased localization to the cell membrane;, features a modification of the amino acid from I to T at position 154.
+The protein's natural variant, known as in NEDSHBA; unknown pathological significance;, features a modification of the amino acid from R to Q at position 658.
+The protein's natural variant, known as in NEDSHBA; unknown pathological significance;, features a modification of the amino acid from R to W at position 658.
+The protein's natural variant, known as in NEDSHBA; unknown pathological significance;, features a modification of the amino acid from T to K at position 675.
+The protein's natural variant, known as in NEDSHBA; unknown pathological significance;, features a modification of the amino acid from E to K at position 891.
+The protein's natural variant, known as in a second clone, features a modification of the amino acid from N to D at position 3.
+The protein's natural variant, known as in a second clone, features a modification of the amino acid from L to V at position 11.
+The protein's natural variant, known as in LAD3; unknown pathological significance; decreases cell adhesion in hematopoietic cells; requires 2 nucleotide substitutions, features a modification of the amino acid from Q to S at position 599.
+The protein's natural variant, known as in strain: ssp. adansonii, ssp. capensis, ssp. carnica, ssp. iberica, ssp. intermissa, ssp. lamarckii, ssp. macedonica, ssp. meda, ssp. monticola, ssp. sahariensis, ssp. scutellata and ssp. sicula, features a modification of the amino acid from F to L at position 14.
+The protein's natural variant, known as in haplotype 9, features a modification of the amino acid from V to M at position 62.
+The protein's natural variant, known as in haplotypes 3, 5, 6, 7 and 10, features a modification of the amino acid from T to I at position 84.
+The protein's natural variant, known as in haplotype 4, MELLI1 and MELLI2, features a modification of the amino acid from V to I at position 138.
+The protein's natural variant, known as in strain: ssp. lamarckii, features a modification of the amino acid from K to S at position 142.
+The protein's natural variant, known as in strain: MELLI1, features a modification of the amino acid from I to T at position 158.
+The protein's natural variant, known as in strain: ssp. carnica, features a modification of the amino acid from F to L at position 203.
+The protein's natural variant, known as in haplotype 6, features a modification of the amino acid from V to D at position 262.
+The protein's natural variant, known as in PKKD; reduces the binding activity of Apple domain 2 to HMW kininogen;, features a modification of the amino acid from G to R at position 123.
+The protein's natural variant, known as in PKKD; reduces the binding activity of Apple domain 2 to HMW kininogen;, features a modification of the amino acid from N to S at position 143.
+The protein's natural variant, known as in PKKD;, features a modification of the amino acid from C to Y at position 548.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 7.
+The protein's natural variant, known as in strain: GAM4B and GAM6B, features a modification of the amino acid from N to H at position 2.
+The protein's natural variant, known as in strain: GAM4B, features a modification of the amino acid from I to F at position 8.
+The protein's natural variant, known as in strain: GAM5A and GAM5B, features a modification of the amino acid from L to V at position 16.
+The protein's natural variant, known as in strain: GAM2B and GAM8B, features a modification of the amino acid from Q to H at position 20.
+The protein's natural variant, known as in strain: GAM12B, features a modification of the amino acid from E to D at position 34.
+The protein's natural variant, known as found in patients with non-obstructive azoospermia; unknown pathological significance; decreased expression of MAP1LC3B; increased programmed cell death in spermatogenic cells;, features a modification of the amino acid from R to L at position 125.
+The protein's natural variant, known as found in patients with non-obstructive azoospermia; unknown pathological significance;, features a modification of the amino acid from V to I at position 273.
+The protein's natural variant, known as found in patients with non-obstructive azoospermia; unknown pathological significance;, features a modification of the amino acid from A to D at position 295.
+The protein's natural variant, known as found in patients with non-obstructive azoospermia; unknown pathological significance;, features a modification of the amino acid from V to M at position 395.
+The protein's natural variant, known as in strain: O44:K74, features a modification of the amino acid from V to A at position 187.
+The protein's natural variant, known as in strain: O44:K74, features a modification of the amino acid from T to A at position 302.
+The protein's natural variant, known as in BOFS, features a modification of the amino acid from L to P at position 249.
+The protein's natural variant, known as in BOFS;, features a modification of the amino acid from R to G at position 254.
+The protein's natural variant, known as in BOFS;, features a modification of the amino acid from R to G at position 255.
+The protein's natural variant, known as in BOFS;, features a modification of the amino acid from G to E at position 262.
+The protein's natural variant, known as in plaC1 mutation; results in a narrower specificity for promoters, features a modification of the amino acid from P to S at position 209.
+The protein's natural variant, known as in strain: CC-503, features a modification of the amino acid from L to I at position 438.
+The protein's natural variant, known as in DFNB36; irregular microvillar organization;, features a modification of the amino acid from S to R at position 719.
+The protein's natural variant, known as in DFNB36; irregular microvillar organization;, features a modification of the amino acid from D to N at position 744.
+The protein's natural variant, known as in DFNB36; sporadic case with mild phenotype; unknown pathological significance;, features a modification of the amino acid from R to Q at position 774.
+The protein's natural variant, known as decreased indoleamine 2,3-dioxygenase activity;, features a modification of the amino acid from R to W at position 248.
+The protein's natural variant, known as in JDSCD; reduced glucuronyltransferase activity; patient fibroblasts have decreased levels of dermatan sulfate, chondroitin sulfate and heparan sulfate proteoglycans;, features a modification of the amino acid from P to L at position 140.
+The protein's natural variant, known as in JDSCD; unknown pathological significance;, features a modification of the amino acid from G to S at position 223.
+The protein's natural variant, known as in JDSCD; reduced glucuronyltransferase activity; patient fibroblasts have decreased levels of dermatan sulfate, chondroitin sulfate and heparan sulfate proteoglycans;, features a modification of the amino acid from R to Q at position 277.
+The natural variant of this protein is characterized by an amino acid alteration from N to S at position 67.
+The protein's natural variant, known as in gutR1; results in the constitutive expression of gutB, features a modification of the amino acid from S to R at position 289.
+The protein's natural variant, known as in strain: B, features a modification of the amino acid from Q to E at position 318.
+The natural variant of this protein is characterized by an amino acid alteration from K to T at position 254.
+The protein's natural variant, known as in AIPCS; complete loss of DNase activity in a single radial enzyme diffusion assay, confirmed by deficiency in DNA degradation in the granulocytes of a homozygous patient; no effect on expression level;, features a modification of the amino acid from Y to C at position 95.
+The protein's natural variant, known as in AIPCS; the genetic variation producing this missense variant predominantly affects splicing and the protein resulting from this aberrant splicing may be unstable; reduced DNase activity, features a modification of the amino acid from G to A at position 116.
+The protein's natural variant, known as in AIPCS; reduced DNase activity, features a modification of the amino acid from D to V at position 121.
+The protein's natural variant, known as in strain: cv. Tsu-1, features a modification of the amino acid from S to P at position 35.
+The protein's natural variant, known as in strain: cv. Kl-1, features a modification of the amino acid from T to I at position 79.
+The protein's natural variant, known as in strain: cv. Bla-6, cv. Bu-2, cv. Di-1 and cv. Pi-0, features a modification of the amino acid from G to V at position 88.
+The protein's natural variant, known as in strain: cv. Tsu-1, features a modification of the amino acid from D to Y at position 123.
+The protein's natural variant, known as in strain: cv. Bla-6, features a modification of the amino acid from Q to K at position 162.
+The protein's natural variant, known as found in a renal cell carcinoma sample; somatic mutation, features a modification of the amino acid from H to N at position 56.
+The protein's natural variant, known as in CVID2 and IGAD2;, features a modification of the amino acid from C to R at position 104.
+The protein's natural variant, known as in CVID2, features a modification of the amino acid from A to G at position 181.
+The protein's natural variant, known as in CVID2;, features a modification of the amino acid from R to H at position 202.
+The protein's natural variant, known as decreases homodimerization but nearly no effect on kinetic parameters;, features a modification of the amino acid from R to C at position 802.
+The protein's natural variant, known as increases homodimerization; abolishes enzymatic activity on phenanthridine; decreases turnover number with benzaldehyde, phtalazine and chloroquinazolinone as substrate, while nearly no effect on the KM;, features a modification of the amino acid from R to H at position 921.
+The protein's natural variant, known as increases homodimerization and turnover number with phenanthridine as substrate; nearly no effect on kinetic parameters with benzaldehyde, phtalazine and chloroquinazolinone as substrate;, features a modification of the amino acid from N to S at position 1135.
+The protein's natural variant, known as no effect on dimerization; no effect on oxidase activity;, features a modification of the amino acid from S to L at position 1271.
+The protein's natural variant, known as increases homodimerization and turnover number with phenanthridine as substrate; nearly no effect on kinetic parameters with benzaldehyde, phtalazine and chloroquinazolinone as substrate;, features a modification of the amino acid from H to R at position 1297.
+The protein's natural variant, known as in RP1;, features a modification of the amino acid from L to R at position 172.
+The protein's natural variant, known as in RP1;, features a modification of the amino acid from D to E at position 202.
+The protein's natural variant, known as in RP1; unknown pathological significance;, features a modification of the amino acid from T to I at position 373.
+The natural variant of this protein is characterized by an amino acid alteration from I to L at position 408.
+The protein's natural variant, known as in RP1; unknown pathological significance;, features a modification of the amino acid from K to N at position 663.
+The protein's natural variant, known as in RP1;, features a modification of the amino acid from A to T at position 669.
+The natural variant of this protein is characterized by an amino acid alteration from C to W at position 727.
+The protein's natural variant, known as in RP1, features a modification of the amino acid from K to N at position 900.
+The protein's natural variant, known as in RP1;, features a modification of the amino acid from D to G at position 984.
+The natural variant of this protein is characterized by an amino acid alteration from L to S at position 1356.
+The protein's natural variant, known as in RP1; unknown pathological significance;, features a modification of the amino acid from K to E at position 1370.
+The protein's natural variant, known as in RP1; unknown pathological significance;, features a modification of the amino acid from R to L at position 1652.
+The protein's natural variant, known as in RP1; unknown pathological significance;, features a modification of the amino acid from L to P at position 1808.
+The protein's natural variant, known as in RP1;, features a modification of the amino acid from T to N at position 2113.
+The protein's natural variant, known as in strain: CLIB 413 haplotype Ha1, features a modification of the amino acid from L to V at position 153.
+The protein's natural variant, known as in strain: CLIB 630, features a modification of the amino acid from I to L at position 203.
+The protein's natural variant, known as in strain: K1, features a modification of the amino acid from V to I at position 204.
+The protein's natural variant, known as in strain: CLIB 413 haplotype Ha2, features a modification of the amino acid from A to E at position 220.
+The protein's natural variant, known as in strain: CLIB 630, features a modification of the amino acid from R to I at position 223.
+The protein's natural variant, known as in strain: CLIB 219, features a modification of the amino acid from K to N at position 236.
+The protein's natural variant, known as in strain: CLIB 388 haplotype Ha2, features a modification of the amino acid from A to T at position 241.
+The natural variant of this protein is characterized by an amino acid alteration from R to W at position 6.
+The protein's natural variant, known as in CSNB1C, features a modification of the amino acid from Y to C at position 56.
+The protein's natural variant, known as in CSNB1C;, features a modification of the amino acid from Y to C at position 72.
+The protein's natural variant, known as in CSNB1C;, features a modification of the amino acid from R to C at position 74.
+The protein's natural variant, known as in CSNB1C;, features a modification of the amino acid from L to P at position 99.
+The protein's natural variant, known as in CSNB1C;, features a modification of the amino acid from L to R at position 364.
+The protein's natural variant, known as in CSNB1C, features a modification of the amino acid from R to P at position 473.
+The protein's natural variant, known as in CSNB1C;, features a modification of the amino acid from G to R at position 534.
+The protein's natural variant, known as in CSNB1C;, features a modification of the amino acid from M to K at position 541.
+The protein's natural variant, known as in CSNB1C;, features a modification of the amino acid from P to H at position 611.
+The protein's natural variant, known as in CSNB1C;, features a modification of the amino acid from R to Q at position 721.
+The protein's natural variant, known as in CSNB1C;, features a modification of the amino acid from E to G at position 883.
+The protein's natural variant, known as in a patient with night blindness started in the third decade; associated in cis with G-1438, features a modification of the amino acid from M to T at position 962.
+The protein's natural variant, known as in CSNB1C;, features a modification of the amino acid from I to F at position 1002.
+The natural variant of this protein is characterized by an amino acid alteration from R to W at position 1422.
+The protein's natural variant, known as in a patient with night blindness started in the third decade; associated in cis with T-962, features a modification of the amino acid from R to G at position 1438.
+The protein's natural variant, known as in strain: I69, features a modification of the amino acid from I to T at position 46.
+The protein's natural variant, known as in strain: I69, features a modification of the amino acid from E to D at position 85.
+The protein's natural variant, known as in strain: I69, features a modification of the amino acid from TWM to IWR at position 153.
+The protein's natural variant, known as in strain: I69, features a modification of the amino acid from SA to LG at position 201.
+The protein's natural variant, known as abrogates exonuclease activity;, features a modification of the amino acid from E to K at position 109.
+The natural variant of this protein is characterized by an amino acid alteration from A to V at position 153.
+The protein's natural variant, known as abrogates exonuclease activity;, features a modification of the amino acid from L to R at position 410.
+The natural variant of this protein is characterized by an amino acid alteration from F to C at position 438.
+The protein's natural variant, known as may be associated with an increased risk of colorectal cancer;, features a modification of the amino acid from T to M at position 439.
+The protein's natural variant, known as reduces interaction with MSH2; abrogates interaction with MSH2; when associated with L-770;, features a modification of the amino acid from P to S at position 640.
+The natural variant of this protein is characterized by an amino acid alteration from H to P at position 726.
+The protein's natural variant, known as may be associated with a reduced risk of colorectal cancer;, features a modification of the amino acid from P to L at position 757.
+The protein's natural variant, known as reduces interaction with MSH2; abrogates interaction with MSH2; when associated with L-770;, features a modification of the amino acid from G to E at position 759.
+The protein's natural variant, known as reduces interaction with MSH2; abrogates interaction with MSH2; when associated with S-640 or E-759;, features a modification of the amino acid from P to L at position 770.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from T to A at position 579.
+The protein's natural variant, known as in a lung squamous cell carcinoma sample; somatic mutation, features a modification of the amino acid from S to C at position 854.
+The protein's natural variant, known as in a lung large cell carcinoma sample; somatic mutation, features a modification of the amino acid from L to F at position 1533.
+The protein's natural variant, known as in a renal clear cell carcinoma sample; somatic mutation, features a modification of the amino acid from S to P at position 1634.
+The protein's natural variant, known as in strain: Diastaticus / ATCC 60715 /YIY2-11A, features a modification of the amino acid from Q to QQQ at position 54.
+The protein's natural variant, known as in strain: Diastaticus / ATCC 60715 / YIY2-11A, features a modification of the amino acid from V to I at position 112.
+The protein's natural variant, known as in strain: Diastaticus / ATCC 60715 / YIY2-11A, features a modification of the amino acid from P to S at position 115.
+The protein's natural variant, known as in strain: Diastaticus / ATCC 60715 / YIY2-11A, features a modification of the amino acid from C to G at position 383.
+The protein's natural variant, known as in strain: Diastaticus / ATCC 60715 / YIY2-11A, features a modification of the amino acid from A to T at position 441.
+The protein's natural variant, known as in strain: Diastaticus / ATCC 60715 / YIY2-11A, features a modification of the amino acid from A to V at position 447.
+The protein's natural variant, known as in strain: Diastaticus / ATCC 60715 / YIY2-11A, features a modification of the amino acid from R to P at position 598.
+The protein's natural variant, known as in chloronerva; has no activity, features a modification of the amino acid from F to S at position 238.
+The protein's natural variant, known as exerts a protective effect in heart failure and ischemia;, features a modification of the amino acid from Q to L at position 41.
+The protein's natural variant, known as in a lung neuroendocrine carcinoma sample; somatic mutation, features a modification of the amino acid from D to E at position 163.
+The protein's natural variant, known as may influence the age-at-onset of Huntington disease; increases binding to mutated HTT; influences HTT degradation;, features a modification of the amino acid from T to M at position 493.
+The natural variant of this protein is characterized by an amino acid alteration from G to R at position 452.
+The natural variant of this protein is characterized by an amino acid alteration from S to C at position 477.
+The natural variant of this protein is characterized by an amino acid alteration from I to S at position 486.
+The natural variant of this protein is characterized by an amino acid alteration from R to P at position 26.
+The natural variant of this protein is characterized by an amino acid alteration from D to N at position 344.
+The natural variant of this protein is characterized by an amino acid alteration from L to P at position 392.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from C to R at position 63.
+The protein's natural variant, known as in NPC1, features a modification of the amino acid from C to Y at position 74.
+The protein's natural variant, known as in NPC1, features a modification of the amino acid from Q to R at position 92.
+The protein's natural variant, known as in NPC1; partially mislocalized from late endocytic organelles diffusely to the cell periphery; localizes to the endoplasmic reticulum Rab7-negative endosomes and the cell surface; does not clear the lysosomal cholesterol accumulation in NPC1-deficient cells;, features a modification of the amino acid from C to R at position 113.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from T to M at position 137.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from P to S at position 166.
+The protein's natural variant, known as in NPC1; late infantile form, features a modification of the amino acid from C to G at position 177.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from C to Y at position 177.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from N to S at position 222.
+The protein's natural variant, known as in NPC1, features a modification of the amino acid from V to G at position 231.
+The protein's natural variant, known as no effect on function; colocalizes with the wild-type protein with Rab7-positive late endosomes; clears the lysosomal cholesterol accumulation in NPC1-deficient cells;, features a modification of the amino acid from P to S at position 237.
+The protein's natural variant, known as in NPC1, features a modification of the amino acid from D to H at position 242.
+The protein's natural variant, known as in NPC1, features a modification of the amino acid from D to N at position 242.
+The protein's natural variant, known as in NPC1, features a modification of the amino acid from C to Y at position 247.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from G to V at position 248.
+The protein's natural variant, known as in NPC1, features a modification of the amino acid from M to R at position 272.
+The natural variant of this protein is characterized by an amino acid alteration from G to D at position 333.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from R to W at position 372.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from V to A at position 378.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from L to F at position 380.
+The natural variant of this protein is characterized by an amino acid alteration from W to C at position 381.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from A to P at position 388.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from R to C at position 389.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from P to T at position 401.
+The protein's natural variant, known as in NPC1, features a modification of the amino acid from R to P at position 404.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from R to Q at position 404.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from R to W at position 404.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from P to L at position 433.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from P to L at position 434.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from E to K at position 451.
+The natural variant of this protein is characterized by an amino acid alteration from L to P at position 472.
+The protein's natural variant, known as in NPC1; late infantile form, features a modification of the amino acid from S to P at position 473.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from P to L at position 474.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from C to Y at position 479.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from Y to S at position 509.
+The protein's natural variant, known as in NPC1; late infantile form, features a modification of the amino acid from H to P at position 510.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from H to R at position 512.
+The protein's natural variant, known as in NPC1; late infantile form; Common in Japanese;, features a modification of the amino acid from R to Q at position 518.
+The protein's natural variant, known as in NPC1; decreased affinity for NPC2; decreased cholesterol transfer from NPC2 to NPC1;, features a modification of the amino acid from R to W at position 518.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from A to S at position 521.
+The protein's natural variant, known as in NPC1, features a modification of the amino acid from F to L at position 537.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from P to L at position 543.
+The protein's natural variant, known as in NPC1, features a modification of the amino acid from T to K at position 574.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from K to R at position 576.
+The protein's natural variant, known as in NPC1, features a modification of the amino acid from A to V at position 605.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from E to D at position 612.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from R to C at position 615.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from R to L at position 615.
+The protein's natural variant, known as in NPC1, features a modification of the amino acid from M to R at position 631.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from G to R at position 640.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from S to W at position 652.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from G to S at position 660.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from V to M at position 664.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from S to N at position 666.
+The protein's natural variant, known as in NPC1, features a modification of the amino acid from C to W at position 670.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from G to V at position 673.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from L to F at position 684.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from P to L at position 691.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from L to V at position 695.
+The protein's natural variant, known as in NPC1, features a modification of the amino acid from D to N at position 700.
+The protein's natural variant, known as in NPC1, features a modification of the amino acid from F to S at position 703.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from L to P at position 724.
+The protein's natural variant, known as in NPC1, features a modification of the amino acid from V to F at position 727.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from S to I at position 734.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from E to K at position 742.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from A to E at position 745.
+The protein's natural variant, known as in NPC1, features a modification of the amino acid from M to K at position 754.
+The natural variant of this protein is characterized by an amino acid alteration from V to A at position 757.
+The protein's natural variant, known as in NPC1, features a modification of the amino acid from F to L at position 763.
+The protein's natural variant, known as in NPC1, features a modification of the amino acid from A to V at position 767.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from Q to P at position 775.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from R to C at position 789.
+The protein's natural variant, known as in NPC1, features a modification of the amino acid from R to G at position 789.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from Y to C at position 825.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from S to I at position 849.
+The protein's natural variant, known as in NPC1, features a modification of the amino acid from Q to L at position 862.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from S to L at position 865.
+The protein's natural variant, known as in NPC1, features a modification of the amino acid from Y to C at position 871.
+The natural variant of this protein is characterized by an amino acid alteration from V to A at position 873.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from D to V at position 874.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from P to S at position 888.
+The protein's natural variant, known as in NPC1; adult form;, features a modification of the amino acid from V to M at position 889.
+The protein's natural variant, known as in NPC1, features a modification of the amino acid from Y to C at position 890.
+The protein's natural variant, known as in NPC1, features a modification of the amino acid from Y to D at position 899.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from G to S at position 910.
+The protein's natural variant, known as in NPC1, features a modification of the amino acid from D to Y at position 917.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from A to T at position 926.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from A to V at position 927.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from Q to P at position 928.
+The protein's natural variant, known as in NPC1, features a modification of the amino acid from L to P at position 929.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from R to Q at position 934.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from S to L at position 940.
+The protein's natural variant, known as in NPC1, features a modification of the amino acid from W to C at position 942.
+The protein's natural variant, known as in NPC1, features a modification of the amino acid from I to M at position 943.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from D to N at position 944.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from D to N at position 945.
+The protein's natural variant, known as in NPC1, features a modification of the amino acid from D to H at position 948.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from D to N at position 948.
+The protein's natural variant, known as in NPC1, features a modification of the amino acid from D to Y at position 948.
+The protein's natural variant, known as in NPC1; adult form;, features a modification of the amino acid from V to M at position 950.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from S to L at position 954.
+The protein's natural variant, known as in NPC1; late infantile form, features a modification of the amino acid from C to Y at position 956.
+The protein's natural variant, known as in NPC1, features a modification of the amino acid from R to L at position 958.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from R to Q at position 958.
+The protein's natural variant, known as in NPC1, features a modification of the amino acid from V to E at position 959.
+The protein's natural variant, known as in NPC1, features a modification of the amino acid from NITDQF to S at position 966.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from N to S at position 961.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from N to S at position 968.
+The natural variant of this protein is characterized by an amino acid alteration from V to G at position 971.
+The protein's natural variant, known as in NPC1, features a modification of the amino acid from C to R at position 976.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from R to C at position 978.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from G to S at position 986.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from G to A at position 992.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from G to R at position 992.
+The protein's natural variant, known as in NPC1; found in the Nova Scotian clinical variant;, features a modification of the amino acid from G to W at position 992.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from M to R at position 996.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from S to L at position 1004.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from P to A at position 1007.
+The protein's natural variant, known as in NPC1, features a modification of the amino acid from G to D at position 1012.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from G to V at position 1015.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from H to R at position 1016.
+The protein's natural variant, known as in NPC1, features a modification of the amino acid from V to G at position 1023.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from G to R at position 1034.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from A to V at position 1035.
+The protein's natural variant, known as in NPC1, features a modification of the amino acid from T to K at position 1036.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from T to M at position 1036.
+The natural variant of this protein is characterized by an amino acid alteration from A to V at position 1049.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from A to T at position 1054.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from R to Q at position 1059.
+The protein's natural variant, known as in NPC1; late infantile form;, features a modification of the amino acid from I to T at position 1061.
+The protein's natural variant, known as in NPC1, features a modification of the amino acid from A to V at position 1062.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from T to N at position 1066.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from F to L at position 1087.
+The protein's natural variant, known as in NPC1; juvenile form;, features a modification of the amino acid from Y to C at position 1088.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from E to K at position 1089.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from I to T at position 1094.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from D to N at position 1097.
+The protein's natural variant, known as in NPC1, features a modification of the amino acid from N to I at position 1137.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from G to V at position 1140.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from M to T at position 1142.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from N to K at position 1150.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from N to I at position 1156.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from N to S at position 1156.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from V to M at position 1165.
+The protein's natural variant, known as in NPC1, features a modification of the amino acid from F to L at position 1167.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from C to Y at position 1168.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from A to V at position 1174.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from R to H at position 1186.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from E to G at position 1189.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from T to K at position 1205.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from T to R at position 1205.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from V to L at position 1212.
+The protein's natural variant, known as in NPC1; juvenile form;, features a modification of the amino acid from L to F at position 1213.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from L to V at position 1213.
+The protein's natural variant, known as in NPC1, features a modification of the amino acid from A to V at position 1216.
+The natural variant of this protein is characterized by an amino acid alteration from I to T at position 1220.
+The protein's natural variant, known as in NPC1, features a modification of the amino acid from F to L at position 1224.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from G to E at position 1236.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from G to R at position 1240.
+The protein's natural variant, known as in NPC1;, features a modification of the amino acid from S to G at position 1249.
+The protein's natural variant, known as in MC1DN32;, features a modification of the amino acid from Y to H at position 62.
+The protein's natural variant, known as in MC1DN32;, features a modification of the amino acid from P to Q at position 76.
+The protein's natural variant, known as in MC1DN32; due to a nucleotide substitution that results in exon 4 skipping or missense variant W-144; patient cells contain both type of transcripts; transcript with the missense variant is the less abundant;, features a modification of the amino acid from C to W at position 144.
+The protein's natural variant, known as found in a patient with lung cancer; abolished formation of N(7)-methylguanine in tRNAs, features a modification of the amino acid from H to P at position 144.
+The protein's natural variant, known as in GAMOS6; unknown pathological significance;, features a modification of the amino acid from D to A at position 164.
+The protein's natural variant, known as in MIGSB, features a modification of the amino acid from R to L at position 170.
+The protein's natural variant, known as in GAMOS6; abolished formation of N(7)-methylguanine in tRNAs;, features a modification of the amino acid from R to Q at position 170.
+The protein's natural variant, known as in HAAKD;, features a modification of the amino acid from G to R at position 40.
+The protein's natural variant, known as in HAAKD;, features a modification of the amino acid from G to R at position 64.
+The protein's natural variant, known as in HAAKD; the same mutation in the chicken sequence shows reduced adenylate kinase activity;, features a modification of the amino acid from R to W at position 128.
+The protein's natural variant, known as in HAAKD;, features a modification of the amino acid from Y to C at position 164.
+The protein's natural variant, known as in strain: 1c11, features a modification of the amino acid from R to K at position 258.
+The protein's natural variant, known as in strain: SAG 26.98 and 1c11, features a modification of the amino acid from H to Y at position 440.
+The protein's natural variant, known as in ECYT1 and erythroleukemia;, features a modification of the amino acid from N to S at position 487.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from S to G at position 983.
+The protein's natural variant, known as in a lung squamous cell carcinoma sample; somatic mutation, features a modification of the amino acid from W to R at position 267.
+The protein's natural variant, known as associated with susceptibility to pre-eclampsia; alters the reactions with renin and angiotensin-converting enzyme;, features a modification of the amino acid from L to F at position 43.
+The protein's natural variant, known as associated with hypertension;, features a modification of the amino acid from T to M at position 207.
+The protein's natural variant, known as associated with susceptibility to hypertension;, features a modification of the amino acid from T to I at position 242.
+The protein's natural variant, known as associated with susceptibility to hypertension;, features a modification of the amino acid from L to R at position 244.
+The protein's natural variant, known as associated with essential hypertension and pre-eclampsia;, features a modification of the amino acid from M to T at position 268.
+The protein's natural variant, known as associated with susceptibility to hypertension; alters the structure, glycosylation and secretion of angiotensinogen;, features a modification of the amino acid from Y to C at position 281.
+The protein's natural variant, known as in RTD;, features a modification of the amino acid from R to Q at position 375.
+The protein's natural variant, known as in CLN2, features a modification of the amino acid from S to T at position 62.
+The protein's natural variant, known as in CLN2; displays very low residual enzyme activity; altered intracellular trafficking;, features a modification of the amino acid from G to R at position 77.
+The protein's natural variant, known as in CLN2; displays residual enzyme activity; effectively transported to the lysosome;, features a modification of the amino acid from R to Q at position 127.
+The protein's natural variant, known as in CLN2;, features a modification of the amino acid from S to P at position 153.
+The protein's natural variant, known as in CLN2; displays no residual enzyme activity; altered intracellular trafficking;, features a modification of the amino acid from P to L at position 202.
+The protein's natural variant, known as in CLN2; displays no residual enzyme activity; altered intracellular trafficking;, features a modification of the amino acid from R to C at position 206.
+The protein's natural variant, known as in CLN2;, features a modification of the amino acid from R to H at position 206.
+The protein's natural variant, known as in CLN2;, features a modification of the amino acid from Y to H at position 209.
+The protein's natural variant, known as in CLN2;, features a modification of the amino acid from R to Q at position 266.
+The protein's natural variant, known as in CLN2; displays no residual enzyme activity; altered intracellular trafficking; demonstrates enhanced processing in response to folding improvement treatment;, features a modification of the amino acid from V to M at position 277.
+The protein's natural variant, known as in CLN2;, features a modification of the amino acid from Q to P at position 278.
+The protein's natural variant, known as in CLN2;, features a modification of the amino acid from Q to R at position 278.
+The protein's natural variant, known as in CLN2; displays no residual enzyme activity; altered intracellular trafficking;, features a modification of the amino acid from G to V at position 284.
+The protein's natural variant, known as in CLN2; enzymatically inactive; lacks one oligosaccharide chain resulting in enzymatic inactivation and possibly prelysosomal protein degradation; altered intracellular trafficking;, features a modification of the amino acid from N to S at position 286.
+The protein's natural variant, known as in CLN2; displays no residual enzyme activity; altered intracellular trafficking;, features a modification of the amino acid from I to N at position 287.
+The protein's natural variant, known as in CLN2;, features a modification of the amino acid from R to Q at position 339.
+The protein's natural variant, known as in CLN2; displays no residual enzyme activity; altered intracellular trafficking;, features a modification of the amino acid from E to K at position 343.
+The protein's natural variant, known as in CLN2;, features a modification of the amino acid from T to P at position 353.
+The protein's natural variant, known as in CLN2; displays no residual enzyme activity; altered intracellular trafficking;, features a modification of the amino acid from C to R at position 365.
+The protein's natural variant, known as in CLN2;, features a modification of the amino acid from C to Y at position 365.
+The protein's natural variant, known as in CLN2, features a modification of the amino acid from S to R at position 382.
+The protein's natural variant, known as in CLN2;, features a modification of the amino acid from V to D at position 385.
+The protein's natural variant, known as in CLN2;, features a modification of the amino acid from G to E at position 389.
+The protein's natural variant, known as in CLN2; displays no residual enzyme activity; altered intracellular trafficking;;, features a modification of the amino acid from Q to H at position 422.
+The protein's natural variant, known as in CLN2, features a modification of the amino acid from K to N at position 428.
+The protein's natural variant, known as in CLN2; displays very low residual enzyme activity; altered intracellular trafficking; demonstrates enhanced processing in response to folding improvement treatment; shows a five fold increase under permissive temperature conditions;, features a modification of the amino acid from R to H at position 447.
+The protein's natural variant, known as in CLN2, features a modification of the amino acid from A to V at position 448.
+The protein's natural variant, known as in CLN2;, features a modification of the amino acid from A to E at position 454.
+The protein's natural variant, known as in SCAR7;, features a modification of the amino acid from V to G at position 466.
+The protein's natural variant, known as in CLN2;, features a modification of the amino acid from G to R at position 473.
+The protein's natural variant, known as in CLN2; displays no residual enzyme activity; effectively transported to the lysosome;, features a modification of the amino acid from S to L at position 475.
+The protein's natural variant, known as in CLN2, features a modification of the amino acid from F to C at position 481.
+The protein's natural variant, known as in CLN2;, features a modification of the amino acid from G to R at position 482.
+The protein's natural variant, known as in CLN2, features a modification of the amino acid from G to C at position 501.
+The protein's natural variant, known as in CLN2, features a modification of the amino acid from N to Y at position 504.
+The protein's natural variant, known as in CLN2; displays residual enzyme activity; effectively transported to the lysosome;, features a modification of the amino acid from P to S at position 544.
+The protein's natural variant, known as in CLN2;, features a modification of the amino acid from W to R at position 548.
+The protein's natural variant, known as in TOF and CTHM; does not affect its ability to interact with GATA4;, features a modification of the amino acid from E to G at position 30.
+The protein's natural variant, known as in CTHM;, features a modification of the amino acid from I to V at position 227.
+The protein's natural variant, known as in SRXY9; results in reduced transactivation activity on the AMH promoter; does not affect its ability to interact with GATA4;, features a modification of the amino acid from R to Q at position 260.
+The protein's natural variant, known as in SRXY9; results in reduced transactivation activity on the AMH promoter; abolished its ability to interact with GATA4;, features a modification of the amino acid from S to R at position 402.
+The protein's natural variant, known as in SRXY9 and TOF; reduced its ability to interact with GATA4;, features a modification of the amino acid from M to I at position 544.
+The protein's natural variant, known as in TOF; slightly impairs its ability to interact with GATA4;, features a modification of the amino acid from S to G at position 657.
+The protein's natural variant, known as in PRAAS4; unknown pathological significance;, features a modification of the amino acid from N to K at position 225.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to H at position 10.
+The protein's natural variant, known as in strain: Isolate South Africa, features a modification of the amino acid from L to F at position 185.
+The protein's natural variant, known as in strain: Isolate South Africa, features a modification of the amino acid from A to V at position 193.
+The protein's natural variant, known as in strain: Isolate South Africa, features a modification of the amino acid from L to F at position 296.
+The protein's natural variant, known as in strain: Isolate South Africa, features a modification of the amino acid from L to F at position 320.
+The protein's natural variant, known as in class 3, features a modification of the amino acid from R to L at position 21.
+The protein's natural variant, known as in class 3, features a modification of the amino acid from S to A at position 52.
+The protein's natural variant, known as in class 3, features a modification of the amino acid from L to F at position 56.
+The protein's natural variant, known as in class 3, features a modification of the amino acid from R to H at position 85.
+The protein's natural variant, known as in class 2 and class 3, features a modification of the amino acid from V to I at position 210.
+The protein's natural variant, known as in class 2 and class 3, features a modification of the amino acid from R to P at position 277.
+The protein's natural variant, known as in class 2, features a modification of the amino acid from G to V at position 334.
+The protein's natural variant, known as in class 2 and class 3, features a modification of the amino acid from TDSESA to SDNEST at position 423.
+The protein's natural variant, known as in class 2 and class 3, features a modification of the amino acid from D to N at position 468.
+The protein's natural variant, known as in class 2, features a modification of the amino acid from G to R at position 503.
+The protein's natural variant, known as in class 2 and class 3, features a modification of the amino acid from H to P at position 586.
+The protein's natural variant, known as in strain: V34, features a modification of the amino acid from FM to LV at position 210.
+The protein's natural variant, known as in strain: V34, features a modification of the amino acid from A to Y at position 288.
+The protein's natural variant, known as in strain: V34, features a modification of the amino acid from FA to GL at position 428.
+The protein's natural variant, known as in DKCD; unknown pathological significance, features a modification of the amino acid from E to K at position 87.
+The protein's natural variant, known as in DKCD; unknown pathological significance, features a modification of the amino acid from Q to H at position 160.
+The protein's natural variant, known as in NEDSG; decreased ability to form thioester bond with UFM1; decreased protein ufmylation;, features a modification of the amino acid from R to Q at position 23.
+The protein's natural variant, known as in NEDSG; decreased ability to form thioester bond with UFM1; decreased protein ufmylation;, features a modification of the amino acid from T to I at position 106.
+The protein's natural variant, known as in a mutant cell line defective in DNA repair, features a modification of the amino acid from E to K at position 102.
+The protein's natural variant, known as in a mutant cell line defective in DNA repair, features a modification of the amino acid from C to Y at position 390.
+The protein's natural variant, known as in MC4DN17; unknown pathological significance;, features a modification of the amino acid from F to S at position 118.
+The protein's natural variant, known as in ARLIAK; unable to transport succinate, 2-oxoglutarate and N-acetylaspartate;, features a modification of the amino acid from A to D at position 254.
+The protein's natural variant, known as in ARLIAK; severely decreased transport of succinate, 2-oxoglutarate and N-acetylaspartate;, features a modification of the amino acid from G to S at position 548.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 4.
+The natural variant of this protein is characterized by an amino acid alteration from V to L at position 97.
+The natural variant of this protein is characterized by an amino acid alteration from E to D at position 187.
+The protein's natural variant, known as in FSGS9; when associated in cis with A-1076; unknown pathological significance;, features a modification of the amino acid from W to C at position 498.
+The protein's natural variant, known as in FSGS9; loss of function mutation;, features a modification of the amino acid from C to S at position 620.
+The protein's natural variant, known as in FSGS9;, features a modification of the amino acid from R to C at position 628.
+The protein's natural variant, known as in FSGS9; moderate loss of function mutation;, features a modification of the amino acid from C to S at position 629.
+The protein's natural variant, known as in VMCKD;, features a modification of the amino acid from R to W at position 633.
+The protein's natural variant, known as in VMCKD; when associated in cis with K-800; unknown pathological significance. In FSGS9; when associated in cis with K-800; unknown pathological significance;, features a modification of the amino acid from E to A at position 643.
+The protein's natural variant, known as found in a fetus with ventriculomegaly with cystic kidney disease; unknown pathological significance;, features a modification of the amino acid from A to P at position 654.
+The protein's natural variant, known as in VMCKD. In VMCKD; when associated in cis with A-643; unknown pathological significance. In FSGS9; when associated in cis with K-643; unknown pathological significance;, features a modification of the amino acid from N to K at position 800.
+The protein's natural variant, known as in FSGS9; when associated in cis with C-628; unknown pathological significance, features a modification of the amino acid from G to W at position 839.
+The protein's natural variant, known as in FSGS9; when associated in cis with S-1064 and 149-E--I-1285 del; unknown pathological significance;, features a modification of the amino acid from T to M at position 902.
+The protein's natural variant, known as in FSGS9; when associated in cis with M-902 and 149-E--I-1285 del; unknown pathological significance;, features a modification of the amino acid from P to S at position 1064.
+The protein's natural variant, known as in FSGS9; when associated in cis with C-498; unknown pathological significance, features a modification of the amino acid from D to A at position 1076.
+The protein's natural variant, known as in FSGS9; when associated in cis with 1098-C--I-1285 del; unknown pathological significance;, features a modification of the amino acid from R to C at position 1115.
+The protein's natural variant, known as in FSGS9; unknown pathological significance, features a modification of the amino acid from C to R at position 1129.
+The protein's natural variant, known as in FSGS9; unknown pathological significance, features a modification of the amino acid from N to T at position 1184.
+The protein's natural variant, known as in RP; unknown pathological significance; reduces protein stability and expression, features a modification of the amino acid from R to G at position 1249.
+The protein's natural variant, known as in FSGS9;, features a modification of the amino acid from R to Q at position 1249.
+The protein's natural variant, known as in DESMOS; decreases production of cholesterol from desmosterol;, features a modification of the amino acid from R to H at position 94.
+The protein's natural variant, known as in DESMOS; decreases production of cholesterol from desmosterol;, features a modification of the amino acid from E to K at position 191.
+The protein's natural variant, known as in DESMOS; decreases production of cholesterol from desmosterol;, features a modification of the amino acid from N to T at position 294.
+The protein's natural variant, known as in DESMOS; decreases production of cholesterol from desmosterol;, features a modification of the amino acid from K to N at position 306.
+The protein's natural variant, known as in DESMOS; complete loss of ability to convert desmosterol to cholesterol;, features a modification of the amino acid from Y to S at position 471.
+The protein's natural variant, known as in DESMOS; decreases production of cholesterol from desmosterol;, features a modification of the amino acid from E to K at position 480.
+The protein's natural variant, known as found in a renal cell carcinoma sample; somatic mutation, features a modification of the amino acid from Q to K at position 39.
+The protein's natural variant, known as in strain: CWL029 and TW-183, features a modification of the amino acid from V to I at position 19.
+The protein's natural variant, known as in allele FABA6; TS, features a modification of the amino acid from P to L at position 76.
+The protein's natural variant, known as in allele FABA2; TS, features a modification of the amino acid from G to D at position 102.
+The protein's natural variant, known as found in a family with intellectual disability; unknown pathological significance;, features a modification of the amino acid from N to S at position 64.
+The protein's natural variant, known as in variant S, features a modification of the amino acid from K to R at position 16.
+The protein's natural variant, known as in DEE100; unknown pathological significance, features a modification of the amino acid from L to R at position 64.
+The protein's natural variant, known as in DEE100; unknown pathological significance, features a modification of the amino acid from A to P at position 66.
+The protein's natural variant, known as found in a renal cell carcinoma case; somatic mutation, features a modification of the amino acid from P to H at position 345.
+The protein's natural variant, known as in DEE100, features a modification of the amino acid from R to G at position 348.
+The protein's natural variant, known as in DEE100;, features a modification of the amino acid from R to L at position 348.
+The protein's natural variant, known as in strain: N'Dama, features a modification of the amino acid from F to C at position 48.
+The protein's natural variant, known as in strain: CN15X, features a modification of the amino acid from H to Y at position 530.
+The protein's natural variant, known as in strain: MS11 / V18, features a modification of the amino acid from N to D at position 92.
+The protein's natural variant, known as in HPMRS4; results in loss of function; the mutant localizes to the Golgi apparatus as the wild-type;, features a modification of the amino acid from G to D at position 92.
+The protein's natural variant, known as in HPMRS4; results in partial functional impairment; the mutant does not localize to the Golgi apparatus but is retained in the endoplasmic reticulum;, features a modification of the amino acid from P to R at position 105.
+The protein's natural variant, known as found in a patient with Toriello-Carey syndrome; unknown pathological significance;, features a modification of the amino acid from H to Y at position 284.
+The protein's natural variant, known as in HPMRS4; results in partial functional impairment; the mutant does not localize to the Golgi apparatus but is retained in the endoplasmic reticulum;, features a modification of the amino acid from D to G at position 305.
+The protein's natural variant, known as in strain: NCTC 11637 and NCTC 11638, features a modification of the amino acid from T to A at position 122.
+The protein's natural variant, known as in strain: 80190; quinolone-resistant, features a modification of the amino acid from S to F at position 464.
+The protein's natural variant, known as in strain: cv. Borszczagowski, features a modification of the amino acid from V to G at position 154.
+The protein's natural variant, known as in strain: cv. Borszczagowski, features a modification of the amino acid from T to S at position 170.
+The protein's natural variant, known as in strain: cv. Borszczagowski, features a modification of the amino acid from C to G at position 175.
+The protein's natural variant, known as in strain: cv. Borszczagowski, features a modification of the amino acid from G to A at position 201.
+The protein's natural variant, known as in strain: cv. Borszczagowski, features a modification of the amino acid from T to I at position 513.
+The protein's natural variant, known as in strain: cv. Borszczagowski, features a modification of the amino acid from F to C at position 748.
+The natural variant of this protein is characterized by an amino acid alteration from D to A at position 11.
+The protein's natural variant, known as in MT-C4D; affect the stability of the COX complex;, features a modification of the amino acid from M to K at position 29.
+The natural variant of this protein is characterized by an amino acid alteration from L to P at position 123.
+The protein's natural variant, known as in colorectal cancer;, features a modification of the amino acid from V to M at position 142.
+The natural variant of this protein is characterized by an amino acid alteration from T to M at position 187.
+The protein's natural variant, known as in HCVAD; decreased beta-carotene 15,15'-monooxygenase activity; 90% decrease compared to wild-type; decreased catalytic efficiency; no effect on affinity for all-trans-beta-carotene;, features a modification of the amino acid from T to M at position 170.
+The protein's natural variant, known as in strain: 129Sv, features a modification of the amino acid from G to S at position 23.
+The natural variant of this protein is characterized by an amino acid alteration from M to L at position 239.
+The protein's natural variant, known as in a breast pleomorphic lobular carcinoma sample; somatic mutation, features a modification of the amino acid from E to Q at position 419.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from E to G at position 1199.
+The protein's natural variant, known as in breast cancer samples; infiltrating ductal carcinoma; somatic mutation, features a modification of the amino acid from Q to E at position 1799.
+The protein's natural variant, known as in a breast pleomorphic lobular carcinoma sample; somatic mutation, features a modification of the amino acid from S to C at position 2190.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation, features a modification of the amino acid from F to L at position 2362.
+The protein's natural variant, known as in PAPRS, features a modification of the amino acid from D to G at position 2.
+The protein's natural variant, known as probable disease-associated variant found in a patient with non-syndromic renal hypodysplasia;, features a modification of the amino acid from G to E at position 24.
+The protein's natural variant, known as in PAPRS, features a modification of the amino acid from G to V at position 25.
+The protein's natural variant, known as in PAPRS, features a modification of the amino acid from L to R at position 33.
+The protein's natural variant, known as in FSGS7; decreased DNA-binding capability and transactivation ability;, features a modification of the amino acid from R to Q at position 56.
+The protein's natural variant, known as in PAPRS, features a modification of the amino acid from S to I at position 61.
+The protein's natural variant, known as in PAPRS, features a modification of the amino acid from S to N at position 61.
+The protein's natural variant, known as in PAPRS, features a modification of the amino acid from L to P at position 69.
+The protein's natural variant, known as in PAPRS;, features a modification of the amino acid from R to T at position 71.
+The protein's natural variant, known as in PAPRS, features a modification of the amino acid from T to TET at position 75.
+The protein's natural variant, known as in PAPRS, features a modification of the amino acid from T to TT at position 75.
+The protein's natural variant, known as in PAPRS;, features a modification of the amino acid from G to S at position 76.
+The protein's natural variant, known as in FSGS7; decreased DNA-binding capability and transactivation ability;, features a modification of the amino acid from P to L at position 80.
+The protein's natural variant, known as in PAPRS, features a modification of the amino acid from G to GSIKPGVIG at position 84.
+The protein's natural variant, known as in PAPRS, features a modification of the amino acid from G to S at position 84.
+The protein's natural variant, known as in PAPRS;, features a modification of the amino acid from R to P at position 117.
+The protein's natural variant, known as in PAPRS, features a modification of the amino acid from P to H at position 130.
+The protein's natural variant, known as in PAPRS, features a modification of the amino acid from P to S at position 130.
+The protein's natural variant, known as in FSGS7; decreased DNA-binding capability and transactivation ability, features a modification of the amino acid from S to F at position 133.
+The protein's natural variant, known as in PAPRS, features a modification of the amino acid from I to V at position 139.
+The protein's natural variant, known as in FSGS7;, features a modification of the amino acid from T to A at position 150.
+The protein's natural variant, known as in FSGS7;, features a modification of the amino acid from T to N at position 164.
+The natural variant of this protein is characterized by an amino acid alteration from S to T at position 175.
+The protein's natural variant, known as in FSGS7; transactivation activity is dramatically decreased in presence of TLE4; dramatically enhances interaction with TLE4;, features a modification of the amino acid from G to R at position 189.
+The protein's natural variant, known as in PAPRS;, features a modification of the amino acid from A to V at position 295.
+The protein's natural variant, known as in PAPRS, features a modification of the amino acid from L to P at position 296.
+The protein's natural variant, known as in PAPRS;, features a modification of the amino acid from P to S at position 298.
+The protein's natural variant, known as in PAPRS, features a modification of the amino acid from T to A at position 329.
+The protein's natural variant, known as found in a patient with bilateral optic nerve colobomas; uncertain pathological significance;, features a modification of the amino acid from S to N at position 387.
+The protein's natural variant, known as in CED1; perturbed ciliary protein trafficking; no effect on interaction with ITF43:WDR35; fail to assemble IFT-A complex at the cilia base; no effect on ciliogenesis;, features a modification of the amino acid from W to C at position 7.
+The protein's natural variant, known as in CED1; no effect on interaction with ITF43:WDR35;, features a modification of the amino acid from S to F at position 322.
+The protein's natural variant, known as in CED1; unknown pathological significance;, features a modification of the amino acid from V to L at position 391.
+The protein's natural variant, known as in CED1; strongly decreases interaction with ITF43:WDR35;, features a modification of the amino acid from G to R at position 495.
+The protein's natural variant, known as in CED1; strongly decreases interaction with ITF43:WDR35;, features a modification of the amino acid from V to G at position 502.
+The protein's natural variant, known as in CED1; unknown pathological significance, features a modification of the amino acid from F to C at position 570.
+The protein's natural variant, known as in CED1; decreased ciliogenesis; perturbed ciliary protein trafficking; strongly decreases interaction with ITF43:WDR35; fail to assemble IFT-A complex at the cilia base;, features a modification of the amino acid from G to V at position 572.
+The protein's natural variant, known as in CED1; unknown pathological significance;, features a modification of the amino acid from L to P at position 712.
+The protein's natural variant, known as in EJM1; associated with H-221; reduces substantially the cell death effect; reduces partly the calcium influx; binds to CACNA1E;, features a modification of the amino acid from P to T at position 77.
+The protein's natural variant, known as in EJM1; no effect on protein expression; defective mitotic spindle organization; defective cytokinesis;, features a modification of the amino acid from H to R at position 89.
+The protein's natural variant, known as in EJM1;, features a modification of the amino acid from R to C at position 118.
+The protein's natural variant, known as in EJM1; unknown pathological significance;, features a modification of the amino acid from R to Q at position 153.
+The protein's natural variant, known as no effect on cell death; binds to CACNA1E as the wild type protein; does not affect subcellular location;, features a modification of the amino acid from R to W at position 159.
+The protein's natural variant, known as associated with susceptibility to JAE1;, features a modification of the amino acid from I to V at position 174.
+The protein's natural variant, known as in EJM1; unknown pathological significance;, features a modification of the amino acid from R to C at position 182.
+The protein's natural variant, known as benign variant; no effect on cell death; binds to CACNA1E;, features a modification of the amino acid from R to H at position 182.
+The protein's natural variant, known as in EJM1; reduces substantially the cell death effect; reduces partly the calcium influx; normally binds to CACNA1E; does not affect subcellular location; results in impaired cell migration;, features a modification of the amino acid from D to N at position 210.
+The protein's natural variant, known as in EJM1; associated with T-77; reduces substantially the cell death effect; reduces partly the calcium influx; normally binds to CACNA1E; does not affect subcellular location; results in impaired cell migration;, features a modification of the amino acid from R to H at position 221.
+The protein's natural variant, known as in EJM1; uncertain pathological significance; also found at homozygosity in neonatal intractable epilepsy; reduces substantially the cell death effect; reduces significantly the calcium influx; normally binds to CACNA1E; does not affect subcellular location; results in impaired cell migration;, features a modification of the amino acid from F to L at position 229.
+The protein's natural variant, known as in EJM1; reduces substantially the cell death effect; reduces partly the calcium influx; normally binds to CACNA1E; does not affect subcellular location; results in impaired cell migration;, features a modification of the amino acid from D to Y at position 253.
+The protein's natural variant, known as associated with susceptibility to JAE1;, features a modification of the amino acid from C to Y at position 259.
+The protein's natural variant, known as in EJM1; no effect on protein expression; defective mitotic spindle organization; defective cytokinesis, features a modification of the amino acid from E to K at position 322.
+The protein's natural variant, known as in EJM1; no effect on protein expression; no effect on the spindle pole localization; defective mitotic spindle organization; defective cytokinesis;, features a modification of the amino acid from R to W at position 353.
+The protein's natural variant, known as in EJM1; no effect on protein expression; defective mitotic spindle organization; defective cytokinesis;, features a modification of the amino acid from Y to C at position 355.
+The protein's natural variant, known as in EJM1; no effect on protein expression; defective mitotic spindle organization; defective cytokinesis;, features a modification of the amino acid from R to W at position 372.
+The protein's natural variant, known as in EJM1; no effect on protein expression; defective mitotic spindle organization; defective cytokinesis, features a modification of the amino acid from K to E at position 378.
+The protein's natural variant, known as in a sporadic case of unclassified epilepsy, features a modification of the amino acid from A to S at position 394.
+The protein's natural variant, known as in EJM1; no effect on protein expression; defective mitotic spindle organization; defective cytokinesis;, features a modification of the amino acid from R to C at position 436.
+The protein's natural variant, known as in EJM1; no effect on protein expression; defective mitotic spindle organization; defective cytokinesis;, features a modification of the amino acid from Y to H at position 485.
+The protein's natural variant, known as in EJM1; no effect on protein expression; defective mitotic spindle organization; defective cytokinesis;, features a modification of the amino acid from N to S at position 519.
+The protein's natural variant, known as in EJM1; no effect on protein expression; defective mitotic spindle organization; defective cytokinesis;, features a modification of the amino acid from V to L at position 556.
+The protein's natural variant, known as no effect on cell death; normally binds to CACNA1E; does not affect subcellular location;, features a modification of the amino acid from I to L at position 619.
+The protein's natural variant, known as in EJM1; no effect on protein expression; defective mitotic spindle organization; defective cytokinesis;, features a modification of the amino acid from I to S at position 619.
+The protein's natural variant, known as in EJM1; no effect on protein expression; defective mitotic spindle organization; defective cytokinesis;, features a modification of the amino acid from Y to C at position 631.
+The protein's natural variant, known as in BOR2; affects Eya1 binding and the ability to activate gene transcription;, features a modification of the amino acid from A to T at position 158.
+The protein's natural variant, known as in BOR2;, features a modification of the amino acid from A to T at position 296.
+The protein's natural variant, known as in BOR2;, features a modification of the amino acid from G to R at position 365.
+The protein's natural variant, known as in BOR2; affects Eya1 binding and the ability to activate gene transcription;, features a modification of the amino acid from T to M at position 552.
+The protein's natural variant, known as in strain: D4 and YF+, features a modification of the amino acid from T to S at position 203.
+The protein's natural variant, known as in strain: D4; loss of activity, features a modification of the amino acid from S to L at position 467.
+The protein's natural variant, known as in strain: D4 and YF+, features a modification of the amino acid from G to R at position 517.
+The protein's natural variant, known as in strain: cv. Doongara, cv. Habataki, cv. IR24 and cv. Milyang 23; allele sd-1; semidwarfing, features a modification of the amino acid from EHG to ARR at position 102.
+The protein's natural variant, known as in strain: cv. Zu-0, features a modification of the amino acid from F to L at position 266.
+The protein's natural variant, known as in strain: cv. Bur-0 and cv. Wu-0, features a modification of the amino acid from A to D at position 287.
+The protein's natural variant, known as in strain: cv. Bur-0 and cv. Wu-0, features a modification of the amino acid from N to I at position 326.
+The protein's natural variant, known as in strain: cv. Bur-0 and cv. Wu-0, features a modification of the amino acid from I to T at position 361.
+The protein's natural variant, known as in strain: cv. Mt-0, features a modification of the amino acid from E to K at position 366.
+The protein's natural variant, known as in strain: cv. Bur-0 and cv. Wu-0, features a modification of the amino acid from KI to ET at position 372.
+The protein's natural variant, known as in CMT1B;, features a modification of the amino acid from I to M at position 30.
+The protein's natural variant, known as in CMT1B; severe, features a modification of the amino acid from V to F at position 32.
+The protein's natural variant, known as in CMT1B, features a modification of the amino acid from T to I at position 34.
+The protein's natural variant, known as in CMT1B and CMTDID;, features a modification of the amino acid from D to Y at position 35.
+The protein's natural variant, known as in CMT1B; slightly reduces intercellular adhesion; does not affect targeting to the cell membrane;, features a modification of the amino acid from H to P at position 39.
+The protein's natural variant, known as in CMT2I and CMT1B;, features a modification of the amino acid from S to F at position 44.
+The protein's natural variant, known as in CMT1B;, features a modification of the amino acid from S to F at position 51.
+The protein's natural variant, known as in CMT1B; severe, features a modification of the amino acid from S to C at position 54.
+The protein's natural variant, known as in CMT1B, features a modification of the amino acid from S to P at position 54.
+The protein's natural variant, known as in CMT2, features a modification of the amino acid from E to K at position 56.
+The protein's natural variant, known as in CMT1B; moderate, features a modification of the amino acid from V to F at position 58.
+The protein's natural variant, known as in CMT2I;, features a modification of the amino acid from D to H at position 60.
+The protein's natural variant, known as in CMT2I;, features a modification of the amino acid from D to G at position 61.
+The protein's natural variant, known as in CMT1B;, features a modification of the amino acid from I to F at position 62.
+The protein's natural variant, known as in CMT2I;, features a modification of the amino acid from I to M at position 62.
+The protein's natural variant, known as in DSS;, features a modification of the amino acid from S to C at position 63.
+The protein's natural variant, known as in CMT1B;, features a modification of the amino acid from S to F at position 63.
+The protein's natural variant, known as in CMT1B;, features a modification of the amino acid from T to A at position 65.
+The protein's natural variant, known as in CMT1B, features a modification of the amino acid from T to I at position 65.
+The protein's natural variant, known as in CMT1B; severe/mild, features a modification of the amino acid from Y to C at position 68.
+The protein's natural variant, known as in CMT2J and CMT2I;, features a modification of the amino acid from D to V at position 75.
+The protein's natural variant, known as in CMT1B; severe;, features a modification of the amino acid from S to L at position 78.
+The protein's natural variant, known as in CMT1B;, features a modification of the amino acid from S to W at position 78.
+The protein's natural variant, known as in CMT1B and CMT2I; severe; reduces intercellular adhesion; does not affect targeting to the cell membrane;, features a modification of the amino acid from H to R at position 81.
+The protein's natural variant, known as in CMT; associated with F-113;, features a modification of the amino acid from H to Y at position 81.
+The protein's natural variant, known as in CMT1B and DSS;, features a modification of the amino acid from Y to C at position 82.
+The protein's natural variant, known as in CMT2I; patient carrying also Met-92 and Met-162;, features a modification of the amino acid from I to N at position 89.
+The protein's natural variant, known as in CMT1B;, features a modification of the amino acid from D to E at position 90.
+The protein's natural variant, known as in CMT2I; patient carrying also Asn-89 and Met-162;, features a modification of the amino acid from V to M at position 92.
+The protein's natural variant, known as in CMT1B;, features a modification of the amino acid from G to E at position 93.
+The protein's natural variant, known as in CMT1B;, features a modification of the amino acid from K to E at position 96.
+The protein's natural variant, known as in CMT2J;, features a modification of the amino acid from E to V at position 97.
+The protein's natural variant, known as in CMT1B and DSS; severe;, features a modification of the amino acid from R to C at position 98.
+The protein's natural variant, known as in CMT1B;, features a modification of the amino acid from R to H at position 98.
+The protein's natural variant, known as in CMT1B;, features a modification of the amino acid from R to P at position 98.
+The protein's natural variant, known as in CMT1B, features a modification of the amino acid from R to S at position 98.
+The protein's natural variant, known as in CMT1B, features a modification of the amino acid from I to T at position 99.
+The protein's natural variant, known as in CMT1B, features a modification of the amino acid from W to C at position 101.
+The protein's natural variant, known as in CMT1B;, features a modification of the amino acid from G to E at position 103.
+The protein's natural variant, known as in CMT1B;, features a modification of the amino acid from D to N at position 109.
+The protein's natural variant, known as in DSS, features a modification of the amino acid from G to D at position 110.
+The protein's natural variant, known as in CMT1B; severe;, features a modification of the amino acid from I to T at position 112.
+The protein's natural variant, known as in CMT; unclassified; associated with Y-81;, features a modification of the amino acid from V to F at position 113.
+The protein's natural variant, known as in CMT2, features a modification of the amino acid from V to I at position 113.
+The protein's natural variant, known as in DSS; associated on the same allele as His-116 and Asn-128 in one patient;, features a modification of the amino acid from I to T at position 114.
+The protein's natural variant, known as in DSS; associated on the same allele as Thr-114 and Asn-128 in one patient;, features a modification of the amino acid from N to H at position 116.
+The protein's natural variant, known as in DSS, features a modification of the amino acid from D to DFY at position 118.
+The protein's natural variant, known as in CMT2I, features a modification of the amino acid from D to N at position 118.
+The protein's natural variant, known as in CMT2I;, features a modification of the amino acid from Y to C at position 119.
+The protein's natural variant, known as in CMT1B; loss of glycosylation site, features a modification of the amino acid from N to S at position 122.
+The protein's natural variant, known as in DSS and CMT1B, features a modification of the amino acid from G to C at position 123.
+The protein's natural variant, known as in CHN2;, features a modification of the amino acid from T to K at position 124.
+The protein's natural variant, known as in CMT1B, CMT2I and CMT2J; CMTJ2 patients present Adie pupil; slightly reduces intercellular adhesion; does not affect targeting to the cell membrane; affects glycosylation;, features a modification of the amino acid from T to M at position 124.
+The protein's natural variant, known as in DSS, features a modification of the amino acid from C to Y at position 127.
+The protein's natural variant, known as in CMT1B, features a modification of the amino acid from D to E at position 128.
+The protein's natural variant, known as in DSS; associated on the same allele as Thr-114 and His-116 in one patient;, features a modification of the amino acid from D to N at position 128.
+The protein's natural variant, known as in CMT1B, CMT2I and DSS;, features a modification of the amino acid from K to R at position 130.
+The protein's natural variant, known as in ROULS;, features a modification of the amino acid from N to K at position 131.
+The protein's natural variant, known as in CMT1B; moderate, features a modification of the amino acid from P to L at position 132.
+The protein's natural variant, known as in CMT1B, features a modification of the amino acid from D to E at position 134.
+The protein's natural variant, known as in CMT1B, features a modification of the amino acid from D to G at position 134.
+The protein's natural variant, known as in CMT1B;, features a modification of the amino acid from D to N at position 134.
+The protein's natural variant, known as in CMT1B and DSS;, features a modification of the amino acid from I to L at position 135.
+The protein's natural variant, known as in CMT1B;, features a modification of the amino acid from I to T at position 135.
+The protein's natural variant, known as in DSS, features a modification of the amino acid from V to E at position 136.
+The protein's natural variant, known as in CMT1B;, features a modification of the amino acid from G to S at position 137.
+The protein's natural variant, known as in CMT1B, features a modification of the amino acid from K to N at position 138.
+The protein's natural variant, known as in CMT1B, features a modification of the amino acid from T to N at position 139.
+The protein's natural variant, known as in CMT1B;, features a modification of the amino acid from S to T at position 140.
+The protein's natural variant, known as in CMT1B;, features a modification of the amino acid from T to M at position 143.
+The protein's natural variant, known as in CMT1B;, features a modification of the amino acid from Y to S at position 145.
+The protein's natural variant, known as in CMT1B, features a modification of the amino acid from V to F at position 146.
+The protein's natural variant, known as in CMT2I; patient carrying also Asn-89 and Met-92;, features a modification of the amino acid from I to M at position 162.
+The protein's natural variant, known as in CMT1B;, features a modification of the amino acid from G to R at position 163.
+The protein's natural variant, known as in CMT1B and DSS; severe, features a modification of the amino acid from G to A at position 167.
+The protein's natural variant, known as in CMT2I and DSS;, features a modification of the amino acid from G to R at position 167.
+The protein's natural variant, known as in CMT1B, features a modification of the amino acid from L to R at position 170.
+The protein's natural variant, known as in CMT1B; referred to as 'T216ER', features a modification of the amino acid from T to ER at position 216.
+The protein's natural variant, known as in DSS, features a modification of the amino acid from A to T at position 221.
+The protein's natural variant, known as in CMT1B; also in two asymptomatic individuals from the same family;, features a modification of the amino acid from D to Y at position 224.
+The protein's natural variant, known as in CMT1B, features a modification of the amino acid from R to S at position 227.
+The protein's natural variant, known as in CMT2I, features a modification of the amino acid from K to E at position 236.
+The natural variant of this protein is characterized by an amino acid alteration from R to C at position 121.
+The protein's natural variant, known as in HSAN1C; reduced activity with L-serine as substrate; increased activity toward L-alanine resulting in the accumulation of 1-deoxy-sphinganine;, features a modification of the amino acid from A to P at position 182.
+The protein's natural variant, known as in HSAN1C; late onset; slightly increased activity with L-serine as substrate; highly increased activity toward L-alanine resulting in the accumulation of 1-deoxy-sphinganine;, features a modification of the amino acid from R to W at position 183.
+The protein's natural variant, known as in HSAN1C; partial loss of normal activity as measured by reduced formation of sphinganine; affects enzymatic affinity resulting in the accumulation of the alternative metabolite 1-deoxy-sphinganine;, features a modification of the amino acid from V to M at position 359.
+The protein's natural variant, known as in HSAN1C; complete loss of normal activity as measured by lack of formation of sphinganine; affects enzymatic affinity resulting in the accumulation of the alternative metabolite 1-deoxy-sphinganine;, features a modification of the amino acid from G to V at position 382.
+The protein's natural variant, known as in HSAN1C; partial loss of normal activity as measured by reduced formation of sphinganine; affects enzymatic affinity resulting in the accumulation of the alternative metabolite 1-deoxy-sphinganine;, features a modification of the amino acid from I to F at position 504.
+The protein's natural variant, known as in SPG82; unknown pathological significance, features a modification of the amino acid from H to Y at position 226.
+The protein's natural variant, known as in SPG82; unknown pathological significance;, features a modification of the amino acid from P to L at position 289.
+The protein's natural variant, known as in XLID93; unknown pathological significance;, features a modification of the amino acid from K to E at position 1596.
+The protein's natural variant, known as in IBGC8;, features a modification of the amino acid from R to H at position 108.
+The protein's natural variant, known as in IBGC8; loss of localization to the plasma membrane; mainly retained in the cytoplasm;, features a modification of the amino acid from W to C at position 168.
+The protein's natural variant, known as in MSUD1A;, features a modification of the amino acid from R to W at position 159.
+The protein's natural variant, known as in MSUD1A, features a modification of the amino acid from Q to K at position 190.
+The protein's natural variant, known as in MSUD1A;, features a modification of the amino acid from T to M at position 211.
+The protein's natural variant, known as in MSUD1A;, features a modification of the amino acid from A to V at position 220.
+The protein's natural variant, known as in MSUD1A;, features a modification of the amino acid from A to T at position 253.
+The protein's natural variant, known as in MSUD1A;, features a modification of the amino acid from G to R at position 290.
+The protein's natural variant, known as in MSUD1A, features a modification of the amino acid from I to T at position 326.
+The protein's natural variant, known as in MSUD1A;, features a modification of the amino acid from R to C at position 346.
+The protein's natural variant, known as in MSUD1A, features a modification of the amino acid from P to PKP at position 403.
+The protein's natural variant, known as in MSUD1A;, features a modification of the amino acid from F to C at position 409.
+The protein's natural variant, known as in MSUD1A, features a modification of the amino acid from Y to C at position 413.
+The protein's natural variant, known as in MSUD1A, features a modification of the amino acid from LA to P at position 428.
+The protein's natural variant, known as in MSUD1A; impedes assembly of the E1 component;, features a modification of the amino acid from Y to N at position 438.
+The protein's natural variant, known as in strain: cv. Bla-1 and cv. Bu-0, features a modification of the amino acid from Y to S at position 147.
+The protein's natural variant, known as in strain: cv. Bla-1 and cv. Bu-0, features a modification of the amino acid from T to A at position 172.
+The protein's natural variant, known as in strain: cv. Bretagny, features a modification of the amino acid from N to I at position 190.
+The protein's natural variant, known as in strain: cv. Bla-1 and cv. Bu-0, features a modification of the amino acid from I to L at position 191.
+The protein's natural variant, known as in strain: cv. Bla-1 and cv. Bu-0, features a modification of the amino acid from IT to TA at position 210.
+The protein's natural variant, known as in strain: AF10, features a modification of the amino acid from M to T at position 18.
+The protein's natural variant, known as in strain: AF10, features a modification of the amino acid from T to A at position 110.
+The protein's natural variant, known as in strain: AF10, features a modification of the amino acid from T to V at position 130.
+The protein's natural variant, known as in strain: AF10, features a modification of the amino acid from D to N at position 292.
+The protein's natural variant, known as in strain: AF10, features a modification of the amino acid from A to E at position 371.
+The protein's natural variant, known as in strain: AF10, features a modification of the amino acid from N to K at position 419.
+The protein's natural variant, known as in strain: AF10, features a modification of the amino acid from I to T at position 437.
+The protein's natural variant, known as in strain: AF10, features a modification of the amino acid from G to D at position 455.
+The protein's natural variant, known as requires 2 nucleotide substitutions, features a modification of the amino acid from C to Q at position 54.
+The natural variant of this protein is characterized by an amino acid alteration from P to A at position 59.
+The protein's natural variant, known as in ARCI3; no effect on enzyme activity;, features a modification of the amino acid from L to M at position 237.
+The protein's natural variant, known as in ARCI3; complete loss of the enzyme activity;, features a modification of the amino acid from G to V at position 281.
+The protein's natural variant, known as in ARCI3; complete loss of the enzyme activity, features a modification of the amino acid from QYVA to P at position 347.
+The protein's natural variant, known as in ARCI3; complete loss of the enzyme activity;, features a modification of the amino acid from R to S at position 396.
+The protein's natural variant, known as in ARCI3;, features a modification of the amino acid from L to P at position 427.
+The protein's natural variant, known as in ARCI3; complete loss of the enzyme activity;, features a modification of the amino acid from V to F at position 500.
+The protein's natural variant, known as in ARCI3; complete loss of the enzyme activity;, features a modification of the amino acid from P to L at position 630.
+The protein's natural variant, known as in CFC4;, features a modification of the amino acid from F to C at position 57.
+The protein's natural variant, known as in CFC4;, features a modification of the amino acid from F to V at position 57.
+The protein's natural variant, known as in CFC4; results in increased kinase activity;, features a modification of the amino acid from P to Q at position 128.
+The protein's natural variant, known as in CFC4;, features a modification of the amino acid from Y to H at position 134.
+The protein's natural variant, known as in NPHS16; increased interaction with ARHGDIA; loss of function in regulation of the Rho signaling pathway; no effect on cytoplasmic localization; loss of function in podocytes migration;, features a modification of the amino acid from S to G at position 181.
+The protein's natural variant, known as in PPKWH;, features a modification of the amino acid from A to V at position 670.
+The protein's natural variant, known as in NPHS16; loss of function in regulation of the Rho signaling pathway; no effect on cytoplasmic localization; decreased function in podocytes migration;, features a modification of the amino acid from S to F at position 676.
+The protein's natural variant, known as in allele: CaO19.11256, features a modification of the amino acid from S to STKHGKVDDSS at position 305.
+The protein's natural variant, known as in 20% of the molecules, features a modification of the amino acid from I to V at position 116.
+The protein's natural variant, known as in strain: ATCC 49503, features a modification of the amino acid from N to S at position 4.
+The protein's natural variant, known as in strain: ATCC 49503, features a modification of the amino acid from L to F at position 9.
+The protein's natural variant, known as in strain: ATCC 49503, features a modification of the amino acid from G to W at position 11.
+The protein's natural variant, known as in strain: ATCC 49503, features a modification of the amino acid from T to A at position 17.
+The protein's natural variant, known as in strain: ATCC 49503, features a modification of the amino acid from G to S at position 91.
+The protein's natural variant, known as in strain: ATCC 49503, features a modification of the amino acid from K to Q at position 194.
+The protein's natural variant, known as in strain: ATCC 49503, features a modification of the amino acid from K to N at position 199.
+The protein's natural variant, known as in strain: ATCC 49503, features a modification of the amino acid from S to G at position 235.
+The protein's natural variant, known as in OFD16; does not affect subcellular location at ciliary transition zone;, features a modification of the amino acid from E to G at position 45.
+The protein's natural variant, known as in strain: 72, features a modification of the amino acid from S to SHP at position 25.
+The protein's natural variant, known as in strain: 2, 47 and 58, features a modification of the amino acid from M to R at position 52.
+The protein's natural variant, known as in strain: 72, features a modification of the amino acid from T to I at position 270.
+The protein's natural variant, known as in strain: 72, features a modification of the amino acid from Y to S at position 276.
+The protein's natural variant, known as in IMD80; no effect on the formation of the replisome, features a modification of the amino acid from R to C at position 427.
+The protein's natural variant, known as in UVSS3; mild phenotype; impairs transcription-coupled nucleotide excision repair ability;, features a modification of the amino acid from C to R at position 32.
+The protein's natural variant, known as in NRCLP1; early-onset; impaired trafficking and processing;, features a modification of the amino acid from L to R at position 16.
+The natural variant of this protein is characterized by an amino acid alteration from S to T at position 227.
+The protein's natural variant, known as in strain: 777-3A, features a modification of the amino acid from I to T at position 122.
+The protein's natural variant, known as in strain: Capensis / YB4237, features a modification of the amino acid from N to D at position 221.
+The protein's natural variant, known as in strain: Capensis / YB4237, features a modification of the amino acid from M to T at position 315.
+The protein's natural variant, known as in strain: 777-3A, features a modification of the amino acid from I to M at position 324.
+The protein's natural variant, known as in strain: Capensis / YB4237, features a modification of the amino acid from T to A at position 355.
+The protein's natural variant, known as in strain: Capensis / YB4237, features a modification of the amino acid from T to H at position 382.
+The protein's natural variant, known as in strain: KCTC 0217BP, features a modification of the amino acid from A to S at position 59.
+The protein's natural variant, known as in strain: KCTC 0217BP, features a modification of the amino acid from S to N at position 86.
+The protein's natural variant, known as in strain: KCTC 0217BP, features a modification of the amino acid from V to A at position 91.
+The protein's natural variant, known as in strain: KCTC 0217BP, features a modification of the amino acid from V to I at position 193.
+The protein's natural variant, known as in strain: KCTC 0217BP, features a modification of the amino acid from N to S at position 231.
+The protein's natural variant, known as in strain: KCTC 0217BP, features a modification of the amino acid from M to I at position 258.
+The protein's natural variant, known as in strain: KCTC 0217BP, features a modification of the amino acid from N to D at position 270.
+The protein's natural variant, known as in strain: KCTC 0217BP, features a modification of the amino acid from I to V at position 363.
+The protein's natural variant, known as in strain: KCTC 0217BP, features a modification of the amino acid from A to S at position 368.
+The protein's natural variant, known as in strain: KCTC 0217BP, features a modification of the amino acid from S to N at position 373.
+The protein's natural variant, known as in strain: KCTC 0217BP, features a modification of the amino acid from N to G at position 422.
+The natural variant of this protein is characterized by an amino acid alteration from G to R at position 263.
+The natural variant of this protein is characterized by an amino acid alteration from E to G at position 278.
+The natural variant of this protein is characterized by an amino acid alteration from L to P at position 304.
+The natural variant of this protein is characterized by an amino acid alteration from M to V at position 113.
+The natural variant of this protein is characterized by an amino acid alteration from R to C at position 181.
+The protein's natural variant, known as found in a patient with Meckel-Gruber like syndrome also carrying variant C-671 in BBS7; unknown pathological significance; hypomorphic variant in vitro;, features a modification of the amino acid from F to Y at position 60.
+The natural variant of this protein is characterized by an amino acid alteration from K to R at position 66.
+The protein's natural variant, known as in NPHP12; with extra-renal features; functionally null mutation in vitro, features a modification of the amino acid from W to R at position 150.
+The protein's natural variant, known as found in a patient with Bardet-Biedl syndrome; probably acts as disease modifier; the patient also carries a frameshift mutation and variant M-501 in BBS12; hypomorphic variant in vitro, features a modification of the amino acid from K to E at position 157.
+The protein's natural variant, known as in NPHP12; also found in a patient with Bardet-Biedl syndrome carrying two variants in BBS4; hypomorphic variant in vitro;, features a modification of the amino acid from P to L at position 209.
+The protein's natural variant, known as found in a patient with Meckel-Gruber like syndrome also carrying variant V-280 on the same allele and variant G-1183 in RPGRIP1L; unknown pathological significance; hypomorphic variant in vitro;, features a modification of the amino acid from Q to L at position 222.
+The protein's natural variant, known as in SRTD4 and NPHP12; also found in a patient with Bardet-Biedl syndrome carrying variants L-159 and T-346 in BBS12; also found in a patient with Meckel-Gruber syndrome carrying a homozygous variant in TMEM216; hypomorphic variant in vitro;, features a modification of the amino acid from T to S at position 231.
+The protein's natural variant, known as found in a patient with Bardet-Biedl syndrome; probably acts as disease modifier; the patient also carries a frameshift mutation and variant P-34 in BBS10; hypomorphic variant in vitro;, features a modification of the amino acid from Y to C at position 255.
+The protein's natural variant, known as found in a patient with Meckel-Gruber like syndrome also carrying L-222 on the same allele and variant G-1183 in RPGRIP1L; unknown pathological significance; hypomorphic variant in vitro;, features a modification of the amino acid from M to V at position 280.
+The protein's natural variant, known as found in a patient with Meckel-Gruber syndrome also carrying a mutation in CC2D2A; unknown pathological significance; hypomorphic variant in vitro, features a modification of the amino acid from A to S at position 327.
+The protein's natural variant, known as found in a patient with Meckel-Gruber syndrome also carrying N-1041 on the same allele; unknown pathological significance; hypomorphic variant in vitro;, features a modification of the amino acid from Y to C at position 347.
+The protein's natural variant, known as found in a patient with Bardet-Biedl syndrome; probably acts as disease modifier; the patient also carries a homozygous frameshift mutation in BBS7; hypomorphic variant in vitro;, features a modification of the amino acid from R to G at position 411.
+The protein's natural variant, known as in NPHP12; unknown pathological significance; functionally null mutation in vitro;, features a modification of the amino acid from H to R at position 566.
+The protein's natural variant, known as in JBTS11; hypomorphic variant in vitro, features a modification of the amino acid from S to N at position 591.
+The protein's natural variant, known as found in a patient with Meckel-Gruber like syndrome carrying variant D-559 in BBS1 and a variant in CC2D2A; unknown pathological significance; functionally null mutation in vitro;, features a modification of the amino acid from P to L at position 753.
+The protein's natural variant, known as in SRTD4; functionally null mutation in vitro, features a modification of the amino acid from D to Y at position 755.
+The protein's natural variant, known as in SRTD4; functionally null mutation in vitro;, features a modification of the amino acid from L to P at position 795.
+The protein's natural variant, known as found in a patient with Meckel-Gruber syndrome; unknown pathological significance; functionally null mutation in vitro;, features a modification of the amino acid from M to V at position 844.
+The protein's natural variant, known as in JBTS11; functionally null mutation in vitro;, features a modification of the amino acid from R to C at position 867.
+The protein's natural variant, known as found in a patient with Meckel-Gruber syndrome also carrying a homozygous variant in CC2D2A; also found in a patient with short-rib thoracic dysplasia without polydactyly compoud heterozygous for causative mutations in IFT81; probably acts as disease modifier; functionally null mutation in vitro;, features a modification of the amino acid from R to H at position 867.
+The protein's natural variant, known as found in a patient with Meckel-Gruber like syndrome; unknown pathological significance; hypomorphic variant in vitro;, features a modification of the amino acid from Q to R at position 869.
+The protein's natural variant, known as hypomorphic variant in vitro;, features a modification of the amino acid from R to Q at position 939.
+The protein's natural variant, known as functionally null mutation in vitro;, features a modification of the amino acid from R to W at position 939.
+The protein's natural variant, known as found in a patient with Meckel-Gruber like syndrome; also found in patients with Bardet-Bied syndrome; also found in a patient with nephronophthisis with extra-renal features; unknown pathological significance; hypomorphic variant in vitro;, features a modification of the amino acid from L to V at position 1002.
+The protein's natural variant, known as in JBTS11;, features a modification of the amino acid from M to T at position 1011.
+The protein's natural variant, known as found in a patient with Meckel-Gruber syndrome also carrying C-347 on the same allele; unknown pathological significance; functionally null mutation in vitro, features a modification of the amino acid from D to N at position 1041.
+The protein's natural variant, known as found in a patient with Bardet-Biedl syndrome; probably acts as disease modifier; the patient also carries two mutations in BBS6; hypomorphic variant in vitro;, features a modification of the amino acid from T to R at position 1103.
+The protein's natural variant, known as in NPHP12; hypomorphic variant in vitro;, features a modification of the amino acid from Y to C at position 1167.
+The protein's natural variant, known as in JBTS11; hypomorphic variant in vitro;, features a modification of the amino acid from M to V at position 1186.
+The protein's natural variant, known as found in a patient with Bardet-Biedl syndrome; probably acts as disease modifier; the patients also carries two mutations in BBS1; functionally null mutation in vitro;, features a modification of the amino acid from I to S at position 1208.
+The natural variant of this protein is characterized by an amino acid alteration from R to G at position 1311.
+The protein's natural variant, known as in PHLU;, features a modification of the amino acid from G to R at position 240.
+The protein's natural variant, known as in PHLU;, features a modification of the amino acid from E to V at position 437.
+The protein's natural variant, known as in OPTA3; unknown pathological significance;, features a modification of the amino acid from R to C at position 714.
+The natural variant of this protein is characterized by an amino acid alteration from N to I at position 320.
+The natural variant of this protein is characterized by an amino acid alteration from S to T at position 342.
+The natural variant of this protein is characterized by an amino acid alteration from D to A at position 454.
+The natural variant of this protein is characterized by an amino acid alteration from A to S at position 64.
+The natural variant of this protein is characterized by an amino acid alteration from A to S at position 38.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation, features a modification of the amino acid from V to M at position 13.
+The protein's natural variant, known as in a head & Neck squamous cell carcinoma sample; somatic mutation, features a modification of the amino acid from K to N at position 56.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from A to V at position 393.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from M to V at position 487.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from N to K at position 521.
+The natural variant of this protein is characterized by an amino acid alteration from S to A at position 337.
+The protein's natural variant, known as associated with prolonged QT interval in heart's electrical cycle; behaves like wild-type in terms of protein expression, subcellular location and shortening of heart's action potential duration, when expressed in neonatal rabbit cardiomyocytes;, features a modification of the amino acid from G to A at position 603.
+The protein's natural variant, known as in isoform C, features a modification of the amino acid from R to T at position 30.
+The protein's natural variant, known as in MRD11; results in a 50% reduction of interaction of 4.1N protein to GRIA1 compared to wild-type;, features a modification of the amino acid from P to S at position 854.
+The natural variant of this protein is characterized by an amino acid alteration from M to V at position 88.
+The natural variant of this protein is characterized by an amino acid alteration from T to A at position 168.
+The natural variant of this protein is characterized by an amino acid alteration from L to F at position 210.
+The protein's natural variant, known as in DYT35; results in decreased H/ACA small nucleolar ribonucleoproteins production when expressed in a heterologous system, features a modification of the amino acid from D to Y at position 175.
+The protein's natural variant, known as in NEDDS; results in decreased H/ACA small nucleolar ribonucleoproteins production when expressed in a heterologous system, features a modification of the amino acid from E to K at position 292.
+The protein's natural variant, known as in NEDDS; unknown pathological significance, features a modification of the amino acid from R to C at position 335.
+The protein's natural variant, known as in NEDDS; unknown pathological significance, features a modification of the amino acid from A to V at position 426.
+The protein's natural variant, known as in AUTSX6; loss of function;, features a modification of the amino acid from D to H at position 244.
+The protein's natural variant, known as in AUTSX6; unknown pathological significance;, features a modification of the amino acid from E to D at position 369.
+The protein's natural variant, known as in 30% of the molecules, features a modification of the amino acid from V to L at position 2.
+The natural variant of this protein is characterized by an amino acid alteration from R to K at position 61.
+The protein's natural variant, known as in HMAG;, features a modification of the amino acid from H to D at position 920.
+The protein's natural variant, known as in HMAG;, features a modification of the amino acid from P to L at position 1173.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from F to L at position 6.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from S to N at position 176.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from A to T at position 182.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from L to R at position 225.
+The protein's natural variant, known as in AI3A; mild form;, features a modification of the amino acid from G to C at position 557.
+The protein's natural variant, known as in traD39; temperature-sensitive, features a modification of the amino acid from P to L at position 396.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from V to M at position 411.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from I to T at position 165.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from A to G at position 690.
+The protein's natural variant, known as in SNDI;, features a modification of the amino acid from Q to P at position 391.
+The natural variant of this protein is characterized by an amino acid alteration from G to C at position 16.
+The natural variant of this protein is characterized by an amino acid alteration from F to L at position 118.
+The protein's natural variant, known as in SCA35; impairs transglutaminase activity;, features a modification of the amino acid from R to C at position 111.
+The protein's natural variant, known as in SCA35; decreased transglutaminase activity; decreased protein stability;, features a modification of the amino acid from D to G at position 327.
+The protein's natural variant, known as in SCA35; decreased protein stability, features a modification of the amino acid from T to N at position 426.
+The protein's natural variant, known as in SCA35; impairs transglutaminase activity;, features a modification of the amino acid from D to H at position 510.
+The protein's natural variant, known as in SCA35; decreased transglutaminase activity; decreased protein stability;, features a modification of the amino acid from L to W at position 517.
+The protein's natural variant, known as in XAN2;, features a modification of the amino acid from A to P at position 57.
+The protein's natural variant, known as in XAN2;, features a modification of the amino acid from T to I at position 294.
+The protein's natural variant, known as in XAN2;, features a modification of the amino acid from R to C at position 776.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation, features a modification of the amino acid from P to L at position 118.
+The natural variant of this protein is characterized by an amino acid alteration from L to F at position 71.
+The protein's natural variant, known as found in patients with orofacial clefting; unknown pathological significance, features a modification of the amino acid from C to Y at position 56.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from D to V at position 1891.
+The natural variant of this protein is characterized by an amino acid alteration from M to I at position 437.
+The natural variant of this protein is characterized by an amino acid alteration from E to ESFKVHAALREASNLSMQ at position 60.
+The natural variant of this protein is characterized by an amino acid alteration from T to TT at position 123.
+The protein's natural variant, known as in FUCA1D; loss of activity;, features a modification of the amino acid from G to D at position 65.
+The protein's natural variant, known as in FUCA1D, features a modification of the amino acid from S to L at position 68.
+The protein's natural variant, known as in allele FUCA1*2;, features a modification of the amino acid from Q to R at position 286.
+The protein's natural variant, known as in FUCA1D; less than 1% of residual activity;, features a modification of the amino acid from L to R at position 410.
+The natural variant of this protein is characterized by an amino acid alteration from N to T at position 139.
+The protein's natural variant, known as in allele DNASE1*4;, features a modification of the amino acid from Q to E at position 31.
+The protein's natural variant, known as in allele DNASE1*5;, features a modification of the amino acid from V to M at position 114.
+The protein's natural variant, known as in allele DNASE1*3;, features a modification of the amino acid from P to A at position 154.
+The protein's natural variant, known as in allele DNASE1*6;, features a modification of the amino acid from R to C at position 207.
+The protein's natural variant, known as in allele DNASE1*1;, features a modification of the amino acid from R to Q at position 244.
+The protein's natural variant, known as in MMSDHD;, features a modification of the amino acid from G to R at position 446.
+The protein's natural variant, known as in a lung small cell carcinoma sample; somatic mutation, features a modification of the amino acid from L to V at position 428.
+The protein's natural variant, known as in NEDMEHM;, features a modification of the amino acid from L to P at position 36.
+The protein's natural variant, known as in NEDMEHM;, features a modification of the amino acid from R to Q at position 145.
+The protein's natural variant, known as decreases levels of sulfotransferase activity;, features a modification of the amino acid from P to H at position 101.
+The protein's natural variant, known as decreases levels of sulfotransferase activity;, features a modification of the amino acid from P to L at position 101.
+The protein's natural variant, known as no effect on sulfotransferase activity;, features a modification of the amino acid from R to C at position 144.
+The protein's natural variant, known as decreases levels of sulfotransferase activity; accelerates proteasome-dependent degradation;, features a modification of the amino acid from K to N at position 234.
+The natural variant of this protein is characterized by an amino acid alteration from S to L at position 88.
+The natural variant of this protein is characterized by an amino acid alteration from K to R at position 89.
+The natural variant of this protein is characterized by an amino acid alteration from D to E at position 228.
+The natural variant of this protein is characterized by an amino acid alteration from P to S at position 254.
+The natural variant of this protein is characterized by an amino acid alteration from R to H at position 366.
+The protein's natural variant, known as in MCPH9;, features a modification of the amino acid from Q to P at position 265.
+The protein's natural variant, known as in SCKL5;, features a modification of the amino acid from K to R at position 667.
+The natural variant of this protein is characterized by an amino acid alteration from N to K at position 504.
+The natural variant of this protein is characterized by an amino acid alteration from N to D at position 543.
+The protein's natural variant, known as in CC-3008; suppresses streptomycin dependence of the S12 mutant P90L, features a modification of the amino acid from Q to P at position 73.
+The protein's natural variant, known as in CC-3010; suppresses streptomycin dependence of the S12 mutant P90L, features a modification of the amino acid from V to GITERQLVNYV at position 90.
+The protein's natural variant, known as in CC-3009; suppresses streptomycin dependence of the S12 mutant P90L, features a modification of the amino acid from K to IVNYVRK at position 92.
+The protein's natural variant, known as in strain: PH392, features a modification of the amino acid from T to I at position 140.
+The protein's natural variant, known as found in a patient with progressive myoclonic epilepsy type 2 also carrying two mutations in EPM2B;, features a modification of the amino acid from N to S at position 249.
+The protein's natural variant, known as in MFM8; also found in a patient with limb-girdle muscular dystrophy; decreased function in cellular response to oxidative stress; no effect on subcellular location in the nucleus and sarcomere. Overexpression in C2C12 cells leads to reduced cell proliferation, migration and differentiation.;, features a modification of the amino acid from N to S at position 155.
+The protein's natural variant, known as in MFM8; decreased function in cellular response to oxidative stress; no effect on subcellular location at nucleus and sarcomere;, features a modification of the amino acid from Q to H at position 372.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from R to G at position 77.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from K to R at position 94.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from G to D at position 361.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from K to N at position 1019.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from W to R at position 3.
+The protein's natural variant, known as in CMTX1;, features a modification of the amino acid from W to S at position 3.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from YT to S at position 8.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from Y to C at position 7.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from T to I at position 8.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from T to P at position 8.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from L to W at position 9.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from S to G at position 11.
+The protein's natural variant, known as in CMTX1;, features a modification of the amino acid from G to S at position 12.
+The protein's natural variant, known as in CMTX1;, features a modification of the amino acid from V to L at position 13.
+The protein's natural variant, known as in CMTX1;, features a modification of the amino acid from V to M at position 13.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from N to K at position 14.
+The protein's natural variant, known as in CMTX1;, features a modification of the amino acid from R to Q at position 15.
+The protein's natural variant, known as in CMTX1; moderate;, features a modification of the amino acid from R to W at position 15.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from H to P at position 16.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from IG to NS at position 21.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from I to S at position 20.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from G to D at position 21.
+The protein's natural variant, known as in CMTX1; non-functional channel, features a modification of the amino acid from R to G at position 22.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from R to P at position 22.
+The protein's natural variant, known as in CMTX1;, features a modification of the amino acid from R to Q at position 22.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from V to A at position 23.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from W to C at position 24.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from L to F at position 25.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from L to P at position 25.
+The protein's natural variant, known as in CMTX1;, features a modification of the amino acid from S to L at position 26.
+The protein's natural variant, known as in CMTX1; severe, features a modification of the amino acid from S to W at position 26.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from I to IIF at position 28.
+The protein's natural variant, known as in CMTX1;, features a modification of the amino acid from I to N at position 28.
+The protein's natural variant, known as in CMTX1;, features a modification of the amino acid from I to T at position 28.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from F to L at position 29.
+The protein's natural variant, known as in CMTX1;, features a modification of the amino acid from I to N at position 30.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from I to T at position 30.
+The protein's natural variant, known as in CMTX1; localized in the Golgi apparatus but also forming rare small junction-like plaques;, features a modification of the amino acid from M to I at position 34.
+The protein's natural variant, known as in CMTX1; localized to the endoplasmic reticulum, features a modification of the amino acid from M to K at position 34.
+The protein's natural variant, known as in CMTX1; functional channel; localized in the Golgi apparatus without reaching the cell membrane;, features a modification of the amino acid from M to T at position 34.
+The protein's natural variant, known as in CMTX1; localized in the Golgi apparatus but also forming rare small gap junction-like plaques, features a modification of the amino acid from M to V at position 34.
+The protein's natural variant, known as in CMTX1; localized mainly on the cell membrane forming gap junction-like plaques, features a modification of the amino acid from V to M at position 35.
+The protein's natural variant, known as in CMTX1; localized in the Golgi apparatus but also forming rare small gap junction-like plaques, features a modification of the amino acid from V to M at position 37.
+The protein's natural variant, known as in CMTX1; localized in the Golgi apparatus without reaching the cell membrane;, features a modification of the amino acid from V to M at position 38.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from A to P at position 39.
+The protein's natural variant, known as in CMTX1;, features a modification of the amino acid from A to V at position 39.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from A to T at position 40.
+The protein's natural variant, known as in CMTX1; localized in the Golgi apparatus without reaching the cell membrane, features a modification of the amino acid from A to V at position 40.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from E to K at position 41.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from V to M at position 43.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from W to L at position 44.
+The protein's natural variant, known as in CMTX1;, features a modification of the amino acid from S to P at position 49.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from S to Y at position 49.
+The protein's natural variant, known as in CMTX1;, features a modification of the amino acid from S to P at position 50.
+The protein's natural variant, known as in CMTX1; suggests a failure to incorporate the mutant protein in the cell membrane, features a modification of the amino acid from C to S at position 53.
+The protein's natural variant, known as in CMTX1;, features a modification of the amino acid from T to A at position 55.
+The protein's natural variant, known as in CMTX1;, features a modification of the amino acid from T to I at position 55.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from T to R at position 55.
+The protein's natural variant, known as in CMTX1; functional channel, features a modification of the amino acid from L to F at position 56.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from Q to H at position 57.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from P to R at position 58.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from G to C at position 59.
+The protein's natural variant, known as in CMTX1;, features a modification of the amino acid from G to R at position 59.
+The protein's natural variant, known as in CMTX1; moderate, features a modification of the amino acid from C to F at position 60.
+The protein's natural variant, known as in CMTX1;, features a modification of the amino acid from V to I at position 63.
+The protein's natural variant, known as in CMTX1; moderate, features a modification of the amino acid from C to F at position 64.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from C to S at position 64.
+The protein's natural variant, known as in CMTX1;, features a modification of the amino acid from Y to C at position 65.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from Y to H at position 65.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from F to L at position 69.
+The protein's natural variant, known as in CMTX1;, features a modification of the amino acid from P to A at position 70.
+The protein's natural variant, known as in CMTX1; localized in the Golgi apparatus without reaching the cell membrane, features a modification of the amino acid from R to P at position 75.
+The protein's natural variant, known as in CMTX1; localized in the Golgi apparatus without reaching the cell membrane;, features a modification of the amino acid from R to Q at position 75.
+The protein's natural variant, known as in CMTX1; localized in the Golgi apparatus without reaching the cell membrane;, features a modification of the amino acid from R to W at position 75.
+The protein's natural variant, known as in CMTX1;, features a modification of the amino acid from W to S at position 77.
+The protein's natural variant, known as in CMTX1;, features a modification of the amino acid from Q to R at position 80.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from L to F at position 81.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from L to P at position 83.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from V to I at position 84.
+The protein's natural variant, known as in CMTX1; mutant have a higher open probability than hemichannels formed of GJB1 wild-type;, features a modification of the amino acid from S to C at position 85.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from S to F at position 85.
+The protein's natural variant, known as in CMTX1; moderate, features a modification of the amino acid from T to A at position 86.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from T to N at position 86.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from T to S at position 86.
+The protein's natural variant, known as in CMTX1;, features a modification of the amino acid from P to A at position 87.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from P to L at position 87.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from P to S at position 87.
+The protein's natural variant, known as in CMTX1;, features a modification of the amino acid from L to P at position 89.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from L to H at position 90.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from L to V at position 90.
+The protein's natural variant, known as in CMTX1;, features a modification of the amino acid from V to M at position 91.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from M to V at position 93.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from H to D at position 94.
+The protein's natural variant, known as in CMTX1; non-functional channel;, features a modification of the amino acid from H to Q at position 94.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from H to Y at position 94.
+The protein's natural variant, known as in CMTX1; non-functional channel;, features a modification of the amino acid from V to M at position 95.
+The protein's natural variant, known as in CMTX1; mild/moderate, features a modification of the amino acid from H to Y at position 100.
+The protein's natural variant, known as in CMTX1; mild phenotype; increased sensitivity to acidification-induced closure;, features a modification of the amino acid from E to G at position 102.
+The protein's natural variant, known as in CMTX1;, features a modification of the amino acid from K to E at position 103.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from K to T at position 104.
+The protein's natural variant, known as in CMTX1;, features a modification of the amino acid from R to W at position 107.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from L to P at position 108.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from V to E at position 120.
+The protein's natural variant, known as in CMTX1;, features a modification of the amino acid from K to E at position 124.
+The protein's natural variant, known as in CMTX1;, features a modification of the amino acid from K to N at position 124.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from V to D at position 125.
+The protein's natural variant, known as in CMTX1;, features a modification of the amino acid from H to Y at position 126.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from I to M at position 127.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from I to S at position 127.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from S to P at position 128.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from T to I at position 130.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from L to P at position 131.
+The protein's natural variant, known as in CMTX1; moderate, features a modification of the amino acid from W to C at position 133.
+The protein's natural variant, known as in CMTX1;, features a modification of the amino acid from W to R at position 133.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from Y to C at position 135.
+The protein's natural variant, known as in CMTX1 and DSS; found in a DSS patient with severe symptoms also carrying W-359 in the EGR2 gene; may act as a modifier of disease severity;, features a modification of the amino acid from V to A at position 136.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from S to N at position 138.
+The protein's natural variant, known as in CMTX1;, features a modification of the amino acid from V to M at position 139.
+The protein's natural variant, known as in CMTX1;, features a modification of the amino acid from F to L at position 141.
+The protein's natural variant, known as in CMTX1; requires 2 nucleotide substitutions, features a modification of the amino acid from R to E at position 142.
+The protein's natural variant, known as in CMTX1;, features a modification of the amino acid from R to Q at position 142.
+The protein's natural variant, known as in CMTX1; moderate;, features a modification of the amino acid from R to W at position 142.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from E to K at position 146.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from A to D at position 147.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from F to I at position 149.
+The protein's natural variant, known as in CMTX1; unknown pathological significance, features a modification of the amino acid from F to V at position 149.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from Y to S at position 151.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from F to S at position 153.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from L to F at position 156.
+The protein's natural variant, known as in CMTX1;, features a modification of the amino acid from L to R at position 156.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from Y to C at position 157.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from P to A at position 158.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from P to R at position 158.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from P to S at position 158.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from G to D at position 159.
+The protein's natural variant, known as in CMTX1;, features a modification of the amino acid from G to S at position 159.
+The protein's natural variant, known as in CMTX1;, features a modification of the amino acid from Y to H at position 160.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from A to P at position 161.
+The protein's natural variant, known as in CMTX1;, features a modification of the amino acid from R to Q at position 164.
+The protein's natural variant, known as in CMTX1; moderate;, features a modification of the amino acid from R to W at position 164.
+The protein's natural variant, known as in CMTX1; demyelinating form, features a modification of the amino acid from C to R at position 168.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from C to Y at position 168.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from P to A at position 172.
+The protein's natural variant, known as in CMTX1;, features a modification of the amino acid from P to L at position 172.
+The protein's natural variant, known as in CMTX1; suggests a failure to incorporate the mutant protein in the cell membrane, features a modification of the amino acid from P to R at position 172.
+The protein's natural variant, known as in CMTX1;, features a modification of the amino acid from P to S at position 172.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from C to R at position 173.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from N to D at position 175.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from V to A at position 177.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from V to E at position 177.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from D to Y at position 178.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from C to R at position 179.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from F to L at position 180.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from F to S at position 180.
+The protein's natural variant, known as in CMTX1; profoundly impaired in their ability to support the earliest stages of regeneration of myelinated fibers, features a modification of the amino acid from V to A at position 181.
+The protein's natural variant, known as in CMTX1;, features a modification of the amino acid from V to M at position 181.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from S to T at position 182.
+The protein's natural variant, known as in CMTX1;, features a modification of the amino acid from R to C at position 183.
+The protein's natural variant, known as in CMTX1;, features a modification of the amino acid from R to H at position 183.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from R to S at position 183.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from P to L at position 184.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from P to R at position 184.
+The protein's natural variant, known as in CMTX1; non-functional channel;, features a modification of the amino acid from E to K at position 186.
+The protein's natural variant, known as in CMTX1;, features a modification of the amino acid from K to E at position 187.
+The protein's natural variant, known as in CMTX1;, features a modification of the amino acid from V to G at position 189.
+The protein's natural variant, known as in CMTX1;, features a modification of the amino acid from V to I at position 189.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from T to A at position 191.
+The protein's natural variant, known as in CMTX1;, features a modification of the amino acid from V to F at position 192.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from F to C at position 193.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from F to L at position 193.
+The protein's natural variant, known as in CMTX1;, features a modification of the amino acid from M to V at position 194.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from S to F at position 198.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from G to R at position 199.
+The protein's natural variant, known as in CMTX1; severe, features a modification of the amino acid from C to R at position 201.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from C to Y at position 201.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from I to N at position 203.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from L to F at position 204.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from L to V at position 204.
+The protein's natural variant, known as in CMTX1; localized to the endoplasmic reticulum, features a modification of the amino acid from N to I at position 205.
+The protein's natural variant, known as in CMTX1; mild;, features a modification of the amino acid from N to S at position 205.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from E to G at position 208.
+The protein's natural variant, known as in CMTX1; non-detectable levels of hemichannel activation and non-detectable levels of electrical coupling;, features a modification of the amino acid from E to K at position 208.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from Y to H at position 211.
+The protein's natural variant, known as in CMTX1, features a modification of the amino acid from II to L at position 214.
+The protein's natural variant, known as in CMTX1; localized mainly on the cell membrane forming gap junction-like plaques;, features a modification of the amino acid from I to V at position 213.
+The protein's natural variant, known as in CMTX1; non-detectable levels of hemichannel activation and non-detectable levels of electrical coupling;, features a modification of the amino acid from R to Q at position 215.
+The protein's natural variant, known as in CMTX1; mild/moderate; non-functional channel;, features a modification of the amino acid from R to W at position 215.
+The protein's natural variant, known as in CMTX1; localized mainly on the cell membrane forming gap junction-like plaques;, features a modification of the amino acid from R to C at position 219.
+The protein's natural variant, known as in CMTX1; localized mainly on the cell membrane forming gap junction-like plaques;, features a modification of the amino acid from R to H at position 219.
+The protein's natural variant, known as in CMTX1; localized mainly on the cell membrane forming gap junction-like plaques;, features a modification of the amino acid from R to G at position 220.
+The protein's natural variant, known as in CMTX1; localized mainly on the cell membrane forming gap junction-like plaques;, features a modification of the amino acid from R to C at position 230.
+The protein's natural variant, known as in CMTX1; localized mainly on the cell membrane forming gap junction-like plaques;, features a modification of the amino acid from R to L at position 230.
+The protein's natural variant, known as in CMTX1; the mutation causes abnormal hemichannel opening with excessive permeability of the plasma membrane and decreased cell survival;, features a modification of the amino acid from F to C at position 235.
+The protein's natural variant, known as in CMTX1; localized mainly on the cell membrane forming gap junction-like plaques;, features a modification of the amino acid from R to H at position 238.
+The protein's natural variant, known as in CMTX1; localized mainly on the cell membrane forming gap junction-like plaques, features a modification of the amino acid from L to I at position 239.
+The protein's natural variant, known as in CMTX1;, features a modification of the amino acid from R to C at position 264.
+The protein's natural variant, known as in CMTX1; forms channels normally, features a modification of the amino acid from C to G at position 280.
+The protein's natural variant, known as in strain: Isolate Atlantic ocean, features a modification of the amino acid from N to D at position 16.
+The protein's natural variant, known as rare variant found in a patient with Van der Woude syndrome; unknown pathological significance;, features a modification of the amino acid from D to Y at position 523.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from R to L at position 496.
+The protein's natural variant, known as in PSPHD; decreased L-phosphoserine phosphatase activity;, features a modification of the amino acid from D to N at position 32.
+The protein's natural variant, known as in PSPHD; decreased L-phosphoserine phosphatase activity, features a modification of the amino acid from A to T at position 35.
+The protein's natural variant, known as in PSPHD; decreased L-phosphoserine phosphatase activity;, features a modification of the amino acid from M to T at position 52.
+The protein's natural variant, known as in strain: Isolate 96T/FRE, features a modification of the amino acid from H to V at position 9.
+The protein's natural variant, known as in strain: Y06, features a modification of the amino acid from N to H at position 35.
+The protein's natural variant, known as in strain: 5060d, YS8 and Isolate 96T/KAD, features a modification of the amino acid from E to G at position 46.
+The protein's natural variant, known as in strain: G21, features a modification of the amino acid from M to L at position 50.
+The protein's natural variant, known as in strain: Isolate 96T/ROS, features a modification of the amino acid from AE to EK at position 56.
+The protein's natural variant, known as in strain: 8826, features a modification of the amino acid from I to L at position 58.
+The protein's natural variant, known as in strain: SS1, G21, YS8, Isolate 96T/THO, Isolate 96T/ROS and Isolate 96T/HAR, features a modification of the amino acid from V to A at position 59.
+The protein's natural variant, known as in strain: 1811a and YS2, features a modification of the amino acid from S to T at position 70.
+The protein's natural variant, known as in strain: 8826, SS1, RHO901a, G21, 1811a, 5060d, YS2, YS8, Y06, Isolate 96T/THO, Isolate 96T/ROS, Isolate 96T/KAD, Isolate 96T/FRE and Isolate 96T/HAR, features a modification of the amino acid from I to L at position 73.
+The protein's natural variant, known as in strain: 8826, features a modification of the amino acid from E to D at position 80.
+The protein's natural variant, known as in strain: G21, features a modification of the amino acid from ILE to FLG at position 97.
+The protein's natural variant, known as in strain: Isolate 96T/ROS, features a modification of the amino acid from E to D at position 97.
+The protein's natural variant, known as in strain: 8826, RHP901a, SS1, DB2, Y06, Isolate 96T/THO and Isolate 96T/FRE, features a modification of the amino acid from E to G at position 97.
+The protein's natural variant, known as in strain: 8826, SS1, DB2, RHP901a, G21, 2A, 2B, 5A, 5D, 1811a, 5060d, YS2, YS8, MI 355, MI 356, MEL-HP27, Y06, Isolate 96T/THO, Isolate 96T/ROS, Isolate 96T/KAD, Isolate 96T/FRE, Isolate 96T/NEW, Isolate 96T/HAR and ATCC 43629, features a modification of the amino acid from Y to H at position 101.
+The protein's natural variant, known as in strain: Isolate 96T/KAD, features a modification of the amino acid from K to E at position 107.
+The protein's natural variant, known as in strain: 8826, SS1, DB2, G21, MI 355, MI 356 and Y06, features a modification of the amino acid from Q to E at position 140.
+The protein's natural variant, known as in strain: CWL029 and TW-183, features a modification of the amino acid from G to S at position 277.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from Q to E at position 29.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from E to G at position 87.
+The protein's natural variant, known as found in patients with global developmental delay and epilepsy with history of choanal atresia; unknown pathological significance;, features a modification of the amino acid from R to C at position 225.
+The natural variant of this protein is characterized by an amino acid alteration from G to A at position 231.
+The protein's natural variant, known as confers resistance to the herbicide norflurazon, features a modification of the amino acid from R to C at position 195.
+The protein's natural variant, known as requires 2 nucleotide substitutions, features a modification of the amino acid from P to M at position 24.
+The natural variant of this protein is characterized by an amino acid alteration from S to C at position 147.
+The protein's natural variant, known as in PeBP(R)-II, features a modification of the amino acid from V to I at position 19.
+The protein's natural variant, known as in strain: Isolate MME-K2, features a modification of the amino acid from A to T at position 125.
+The protein's natural variant, known as in strain: Isolate MME-TKY3, features a modification of the amino acid from I to F at position 257.
+The protein's natural variant, known as in strain: Isolate MME-1, Isolate MME-G1, Isolate MME-G5, Isolate MME-TSU1 and Isolate TH017, features a modification of the amino acid from S to N at position 263.
+The protein's natural variant, known as in strain: Isolate MME-K2, features a modification of the amino acid from F to L at position 276.
+The protein's natural variant, known as in strain: Isolate MME-G1, Isolate MME-G5 and Isolate MME-TSU1, features a modification of the amino acid from I to V at position 304.
+The protein's natural variant, known as in strain: Isolate MME-TKY3, features a modification of the amino acid from E to G at position 344.
+The protein's natural variant, known as in mutant W7 which is respiratory deficient, features a modification of the amino acid from G to S at position 131.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from E to K at position 817.
+The protein's natural variant, known as found in a patient with hereditary motor and sensory neuropathy; unknown pathological significance;, features a modification of the amino acid from V to M at position 212.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from T to I at position 1087.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from R to H at position 1152.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from V to E at position 148.
+The protein's natural variant, known as in ARWH3; reduces keratin intermediate filamen formation; impairs cytoskeleton assembly;, features a modification of the amino acid from V to L at position 238.
+The protein's natural variant, known as in ARWH3;, features a modification of the amino acid from L to P at position 317.
+The protein's natural variant, known as in ARWH3; disruption of keratin intermediate filament formation formed via heterodimerization with KRT5, features a modification of the amino acid from L to R at position 376.
+The protein's natural variant, known as in SIFD; unknown pathological significance, features a modification of the amino acid from M to V at position 30.
+The protein's natural variant, known as in SIFD, features a modification of the amino acid from R to W at position 99.
+The protein's natural variant, known as in SIFD; unknown pathological significance, features a modification of the amino acid from I to T at position 101.
+The protein's natural variant, known as in SIFD, features a modification of the amino acid from T to I at position 110.
+The protein's natural variant, known as in SIFD; unknown pathological significance, features a modification of the amino acid from E to D at position 121.
+The protein's natural variant, known as in SIFD, features a modification of the amino acid from D to G at position 128.
+The protein's natural variant, known as in SIFD, features a modification of the amino acid from A to V at position 148.
+The protein's natural variant, known as in SIFD; reduced CCA tRNA nucleotidyltransferasevactivity; decreased stability;, features a modification of the amino acid from T to I at position 154.
+The protein's natural variant, known as in SIFD, features a modification of the amino acid from I to T at position 155.
+The protein's natural variant, known as in SIFD; loss of CCA tRNA nucleotidyltransferase activity;, features a modification of the amino acid from M to V at position 158.
+The protein's natural variant, known as in SIFD, features a modification of the amino acid from D to V at position 163.
+The protein's natural variant, known as in SIFD; loss of CCA tRNA nucleotidyltransferase activity; decreased stability;, features a modification of the amino acid from L to S at position 166.
+The protein's natural variant, known as in SIFD, features a modification of the amino acid from Y to F at position 173.
+The protein's natural variant, known as in SIFD; loss of CCA tRNA nucleotidyltransferase activity;, features a modification of the amino acid from R to I at position 190.
+The protein's natural variant, known as in SIFD, features a modification of the amino acid from R to K at position 203.
+The protein's natural variant, known as in SIFD, features a modification of the amino acid from H to R at position 215.
+The protein's natural variant, known as in SIFD; loss of CCA tRNA nucleotidyltransferase activity;, features a modification of the amino acid from I to T at position 223.
+The protein's natural variant, known as in SIFD; unknown pathological significance, features a modification of the amino acid from L to S at position 313.
+The protein's natural variant, known as in SIFD; decreased CCA tRNA nucleotidyltransferase activity; abolished homodimerization and disulfide bond formation, features a modification of the amino acid from I to T at position 326.
+The protein's natural variant, known as in SIFD;, features a modification of the amino acid from K to E at position 416.
+The protein's natural variant, known as in strain: SC96_47, features a modification of the amino acid from D to A at position 380.
+The protein's natural variant, known as found in patients with atypical hemolytic uremic syndrome;, features a modification of the amino acid from L to R at position 105.
+The protein's natural variant, known as found in patients with atypical hemolytic uremic syndrome;, features a modification of the amino acid from S to T at position 195.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from N to S at position 216.
+The protein's natural variant, known as found in a patient with atypical hemolytic uremic syndrome;, features a modification of the amino acid from Y to N at position 277.
+The protein's natural variant, known as found in patients with atypical hemolytic uremic syndrome;, features a modification of the amino acid from V to L at position 379.
+The protein's natural variant, known as found in patients with atypical hemolytic uremic syndrome;, features a modification of the amino acid from W to C at position 436.
+The natural variant of this protein is characterized by an amino acid alteration from A to G at position 22.
+The protein's natural variant, known as in plasmid pCP301, features a modification of the amino acid from V to I at position 296.
+The protein's natural variant, known as in strain: Isolate MVZ 174053 and Isolate MVZ 174054, features a modification of the amino acid from V to A at position 108.
+The protein's natural variant, known as in strain: Isolate MVZ 174053 and Isolate MVZ 174054, features a modification of the amino acid from V to I at position 115.
+The natural variant of this protein is characterized by an amino acid alteration from S to C at position 22.
+The natural variant of this protein is characterized by an amino acid alteration from P to S at position 61.
+The natural variant of this protein is characterized by an amino acid alteration from G to R at position 78.
+The natural variant of this protein is characterized by an amino acid alteration from T to S at position 122.
+The natural variant of this protein is characterized by an amino acid alteration from N to S at position 165.
+The natural variant of this protein is characterized by an amino acid alteration from G to A at position 171.
+The protein's natural variant, known as in USH4; loss of sulfatase activity toward p-nitrocatechol sulfate; loss of processing of the precursor protein suggesting impaired transport to lysosomes, features a modification of the amino acid from D to Y at position 45.
+The natural variant of this protein is characterized by an amino acid alteration from D to E at position 31.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 79.
+The natural variant of this protein is characterized by an amino acid alteration from E to D at position 83.
+The protein's natural variant, known as in a gastric carcinoma sample; somatic mutation, features a modification of the amino acid from T to I at position 32.
+The protein's natural variant, known as in a gastric carcinoma sample; somatic mutation, features a modification of the amino acid from T to K at position 32.
+The protein's natural variant, known as in a gastric carcinoma sample; somatic mutation; abolishes inhibition of gastric cancer cell growth; abolishes inhibition of apoptosis in gasterointestinal epithelial cells; increases invasive activity in epithelial cells;, features a modification of the amino acid from A to D at position 34.
+The protein's natural variant, known as in a gastric carcinoma sample; somatic mutation; abolishes inhibition of gastric cancer cell growth; abolishes inhibition of apoptosis in gasterointestinal epithelial cells; increases invasive activity in epithelial cells, features a modification of the amino acid from E to K at position 37.
+The protein's natural variant, known as in a gastric adenoma sample; somatic mutation, features a modification of the amino acid from V to I at position 46.
+The protein's natural variant, known as in a gastric carcinoma sample; somatic mutation;, features a modification of the amino acid from G to V at position 55.
+The protein's natural variant, known as in ODLURO, features a modification of the amino acid from V to I at position 140.
+The protein's natural variant, known as in ODLURO, features a modification of the amino acid from Y to H at position 284.
+The protein's natural variant, known as in ODLURO;, features a modification of the amino acid from D to V at position 907.
+The protein's natural variant, known as in ODLURO;, features a modification of the amino acid from P to S at position 1376.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation, features a modification of the amino acid from T to I at position 140.
+The protein's natural variant, known as in a lung squamous cell carcinoma sample; somatic mutation, features a modification of the amino acid from S to Y at position 303.
+The protein's natural variant, known as in ALS19; reduces autophosphorylation upon NRG1 stimulation;, features a modification of the amino acid from R to Q at position 927.
+The protein's natural variant, known as in ALS19; reduces autophosphorylation upon NRG1 stimulation;, features a modification of the amino acid from R to W at position 1275.
+The protein's natural variant, known as in DEE68; unknown pathological significance;, features a modification of the amino acid from L to P at position 329.
+The protein's natural variant, known as in a lung large cell carcinoma sample; somatic mutation, features a modification of the amino acid from L to V at position 160.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation, features a modification of the amino acid from Q to H at position 863.
+The protein's natural variant, known as in strain: 2.6.1 / French, features a modification of the amino acid from K to P at position 48.
+The protein's natural variant, known as found in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to C at position 474.
+The protein's natural variant, known as found in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to Q at position 602.
+The protein's natural variant, known as in CMD1L;, features a modification of the amino acid from S to A at position 150.
+The protein's natural variant, known as in LGMDR6;, features a modification of the amino acid from E to K at position 261.
+The protein's natural variant, known as in strain: r0, features a modification of the amino acid from P to K at position 61.
+The protein's natural variant, known as found in a family with foveal hypoplasia; unknown pathological significance;, features a modification of the amino acid from G to R at position 15.
+The protein's natural variant, known as in OPA3;, features a modification of the amino acid from G to S at position 93.
+The protein's natural variant, known as in OPA3;, features a modification of the amino acid from Q to E at position 105.
+The protein's natural variant, known as in MRD53; no effect on protein abundance; decreased autophosphorylation; decreased neuronal migration;, features a modification of the amino acid from F to S at position 98.
+The protein's natural variant, known as in MRD53; no effect on protein abundance; increased autophosphorylation; decreased neuronal migration, features a modification of the amino acid from E to D at position 109.
+The protein's natural variant, known as in MRD53; unknown pathological significance, features a modification of the amino acid from A to V at position 112.
+The protein's natural variant, known as in MRD53; unknown pathological significance; no effect on protein abundance; no effect on autophosphorylation; no effect on neuronal migration, features a modification of the amino acid from P to A at position 138.
+The protein's natural variant, known as in MRD53; increased ubiquitin-mediated proteasomal degradation with a dominant negative effect on wild-type protein; decreased localization to dendritic spines; no effect on holoenzyme assembly; loss of interaction with SHANK3; loss of interaction with GRIN2B; loss of interaction with CACNB2; loss of interaction with LRRC7; loss of interaction with GRM5; decreased protein serine/threonine kinase activity with a dominant negative effect on wild-type protein; decreased autophosphorylation; changed dendritic spine development; decreased neuronal migration;, features a modification of the amino acid from E to V at position 183.
+The protein's natural variant, known as in MRD53; unknown pathological significance; no effect on protein abundance; no effect on autophosphorylation; no effect on neuronal migration;, features a modification of the amino acid from P to L at position 212.
+The protein's natural variant, known as in MRD53; increased basal autophosphorylation, features a modification of the amino acid from P to Q at position 212.
+The protein's natural variant, known as in MRD53; unknown pathological significance; no effect on protein abundance; no effect on autophosphorylation; no effect on neuronal migration;, features a modification of the amino acid from P to L at position 235.
+The protein's natural variant, known as in MRD53; decreased protein abundance; increased autophosphorylation; decreased neuronal migration;, features a modification of the amino acid from H to R at position 282.
+The protein's natural variant, known as in MRD53; no effect on protein abundance; loss of autophosphorylation; loss of neuronal migration;, features a modification of the amino acid from T to P at position 286.
+The protein's natural variant, known as in MRT63; decreased oligomerization;, features a modification of the amino acid from H to Y at position 466.
+The natural variant of this protein is characterized by an amino acid alteration from P to A at position 264.
+The natural variant of this protein is characterized by an amino acid alteration from T to A at position 395.
+The natural variant of this protein is characterized by an amino acid alteration from A to AAAA at position 62.
+The protein's natural variant, known as in about 50% of the molecules, features a modification of the amino acid from I to T at position 58.
+The protein's natural variant, known as in strain: 129/Sv and CBA/J, features a modification of the amino acid from E to D at position 59.
+The protein's natural variant, known as in strain: 129/Sv; requires 2 nucleotide substitutions, features a modification of the amino acid from G to L at position 94.
+The protein's natural variant, known as in strain: 129/Sv and CBA/J, features a modification of the amino acid from R to K at position 139.
+The protein's natural variant, known as in strain: A/J, features a modification of the amino acid from V to G at position 283.
+The protein's natural variant, known as in strain: 129/Sv and CBA/J, features a modification of the amino acid from L to P at position 308.
+The protein's natural variant, known as in strain: A/J, features a modification of the amino acid from S to T at position 341.
+The protein's natural variant, known as in strain: 129/Sv and CBA/J, features a modification of the amino acid from H to Q at position 1029.
+The protein's natural variant, known as in strain: 129/Sv and CBA/J, features a modification of the amino acid from SS to NN at position 1056.
+The protein's natural variant, known as in strain: Miho Golden and Haruna Nijo. In allele rym5, features a modification of the amino acid from P to S at position 53.
+The protein's natural variant, known as in alleles 40 and 44. In allele rym4, features a modification of the amino acid from S to F at position 57.
+The protein's natural variant, known as in allele 44. In allele rym4, features a modification of the amino acid from K to I at position 118.
+The protein's natural variant, known as in alleles 40 and 43. In allele rym4, features a modification of the amino acid from K to T at position 118.
+The protein's natural variant, known as in strain: Sukai Golden and Mikamo Golden. In allele rym5, features a modification of the amino acid from T to S at position 120.
+The protein's natural variant, known as in alleles 38 and 39, features a modification of the amino acid from NQ to KE at position 161.
+The protein's natural variant, known as in strain: Sukai Golden and Mikamo Golden. In allele rym5, features a modification of the amino acid from N to D at position 160.
+The protein's natural variant, known as in strain: Miho Golden and Haruna Nijo, features a modification of the amino acid from Q to H at position 161.
+The protein's natural variant, known as in strain: Sukai Golden and Mikamo Golden. In allele rym5, features a modification of the amino acid from Q to K at position 161.
+The protein's natural variant, known as in allele 41, features a modification of the amino acid from T to I at position 175.
+The protein's natural variant, known as in allele 42, features a modification of the amino acid from G to V at position 195.
+The protein's natural variant, known as in allele rym4, features a modification of the amino acid from S to F at position 205.
+The protein's natural variant, known as in alleles 40, 43 and 44. In allele rym4, features a modification of the amino acid from D to G at position 206.
+The protein's natural variant, known as in alleles 40, 43 and 44, features a modification of the amino acid from G to A at position 208.
+The protein's natural variant, known as in alleles 40, 43 and 44, features a modification of the amino acid from G to S at position 208.
+The protein's natural variant, known as in allele 39, features a modification of the amino acid from A to G at position 209.
+The protein's natural variant, known as in PPH1;, features a modification of the amino acid from C to Y at position 60.
+The protein's natural variant, known as in PPH1; unknown pathological significance; unchanged subcellular localization, features a modification of the amino acid from S to R at position 64.
+The protein's natural variant, known as in PPH1; significant decrease in nitric oxide synthesis by endothelial cells;, features a modification of the amino acid from Y to C at position 67.
+The protein's natural variant, known as in PPH1; unknown pathological significance; unchanged subcellular localization, features a modification of the amino acid from I to L at position 77.
+The protein's natural variant, known as in PPH1;, features a modification of the amino acid from Q to H at position 82.
+The protein's natural variant, known as in PPH1; alters alternative splicing of BMPR2;, features a modification of the amino acid from C to F at position 84.
+The protein's natural variant, known as in PPH1; unknown pathological significance; unchanged subcellular localization, features a modification of the amino acid from H to Y at position 87.
+The protein's natural variant, known as in PPH1; unknown pathological significance; unchanged subcellular localization, features a modification of the amino acid from Q to L at position 92.
+The protein's natural variant, known as in PPH1; unknown pathological significance; unchanged subcellular localization, features a modification of the amino acid from Q to H at position 109.
+The protein's natural variant, known as in PPH1;, features a modification of the amino acid from C to Y at position 117.
+The protein's natural variant, known as in PPH1;, features a modification of the amino acid from C to W at position 118.
+The protein's natural variant, known as in PPH1;, features a modification of the amino acid from C to R at position 123.
+The protein's natural variant, known as in PPH1;, features a modification of the amino acid from C to S at position 123.
+The protein's natural variant, known as in PPH1; unknown pathological significance; unchanged subcellular localization, features a modification of the amino acid from P to A at position 138.
+The protein's natural variant, known as in PPH1; unknown pathological significance; unchanged subcellular localization, features a modification of the amino acid from A to P at position 162.
+The protein's natural variant, known as in PPH1;, features a modification of the amino acid from G to D at position 182.
+The protein's natural variant, known as in PPH1; unknown pathological significance; unchanged subcellular localization, features a modification of the amino acid from R to G at position 248.
+The protein's natural variant, known as in PPH1; unknown pathological significance; unchanged subcellular localization, features a modification of the amino acid from D to N at position 264.
+The protein's natural variant, known as in PPH1; unknown pathological significance; unchanged subcellular localization;, features a modification of the amino acid from V to M at position 341.
+The protein's natural variant, known as in PPH1;, features a modification of the amino acid from C to Y at position 347.
+The protein's natural variant, known as in PPH1;, features a modification of the amino acid from C to R at position 420.
+The protein's natural variant, known as in PPH1; unknown pathological significance; unchanged subcellular localization, features a modification of the amino acid from K to R at position 467.
+The protein's natural variant, known as in PPH1; sporadic;, features a modification of the amino acid from C to R at position 483.
+The protein's natural variant, known as in PPH1; complete loss of function;, features a modification of the amino acid from D to G at position 485.
+The protein's natural variant, known as in PPH1; sporadic;, features a modification of the amino acid from R to Q at position 491.
+The protein's natural variant, known as in PPH1;, features a modification of the amino acid from R to W at position 491.
+The protein's natural variant, known as in PPH1;, features a modification of the amino acid from K to T at position 512.
+The protein's natural variant, known as in PPH1;, features a modification of the amino acid from N to K at position 519.
+The protein's natural variant, known as unchanged subcellular localization;, features a modification of the amino acid from S to N at position 775.
+The protein's natural variant, known as in PPH1; abnormal subcellular localization; significant increase in apoptosis of endothelial cells; significant decrease in proliferation of endothelial cells; significant decrease in nitric oxide synthesis by endothelial cells; significant increase in endothelin 1 synthesis by endothelial cells;, features a modification of the amino acid from S to N at position 863.
+The protein's natural variant, known as in PPH1; leads to constitutive activation of the MAPK14 pathway;, features a modification of the amino acid from R to P at position 899.
+The protein's natural variant, known as in strain: cv. Tc, features a modification of the amino acid from R to C at position 156.
+The protein's natural variant, known as in strain: cv. Tc, features a modification of the amino acid from F to V at position 229.
+The protein's natural variant, known as in strain: cv. Tc, features a modification of the amino acid from I to V at position 266.
+The protein's natural variant, known as in strain: cv. Tc, features a modification of the amino acid from I to T at position 386.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from S to F at position 514.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from R to C at position 519.
+The natural variant of this protein is characterized by an amino acid alteration from T to A at position 67.
+The natural variant of this protein is characterized by an amino acid alteration from G to V at position 136.
+The natural variant of this protein is characterized by an amino acid alteration from T to N at position 147.
+The natural variant of this protein is characterized by an amino acid alteration from I to M at position 164.
+The protein's natural variant, known as in strain: LA0411, LA1420 and LA0409, allele pot1(2), haplotypes 1 and 4, features a modification of the amino acid from V to K at position 54.
+The protein's natural variant, known as in strain: LA1478, LA1582 and LA1593, haplotype 2, features a modification of the amino acid from L to V at position 58.
+The protein's natural variant, known as in strain: LA0411, allele pot1(2), haplotype 4, features a modification of the amino acid from D to G at position 112.
+The protein's natural variant, known as in strain: LA1245, haplotype 3, features a modification of the amino acid from T to M at position 151.
+The protein's natural variant, known as in 25% of the molecules, features a modification of the amino acid from V to I at position 48.
+The natural variant of this protein is characterized by an amino acid alteration from L to T at position 66.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 98.
+The natural variant of this protein is characterized by an amino acid alteration from N to E at position 148.
+The protein's natural variant, known as in strain: VT847, features a modification of the amino acid from P to S at position 39.
+The protein's natural variant, known as in strain: VT847, features a modification of the amino acid from N to S at position 67.
+The protein's natural variant, known as in strain: JU403, JU439, JU516 and JU793, features a modification of the amino acid from T to I at position 90.
+The protein's natural variant, known as in strain: ED3036, features a modification of the amino acid from E to D at position 101.
+The protein's natural variant, known as in strain: BW287, features a modification of the amino acid from I to V at position 123.
+The protein's natural variant, known as in strain: BW287, ED3033, ED3034, ED3035, ED3037, ED3092, ED3101, EG4181, EG4207A, HK104, HK105, JU403, JU439, JU516, JU725, JU793, PB800, PB826 and VT847, features a modification of the amino acid from V to I at position 175.
+The protein's natural variant, known as in strain: ED3033, ED3034, ED3035 and ED3037, features a modification of the amino acid from A to V at position 243.
+The protein's natural variant, known as in strain: BW287, ED3033, ED3034, ED3035, ED3037, ED3092, ED3101, HK104, HK105, JU403, JU439, JU516, JU793, PB826 and VT847, features a modification of the amino acid from S to A at position 244.
+The protein's natural variant, known as in strain: EG4181, EG4207A and PB800, features a modification of the amino acid from S to V at position 244.
+The protein's natural variant, known as in strain: ED3092 and ED3101, features a modification of the amino acid from I to M at position 247.
+The protein's natural variant, known as in strain: JU793, features a modification of the amino acid from I to M at position 250.
+The protein's natural variant, known as in allelic sequence, features a modification of the amino acid from K to N at position 120.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from G to A at position 42.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to H at position 231.
+The protein's natural variant, known as in FASPS2; strongly reduces kinase activity;, features a modification of the amino acid from T to A at position 44.
+The protein's natural variant, known as in FASPS2; strongly reduces kinase activity;, features a modification of the amino acid from H to R at position 46.
+The protein's natural variant, known as in breast cancer samples; infiltrating ductal carcinoma; somatic mutation, features a modification of the amino acid from S to C at position 97.
+The protein's natural variant, known as in CPHD3;, features a modification of the amino acid from Y to C at position 111.
+The protein's natural variant, known as in CPHD3; unknown pathological significance, features a modification of the amino acid from C to F at position 141.
+The protein's natural variant, known as in CPHD3; associated with diminished DNA binding and pituitary gene activation;, features a modification of the amino acid from A to V at position 210.
+The protein's natural variant, known as in a glioblastoma multiforme sample; somatic mutation, features a modification of the amino acid from V to M at position 716.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 364.
+The protein's natural variant, known as in HHD; has normal catalytic cycle, features a modification of the amino acid from P to L at position 201.
+The protein's natural variant, known as in HHD, features a modification of the amino acid from G to E at position 220.
+The protein's natural variant, known as in HHD;, features a modification of the amino acid from A to T at position 304.
+The protein's natural variant, known as in HHD; impairs manganese-dependent autophosphorylation in the presence of ATP; impairs manganese transporter activity, features a modification of the amino acid from G to C at position 309.
+The protein's natural variant, known as in HHD;, features a modification of the amino acid from G to V at position 309.
+The protein's natural variant, known as in HHD, features a modification of the amino acid from L to P at position 318.
+The protein's natural variant, known as in HHD; decreases protein expression, features a modification of the amino acid from L to P at position 341.
+The protein's natural variant, known as in HHD; decreases protein expression, features a modification of the amino acid from C to Y at position 344.
+The protein's natural variant, known as in HHD; decreases protein expression, features a modification of the amino acid from C to R at position 411.
+The protein's natural variant, known as in HHD;, features a modification of the amino acid from C to F at position 490.
+The protein's natural variant, known as in HHD; decreases protein expression, features a modification of the amino acid from T to I at position 570.
+The protein's natural variant, known as in HHD; impairs phosphoenzyme dephosphorylation;, features a modification of the amino acid from I to V at position 580.
+The protein's natural variant, known as in HHD;, features a modification of the amino acid from L to P at position 584.
+The protein's natural variant, known as in HHD, features a modification of the amino acid from M to R at position 641.
+The protein's natural variant, known as in HHD, features a modification of the amino acid from G to R at position 645.
+The protein's natural variant, known as in HHD;, features a modification of the amino acid from T to M at position 709.
+The protein's natural variant, known as in HHD, features a modification of the amino acid from A to D at position 731.
+The protein's natural variant, known as in HHD; impairs calcium- and manganese-dependent autophosphorylation, features a modification of the amino acid from D to Y at position 742.
+The protein's natural variant, known as in HHD, features a modification of the amino acid from P to R at position 744.
+The protein's natural variant, known as in HHD; decreases protein expression, features a modification of the amino acid from G to R at position 789.
+The protein's natural variant, known as in IDDAM; unknown pathological significance;, features a modification of the amino acid from V to I at position 744.
+The natural variant of this protein is characterized by an amino acid alteration from T to I at position 57.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 105.
+The natural variant of this protein is characterized by an amino acid alteration from S to A at position 134.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from S to I at position 442.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from R to C at position 66.
+The protein's natural variant, known as in MYP6; unknown pathological significance;, features a modification of the amino acid from R to W at position 112.
+The protein's natural variant, known as in MYP6; remains stable in mitochondria; reduces the level of the protein copurifying with COA6 by 80%;, features a modification of the amino acid from R to H at position 114.
+The protein's natural variant, known as in MYP6; unknown pathological significance;, features a modification of the amino acid from R to W at position 120.
+The protein's natural variant, known as in MC4DN2;, features a modification of the amino acid from C to Y at position 133.
+The protein's natural variant, known as in MC4DN2 and MYP6; reduced cytochrome c oxidase subunit II synthesis and reduced ability to regulate cellular copper homeostasis;, features a modification of the amino acid from E to K at position 140.
+The protein's natural variant, known as in MC4DN2; renders the protein unstable;, features a modification of the amino acid from R to W at position 171.
+The protein's natural variant, known as in MC4DN2;, features a modification of the amino acid from G to S at position 193.
+The protein's natural variant, known as in MC4DN2;, features a modification of the amino acid from S to F at position 225.
+The protein's natural variant, known as in MC4DN2;, features a modification of the amino acid from M to T at position 258.
+The protein's natural variant, known as in MYP6; likely benign variant;, features a modification of the amino acid from A to V at position 259.
+The protein's natural variant, known as in strain: Ryukyu wild boar 6, features a modification of the amino acid from V to I at position 123.
+The protein's natural variant, known as in strain: Ryukyu wild boar 6, features a modification of the amino acid from I to T at position 184.
+The protein's natural variant, known as in strain: Japanese wild boar 4, Japanese wild boar 11 and AWB10, features a modification of the amino acid from M to I at position 215.
+The protein's natural variant, known as in strain: Bulgarian 2 and Meishan, features a modification of the amino acid from V to M at position 295.
+The protein's natural variant, known as in strain: Asian domestic pig, Landrace, Chinese Diannan short-ear, Large white 1, Japanese wild boar, P2, Ryukyu wild boar, Satsumae 28, Seishan, Ssc2, AWB10, AWB11, EWB3 and LW1, features a modification of the amino acid from G to S at position 314.
+The protein's natural variant, known as in strain: IB9, IB14, IB16, Sardinian wild boar 2 and Ssc3, features a modification of the amino acid from I to V at position 368.
+The natural variant of this protein is characterized by an amino acid alteration from T to A at position 73.
+The protein's natural variant, known as in HIDEA;, features a modification of the amino acid from H to P at position 161.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from S to P at position 16.
+The protein's natural variant, known as in HPA;, features a modification of the amino acid from Q to L at position 20.
+The protein's natural variant, known as in HPA and PKU; haplotype 1;, features a modification of the amino acid from F to L at position 39.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from S to L at position 40.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from L to F at position 41.
+The protein's natural variant, known as in PKU; mild;, features a modification of the amino acid from L to P at position 41.
+The protein's natural variant, known as in PKU; haplotype 21;, features a modification of the amino acid from K to I at position 42.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from V to A at position 45.
+The protein's natural variant, known as in PKU; haplotype 5; significantly reduces phenylalanine binding;, features a modification of the amino acid from G to S at position 46.
+The protein's natural variant, known as in non-PKUHPA; haplotype 4; significantly reduces phenylalanine binding;, features a modification of the amino acid from A to V at position 47.
+The protein's natural variant, known as in PKU; mild; haplotypes 3,4;, features a modification of the amino acid from L to S at position 48.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from R to H at position 53.
+The protein's natural variant, known as in HPA and PKU; does not affect oligomerization; results in loss of substrate activation;, features a modification of the amino acid from F to L at position 55.
+The protein's natural variant, known as in PKU; haplotype 10;, features a modification of the amino acid from E to D at position 56.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from N to D at position 61.
+The protein's natural variant, known as in PKU, features a modification of the amino acid from L to P at position 62.
+The protein's natural variant, known as in PKU; haplotype 1; abolishes phenylalanine binding, features a modification of the amino acid from TH to PN at position 64.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from I to N at position 65.
+The protein's natural variant, known as in PKU; results in disturbed oligomerization; results in loss of substrate activation;, features a modification of the amino acid from I to S at position 65.
+The protein's natural variant, known as in PKU; haplotypes 1,5,9,21,B; abolishes phenylalanine binding;, features a modification of the amino acid from I to T at position 65.
+The protein's natural variant, known as in HPA and PKU;, features a modification of the amino acid from I to V at position 65.
+The protein's natural variant, known as in PKU; haplotype 4;, features a modification of the amino acid from S to P at position 67.
+The protein's natural variant, known as in PKU; haplotype 1;, features a modification of the amino acid from R to S at position 68.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from E to A at position 76.
+The protein's natural variant, known as in non-PKUHPA;, features a modification of the amino acid from E to G at position 76.
+The protein's natural variant, known as in PKU; haplotype 4;, features a modification of the amino acid from D to Y at position 84.
+The protein's natural variant, known as in non-PKUHPA; haplotype 1;, features a modification of the amino acid from S to R at position 87.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from T to I at position 92.
+The protein's natural variant, known as in non-PKUHPA;, features a modification of the amino acid from L to S at position 98.
+The protein's natural variant, known as in PKU; mild; haplotype 1;, features a modification of the amino acid from A to D at position 104.
+The protein's natural variant, known as in HPA, features a modification of the amino acid from S to C at position 110.
+The protein's natural variant, known as in HPA, features a modification of the amino acid from F to L at position 121.
+The protein's natural variant, known as in PKU; haplotype 28;, features a modification of the amino acid from T to I at position 124.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from D to Y at position 129.
+The protein's natural variant, known as in PKU; haplotype 11;, features a modification of the amino acid from D to G at position 143.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from D to V at position 145.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from H to Y at position 146.
+The protein's natural variant, known as in PKU; haplotypes 1,2,7;, features a modification of the amino acid from G to S at position 148.
+The protein's natural variant, known as in PKU; haplotypes 1,8;, features a modification of the amino acid from D to H at position 151.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from Y to N at position 154.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from R to P at position 155.
+The protein's natural variant, known as in PKU; severe; 5% activity; requires 2 nucleotide substitutions;, features a modification of the amino acid from R to N at position 157.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from R to S at position 157.
+The protein's natural variant, known as in PKU; haplotypes 1,2,4,7,16, 28;, features a modification of the amino acid from R to Q at position 158.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from R to W at position 158.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from Q to P at position 160.
+The protein's natural variant, known as in PKU; haplotype 4;, features a modification of the amino acid from F to S at position 161.
+The protein's natural variant, known as in PKU; haplotype 1;, features a modification of the amino acid from I to T at position 164.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from N to I at position 167.
+The protein's natural variant, known as in HPA;, features a modification of the amino acid from N to S at position 167.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from R to H at position 169.
+The protein's natural variant, known as in HPA;, features a modification of the amino acid from H to D at position 170.
+The protein's natural variant, known as in PKU; does not affect oligomerization;, features a modification of the amino acid from H to Q at position 170.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from H to R at position 170.
+The protein's natural variant, known as in PKU; haplotype 1;, features a modification of the amino acid from G to A at position 171.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from G to R at position 171.
+The protein's natural variant, known as in PKU; haplotype 4;, features a modification of the amino acid from P to T at position 173.
+The protein's natural variant, known as in PKU; haplotype 1;, features a modification of the amino acid from I to T at position 174.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from I to V at position 174.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from P to A at position 175.
+The protein's natural variant, known as in non-PKUHPA;, features a modification of the amino acid from R to L at position 176.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from R to P at position 176.
+The protein's natural variant, known as in PKU; haplotype 6;, features a modification of the amino acid from V to L at position 177.
+The protein's natural variant, known as in HPA;, features a modification of the amino acid from V to M at position 177.
+The protein's natural variant, known as in non-PKUHPA;, features a modification of the amino acid from E to G at position 178.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from E to Q at position 183.
+The protein's natural variant, known as in PKU; haplotype 3;, features a modification of the amino acid from V to A at position 190.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from L to P at position 194.
+The protein's natural variant, known as in HPA;, features a modification of the amino acid from S to Y at position 196.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from H to R at position 201.
+The protein's natural variant, known as in non-PKUHPA; haplotype 1;, features a modification of the amino acid from H to Y at position 201.
+The protein's natural variant, known as in PKU; mild; haplotypes 3,4;, features a modification of the amino acid from Y to C at position 204.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from E to A at position 205.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from Y to D at position 206.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from N to D at position 207.
+The protein's natural variant, known as in PKU; severe; haplotype 4;, features a modification of the amino acid from N to S at position 207.
+The protein's natural variant, known as in PKU; haplotype 4;, features a modification of the amino acid from P to T at position 211.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from L to P at position 212.
+The protein's natural variant, known as in PKU; severe;, features a modification of the amino acid from L to P at position 213.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from C to G at position 217.
+The protein's natural variant, known as in PKU; haplotypes 1,2;, features a modification of the amino acid from G to V at position 218.
+The protein's natural variant, known as in PKU; haplotype 4;, features a modification of the amino acid from E to G at position 221.
+The protein's natural variant, known as in PKU; haplotypes 3,4;, features a modification of the amino acid from D to V at position 222.
+The protein's natural variant, known as in PKU; haplotype 4;, features a modification of the amino acid from I to M at position 224.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from P to R at position 225.
+The protein's natural variant, known as in PKU; haplotype 1;, features a modification of the amino acid from P to T at position 225.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from Q to H at position 226.
+The protein's natural variant, known as in non-PKUHPA; haplotype 4;, features a modification of the amino acid from V to I at position 230.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from S to F at position 231.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from S to P at position 231.
+The protein's natural variant, known as in PKU; haplotypes 2,3;, features a modification of the amino acid from F to L at position 233.
+The protein's natural variant, known as in PKU; haplotype 4;, features a modification of the amino acid from T to P at position 238.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from G to S at position 239.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from F to S at position 240.
+The protein's natural variant, known as in non-PKUHPA and PKU; haplotype 34;, features a modification of the amino acid from R to C at position 241.
+The protein's natural variant, known as in PKU; haplotypes 1,5;, features a modification of the amino acid from R to H at position 241.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from R to L at position 241.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from L to F at position 242.
+The protein's natural variant, known as in non-PKUHPA and PKU; haplotypes 4,7,9;, features a modification of the amino acid from R to Q at position 243.
+The protein's natural variant, known as in PKU; haplotype 12;, features a modification of the amino acid from P to L at position 244.
+The protein's natural variant, known as in PKU, HPA and non-PKUHPA; haplotypes 3,7;, features a modification of the amino acid from V to A at position 245.
+The protein's natural variant, known as in PKU; haplotype 11;, features a modification of the amino acid from V to E at position 245.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from V to L at position 245.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from A to D at position 246.
+The protein's natural variant, known as in PKU; haplotype 4;, features a modification of the amino acid from G to V at position 247.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from L to P at position 248.
+The protein's natural variant, known as in PKU; haplotype 1;, features a modification of the amino acid from L to F at position 249.
+The protein's natural variant, known as in PKU; haplotype 7;, features a modification of the amino acid from R to G at position 252.
+The protein's natural variant, known as in PKU; haplotype 1;, features a modification of the amino acid from R to Q at position 252.
+The protein's natural variant, known as in PKU; haplotypes 1,6,7,8,42, 69; complete loss of activity;, features a modification of the amino acid from R to W at position 252.
+The protein's natural variant, known as in PKU; haplotype 36;, features a modification of the amino acid from L to S at position 255.
+The protein's natural variant, known as in PKU; haplotypes 18,21;, features a modification of the amino acid from L to V at position 255.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from G to C at position 257.
+The protein's natural variant, known as in PKU; haplotype 3;, features a modification of the amino acid from A to T at position 259.
+The protein's natural variant, known as in PKU; haplotypes 7,42;, features a modification of the amino acid from A to V at position 259.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from R to P at position 261.
+The protein's natural variant, known as in HPA and PKU; mild; haplotypes 1,2,4,22, 24,28;, features a modification of the amino acid from R to Q at position 261.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from F to L at position 263.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from H to L at position 264.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from C to G at position 265.
+The protein's natural variant, known as in non-PKUHPA;, features a modification of the amino acid from I to L at position 269.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from R to K at position 270.
+The protein's natural variant, known as in PKU; haplotype 1;, features a modification of the amino acid from R to S at position 270.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from H to Y at position 271.
+The protein's natural variant, known as in PKU; haplotype 7;, features a modification of the amino acid from S to F at position 273.
+The protein's natural variant, known as in PKU; reduced activity; increased affinity for the substrate; mildly reduced substrate activation; decreased cofactor affinity;, features a modification of the amino acid from P to L at position 275.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from M to I at position 276.
+The protein's natural variant, known as in PKU; haplotype 4;, features a modification of the amino acid from M to V at position 276.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from Y to C at position 277.
+The protein's natural variant, known as in PKU; haplotype 2;, features a modification of the amino acid from Y to D at position 277.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from T to A at position 278.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from T to N at position 278.
+The protein's natural variant, known as in PKU; haplotypes 1,2,4,16,38; partial residual activity;, features a modification of the amino acid from E to K at position 280.
+The protein's natural variant, known as in PKU; haplotypes 1,4;, features a modification of the amino acid from P to L at position 281.
+The protein's natural variant, known as in PKU; haplotype 1;, features a modification of the amino acid from D to N at position 282.
+The protein's natural variant, known as in PKU; haplotype 21;, features a modification of the amino acid from I to F at position 283.
+The protein's natural variant, known as in PKU; severe;, features a modification of the amino acid from I to N at position 283.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from H to Y at position 290.
+The protein's natural variant, known as in PKU; haplotype 4;, features a modification of the amino acid from R to C at position 297.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from R to H at position 297.
+The protein's natural variant, known as in PKU; haplotype 8;, features a modification of the amino acid from F to C at position 299.
+The protein's natural variant, known as in PKU and HPA; haplotype 1; does not affect oligomerization; reduction in activity is probably due to a global conformational change in the protein that reduces allostery;, features a modification of the amino acid from A to S at position 300.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from A to V at position 300.
+The protein's natural variant, known as in PKU; haplotype 5;, features a modification of the amino acid from S to P at position 303.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from Q to R at position 304.
+The protein's natural variant, known as in non-PKUHPA; haplotype 4;, features a modification of the amino acid from I to V at position 306.
+The protein's natural variant, known as in PKU; haplotype 7;, features a modification of the amino acid from A to D at position 309.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from A to V at position 309.
+The protein's natural variant, known as in PKU; haplotype 7;, features a modification of the amino acid from S to F at position 310.
+The protein's natural variant, known as in HPA; reduction in activity is probably due to a global conformational change in the protein that reduces allostery;, features a modification of the amino acid from S to Y at position 310.
+The protein's natural variant, known as in PKU; haplotypes 1,7,10;, features a modification of the amino acid from L to P at position 311.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from P to H at position 314.
+The protein's natural variant, known as in HPA; does not affect oligomerization; reduction in activity is probably due to a global conformational change in the protein that reduces allostery;, features a modification of the amino acid from P to S at position 314.
+The protein's natural variant, known as in PKU; partial loss of activity;, features a modification of the amino acid from I to T at position 318.
+The protein's natural variant, known as in PKU; haplotype 12;, features a modification of the amino acid from A to G at position 322.
+The protein's natural variant, known as in PKU; haplotype 1;, features a modification of the amino acid from A to T at position 322.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from A to V at position 322.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from Y to C at position 325.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from E to D at position 330.
+The protein's natural variant, known as in PKU; haplotype 1;, features a modification of the amino acid from F to L at position 331.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from L to F at position 333.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from C to S at position 334.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from G to V at position 337.
+The protein's natural variant, known as in PKU; haplotype 4;, features a modification of the amino acid from D to Y at position 338.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from K to R at position 341.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from K to T at position 341.
+The protein's natural variant, known as in PKU; haplotype 5;, features a modification of the amino acid from A to T at position 342.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from Y to C at position 343.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from G to R at position 344.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from G to V at position 344.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from A to S at position 345.
+The protein's natural variant, known as in PKU; haplotype 7;, features a modification of the amino acid from A to T at position 345.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from L to F at position 347.
+The protein's natural variant, known as in PKU; mild haplotype 9;, features a modification of the amino acid from L to V at position 348.
+The protein's natural variant, known as in PKU; severe;, features a modification of the amino acid from S to L at position 349.
+The protein's natural variant, known as in PKU; haplotypes 1,4;, features a modification of the amino acid from S to P at position 349.
+The protein's natural variant, known as in PKU; haplotype 2;, features a modification of the amino acid from S to T at position 350.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from C to G at position 357.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from P to T at position 362.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from P to H at position 366.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from T to S at position 372.
+The protein's natural variant, known as in PKU; haplotype 4;, features a modification of the amino acid from Y to C at position 377.
+The protein's natural variant, known as in non-PKUHPA; haplotype 4;, features a modification of the amino acid from T to M at position 380.
+The protein's natural variant, known as in PKU; common mutation;, features a modification of the amino acid from Y to C at position 386.
+The protein's natural variant, known as in PKU; haplotype 1;, features a modification of the amino acid from Y to H at position 387.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from V to L at position 388.
+The protein's natural variant, known as in PKU; haplotypes 1,4;, features a modification of the amino acid from V to M at position 388.
+The protein's natural variant, known as in PKU and non-PKUHPA; haplotype 4;, features a modification of the amino acid from E to G at position 390.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from D to A at position 394.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from D to H at position 394.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from A to G at position 395.
+The protein's natural variant, known as in PKU; haplotype 1;, features a modification of the amino acid from A to P at position 395.
+The protein's natural variant, known as in non-PKUHPA and PKU; haplotype 43;, features a modification of the amino acid from A to V at position 403.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from P to L at position 407.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from P to S at position 407.
+The protein's natural variant, known as in PKU; haplotypes 4,12;, features a modification of the amino acid from R to Q at position 408.
+The protein's natural variant, known as in HPA and PKU; haplotypes 1,2,4,5,13,34, 41,44; most common mutation; reduction in activity is probably due to a global conformational change in the protein that reduces allostery;, features a modification of the amino acid from R to W at position 408.
+The protein's natural variant, known as in PKU; mild;, features a modification of the amino acid from F to S at position 410.
+The protein's natural variant, known as in non-PKUHPA and PKU; haplotype 4;, features a modification of the amino acid from R to P at position 413.
+The protein's natural variant, known as in PKU; haplotype 1;, features a modification of the amino acid from R to S at position 413.
+The protein's natural variant, known as in HPA and PKU; haplotype 4; does not affect oligomerization; reduction in activity is probably due to a global conformational change in the protein that reduces allostery;, features a modification of the amino acid from Y to C at position 414.
+The protein's natural variant, known as in PKU, HPA and non-PKUHPA; haplotype 1;, features a modification of the amino acid from D to N at position 415.
+The protein's natural variant, known as in PKU; reduction in activity is probably due to a global conformational change in the protein that reduces allostery;, features a modification of the amino acid from Y to H at position 417.
+The protein's natural variant, known as in PKU; haplotype 4;, features a modification of the amino acid from T to P at position 418.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from I to S at position 421.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from L to P at position 430.
+The protein's natural variant, known as in PKU;, features a modification of the amino acid from A to D at position 447.
+The natural variant of this protein is characterized by an amino acid alteration from E to D at position 287.
+The protein's natural variant, known as in allele TLR4*B; reduced LPS-response; associated with an increased risk for age-related macular degeneration in Caucasian carriers;, features a modification of the amino acid from D to G at position 299.
+The protein's natural variant, known as in allele TLR4*B; reduced LPS-response;, features a modification of the amino acid from T to I at position 399.
+The natural variant of this protein is characterized by an amino acid alteration from Q to H at position 834.
+The natural variant of this protein is characterized by an amino acid alteration from I to T at position 1130.
+The protein's natural variant, known as in SIHIWES;, features a modification of the amino acid from S to Y at position 851.
+The protein's natural variant, known as in SIHIWES, features a modification of the amino acid from G to D at position 1003.
+The protein's natural variant, known as in SIHIWES;, features a modification of the amino acid from R to H at position 1068.
+The protein's natural variant, known as in SIHIWES; no effect on interaction with HDAC1; no effect on nuclear localization;, features a modification of the amino acid from R to Q at position 1127.
+The protein's natural variant, known as in SIHIWES;, features a modification of the amino acid from W to L at position 1148.
+The protein's natural variant, known as in SIHIWES; no effect on interaction with HDAC1; no effect on nuclear localization;, features a modification of the amino acid from R to L at position 1173.
+The protein's natural variant, known as in SIHIWES; unknown pathological significance;, features a modification of the amino acid from V to I at position 1608.
+The protein's natural variant, known as in allele LMP7C;, features a modification of the amino acid from G to R at position 8.
+The protein's natural variant, known as in allele LPM7C, features a modification of the amino acid from PGH to RPD at position 32.
+The protein's natural variant, known as in PRAAS1; markedly decreased chymotrypsin-like activity consistent with a decrease in proteasomal activity and loss of function; some patients are heterozygotes for this mutation and also carry a mutation in PSMA3; patients' cells show reduction of proteasome content and endopeptidase activity of the proteasome;, features a modification of the amino acid from T to M at position 75.
+The protein's natural variant, known as in PRAAS1; unknown pathological significance, features a modification of the amino acid from A to P at position 94.
+The protein's natural variant, known as in PRAAS1; some patients are heterozygotes for this mutation and also carry a mutation in PSMB4;, features a modification of the amino acid from K to Q at position 105.
+The protein's natural variant, known as in PRAAS1; affects immunoproteasome assembly; reduced proteasome levels; reduced chymotrypsin-like activity consistent with a decrease in proteasomal activity;, features a modification of the amino acid from G to V at position 201.
+The protein's natural variant, known as in CADASIL1, features a modification of the amino acid from C to G at position 43.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from C to F at position 49.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from C to Y at position 49.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from R to C at position 54.
+The protein's natural variant, known as in CADASIL1, features a modification of the amino acid from S to C at position 60.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from C to S at position 65.
+The protein's natural variant, known as in CADASIL1, features a modification of the amino acid from C to Y at position 67.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from W to C at position 71.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from C to R at position 76.
+The protein's natural variant, known as in CADASIL1, features a modification of the amino acid from C to W at position 76.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from C to R at position 87.
+The protein's natural variant, known as in CADASIL1, features a modification of the amino acid from C to Y at position 87.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from R to C at position 90.
+The protein's natural variant, known as in CADASIL1, features a modification of the amino acid from C to F at position 93.
+The protein's natural variant, known as in CADASIL1, features a modification of the amino acid from C to Y at position 93.
+The protein's natural variant, known as in CADASIL1, features a modification of the amino acid from C to W at position 106.
+The protein's natural variant, known as in CADASIL1, features a modification of the amino acid from C to W at position 108.
+The protein's natural variant, known as in CADASIL1, features a modification of the amino acid from C to Y at position 108.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from R to C at position 110.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from C to F at position 117.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from S to C at position 118.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from C to F at position 123.
+The protein's natural variant, known as in CADASIL1, features a modification of the amino acid from C to Y at position 123.
+The protein's natural variant, known as in CADASIL1, features a modification of the amino acid from C to Y at position 128.
+The protein's natural variant, known as in CADASIL1; no effect on ligand-binding; no effect on cell membrane localization; reduced proteolytic processing;, features a modification of the amino acid from R to C at position 133.
+The protein's natural variant, known as in CADASIL1, features a modification of the amino acid from C to W at position 134.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from R to C at position 141.
+The protein's natural variant, known as in CADASIL1, features a modification of the amino acid from F to C at position 142.
+The protein's natural variant, known as in CADASIL1, features a modification of the amino acid from C to F at position 144.
+The protein's natural variant, known as in CADASIL1, features a modification of the amino acid from C to S at position 144.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from C to Y at position 144.
+The protein's natural variant, known as in CADASIL1, features a modification of the amino acid from S to C at position 145.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from C to R at position 146.
+The protein's natural variant, known as in CADASIL1, features a modification of the amino acid from G to C at position 149.
+The protein's natural variant, known as in CADASIL1, features a modification of the amino acid from Y to C at position 150.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from R to C at position 153.
+The protein's natural variant, known as in CADASIL1, features a modification of the amino acid from C to S at position 155.
+The protein's natural variant, known as in CADASIL1, features a modification of the amino acid from C to S at position 162.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from R to C at position 169.
+The protein's natural variant, known as in CADASIL1, features a modification of the amino acid from G to C at position 171.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from C to F at position 174.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from C to R at position 174.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from C to Y at position 174.
+The protein's natural variant, known as in CADASIL1, features a modification of the amino acid from S to C at position 180.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from R to C at position 182.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from C to F at position 183.
+The protein's natural variant, known as in CADASIL1; no effect on ligand-binding; no effect on cell membrane localization; reduced proteolytic processing, features a modification of the amino acid from C to R at position 183.
+The protein's natural variant, known as in CADASIL1, features a modification of the amino acid from C to S at position 183.
+The protein's natural variant, known as in CADASIL1, features a modification of the amino acid from C to G at position 185.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from C to R at position 185.
+The protein's natural variant, known as in CADASIL1, features a modification of the amino acid from Y to C at position 189.
+The protein's natural variant, known as in CADASIL1, features a modification of the amino acid from C to F at position 194.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from C to R at position 194.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from C to S at position 194.
+The protein's natural variant, known as in CADASIL1, features a modification of the amino acid from C to Y at position 194.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from C to Y at position 201.
+The protein's natural variant, known as in CADASIL1, features a modification of the amino acid from C to Y at position 206.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from R to C at position 207.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from C to S at position 212.
+The protein's natural variant, known as in CADASIL1, features a modification of the amino acid from R to K at position 213.
+The protein's natural variant, known as in CADASIL1, features a modification of the amino acid from C to G at position 222.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from C to Y at position 222.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from C to Y at position 224.
+The protein's natural variant, known as in CADASIL1, features a modification of the amino acid from C to S at position 233.
+The protein's natural variant, known as in CADASIL1, features a modification of the amino acid from C to Y at position 233.
+The protein's natural variant, known as in CADASIL1, features a modification of the amino acid from C to S at position 240.
+The protein's natural variant, known as in CADASIL1, features a modification of the amino acid from C to R at position 245.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from C to R at position 251.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from Y to C at position 258.
+The protein's natural variant, known as in CADASIL1, features a modification of the amino acid from C to Y at position 260.
+The protein's natural variant, known as in CADASIL1; requires 2 nucleotide substitutions, features a modification of the amino acid from A to C at position 319.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from R to C at position 332.
+The protein's natural variant, known as in CADASIL1, features a modification of the amino acid from S to C at position 335.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from Y to C at position 337.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from C to S at position 379.
+The protein's natural variant, known as in CADASIL1, features a modification of the amino acid from C to R at position 395.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from G to C at position 420.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from R to C at position 421.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from C to S at position 428.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from C to Y at position 428.
+The protein's natural variant, known as in CADASIL1, features a modification of the amino acid from C to G at position 440.
+The protein's natural variant, known as in CADASIL1, features a modification of the amino acid from C to R at position 440.
+The protein's natural variant, known as in CADASIL1, features a modification of the amino acid from C to S at position 446.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from R to C at position 449.
+The protein's natural variant, known as in CADASIL1; impaired ligand-binding; strongly reduced signaling activity; no effect on cell membrane localization; reduced proteolytic processing;, features a modification of the amino acid from C to R at position 455.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from C to F at position 484.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from C to Y at position 484.
+The protein's natural variant, known as in CADASIL1, features a modification of the amino acid from C to Y at position 495.
+The protein's natural variant, known as in CADASIL1, features a modification of the amino acid from C to R at position 511.
+The protein's natural variant, known as in CADASIL1, features a modification of the amino acid from C to Y at position 542.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from R to C at position 544.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from C to Y at position 549.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from R to C at position 558.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from R to C at position 578.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from R to C at position 607.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from Y to C at position 710.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from R to C at position 728.
+The protein's natural variant, known as in CADASIL1, features a modification of the amino acid from C to S at position 775.
+The protein's natural variant, known as in CADASIL1, features a modification of the amino acid from G to C at position 953.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from F to C at position 984.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from R to C at position 985.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from R to C at position 1006.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from C to R at position 1015.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from Y to C at position 1021.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from R to C at position 1031.
+The protein's natural variant, known as in CADASIL1; requires 2 nucleotide substitutions, features a modification of the amino acid from D to C at position 1063.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from R to C at position 1231.
+The protein's natural variant, known as in CADASIL1, features a modification of the amino acid from C to R at position 1261.
+The protein's natural variant, known as in CADASIL1;, features a modification of the amino acid from C to Y at position 1261.
+The protein's natural variant, known as in brain small-vessel-disease; exhibits increased NOTCH3 signaling in a ligand-independent fashion, features a modification of the amino acid from L to P at position 1515.
+The protein's natural variant, known as in IMF2;, features a modification of the amino acid from L to P at position 1519.
+The protein's natural variant, known as in GRTHD; impairs hormone binding and ligand-dependent conformational changes;, features a modification of the amino acid from A to T at position 234.
+The protein's natural variant, known as in GRTHD;, features a modification of the amino acid from R to W at position 243.
+The protein's natural variant, known as in GRTHD, features a modification of the amino acid from A to G at position 268.
+The protein's natural variant, known as in PRTH; impairs hormone binding;, features a modification of the amino acid from R to H at position 316.
+The protein's natural variant, known as in GRTHD; impairs hormone binding;, features a modification of the amino acid from A to T at position 317.
+The protein's natural variant, known as in GRTHD;, features a modification of the amino acid from R to C at position 320.
+The protein's natural variant, known as in GRTHD;, features a modification of the amino acid from R to H at position 320.
+The protein's natural variant, known as in GRTHD, features a modification of the amino acid from N to D at position 331.
+The protein's natural variant, known as in GRTHD;, features a modification of the amino acid from G to R at position 332.
+The protein's natural variant, known as in GRTHD, features a modification of the amino acid from A to P at position 335.
+The protein's natural variant, known as in GRTHD;, features a modification of the amino acid from R to W at position 338.
+The protein's natural variant, known as in GRTHD;, features a modification of the amino acid from Q to H at position 340.
+The protein's natural variant, known as in GRTHD, features a modification of the amino acid from L to P at position 341.
+The protein's natural variant, known as in GRTHD, features a modification of the amino acid from K to I at position 342.
+The protein's natural variant, known as in GRTHD;, features a modification of the amino acid from G to R at position 345.
+The protein's natural variant, known as in GRTHD;, features a modification of the amino acid from G to S at position 345.
+The protein's natural variant, known as in GRTHD;, features a modification of the amino acid from G to V at position 345.
+The protein's natural variant, known as in GRTHD, features a modification of the amino acid from L to F at position 346.
+The protein's natural variant, known as in GRTHD;, features a modification of the amino acid from G to E at position 347.
+The protein's natural variant, known as in GRTHD, features a modification of the amino acid from V to E at position 348.
+The protein's natural variant, known as in GRTHD, features a modification of the amino acid from T to I at position 426.
+The protein's natural variant, known as in PRTH;, features a modification of the amino acid from R to Q at position 429.
+The protein's natural variant, known as in GRTHD;, features a modification of the amino acid from I to M at position 431.
+The protein's natural variant, known as in GRTHD;, features a modification of the amino acid from R to H at position 438.
+The protein's natural variant, known as in GRTHD;, features a modification of the amino acid from M to V at position 442.
+The protein's natural variant, known as in GRTHD;, features a modification of the amino acid from K to E at position 443.
+The protein's natural variant, known as in GRTHD;, features a modification of the amino acid from C to R at position 446.
+The protein's natural variant, known as in GRTHD, features a modification of the amino acid from P to T at position 447.
+The protein's natural variant, known as in GRTHD;, features a modification of the amino acid from P to H at position 453.
+The protein's natural variant, known as in GRTHD, features a modification of the amino acid from P to L at position 453.
+The protein's natural variant, known as in GRTHD;, features a modification of the amino acid from P to S at position 453.
+The protein's natural variant, known as in GRTHD;, features a modification of the amino acid from P to T at position 453.
+The protein's natural variant, known as in GRTHD;, features a modification of the amino acid from F to C at position 459.
+The protein's natural variant, known as in SCOLIV; unknown pathological significance; when associated with P-1232, features a modification of the amino acid from R to C at position 563.
+The protein's natural variant, known as in SCOLIV; unknown pathological significance, features a modification of the amino acid from G to R at position 1177.
+The protein's natural variant, known as in SCOLIV; unknown pathological significance; when associated with C-563, features a modification of the amino acid from A to P at position 1232.
+The protein's natural variant, known as in SCOLIV; unknown pathological significance, features a modification of the amino acid from K to N at position 1668.
+The protein's natural variant, known as in SCOLIV; unknown pathological significance, features a modification of the amino acid from L to P at position 1780.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from D to H at position 301.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from G to E at position 479.
+The protein's natural variant, known as in a cutaneous metastatic melanoma sample; somatic mutation, features a modification of the amino acid from G to E at position 712.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from L to F at position 792.
+The protein's natural variant, known as in a cutaneous metastatic melanoma sample; somatic mutation;, features a modification of the amino acid from P to S at position 893.
+The protein's natural variant, known as in DFNB25;, features a modification of the amino acid from P to L at position 38.
+The protein's natural variant, known as in DFNB25;, features a modification of the amino acid from G to S at position 64.
+The protein's natural variant, known as in DFNB25;, features a modification of the amino acid from R to C at position 138.
+The protein's natural variant, known as in DFNB25;, features a modification of the amino acid from F to V at position 153.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from R to Q at position 417.
+The protein's natural variant, known as in a lung large cell carcinoma sample; somatic mutation, features a modification of the amino acid from E to K at position 503.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from G to E at position 582.
+The protein's natural variant, known as in a lung squamous cell carcinoma sample; somatic mutation, features a modification of the amino acid from T to I at position 856.
+The protein's natural variant, known as in a lung large cell carcinoma sample; somatic mutation, features a modification of the amino acid from N to S at position 1032.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from M to T at position 133.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from R to Q at position 211.
+The protein's natural variant, known as in HLTS;, features a modification of the amino acid from W to R at position 95.
+The protein's natural variant, known as in HLTS;, features a modification of the amino acid from A to P at position 104.
+The protein's natural variant, known as in PBD-CG3; benign variant;, features a modification of the amino acid from R to S at position 34.
+The protein's natural variant, known as in PBD3B; attenuates interaction with PEX10 and decreases peroxisomal protein import;, features a modification of the amino acid from S to F at position 320.
+The protein's natural variant, known as in strain: cv. Glen, features a modification of the amino acid from Y to T at position 66.
+The protein's natural variant, known as in strain: cv. Glen, features a modification of the amino acid from H to D at position 92.
+The protein's natural variant, known as in strain: cv. Glen, features a modification of the amino acid from S to C at position 316.
+The protein's natural variant, known as in GSD9D;, features a modification of the amino acid from D to V at position 299.
+The protein's natural variant, known as in strain: C3H/He, features a modification of the amino acid from A to V at position 192.
+The protein's natural variant, known as in strain: YJM339, features a modification of the amino acid from V to A at position 188.
+The protein's natural variant, known as in strain: YJM280, YJM 20 and YJM339, features a modification of the amino acid from L to H at position 301.
+The protein's natural variant, known as in strain: YJM627, features a modification of the amino acid from S to P at position 319.
+The protein's natural variant, known as in strain: YJM339, features a modification of the amino acid from D to N at position 494.
+The protein's natural variant, known as in strain: SK1, V1-09, YJM269, YJM270, YJM280, YJM320, YJM326, YJM339, YJM627 and YJM1129, features a modification of the amino acid from I to T at position 505.
+The protein's natural variant, known as in strain: YJM269, YJM270, YJM326 and YJM1129, features a modification of the amino acid from G to D at position 522.
+The protein's natural variant, known as in strain: YJM280 and YJM320, features a modification of the amino acid from N to T at position 547.
+The protein's natural variant, known as in strain: YJM269, YJM270, YJM326 and YJM1129, features a modification of the amino acid from S to R at position 567.
+The protein's natural variant, known as in strain: YJM269, YJM270, YJM280, YJM320, YJM326 and YJM1129, features a modification of the amino acid from N to S at position 574.
+The protein's natural variant, known as in strain: V1-09, YJM269, YJM270, YJM280, YJM320, YJM326, YJM339 and YJM1129, features a modification of the amino acid from S to N at position 577.
+The protein's natural variant, known as in strain: V1-09 and YJM339, features a modification of the amino acid from G to S at position 622.
+The protein's natural variant, known as in strain: YJM280 and YJM320, features a modification of the amino acid from D to G at position 650.
+The protein's natural variant, known as in strain: YJM269 and YJM270, features a modification of the amino acid from P to S at position 740.
+The protein's natural variant, known as in strain: YJM 69, YJM270, YJM326 and YJM1129, features a modification of the amino acid from T to A at position 807.
+The protein's natural variant, known as in strain: YJM269, YJM270, YJM280, YJM320, YJM326 and YJM1129, features a modification of the amino acid from S to P at position 823.
+The protein's natural variant, known as in strain: YJM280 and YJM320, features a modification of the amino acid from D to N at position 835.
+The protein's natural variant, known as in strain: V1-09, features a modification of the amino acid from G to V at position 844.
+The protein's natural variant, known as in strain: YJM280, YJM320 and YJM627, features a modification of the amino acid from S to P at position 851.
+The protein's natural variant, known as in strain: YJM269, YJM270, YJM326 and YJM1129, features a modification of the amino acid from M to I at position 854.
+The protein's natural variant, known as in strain: YJM269 and YJM270, features a modification of the amino acid from E to Q at position 864.
+The protein's natural variant, known as in strain: YJM269, YJM270, YJM326 and YJM1129, features a modification of the amino acid from L to S at position 865.
+The protein's natural variant, known as in strain: YJM627, features a modification of the amino acid from D to A at position 866.
+The protein's natural variant, known as in strain: YJM280 and YJM320, features a modification of the amino acid from A to T at position 909.
+The protein's natural variant, known as in strain: YJM627, features a modification of the amino acid from I to L at position 945.
+The protein's natural variant, known as in strain: V1-09, features a modification of the amino acid from D to E at position 951.
+The protein's natural variant, known as in alpha-2, features a modification of the amino acid from T to S at position 8.
+The protein's natural variant, known as in alpha-1, features a modification of the amino acid from G to D at position 15.
+The protein's natural variant, known as in alpha-2, features a modification of the amino acid from H to Q at position 78.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from A to V at position 392.
+The protein's natural variant, known as in TOLCAS; unknown pathological significance, features a modification of the amino acid from W to C at position 161.
+The protein's natural variant, known as in TOLCAS; unknown pathological significance, features a modification of the amino acid from M to T at position 625.
+The protein's natural variant, known as in TOLCAS; unknown pathological significance, features a modification of the amino acid from W to R at position 659.
+The protein's natural variant, known as in TOLCAS; unknown pathological significance, features a modification of the amino acid from S to L at position 766.
+The protein's natural variant, known as in IDDOF; decreased protein abundance in patient cells; decreased function suggested by rescue assays in mutant fly, features a modification of the amino acid from R to W at position 671.
+The protein's natural variant, known as in HALP2;, features a modification of the amino acid from K to E at position 78.
+The protein's natural variant, known as in C-III-0; unglycosylated;, features a modification of the amino acid from T to A at position 94.
+The natural variant of this protein is characterized by an amino acid alteration from E to Q at position 56.
+The protein's natural variant, known as in SMDCRD;, features a modification of the amino acid from A to T at position 99.
+The protein's natural variant, known as in SMDCRD;, features a modification of the amino acid from A to V at position 99.
+The protein's natural variant, known as in SMDCRD;, features a modification of the amino acid from E to K at position 129.
+The protein's natural variant, known as in SMDCRD;, features a modification of the amino acid from P to A at position 150.
+The protein's natural variant, known as in SMDCRD;, features a modification of the amino acid from F to L at position 191.
+The protein's natural variant, known as in SMDCRD;, features a modification of the amino acid from R to S at position 223.
+The protein's natural variant, known as in strain: cv. Wassilewskija, features a modification of the amino acid from K to KES at position 340.
+The protein's natural variant, known as in LCA19; unknown pathological significance, features a modification of the amino acid from R to Q at position 312.
+The natural variant of this protein is characterized by an amino acid alteration from E to K at position 441.
+The protein's natural variant, known as in strain: RM 7004, features a modification of the amino acid from A to P at position 285.
+The protein's natural variant, known as in strain: RM 7004, features a modification of the amino acid from P to S at position 333.
+The protein's natural variant, known as in strain: 12261, features a modification of the amino acid from E to D at position 29.
+The protein's natural variant, known as in strain: 12261, features a modification of the amino acid from V to I at position 51.
+The protein's natural variant, known as in strain: 12261, features a modification of the amino acid from N to D at position 58.
+The protein's natural variant, known as in strain: 12261, features a modification of the amino acid from T to K at position 131.
+The protein's natural variant, known as in VEXAS; somatic mutation; the underlying nucleotide substitution affects normal alternative translation initiation and leads to aberrant initiation from M-67 to produce a shorter protein with strongly reduced enzymatic activity, features a modification of the amino acid from M to L at position 41.
+The protein's natural variant, known as in VEXAS; somatic mutation; the underlying nucleotide substitution affects normal alternative translation initiation and leads to aberrant initiation from M-67 to produce a shorter protein with strongly reduced enzymatic activity, features a modification of the amino acid from M to T at position 41.
+The protein's natural variant, known as in VEXAS; somatic mutation; does not affect ubiquitin activating enzyme activity; does not affect subcellular localization; the underlying nucleotide substitution affects normal alternative translation initiation and leads to aberrant initiation from M-67 to produce a shorter protein with strongly reduced enzymatic activity, features a modification of the amino acid from M to V at position 41.
+The protein's natural variant, known as in SMAX2;, features a modification of the amino acid from M to I at position 539.
+The protein's natural variant, known as in SMAX2;, features a modification of the amino acid from S to G at position 547.
+The protein's natural variant, known as in SMAX2, features a modification of the amino acid from E to V at position 557.
+The protein's natural variant, known as in CISS1;, features a modification of the amino acid from L to P at position 74.
+The protein's natural variant, known as in CISS1, features a modification of the amino acid from Y to D at position 75.
+The protein's natural variant, known as in CISS1;, features a modification of the amino acid from W to G at position 76.
+The protein's natural variant, known as in CISS1;, features a modification of the amino acid from R to H at position 81.
+The protein's natural variant, known as in CISS1; together with P-114, features a modification of the amino acid from N to I at position 113.
+The protein's natural variant, known as in CISS1; together with I-113;, features a modification of the amino acid from L to P at position 114.
+The protein's natural variant, known as in CISS1;, features a modification of the amino acid from P to L at position 138.
+The protein's natural variant, known as in CISS1, features a modification of the amino acid from S to P at position 145.
+The protein's natural variant, known as in CISS1;, features a modification of the amino acid from R to C at position 216.
+The protein's natural variant, known as in CISS1;, features a modification of the amino acid from F to S at position 268.
+The protein's natural variant, known as in CISS1;, features a modification of the amino acid from W to C at position 284.
+The protein's natural variant, known as in CISS1;, features a modification of the amino acid from R to P at position 312.
+The protein's natural variant, known as in CISS1;, features a modification of the amino acid from R to C at position 340.
+The protein's natural variant, known as in CISS1;, features a modification of the amino acid from L to R at position 374.
+The protein's natural variant, known as in CLCRP2;, features a modification of the amino acid from Q to P at position 978.
+The protein's natural variant, known as in CLCRP2;, features a modification of the amino acid from S to F at position 1015.
+The natural variant of this protein is characterized by an amino acid alteration from N to R at position 9.
+The natural variant of this protein is characterized by an amino acid alteration from I to L at position 10.
+The protein's natural variant, known as in allele 6M1-18*02;, features a modification of the amino acid from A to T at position 165.
+The protein's natural variant, known as in strain: NCPPB 1125, features a modification of the amino acid from L to I at position 177.
+The protein's natural variant, known as in strain: NCPPB 1125, features a modification of the amino acid from K to R at position 199.
+The protein's natural variant, known as in strain: NCPPB 1125, features a modification of the amino acid from M to L at position 288.
+The protein's natural variant, known as in strain: NCPPB 1125, features a modification of the amino acid from I to M at position 295.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from G to R at position 92.
+The protein's natural variant, known as found in patients with isolated growth hormone deficiency;, features a modification of the amino acid from T to A at position 3.
+The protein's natural variant, known as in IGHD1B; suppresses secretion, features a modification of the amino acid from L to P at position 16.
+The protein's natural variant, known as in IGHD1B, features a modification of the amino acid from D to N at position 37.
+The protein's natural variant, known as in IGHD1B; reduced secretion;, features a modification of the amino acid from R to C at position 42.
+The protein's natural variant, known as in IGHD1B; reduced ability to activate the JAK/STAT pathway, features a modification of the amino acid from T to I at position 53.
+The protein's natural variant, known as in IGHD1B; reduced ability to activate the JAK/STAT pathway, features a modification of the amino acid from K to R at position 67.
+The protein's natural variant, known as in IGHD1B; reduced ability to activate the JAK/STAT pathway;, features a modification of the amino acid from N to D at position 73.
+The protein's natural variant, known as in short stature; idiopathic autosomal; affects binding affinity of GH for GHR and the potency of GH to activate the JAK2/STAT5 signaling pathway;, features a modification of the amino acid from C to S at position 79.
+The protein's natural variant, known as in IGHD1B; reduced ability to activate the JAK/STAT pathway, features a modification of the amino acid from S to F at position 97.
+The protein's natural variant, known as in IGHD1B, features a modification of the amino acid from E to K at position 100.
+The protein's natural variant, known as in KWKS; no effect on GHR signaling pathway; does not affect interaction with GHR; results in a stronger interaction with GHBP; does not affect subcellular location;, features a modification of the amino acid from R to C at position 103.
+The protein's natural variant, known as in IGHD1B; reduced secretion, features a modification of the amino acid from Q to L at position 117.
+The protein's natural variant, known as in IGHD1B, features a modification of the amino acid from S to C at position 134.
+The protein's natural variant, known as in IGHD1B; reduced ability to activate the JAK/STAT pathway, features a modification of the amino acid from S to R at position 134.
+The protein's natural variant, known as in KWKS; loss of activity;, features a modification of the amino acid from D to G at position 138.
+The protein's natural variant, known as in IGHD1B; reduced ability to activate the JAK/STAT pathway, features a modification of the amino acid from T to A at position 201.
+The protein's natural variant, known as in short stature; idiopathic autosomal;, features a modification of the amino acid from I to M at position 205.
+The protein's natural variant, known as in IGHD2;, features a modification of the amino acid from R to H at position 209.
+The protein's natural variant, known as in MRT18; specifically impairs the response of JUN and FOS immediate early genes to serum mitogens by altering the interaction between enhancer-bound transcription factors TCF7L2 and ELK1 and the Mediator complex;, features a modification of the amino acid from R to Q at position 611.
+The protein's natural variant, known as in strain: IL1403, features a modification of the amino acid from V to M at position 128.
+The protein's natural variant, known as in strain: IL1403, features a modification of the amino acid from A to T at position 308.
+The protein's natural variant, known as in BBS9; severe loss of protein stability, probably due to aberrant folding;, features a modification of the amino acid from G to R at position 141.
+The protein's natural variant, known as in SPGF44; unknown pathological significance, features a modification of the amino acid from R to W at position 692.
+The protein's natural variant, known as in SPGF44; unknown pathological significance, features a modification of the amino acid from R to C at position 702.
+The protein's natural variant, known as in LUTO; unknown pathological significance;, features a modification of the amino acid from T to I at position 158.
+The protein's natural variant, known as in LUTO; unknown pathological significance;, features a modification of the amino acid from E to Q at position 346.
+The protein's natural variant, known as in LUTO;, features a modification of the amino acid from H to R at position 888.
+The protein's natural variant, known as in strain: Yak_5, features a modification of the amino acid from N to K at position 481.
+The protein's natural variant, known as in strain: Yak_4 and Yak_8, features a modification of the amino acid from S to N at position 526.
+The protein's natural variant, known as found in a patient with spinocerebellar ataxia; unknown pathological significance;, features a modification of the amino acid from D to N at position 1904.
+The natural variant of this protein is characterized by an amino acid alteration from S to A at position 55.
+The protein's natural variant, known as in DFNB29;, features a modification of the amino acid from R to H at position 81.
+The protein's natural variant, known as in DFNB29;, features a modification of the amino acid from V to D at position 85.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 86.
+The protein's natural variant, known as in DFNB29, features a modification of the amino acid from S to I at position 87.
+The protein's natural variant, known as in DFNB29, features a modification of the amino acid from A to V at position 94.
+The protein's natural variant, known as in DFNB29;, features a modification of the amino acid from G to R at position 232.
+The protein's natural variant, known as in NEDVIBA;, features a modification of the amino acid from G to E at position 414.
+The protein's natural variant, known as in NEDVIBA; no effect on the affinity for glucose or ATP; no effect on thermal stability;, features a modification of the amino acid from K to E at position 418.
+The protein's natural variant, known as in NEDVIBA; no effect on the affinity for glucose or ATP; no effect on thermal stability;, features a modification of the amino acid from S to L at position 445.
+The protein's natural variant, known as in NEDVIBA;, features a modification of the amino acid from T to M at position 457.
+The protein's natural variant, known as in HK deficiency;, features a modification of the amino acid from L to S at position 529.
+The protein's natural variant, known as in HK deficiency; HKUtrecht;, features a modification of the amino acid from T to S at position 680.
+The protein's natural variant, known as in RP79; unknown pathological significance; no effect on hexokinase activity; no effect on protein abundance;, features a modification of the amino acid from E to K at position 847.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from F to I at position 106.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from G to R at position 19.
+The protein's natural variant, known as in strain: MJBC 95.1, MJS 93 and VRF, features a modification of the amino acid from R to S at position 28.
+The protein's natural variant, known as in strain: MJBC 33.3, features a modification of the amino acid from T to S at position 71.
+The protein's natural variant, known as in strain: VRF, features a modification of the amino acid from A to T at position 92.
+The protein's natural variant, known as in strain: MJS 115, MJS 147.2F, MJS 16F, MJS 122, MJS 127, MJS 132, MJS 14, MJS 154, MJS 36, MJS 58.2, MJS 68, MJS 84 and MJS 87, features a modification of the amino acid from H to Y at position 98.
+The protein's natural variant, known as in strain: VRF, features a modification of the amino acid from V to L at position 112.
+The protein's natural variant, known as in strain: MJS 115, MJS 122, MJS 127, MJS 132, MJS 133, MJS 14, MJS 147.2F, MJS 154, MJS 16F, MJS 36, MJS 58.2, MJS 68, MJS 84, MJS 87, MJS 93 and VRF, features a modification of the amino acid from I to T at position 115.
+The protein's natural variant, known as in strain: MJS 115, MJS 122, MJS 127, MJS 132, MJS 133, MJS 14, MJS 147.2F, MJS 154, MJS 16F, MJS 36, MJS 58.2, MJS 68, MJS 84, MJS 87, MJS 93 and VRF, features a modification of the amino acid from V to I at position 136.
+The protein's natural variant, known as in strain: VRF, features a modification of the amino acid from Y to L at position 146.
+The protein's natural variant, known as in strain: VRF, features a modification of the amino acid from Q to P at position 147.
+The protein's natural variant, known as in strain: VRF, features a modification of the amino acid from E to Q at position 226.
+The protein's natural variant, known as in strain: MJS 115, MJS 122, MJS 127, MJS 132, MJS 133, MJS 14, MJS 147.2F, MJS 154, MJS 16F, MJS 36, MJS 58.2, MJS 68, MJS 84, MJS 87, MJS 93 and VRF, features a modification of the amino acid from V to L at position 236.
+The natural variant of this protein is characterized by an amino acid alteration from S to P at position 12.
+The protein's natural variant, known as in CMD2C; loss of phosphopantothenate--cysteine ligase activity; decreased protein abundance in patient fibroblasts;, features a modification of the amino acid from A to P at position 180.
+The protein's natural variant, known as in CMD2C; decreased phosphopantothenate--cysteine ligase activity; decreased protein abundance in patient fibroblasts;, features a modification of the amino acid from E to V at position 233.
+The protein's natural variant, known as in strain: 64147, features a modification of the amino acid from E to G at position 333.
+The protein's natural variant, known as in strain: 64147, features a modification of the amino acid from TQAYGSF to PAFSRPM at position 432.
+The protein's natural variant, known as in strain: 64147, features a modification of the amino acid from T to A at position 446.
+The protein's natural variant, known as in strain: 64147, features a modification of the amino acid from E to G at position 476.
+The protein's natural variant, known as in strain: 64147, features a modification of the amino acid from T to S at position 489.
+The protein's natural variant, known as in strain: 64147, features a modification of the amino acid from Y to F at position 512.
+The protein's natural variant, known as in strain: 64147, features a modification of the amino acid from N to D at position 538.
+The protein's natural variant, known as in strain: 64147, features a modification of the amino acid from G to E at position 597.
+The protein's natural variant, known as in strain: 64147, features a modification of the amino acid from QKY to NQH at position 676.
+The natural variant of this protein is characterized by an amino acid alteration from G to R at position 39.
+The natural variant of this protein is characterized by an amino acid alteration from S to L at position 54.
+The protein's natural variant, known as in MSUD2;, features a modification of the amino acid from I to M at position 98.
+The protein's natural variant, known as in MSUD2;, features a modification of the amino acid from F to C at position 276.
+The protein's natural variant, known as in MSUD2;, features a modification of the amino acid from G to S at position 384.
+The protein's natural variant, known as in allele B6, features a modification of the amino acid from E to A at position 35.
+The protein's natural variant, known as in allele B6, features a modification of the amino acid from G to S at position 42.
+The protein's natural variant, known as in allele B6, features a modification of the amino acid from D to E at position 45.
+The protein's natural variant, known as in allele B6, features a modification of the amino acid from V to I at position 48.
+The protein's natural variant, known as in allele B6, features a modification of the amino acid from D to E at position 65.
+The protein's natural variant, known as in allele B6, features a modification of the amino acid from L to M at position 75.
+The protein's natural variant, known as in allele B3, allele B4 and allele B5, features a modification of the amino acid from M to I at position 119.
+The protein's natural variant, known as in allele B6, features a modification of the amino acid from T to K at position 123.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 63.
+The natural variant of this protein is characterized by an amino acid alteration from N to F at position 76.
+The natural variant of this protein is characterized by an amino acid alteration from N to D at position 94.
+The natural variant of this protein is characterized by an amino acid alteration from A to S at position 104.
+The protein's natural variant, known as in NEDSSWI; decreased deoxyhypusine synthase activity;, features a modification of the amino acid from N to S at position 173.
+The protein's natural variant, known as moderately reduces phosphatase activity;, features a modification of the amino acid from S to F at position 201.
+The protein's natural variant, known as reduces risk of SLE and RA but not T1D; associated with reduced risk of ulcerative colitis but not of Crohn disease; severely reduces phosphatase activity;, features a modification of the amino acid from R to Q at position 263.
+The protein's natural variant, known as severely reduces phosphatase activity;, features a modification of the amino acid from R to W at position 266.
+The protein's natural variant, known as in T1D, RA, SLE and VTLG; also found in patients with Graves disease, Hashimoto thyroiditis and Addison disease; associated with reduced risk of Crohn disease but not of ulcerative colitis; affects CSK kinase binding; alters B cell receptor signaling and memory B cell proliferation;, features a modification of the amino acid from R to W at position 620.
+The protein's natural variant, known as in strain: Pasteur, features a modification of the amino acid from Y to C at position 151.
+The protein's natural variant, known as found in a patient with Joubert syndrome also carrying 2 mutations in MKS1 gene, a deletion in intron 15 and a missense mutation 'C-80'; unknown pathological significance;, features a modification of the amino acid from T to P at position 95.
+The protein's natural variant, known as in JBTS18;, features a modification of the amino acid from G to R at position 314.
+The protein's natural variant, known as in IDDFBA;, features a modification of the amino acid from R to S at position 138.
+The protein's natural variant, known as in IDDFBA;, features a modification of the amino acid from Q to R at position 156.
+The protein's natural variant, known as found in a patient with lymphoma;, features a modification of the amino acid from Y to C at position 206.
+The protein's natural variant, known as in IDDFBA;, features a modification of the amino acid from I to V at position 538.
+The protein's natural variant, known as in IDDFBA;, features a modification of the amino acid from T to R at position 623.
+The protein's natural variant, known as found in a lymphoma cell line; diminishes ubiquitin-mediated degradation of BCL6, features a modification of the amino acid from Y to C at position 644.
+The protein's natural variant, known as found in a patient with lymphoma; strongly diminishes ubiquitin-mediated degradation of BCL6, features a modification of the amino acid from G to E at position 684.
+The protein's natural variant, known as found in a patient with lymphoma; strongly diminishes ubiquitin-mediated degradation of BCL6;, features a modification of the amino acid from K to N at position 715.
+The protein's natural variant, known as found in a patient with lymphoma; almost abolishes ubiquitin-mediated degradation of BCL6, features a modification of the amino acid from K to Q at position 715.
+The protein's natural variant, known as in IDDFBA;, features a modification of the amino acid from S to P at position 840.
+The protein's natural variant, known as found in a patient with severe intellectual disability and muscular hypotonia; unknown pathological significance, features a modification of the amino acid from V to M at position 866.
+The protein's natural variant, known as in IDDFBA;, features a modification of the amino acid from A to D at position 892.
+The protein's natural variant, known as in IDDFBA;, features a modification of the amino acid from P to R at position 905.
+The protein's natural variant, known as in IDDFBA;, features a modification of the amino acid from D to G at position 910.
+The natural variant of this protein is characterized by an amino acid alteration from A to D at position 315.
+The protein's natural variant, known as related to abnormal induction of sister chromatid exchanges, features a modification of the amino acid from P to S at position 1006.
+The protein's natural variant, known as in RESDX; unknown pathological significance; affects intracellular processing; increases the interaction with PLAUR;, features a modification of the amino acid from Y to S at position 72.
+The protein's natural variant, known as in RESDX; unknown pathological significance; results in a gain of glycosylation; affects intracellular processing; does not affect interaction with PLAUR;, features a modification of the amino acid from N to S at position 327.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from Y to C at position 175.
+The protein's natural variant, known as in strain: 168 / LH45, features a modification of the amino acid from D to E at position 68.
+The protein's natural variant, known as in strain: 168 / LH45, features a modification of the amino acid from V to E at position 72.
+The protein's natural variant, known as in strain: 168 / LH45, features a modification of the amino acid from I to F at position 82.
+The protein's natural variant, known as in strain: 168 / LH45, features a modification of the amino acid from Q to H at position 110.
+The protein's natural variant, known as in strain: 168 / LH45, features a modification of the amino acid from V to L at position 129.
+The protein's natural variant, known as in strain: 168 / LH45, features a modification of the amino acid from Q to K at position 259.
+The protein's natural variant, known as in strain: 168 / LH45, features a modification of the amino acid from S to G at position 313.
+The protein's natural variant, known as in strain: 168 / LH45, features a modification of the amino acid from I to L at position 320.
+The protein's natural variant, known as in strain: 168 / LH45, features a modification of the amino acid from V to I at position 341.
+The protein's natural variant, known as in strain: 168 / LH45, features a modification of the amino acid from ED to GN at position 350.
+The protein's natural variant, known as in a lung large cell carcinoma sample; somatic mutation, features a modification of the amino acid from S to F at position 806.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation;, features a modification of the amino acid from P to S at position 855.
+The protein's natural variant, known as in TFM; has only 10-15% of the androgen-binding capacity of wild-type AR, features a modification of the amino acid from R to Q at position 735.
+The protein's natural variant, known as in MC1DN25;, features a modification of the amino acid from W to R at position 22.
+The protein's natural variant, known as in BARTS4A; completely abolishes CLCNKA activation; mutated protein fails to increase surface expression of CLCNKA; intracellular localization; probably retained in the ER;, features a modification of the amino acid from R to L at position 8.
+The protein's natural variant, known as in BARTS4A; completely abolishes CLCNKA activation;, features a modification of the amino acid from R to W at position 8.
+The protein's natural variant, known as in BARTS4A; increases CLCNKA currents over those obtained with wild-type; still activates CLCNKA to an extent similar to that of wild-type; intracellular but some plasma membrane localization as well;, features a modification of the amino acid from G to S at position 10.
+The protein's natural variant, known as in BARTS4A; atypical;, features a modification of the amino acid from G to R at position 47.
+The protein's natural variant, known as in SCAN1; reduces enzyme activity and leads to the accumulation of covalent complexes between TDP1 and DNA;, features a modification of the amino acid from H to R at position 493.
+The protein's natural variant, known as in autosomal recessive or sporadic spinocerebellar ataxia affected Japanese individuals;, features a modification of the amino acid from P to L at position 566.
+The protein's natural variant, known as in DMGDHD; shows 10 fold lower catalytic efficiency due to lower cofactor saturation and reduced thermal stability;, features a modification of the amino acid from H to R at position 109.
+The protein's natural variant, known as possible variant of component I, features a modification of the amino acid from S to T at position 6.
+The protein's natural variant, known as in component II, features a modification of the amino acid from A to T at position 12.
+The protein's natural variant, known as possible variant of component I, features a modification of the amino acid from S to T at position 17.
+The protein's natural variant, known as possible variant of component I, features a modification of the amino acid from S to T at position 18.
+The protein's natural variant, known as in component III, features a modification of the amino acid from K to R at position 39.
+The protein's natural variant, known as probable disease-associated variant found in a patient with non-syndromic early-onset epilepsy associated with severe developmental delay and microcephaly;, features a modification of the amino acid from R to W at position 230.
+The protein's natural variant, known as may be associated with atopic dermatitis;, features a modification of the amino acid from V to M at position 147.
+The protein's natural variant, known as in allele GSTO1*C; no effect on protein stability;, features a modification of the amino acid from A to D at position 140.
+The protein's natural variant, known as in CVDP1;, features a modification of the amino acid from H to P at position 442.
+The protein's natural variant, known as in MNMN;, features a modification of the amino acid from Y to H at position 169.
+The protein's natural variant, known as in CMT4C;, features a modification of the amino acid from R to Q at position 529.
+The protein's natural variant, known as in CMT4C;, features a modification of the amino acid from E to K at position 657.
+The protein's natural variant, known as in CMT4C;, features a modification of the amino acid from R to C at position 658.
+The protein's natural variant, known as in CMT4C; unknown pathological significance;, features a modification of the amino acid from G to D at position 1217.
+The protein's natural variant, known as in ACHM2;, features a modification of the amino acid from D to V at position 162.
+The protein's natural variant, known as in ACHM2;, features a modification of the amino acid from P to L at position 163.
+The protein's natural variant, known as in ACHM2; also found in patients with cone-rod dystrophy;, features a modification of the amino acid from W to C at position 171.
+The protein's natural variant, known as in ACHM2, features a modification of the amino acid from Y to C at position 181.
+The protein's natural variant, known as in ACHM2, features a modification of the amino acid from N to Y at position 182.
+The protein's natural variant, known as in ACHM2, features a modification of the amino acid from L to F at position 186.
+The protein's natural variant, known as in ACHM2;, features a modification of the amino acid from C to Y at position 191.
+The protein's natural variant, known as in ACHM2, features a modification of the amino acid from E to K at position 194.
+The protein's natural variant, known as in ACHM2;, features a modification of the amino acid from R to Q at position 223.
+The protein's natural variant, known as in ACHM2; also found in patients with cone-rod dystrophy;, features a modification of the amino acid from R to W at position 223.
+The protein's natural variant, known as probable disease-associated variant found in patients with cone-rod dystrophy, features a modification of the amino acid from T to I at position 224.
+The protein's natural variant, known as in ACHM2, features a modification of the amino acid from T to R at position 224.
+The protein's natural variant, known as in ACHM2; unknown pathological significance; the dose-response relationship for cGMP-activation is not significantly different from that of wild-type CNGA3; the dose-response relationship of the mutant CNGA3 + CNGB3 is similar to that of the wild-type protein; the channel density into the cell membrane is considerably improved by decreasing the cultivation temperature;, features a modification of the amino acid from E to K at position 228.
+The protein's natural variant, known as in ACHM2, features a modification of the amino acid from F to S at position 249.
+The protein's natural variant, known as probable disease-associated variant found in patients with cone-rod dystrophy, features a modification of the amino acid from P to R at position 258.
+The protein's natural variant, known as in ACHM2; also found in patients with cone-rod dystrophy;, features a modification of the amino acid from D to N at position 260.
+The protein's natural variant, known as in ACHM2;, features a modification of the amino acid from Y to D at position 263.
+The protein's natural variant, known as in ACHM2;, features a modification of the amino acid from G to D at position 267.
+The protein's natural variant, known as in ACHM2, features a modification of the amino acid from R to K at position 274.
+The protein's natural variant, known as in ACHM2; also found in patients with cone-rod dystrophy; does not form functional homomeric or heteromeric channels;, features a modification of the amino acid from R to C at position 277.
+The protein's natural variant, known as in ACHM2; also found in patients with cone-rod dystrophy;, features a modification of the amino acid from R to H at position 277.
+The protein's natural variant, known as in ACHM2;, features a modification of the amino acid from L to P at position 278.
+The protein's natural variant, known as in ACHM2; does not reveal any detectable calcium influx upon agonist application at 37 degrees Celsius; the channel function could be restored by incubating the transfected cells at 27 degrees Celsius; the dose-response relationship for cGMP-activation is not significantly different from that of wild-type CNGA3; the dose-response relationship of the mutant CNGA3 + CNGB3 is similar to that of the wild-type protein; a substantial reduction of macroscopic cGMP maximum current to only one-third of the mean value for wild-type CNGA3 + CNGB3 is observed for the mutant CNGA3 + CNGB3; the channel density into the cell membrane is considerably improved by decreasing the cultivation temparature;, features a modification of the amino acid from R to Q at position 283.
+The protein's natural variant, known as in ACHM2; also found in patients with cone-rod dystrophy;, features a modification of the amino acid from R to W at position 283.
+The protein's natural variant, known as in ACHM2; does not reveal any detectable calcium influx upon agonist application at 37 degrees Celsius; the channel function could be restored by incubating the transfected cells at 27 degrees Celsius; the K(1/2) value is shifted toward a higher cGMP concentration by a factor of 1.8; no positive influence of the CNGB3 subunit in the cGMP sensitivity is observed; a substantial reduction of macroscopic cGMP maximum current to only one-third of the mean value for wild-type CNGA3 + CNGB3 is observed for the mutant CNGA3 + CNGB3; the channel density into the cell membrane is considerably improved by decreasing the cultivation temparature;, features a modification of the amino acid from T to R at position 291.
+The protein's natural variant, known as in ACHM2, features a modification of the amino acid from F to S at position 322.
+The protein's natural variant, known as in ACHM2, features a modification of the amino acid from A to D at position 323.
+The protein's natural variant, known as probable disease-associated variant found in patients with cone-rod dystrophy, features a modification of the amino acid from F to S at position 330.
+The protein's natural variant, known as probable disease-associated variant found in patients with cone-rod dystrophy, features a modification of the amino acid from S to F at position 334.
+The natural variant of this protein is characterized by an amino acid alteration from W to C at position 335.
+The protein's natural variant, known as in ACHM2;, features a modification of the amino acid from S to P at position 341.
+The protein's natural variant, known as in ACHM2;, features a modification of the amino acid from T to S at position 369.
+The protein's natural variant, known as in ACHM2;, features a modification of the amino acid from P to S at position 372.
+The protein's natural variant, known as in ACHM2;, features a modification of the amino acid from F to S at position 380.
+The protein's natural variant, known as in ACHM2;, features a modification of the amino acid from S to P at position 401.
+The protein's natural variant, known as in ACHM2;, features a modification of the amino acid from M to T at position 406.
+The protein's natural variant, known as in ACHM2;, features a modification of the amino acid from R to W at position 410.
+The protein's natural variant, known as in ACHM2;, features a modification of the amino acid from R to C at position 427.
+The protein's natural variant, known as in ACHM2;, features a modification of the amino acid from R to Q at position 436.
+The protein's natural variant, known as in ACHM2; also found in patients with cone-rod dystrophy;, features a modification of the amino acid from R to W at position 436.
+The protein's natural variant, known as in ACHM2; also found in patients with cone-rod dystrophy; does not reveal any detectable calcium influx upon agonist application at 37 degrees Celsius;, features a modification of the amino acid from R to W at position 439.
+The protein's natural variant, known as in ACHM2; the dose-response relationship for cGMP-activation is shifted toward a lower cGMP concentration; the left shift in the dose-response relationship of the mutant CNGA3 is less distinctive than in homomeric channels with this mutation indicating a partial rescue effect of the CNGB3 subunit; is in large part located in the cell membrane at 37 and 27 degrees Celsius;, features a modification of the amino acid from A to T at position 469.
+The protein's natural variant, known as in ACHM2; mutant CNGA3 alone or together with the CNGB3 subunit exhibit an increase in apparent affinity for cGMP and an increase in the relative agonist efficacy of cAMP compared with cGMP; cell surface expression levels is unchanged;, features a modification of the amino acid from N to S at position 471.
+The protein's natural variant, known as in ACHM2, features a modification of the amino acid from D to V at position 485.
+The protein's natural variant, known as in ACHM2;, features a modification of the amino acid from C to S at position 510.
+The protein's natural variant, known as in ACHM2, features a modification of the amino acid from G to E at position 513.
+The protein's natural variant, known as in ACHM2, features a modification of the amino acid from G to E at position 516.
+The protein's natural variant, known as in ACHM2, features a modification of the amino acid from I to T at position 522.
+The protein's natural variant, known as in ACHM2, features a modification of the amino acid from G to D at position 525.
+The protein's natural variant, known as found in a patient with Leber congenital amaurosis; unknown pathological significance, features a modification of the amino acid from L to M at position 527.
+The protein's natural variant, known as in ACHM2; also found in patients with cone-rod dystrophy;, features a modification of the amino acid from V to M at position 529.
+The protein's natural variant, known as probable disease-associated variant found in patients with cone-rod dystrophy;, features a modification of the amino acid from D to H at position 533.
+The protein's natural variant, known as in ACHM2; does not reveal any detectable calcium influx upon agonist application at 37 degrees Celsius; the channel function could be restored by incubating the transfected cells at 27 degrees Celsius; the dose-response relationship for cGMP-activation is shifted toward a lower cGMP concentration; a substantial reduction of macroscopic cGMP maximum current to only one-third of the mean value for wild-type CNGA3 + CNGB3 is observed for the mutant CNGA3 + CNGB3; is in large part located in the cell membrane at 37 and 27 degrees Celsius;, features a modification of the amino acid from F to L at position 547.
+The protein's natural variant, known as in ACHM2;, features a modification of the amino acid from G to R at position 548.
+The protein's natural variant, known as in ACHM2; the K(1/2) value is shifted toward a higher cGMP concentration by a factor of 3.0; no positive influence of the CNGB3 subunit in the cGMP sensitivity is observed; average cGMP maximum current is decreased to half of the mean wild-type value for the mutant CNGA3 + CNGB3;, features a modification of the amino acid from G to R at position 557.
+The protein's natural variant, known as in ACHM2; mutant CNGA3 alone or together with the CNGB3 subunit exhibit an increase in apparent affinity for cGMP and an increase in the relative agonist efficacy of cAMP compared with cGMP; cell surface expression levels is significantly reduced;, features a modification of the amino acid from R to H at position 563.
+The protein's natural variant, known as in ACHM2;, features a modification of the amino acid from T to M at position 565.
+The protein's natural variant, known as in ACHM2;, features a modification of the amino acid from R to H at position 569.
+The protein's natural variant, known as probable disease-associated variant found in patients with cone-rod dystrophy, features a modification of the amino acid from S to N at position 570.
+The protein's natural variant, known as in ACHM2, features a modification of the amino acid from Y to C at position 573.
+The protein's natural variant, known as in ACHM2; also found in patients with cone-rod dystrophy; the dose-response relationship for cGMP-activation is shifted toward a lower cGMP concentration;, features a modification of the amino acid from E to K at position 590.
+The protein's natural variant, known as in ACHM2;, features a modification of the amino acid from E to K at position 593.
+The natural variant of this protein is characterized by an amino acid alteration from S to G at position 57.
+The natural variant of this protein is characterized by an amino acid alteration from I to S at position 98.
+The protein's natural variant, known as found in a patient with primary pulmonary hypertension; unknown pathological significance; affects SMAD-mediated signaling;, features a modification of the amino acid from V to A at position 3.
+The protein's natural variant, known as in cadmium sensitive strain, features a modification of the amino acid from E to K at position 396.
+The protein's natural variant, known as in AIP, features a modification of the amino acid from M to I at position 18.
+The protein's natural variant, known as in AIP;, features a modification of the amino acid from R to C at position 22.
+The protein's natural variant, known as in AIP; severely decreased hydroxymethylbilane synthase activity, features a modification of the amino acid from G to S at position 24.
+The protein's natural variant, known as in AIP; severely decreased hydroxymethylbilane synthase activity;, features a modification of the amino acid from R to C at position 26.
+The protein's natural variant, known as in AIP; severely decreased in hydroxymethylbilane synthase activity;, features a modification of the amino acid from R to H at position 26.
+The protein's natural variant, known as in AIP; severely decreased hydroxymethylbilane synthase activity, features a modification of the amino acid from S to N at position 28.
+The protein's natural variant, known as in AIP; severely decreased hydroxymethylbilane synthase activity, features a modification of the amino acid from L to F at position 30.
+The protein's natural variant, known as in AIP, features a modification of the amino acid from A to P at position 31.
+The protein's natural variant, known as in AIP;, features a modification of the amino acid from A to T at position 31.
+The protein's natural variant, known as in AIP; severely decreased hydroxymethylbilane synthase activity corresponding to less than 1% of wild-type activity, features a modification of the amino acid from R to P at position 32.
+The protein's natural variant, known as in AIP;, features a modification of the amino acid from Q to K at position 34.
+The protein's natural variant, known as in AIP; severely decreased hydroxymethylbilane synthase activity, features a modification of the amino acid from Q to P at position 34.
+The protein's natural variant, known as in AIP, features a modification of the amino acid from Q to R at position 34.
+The protein's natural variant, known as in AIP; severely decreased hydroxymethylbilane synthase activity;, features a modification of the amino acid from T to M at position 35.
+The protein's natural variant, known as in AIP, features a modification of the amino acid from L to S at position 42.
+The protein's natural variant, known as in AIP;, features a modification of the amino acid from A to S at position 55.
+The protein's natural variant, known as in AIP; unknown pathological significance; has 80% of wild-type activity;, features a modification of the amino acid from T to I at position 59.
+The protein's natural variant, known as in AIP, features a modification of the amino acid from D to N at position 61.
+The protein's natural variant, known as in AIP, features a modification of the amino acid from D to Y at position 61.
+The protein's natural variant, known as in AIP, features a modification of the amino acid from T to P at position 78.
+The protein's natural variant, known as in AIP, features a modification of the amino acid from E to G at position 80.
+The protein's natural variant, known as in AIP;, features a modification of the amino acid from L to P at position 81.
+The protein's natural variant, known as in AIP, features a modification of the amino acid from L to R at position 85.
+The protein's natural variant, known as in AIP;, features a modification of the amino acid from E to V at position 86.
+The protein's natural variant, known as in AIP, features a modification of the amino acid from V to G at position 90.
+The protein's natural variant, known as in AIP;, features a modification of the amino acid from L to P at position 92.
+The protein's natural variant, known as in AIP; loss of activity, features a modification of the amino acid from V to F at position 93.
+The protein's natural variant, known as in AIP; severely decreased hydroxymethylbilane synthase activity, features a modification of the amino acid from S to F at position 96.
+The protein's natural variant, known as in AIP, features a modification of the amino acid from K to R at position 98.
+The protein's natural variant, known as in AIP; complete loss of hydroxymethylbilane synthase activity, features a modification of the amino acid from D to G at position 99.
+The protein's natural variant, known as in AIP, features a modification of the amino acid from D to H at position 99.
+The protein's natural variant, known as in AIP, features a modification of the amino acid from D to N at position 99.
+The protein's natural variant, known as in AIP; severely decreased hydroxymethylbilane synthase activity;, features a modification of the amino acid from G to R at position 111.
+The protein's natural variant, known as in AIP, features a modification of the amino acid from I to T at position 113.
+The protein's natural variant, known as in AIP;, features a modification of the amino acid from R to Q at position 116.
+The protein's natural variant, known as in AIP; severely decreased, if any, hydroxymethylbilane synthase activity; affects protein conformation; lower thermal stability than wild-type enzyme;, features a modification of the amino acid from R to W at position 116.
+The protein's natural variant, known as in AIP, features a modification of the amino acid from P to L at position 119.
+The protein's natural variant, known as in AIP, features a modification of the amino acid from A to G at position 122.
+The protein's natural variant, known as in AIP; severely decreased hydroxymethylbilane synthase activity, features a modification of the amino acid from V to D at position 124.
+The protein's natural variant, known as found in a patient with unclear porphyria-related biochemical findings and abdominal pain; unknown pathological significance; does not affect hydroxymethylbilane synthase activity; does not affect Vmax; does not affect KM; does not affect thermal stability;, features a modification of the amino acid from K to N at position 132.
+The protein's natural variant, known as in AIP; severely decreased hydroxymethylbilane synthase activity, features a modification of the amino acid from R to L at position 149.
+The protein's natural variant, known as in AIP; severely decreased, if any, hydroxymethylbilane synthase activity;, features a modification of the amino acid from R to Q at position 149.
+The protein's natural variant, known as in AIP; decreased hydroxymethylbilane synthase activity due to defective enzyme-intermediate complexes turnover and regeneration of free enzyme molecules;, features a modification of the amino acid from R to Q at position 167.
+The protein's natural variant, known as in AIP; severely decreased hydroxymethylbilane synthase activity; results in less than 5% of wild-type activity; 2-fold decrease of Vmax; 33-fold increase of KM;, features a modification of the amino acid from R to W at position 167.
+The protein's natural variant, known as in AIP; less than 1% of wild-type activity;, features a modification of the amino acid from R to Q at position 173.
+The protein's natural variant, known as in AIP; loss of hydroxymethylbilane synthase activity; 1% of wild-type activity; lower thermal stability than wild-type enzyme;, features a modification of the amino acid from R to W at position 173.
+The protein's natural variant, known as in AIP;, features a modification of the amino acid from L to R at position 177.
+The protein's natural variant, known as in AIP; unknown pathological significance; slightly decreased hydroxymethylbilane synthase activity corresponding to 80% of wild-type activity;, features a modification of the amino acid from D to N at position 178.
+The protein's natural variant, known as in AIP; severely decreased, if any, hydroxymethylbilane synthase activity;, features a modification of the amino acid from R to C at position 195.
+The protein's natural variant, known as in AIP; residual activity;, features a modification of the amino acid from R to W at position 201.
+The protein's natural variant, known as in AIP;, features a modification of the amino acid from V to L at position 202.
+The protein's natural variant, known as in AIP; 46% wild-type deaminase activity; decreased enzyme stability, features a modification of the amino acid from Q to K at position 204.
+The protein's natural variant, known as in AIP;, features a modification of the amino acid from E to K at position 209.
+The protein's natural variant, known as in AIP; <2% residual activity;, features a modification of the amino acid from M to V at position 212.
+The protein's natural variant, known as in AIP; unknown pathological significance; decreased hydroxymethylbilane synthase activity; results in 30% of wild-type activity; 3-fold decrease of Vmax; normal KM; affects protein conformation;, features a modification of the amino acid from V to E at position 215.
+The protein's natural variant, known as in AIP; 19% of wild-type deaminase activity, features a modification of the amino acid from V to M at position 215.
+The protein's natural variant, known as in AIP;, features a modification of the amino acid from G to D at position 216.
+The protein's natural variant, known as in AIP; severely decreased hydroxymethylbilane synthase activity, features a modification of the amino acid from Q to H at position 217.
+The protein's natural variant, known as in AIP, features a modification of the amino acid from Q to L at position 217.
+The protein's natural variant, known as in AIP, features a modification of the amino acid from A to D at position 219.
+The protein's natural variant, known as in AIP;, features a modification of the amino acid from V to M at position 222.
+The protein's natural variant, known as in AIP;, features a modification of the amino acid from E to K at position 223.
+The protein's natural variant, known as in AIP, features a modification of the amino acid from R to G at position 225.
+The protein's natural variant, known as in AIP; unknown pathological significance;, features a modification of the amino acid from R to Q at position 225.
+The protein's natural variant, known as in AIP; severely decreased hydroxymethylbilane synthase activity, features a modification of the amino acid from V to E at position 235.
+The protein's natural variant, known as in AIP;, features a modification of the amino acid from G to S at position 236.
+The protein's natural variant, known as in AIP; unknown pathological significance, features a modification of the amino acid from L to P at position 238.
+The protein's natural variant, known as in AIP, features a modification of the amino acid from L to R at position 238.
+The protein's natural variant, known as in AIP, features a modification of the amino acid from L to P at position 244.
+The protein's natural variant, known as in AIP;, features a modification of the amino acid from L to R at position 245.
+The protein's natural variant, known as in AIP; residual activity, features a modification of the amino acid from C to F at position 247.
+The protein's natural variant, known as in AIP; severely decreased hydroxymethylbilane synthase activity;, features a modification of the amino acid from C to R at position 247.
+The protein's natural variant, known as in AIP, features a modification of the amino acid from I to IETLLRCI at position 248.
+The protein's natural variant, known as in AIP; severely decreased hydroxymethylbilane synthase activity, features a modification of the amino acid from E to A at position 250.
+The protein's natural variant, known as in AIP; less than 1% of wild-type deaminase activity, features a modification of the amino acid from E to D at position 250.
+The protein's natural variant, known as in AIP;, features a modification of the amino acid from E to K at position 250.
+The protein's natural variant, known as in AIP; severely decreased hydroxymethylbilane synthase activity, features a modification of the amino acid from E to Q at position 250.
+The protein's natural variant, known as in AIP; severely decreased hydroxymethylbilane synthase activity, features a modification of the amino acid from E to V at position 250.
+The protein's natural variant, known as in AIP;, features a modification of the amino acid from A to T at position 252.
+The protein's natural variant, known as in AIP;, features a modification of the amino acid from A to V at position 252.
+The protein's natural variant, known as in AIP, features a modification of the amino acid from L to P at position 254.
+The protein's natural variant, known as in AIP;, features a modification of the amino acid from H to N at position 256.
+The protein's natural variant, known as in AIP; severely decreased hydroxymethylbilane synthase activity, features a modification of the amino acid from H to Y at position 256.
+The protein's natural variant, known as in AIP;, features a modification of the amino acid from G to D at position 260.
+The protein's natural variant, known as in AIP;, features a modification of the amino acid from C to Y at position 261.
+The protein's natural variant, known as in AIP; severely decreased hydroxymethylbilane synthase activity;, features a modification of the amino acid from V to M at position 267.
+The protein's natural variant, known as in AIP, features a modification of the amino acid from T to I at position 269.
+The protein's natural variant, known as in AIP, features a modification of the amino acid from A to D at position 270.
+The protein's natural variant, known as in AIP, features a modification of the amino acid from A to G at position 270.
+The protein's natural variant, known as in AIP, features a modification of the amino acid from G to R at position 274.
+The protein's natural variant, known as in AIP, features a modification of the amino acid from L to P at position 278.
+The protein's natural variant, known as in AIP, features a modification of the amino acid from G to R at position 280.
+The protein's natural variant, known as in AIP, features a modification of the amino acid from A to P at position 330.
+The protein's natural variant, known as in AIP, features a modification of the amino acid from G to D at position 335.
+The protein's natural variant, known as in AIP; less than 3% of activity, features a modification of the amino acid from G to S at position 335.
+The protein's natural variant, known as in AIP, features a modification of the amino acid from L to P at position 338.
+The protein's natural variant, known as in AIP, features a modification of the amino acid from L to P at position 343.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation, features a modification of the amino acid from H to R at position 732.
+The protein's natural variant, known as in LCA11; does not alter the enzymatic affinity of the corresponding enzyme; alters the affinity and/or the specificity of single-stranded nucleic acid, features a modification of the amino acid from R to W at position 105.
+The protein's natural variant, known as in RP10; does not alter the enzymatic affinity of the corresponding enzyme; alters the affinity and/or the specificity of single-stranded nucleic acid, features a modification of the amino acid from T to M at position 116.
+The protein's natural variant, known as in LCA11; does not alter the enzymatic affinity of the corresponding enzyme; alters the affinity and/or the specificity of single-stranded nucleic acid, features a modification of the amino acid from N to K at position 198.
+The protein's natural variant, known as in RP10, features a modification of the amino acid from R to P at position 224.
+The protein's natural variant, known as in RP10, features a modification of the amino acid from D to N at position 226.
+The protein's natural variant, known as in RP10, features a modification of the amino acid from V to I at position 268.
+The natural variant of this protein is characterized by an amino acid alteration from A to T at position 285.
+The protein's natural variant, known as does not alter the enzymatic affinity of the corresponding enzyme; does not affect the affinity for single-stranded nucleic acid, features a modification of the amino acid from G to D at position 324.
+The protein's natural variant, known as in RP10; alters the affinity and/or the specificity of single-stranded nucleic acid, features a modification of the amino acid from H to P at position 372.
+The protein's natural variant, known as in strain: 1674, features a modification of the amino acid from E to D at position 33.
+The protein's natural variant, known as in strain: 1706, features a modification of the amino acid from E to Q at position 132.
+The protein's natural variant, known as in strain: 1595, features a modification of the amino acid from R to C at position 299.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from P to S at position 209.
+The protein's natural variant, known as in mesotoxin-2, features a modification of the amino acid from N to D at position 74.
+The protein's natural variant, known as in mesotoxin-3, features a modification of the amino acid from T to A at position 77.
+The protein's natural variant, known as in RPS12-B, features a modification of the amino acid from LQ to SR at position 114.
+The protein's natural variant, known as in minC19; reduces affinity of MinC for FtsZ, features a modification of the amino acid from G to D at position 10.
+The protein's natural variant, known as in strain: C3H/He, features a modification of the amino acid from D to G at position 544.
+The protein's natural variant, known as in strain: C3H/He, features a modification of the amino acid from D to A at position 550.
+The protein's natural variant, known as in strain: C3H/He, features a modification of the amino acid from E to Q at position 606.
+The protein's natural variant, known as in strain: C3H/He, features a modification of the amino acid from L to S at position 692.
+The protein's natural variant, known as in strain: C3H/He, features a modification of the amino acid from R to S at position 710.
+The protein's natural variant, known as in strain: C3H/He, features a modification of the amino acid from E to A at position 736.
+The protein's natural variant, known as in strain: C3H/He, features a modification of the amino acid from D to E at position 747.
+The protein's natural variant, known as in metmyoglobin, features a modification of the amino acid from G to A at position 122.
+The protein's natural variant, known as in strain: Isolate LAF1595, features a modification of the amino acid from A to T at position 7.
+The protein's natural variant, known as in allele ALS4-2, features a modification of the amino acid from I to M at position 125.
+The protein's natural variant, known as in allele ALS4-2, features a modification of the amino acid from N to S at position 198.
+The protein's natural variant, known as in allele ALS4-2, features a modification of the amino acid from F to Y at position 265.
+The protein's natural variant, known as in allele ALS4-2, features a modification of the amino acid from I to V at position 280.
+The protein's natural variant, known as in allele ALS4-2, features a modification of the amino acid from I to II at position 697.
+The protein's natural variant, known as in allele ALS4-2, features a modification of the amino acid from STSL to GTSS at position 729.
+The protein's natural variant, known as in DIAR1;, features a modification of the amino acid from G to S at position 120.
+The protein's natural variant, known as in DIAR1;, features a modification of the amino acid from H to L at position 124.
+The protein's natural variant, known as in DIAR1;, features a modification of the amino acid from P to L at position 129.
+The protein's natural variant, known as in DIAR1;, features a modification of the amino acid from P to L at position 131.
+The protein's natural variant, known as in DIAR1;, features a modification of the amino acid from P to R at position 131.
+The protein's natural variant, known as in DIAR1, features a modification of the amino acid from S to N at position 134.
+The protein's natural variant, known as in DIAR1;, features a modification of the amino acid from M to I at position 136.
+The protein's natural variant, known as in DIAR1;, features a modification of the amino acid from R to S at position 175.
+The protein's natural variant, known as in DIAR1;, features a modification of the amino acid from Y to D at position 204.
+The protein's natural variant, known as in DIAR1;, features a modification of the amino acid from S to P at position 206.
+The protein's natural variant, known as in DIAR1;, features a modification of the amino acid from H to P at position 220.
+The protein's natural variant, known as in DIAR1;, features a modification of the amino acid from C to Y at position 343.
+The protein's natural variant, known as in DIAR1, features a modification of the amino acid from FGIAMV to DA at position 349.
+The protein's natural variant, known as in DIAR1;, features a modification of the amino acid from G to A at position 379.
+The protein's natural variant, known as in DIAR1;, features a modification of the amino acid from S to I at position 394.
+The protein's natural variant, known as in DIAR1;, features a modification of the amino acid from S to F at position 398.
+The protein's natural variant, known as in DIAR1;, features a modification of the amino acid from S to P at position 438.
+The protein's natural variant, known as in DIAR1;, features a modification of the amino acid from D to V at position 468.
+The protein's natural variant, known as in DIAR1, features a modification of the amino acid from Q to P at position 495.
+The protein's natural variant, known as in DIAR1;, features a modification of the amino acid from L to R at position 496.
+The protein's natural variant, known as in DIAR1, features a modification of the amino acid from C to R at position 508.
+The protein's natural variant, known as in DIAR1;, features a modification of the amino acid from Y to C at position 520.
+The protein's natural variant, known as in DIAR1;, features a modification of the amino acid from K to N at position 521.
+The protein's natural variant, known as in DIAR1;, features a modification of the amino acid from I to N at position 544.
+The protein's natural variant, known as in DIAR1, features a modification of the amino acid from A to E at position 547.
+The protein's natural variant, known as in DIAR1;, features a modification of the amino acid from D to N at position 652.
+The protein's natural variant, known as in DIAR1, features a modification of the amino acid from S to P at position 654.
+The protein's natural variant, known as in DIAR1;, features a modification of the amino acid from I to II at position 675.
+The protein's natural variant, known as reduced activity; increased sensitivity to inhibition by oseltamivir carboxylate;, features a modification of the amino acid from R to Q at position 41.
+The protein's natural variant, known as associated with susceptibility to HVB infection; lower cell surface levels; lower induction of MHC class 1 expression by INF-alpha;, features a modification of the amino acid from F to S at position 8.
+The protein's natural variant, known as no effect on activation of STAT1 upon IFNA2 or IFNG binding;, features a modification of the amino acid from E to Q at position 37.
+The protein's natural variant, known as no effect on activation of STAT1 upon IFNA2 or IFNG binding;, features a modification of the amino acid from M to V at position 73.
+The protein's natural variant, known as no effect on activation of STAT1 upon IFNA2 or IFNG binding, features a modification of the amino acid from E to V at position 138.
+The protein's natural variant, known as no effect on activation of STAT1 upon IFNA2 or IFNG binding;, features a modification of the amino acid from S to G at position 215.
+The protein's natural variant, known as no effect on activation of STAT1 upon IFNA2 or IFNG binding;, features a modification of the amino acid from H to R at position 283.
+The protein's natural variant, known as no effect on activation of STAT1 upon IFNA2 or IFNG binding;, features a modification of the amino acid from P to L at position 295.
+The protein's natural variant, known as no effect on activation of STAT1 upon IFNA2 or IFNG binding;, features a modification of the amino acid from Y to C at position 318.
+The protein's natural variant, known as no effect on activation of STAT1 upon IFNA2 or IFNG binding;, features a modification of the amino acid from S to N at position 324.
+The protein's natural variant, known as no effect on activation of STAT1 upon IFNA2 or IFNG binding;, features a modification of the amino acid from P to S at position 346.
+The protein's natural variant, known as no effect on activation of STAT1 upon IFNA2 or IFNG binding;, features a modification of the amino acid from P to S at position 362.
+The protein's natural variant, known as no effect on activation of STAT1 upon IFNA2 or IFNG binding;, features a modification of the amino acid from P to L at position 385.
+The protein's natural variant, known as no effect on activation of STAT1 upon IFNA2 or IFNG binding;, features a modification of the amino acid from S to L at position 450.
+The natural variant of this protein is characterized by an amino acid alteration from S to P at position 121.
+The natural variant of this protein is characterized by an amino acid alteration from V to G at position 132.
+The natural variant of this protein is characterized by an amino acid alteration from A to P at position 39.
+The protein's natural variant, known as in RPL27-5, features a modification of the amino acid from E to D at position 35.
+The protein's natural variant, known as in RPL27-3, RPL27-4 and RPL27-5, features a modification of the amino acid from F to Y at position 49.
+The protein's natural variant, known as in RPL27-4, features a modification of the amino acid from P to S at position 50.
+The protein's natural variant, known as in RPL27-2 and RPL27-4, features a modification of the amino acid from L to V at position 117.
+The protein's natural variant, known as in SPG8; dopamine responsive spasticity;, features a modification of the amino acid from I to T at position 226.
+The protein's natural variant, known as in SPG8; does not alter subcellular distribution; no effect on its binding to VCP; no effect on assembly in the WASH complex;, features a modification of the amino acid from N to D at position 471.
+The protein's natural variant, known as in SPG8; fails to rescue the curly phenotype in a zebrafish model; no effect on assembly in the WASH complex;, features a modification of the amino acid from L to F at position 619.
+The protein's natural variant, known as in SPG8, features a modification of the amino acid from V to A at position 620.
+The protein's natural variant, known as in SPG8; fails to rescue the curly phenotype in a zebrafish model; no effect on assembly in the WASH complex;, features a modification of the amino acid from V to F at position 626.
+The protein's natural variant, known as in SPG8;, features a modification of the amino acid from G to A at position 696.
+The protein's natural variant, known as found in dogs with neurodegenerative disease, features a modification of the amino acid from A to T at position 430.
+The natural variant of this protein is characterized by an amino acid alteration from D to S at position 205.
+The protein's natural variant, known as in HTNB; increased 3',5'-cyclic-AMP phosphodiesterase activity; increased function in cAMP-mediated signaling;, features a modification of the amino acid from T to A at position 445.
+The protein's natural variant, known as in HTNB; increased phosphorylation at S-428 and S-438; increased affinity for 3',5'-cyclic-AMP; no effect on protein reaction kinetics for 3',5'-cyclic-AMP phosphodiesterase activity; increased 3',5'-cyclic-AMP phosphodiesterase activity; no effect on inhibition by 3',5'-cyclic-GMP; changed function in cAMP-mediated signaling;, features a modification of the amino acid from T to N at position 445.
+The protein's natural variant, known as in HTNB; increased 3',5'-cyclic-AMP phosphodiesterase activity; changed function in cAMP-mediated signaling;, features a modification of the amino acid from T to S at position 445.
+The protein's natural variant, known as in HTNB; increased 3',5'-cyclic-AMP phosphodiesterase activity; changed function in cAMP-mediated signaling;, features a modification of the amino acid from A to T at position 447.
+The protein's natural variant, known as in HTNB; increased 3',5'-cyclic-AMP phosphodiesterase activity; changed function in cAMP-mediated signaling;, features a modification of the amino acid from A to V at position 447.
+The protein's natural variant, known as in HTNB; increased 3',5'-cyclic-AMP phosphodiesterase activity; changed function in cAMP-mediated signaling;, features a modification of the amino acid from G to V at position 449.
+The protein's natural variant, known as in NEDMABA, features a modification of the amino acid from L to P at position 231.
+The protein's natural variant, known as in NEDMABA; unknown pathological significance;, features a modification of the amino acid from P to L at position 446.
+The protein's natural variant, known as in NEDMABA; unknown pathological significance;, features a modification of the amino acid from A to V at position 661.
+The protein's natural variant, known as found in patient with putative diagnosis of PXE; uncertain pathological significance; loss-of-function mutation; localization comparable to wild-type;, features a modification of the amino acid from P to H at position 4.
+The protein's natural variant, known as found in patient with putative diagnosis of PXE; uncertain pathological significance; loss-of-function mutation; localization comparable to wild-type;, features a modification of the amino acid from A to E at position 9.
+The protein's natural variant, known as found in patient with putative diagnosis of PXE; uncertain pathological significance; loss-of-function mutation; localization comparable to wild-type;, features a modification of the amino acid from P to S at position 21.
+The protein's natural variant, known as found in patient with putative diagnosis of PXE; uncertain pathological significance; localization comparable to wild-type;, features a modification of the amino acid from R to Q at position 64.
+The protein's natural variant, known as in PXE;, features a modification of the amino acid from A to T at position 78.
+The protein's natural variant, known as found in patient with putative diagnosis of PXE; uncertain pathological significance;, features a modification of the amino acid from A to T at position 90.
+The protein's natural variant, known as in PXE; loss-of-function variant; localization comparable to wild-type;, features a modification of the amino acid from E to K at position 125.
+The protein's natural variant, known as in PXE; autosomal recessive;, features a modification of the amino acid from G to E at position 129.
+The protein's natural variant, known as in PXE; autosomal recessive;, features a modification of the amino acid from S to R at position 317.
+The protein's natural variant, known as in GACI2 and PXE; autosomal recessive;, features a modification of the amino acid from L to R at position 355.
+The protein's natural variant, known as in PXE; autosomal recessive;, features a modification of the amino acid from T to R at position 364.
+The protein's natural variant, known as in PXE; autosomal recessive;, features a modification of the amino acid from N to D at position 370.
+The protein's natural variant, known as in PXE;, features a modification of the amino acid from R to W at position 382.
+The protein's natural variant, known as in GACI2 and PXE; autosomal recessive;, features a modification of the amino acid from R to G at position 391.
+The protein's natural variant, known as in PXE;, features a modification of the amino acid from K to N at position 392.
+The protein's natural variant, known as in PXE; autosomal recessive;, features a modification of the amino acid from S to G at position 398.
+The protein's natural variant, known as in PXE; autosomal dominant;, features a modification of the amino acid from N to K at position 411.
+The protein's natural variant, known as found in patient with putative diagnosis of PXE; uncertain pathological significance; loss-of-function mutation; localization comparable to wild-type;, features a modification of the amino acid from R to Q at position 419.
+The protein's natural variant, known as in PXE; autosomal recessive;, features a modification of the amino acid from C to G at position 440.
+The protein's natural variant, known as in PXE; autosomal dominant;, features a modification of the amino acid from A to P at position 455.
+The protein's natural variant, known as in PXE;, features a modification of the amino acid from L to H at position 463.
+The protein's natural variant, known as in PXE; autosomal recessive;, features a modification of the amino acid from L to H at position 495.
+The protein's natural variant, known as in PXE; autosomal recessive;, features a modification of the amino acid from R to Q at position 518.
+The protein's natural variant, known as in PXE;, features a modification of the amino acid from S to P at position 535.
+The protein's natural variant, known as in PXE; autosomal recessive;, features a modification of the amino acid from F to S at position 551.
+The protein's natural variant, known as in PXE; autosomal dominant;, features a modification of the amino acid from F to S at position 568.
+The protein's natural variant, known as in GACI2;, features a modification of the amino acid from S to F at position 590.
+The protein's natural variant, known as in PXE; autosomal recessive;, features a modification of the amino acid from A to V at position 594.
+The protein's natural variant, known as in PXE; autosomal recessive;, features a modification of the amino acid from R to C at position 600.
+The protein's natural variant, known as found in patient with putative diagnosis of PEX; uncertain pathological significance; mutant protein is retained in the cytoplasm;, features a modification of the amino acid from L to P at position 605.
+The protein's natural variant, known as in PXE; affects protein expression and trafficking; expression is reduced to less than 10%, when compared with the WT protein;, features a modification of the amino acid from G to C at position 663.
+The protein's natural variant, known as in PXE; autosomal dominant; affects protein expression and trafficking; expression is reduced to less than 10%, when compared with the WT protein;, features a modification of the amino acid from L to P at position 673.
+The protein's natural variant, known as in PXE; autosomal recessive;, features a modification of the amino acid from L to P at position 677.
+The protein's natural variant, known as in PXE; does not change protein biosynthesis and folding;, features a modification of the amino acid from Q to P at position 698.
+The protein's natural variant, known as in PXE; does not change protein biosynthesis and folding;, features a modification of the amino acid from E to D at position 699.
+The protein's natural variant, known as found in patient with putative diagnosis of PEX; uncertain pathological significance; loss-of-function mutation; localization comparable to wild-type;, features a modification of the amino acid from E to G at position 709.
+The natural variant of this protein is characterized by an amino acid alteration from R to L at position 724.
+The protein's natural variant, known as in PXE; affects protein expression and trafficking; expression is reduced to less than 10%, when compared with the WT protein;, features a modification of the amino acid from L to P at position 726.
+The protein's natural variant, known as in PXE;, features a modification of the amino acid from M to K at position 751.
+The protein's natural variant, known as in PXE; does not change protein biosynthesis and folding;, features a modification of the amino acid from G to R at position 755.
+The protein's natural variant, known as in PXE; autosomal recessive; protein level is 15-20% that of the WT proteins; maturation of glycan chains is not affected indicating normal trafficking from the endoplasmic reticulum to the cell membrane;, features a modification of the amino acid from R to W at position 760.
+The protein's natural variant, known as in PXE; autosomal dominant and autosomal recessive; affects protein expression and trafficking; expression is reduced to less than 10%, when compared with the WT protein;, features a modification of the amino acid from R to Q at position 765.
+The protein's natural variant, known as in PXE; autosomal recessive; affects protein expression and trafficking; expression is reduced to less than 10%, when compared with the WT protein;, features a modification of the amino acid from A to D at position 766.
+The protein's natural variant, known as in PXE; affects protein expression and trafficking; affects protein expression and trafficking; expression is reduced to less than 10%, when compared with the WT protein;, features a modification of the amino acid from D to N at position 777.
+The protein's natural variant, known as in PXE; autosomal recessive;, features a modification of the amino acid from R to Q at position 807.
+The protein's natural variant, known as in PXE; autosomal recessive;, features a modification of the amino acid from R to W at position 807.
+The protein's natural variant, known as in PXE; autosomal recessive; protein level is 15-20% that of the WT proteins; maturation of glycan chains is not affected indicating normal trafficking from the endoplasmic reticulum to the cell membrane;, features a modification of the amino acid from V to M at position 810.
+The protein's natural variant, known as in PXE; protein level is 15-20% that of the WT proteins; maturation of glycan chains is not affected indicating normal trafficking from the endoplasmic reticulum to the cell membrane;, features a modification of the amino acid from T to M at position 811.
+The protein's natural variant, known as in PXE; autosomal recessive; affects protein expression and trafficking;, features a modification of the amino acid from A to P at position 820.
+The protein's natural variant, known as found in patient with putative diagnosis of PEX; uncertain pathological significance; loss-of-function mutation; localization comparable to wild-type;, features a modification of the amino acid from M to T at position 834.
+The protein's natural variant, known as in PXE;, features a modification of the amino acid from R to S at position 881.
+The protein's natural variant, known as in PXE;, features a modification of the amino acid from T to I at position 944.
+The protein's natural variant, known as found in patient with putative diagnosis of PEX; uncertain pathological significance; loss-of-function mutation; localization comparable to wild-type;, features a modification of the amino acid from L to P at position 948.
+The protein's natural variant, known as in PXE;, features a modification of the amino acid from A to T at position 950.
+The protein's natural variant, known as in PXE;, features a modification of the amino acid from G to R at position 992.
+The protein's natural variant, known as in PXE;, features a modification of the amino acid from D to E at position 1056.
+The protein's natural variant, known as in GACI2 and PXE; autosomal recessive;, features a modification of the amino acid from R to C at position 1114.
+The protein's natural variant, known as in PXE; autosomal recessive;, features a modification of the amino acid from R to P at position 1114.
+The protein's natural variant, known as in PXE;, features a modification of the amino acid from S to L at position 1121.
+The protein's natural variant, known as in PXE; autosomal dominant;, features a modification of the amino acid from S to W at position 1121.
+The protein's natural variant, known as in PXE; autosomal recessive;, features a modification of the amino acid from T to M at position 1130.
+The protein's natural variant, known as in PXE;, features a modification of the amino acid from G to A at position 1133.
+The protein's natural variant, known as in PXE; autosomal dominant;, features a modification of the amino acid from R to P at position 1138.
+The protein's natural variant, known as in PXE; autosomal recessive;, features a modification of the amino acid from R to Q at position 1138.
+The protein's natural variant, known as in PXE; autosomal recessive;, features a modification of the amino acid from R to W at position 1138.
+The protein's natural variant, known as in PXE;, features a modification of the amino acid from A to T at position 1139.
+The protein's natural variant, known as in PXE; autosomal recessive;, features a modification of the amino acid from R to Q at position 1164.
+The protein's natural variant, known as in PXE; autosomal dominant;, features a modification of the amino acid from G to D at position 1203.
+The protein's natural variant, known as in PXE; autosomal recessive;, features a modification of the amino acid from R to C at position 1221.
+The protein's natural variant, known as in GACI2;, features a modification of the amino acid from R to H at position 1221.
+The protein's natural variant, known as in PXE;, features a modification of the amino acid from L to I at position 1226.
+The protein's natural variant, known as in PXE; autosomal recessive;, features a modification of the amino acid from R to W at position 1235.
+The protein's natural variant, known as in PXE; pseudodominant;, features a modification of the amino acid from D to H at position 1238.
+The protein's natural variant, known as associated with lower plasma triglycerides and higher plasma HDL cholesterol;, features a modification of the amino acid from R to Q at position 1268.
+The protein's natural variant, known as in PXE; autosomal dominant; abolishes LTC4 and NEM-GS transport; does not affect plasma membrane localization; does not increase extracellular pyrophosphate levels;, features a modification of the amino acid from V to F at position 1298.
+The protein's natural variant, known as in PXE; autosomal dominant;, features a modification of the amino acid from T to I at position 1301.
+The protein's natural variant, known as in PXE; autosomal dominant and autosomal recessive; abolishes LTC4 and NEM-GS transport;, features a modification of the amino acid from G to R at position 1302.
+The protein's natural variant, known as in PXE; autosomal dominant and autosomal recessive;, features a modification of the amino acid from A to P at position 1303.
+The protein's natural variant, known as in PXE; autosomal dominant and autosomal recessive;, features a modification of the amino acid from R to Q at position 1314.
+The protein's natural variant, known as in GACI2 and PXE; autosomal recessive;, features a modification of the amino acid from R to W at position 1314.
+The protein's natural variant, known as in PXE; autosomal dominant; abolishes LTC4 and NEM-GS transport;, features a modification of the amino acid from G to S at position 1321.
+The protein's natural variant, known as in PXE; autosomal recessive;, features a modification of the amino acid from L to P at position 1335.
+The protein's natural variant, known as in PXE;, features a modification of the amino acid from L to Q at position 1335.
+The protein's natural variant, known as in PXE; autosomal recessive;, features a modification of the amino acid from R to C at position 1339.
+The protein's natural variant, known as in PXE; autosomal recessive;, features a modification of the amino acid from R to H at position 1339.
+The protein's natural variant, known as in PXE; autosomal recessive;, features a modification of the amino acid from R to L at position 1339.
+The protein's natural variant, known as in PXE; autosomal recessive;, features a modification of the amino acid from P to S at position 1346.
+The protein's natural variant, known as in PXE; autosomal dominant;, features a modification of the amino acid from Q to H at position 1347.
+The protein's natural variant, known as in PXE; autosomal recessive;, features a modification of the amino acid from G to R at position 1354.
+The protein's natural variant, known as in PXE; autosomal recessive;, features a modification of the amino acid from R to W at position 1357.
+The protein's natural variant, known as in PXE; autosomal dominant;, features a modification of the amino acid from D to N at position 1361.
+The protein's natural variant, known as in PXE; autosomal recessive;, features a modification of the amino acid from E to K at position 1400.
+The protein's natural variant, known as in PXE; autosomal recessive;, features a modification of the amino acid from Q to K at position 1406.
+The protein's natural variant, known as in PXE; autosomal dominant;, features a modification of the amino acid from I to T at position 1424.
+The protein's natural variant, known as found in patient with putative diagnosis of PEX; uncertain pathological significance;, features a modification of the amino acid from A to T at position 1442.
+The protein's natural variant, known as in PXE; putative autosomal dominant;, features a modification of the amino acid from R to C at position 1459.
+The protein's natural variant, known as in ARCL3A; reduction of activity;, features a modification of the amino acid from R to Q at position 84.
+The protein's natural variant, known as in ARCL3A, features a modification of the amino acid from G to R at position 93.
+The protein's natural variant, known as in SPG9A;, features a modification of the amino acid from V to A at position 120.
+The protein's natural variant, known as in SPG9B;, features a modification of the amino acid from R to H at position 128.
+The protein's natural variant, known as in ADCL3;, features a modification of the amino acid from R to L at position 138.
+The protein's natural variant, known as in ADCL3;, features a modification of the amino acid from R to Q at position 138.
+The protein's natural variant, known as in ADCL3; no effect on protein abundance; altered sub-mitochondrial distribution; decreased proline biosynthetic process;, features a modification of the amino acid from R to W at position 138.
+The protein's natural variant, known as in SPG9A; decreased protein abundance; no effect on localization to the mitochondrion; altered homohexamerization; loss of glutamate 5-kinase activity; no effect on glutamate-5-semialdehyde dehydrogenase activity; decreased amino acid biosynthetic process;, features a modification of the amino acid from V to L at position 243.
+The protein's natural variant, known as in SPG9A; altered homohexamerization; no effect on localization to the mitochondrion; loss of glutamate 5-kinase activity; no effect on glutamate-5-semialdehyde dehydrogenase activity; decreased amino acid biosynthetic process;, features a modification of the amino acid from R to Q at position 252.
+The protein's natural variant, known as in ARCL3A; benign variant;, features a modification of the amino acid from T to I at position 299.
+The protein's natural variant, known as in SPG9B;, features a modification of the amino acid from L to P at position 637.
+The protein's natural variant, known as in SPG9A, features a modification of the amino acid from S to F at position 652.
+The protein's natural variant, known as in SPG9A;, features a modification of the amino acid from R to L at position 665.
+The protein's natural variant, known as in SPG9B;, features a modification of the amino acid from D to H at position 715.
+The protein's natural variant, known as in ARCL3A;, features a modification of the amino acid from Y to C at position 782.
+The protein's natural variant, known as in ARCL3A; does not affect proline and ornithine biosynthetic activity;, features a modification of the amino acid from H to Y at position 784.
+The protein's natural variant, known as in IDDMOH; unknown pathological significance, features a modification of the amino acid from G to S at position 47.
+The protein's natural variant, known as in IDDMOH; unknown pathological significance, features a modification of the amino acid from H to D at position 48.
+The protein's natural variant, known as in IDDMOH, features a modification of the amino acid from I to N at position 49.
+The protein's natural variant, known as in IDDMOH; decreased function in positive regulation of DNA-templated transcription; compared to the wild-type, the mutant induces a severely reduced GDF5 promoter activation using an in vitro reporter system, features a modification of the amino acid from K to N at position 50.
+The protein's natural variant, known as in IDDMOH, features a modification of the amino acid from K to Q at position 50.
+The protein's natural variant, known as in IDDMOH, features a modification of the amino acid from R to G at position 51.
+The protein's natural variant, known as in IDDMOH, features a modification of the amino acid from R to L at position 51.
+The protein's natural variant, known as in IDDMOH, features a modification of the amino acid from R to Q at position 51.
+The protein's natural variant, known as in IDDMOH, features a modification of the amino acid from R to W at position 51.
+The protein's natural variant, known as in IDDMOH, features a modification of the amino acid from P to L at position 52.
+The protein's natural variant, known as in IDDMOH, features a modification of the amino acid from M to I at position 53.
+The protein's natural variant, known as in IDDMOH, features a modification of the amino acid from M to R at position 53.
+The protein's natural variant, known as in IDDMOH, features a modification of the amino acid from M to V at position 53.
+The protein's natural variant, known as in IDDMOH, features a modification of the amino acid from A to T at position 55.
+The protein's natural variant, known as in IDDMOH, features a modification of the amino acid from F to L at position 56.
+The protein's natural variant, known as in IDDMOH, features a modification of the amino acid from M to T at position 57.
+The protein's natural variant, known as in IDDMOH; decreases transcriptional activity;, features a modification of the amino acid from S to P at position 60.
+The protein's natural variant, known as in IDDMOH, features a modification of the amino acid from R to C at position 64.
+The protein's natural variant, known as in IDDMOH, features a modification of the amino acid from R to L at position 64.
+The protein's natural variant, known as in IDDMOH, features a modification of the amino acid from R to P at position 64.
+The protein's natural variant, known as in IDDMOH, features a modification of the amino acid from R to S at position 64.
+The protein's natural variant, known as in IDDMOH, features a modification of the amino acid from H to D at position 75.
+The protein's natural variant, known as in IDDMOH, features a modification of the amino acid from N to D at position 76.
+The protein's natural variant, known as in IDDMOH, features a modification of the amino acid from G to S at position 84.
+The protein's natural variant, known as in IDDMOH, features a modification of the amino acid from W to R at position 87.
+The protein's natural variant, known as in IDDMOH; unknown pathological significance, features a modification of the amino acid from F to L at position 98.
+The protein's natural variant, known as in IDDMOH, features a modification of the amino acid from R to P at position 100.
+The protein's natural variant, known as in IDDMOH, features a modification of the amino acid from A to V at position 102.
+The protein's natural variant, known as in IDDMOH, features a modification of the amino acid from R to P at position 106.
+The protein's natural variant, known as in IDDMOH, features a modification of the amino acid from H to P at position 109.
+The protein's natural variant, known as in IDDMOH; decreased function in positive regulation of DNA-templated transcription; compared to the wild-type, the mutant induces reduced GDF5 promoter activation using an in vitro reporter system; no effect on nuclear localization, features a modification of the amino acid from Y to H at position 113.
+The protein's natural variant, known as in IDDMOH; decreases transcriptional activity;, features a modification of the amino acid from Y to C at position 116.
+The protein's natural variant, known as in IDDMOH; decreased function in positive regulation of DNA-templated transcription; compared to the wild-type, the mutant induces a reduced GDF5 promoter activation using an in vitro reporter system, features a modification of the amino acid from P to H at position 120.
+The protein's natural variant, known as in IDDMOH; unknown pathological significance; no effect on nuclear localization, features a modification of the amino acid from A to G at position 142.
+The protein's natural variant, known as in IDDMOH; unknown pathological significance, features a modification of the amino acid from A to E at position 176.
+The natural variant of this protein is characterized by an amino acid alteration from L to V at position 211.
+The protein's natural variant, known as in PEERB; altered intracellular trafficking from the ER to the Golgi to the plasma membrane;, features a modification of the amino acid from D to Y at position 37.
+The protein's natural variant, known as in FHL2;, features a modification of the amino acid from V to M at position 50.
+The protein's natural variant, known as in FHL2;, features a modification of the amino acid from V to G at position 183.
+The protein's natural variant, known as in FHL2, features a modification of the amino acid from I to N at position 224.
+The protein's natural variant, known as in FHL2;, features a modification of the amino acid from R to W at position 225.
+The protein's natural variant, known as in FHL2;, features a modification of the amino acid from N to S at position 252.
+The protein's natural variant, known as in FHL2;, features a modification of the amino acid from C to Y at position 279.
+The protein's natural variant, known as in FHL2;, features a modification of the amino acid from P to L at position 345.
+The protein's natural variant, known as in FHL2;, features a modification of the amino acid from G to E at position 429.
+The protein's natural variant, known as in MRT66;, features a modification of the amino acid from L to P at position 328.
+The protein's natural variant, known as in CRS6;, features a modification of the amino acid from G to R at position 400.
+The protein's natural variant, known as in forms A3, A4, A5 and A2 from strain Liverpool, features a modification of the amino acid from K to Q at position 2.
+The protein's natural variant, known as in form A4, features a modification of the amino acid from S to P at position 3.
+The protein's natural variant, known as in forms A2, A3, A4 and A2 from strain Liverpool, features a modification of the amino acid from I to L at position 4.
+The protein's natural variant, known as in forms A2, A3, A4, A5, B2, A1 from strain Liverpool and A2 from strain Liverpool, features a modification of the amino acid from V to G at position 15.
+The protein's natural variant, known as in form B2, A1 from strain Liverpool, features a modification of the amino acid from A to S at position 16.
+The protein's natural variant, known as in form A1 from strain Liverpool, features a modification of the amino acid from E to D at position 24.
+The protein's natural variant, known as in strain: 41, features a modification of the amino acid from D to E at position 88.
+The protein's natural variant, known as in strain: 41, features a modification of the amino acid from T to A at position 256.
+The protein's natural variant, known as in strain: 41, features a modification of the amino acid from P to S at position 268.
+The protein's natural variant, known as in strain: cv. Bl-1, cv. Shokei and cv. Yo-0, features a modification of the amino acid from N to K at position 17.
+The protein's natural variant, known as in strain: cv. Aa-0, features a modification of the amino acid from A to T at position 106.
+The protein's natural variant, known as in strain: cv. Yo-0, features a modification of the amino acid from G to S at position 127.
+The protein's natural variant, known as in strain: cv. Ci-0, features a modification of the amino acid from N to D at position 206.
+The natural variant of this protein is characterized by an amino acid alteration from H to G at position 107.
+The natural variant of this protein is characterized by an amino acid alteration from P to M at position 138.
+The natural variant of this protein is characterized by an amino acid alteration from I to T at position 416.
+The protein's natural variant, known as in plasmid NR1, features a modification of the amino acid from P to A at position 70.
+The protein's natural variant, known as in plasmid NR1, features a modification of the amino acid from VR to EG at position 342.
+The natural variant of this protein is characterized by an amino acid alteration from Q to H at position 23.
+The natural variant of this protein is characterized by an amino acid alteration from A to P at position 80.
+The protein's natural variant, known as in VWM;, features a modification of the amino acid from V to F at position 183.
+The protein's natural variant, known as in VWM;, features a modification of the amino acid from N to Y at position 208.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from S to L at position 52.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from E to Q at position 112.
+The protein's natural variant, known as in MC1DN2; unknown pathological significance;, features a modification of the amino acid from R to C at position 18.
+The protein's natural variant, known as in MC1DN2; decrease in enzyme activity; impaired assembly of complex I;, features a modification of the amino acid from E to Q at position 63.
+The protein's natural variant, known as in MC1DN2; unknown pathological significance; decrease in enzyme activity; impaired assembly of complex I;, features a modification of the amino acid from R to W at position 77.
+The protein's natural variant, known as in MC1DN2;, features a modification of the amino acid from P to L at position 79.
+The protein's natural variant, known as in MC1DN2; unknown pathological significance;, features a modification of the amino acid from P to L at position 85.
+The protein's natural variant, known as in MC1DN2;, features a modification of the amino acid from R to H at position 102.
+The protein's natural variant, known as in MC1DN2; unknown pathological significance;, features a modification of the amino acid from R to H at position 138.
+The protein's natural variant, known as in MC1DN2; unknown pathological significance; decrease in enzyme activity; impaired assembly of complex I;, features a modification of the amino acid from A to D at position 159.
+The protein's natural variant, known as in strain: cv. cvi-1, features a modification of the amino acid from P to H at position 37.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from S to N at position 60.
+The protein's natural variant, known as in strain: cv. C24 and cv. Landsberg erecta, features a modification of the amino acid from N to T at position 136.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from TV to SG at position 148.
+The protein's natural variant, known as in strain: cv. C24, features a modification of the amino acid from T to S at position 147.
+The protein's natural variant, known as in strain: cv. cvi-1, features a modification of the amino acid from K to N at position 160.
+The protein's natural variant, known as in strain: cv. C24, features a modification of the amino acid from C to R at position 167.
+The protein's natural variant, known as in strain: cv. C24 and cv. Landsberg erecta, features a modification of the amino acid from I to T at position 172.
+The protein's natural variant, known as in strain: cv. C24 and cv. Landsberg erecta, features a modification of the amino acid from S to N at position 179.
+The protein's natural variant, known as in strain: cv. C24 and cv. Landsberg erecta, features a modification of the amino acid from I to M at position 215.
+The protein's natural variant, known as in strain: cv. C24 and cv. Landsberg erecta, features a modification of the amino acid from A to T at position 220.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from S to F at position 88.
+The protein's natural variant, known as may contribute to Hirschsprung disease in patients carrying a RET mutation;, features a modification of the amino acid from A to S at position 96.
+The protein's natural variant, known as in allele C3F; associated with susceptibility to ARMD9; results in decreased binding affinity for regulator factor H; results in reduced sensitivity to cleavage by factor I;, features a modification of the amino acid from R to G at position 102.
+The protein's natural variant, known as in ARMD9; results in resistance to proteolytic inactivation by CFH and CFI;, features a modification of the amino acid from K to Q at position 155.
+The protein's natural variant, known as in C3D; impairs secretion; variant confirmed at protein level;, features a modification of the amino acid from D to N at position 549.
+The protein's natural variant, known as in AHUS5; leads to impaired binding to the regulator CD46/MCP and resistance to cleavage by factor I;, features a modification of the amino acid from R to Q at position 592.
+The protein's natural variant, known as in AHUS5; leads to impaired binding to the regulator CD46/MCP and resistance to cleavage by factor I;, features a modification of the amino acid from R to W at position 592.
+The protein's natural variant, known as in AHUS5, features a modification of the amino acid from F to V at position 603.
+The protein's natural variant, known as in AHUS5;, features a modification of the amino acid from R to W at position 735.
+The protein's natural variant, known as in AHUS5, features a modification of the amino acid from R to L at position 1042.
+The protein's natural variant, known as in AHUS5; leads to impaired binding to the regulator CD46/MCP and resistance to cleavage by factor I;, features a modification of the amino acid from A to V at position 1094.
+The protein's natural variant, known as in AHUS5; leads to impaired binding to the regulator CD46/MCP and resistance to cleavage by factor I;, features a modification of the amino acid from D to N at position 1115.
+The protein's natural variant, known as in AHUS5, features a modification of the amino acid from C to W at position 1158.
+The protein's natural variant, known as in AHUS5; leads to impaired binding to the regulator CD46/MCP and resistance to cleavage by factor I, features a modification of the amino acid from Q to K at position 1161.
+The protein's natural variant, known as in AHUS5, features a modification of the amino acid from H to D at position 1464.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from A to T at position 48.
+The protein's natural variant, known as in AHMIO1;, features a modification of the amino acid from G to V at position 212.
+The protein's natural variant, known as in AHMIO1; increased skipping of exon 12;, features a modification of the amino acid from E to D at position 399.
+The protein's natural variant, known as in AHMIO1;, features a modification of the amino acid from R to C at position 416.
+The protein's natural variant, known as in AUTS20; risk factor for disease development; decreased function in dendritic spine formation; decreased protein abundance; does not localize to the plasma membrane but is retained in the endoplasmic reticulum, features a modification of the amino acid from P to L at position 89.
+The protein's natural variant, known as in AUTS20; unknown pathological significance; does not affect dendritic spine formation; no effect on protein abundance; no effect on subcellular localization, features a modification of the amino acid from T to I at position 90.
+The protein's natural variant, known as in AUTS20; risk factor for disease development; decreased function in dendritic spine formation; decreased protein abundance; does not localize to the plasma membrane but is retained in the endoplasmic reticulum, features a modification of the amino acid from L to P at position 309.
+The protein's natural variant, known as in AUTS20; risk factor for disease development; decreased function in dendritic spine formation; decreased protein abundance; does not localize to the plasma membrane but is retained in the endoplasmic reticulum, features a modification of the amino acid from G to E at position 337.
+The protein's natural variant, known as likely benign variant; does not affect dendritic spine formation; does not affect localization to plasma membrane, features a modification of the amino acid from R to H at position 756.
+The protein's natural variant, known as in AUTS20; risk factor for disease development; decreased function in dendritic spine formation; decreased protein abundance; does not affect subcellular location, features a modification of the amino acid from H to Y at position 835.
+The protein's natural variant, known as in strain: ZBMEL191, features a modification of the amino acid from N to K at position 104.
+The protein's natural variant, known as in strain: ZBMEL191, features a modification of the amino acid from A to T at position 146.
+The protein's natural variant, known as in strain: Oregon-R, ZBMEL84, ZBMEL95, ZBMEL131, ZBMEL157, ZBMEL186, ZBMEL191 and ZBMEL229, features a modification of the amino acid from G to A at position 149.
+The protein's natural variant, known as in strain: SK1, V1-09, YJM339 and YJM627, features a modification of the amino acid from N to S at position 30.
+The protein's natural variant, known as in strain: V1-09 and YJM627, features a modification of the amino acid from P to S at position 68.
+The protein's natural variant, known as in strain: YJM1129, features a modification of the amino acid from N to H at position 277.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from L to S at position 359.
+The protein's natural variant, known as in strain: YJM269 and YJM270, features a modification of the amino acid from N to I at position 364.
+The protein's natural variant, known as in strain: YJM1129, features a modification of the amino acid from Y to H at position 385.
+The protein's natural variant, known as in strain: V1-09, features a modification of the amino acid from E to G at position 429.
+The protein's natural variant, known as found in Jr(a-) blood group phenotype;, features a modification of the amino acid from V to M at position 12.
+The protein's natural variant, known as associated with high serum levels of uric acid and increased risk of gout; results in lower urate transport rates compared to wild-type; decreased protein abundance;, features a modification of the amino acid from Q to K at position 141.
+The protein's natural variant, known as loss of protein expression; loss of localization to the plasma membrane;, features a modification of the amino acid from R to W at position 147.
+The protein's natural variant, known as decreased protein abundance; no effect on localization to the plasma membrane; no effect on substrate transmembrane transport; decreased ATPase activity; no effect on ATPase-coupled transmembrane transporter activity;, features a modification of the amino acid from T to M at position 153.
+The natural variant of this protein is characterized by an amino acid alteration from T to P at position 316.
+The protein's natural variant, known as decreased protein abundance; decreased localization to the plasma membrane; no effect on ATPase-coupled transmembrane transporter activity;, features a modification of the amino acid from F to C at position 373.
+The protein's natural variant, known as no effect on protein abundance; no effect on substrate transmembrane transport;, features a modification of the amino acid from T to A at position 421.
+The natural variant of this protein is characterized by an amino acid alteration from F to L at position 431.
+The protein's natural variant, known as no effect on protein abundance; no effect on localization to the plasma membrane; increased ATPase activity; decreased ATPase-coupled transmembrane transporter activity;, features a modification of the amino acid from T to M at position 434.
+The protein's natural variant, known as no effect on protein abundance; no effect on localization to the plasma membrane; no effect on ATPase activity; decreased ATPase-coupled transmembrane transporter activity;, features a modification of the amino acid from S to P at position 476.
+The protein's natural variant, known as decreased protein abundance; loss of localization to the plasma membrane;, features a modification of the amino acid from S to R at position 572.
+The protein's natural variant, known as no effect on protein abundance; no effect on substrate transmembrane transport;, features a modification of the amino acid from D to N at position 620.
+The protein's natural variant, known as in MTB, features a modification of the amino acid from N to G at position 60.
+The protein's natural variant, known as in isoform II, features a modification of the amino acid from P to S at position 17.
+The natural variant of this protein is characterized by an amino acid alteration from T to M at position 72.
+The natural variant of this protein is characterized by an amino acid alteration from A to P at position 95.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from P to S at position 456.
+The protein's natural variant, known as in SCPIII, features a modification of the amino acid from Y to M at position 20.
+The protein's natural variant, known as in SCPIV, features a modification of the amino acid from D to N at position 23.
+The protein's natural variant, known as does not affect serine protease activity; shows reduced tumor suppressor activity; shows reduced ability to down-regulate phosphatidylethanolamine (PtdEtn) levels;, features a modification of the amino acid from R to K at position 469.
+The protein's natural variant, known as in strain: SJL/J, features a modification of the amino acid from QTFILEPSCLG to RT at position 104.
+The protein's natural variant, known as in CSS8, features a modification of the amino acid from N to D at position 134.
+The protein's natural variant, known as in CSS8, features a modification of the amino acid from L to P at position 609.
+The protein's natural variant, known as in CSS8;, features a modification of the amino acid from L to P at position 610.
+The protein's natural variant, known as in CSS8, features a modification of the amino acid from L to P at position 613.
+The protein's natural variant, known as in CSS8; unknown pathological significance, features a modification of the amino acid from C to R at position 635.
+The protein's natural variant, known as in CSS8; unknown pathological significance;, features a modification of the amino acid from M to V at position 896.
+The protein's natural variant, known as in CSS8; unknown pathological significance, features a modification of the amino acid from E to G at position 900.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from Q to R at position 103.
+The protein's natural variant, known as in CHDFIDD;, features a modification of the amino acid from G to R at position 714.
+The protein's natural variant, known as in CHDFIDD;, features a modification of the amino acid from G to R at position 717.
+The protein's natural variant, known as in CHDFIDD;, features a modification of the amino acid from K to E at position 734.
+The protein's natural variant, known as in CHDFIDD;, features a modification of the amino acid from R to Q at position 751.
+The protein's natural variant, known as in CHDFIDD;, features a modification of the amino acid from N to D at position 842.
+The protein's natural variant, known as in CHDFIDD;, features a modification of the amino acid from N to S at position 842.
+The protein's natural variant, known as in lysozyme-2, features a modification of the amino acid from L to R at position 34.
+The protein's natural variant, known as in lysozyme-2 and lysozyme-3, features a modification of the amino acid from T to S at position 85.
+The natural variant of this protein is characterized by an amino acid alteration from G to R at position 105.
+The protein's natural variant, known as in HYTG2; unknown pathological significance; no effect on transactivation activity in APOA4, APOC2 or FGF21 promoter-driven luciferase assays;, features a modification of the amino acid from P to L at position 166.
+The protein's natural variant, known as in HYTG2; unknown pathological significance; no effect on transactivation activity in APOA4, APOC2 or FGF21 promoter-driven luciferase assays;, features a modification of the amino acid from V to M at position 180.
+The protein's natural variant, known as in HYTG2; unknown pathological significance; no effect on transactivation activity in APOA4, APOC2 or FGF21 promoter-driven luciferase assays;, features a modification of the amino acid from D to N at position 182.
+The protein's natural variant, known as in HYTG2; risk factor; severely reduced transactivation activity in APOA4, APOC2 or FGF21 promoter-driven luciferase assays;, features a modification of the amino acid from E to K at position 240.
+The protein's natural variant, known as in strain: GA2.1S, HFL2.1S and HFL4.1S, features a modification of the amino acid from V to F at position 15.
+The protein's natural variant, known as in strain: GA2.1S, HFL2.1S, HFL4.1S and VA8.1S, features a modification of the amino acid from L to P at position 27.
+The protein's natural variant, known as in strain: HFL2.1S, HFL4.1S and VA8.1S, features a modification of the amino acid from T to A at position 60.
+The protein's natural variant, known as in strain: CT2.1S, CT5.1S, CT6.1S and VA6.1S, features a modification of the amino acid from K to R at position 277.
+The protein's natural variant, known as in strain: GA2.1S, features a modification of the amino acid from V to L at position 345.
+The protein's natural variant, known as in strain: HFL2.1S, VA7.1S and VA8.1S, features a modification of the amino acid from G to A at position 442.
+The protein's natural variant, known as in strain: HFL4.1S, features a modification of the amino acid from E to V at position 491.
+The protein's natural variant, known as in strain: GA2.1S, GA4.1S, GA5.1S, HFL1.1S, HFL2.1S, HFL4.1S, VA7.1S and VA8.1S, features a modification of the amino acid from D to N at position 496.
+The protein's natural variant, known as in strain: F/IC-Cal-13, features a modification of the amino acid from V to A at position 157.
+The protein's natural variant, known as in strain: F/IC-Cal-13, features a modification of the amino acid from I to V at position 348.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from F to L at position 881.
+The protein's natural variant, known as in strain: ATCC 90240 / AF-10, features a modification of the amino acid from L to N at position 398.
+The protein's natural variant, known as in strain: ATCC 90240 / AF-10, features a modification of the amino acid from I to V at position 573.
+The natural variant of this protein is characterized by an amino acid alteration from M to I at position 173.
+The natural variant of this protein is characterized by an amino acid alteration from L to I at position 704.
+The natural variant of this protein is characterized by an amino acid alteration from C to Y at position 1047.
+The natural variant of this protein is characterized by an amino acid alteration from K to Q at position 264.
+The natural variant of this protein is characterized by an amino acid alteration from R to Q at position 333.
+The protein's natural variant, known as in JBTS2;, features a modification of the amino acid from R to C at position 73.
+The protein's natural variant, known as in JBTS2 and MKS2;, features a modification of the amino acid from R to H at position 73.
+The protein's natural variant, known as in JBTS2;, features a modification of the amino acid from R to L at position 73.
+The protein's natural variant, known as in MKS2;, features a modification of the amino acid from G to A at position 77.
+The protein's natural variant, known as in JBTS2;, features a modification of the amino acid from L to F at position 89.
+The protein's natural variant, known as in MKS2;, features a modification of the amino acid from L to R at position 114.
+The protein's natural variant, known as in HPS5;, features a modification of the amino acid from L to R at position 624.
+The protein's natural variant, known as in HPS5;, features a modification of the amino acid from T to I at position 1098.
+The protein's natural variant, known as in BVVLS1; loss of riboflavin transport; no effect on localization to cell membrane; does not affect protein abundance;, features a modification of the amino acid from W to R at position 17.
+The protein's natural variant, known as in BVVLS1; loss of localization to cell membrane; loss of riboflavin transport;, features a modification of the amino acid from N to S at position 21.
+The protein's natural variant, known as in BVVLS1; loss of localization to cell membrane; loss of riboflavin transport; does not affect protein abundance;, features a modification of the amino acid from P to T at position 28.
+The protein's natural variant, known as in BVVLS1; loss of localization to cell membrane; loss of riboflavin transport; does not affect protein abundance;, features a modification of the amino acid from E to K at position 36.
+The protein's natural variant, known as in BVVLS1;, features a modification of the amino acid from V to D at position 58.
+The protein's natural variant, known as in BVVLS1; loss of localization to cell membrane; loss of riboflavin transport; does not affect protein abundance;, features a modification of the amino acid from E to K at position 71.
+The protein's natural variant, known as in BVVLS1; loss of localization to cell membrane; loss of riboflavin transport; does not affect protein abundance;, features a modification of the amino acid from R to W at position 132.
+The protein's natural variant, known as in BVVLS1; unknown pathological significance;, features a modification of the amino acid from P to H at position 220.
+The protein's natural variant, known as in BVVLS1;, features a modification of the amino acid from F to L at position 224.
+The protein's natural variant, known as in BVVLS1; unknown pathological significance;, features a modification of the amino acid from R to W at position 266.
+The protein's natural variant, known as in BVVLS1; unknown pathological significance;, features a modification of the amino acid from A to V at position 312.
+The protein's natural variant, known as in BVVLS1; unknown pathological significance;, features a modification of the amino acid from P to S at position 319.
+The protein's natural variant, known as in BVVLS1; unknown pathological significance;, features a modification of the amino acid from G to V at position 330.
+The protein's natural variant, known as no effect on riboflavin transport; no effect on localization to cell membrane;, features a modification of the amino acid from L to M at position 350.
+The protein's natural variant, known as in BVVLS1; unknown pathological significance;, features a modification of the amino acid from G to D at position 375.
+The protein's natural variant, known as in BVVLS1;, features a modification of the amino acid from V to A at position 413.
+The protein's natural variant, known as in BVVLS1;, features a modification of the amino acid from F to L at position 457.
+The protein's natural variant, known as in strain: MI 212, features a modification of the amino acid from T to A at position 12.
+The protein's natural variant, known as in strain: MI 212, features a modification of the amino acid from A to V at position 26.
+The protein's natural variant, known as confers streptomycin independence on streptomycin-dependent S12 mutant P90L, features a modification of the amino acid from G to D at position 102.
+The protein's natural variant, known as in strain: JB279; fast-growing suppressor of streptomycin resistant S12 mutant K42N, features a modification of the amino acid from G to S at position 109.
+The protein's natural variant, known as confers streptomycin independence on streptomycin-dependent S12 mutant P90L, features a modification of the amino acid from R to C at position 112.
+The protein's natural variant, known as in strain: Gif-sur-Yvette stock 115, features a modification of the amino acid from H to Q at position 211.
+The protein's natural variant, known as in strain: Gif-sur-Yvette stock 115, features a modification of the amino acid from T to N at position 213.
+The protein's natural variant, known as in strain: Gif-sur-Yvette stock 115, features a modification of the amino acid from G to R at position 233.
+The protein's natural variant, known as in IFAP1; does not affect subcellular localization; impairs activity;, features a modification of the amino acid from M to I at position 87.
+The protein's natural variant, known as in IFAP1; does not affect subcellular localization; impairs activity;, features a modification of the amino acid from W to L at position 226.
+The protein's natural variant, known as in IFAP1; does not affect subcellular localization; impairs activity;, features a modification of the amino acid from H to L at position 227.
+The protein's natural variant, known as in IFAP1; does not affect subcellular localization; impairs activity;, features a modification of the amino acid from R to H at position 429.
+The protein's natural variant, known as in OI19; decreased regulated intramembrane proteolysis resulting in reduced transcriptional activation of genes relevant to osteoblast differentiation and bone formation;, features a modification of the amino acid from N to S at position 459.
+The protein's natural variant, known as in OLMSX;, features a modification of the amino acid from F to S at position 464.
+The protein's natural variant, known as in IFAP1; does not affect subcellular localization; impairs activity;, features a modification of the amino acid from F to S at position 475.
+The protein's natural variant, known as in OI19; decreased regulated intramembrane proteolysis resulting in reduced transcriptional activation of genes relevant to osteoblast differentiation and bone formation;, features a modification of the amino acid from L to F at position 505.
+The protein's natural variant, known as in KFSDX; sterol responsiveness is reduced by half;, features a modification of the amino acid from N to S at position 508.
+The protein's natural variant, known as in strain: 85P, features a modification of the amino acid from V to D at position 76.
+The protein's natural variant, known as in strain: 85P, features a modification of the amino acid from A to P at position 123.
+The protein's natural variant, known as in strain: 85P, features a modification of the amino acid from I to V at position 293.
+The protein's natural variant, known as in strain: 85P, features a modification of the amino acid from GR to K at position 321.
+The natural variant of this protein is characterized by an amino acid alteration from L to P at position 64.
+The protein's natural variant, known as abolishes tyrosine sulfation;, features a modification of the amino acid from D to H at position 153.
+The protein's natural variant, known as found in a clear cell renal carcinoma; somatic mutation, features a modification of the amino acid from R to K at position 1020.
+The protein's natural variant, known as found in a gastric cancer sample; somatic mutation;, features a modification of the amino acid from R to W at position 1658.
+The protein's natural variant, known as found in a breast cancer sample; somatic mutation;, features a modification of the amino acid from I to F at position 1907.
+The protein's natural variant, known as found in a breast cancer sample; somatic mutation;, features a modification of the amino acid from G to R at position 2087.
+The protein's natural variant, known as found in a clear cell renal carcinoma case; somatic mutation, features a modification of the amino acid from L to P at position 2089.
+The protein's natural variant, known as in strain: Isolate Anna, features a modification of the amino acid from T to I at position 68.
+The protein's natural variant, known as in PAH-ENU1; mild PKU phenotype, features a modification of the amino acid from V to A at position 106.
+The protein's natural variant, known as in PAH-ENU2; severe PKU phenotype, features a modification of the amino acid from F to S at position 263.
+The protein's natural variant, known as in NMAN; negligible protein expression due to post-translational degradation; loss of homodimerization; significant decrease in adenosine 5'-monophosphoramidase activity; reduced SUMO-specific isopeptidase activity;, features a modification of the amino acid from R to P at position 37.
+The protein's natural variant, known as in NMAN; no mutant protein is detected due to post-translational degradation; no effect on SUMO-specific isopeptidase activity;, features a modification of the amino acid from H to R at position 51.
+The protein's natural variant, known as in NMAN; negligible protein expression due to post-translational degradation; no effect on homodimerization; no effect on adenosine 5'-monophosphoramidase; no effect on affinity for tryptamine adenosine phosphoramidate; loss of SUMO-specific isopeptidase activity;, features a modification of the amino acid from C to R at position 84.
+The protein's natural variant, known as in NMAN; no effect on homodimerization; no effect on adenosine 5'-monophosphoramidase activity; no effect on affinity for tryptamine adenosine phosphoramidate; loss of SUMO-specific isopeptidase activity;, features a modification of the amino acid from G to V at position 89.
+The protein's natural variant, known as in NMAN; loss of homodimerization; significant decrease in adenosine 5'-monophosphoramidase activity; approximately 40-fold increased affinity for tryptamine adenosine phosphoramidate; loss of SUMO-specific isopeptidase activity;, features a modification of the amino acid from G to D at position 93.
+The protein's natural variant, known as in NMAN; the enzyme has no residual activity although the mutant protein is expressed at normal levels; no effect on homodimerization; loss of SUMO-specific isopeptidase activity;, features a modification of the amino acid from H to N at position 112.
+The protein's natural variant, known as in In(A) antigen;, features a modification of the amino acid from R to P at position 46.
+The natural variant of this protein is characterized by an amino acid alteration from C to G at position 74.
+The natural variant of this protein is characterized by an amino acid alteration from C to S at position 74.
+The natural variant of this protein is characterized by an amino acid alteration from C to S at position 80.
+The natural variant of this protein is characterized by an amino acid alteration from F to Y at position 144.
+The natural variant of this protein is characterized by an amino acid alteration from S to V at position 232.
+The natural variant of this protein is characterized by an amino acid alteration from C to D at position 276.
+The natural variant of this protein is characterized by an amino acid alteration from C to N at position 276.
+The natural variant of this protein is characterized by an amino acid alteration from Q to H at position 284.
+The protein's natural variant, known as in allele TYKY2, features a modification of the amino acid from HTIE to QAWQ at position 26.
+The protein's natural variant, known as in allele TYKY2, features a modification of the amino acid from GYNR to TPNG at position 33.
+The protein's natural variant, known as in strain: cv. Bintje, features a modification of the amino acid from E to R at position 57.
+The protein's natural variant, known as in strain: cv. Bintje, features a modification of the amino acid from E to K at position 62.
+The protein's natural variant, known as in strain: cv. Bintje, features a modification of the amino acid from K to T at position 65.
+The protein's natural variant, known as in allele TYKY2, features a modification of the amino acid from R to H at position 121.
+The protein's natural variant, known as in allele TYKY2, features a modification of the amino acid from T to I at position 216.
+The protein's natural variant, known as in CMD1JJ; loss of integrin-binding capacity, features a modification of the amino acid from P to L at position 950.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from L to S at position 213.
+The protein's natural variant, known as in HH25; no effect on protein abundance; no effect on function in cellular response to fibroblast growth factor stimulus;, features a modification of the amino acid from T to S at position 201.
+The protein's natural variant, known as in BJS; with mild mitochondrial complex III deficiency;, features a modification of the amino acid from G to R at position 35.
+The protein's natural variant, known as in MC3DN1;, features a modification of the amino acid from R to C at position 45.
+The protein's natural variant, known as in MC3DN1;, features a modification of the amino acid from T to A at position 50.
+The protein's natural variant, known as in MC3DN1;, features a modification of the amino acid from R to C at position 73.
+The protein's natural variant, known as in GRACILE;, features a modification of the amino acid from S to G at position 78.
+The protein's natural variant, known as in MC3DN1;, features a modification of the amino acid from P to L at position 99.
+The protein's natural variant, known as in BJS;, features a modification of the amino acid from R to W at position 114.
+The protein's natural variant, known as in MC3DN1;, features a modification of the amino acid from G to R at position 129.
+The protein's natural variant, known as in GRACILE;, features a modification of the amino acid from R to Q at position 144.
+The protein's natural variant, known as in MC3DN1; abolishes interaction with LETM1;, features a modification of the amino acid from R to P at position 155.
+The protein's natural variant, known as in MC3DN1; causes a decreased incorporation of the Rieske iron-sulfur protein UQCRFS1 into complex III;, features a modification of the amino acid from R to C at position 183.
+The protein's natural variant, known as in BJS;, features a modification of the amino acid from R to H at position 183.
+The protein's natural variant, known as in MC3DN1 and BJS; with mild mitochondrial complex III deficiency; causes a decreased incorporation of the Rieske iron-sulfur protein UQCRFS1 into complex III;, features a modification of the amino acid from R to C at position 184.
+The protein's natural variant, known as in MC3DN1;, features a modification of the amino acid from S to N at position 277.
+The protein's natural variant, known as in BJS;, features a modification of the amino acid from Y to N at position 301.
+The protein's natural variant, known as in BJS;, features a modification of the amino acid from Q to E at position 302.
+The protein's natural variant, known as in BJS;, features a modification of the amino acid from R to H at position 306.
+The protein's natural variant, known as in GRACILE;, features a modification of the amino acid from V to A at position 327.
+The protein's natural variant, known as in MC3DN1;, features a modification of the amino acid from V to M at position 353.
+The protein's natural variant, known as in MC3DN1, features a modification of the amino acid from F to I at position 368.
+The protein's natural variant, known as in breast cancer samples; infiltrating ductal carcinoma; somatic mutation;, features a modification of the amino acid from H to Y at position 539.
+The protein's natural variant, known as in strain: SRRC 2043, features a modification of the amino acid from A to S at position 143.
+The protein's natural variant, known as in strain: SRRC 2043; loss of activity, features a modification of the amino acid from H to L at position 400.
+The protein's natural variant, known as in strain: SRRC 2043, features a modification of the amino acid from I to Y at position 528.
+The protein's natural variant, known as in a lung bronchoalveolar carcinoma sample; somatic mutation, features a modification of the amino acid from R to K at position 104.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from I to V at position 164.
+The protein's natural variant, known as in AILJK; causes a defect in retrograde transport from the Golgi to the endoplasmic reticulum;, features a modification of the amino acid from K to N at position 230.
+The protein's natural variant, known as in AILJK;, features a modification of the amino acid from R to H at position 233.
+The protein's natural variant, known as in AILJK; causes a defect in retrograde transport from the Golgi to the endoplasmic reticulum;, features a modification of the amino acid from E to K at position 241.
+The protein's natural variant, known as in AILJK;, features a modification of the amino acid from D to G at position 243.
+The protein's natural variant, known as in LEPRD; unknown pathological significance, features a modification of the amino acid from Y to H at position 422.
+The protein's natural variant, known as in LEPRD; unknown pathological significance, features a modification of the amino acid from C to G at position 604.
+The protein's natural variant, known as in LEPRD; unknown pathological significance;, features a modification of the amino acid from L to P at position 786.
+The protein's natural variant, known as in HMMS; hypomorphic mutation;, features a modification of the amino acid from A to P at position 150.
+The protein's natural variant, known as in HMMS; hypomorphic mutation;, features a modification of the amino acid from N to K at position 166.
+The protein's natural variant, known as in MRD10; significantly reduced ability to bind GRIA1 or GRIA2 AMPARs; cell surface expression of GRIA1 is reduced in transfected hippocampal neurons and HEK293 cells producing mutant protein compared to cells producing the wild-type, features a modification of the amino acid from V to L at position 143.
+The protein's natural variant, known as in strain: CBS 1907, features a modification of the amino acid from Y to F at position 143.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from V to M at position 329.
+The protein's natural variant, known as in strain: C57BL/6J, features a modification of the amino acid from L to R at position 20.
+The protein's natural variant, known as in strain: APEC13, features a modification of the amino acid from G to W at position 175.
+The protein's natural variant, known as in strain: APEC13, features a modification of the amino acid from D to G at position 183.
+The protein's natural variant, known as in strain: A2363 and APEC13, features a modification of the amino acid from Q to K at position 209.
+The protein's natural variant, known as in strain: A2363, features a modification of the amino acid from F to S at position 326.
+The protein's natural variant, known as in strain: A2363, features a modification of the amino acid from H to Y at position 422.
+The protein's natural variant, known as in strain: A2363, features a modification of the amino acid from G to S at position 634.
+The protein's natural variant, known as in strain: A2363, features a modification of the amino acid from A to T at position 842.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from P to S at position 454.
+The protein's natural variant, known as in DFNA2A;, features a modification of the amino acid from L to H at position 274.
+The protein's natural variant, known as in DFNA2A;, features a modification of the amino acid from W to S at position 276.
+The protein's natural variant, known as in DFNA2A;, features a modification of the amino acid from L to S at position 281.
+The protein's natural variant, known as in DFNA2A; loss of potassium selectivity of the pore;, features a modification of the amino acid from G to C at position 285.
+The protein's natural variant, known as in DFNA2A; dominant negative effect; abolishes potassium current;, features a modification of the amino acid from G to S at position 285.
+The protein's natural variant, known as in DFNA2A;, features a modification of the amino acid from G to R at position 287.
+The protein's natural variant, known as in DFNA2A;, features a modification of the amino acid from G to S at position 321.
+The protein's natural variant, known as in CD8 deficiency; prevents CD8 expression;, features a modification of the amino acid from G to S at position 111.
+The protein's natural variant, known as found in a patient with spastic paraplegia; unknown pathological significance;, features a modification of the amino acid from Q to K at position 310.
+The protein's natural variant, known as in PITA4; somatic mutation; unknown pathological significance;, features a modification of the amino acid from S to C at position 718.
+The protein's natural variant, known as in PITA4; somatic mutation; unknown pathological significance; localizes to nucleus instead of cytoplasm;, features a modification of the amino acid from S to P at position 718.
+The protein's natural variant, known as in PITA4; somatic mutation; unknown pathological significance;, features a modification of the amino acid from P to R at position 720.
+The protein's natural variant, known as found in siblings with familial natural-killer/T-cell lymphoma; unknown pathological significance, features a modification of the amino acid from R to C at position 943.
+The protein's natural variant, known as in MJDS;, features a modification of the amino acid from S to L at position 734.
+The protein's natural variant, known as in NMOAS, features a modification of the amino acid from G to E at position 427.
+The protein's natural variant, known as in NMOAS; unknown pathological significance, features a modification of the amino acid from F to I at position 582.
+The protein's natural variant, known as in NMOAS; unknown pathological significance, features a modification of the amino acid from T to M at position 674.
+The protein's natural variant, known as in NMOAS; unknown pathological significance, features a modification of the amino acid from Q to H at position 697.
+The protein's natural variant, known as found in a patient with early-onset epithelial ovarian tumor; unknown pathological significance; alters the ratio of secreted activins and ihibins, features a modification of the amino acid from R to L at position 60.
+The protein's natural variant, known as may play a role in premature ovarian failure;, features a modification of the amino acid from A to T at position 257.
+The protein's natural variant, known as in NPHP3;, features a modification of the amino acid from S to T at position 360.
+The protein's natural variant, known as in NPHP3;, features a modification of the amino acid from N to S at position 386.
+The protein's natural variant, known as in NPHP3;, features a modification of the amino acid from R to H at position 397.
+The protein's natural variant, known as in RHPD1;, features a modification of the amino acid from R to Q at position 973.
+The protein's natural variant, known as in NPHP3;, features a modification of the amino acid from L to P at position 1141.
+The protein's natural variant, known as in NPHP3;, features a modification of the amino acid from A to V at position 1221.
+The protein's natural variant, known as in NPHP3;, features a modification of the amino acid from S to R at position 1252.
+The protein's natural variant, known as in NPHP3; likely benign variant;, features a modification of the amino acid from S to T at position 1314.
+The protein's natural variant, known as in CSTLO;, features a modification of the amino acid from G to A at position 12.
+The protein's natural variant, known as in CSTLO;, features a modification of the amino acid from G to C at position 12.
+The protein's natural variant, known as in CSTLO; severe mutation;, features a modification of the amino acid from G to D at position 12.
+The protein's natural variant, known as in CSTLO, features a modification of the amino acid from G to E at position 12.
+The protein's natural variant, known as in CSTLO and CMEMS; also found in patients with oral squamous cell carcinoma;, features a modification of the amino acid from G to S at position 12.
+The protein's natural variant, known as in CSTLO, bladder carcinoma and CMEMS; constitutively activated; interacts and recruits PLCE1 to plasma membrane;, features a modification of the amino acid from G to V at position 12.
+The protein's natural variant, known as in CSTLO;, features a modification of the amino acid from G to C at position 13.
+The protein's natural variant, known as in CSTLO;, features a modification of the amino acid from G to D at position 13.
+The protein's natural variant, known as in SFM; somatic mutation; shows constitutive activation of the MAPK and PI3K-AKT signaling pathways;, features a modification of the amino acid from G to R at position 13.
+The protein's natural variant, known as in CMEMS;, features a modification of the amino acid from Q to K at position 22.
+The protein's natural variant, known as in CSTLO, features a modification of the amino acid from E to EE at position 37.
+The protein's natural variant, known as in CSTLO;, features a modification of the amino acid from T to I at position 58.
+The protein's natural variant, known as in NMTC2; somatic mutation; increases transformation of cultured cell lines;, features a modification of the amino acid from Q to K at position 61.
+The protein's natural variant, known as in melanoma; strongly reduced GTP hydrolysis in the presence of RAF1; increases transformation of cultured cell lines;, features a modification of the amino acid from Q to L at position 61.
+The protein's natural variant, known as in CMEMS;, features a modification of the amino acid from E to K at position 63.
+The protein's natural variant, known as found in a patient with severe fetal hydrops and pleural effusion; unknown pathological significance; decreased activation of Ras protein signal transduction;, features a modification of the amino acid from S to C at position 89.
+The protein's natural variant, known as in CSTLO;, features a modification of the amino acid from K to R at position 117.
+The protein's natural variant, known as in CSTLO;, features a modification of the amino acid from A to T at position 146.
+The protein's natural variant, known as in CSTLO;, features a modification of the amino acid from A to V at position 146.
+The natural variant of this protein is characterized by an amino acid alteration from H to R at position 127.
+The protein's natural variant, known as associated with susceptibility to ischemic stroke;, features a modification of the amino acid from L to V at position 640.
+The protein's natural variant, known as reduced frequency in patients with myocardial infarction;, features a modification of the amino acid from T to P at position 756.
+The natural variant of this protein is characterized by an amino acid alteration from E to D at position 88.
+The natural variant of this protein is characterized by an amino acid alteration from S to P at position 558.
+The protein's natural variant, known as more susceptible to N-terminal truncation and shows greater distribution to the VLDL than the protein with T-71;, features a modification of the amino acid from T to S at position 71.
+The protein's natural variant, known as in LPHDST;, features a modification of the amino acid from S to L at position 125.
+The protein's natural variant, known as in PBD9B;, features a modification of the amino acid from T to P at position 14.
+The protein's natural variant, known as in RCDP1; unknown pathological significance;, features a modification of the amino acid from G to R at position 217.
+The protein's natural variant, known as in RCDP1;, features a modification of the amino acid from A to V at position 218.
+The protein's natural variant, known as in SPGF50 and POF17; due to a nucleotide substitution that causes partial exon 2 skipping; patient cells contain both normally spliced transcripts and transcripts lacking exon 2;, features a modification of the amino acid from L to P at position 14.
+The protein's natural variant, known as does not affect function in double-strand break repair via homologous recombination as shown in rescue assays of XRCC2-deficient cells;, features a modification of the amino acid from A to S at position 16.
+The protein's natural variant, known as does not affect function in double-strand break repair via homologous recombination as shown in rescue assays of XRCC2-deficient cells;, features a modification of the amino acid from H to R at position 47.
+The protein's natural variant, known as does not affect function in double-strand break repair via homologous recombination as shown in rescue assays of XRCC2-deficient cells;, features a modification of the amino acid from L to I at position 61.
+The protein's natural variant, known as does not affect function in double-strand break repair via homologous recombination as shown in rescue assays of XRCC2-deficient cells;, features a modification of the amino acid from E to Q at position 75.
+The protein's natural variant, known as rare variant; found in breast cancer; unknown pathological significance; moderately decreased function in double-strand break repair via homologous recombination as shown in rescue assays of XRCC2-deficient cells;, features a modification of the amino acid from R to W at position 91.
+The protein's natural variant, known as does not affect function in double-strand break repair via homologous recombination as shown in rescue assays of XRCC2-deficient cells;, features a modification of the amino acid from I to V at position 95.
+The protein's natural variant, known as does not affect function in double-strand break repair via homologous recombination as shown in rescue assays of XRCC2-deficient cells;, features a modification of the amino acid from V to A at position 118.
+The protein's natural variant, known as rare variant; found in breast cancer; unknown pathological significance; moderately decreased function in double-strand break repair via homologous recombination as shown in rescue assays of XRCC2-deficient cells;, features a modification of the amino acid from C to Y at position 120.
+The protein's natural variant, known as rare variant; found in breast cancer; unknown pathological significance; moderately decreased function in double-strand break repair via homologous recombination as shown in rescue assays of XRCC2-deficient cells;, features a modification of the amino acid from L to P at position 133.
+The protein's natural variant, known as does not affect function in double-strand break repair via homologous recombination as shown in rescue assays of XRCC2-deficient cells;, features a modification of the amino acid from E to Q at position 164.
+The protein's natural variant, known as does not affect function in double-strand break repair via homologous recombination as shown in rescue assays of XRCC2-deficient cells;, features a modification of the amino acid from E to A at position 170.
+The protein's natural variant, known as does not affect function in double-strand break repair via homologous recombination as shown in rescue assays of XRCC2-deficient cells;, features a modification of the amino acid from R to C at position 188.
+The protein's natural variant, known as does not affect function in double-strand break repair via homologous recombination as shown in rescue assays of XRCC2-deficient cells;, features a modification of the amino acid from R to H at position 188.
+The protein's natural variant, known as does not affect function in double-strand break repair via homologous recombination as shown in rescue assays of XRCC2-deficient cells;, features a modification of the amino acid from T to M at position 194.
+The protein's natural variant, known as likely benign variant; does not affect function in double-strand break repair via homologous recombination as shown in rescue assays of XRCC2-deficient cells;, features a modification of the amino acid from M to L at position 199.
+The protein's natural variant, known as does not affect function in double-strand break repair via homologous recombination as shown in rescue assays of XRCC2-deficient cells;, features a modification of the amino acid from E to G at position 207.
+The protein's natural variant, known as does not affect function in double-strand break repair via homologous recombination as shown in rescue assays of XRCC2-deficient cells;, features a modification of the amino acid from D to V at position 220.
+The protein's natural variant, known as does not affect function in double-strand break repair via homologous recombination as shown in rescue assays of XRCC2-deficient cells;, features a modification of the amino acid from W to C at position 231.
+The protein's natural variant, known as does not affect function in double-strand break repair via homologous recombination as shown in rescue assays of XRCC2-deficient cells;, features a modification of the amino acid from R to S at position 238.
+The protein's natural variant, known as does not affect function in double-strand break repair via homologous recombination as shown in rescue assays of XRCC2-deficient cells;, features a modification of the amino acid from Q to E at position 248.
+The protein's natural variant, known as does not affect function in double-strand break repair via homologous recombination as shown in rescue assays of XRCC2-deficient cells;, features a modification of the amino acid from R to C at position 258.
+The protein's natural variant, known as does not affect function in double-strand break repair via homologous recombination as shown in rescue assays of XRCC2-deficient cells;, features a modification of the amino acid from F to V at position 270.
+The protein's natural variant, known as in MC1DN33, features a modification of the amino acid from R to P at position 64.
+The protein's natural variant, known as in allele asc-1, features a modification of the amino acid from RKKINKFKESAWKFVYFLS to EEDQQIQRVSMEICIFSIC at position 87.
+The protein's natural variant, known as in strain: cv. Cvi-1, cv. Fe-1a, cv. Goe-0, cv. Ita-0, cv. Nd-1 and cv. Wei-0, features a modification of the amino acid from F to S at position 3.
+The protein's natural variant, known as in strain: cv. Cvi-1, cv. Fe-1a, cv. Goe-0, cv. Ita-0, cv. Nd-1 and cv. Wei-0, features a modification of the amino acid from L to F at position 8.
+The protein's natural variant, known as in strain: cv. Cvi-1, cv. Fe-1a, cv. Goe-0, cv. Ita-0, cv. Nd-1 and cv. Wei-0, features a modification of the amino acid from F to I at position 13.
+The protein's natural variant, known as probable disease-associated variant found in patient with an acute aortic dissection and ascending aortic aneurysm;, features a modification of the amino acid from E to Q at position 15.
+The protein's natural variant, known as probable disease-associated variant found in patient with basilar tip artery aneurysm and distal left internal carotid artery aneurysm;, features a modification of the amino acid from E to G at position 44.
+The protein's natural variant, known as in NEDHSB;, features a modification of the amino acid from R to Q at position 84.
+The protein's natural variant, known as in NEDHSB;, features a modification of the amino acid from S to I at position 90.
+The protein's natural variant, known as in NEDHSB;, features a modification of the amino acid from A to T at position 100.
+The protein's natural variant, known as in NEDHSB;, features a modification of the amino acid from S to L at position 448.
+The protein's natural variant, known as in NEDHSB, features a modification of the amino acid from V to L at position 488.
+The protein's natural variant, known as in NEDHSB;, features a modification of the amino acid from R to Q at position 529.
+The protein's natural variant, known as in NEDHSB;, features a modification of the amino acid from W to C at position 626.
+The protein's natural variant, known as in NEDHSB; impaired maturation of pre-60S ribosome;, features a modification of the amino acid from D to G at position 628.
+The protein's natural variant, known as in NEDHSB;, features a modification of the amino acid from R to Q at position 784.
+The protein's natural variant, known as in NEDHSB;, features a modification of the amino acid from A to V at position 844.
+The protein's natural variant, known as in a patient with diffuse large B-cell lymphoma; unknown pathological significance;, features a modification of the amino acid from K to E at position 200.
+The protein's natural variant, known as in a patient with diffuse large B-cell lymphoma; unknown pathological significance;, features a modification of the amino acid from R to S at position 285.
+The protein's natural variant, known as in PCH10; decreases kinase activity, impairs formation of the tRNA splicing endonuclease complex and impairs ability to mediate tRNA splicing and maturation;, features a modification of the amino acid from R to H at position 140.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from K to R at position 87.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from N to S at position 223.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from N to S at position 353.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from D to N at position 586.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from M to V at position 607.
+The natural variant of this protein is characterized by an amino acid alteration from L to P at position 14.
+The natural variant of this protein is characterized by an amino acid alteration from T to P at position 157.
+The protein's natural variant, known as in IBS; unknown pathological significance;, features a modification of the amino acid from E to K at position 178.
+The protein's natural variant, known as in IBS;, features a modification of the amino acid from Q to P at position 181.
+The protein's natural variant, known as in IBS;, features a modification of the amino acid from I to N at position 182.
+The protein's natural variant, known as in IBS;, features a modification of the amino acid from N to D at position 186.
+The protein's natural variant, known as in IBS;, features a modification of the amino acid from N to K at position 186.
+The protein's natural variant, known as in IBS;, features a modification of the amino acid from N to Y at position 186.
+The protein's natural variant, known as in IBS, features a modification of the amino acid from E to D at position 465.
+The protein's natural variant, known as in IBS;, features a modification of the amino acid from E to K at position 465.
+The protein's natural variant, known as in IBS;, features a modification of the amino acid from E to K at position 476.
+The protein's natural variant, known as in IBS;, features a modification of the amino acid from E to V at position 476.
+The protein's natural variant, known as in IBS, features a modification of the amino acid from I to N at position 477.
+The protein's natural variant, known as in IBS;, features a modification of the amino acid from T to P at position 479.
+The protein's natural variant, known as in IBS;, features a modification of the amino acid from L to P at position 484.
+The protein's natural variant, known as in IBS;, features a modification of the amino acid from E to D at position 487.
+The protein's natural variant, known as in IBS;, features a modification of the amino acid from E to K at position 487.
+The protein's natural variant, known as in IBS;, features a modification of the amino acid from E to K at position 488.
+The protein's natural variant, known as in CSS3; patient with original diagnosis of Kleefstra syndrome; unknown pathological significance;, features a modification of the amino acid from R to H at position 37.
+The protein's natural variant, known as in CSS3;, features a modification of the amino acid from R to C at position 366.
+The protein's natural variant, known as in CSS3;, features a modification of the amino acid from R to Q at position 374.
+The protein's natural variant, known as in CSS3;, features a modification of the amino acid from R to H at position 377.
+The protein's natural variant, known as in DAND;, features a modification of the amino acid from W to R at position 321.
+The natural variant of this protein is characterized by an amino acid alteration from R to E at position 18.
+The natural variant of this protein is characterized by an amino acid alteration from E to R at position 47.
+The natural variant of this protein is characterized by an amino acid alteration from E to S at position 47.
+The natural variant of this protein is characterized by an amino acid alteration from D to N at position 48.
+The protein's natural variant, known as in CFEOM1; de novo mutation, features a modification of the amino acid from D to E at position 352.
+The protein's natural variant, known as in CFEOM1;, features a modification of the amino acid from M to T at position 356.
+The protein's natural variant, known as in CFEOM1, features a modification of the amino acid from E to Q at position 944.
+The protein's natural variant, known as in CFEOM1;, features a modification of the amino acid from M to R at position 947.
+The protein's natural variant, known as in CFEOM1, features a modification of the amino acid from M to T at position 947.
+The protein's natural variant, known as in CFEOM1;, features a modification of the amino acid from M to V at position 947.
+The protein's natural variant, known as in CFEOM1, features a modification of the amino acid from R to L at position 954.
+The protein's natural variant, known as in CFEOM1;, features a modification of the amino acid from R to Q at position 954.
+The protein's natural variant, known as in CFEOM1;, features a modification of the amino acid from R to W at position 954.
+The protein's natural variant, known as in CFEOM1, features a modification of the amino acid from A to P at position 1008.
+The protein's natural variant, known as in CFEOM1;, features a modification of the amino acid from I to T at position 1010.
+The natural variant of this protein is characterized by an amino acid alteration from V to A at position 1025.
+The protein's natural variant, known as in strain: cv. Cvi-1, features a modification of the amino acid from N to S at position 2.
+The protein's natural variant, known as in strain: cv. Cvi-1, features a modification of the amino acid from V to I at position 19.
+The protein's natural variant, known as in strain: cv. Cvi-1, features a modification of the amino acid from A to V at position 142.
+The protein's natural variant, known as in strain: Rockefeller, features a modification of the amino acid from E to A at position 9.
+The protein's natural variant, known as in strain: Rockefeller, features a modification of the amino acid from V to P at position 30.
+The protein's natural variant, known as in strain: Rockefeller, features a modification of the amino acid from V to A at position 61.
+The protein's natural variant, known as in strain: Rockefeller, features a modification of the amino acid from N to K at position 224.
+The protein's natural variant, known as in strain: Rockefeller, features a modification of the amino acid from L to I at position 284.
+The protein's natural variant, known as in strain: Rockefeller, features a modification of the amino acid from EE to DT at position 315.
+The protein's natural variant, known as in strain: Rockefeller, features a modification of the amino acid from KN to QH at position 320.
+The protein's natural variant, known as in strain: Rockefeller, features a modification of the amino acid from A to E at position 347.
+The protein's natural variant, known as in strain: Rockefeller, features a modification of the amino acid from M to K at position 361.
+The protein's natural variant, known as in strain: Rockefeller, features a modification of the amino acid from V to I at position 472.
+The protein's natural variant, known as in strain: Rockefeller, features a modification of the amino acid from K to E at position 491.
+The protein's natural variant, known as in strain: Rockefeller, features a modification of the amino acid from E to Q at position 498.
+The protein's natural variant, known as in DIAR4; attenuated NEUROG3 function in vivo;, features a modification of the amino acid from R to L at position 93.
+The protein's natural variant, known as in DIAR4; attenuated NEUROG3 function in vivo;, features a modification of the amino acid from R to S at position 107.
+The protein's natural variant, known as found in a renal cell carcinoma case; somatic mutation, features a modification of the amino acid from N to S at position 39.
+The protein's natural variant, known as in AI2A6;, features a modification of the amino acid from L to P at position 74.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from R to Q at position 60.
+The protein's natural variant, known as in variant 1, features a modification of the amino acid from H to L at position 3.
+The protein's natural variant, known as in variants 2 and 3, features a modification of the amino acid from L to M at position 17.
+The protein's natural variant, known as in variants 2, 3 and 4, features a modification of the amino acid from K to T at position 68.
+The protein's natural variant, known as in variant 2, features a modification of the amino acid from V to L at position 138.
+The protein's natural variant, known as in strain: Isolate TK 25127, features a modification of the amino acid from A to T at position 39.
+The protein's natural variant, known as in strain: Isolate TK 15571 and Isolate TK 25127, features a modification of the amino acid from I to V at position 98.
+The protein's natural variant, known as in strain: Isolate TK 15571 and Isolate TK 25127, features a modification of the amino acid from M to V at position 194.
+The protein's natural variant, known as in strain: Isolate TK 15571 and Isolate TK 25127, features a modification of the amino acid from IV to VI at position 304.
+The protein's natural variant, known as in strain: Isolate TK 15571, features a modification of the amino acid from M to T at position 316.
+The protein's natural variant, known as in strain: Isolate TK 15571 and Isolate TK 25127, features a modification of the amino acid from M to V at position 353.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation;, features a modification of the amino acid from E to K at position 11.
+The natural variant of this protein is characterized by an amino acid alteration from P to S at position 1301.
+The natural variant of this protein is characterized by an amino acid alteration from D to N at position 152.
+The protein's natural variant, known as in AMEDS;, features a modification of the amino acid from A to P at position 278.
+The protein's natural variant, known as in strain: NCTC 11906 and PO-329, features a modification of the amino acid from I to V at position 14.
+The protein's natural variant, known as in strain: NCTC 11906 and PO-329, features a modification of the amino acid from T to I at position 74.
+The protein's natural variant, known as in strain: 1006, features a modification of the amino acid from I to M at position 482.
+The protein's natural variant, known as in strain: cv. C24, features a modification of the amino acid from V to I at position 361.
+The protein's natural variant, known as in tr-J, features a modification of the amino acid from L to P at position 16.
+The protein's natural variant, known as in tr, features a modification of the amino acid from G to D at position 150.
+The protein's natural variant, known as in HTOCD;, features a modification of the amino acid from H to Y at position 60.
+The protein's natural variant, known as in HTOCD, features a modification of the amino acid from D to E at position 207.
+The protein's natural variant, known as in HTOCD;, features a modification of the amino acid from G to C at position 380.
+The protein's natural variant, known as in HTOCD; mutant channels show reduced ATP sensitivity; rat ABCC9 construct containing this mutation shows gain of function, features a modification of the amino acid from P to L at position 432.
+The protein's natural variant, known as in HTOCD; rat ABCC9 construct containing this mutation shows gain of function;, features a modification of the amino acid from A to V at position 478.
+The protein's natural variant, known as in HTOCD;, features a modification of the amino acid from S to P at position 1020.
+The protein's natural variant, known as in HTOCD, features a modification of the amino acid from F to S at position 1039.
+The protein's natural variant, known as in HTOCD; rat ABCC9 construct containing this mutation shows gain of function;, features a modification of the amino acid from C to Y at position 1043.
+The protein's natural variant, known as in HTOCD, features a modification of the amino acid from S to Y at position 1054.
+The protein's natural variant, known as in HTOCD;, features a modification of the amino acid from R to C at position 1116.
+The protein's natural variant, known as in HTOCD; mutant channels show reduced ATP sensitivity;, features a modification of the amino acid from R to H at position 1116.
+The protein's natural variant, known as in HTOCD; mutant channels show reduced ATP sensitivity;, features a modification of the amino acid from R to Q at position 1154.
+The protein's natural variant, known as in HTOCD;, features a modification of the amino acid from R to W at position 1154.
+The protein's natural variant, known as unknown pathological significance;, features a modification of the amino acid from L to R at position 1160.
+The protein's natural variant, known as in CMD1O;, features a modification of the amino acid from A to T at position 1513.
+The protein's natural variant, known as in ATFB12; compromises adenine nucleotide-dependent induction of KATP current; mutant ABCC9 that is coexpressed with KCNJ11 pore generates an aberrant channel that retains ATP-induced inhibition of potassium current, but shows a blunted response to ADP;, features a modification of the amino acid from T to I at position 1547.
+The protein's natural variant, known as probable disease-associated variant found in patients with hypercholesterolemia;, features a modification of the amino acid from T to M at position 56.
+The protein's natural variant, known as in FHCL4; Lebanon; requires 2 nucleotide substitutions;, features a modification of the amino acid from S to H at position 202.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from S to L at position 22.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from T to I at position 201.
+The protein's natural variant, known as in AMYL5; does not result in actin depolymerization in absence of calcium;, features a modification of the amino acid from D to N at position 214.
+The protein's natural variant, known as in AMYL5;, features a modification of the amino acid from D to Y at position 214.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from S to N at position 611.
+The protein's natural variant, known as in HLRCC;, features a modification of the amino acid from N to T at position 107.
+The protein's natural variant, known as in HLRCC;, features a modification of the amino acid from A to P at position 117.
+The protein's natural variant, known as in HLRCC;, features a modification of the amino acid from H to R at position 180.
+The protein's natural variant, known as in HLRCC;, features a modification of the amino acid from Q to R at position 185.
+The protein's natural variant, known as in FMRD and HLRCC;, features a modification of the amino acid from K to R at position 230.
+The protein's natural variant, known as in HLRCC; catalytically inactive mutant; abolished ability to promote DNA repair;, features a modification of the amino acid from R to H at position 233.
+The protein's natural variant, known as in HLRCC;, features a modification of the amino acid from G to V at position 282.
+The protein's natural variant, known as in FMRD;, features a modification of the amino acid from A to T at position 308.
+The protein's natural variant, known as in FMRD;, features a modification of the amino acid from F to C at position 312.
+The protein's natural variant, known as in HLRCC, features a modification of the amino acid from M to R at position 328.
+The protein's natural variant, known as in HLRCC;, features a modification of the amino acid from E to Q at position 362.
+The protein's natural variant, known as in FMRD, features a modification of the amino acid from D to V at position 425.
+The protein's natural variant, known as in ASGD8;, features a modification of the amino acid from S to P at position 1404.
+The natural variant of this protein is characterized by an amino acid alteration from L to S at position 15.
+The natural variant of this protein is characterized by an amino acid alteration from R to A at position 142.
+The natural variant of this protein is characterized by an amino acid alteration from N to NN at position 58.
+The protein's natural variant, known as in strain: Pasteur, features a modification of the amino acid from S to N at position 400.
+The protein's natural variant, known as in HFE2A;, features a modification of the amino acid from C to R at position 80.
+The protein's natural variant, known as in HFE2A;, features a modification of the amino acid from S to P at position 85.
+The protein's natural variant, known as in HFE2A;, features a modification of the amino acid from G to R at position 99.
+The protein's natural variant, known as in HFE2A;, features a modification of the amino acid from L to P at position 101.
+The protein's natural variant, known as in HFE2A;, features a modification of the amino acid from A to D at position 168.
+The protein's natural variant, known as in HFE2A;, features a modification of the amino acid from F to S at position 170.
+The protein's natural variant, known as in HFE2A;, features a modification of the amino acid from D to E at position 172.
+The protein's natural variant, known as in HFE2A;, features a modification of the amino acid from W to C at position 191.
+The protein's natural variant, known as in HFE2A;, features a modification of the amino acid from S to R at position 205.
+The protein's natural variant, known as in HFE2A;, features a modification of the amino acid from I to N at position 222.
+The protein's natural variant, known as in HFE2A;, features a modification of the amino acid from G to V at position 250.
+The protein's natural variant, known as in HFE2A;, features a modification of the amino acid from R to W at position 288.
+The protein's natural variant, known as in HFE2A;, features a modification of the amino acid from G to V at position 320.
+The protein's natural variant, known as in HFE2A;, features a modification of the amino acid from C to W at position 321.
+The protein's natural variant, known as in allele MICB*001;, features a modification of the amino acid from G to E at position 39.
+The protein's natural variant, known as in allele MICB*011;, features a modification of the amino acid from P to H at position 68.
+The protein's natural variant, known as in allele MICB*001, allele MICB*002, allele MICB*003, allele MICB*005, allele MICB*006, allele MICB*007, allele MICB*008, allele MICB*010, allele MICB*011, allele MICB*012, allele MICB*013, allele MICB*014, allele MICB*015, allele MICB*016, allele MICB*018, allele MICB*019 and allele MICB*022;, features a modification of the amino acid from N to D at position 75.
+The protein's natural variant, known as in allele MICB*002, allele MICB*007, allele MICB*008, allele MICB*014, allele MICB*015, allele MICB*016, allele MICB*019 and allele MICB*022;, features a modification of the amino acid from K to E at position 80.
+The protein's natural variant, known as in allele MICB*022;, features a modification of the amino acid from D to G at position 88.
+The protein's natural variant, known as in allele MICB*012;, features a modification of the amino acid from D to G at position 105.
+The protein's natural variant, known as in allele MICB*008;, features a modification of the amino acid from I to M at position 121.
+The protein's natural variant, known as in allele MICB*002, allele MICB*007, allele MICB*008, allele MICB*014, allele MICB*015, allele MICB*018, allele MICB*020 and allele MICB*022;, features a modification of the amino acid from D to N at position 136.
+The protein's natural variant, known as in allele MICB*003;, features a modification of the amino acid from T to I at position 212.
+The protein's natural variant, known as in allele MICB*006 and allele MICB*015;, features a modification of the amino acid from E to K at position 215.
+The protein's natural variant, known as in allele MICB*007;, features a modification of the amino acid from R to K at position 279.
+The protein's natural variant, known as in allele MICB*013, allele MICB*014, allele MICB*015 and allele MICB*016;, features a modification of the amino acid from G to S at position 291.
+The protein's natural variant, known as in allele MICB*001, allele MICB*016, allele MICB*018, allele MICB*019, allele MICB*020 and allele MICB*022;, features a modification of the amino acid from A to V at position 300.
+The protein's natural variant, known as in allele MICB*001, allele MICB*002, allele MICB*005, allele MICB*006, allele MICB*007, allele MICB*008, allele MICB*012, allele MICB*013, allele MICB*014, allele MICB*015, allele MICB*016, allele MICB*018, allele MICB*019, allele MICB*020 and allele MICB*022;, features a modification of the amino acid from T to A at position 383.
+The protein's natural variant, known as probable disease-associated variant found in a patient with obsessive-compulsive disorder; decreased levels of mature protein; decreased localization to the cell membrane surface expression; decreased function in synaptogenesis, features a modification of the amino acid from N to I at position 400.
+The protein's natural variant, known as probable disease-associated variant found in a patient with obsessive-compulsive disorder; decreased levels of mature protein; decreased localization to the cell membrane surface expression; decreased function in synaptogenesis;, features a modification of the amino acid from T to S at position 418.
+The protein's natural variant, known as in TTM; unknown pathological significance; does not affect synaptogenesis;, features a modification of the amino acid from R to K at position 584.
+The protein's natural variant, known as in TTM; unknown pathological significance; does not affect synaptogenesis;, features a modification of the amino acid from S to G at position 593.
+The protein's natural variant, known as in T41 mutant, features a modification of the amino acid from Y to D at position 282.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from N to S at position 149.
+The protein's natural variant, known as in HPE11; benign variant;, features a modification of the amino acid from T to S at position 684.
+The protein's natural variant, known as in HPE11;, features a modification of the amino acid from P to A at position 689.
+The protein's natural variant, known as in HPE11;, features a modification of the amino acid from V to M at position 691.
+The protein's natural variant, known as in HPE11;, features a modification of the amino acid from V to E at position 780.
+The protein's natural variant, known as in HPE11;, features a modification of the amino acid from T to A at position 790.
+The protein's natural variant, known as in HPE11;, features a modification of the amino acid from S to R at position 940.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from P to R at position 88.
+The protein's natural variant, known as may be associated with increased risk for febrile seizures; decreased zinc transport; decreased localization to synaptic vesicles;, features a modification of the amino acid from R to C at position 298.
+The natural variant of this protein is characterized by an amino acid alteration from A to E at position 125.
+The protein's natural variant, known as in SPGF79; severely decreased protein abundance in patient sperm, features a modification of the amino acid from I to F at position 413.
+The protein's natural variant, known as in SPGF79; no protein detected in patient sperm; a knockin mouse model recapitulates the phenotype of male infertility, features a modification of the amino acid from H to R at position 715.
+The protein's natural variant, known as in allele NKG2-C*02;, features a modification of the amino acid from N to S at position 2.
+The protein's natural variant, known as in allele NKG2-C*02;, features a modification of the amino acid from F to S at position 102.
+The natural variant of this protein is characterized by an amino acid alteration from K to E at position 1207.
+The protein's natural variant, known as in METHB-CYB5R3; type 1; 62% of activity;, features a modification of the amino acid from R to Q at position 58.
+The protein's natural variant, known as in METHB-CYB5R3; type 1;, features a modification of the amino acid from L to P at position 73.
+The protein's natural variant, known as in METHB-CYB5R3; type 1; 77% of activity;, features a modification of the amino acid from V to M at position 106.
+The protein's natural variant, known as in METHB-CYB5R3; type 2; Hiroshima; decreased NADH-cytochrome b5 reductase activity; highly increased Km for NADH and decreased Kcat;, features a modification of the amino acid from S to P at position 128.
+The protein's natural variant, known as in METHB-CYB5R3;, features a modification of the amino acid from L to P at position 149.
+The protein's natural variant, known as in METHB-CYB5R3; type 1;, features a modification of the amino acid from A to V at position 179.
+The protein's natural variant, known as in METHB-CYB5R3; type 2;, features a modification of the amino acid from C to R at position 204.
+The protein's natural variant, known as in METHB-CYB5R3; type 1; reduced protein stability; no effect on NADH-cytochrome b5 reductase activity;, features a modification of the amino acid from C to Y at position 204.
+The protein's natural variant, known as in METHB-CYB5R3; type 1; retains approximately 58% of residual NADH-cytochrome b5 reductase activity;, features a modification of the amino acid from G to D at position 292.
+The protein's natural variant, known as in strain: ATCC 96044 / SRRC 1273 / AF13, features a modification of the amino acid from P to L at position 423.
+The protein's natural variant, known as in strain: ATCC 96044 / SRRC 1273 / AF13, features a modification of the amino acid from D to H at position 517.
+The protein's natural variant, known as in strain: cv. Sorbo, features a modification of the amino acid from S to I at position 10.
+The protein's natural variant, known as in strain: cv. Bl-0, cv. Di-G, cv. Ema-1, cv. Ka-0, cv. Landsberg erecta, cv. Lip-0, cv. No-0, cv. Petergof, cv. Sei-0, cv. Sorbo, cv. Tsu-1, cv. Wl-0 and cv.Pla-0, features a modification of the amino acid from R to P at position 17.
+The protein's natural variant, known as in strain: cv. Sorbo, features a modification of the amino acid from G to A at position 24.
+The protein's natural variant, known as in strain: cv. Sorbo, features a modification of the amino acid from F to L at position 46.
+The protein's natural variant, known as in strain: cv. Ema-1, features a modification of the amino acid from F to S at position 46.
+The protein's natural variant, known as in strain: cv. Bl-0, cv. Di-G, cv. Landsberg erecta and cv. Petergof, features a modification of the amino acid from M to V at position 68.
+The protein's natural variant, known as in strain: cv. Ka-0, cv. Lip-0, cv. No-0, cv. Sei-0, cv. Tsu-1 and cv. Wl-0, features a modification of the amino acid from V to A at position 156.
+The protein's natural variant, known as in strain: cv. Bl-0, cv. Di-G, cv. Ka-0, cv. Landsberg erecta, cv. Lip-0, cv. No-0, cv. Petergof, cv. Sei-0, cv. Tsu-1 and cv. Wl-0, features a modification of the amino acid from I to L at position 241.
+The protein's natural variant, known as in TRPS567C; reduced activity, thermolabile, features a modification of the amino acid from T to R at position 60.
+The protein's natural variant, known as in TRPS10330; reduced activity, features a modification of the amino acid from L to F at position 91.
+The protein's natural variant, known as in TRPS9969; no effect in activity, features a modification of the amino acid from D to E at position 112.
+The protein's natural variant, known as in TRPS9969; reduced activity, features a modification of the amino acid from P to S at position 129.
+The protein's natural variant, known as in TRPS42C; reduced activity, features a modification of the amino acid from A to E at position 133.
+The protein's natural variant, known as in TRPS271C; activity largely reduced, features a modification of the amino acid from M to I at position 196.
+The protein's natural variant, known as in TRPS4040; reduced activity, features a modification of the amino acid from G to S at position 329.
+The protein's natural variant, known as decreases phosphorylation at Ser-16; abolishes cardioprotective effects;, features a modification of the amino acid from P to L at position 20.
+The natural variant of this protein is characterized by an amino acid alteration from S to G at position 38.
+The protein's natural variant, known as in CDG1H;, features a modification of the amino acid from T to P at position 47.
+The protein's natural variant, known as in CDG1H;, features a modification of the amino acid from G to D at position 275.
+The protein's natural variant, known as in MDDGA10; unknown pathological significance; loss of binding activity of alpha-dystroglycan (DAG1) for the ligand laminin in fibroblasts from patients; loss of alpha-dystroglycan functional glycosylation in fibroblasts from patients; does not affect Golgi apparatus localization;, features a modification of the amino acid from G to R at position 333.
+The protein's natural variant, known as in MDDGA10; abolishes xylosyltransferase activity;, features a modification of the amino acid from Y to C at position 339.
+The protein's natural variant, known as in MDDGA10; abolishes xylosyltransferase activity;, features a modification of the amino acid from R to L at position 340.
+The protein's natural variant, known as in HNSCC, features a modification of the amino acid from A to D at position 335.
+The protein's natural variant, known as in HNSCC, features a modification of the amino acid from C to S at position 358.
+The protein's natural variant, known as in HNSCC, features a modification of the amino acid from N to S at position 359.
+The protein's natural variant, known as in MRXS14;, features a modification of the amino acid from Y to D at position 160.
+The protein's natural variant, known as in LIKNS; causes reduced expression of the mutant protein; hypoglycosylated; does not localize properly at the plasma membrane; small residual activity;, features a modification of the amino acid from G to R at position 305.
+The protein's natural variant, known as in LIKNS; unknown pathological significance, features a modification of the amino acid from G to E at position 313.
+The protein's natural variant, known as in a gastric adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from A to V at position 89.
+The protein's natural variant, known as in a lung neuroendocrine carcinoma sample; somatic mutation, features a modification of the amino acid from H to Y at position 288.
+The protein's natural variant, known as in SPGF21; no effect on protein expression; unknown pathological significance;, features a modification of the amino acid from G to D at position 928.
+The protein's natural variant, known as in a breast carcinoma sample; somatic mutation; reduced ability to induce pyroptosis, features a modification of the amino acid from D to Y at position 14.
+The protein's natural variant, known as in a colon adenocarcinoma sample; somatic mutation; reduced ability to induce pyroptosis, features a modification of the amino acid from D to V at position 18.
+The protein's natural variant, known as in a colon adenocarcinoma sample; somatic mutation; reduced ability to induce pyroptosis, features a modification of the amino acid from N to D at position 24.
+The protein's natural variant, known as in a lung cancer adenocarcinoma sample; somatic mutation; reduced ability to induce pyroptosis, features a modification of the amino acid from W to C at position 44.
+The protein's natural variant, known as in an uterine corpus endometrioid carcinoma sample; somatic mutation; reduced ability to induce pyroptosis, features a modification of the amino acid from R to I at position 48.
+The protein's natural variant, known as in an uterine corpus endometrioid carcinoma sample; somatic mutation; reduced ability to induce pyroptosis, features a modification of the amino acid from I to T at position 137.
+The protein's natural variant, known as in an uterine corpus endometrioid carcinoma sample; somatic mutation; reduced ability to induce pyroptosis, features a modification of the amino acid from G to E at position 199.
+The protein's natural variant, known as in a melanoma sample; somatic mutation; reduced ability to induce pyroptosis, features a modification of the amino acid from P to L at position 212.
+The protein's natural variant, known as in a lung cancer adenocarcinoma sample; somatic mutation; reduced ability to induce pyroptosis, features a modification of the amino acid from I to N at position 217.
+The protein's natural variant, known as in RP62; results in a complete loss of kinase activity compared to wild-type;, features a modification of the amino acid from G to S at position 13.
+The protein's natural variant, known as in RP62;, features a modification of the amino acid from G to R at position 27.
+The protein's natural variant, known as in RP62; results in a complete loss of kinase activity compared to wild-type;, features a modification of the amino acid from N to H at position 130.
+The protein's natural variant, known as in RP62;, features a modification of the amino acid from R to H at position 166.
+The protein's natural variant, known as in RP62;, features a modification of the amino acid from I to T at position 181.
+The protein's natural variant, known as in a breast infiltrating ductal carcinoma sample; somatic mutation, features a modification of the amino acid from R to P at position 272.
+The protein's natural variant, known as in LqqIT1', features a modification of the amino acid from D to E at position 33.
+The protein's natural variant, known as in strain: 1479, features a modification of the amino acid from V to A at position 48.
+The protein's natural variant, known as in strain: 1479, features a modification of the amino acid from K to R at position 142.
+The protein's natural variant, known as in strain: 1479, features a modification of the amino acid from A to P at position 165.
+The protein's natural variant, known as in strain: 1479, features a modification of the amino acid from A to R at position 190.
+The protein's natural variant, known as in strain: 1479, features a modification of the amino acid from V to A at position 203.
+The protein's natural variant, known as in strain: 1479, features a modification of the amino acid from D to A at position 227.
+The protein's natural variant, known as in strain: 1479, features a modification of the amino acid from A to AKAAAEAKAKA at position 232.
+The protein's natural variant, known as in strain: 1479, features a modification of the amino acid from T to A at position 234.
+The protein's natural variant, known as in strain: 1479, features a modification of the amino acid from L to F at position 249.
+The protein's natural variant, known as in strain: 1479, features a modification of the amino acid from I to V at position 254.
+The protein's natural variant, known as in strain: 1479, features a modification of the amino acid from N to S at position 306.
+The protein's natural variant, known as in strain: 1479, features a modification of the amino acid from T to A at position 323.
+The protein's natural variant, known as in strain: 1479, features a modification of the amino acid from S to P at position 333.
+The protein's natural variant, known as in STLS;, features a modification of the amino acid from G to R at position 697.
+The protein's natural variant, known as in HSN1D; shows no significant changes in GTPase activity and no changes in endoplasmic reticulum morphology;, features a modification of the amino acid from E to Q at position 66.
+The protein's natural variant, known as in SPG3;, features a modification of the amino acid from R to Q at position 118.
+The protein's natural variant, known as in SPG3, features a modification of the amino acid from Q to E at position 154.
+The protein's natural variant, known as in SPG3;, features a modification of the amino acid from L to W at position 157.
+The protein's natural variant, known as in SPG3; affects endoplasmic reticulum and Golgi morphology, features a modification of the amino acid from A to P at position 161.
+The protein's natural variant, known as in a patient with hereditary spastic paraplegia; unknown pathological significance; no effect on homodimerization and GTPase activity;, features a modification of the amino acid from Y to C at position 196.
+The protein's natural variant, known as in SPG3; abolishes homodimerization and GTPase activity and alters endoplasmic reticulum morphology;, features a modification of the amino acid from R to Q at position 217.
+The protein's natural variant, known as in SPG3; affects endoplasmic reticulum and Golgi morphology;, features a modification of the amino acid from R to C at position 239.
+The protein's natural variant, known as in SPG3, features a modification of the amino acid from H to P at position 247.
+The protein's natural variant, known as in SPG3;, features a modification of the amino acid from V to I at position 253.
+The protein's natural variant, known as in SPG3;, features a modification of the amino acid from H to R at position 258.
+The protein's natural variant, known as in SPG3;, features a modification of the amino acid from S to Y at position 259.
+The protein's natural variant, known as in HSN1D; the mutant protein has decreased GTPase activity compared to wild-type and causes disruption of endoplasmic reticulum network morphology;, features a modification of the amino acid from N to K at position 355.
+The protein's natural variant, known as in SPG3;, features a modification of the amino acid from M to V at position 408.
+The protein's natural variant, known as in SPG3, features a modification of the amino acid from F to V at position 413.
+The protein's natural variant, known as in SPG3;, features a modification of the amino acid from R to Q at position 415.
+The protein's natural variant, known as in SPG3;, features a modification of the amino acid from R to W at position 415.
+The protein's natural variant, known as in SPG3;, features a modification of the amino acid from R to C at position 416.
+The protein's natural variant, known as in SPG3, features a modification of the amino acid from N to T at position 440.
+The protein's natural variant, known as in SPG3; affects endoplasmic reticulum and Golgi morphology;, features a modification of the amino acid from R to W at position 495.
+The protein's natural variant, known as in strain: W, features a modification of the amino acid from D to V at position 5.
+The protein's natural variant, known as in strain: W, features a modification of the amino acid from L to I at position 311.
+The protein's natural variant, known as in strain: W, features a modification of the amino acid from I to T at position 315.
+The protein's natural variant, known as in strain: cv. Serrana and cv. Texas Early White, features a modification of the amino acid from S to L at position 168.
+The protein's natural variant, known as in strain: cv. Serrana and cv. Texas Early White, features a modification of the amino acid from S to P at position 170.
+The protein's natural variant, known as in strain: cv. Texas Early White, features a modification of the amino acid from H to Y at position 194.
+The protein's natural variant, known as in CTRCT30; the mutation increases the proteasome activity in transfected cells; causes also a severe kinetic defect in vimentin assembly both in vitro and in vivo;, features a modification of the amino acid from E to K at position 151.
+The protein's natural variant, known as in CTRCT30; unknown pathological significance;, features a modification of the amino acid from Q to R at position 208.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from F to L at position 117.
+The protein's natural variant, known as in a lung cancer cell line; reduced interaction with TP53, loss of TP53 activation and loss of proapoptotic activity, features a modification of the amino acid from I to V at position 92.
+The protein's natural variant, known as in a lung cancer cell line; no effect on proapoptotic activity, features a modification of the amino acid from EPT to DLS at position 99.
+The protein's natural variant, known as in a lung cancer cell line; no effect on proapoptotic activity;, features a modification of the amino acid from G to S at position 209.
+The protein's natural variant, known as in CIPA; aberrantly processed; shows diminished autophosphorylation in neuronal cells, features a modification of the amino acid from L to P at position 93.
+The protein's natural variant, known as in an ovarian serous carcinoma sample; somatic mutation;, features a modification of the amino acid from A to V at position 107.
+The protein's natural variant, known as in CIPA, features a modification of the amino acid from A to D at position 110.
+The protein's natural variant, known as in CIPA; aberrantly processed; shows diminished autophosphorylation in neuronal cells;, features a modification of the amino acid from L to P at position 213.
+The protein's natural variant, known as in CIPA;, features a modification of the amino acid from Y to C at position 359.
+The protein's natural variant, known as in CIPA;, features a modification of the amino acid from E to K at position 492.
+The protein's natural variant, known as in CIPA; following transfection in neuroblastoma cells and NGF treatment, small decrease in the percentage of cells differentiated into neuronal phenotype, but in differentiated cells, the average neurite length is comparable to wild-type; no effect on N-glycosylation, subcellular location, nor on basal and NGF-induced autophosphorylation; loss of NGF-stimulated calcium flux;, features a modification of the amino acid from G to E at position 517.
+The protein's natural variant, known as in CIPA; no effect on N-glycosylation, nor on subcellular location; reduced basal autophosphorylation and complete loss of NGF-induced autophosphorylation; loss of NGF-stimulated calcium flux, features a modification of the amino acid from G to E at position 522.
+The protein's natural variant, known as in CIPA; processed as wild-type but shows significantly diminished autophosphorylation in both neuronal and non-neuronal cells;, features a modification of the amino acid from G to R at position 522.
+The protein's natural variant, known as in CIPA, features a modification of the amino acid from I to S at position 572.
+The protein's natural variant, known as in CIPA; loss of function; processed as wild-type but shows significantly diminished autophosphorylation in both neuronal and non-neuronal cells;, features a modification of the amino acid from G to R at position 577.
+The protein's natural variant, known as in CIPA;, features a modification of the amino acid from M to V at position 587.
+The protein's natural variant, known as in CIPA; abolishes autophosphorylation, features a modification of the amino acid from D to N at position 596.
+The protein's natural variant, known as in CIPA;, features a modification of the amino acid from R to Q at position 649.
+The protein's natural variant, known as in CIPA; processed as wild-type but shows significantly diminished autophosphorylation in both neuronal and non-neuronal cells;, features a modification of the amino acid from R to W at position 649.
+The protein's natural variant, known as in CIPA; processed as wild-type but shows significantly diminished autophosphorylation in both neuronal and non-neuronal cells;, features a modification of the amino acid from R to C at position 654.
+The protein's natural variant, known as in CIPA; following transfection in neuroblastoma cells and NGF treatment, loss of differentiation into neuronal phenotype; partially decreased N-glycosylation; reduced expression at the plasma membrane; reduced basal autophosphorylation and complete loss of NGF-induced autophosphorylation; loss of NGF-stimulated calcium flux, features a modification of the amino acid from L to P at position 657.
+The protein's natural variant, known as in CIPA; might impair the function of the enzyme without compromising autophosphorylation;, features a modification of the amino acid from D to Y at position 674.
+The protein's natural variant, known as in CIPA;, features a modification of the amino acid from P to L at position 695.
+The protein's natural variant, known as in CIPA; partially decreased N-glycosylation; reduced expression at the plasma membrane; reduced basal autophosphorylation and complete loss of NGF-induced autophosphorylation; loss of NGF-stimulated calcium flux, features a modification of the amino acid from I to T at position 699.
+The protein's natural variant, known as in CIPA, features a modification of the amino acid from L to P at position 700.
+The protein's natural variant, known as in CIPA; processed as wild-type but shows significantly diminished autophosphorylation in both neuronal and non-neuronal cells;, features a modification of the amino acid from G to S at position 714.
+The protein's natural variant, known as in CIPA, features a modification of the amino acid from L to R at position 717.
+The protein's natural variant, known as in CIPA; unknown pathological significance; following transfection in neuroblastoma cells and NGF treatment, no effect on neurite outgrowth, nor neurite length; no effect on N-glycosylation, subcellular location, basal and NGF-induced autophosphorylation, nor on NGF-stimulated calcium flux, features a modification of the amino acid from C to S at position 752.
+The protein's natural variant, known as in CIPA; following transfection in neuroblastoma cells and NGF treatment, decreased percentage of cells differentiated into neuronal phenotype and reduced neurite length compared with wild-type; slightly decreased N-glycosylation; reduced expression at the plasma membrane; reduced basal and NGF-induced autophosphorylation; small reduction in NGF-stimulated calcium flux, features a modification of the amino acid from C to S at position 763.
+The protein's natural variant, known as in CIPA; partially decreased N-glycosylation; reduced expression at the plasma membrane; reduced basal autophosphorylation and complete loss of NGF-induced autophosphorylation; loss of NGF-stimulated calcium flux;, features a modification of the amino acid from R to C at position 771.
+The protein's natural variant, known as in CIPA; loss of function;, features a modification of the amino acid from R to P at position 780.
+The natural variant of this protein is characterized by an amino acid alteration from G to QQQQQQQQQQQQR at position 306.
+The protein's natural variant, known as in strain: ATCCVR-358 / Fuller / CIP 107027, features a modification of the amino acid from F to FSFSP at position 4.
+The natural variant of this protein is characterized by an amino acid alteration from T to P at position 104.
+The natural variant of this protein is characterized by an amino acid alteration from N to I at position 106.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from P to A at position 100.
+The protein's natural variant, known as in CDCBM7;, features a modification of the amino acid from L to P at position 117.
+The protein's natural variant, known as in CDCBM7; affects microtubules assembly;, features a modification of the amino acid from S to P at position 172.
+The protein's natural variant, known as in CDCBM7, features a modification of the amino acid from I to T at position 210.
+The protein's natural variant, known as in CDCBM7;, features a modification of the amino acid from L to P at position 228.
+The protein's natural variant, known as in CDCBM7; decreased tubulin heterodimer formation; decreased ability to incorporate into the cytoskeleton; no effect on microtubules disintegration; increased ability to repolymerize;, features a modification of the amino acid from C to F at position 239.
+The protein's natural variant, known as in CDCBM7;, features a modification of the amino acid from N to S at position 256.
+The protein's natural variant, known as in CDCBM7; affects microtubules assembly;, features a modification of the amino acid from F to L at position 265.
+The protein's natural variant, known as in CDCBM7, features a modification of the amino acid from T to M at position 312.
+The protein's natural variant, known as found in a patient with cerebellar ataxia intellectual disability and dysequilibrium syndrome; unknown pathological significance; no effect on protein folding; no effect on tubulin heterodimer formation; no effect on integration into the microtubule lattice; no effect on cytoskeleton subcellular location, features a modification of the amino acid from R to Q at position 390.
+The protein's natural variant, known as in CDCBM7;, features a modification of the amino acid from D to N at position 417.
+The protein's natural variant, known as in CDCBM7; decreased protein expression; decreased tubulin heterodimer formation; no effect on integration into the microtubule lattice; no effect on microtubule cytoskeleton subcellular location; loss of axon guidance;, features a modification of the amino acid from E to K at position 421.
+The protein's natural variant, known as in a colon adenocarcinoma sample;, features a modification of the amino acid from P to H at position 63.
+The protein's natural variant, known as in a breast cancer sample; invasive ductal;, features a modification of the amino acid from G to R at position 325.
+The protein's natural variant, known as in a non-Hodgkin lymphoma sample;, features a modification of the amino acid from V to E at position 444.
+The protein's natural variant, known as in plasmid pGTK3, features a modification of the amino acid from N to I at position 182.
+The protein's natural variant, known as in DEE9, features a modification of the amino acid from L to P at position 25.
+The protein's natural variant, known as in DEE9, features a modification of the amino acid from V to G at position 72.
+The protein's natural variant, known as in DEE9;, features a modification of the amino acid from L to R at position 81.
+The protein's natural variant, known as in DEE9; disease features overlapping with Dravet syndrome;, features a modification of the amino acid from D to N at position 121.
+The protein's natural variant, known as in DEE9, features a modification of the amino acid from A to ASEA at position 141.
+The protein's natural variant, known as in DEE9;, features a modification of the amino acid from T to R at position 146.
+The protein's natural variant, known as in DEE9, features a modification of the amino acid from A to T at position 153.
+The protein's natural variant, known as in DEE9, features a modification of the amino acid from L to R at position 190.
+The protein's natural variant, known as in DEE9;, features a modification of the amino acid from V to L at position 191.
+The protein's natural variant, known as in DEE9; disease features overlapping with Dravet syndrome, features a modification of the amino acid from E to Q at position 199.
+The protein's natural variant, known as in DEE9; disease features overlapping with Dravet syndrome; associated with Cys-206, features a modification of the amino acid from H to P at position 203.
+The protein's natural variant, known as in DEE9; disease features overlapping with Dravet syndrome; associated with Pro-203;, features a modification of the amino acid from F to C at position 206.
+The protein's natural variant, known as in DEE9, features a modification of the amino acid from F to Y at position 206.
+The protein's natural variant, known as in DEE9; unknown pathological significance, features a modification of the amino acid from D to N at position 230.
+The protein's natural variant, known as in DEE9;, features a modification of the amino acid from N to S at position 232.
+The protein's natural variant, known as in DEE9;, features a modification of the amino acid from N to S at position 234.
+The protein's natural variant, known as in DEE9;, features a modification of the amino acid from P to L at position 236.
+The protein's natural variant, known as in DEE9, features a modification of the amino acid from P to S at position 236.
+The protein's natural variant, known as in DEE9, features a modification of the amino acid from E to D at position 249.
+The protein's natural variant, known as in DEE9;, features a modification of the amino acid from A to D at position 262.
+The protein's natural variant, known as in DEE9, features a modification of the amino acid from S to P at position 276.
+The protein's natural variant, known as in DEE9; disease features overlapping with Dravet syndrome;, features a modification of the amino acid from N to S at position 340.
+The protein's natural variant, known as in DEE9, features a modification of the amino acid from D to E at position 341.
+The protein's natural variant, known as in DEE9, features a modification of the amino acid from P to R at position 344.
+The protein's natural variant, known as in DEE9, features a modification of the amino acid from D to E at position 377.
+The protein's natural variant, known as in DEE9; disease features overlapping with Dravet syndrome;, features a modification of the amino acid from D to H at position 377.
+The protein's natural variant, known as in DEE9; disease features overlapping with Dravet syndrome, features a modification of the amino acid from T to I at position 404.
+The protein's natural variant, known as in DEE9; disease features overlapping with Dravet syndrome, features a modification of the amino acid from E to Q at position 414.
+The protein's natural variant, known as in DEE9, features a modification of the amino acid from L to P at position 433.
+The protein's natural variant, known as in DEE9;, features a modification of the amino acid from V to E at position 441.
+The protein's natural variant, known as probable disease-associated variant found in a patient with drug-resistant epilepsy, features a modification of the amino acid from N to H at position 447.
+The protein's natural variant, known as in DEE9, features a modification of the amino acid from G to R at position 513.
+The protein's natural variant, known as in DEE9; disease features overlapping with Dravet syndrome, features a modification of the amino acid from L to P at position 543.
+The protein's natural variant, known as in DEE9;, features a modification of the amino acid from N to K at position 557.
+The protein's natural variant, known as in DEE9;, features a modification of the amino acid from P to R at position 561.
+The protein's natural variant, known as in DEE9;, features a modification of the amino acid from P to L at position 567.
+The protein's natural variant, known as in DEE9, features a modification of the amino acid from D to N at position 618.
+The protein's natural variant, known as in DEE9;, features a modification of the amino acid from V to M at position 642.
+The protein's natural variant, known as in a glioblastoma multiforme sample; somatic mutation, features a modification of the amino acid from A to T at position 343.
+The protein's natural variant, known as in UW-dbr, features a modification of the amino acid from D to N at position 153.
+The protein's natural variant, known as in UW-dbr, features a modification of the amino acid from S to P at position 435.
+The protein's natural variant, known as in EJM10; unknown pathological significance;, features a modification of the amino acid from I to L at position 102.
+The protein's natural variant, known as in a renal clear cell carcinoma sample; somatic mutation, features a modification of the amino acid from F to Y at position 115.
+The protein's natural variant, known as in EJM10; impairs mitosis, cell-cycle exit and radial neuroblast migration, while promoting apoptosis, when tested in a heterologous system, features a modification of the amino acid from K to E at position 220.
+The protein's natural variant, known as in ECO; significantly impairs kinase activity; decreased localization at the ciliary tips; impaired ciliogenesis; results in abnormally elongated cilia; impairs mitosis, cell-cycle exit and radial neuroblast migration, while promoting apoptosis, when tested in a heterologous system; loss of nuclear localization;, features a modification of the amino acid from R to Q at position 272.
+The protein's natural variant, known as in EJM10; impairs mitosis, cell-cycle exit and radial neuroblast migration, while promoting apoptosis, when tested in a heterologous system;, features a modification of the amino acid from K to T at position 305.
+The protein's natural variant, known as in EJM10; unknown pathological significance; impairs mitosis, cell-cycle exit and radial neuroblast migration, while promoting apoptosis, when tested in a heterologous system;, features a modification of the amino acid from A to T at position 615.
+The protein's natural variant, known as in clones PSCI267, PSCI268, PSCI270 and PSCI272, features a modification of the amino acid from FS to LA at position 7.
+The protein's natural variant, known as in clones PSCI268, PSCI270 and PSCI272, features a modification of the amino acid from V to I at position 11.
+The protein's natural variant, known as in clones PSCI268, PSCI270 and PSCI272, features a modification of the amino acid from F to S at position 19.
+The natural variant of this protein is characterized by an amino acid alteration from S to G at position 96.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from A to S at position 170.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from D to Y at position 179.
+The protein's natural variant, known as in MW145; suppresses a rimM deletion, features a modification of the amino acid from H to Y at position 83.
+The protein's natural variant, known as in GSL;, features a modification of the amino acid from Q to R at position 49.
+The protein's natural variant, known as in GSL;, features a modification of the amino acid from S to Y at position 51.
+The protein's natural variant, known as in GSL;, features a modification of the amino acid from W to R at position 65.
+The protein's natural variant, known as in GSL;, features a modification of the amino acid from S to L at position 90.
+The protein's natural variant, known as in GSL;, features a modification of the amino acid from V to M at position 132.
+The protein's natural variant, known as in GSL;, features a modification of the amino acid from L to P at position 236.
+The protein's natural variant, known as in GSL; small amount of activity;, features a modification of the amino acid from Y to N at position 249.
+The protein's natural variant, known as in GSL; loss of activity;, features a modification of the amino acid from Y to C at position 395.
+The protein's natural variant, known as in GSL;, features a modification of the amino acid from M to T at position 406.
+The protein's natural variant, known as in GSL;, features a modification of the amino acid from G to S at position 439.
+The protein's natural variant, known as in GSL;, features a modification of the amino acid from F to V at position 440.
+The protein's natural variant, known as in GSL;, features a modification of the amino acid from K to E at position 453.
+The protein's natural variant, known as in MC2DN2; reduces but does not prevent interaction with HSC20 or SDHB;, features a modification of the amino acid from R to P at position 55.
+The protein's natural variant, known as in MC2DN2;, features a modification of the amino acid from G to E at position 57.
+The protein's natural variant, known as in MC2DN2; abolishes binding to the iron-sulfur transfer complex formed by HSC20, HSPA9 and ICSU; prevents interaction with SDHB; leads to rapid degradation of SDHAF1;, features a modification of the amino acid from G to R at position 57.
+The protein's natural variant, known as in LGSS, features a modification of the amino acid from W to C at position 31.
+The protein's natural variant, known as in LGSS;, features a modification of the amino acid from V to D at position 44.
+The protein's natural variant, known as in CMS3B; results in reduced gating efficiency; slows opening of the channel; decreases probability that the channel will open in response to ACh, features a modification of the amino acid from L to P at position 42.
+The protein's natural variant, known as in CMS3B; prevents expression of the AChR on the cell surface; is a null mutation;, features a modification of the amino acid from I to K at position 79.
+The protein's natural variant, known as in CMS3B; reduced adult and fetal AChR expression and a reduced probability of both adult and fetal AChR being in the open state;, features a modification of the amino acid from E to K at position 80.
+The protein's natural variant, known as in LMPS;, features a modification of the amino acid from F to L at position 95.
+The protein's natural variant, known as has no appreciable kinetic effects; allows for robust AChR expression;, features a modification of the amino acid from V to L at position 114.
+The protein's natural variant, known as in CMS3B; burst duration was decreased and disassociation of ACh was increased resulting in brief channel opening episodes; shows abnormal association with alpha CHRNA1 subunit resulting in a decreased number of fully assembled AChRs;, features a modification of the amino acid from P to Q at position 271.
+The protein's natural variant, known as in CMS3A; delayed closure of AchR ion channels, increasing the propensity for open-channel block, as well as a reduced rate of channel opening;, features a modification of the amino acid from S to F at position 289.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from D to E at position 398.
+The protein's natural variant, known as in CMS3C; results in reduced expression of the AChR at the cell surface; impairs normal clustering of the AChR channel with RAPSN;, features a modification of the amino acid from E to K at position 402.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from E to Q at position 168.
+The protein's natural variant, known as in strain: MT103, features a modification of the amino acid from A to V at position 256.
+The protein's natural variant, known as in PCC;, features a modification of the amino acid from W to S at position 53.
+The protein's natural variant, known as in PCC; localized diffusely within the cytoplasm;, features a modification of the amino acid from D to N at position 70.
+The protein's natural variant, known as in PCC;, features a modification of the amino acid from G to R at position 73.
+The protein's natural variant, known as in PCC;, features a modification of the amino acid from V to M at position 90.
+The protein's natural variant, known as in PCC; localized diffusely within the cytoplasm;, features a modification of the amino acid from R to W at position 94.
+The protein's natural variant, known as in PCC; localized diffusely within the cytoplasm;, features a modification of the amino acid from C to R at position 140.
+The protein's natural variant, known as in PCC; localized diffusely within the cytoplasm;, features a modification of the amino acid from C to Y at position 140.
+The protein's natural variant, known as in strain: CLIB 219, features a modification of the amino acid from Q to K at position 2.
+The protein's natural variant, known as in strain: CLIB 219, CLIB 410, CLIB 413, CLIB 630 haplotype Ha1, K1, YIIc12 haplotype Ha2 and CLIB 382, features a modification of the amino acid from M to T at position 42.
+The protein's natural variant, known as in strain: CLIB 630, features a modification of the amino acid from V to I at position 215.
+The protein's natural variant, known as in strain: 3976 / Serogroup B / Serotype NT, features a modification of the amino acid from ARH to VGC at position 4.
+The protein's natural variant, known as in strain: 3976 / Serogroup B / Serotype NT, features a modification of the amino acid from F to L at position 31.
+The protein's natural variant, known as in strain: BT490 / Serogroup B / Serotype 15, 952 / Serogroup B / Serotype NT and 3976 / Serogroup B / Serotype NT, features a modification of the amino acid from V to A at position 36.
+The protein's natural variant, known as in strain: 3976 / Serogroup B / Serotype NT, features a modification of the amino acid from Q to R at position 42.
+The protein's natural variant, known as in strain: BT490 / Serogroup B / Serotype 15, 952 / Serogroup B / Serotype NT and 3976 / Serogroup B / Serotype NT, features a modification of the amino acid from Q to R at position 50.
+The protein's natural variant, known as in strain: BT490 / Serogroup B / Serotype 15, 952 / Serogroup B / Serotype NT and 3976 / Serogroup B / Serotype NT, features a modification of the amino acid from S to P at position 68.
+The protein's natural variant, known as in strain: BT490 / Serogroup B / Serotype 15, features a modification of the amino acid from G to C at position 69.
+The protein's natural variant, known as in strain: 3976 / Serogroup B / Serotype NT, features a modification of the amino acid from P to S at position 84.
+The protein's natural variant, known as in strain: BT490 / Serogroup B / Serotype 15, 952 / Serogroup B / Serotype NT and 3976 / Serogroup B / Serotype NT, features a modification of the amino acid from I to V at position 96.
+The protein's natural variant, known as in strain: 3976 / Serogroup B / Serotype NT, features a modification of the amino acid from R to H at position 102.
+The protein's natural variant, known as in strain: 952 / Serogroup B / Serotype NT and 3976 / Serogroup B / Serotype NT, features a modification of the amino acid from I to V at position 105.
+The protein's natural variant, known as in strain: BT490 / Serogroup B / Serotype 15, 952 / Serogroup B / Serotype NT and 3976 / Serogroup B / Serotype NT, features a modification of the amino acid from N to T at position 125.
+The protein's natural variant, known as in strain: 3976 / Serogroup B / Serotype NT, features a modification of the amino acid from V to L at position 130.
+The protein's natural variant, known as in strain: 3976 / Serogroup B / Serotype NT, features a modification of the amino acid from R to C at position 135.
+The protein's natural variant, known as in strain: BT490 / Serogroup B / Serotype 15, features a modification of the amino acid from A to T at position 137.
+The protein's natural variant, known as in strain: BT490 / Serogroup B / Serotype 15, features a modification of the amino acid from Q to R at position 147.
+The protein's natural variant, known as in strain: BT490 / Serogroup B / Serotype 15 and 952 / Serogroup B / Serotype NT, features a modification of the amino acid from K to E at position 151.
+The protein's natural variant, known as in strain: BT490 / Serogroup B / Serotype 15, 952 / Serogroup B / Serotype NT and 3976 / Serogroup B / Serotype NT, features a modification of the amino acid from T to N at position 152.
+The protein's natural variant, known as in strain: 952 / Serogroup B / Serotype NT, features a modification of the amino acid from A to T at position 172.
+The protein's natural variant, known as in strain: BT490 / Serogroup B / Serotype 15 and 3976 / Serogroup B / Serotype NT, features a modification of the amino acid from S to A at position 174.
+The protein's natural variant, known as in strain: 952 / Serogroup B /Serotype NT, features a modification of the amino acid from AECI to ETCV at position 178.
+The protein's natural variant, known as in strain: BT490 / Serogroup B / Serotype 15, 952 / Serogroup B / Serotype NT and 3976 / Serogroup B / Serotype NT, features a modification of the amino acid from I to T at position 188.
+The protein's natural variant, known as in strain: 3976 / Serogroup B / Serotype NT, features a modification of the amino acid from G to C at position 196.
+The protein's natural variant, known as in strain: 952 / Serogroup B / Serotype NT and 3976 / Serogroup B / Serotype NT, features a modification of the amino acid from P to T at position 200.
+The protein's natural variant, known as in strain: 3976 / Serogroup B / Serotype NT, features a modification of the amino acid from A to T at position 206.
+The protein's natural variant, known as in strain: BT490 / Serogroup B / Serotype 15, features a modification of the amino acid from M to V at position 208.
+The protein's natural variant, known as in strain: 3976 / Serogroup B / Serotype NT, features a modification of the amino acid from F to Y at position 220.
+The protein's natural variant, known as in strain: 952 / Serogroup B / Serotype NT and BT490 / Serogroup B / Serotype 15, features a modification of the amino acid from S to R at position 230.
+The protein's natural variant, known as in strain: BT490 / Serogroup B / Serotype 15, 952 / Serogroup B / Serotype NT and 3976 / Serogroup B / Serotype NT, features a modification of the amino acid from T to M at position 231.
+The protein's natural variant, known as in strain: BT490 / Serogroup B / Serotype 15, features a modification of the amino acid from I to V at position 232.
+The protein's natural variant, known as in strain: BT490 / Serogroup B / Serotype 15, features a modification of the amino acid from A to S at position 239.
+The protein's natural variant, known as in strain: 3976 / Serogroup B / Serotype NT, features a modification of the amino acid from A to T at position 239.
+The protein's natural variant, known as in strain: BT490 / Serogroup B / Serotype 15, 952 / Serogroup B / Serotype NT and 3976 / Serogroup B / Serotype NT, features a modification of the amino acid from N to D at position 240.
+The protein's natural variant, known as in strain: BT490 / Serogroup B / Serotype 15 and 3976 / Serogroup B / Serotype NT, features a modification of the amino acid from E to A at position 243.
+The protein's natural variant, known as in strain: 3976 / Serogroup B / Serotype NT, features a modification of the amino acid from V to G at position 245.
+The protein's natural variant, known as in strain: BT490 / Serogroup B / Serotype 15, features a modification of the amino acid from L to V at position 253.
+The protein's natural variant, known as in strain: BT490 / Serogroup B / Serotype 15 and 3976 / Serogroup B / Serotype NT, features a modification of the amino acid from S to A at position 255.
+The protein's natural variant, known as in strain: 3976 / Serogroup B / Serotype NT, features a modification of the amino acid from Q to K at position 261.
+The protein's natural variant, known as in strain: 3976 / Serogroup B / Serotype NT, features a modification of the amino acid from V to A at position 277.
+The protein's natural variant, known as in BCNS; sporadic BCC, features a modification of the amino acid from L to P at position 175.
+The protein's natural variant, known as in BCNS, features a modification of the amino acid from T to P at position 230.
+The protein's natural variant, known as in BCNS, features a modification of the amino acid from F to S at position 376.
+The protein's natural variant, known as in HPE7;, features a modification of the amino acid from A to T at position 393.
+The protein's natural variant, known as in HPE7;, features a modification of the amino acid from A to G at position 443.
+The protein's natural variant, known as in BCNS, features a modification of the amino acid from FL to LR at position 506.
+The protein's natural variant, known as in BCNS; unknown pathological significance, features a modification of the amino acid from G to R at position 509.
+The protein's natural variant, known as in BCNS, features a modification of the amino acid from G to V at position 509.
+The protein's natural variant, known as in BCNS, features a modification of the amino acid from D to Y at position 513.
+The protein's natural variant, known as in HPE7;, features a modification of the amino acid from T to M at position 728.
+The protein's natural variant, known as in HPE7, features a modification of the amino acid from V to G at position 751.
+The protein's natural variant, known as in BCNS, features a modification of the amino acid from I to IPNI at position 815.
+The protein's natural variant, known as in HPE7;, features a modification of the amino acid from S to G at position 827.
+The protein's natural variant, known as in squamous cell carcinoma;, features a modification of the amino acid from V to M at position 829.
+The protein's natural variant, known as in HPE7;, features a modification of the amino acid from V to G at position 908.
+The protein's natural variant, known as in HPE7;, features a modification of the amino acid from T to M at position 1052.
+The protein's natural variant, known as in BCNS, features a modification of the amino acid from G to R at position 1069.
+The protein's natural variant, known as in BCNS, features a modification of the amino acid from V to VV at position 1083.
+The protein's natural variant, known as in BCNS and BCC;, features a modification of the amino acid from R to W at position 1114.
+The protein's natural variant, known as in BCNS;, features a modification of the amino acid from S to P at position 1132.
+The protein's natural variant, known as in BCNS, features a modification of the amino acid from S to Y at position 1132.
+The protein's natural variant, known as in squamous cell carcinoma;, features a modification of the amino acid from E to K at position 1242.
+The protein's natural variant, known as in BCNS; sporadic NBCCS, features a modification of the amino acid from E to D at position 1438.
+The protein's natural variant, known as in MCC2D; has some wild-type residual activity;, features a modification of the amino acid from S to F at position 39.
+The protein's natural variant, known as in MCC2D; unknown pathological significance;, features a modification of the amino acid from G to V at position 68.
+The protein's natural variant, known as in MCC2D; severe and mild form;, features a modification of the amino acid from E to Q at position 99.
+The protein's natural variant, known as in MCC2D;, features a modification of the amino acid from S to F at position 101.
+The protein's natural variant, known as in MCC2D; unknown pathological significance, features a modification of the amino acid from G to R at position 105.
+The protein's natural variant, known as in MCC2D, features a modification of the amino acid from C to F at position 131.
+The protein's natural variant, known as in MCC2D, features a modification of the amino acid from T to I at position 139.
+The protein's natural variant, known as in MCC2D; has some wild-type residual activity, features a modification of the amino acid from Y to N at position 146.
+The protein's natural variant, known as in MCC2D;, features a modification of the amino acid from K to T at position 152.
+The protein's natural variant, known as in MCC2D; mild form;, features a modification of the amino acid from R to Q at position 155.
+The protein's natural variant, known as in MCC2D;, features a modification of the amino acid from R to W at position 155.
+The protein's natural variant, known as in MCC2D; unknown pathological significance, features a modification of the amino acid from N to D at position 163.
+The protein's natural variant, known as in MCC2D;, features a modification of the amino acid from C to R at position 167.
+The protein's natural variant, known as in MCC2D, features a modification of the amino acid from Y to D at position 169.
+The protein's natural variant, known as in MCC2D; severe form;, features a modification of the amino acid from S to L at position 173.
+The protein's natural variant, known as in MCC2D;, features a modification of the amino acid from H to R at position 190.
+The protein's natural variant, known as in MCC2D; produces severely decreased wild-type residual activity;, features a modification of the amino acid from H to Y at position 190.
+The protein's natural variant, known as in MCC2D; mild form;, features a modification of the amino acid from R to C at position 193.
+The protein's natural variant, known as in MCC2D;, features a modification of the amino acid from R to H at position 193.
+The protein's natural variant, known as in MCC2D; unknown pathological significance;, features a modification of the amino acid from I to N at position 200.
+The protein's natural variant, known as in MCC2D;, features a modification of the amino acid from G to A at position 214.
+The protein's natural variant, known as in MCC2D, features a modification of the amino acid from C to W at position 216.
+The protein's natural variant, known as in MCC2D;, features a modification of the amino acid from A to T at position 218.
+The protein's natural variant, known as in MCC2D;, features a modification of the amino acid from A to V at position 218.
+The protein's natural variant, known as in MCC2D;, features a modification of the amino acid from G to E at position 220.
+The protein's natural variant, known as in MCC2D;, features a modification of the amino acid from P to L at position 224.
+The protein's natural variant, known as in MCC2D;, features a modification of the amino acid from N to D at position 230.
+The protein's natural variant, known as in MCC2D, features a modification of the amino acid from G to D at position 237.
+The protein's natural variant, known as in MCC2D, features a modification of the amino acid from H to L at position 266.
+The protein's natural variant, known as in MCC2D; asymptomatic form;, features a modification of the amino acid from R to T at position 268.
+The protein's natural variant, known as in MCC2D;, features a modification of the amino acid from D to Y at position 280.
+The protein's natural variant, known as in MCC2D; has some wild-type residual activity, features a modification of the amino acid from H to R at position 282.
+The protein's natural variant, known as in MCC2D; mild form;, features a modification of the amino acid from P to R at position 310.
+The protein's natural variant, known as in MCC2D;, features a modification of the amino acid from Y to C at position 318.
+The protein's natural variant, known as in MCC2D;, features a modification of the amino acid from G to R at position 319.
+The protein's natural variant, known as in MCC2D; severe form;, features a modification of the amino acid from V to M at position 339.
+The protein's natural variant, known as in MCC2D;, features a modification of the amino acid from D to V at position 340.
+The protein's natural variant, known as in MCC2D; produces severely decreased wild-type residual activity;, features a modification of the amino acid from G to R at position 352.
+The protein's natural variant, known as in MCC2D;, features a modification of the amino acid from L to F at position 355.
+The protein's natural variant, known as in MCC2D, features a modification of the amino acid from V to F at position 375.
+The protein's natural variant, known as in MCC2D; unknown pathological significance;, features a modification of the amino acid from F to V at position 387.
+The protein's natural variant, known as in MCC2D;, features a modification of the amino acid from Q to P at position 393.
+The protein's natural variant, known as in MCC2D;, features a modification of the amino acid from N to T at position 403.
+The protein's natural variant, known as in MCC2D;, features a modification of the amino acid from G to D at position 410.
+The protein's natural variant, known as in MCC2D, features a modification of the amino acid from G to R at position 410.
+The protein's natural variant, known as in MCC2D; has some wild-type residual activity;, features a modification of the amino acid from V to L at position 434.
+The protein's natural variant, known as in MCC2D; mild form;, features a modification of the amino acid from I to V at position 437.
+The protein's natural variant, known as in MCC2D; unknown pathological significance;, features a modification of the amino acid from I to T at position 441.
+The protein's natural variant, known as in MCC2D; shows virtually no enzyme activity;, features a modification of the amino acid from A to V at position 456.
+The protein's natural variant, known as in MCC2D;, features a modification of the amino acid from P to S at position 459.
+The protein's natural variant, known as in MCC2D, features a modification of the amino acid from F to V at position 461.
+The protein's natural variant, known as in MCC2D; has some wild-type residual activity;, features a modification of the amino acid from G to R at position 475.
+The protein's natural variant, known as in MCC2D;, features a modification of the amino acid from Q to R at position 477.
+The protein's natural variant, known as in MCC2D;, features a modification of the amino acid from G to R at position 517.
+The protein's natural variant, known as in MCC2D;, features a modification of the amino acid from Y to S at position 520.
+The protein's natural variant, known as in MCC2D; has some wild-type residual activity;, features a modification of the amino acid from S to G at position 523.
+The protein's natural variant, known as in MCC2D;, features a modification of the amino acid from A to T at position 524.
+The protein's natural variant, known as in MCC2D;, features a modification of the amino acid from K to E at position 555.
+The natural variant of this protein is characterized by an amino acid alteration from G to E at position 746.
+The protein's natural variant, known as in a lung neuroendocrine carcinoma sample; somatic mutation;, features a modification of the amino acid from P to S at position 1193.
+The protein's natural variant, known as in PCH2E;, features a modification of the amino acid from Q to R at position 695.
+The protein's natural variant, known as in MONA;, features a modification of the amino acid from R to H at position 101.
+The natural variant of this protein is characterized by an amino acid alteration from D to Y at position 210.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from A to T at position 228.
+The protein's natural variant, known as in MONA;, features a modification of the amino acid from E to K at position 404.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from T to M at position 498.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from S to I at position 644.
+The protein's natural variant, known as found in a patient with early-onset epithelial ovarian tumor; uncertain pathological significance, features a modification of the amino acid from G to E at position 280.
+The protein's natural variant, known as found in a patient with early-onset epithelial ovarian tumor; alters the ratio of secreted activins and ihibins; uncertain pathological significance;, features a modification of the amino acid from N to S at position 386.
+The protein's natural variant, known as in strain: Biovar equi /isolate 155, features a modification of the amino acid from VV to FA at position 6.
+The protein's natural variant, known as in strain: Biovar equi / isolate 155, features a modification of the amino acid from F to L at position 8.
+The protein's natural variant, known as in strain: Biovar equi / isolate 155, features a modification of the amino acid from E to G at position 189.
+The protein's natural variant, known as in strain: Biovar equi / isolate 155, features a modification of the amino acid from N to D at position 205.
+The protein's natural variant, known as in strain: Biovar equi / isolate 155, features a modification of the amino acid from I to M at position 270.
+The protein's natural variant, known as in strain: Biovar equi / isolate 155, features a modification of the amino acid from A to P at position 277.
+The protein's natural variant, known as probable disease-associated variant found in a patient with dilated cardiomyopathy, features a modification of the amino acid from E to K at position 85.
+The protein's natural variant, known as in CMH17; modifies the secondary structure of the protein which is more flexible but does not undergo structural transition upon binding to membrane lipids; increases the affinity for phosphatidylserine; affects intracellular calcium handling and homeostasis;, features a modification of the amino acid from S to R at position 101.
+The protein's natural variant, known as in CMH17; results in vacuolization of intracellular structures and cardiomyocyte hypertrophy; affects intracellular calcium handling and homeostasis;, features a modification of the amino acid from Y to H at position 141.
+The protein's natural variant, known as in CMH17;, features a modification of the amino acid from T to K at position 161.
+The protein's natural variant, known as in CMH17; results in vacuolization of intracellular structures and cardiomyocyte hypertrophy; affects intracellular calcium handling and homeostasis. Greatly reduced phosphorylation. Increased myotube diameter. Reduced RYR1 activity and EC gain. Disruption of interaction with TRPC3;, features a modification of the amino acid from S to F at position 165.
+The protein's natural variant, known as probable disease-associated variant found in a patient with atrial fibrillation, features a modification of the amino acid from E to K at position 169.
+The protein's natural variant, known as in CMH17; unknown pathological significance;, features a modification of the amino acid from A to S at position 405.
+The protein's natural variant, known as does not affect protein conformation as shown by circular dichroism;, features a modification of the amino acid from G to S at position 505.
+The protein's natural variant, known as in AAT8; impairs cGMP binding; the mutant protein is constitutively active;, features a modification of the amino acid from R to Q at position 177.
+The protein's natural variant, known as in POROK8;, features a modification of the amino acid from R to C at position 9.
+The protein's natural variant, known as in POROK8;, features a modification of the amino acid from R to Q at position 311.
+The natural variant of this protein is characterized by an amino acid alteration from A to V at position 474.
+The natural variant of this protein is characterized by an amino acid alteration from C to CPGPGPGPS at position 486.
+The protein's natural variant, known as in MCOPS11; loss of function mutation;, features a modification of the amino acid from R to S at position 152.
+The protein's natural variant, known as changed function; unable to rescue the corresponding loss of function zebrafish mutant which displays a cilium function alteration phenotype;, features a modification of the amino acid from R to L at position 5.
+The protein's natural variant, known as in NPHP1; associated with Cogan-type congenital ocular motor apraxia;, features a modification of the amino acid from G to R at position 342.
+The protein's natural variant, known as in strain: B5233 / ATCC 13073, features a modification of the amino acid from P to Q at position 15.
+The protein's natural variant, known as in strain: B5233 / ATCC 13073, features a modification of the amino acid from E to G at position 271.
+The protein's natural variant, known as in HLCS deficiency; benign variant; conserves enzymatic wild-type activity;, features a modification of the amino acid from E to D at position 42.
+The protein's natural variant, known as in HLCS deficiency; has normal or low KM values for biotin (non-KM mutant), features a modification of the amino acid from R to P at position 183.
+The protein's natural variant, known as in HLCS deficiency; has normal or low KM values for biotin (non-KM mutant); growth of patients' fibroblasts is compromised compared with normal fibroblasts; patients cells are not sensitive to biotin-depletion from the media; growth rates cannot be restored by re-administration of biotin; enzyme activity is severely compromised and cannot be increased by additional biotin; turn-over rate for the mutant protein is double that of wild-type enzyme;, features a modification of the amino acid from L to R at position 216.
+The protein's natural variant, known as in HLCS deficiency; has normal or low KM values for biotin (non-KM mutant);, features a modification of the amino acid from L to P at position 237.
+The protein's natural variant, known as in HLCS deficiency, features a modification of the amino acid from G to W at position 241.
+The protein's natural variant, known as in HLCS deficiency; <10% activity; has normal or low KM values for biotin (non-KM mutant);, features a modification of the amino acid from V to E at position 333.
+The protein's natural variant, known as in HLCS deficiency; 22% activity; shows elevated KM values for biotin (KM mutant) compared with that of the wild-type form;, features a modification of the amino acid from R to S at position 360.
+The protein's natural variant, known as in HLCS deficiency; has normal or low KM values for biotin (non-KM mutant);, features a modification of the amino acid from V to D at position 363.
+The protein's natural variant, known as in HLCS deficiency; 0.2% activity;, features a modification of the amino acid from Y to C at position 456.
+The protein's natural variant, known as in HLCS deficiency; <10% activity;, features a modification of the amino acid from T to I at position 462.
+The protein's natural variant, known as in HLCS deficiency; 4.3% activity;, features a modification of the amino acid from L to S at position 470.
+The protein's natural variant, known as in HLCS deficiency;, features a modification of the amino acid from G to R at position 505.
+The protein's natural variant, known as in HLCS deficiency;, features a modification of the amino acid from R to W at position 508.
+The protein's natural variant, known as in HLCS deficiency, features a modification of the amino acid from N to K at position 511.
+The protein's natural variant, known as in HLCS deficiency, features a modification of the amino acid from G to E at position 518.
+The protein's natural variant, known as in HLCS deficiency; 3.4% activity, features a modification of the amino acid from V to G at position 547.
+The protein's natural variant, known as in HLCS deficiency;, features a modification of the amino acid from V to M at position 550.
+The protein's natural variant, known as in HLCS deficiency; almost no activity;, features a modification of the amino acid from D to N at position 571.
+The protein's natural variant, known as in HLCS deficiency; <10% activity;, features a modification of the amino acid from G to S at position 581.
+The protein's natural variant, known as in HLCS deficiency;, features a modification of the amino acid from G to R at position 582.
+The protein's natural variant, known as in HLCS deficiency, features a modification of the amino acid from D to Y at position 615.
+The protein's natural variant, known as in HLCS deficiency;, features a modification of the amino acid from D to N at position 634.
+The protein's natural variant, known as in HLCS deficiency; 12% activity, features a modification of the amino acid from D to Y at position 634.
+The protein's natural variant, known as in HLCS deficiency, features a modification of the amino acid from D to G at position 715.
+The protein's natural variant, known as in COXPD7; decreased cytochrome c oxidase activity in fibroblasts; severe assembly defects in mitochondrial complexes I, IV and V with a milder defect in the assembly of complex III; no effect on mitochondrial transcripts, rRNAs and tRNAs levels, features a modification of the amino acid from VLKHIPSGIVVKCHQTRSVDQNRKLARKILQEKVDVFYNGENSPVHKEKREAAKKKQERKKRAKETLEKKKLLKELWESSKKVH to G at position 166.
+The natural variant of this protein is characterized by an amino acid alteration from S to G at position 30.
+The protein's natural variant, known as in AYGRP;, features a modification of the amino acid from S to L at position 54.
+The protein's natural variant, known as in AYGRP;, features a modification of the amino acid from T to A at position 58.
+The protein's natural variant, known as in AYGRP;, features a modification of the amino acid from T to I at position 58.
+The protein's natural variant, known as in AYGRP;, features a modification of the amino acid from P to H at position 59.
+The protein's natural variant, known as in AYGRP;, features a modification of the amino acid from P to L at position 59.
+The protein's natural variant, known as in AYGRP;, features a modification of the amino acid from T to R at position 62.
+The protein's natural variant, known as in AYGRP;, features a modification of the amino acid from P to R at position 69.
+The protein's natural variant, known as in CTRCT21;, features a modification of the amino acid from R to P at position 288.
+The protein's natural variant, known as in CTRCT21;, features a modification of the amino acid from K to R at position 297.
+The protein's natural variant, known as in CTRCT21, features a modification of the amino acid from Q to L at position 303.
+The protein's natural variant, known as in CTRCT21; unknown pathological significance, features a modification of the amino acid from E to G at position 317.
+The protein's natural variant, known as in CTRCT21;, features a modification of the amino acid from K to E at position 320.
+The protein's natural variant, known as in Lurcher, features a modification of the amino acid from A to T at position 654.
+The protein's natural variant, known as in COXPD38;, features a modification of the amino acid from R to C at position 108.
+The protein's natural variant, known as in MCF-12A cell line, features a modification of the amino acid from Y to S at position 323.
+The protein's natural variant, known as in MRD33;, features a modification of the amino acid from M to L at position 385.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from P to H at position 180.
+The natural variant of this protein is characterized by an amino acid alteration from MFAFICLLAIAS to LAIAN at position 12.
+The natural variant of this protein is characterized by an amino acid alteration from SK to AN at position 22.
+The natural variant of this protein is characterized by an amino acid alteration from IEK to VEA at position 32.
+The natural variant of this protein is characterized by an amino acid alteration from KFVDSFNKI to RFVAEFNKK at position 52.
+The natural variant of this protein is characterized by an amino acid alteration from T to V at position 81.
+The natural variant of this protein is characterized by an amino acid alteration from QVK to KVT at position 88.
+The natural variant of this protein is characterized by an amino acid alteration from KE to AQ at position 103.
+The natural variant of this protein is characterized by an amino acid alteration from D to N at position 138.
+The protein's natural variant, known as may influence susceptibility to autoimmune and inflammatory diseases such as systemic lupus erythematosus, atopic asthma and atopic dermatitis complicated by eczema herpeticum; no significant effect on interferon-gamma-mediated signaling pathway;, features a modification of the amino acid from V to M at position 14.
+The protein's natural variant, known as in IMD27A;, features a modification of the amino acid from I to T at position 37.
+The protein's natural variant, known as in IMD27A; interferon-gamma-mediated signaling pathway completely abrogated;, features a modification of the amino acid from V to E at position 61.
+The protein's natural variant, known as may influence susceptibility to atopic dermatitis complicated by eczema herpeticum; could be detected on the cell surface; no significant effect on interferon-gamma-mediated signaling pathway;, features a modification of the amino acid from V to I at position 61.
+The protein's natural variant, known as in IMD27A; interferon-gamma-mediated signaling pathway severely reduced although not completely abrogated, features a modification of the amino acid from V to G at position 63.
+The protein's natural variant, known as in IMD27A; could be detected on the cell surface; interferon-gamma-mediated signaling pathway completely abrogated, features a modification of the amino acid from Y to C at position 66.
+The protein's natural variant, known as in IMD27A; interferon-gamma-mediated signaling pathway completely abrogated, features a modification of the amino acid from C to F at position 77.
+The protein's natural variant, known as in IMD27A; fails to bind IFN-gamma; could be detected on the cell surface; interferon-gamma-mediated signaling pathway completely abrogated;, features a modification of the amino acid from C to Y at position 77.
+The protein's natural variant, known as in IMD27A; interferon-gamma-mediated signaling pathway completely abrogated, features a modification of the amino acid from C to Y at position 85.
+The protein's natural variant, known as in IMD27A; interferon-gamma-mediated signaling pathway severely reduced;, features a modification of the amino acid from I to T at position 87.
+The protein's natural variant, known as could be detected on the cell surface; does not affect interferon-gamma-mediated signaling pathway;, features a modification of the amino acid from S to L at position 149.
+The protein's natural variant, known as in IMD27A;, features a modification of the amino acid from G to R at position 219.
+The protein's natural variant, known as associated with susceptibility to Helicobacter pylori infection; no significant effect on interferon-gamma-mediated signaling pathway;, features a modification of the amino acid from H to P at position 335.
+The protein's natural variant, known as no significant effect on interferon-gamma-mediated signaling pathway;, features a modification of the amino acid from I to M at position 352.
+The protein's natural variant, known as associated with susceptibility to atopic dermatitis complicated by eczema herpeticum; does not affect completely interferon-gamma-mediated signaling pathway;, features a modification of the amino acid from Y to C at position 397.
+The protein's natural variant, known as associated with susceptibility to Helicobacter pylori infection; may influence susceptibility to allergic diseases such as bronchial asthma and allergic rhinitis; could be detected on the cell surface; no significant effect on interferon-gamma-mediated signaling pathway;, features a modification of the amino acid from L to P at position 467.
+The protein's natural variant, known as in IMD27A;, features a modification of the amino acid from S to F at position 485.
+The natural variant of this protein is characterized by an amino acid alteration from P to T at position 185.
+The protein's natural variant, known as in PNSED; decreased mitochondrial tRNA methylation;, features a modification of the amino acid from R to H at position 291.
+The protein's natural variant, known as in PNSED; decreased mitochondrial tRNA methylation;, features a modification of the amino acid from M to V at position 386.
+The protein's natural variant, known as in strain: Wistar Gunn, features a modification of the amino acid from V to A at position 4.
+The protein's natural variant, known as in strain: Wistar Gunn, features a modification of the amino acid from N to S at position 116.
+The protein's natural variant, known as in strain: Wistar Gunn, features a modification of the amino acid from F to L at position 187.
+The protein's natural variant, known as in bursal lymphoma, features a modification of the amino acid from R to H at position 581.
+The protein's natural variant, known as in bursal lymphoma, features a modification of the amino acid from K to Q at position 736.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from S to G at position 402.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from Q to H at position 165.
+The protein's natural variant, known as in KABAMAS; decreased protein abundance;, features a modification of the amino acid from K to Q at position 123.
+The protein's natural variant, known as in SCN5; patient fibroblasts are characterized by impaired motility and increased apoptosis;, features a modification of the amino acid from T to N at position 224.
+The protein's natural variant, known as in SCN5;, features a modification of the amino acid from E to K at position 238.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from L to V at position 432.
+The protein's natural variant, known as in SIOD, features a modification of the amino acid from A to P at position 468.
+The protein's natural variant, known as in SIOD;, features a modification of the amino acid from I to N at position 548.
+The protein's natural variant, known as in SIOD, features a modification of the amino acid from S to L at position 579.
+The protein's natural variant, known as in SIOD; impairs without abolishing annealing helicase activity; no effect on specific binding to fork DNA; no effect on recruitment to sites of DNA damage;, features a modification of the amino acid from R to W at position 586.
+The protein's natural variant, known as in SIOD;, features a modification of the amino acid from R to W at position 644.
+The protein's natural variant, known as in SIOD;, features a modification of the amino acid from R to C at position 645.
+The protein's natural variant, known as in SIOD, features a modification of the amino acid from K to Q at position 647.
+The protein's natural variant, known as in SIOD, features a modification of the amino acid from K to T at position 647.
+The protein's natural variant, known as in SIOD;, features a modification of the amino acid from T to I at position 705.
+The protein's natural variant, known as in SIOD; abolishes annealing helicase activity; no effect on specific binding to fork DNA; no effect on recruitment to sites of DNA damage;, features a modification of the amino acid from R to Q at position 764.
+The protein's natural variant, known as in SIOD;, features a modification of the amino acid from R to H at position 820.
+The protein's natural variant, known as in MLC2A, features a modification of the amino acid from L to H at position 23.
+The protein's natural variant, known as in MLC2B;, features a modification of the amino acid from G to D at position 89.
+The protein's natural variant, known as in MLC2B;, features a modification of the amino acid from G to S at position 89.
+The protein's natural variant, known as in MLC2A;, features a modification of the amino acid from R to Q at position 92.
+The protein's natural variant, known as in MLC2B;, features a modification of the amino acid from R to W at position 92.
+The protein's natural variant, known as in MLC2A;, features a modification of the amino acid from R to C at position 98.
+The protein's natural variant, known as in MLC2B, features a modification of the amino acid from D to N at position 128.
+The protein's natural variant, known as in MLC2A;, features a modification of the amino acid from P to S at position 148.
+The protein's natural variant, known as in MLC2A;, features a modification of the amino acid from S to Y at position 196.
+The protein's natural variant, known as in MLC2A;, features a modification of the amino acid from D to N at position 211.
+The protein's natural variant, known as in MLC2B;, features a modification of the amino acid from R to C at position 288.
+The protein's natural variant, known as in MDM; no expression of the protein;, features a modification of the amino acid from W to R at position 15.
+The protein's natural variant, known as in MDM; reduced expression of the protein; decreased secretion;, features a modification of the amino acid from R to H at position 71.
+The protein's natural variant, known as in MDM; decreased secretion, features a modification of the amino acid from R to P at position 71.
+The protein's natural variant, known as in MDM; decreased secretion;, features a modification of the amino acid from C to R at position 77.
+The protein's natural variant, known as in MDM; unknown pathological significance; no effect on secretion;, features a modification of the amino acid from P to S at position 82.
+The protein's natural variant, known as in MDM; reduced expression of the protein;, features a modification of the amino acid from G to R at position 86.
+The protein's natural variant, known as in MDM; decreased secretion;, features a modification of the amino acid from C to S at position 94.
+The protein's natural variant, known as in MDM; decreased secretion, features a modification of the amino acid from L to P at position 98.
+The protein's natural variant, known as in MDM;, features a modification of the amino acid from C to Y at position 99.
+The protein's natural variant, known as in strain: W, features a modification of the amino acid from S to P at position 14.
+The protein's natural variant, known as in strain: W, features a modification of the amino acid from P to S at position 169.
+The protein's natural variant, known as in strain: W, features a modification of the amino acid from DAET to ETEA at position 227.
+The protein's natural variant, known as in COXPD33; unknown pathological significance;, features a modification of the amino acid from C to S at position 186.
+The protein's natural variant, known as in COXPD33; unknown pathological significance;, features a modification of the amino acid from F to L at position 204.
+The protein's natural variant, known as in COXPD33;, features a modification of the amino acid from G to W at position 247.
+The protein's natural variant, known as in COXPD33; unknown pathological significance;, features a modification of the amino acid from L to F at position 275.
+The protein's natural variant, known as in COXPD33;, features a modification of the amino acid from L to P at position 275.
+The protein's natural variant, known as in plasmid pLMO150, features a modification of the amino acid from R to P at position 32.
+The protein's natural variant, known as in plasmid pLMO20, features a modification of the amino acid from A to P at position 82.
+The protein's natural variant, known as in plasmid pLMO20, features a modification of the amino acid from A to P at position 84.
+The protein's natural variant, known as in plasmid RGN238, features a modification of the amino acid from E to Q at position 205.
+The protein's natural variant, known as in LAMM; probably impairs secretion;, features a modification of the amino acid from L to P at position 6.
+The protein's natural variant, known as in LAMM;, features a modification of the amino acid from S to P at position 156.
+The protein's natural variant, known as in strain: LT7, features a modification of the amino acid from A to R at position 17.
+The protein's natural variant, known as in strain: LT7, features a modification of the amino acid from KLILRR to EINPPT at position 298.
+The protein's natural variant, known as in strain: LT7, features a modification of the amino acid from S to T at position 350.
+The protein's natural variant, known as in strain: LT7, features a modification of the amino acid from L to V at position 420.
+The protein's natural variant, known as in strain: LT7, features a modification of the amino acid from SG to R at position 465.
+The protein's natural variant, known as in strain: LT7, features a modification of the amino acid from GL to AV at position 537.
+The protein's natural variant, known as in strain: LT7, features a modification of the amino acid from DQVILDAQRKFFDMLRRQNINVEFAEATSAPAVFSTINGLIEGKAN to IRLFLMRNVNSSICCVGKISMSSLRKDQRAGGIFYDQWLD at position 990.
+The protein's natural variant, known as found in a consanguineous family with intellectual disability; unknown pathological significance;, features a modification of the amino acid from R to G at position 182.
+The protein's natural variant, known as in DEE63; unknown pathological significance;, features a modification of the amino acid from L to M at position 128.
+The protein's natural variant, known as in LGMDR2;, features a modification of the amino acid from W to R at position 52.
+The protein's natural variant, known as in MMD1 and LGMDR2; Reduces calcium-sensitive phospholipid binding and interaction with AHNAK and AHNAK2;, features a modification of the amino acid from V to D at position 67.
+The protein's natural variant, known as in LGMDR2;, features a modification of the amino acid from G to R at position 155.
+The protein's natural variant, known as in LGMDR2;, features a modification of the amino acid from G to E at position 234.
+The protein's natural variant, known as found in patients with isolated hyperCKemia;, features a modification of the amino acid from R to W at position 253.
+The protein's natural variant, known as in pseudometabolic myopathy, features a modification of the amino acid from L to P at position 266.
+The protein's natural variant, known as in LGMDR2;, features a modification of the amino acid from I to T at position 284.
+The protein's natural variant, known as in MMD1;, features a modification of the amino acid from G to E at position 299.
+The protein's natural variant, known as in LGMDR2 and proximodistal myopathy;, features a modification of the amino acid from G to R at position 299.
+The protein's natural variant, known as in MMD1;, features a modification of the amino acid from G to W at position 299.
+The natural variant of this protein is characterized by an amino acid alteration from G to A at position 335.
+The protein's natural variant, known as in proximodistal myopathy;, features a modification of the amino acid from S to R at position 340.
+The protein's natural variant, known as in MMD1, features a modification of the amino acid from FRAED to Y at position 390.
+The protein's natural variant, known as in MMD1, features a modification of the amino acid from E to Q at position 389.
+The protein's natural variant, known as in MMD1;, features a modification of the amino acid from G to R at position 426.
+The protein's natural variant, known as in MMD1, features a modification of the amino acid from G to V at position 426.
+The protein's natural variant, known as in MMD1, features a modification of the amino acid from C to W at position 456.
+The protein's natural variant, known as in MMD1;, features a modification of the amino acid from G to R at position 519.
+The protein's natural variant, known as in LGMDR2 and MMD1; also found in patients with isolated hyperCKemia;, features a modification of the amino acid from R to W at position 555.
+The protein's natural variant, known as in MMD1 and LGMDR2;, features a modification of the amino acid from G to R at position 618.
+The protein's natural variant, known as in LGMDR2;, features a modification of the amino acid from G to R at position 621.
+The protein's natural variant, known as in LGMDR2;, features a modification of the amino acid from D to Y at position 625.
+The protein's natural variant, known as in LGMDR2, features a modification of the amino acid from P to R at position 731.
+The protein's natural variant, known as in MMD1 and LGMDR2;, features a modification of the amino acid from P to R at position 791.
+The protein's natural variant, known as in LGMDR2; unknown pathological significance;, features a modification of the amino acid from W to C at position 930.
+The protein's natural variant, known as in MMD1 and LGMDR2;, features a modification of the amino acid from R to W at position 959.
+The protein's natural variant, known as in MMD1;, features a modification of the amino acid from W to C at position 999.
+The protein's natural variant, known as in MMD1, features a modification of the amino acid from P to L at position 1029.
+The protein's natural variant, known as in LGMDR2;, features a modification of the amino acid from R to Q at position 1038.
+The protein's natural variant, known as in MMD1;, features a modification of the amino acid from R to C at position 1041.
+The protein's natural variant, known as in MMD1; dbNP:28939700;, features a modification of the amino acid from R to H at position 1046.
+The natural variant of this protein is characterized by an amino acid alteration from E to EAE at position 1065.
+The protein's natural variant, known as in LGMDR2; unknown pathological significance;, features a modification of the amino acid from I to M at position 1208.
+The protein's natural variant, known as in LGMDR2, features a modification of the amino acid from L to P at position 1228.
+The protein's natural variant, known as in proximodistal myopathy, features a modification of the amino acid from L to V at position 1276.
+The protein's natural variant, known as in MMD1 and LGMDR2;, features a modification of the amino acid from I to V at position 1298.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from I to M at position 1325.
+The protein's natural variant, known as in MMD1 and LGMDR2;, features a modification of the amino acid from E to K at position 1335.
+The protein's natural variant, known as in LGMDR2;, features a modification of the amino acid from L to P at position 1341.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from L to V at position 1349.
+The protein's natural variant, known as in MMD1;, features a modification of the amino acid from C to R at position 1361.
+The protein's natural variant, known as in LGMDR2;, features a modification of the amino acid from Y to C at position 1505.
+The protein's natural variant, known as in LGMDR2;, features a modification of the amino acid from K to T at position 1526.
+The protein's natural variant, known as in LGMDR2, features a modification of the amino acid from G to D at position 1543.
+The protein's natural variant, known as in MMD1, features a modification of the amino acid from T to R at position 1662.
+The protein's natural variant, known as found in patients with isolated hyperCKemia;, features a modification of the amino acid from C to S at position 1678.
+The protein's natural variant, known as in MMD1, features a modification of the amino acid from G to E at position 1679.
+The protein's natural variant, known as in MMD1;, features a modification of the amino acid from R to Q at position 1693.
+The protein's natural variant, known as in MMD1;, features a modification of the amino acid from R to W at position 1693.
+The protein's natural variant, known as in LGMDR2;, features a modification of the amino acid from E to G at position 1734.
+The protein's natural variant, known as in proximodistal myopathy, features a modification of the amino acid from E to V at position 1748.
+The protein's natural variant, known as in LGMDR2 and proximodistal myopathy; unknown pathological significance;, features a modification of the amino acid from R to W at position 1768.
+The protein's natural variant, known as in MMD1;, features a modification of the amino acid from D to N at position 1837.
+The protein's natural variant, known as in MMD1;, features a modification of the amino acid from G to D at position 1842.
+The protein's natural variant, known as in MMD1;, features a modification of the amino acid from H to R at position 1857.
+The protein's natural variant, known as in MMD1, features a modification of the amino acid from L to P at position 1922.
+The protein's natural variant, known as in MMD1, features a modification of the amino acid from C to G at position 1942.
+The natural variant of this protein is characterized by an amino acid alteration from G to S at position 1967.
+The protein's natural variant, known as in LGMDR2;, features a modification of the amino acid from P to S at position 1970.
+The protein's natural variant, known as in MMD1;, features a modification of the amino acid from R to Q at position 2000.
+The protein's natural variant, known as in MMD1, LGMDR2 and proximodistal myopathy;, features a modification of the amino acid from R to C at position 2042.
+The protein's natural variant, known as in MMD1;, features a modification of the amino acid from P to L at position 2068.
+The protein's natural variant, known as in NPHS1; lack of protein expression on the cell surface;, features a modification of the amino acid from W to S at position 64.
+The protein's natural variant, known as in NPHS1;, features a modification of the amino acid from L to V at position 96.
+The protein's natural variant, known as in NPHS1;, features a modification of the amino acid from A to E at position 107.
+The protein's natural variant, known as in NPHS1;, features a modification of the amino acid from A to T at position 107.
+The protein's natural variant, known as in NPHS1;, features a modification of the amino acid from A to V at position 107.
+The protein's natural variant, known as in NPHS1;, features a modification of the amino acid from P to L at position 167.
+The protein's natural variant, known as in NPHS1; lack of protein expression on the cell surface;, features a modification of the amino acid from I to N at position 171.
+The protein's natural variant, known as in NPHS1; lack of protein expression on the cell surface;, features a modification of the amino acid from I to N at position 173.
+The protein's natural variant, known as in NPHS1;, features a modification of the amino acid from N to I at position 188.
+The protein's natural variant, known as in NPHS1;, features a modification of the amino acid from E to K at position 189.
+The protein's natural variant, known as in NPHS1, features a modification of the amino acid from TPR to I at position 207.
+The protein's natural variant, known as in NPHS1;, features a modification of the amino acid from L to P at position 237.
+The protein's natural variant, known as in NPHS1;, features a modification of the amino acid from R to W at position 256.
+The protein's natural variant, known as in NPHS1;, features a modification of the amino acid from C to R at position 265.
+The protein's natural variant, known as in NPHS1; lack of protein expression on the cell surface;, features a modification of the amino acid from G to C at position 270.
+The protein's natural variant, known as in NPHS1; benign variant;, features a modification of the amino acid from T to I at position 294.
+The protein's natural variant, known as in NPHS1;, features a modification of the amino acid from R to C at position 299.
+The protein's natural variant, known as in NPHS1;, features a modification of the amino acid from P to H at position 340.
+The protein's natural variant, known as in NPHS1;, features a modification of the amino acid from G to E at position 347.
+The protein's natural variant, known as in NPHS1; lack of protein expression on the cell surface;, features a modification of the amino acid from S to P at position 350.
+The protein's natural variant, known as in NPHS1; lack of protein expression on the cell surface; the mutant protein is retained in the endoplasmic reticulum;, features a modification of the amino acid from S to R at position 366.
+The protein's natural variant, known as in NPHS1; lack of protein expression on the cell surface;, features a modification of the amino acid from R to C at position 367.
+The protein's natural variant, known as in NPHS1;, features a modification of the amino acid from P to L at position 368.
+The protein's natural variant, known as in NPHS1; lack of protein expression on the cell surface;, features a modification of the amino acid from P to S at position 368.
+The protein's natural variant, known as in NPHS1; does not affect protein expression on the cell surface;, features a modification of the amino acid from L to V at position 376.
+The protein's natural variant, known as in NPHS1;, features a modification of the amino acid from R to W at position 379.
+The protein's natural variant, known as in NPHS1;, features a modification of the amino acid from R to W at position 407.
+The protein's natural variant, known as does not affect protein expression on the cell surface;, features a modification of the amino acid from R to Q at position 408.
+The protein's natural variant, known as in NPHS1;, features a modification of the amino acid from G to C at position 412.
+The protein's natural variant, known as in NPHS1;, features a modification of the amino acid from C to F at position 417.
+The protein's natural variant, known as in NPHS1; unknown pathological significance;, features a modification of the amino acid from I to N at position 446.
+The protein's natural variant, known as in NPHS1;, features a modification of the amino acid from R to Q at position 460.
+The protein's natural variant, known as in NPHS1; lack of protein expression on the cell surface;, features a modification of the amino acid from C to Y at position 465.
+The protein's natural variant, known as in NPHS1;, features a modification of the amino acid from P to S at position 519.
+The protein's natural variant, known as in NPHS1; lack of protein expression on the cell surface;, features a modification of the amino acid from C to F at position 528.
+The protein's natural variant, known as in NPHS1;, features a modification of the amino acid from R to C at position 558.
+The protein's natural variant, known as in NPHS1;, features a modification of the amino acid from C to S at position 567.
+The protein's natural variant, known as in NPHS1;, features a modification of the amino acid from S to R at position 569.
+The protein's natural variant, known as in NPHS1;, features a modification of the amino acid from S to N at position 572.
+The protein's natural variant, known as in NPHS1;, features a modification of the amino acid from P to Q at position 575.
+The protein's natural variant, known as in NPHS1;, features a modification of the amino acid from R to G at position 586.
+The protein's natural variant, known as in NPHS1;, features a modification of the amino acid from L to R at position 587.
+The protein's natural variant, known as in NPHS1;, features a modification of the amino acid from V to I at position 608.
+The protein's natural variant, known as in NPHS1; lack of protein expression on the cell surface;, features a modification of the amino acid from L to Q at position 610.
+The protein's natural variant, known as found in patients with nephrotic syndrome; unknown pathological significance;, features a modification of the amino acid from H to R at position 617.
+The protein's natural variant, known as in NPHS1; lack of protein expression on the cell surface;, features a modification of the amino acid from C to F at position 623.
+The protein's natural variant, known as in NPHS1;, features a modification of the amino acid from N to K at position 673.
+The protein's natural variant, known as in NPHS1;, features a modification of the amino acid from W to C at position 681.
+The protein's natural variant, known as in NPHS1;, features a modification of the amino acid from V to G at position 709.
+The protein's natural variant, known as in NPHS1; unknown pathological significance;, features a modification of the amino acid from R to H at position 711.
+The protein's natural variant, known as in NPHS1; does not affect protein expression on the cell surface;, features a modification of the amino acid from S to C at position 724.
+The protein's natural variant, known as found in patients with nephrotic syndrome; unknown pathological significance, features a modification of the amino acid from E to D at position 725.
+The protein's natural variant, known as in NPHS1; unknown pathological significance;, features a modification of the amino acid from V to M at position 736.
+The protein's natural variant, known as in NPHS1;, features a modification of the amino acid from A to V at position 739.
+The protein's natural variant, known as in NPHS1;, features a modification of the amino acid from I to T at position 742.
+The protein's natural variant, known as in NPHS1; does not affect protein expression on the cell surface;, features a modification of the amino acid from R to C at position 743.
+The protein's natural variant, known as in NPHS1; lack of protein expression on the cell surface;, features a modification of the amino acid from R to P at position 802.
+The protein's natural variant, known as in NPHS1; lack of protein expression on the cell surface;, features a modification of the amino acid from R to W at position 802.
+The protein's natural variant, known as in NPHS1; lack of protein expression on the cell surface;, features a modification of the amino acid from A to D at position 806.
+The protein's natural variant, known as in NPHS1;, features a modification of the amino acid from D to V at position 819.
+The protein's natural variant, known as in NPHS1;, features a modification of the amino acid from V to M at position 822.
+The protein's natural variant, known as in NPHS1; lack of protein expression on the cell surface;, features a modification of the amino acid from R to C at position 831.
+The protein's natural variant, known as in NPHS1; the mutant protein is retained in the endoplasmic reticulum;, features a modification of the amino acid from L to P at position 832.
+The protein's natural variant, known as in NPHS1;, features a modification of the amino acid from V to F at position 834.
+The protein's natural variant, known as in NPHS1; unknown pathological significance, features a modification of the amino acid from A to V at position 851.
+The protein's natural variant, known as in NPHS1;, features a modification of the amino acid from S to P at position 910.
+The protein's natural variant, known as in NPHS1;, features a modification of the amino acid from A to T at position 912.
+The protein's natural variant, known as in NPHS1;, features a modification of the amino acid from R to S at position 976.
+The protein's natural variant, known as in NPHS1;, features a modification of the amino acid from S to N at position 1016.
+The protein's natural variant, known as in NPHS1;, features a modification of the amino acid from G to V at position 1020.
+The protein's natural variant, known as in NPHS1; unknown pathological significance, features a modification of the amino acid from G to C at position 1096.
+The protein's natural variant, known as in NPHS1; does not affect protein expression on the cell surface;, features a modification of the amino acid from R to C at position 1140.
+The protein's natural variant, known as in PVNH8; decreased interaction with GGA3;, features a modification of the amino acid from Y to H at position 35.
+The protein's natural variant, known as in PVNH8; unknown pathological significance, features a modification of the amino acid from R to H at position 99.
+The protein's natural variant, known as in PVNH8, features a modification of the amino acid from K to E at position 127.
+The protein's natural variant, known as in VDDR1B; complete loss of activity;, features a modification of the amino acid from L to P at position 99.
+The protein's natural variant, known as reduces 25-hydroxylase activity, features a modification of the amino acid from K to N at position 242.
+The protein's natural variant, known as in Dau C 1.2, features a modification of the amino acid from P to T at position 36.
+The protein's natural variant, known as in Dau C 1.3 and CR16/Gea20, features a modification of the amino acid from E to D at position 43.
+The protein's natural variant, known as in Dau C 1.2, features a modification of the amino acid from S to T at position 66.
+The protein's natural variant, known as in Dau C 1.2, features a modification of the amino acid from T to S at position 80.
+The protein's natural variant, known as in CR16/Gea20, features a modification of the amino acid from G to E at position 93.
+The protein's natural variant, known as in Dau C 1.2 and CR16/Gea20, features a modification of the amino acid from L to M at position 102.
+The protein's natural variant, known as in Dau C 1.3, features a modification of the amino acid from A to E at position 138.
+The protein's natural variant, known as in SNIBCPS;, features a modification of the amino acid from H to R at position 886.
+The protein's natural variant, known as in SNIBCPS; increased function in chromatin remodeling;, features a modification of the amino acid from L to F at position 915.
+The protein's natural variant, known as in SNIBCPS;, features a modification of the amino acid from E to K at position 921.
+The protein's natural variant, known as in SNIBCPS;, features a modification of the amino acid from G to E at position 961.
+The protein's natural variant, known as in SNIBCPS;, features a modification of the amino acid from R to Q at position 985.
+The protein's natural variant, known as in SNIBCPS;, features a modification of the amino acid from R to W at position 985.
+The protein's natural variant, known as in SNIBCPS; the patient also carries a truncating variant in CIC; both variants may contribute to disease phenotype, features a modification of the amino acid from D to H at position 1120.
+The protein's natural variant, known as in SNIBCPS; decreased function in chromatin remodeling; decreased ATPase activity;, features a modification of the amino acid from R to P at position 1121.
+The protein's natural variant, known as in SNIBCPS;, features a modification of the amino acid from T to I at position 1136.
+The protein's natural variant, known as in SNIBCPS; highly decreased function in chromatin remodeling;, features a modification of the amino acid from W to R at position 1158.
+The protein's natural variant, known as in SNIBCPS; highly decreased function in chromatin remodeling;, features a modification of the amino acid from N to K at position 1159.
+The protein's natural variant, known as in SNIBCPS;, features a modification of the amino acid from H to R at position 1161.
+The protein's natural variant, known as in SNIBCPS;, features a modification of the amino acid from R to W at position 1169.
+The protein's natural variant, known as in SNIBCPS;, features a modification of the amino acid from H to R at position 1171.
+The protein's natural variant, known as in SNIBCPS; decreased function in chromatin remodeling; decreased ATPase activity;, features a modification of the amino acid from R to Q at position 1172.
+The protein's natural variant, known as in SNIBCPS; unknown pathological significance; does not affect function in chromatin remodeling; no effect on ATPase activity;, features a modification of the amino acid from R to P at position 1187.
+The protein's natural variant, known as in SNIBCPS;, features a modification of the amino acid from L to P at position 1236.
+The protein's natural variant, known as in SNIBCPS;, features a modification of the amino acid from R to Q at position 1342.
+The protein's natural variant, known as in SNIBCPS;, features a modification of the amino acid from R to L at position 1881.
+The protein's natural variant, known as in IMD9;, features a modification of the amino acid from R to W at position 91.
+The protein's natural variant, known as in TAM2; constitutively active Ca(+2) channel, independently of STIM proteins; no effect on localization to the cell membrane;, features a modification of the amino acid from G to S at position 98.
+The protein's natural variant, known as in TAM2; constitutively active Ca(+2) channel, independently of STIM proteins; no effect on localization to the cell membrane, features a modification of the amino acid from V to M at position 107.
+The protein's natural variant, known as in TAM2; mediates excessive Ca(2+) entry when gated by STIM1; no effect on localization to the cell membrane;, features a modification of the amino acid from T to M at position 184.
+The protein's natural variant, known as in TAM2; increases activation of the Ca2+ release-activated Ca2+ (CRAC) channel;, features a modification of the amino acid from P to L at position 245.
+The protein's natural variant, known as in MCPH12;, features a modification of the amino acid from A to T at position 197.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation, features a modification of the amino acid from P to L at position 199.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from K to M at position 910.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from M to I at position 1192.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from E to Q at position 1702.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from P to T at position 1839.
+The protein's natural variant, known as in strain: Erdman, features a modification of the amino acid from N to K at position 467.
+The protein's natural variant, known as in strain: ATCC 6633, features a modification of the amino acid from Q to H at position 22.
+The protein's natural variant, known as in strain: ATCC 6633, features a modification of the amino acid from F to Y at position 57.
+The protein's natural variant, known as in strain: ATCC 6633, features a modification of the amino acid from R to G at position 60.
+The protein's natural variant, known as in strain: ATCC 6633, features a modification of the amino acid from T to I at position 82.
+The protein's natural variant, known as in strain: ATCC 6633, features a modification of the amino acid from Q to R at position 117.
+The protein's natural variant, known as in strain: ATCC 6633, features a modification of the amino acid from A to E at position 187.
+The protein's natural variant, known as in strain: ATCC 6633, features a modification of the amino acid from Y to F at position 207.
+The protein's natural variant, known as in CORD5;, features a modification of the amino acid from Q to H at position 626.
+The protein's natural variant, known as in strain: CWL029 and TW-183, features a modification of the amino acid from Y to H at position 243.
+The protein's natural variant, known as in prolactin-1, features a modification of the amino acid from E to P at position 90.
+The protein's natural variant, known as in CONCL; inactive, features a modification of the amino acid from D to N at position 268.
+The protein's natural variant, known as in strain: NCTC 11638, features a modification of the amino acid from L to V at position 3.
+The protein's natural variant, known as in strain: NCTC 11638, features a modification of the amino acid from I to T at position 9.
+The protein's natural variant, known as in strain: NCTC 11638, features a modification of the amino acid from S to N at position 144.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from D to N at position 100.
+The protein's natural variant, known as in XLID29;, features a modification of the amino acid from L to P at position 33.
+The protein's natural variant, known as in DEE1, features a modification of the amino acid from A to AAAAAAAA at position 115.
+The protein's natural variant, known as in DEE1 and PRTS; also found in non-specific intellectual disability families; frequent variant, features a modification of the amino acid from A to AAAAAAAAA at position 155.
+The protein's natural variant, known as in XLID29;, features a modification of the amino acid from G to S at position 286.
+The protein's natural variant, known as in LISX2;, features a modification of the amino acid from R to H at position 332.
+The protein's natural variant, known as in LISX2; abolishes transcriptional activation of KDM5C; abolishes sequence-specific DNA-binding; reduces transcriptional repression of LMO1 and SHOX2, features a modification of the amino acid from R to P at position 332.
+The protein's natural variant, known as in ACCAG; abolishes transcriptional activation of KDM5C; abolishes sequence-specific DNA-binding; reduces transcriptional repression of LMO1 and SHOX2;, features a modification of the amino acid from T to N at position 333.
+The protein's natural variant, known as in LISX2; abolishes transcriptional activation of KDM5C; abolishes sequence-specific DNA-binding; reduces transcriptional repression of LMO1 and SHOX2;, features a modification of the amino acid from L to Q at position 343.
+The protein's natural variant, known as in DEE1; corpus callosum hypoplasia and simplified gyral pattern observed in one patient; reduces sequence-specific DNA-binding; slightly reduces transcriptional repression of LMO1;, features a modification of the amino acid from P to L at position 353.
+The protein's natural variant, known as in LISX2; abolishes transcriptional activation of KDM5C; abolishes sequence-specific DNA-binding; reduces transcriptional repression of LMO1 and SHOX2, features a modification of the amino acid from P to R at position 353.
+The protein's natural variant, known as in LISX2; severe phenotype;, features a modification of the amino acid from A to T at position 521.
+The protein's natural variant, known as in NBIA2A;, features a modification of the amino acid from V to E at position 310.
+The protein's natural variant, known as in NBIA2A; complete loss of phospholipase and lysophospholipase activities, features a modification of the amino acid from A to T at position 341.
+The protein's natural variant, known as in NBIA2A, features a modification of the amino acid from D to G at position 484.
+The protein's natural variant, known as in NBIA2A; complete loss of phospholipase and lysophospholipase activities, features a modification of the amino acid from G to C at position 517.
+The protein's natural variant, known as in NBIA2B;, features a modification of the amino acid from K to T at position 545.
+The protein's natural variant, known as in NBIA2B; increases phospholipase, lysophospholipase and thioesterase activities;, features a modification of the amino acid from R to W at position 632.
+The protein's natural variant, known as in NBIA2A; complete loss of phospholipase and lysophospholipase activities, features a modification of the amino acid from G to R at position 638.
+The protein's natural variant, known as in NBIA2A;, features a modification of the amino acid from T to M at position 661.
+The protein's natural variant, known as in PARK14; has no effect on phospholipase, lysophospholipase and thioesterase activities;, features a modification of the amino acid from R to Q at position 741.
+The protein's natural variant, known as in NBIA2A; significantly reduces phospholipase and lysophospholipase activities, features a modification of the amino acid from R to W at position 741.
+The protein's natural variant, known as in PARK14; has no effect on phospholipase, lysophospholipase and thioesterase activities;, features a modification of the amino acid from R to W at position 747.
+The protein's natural variant, known as in strain: cv. Lip-0, features a modification of the amino acid from RL to PP at position 231.
+The protein's natural variant, known as in strain: cv. Aa-0, features a modification of the amino acid from L to P at position 231.
+The protein's natural variant, known as in strain: cv. Goe-2, features a modification of the amino acid from G to S at position 248.
+The protein's natural variant, known as in strain: cv. Ri-0, features a modification of the amino acid from T to R at position 250.
+The protein's natural variant, known as in strain: cv. Gre-0 and cv. Kas-1, features a modification of the amino acid from K to E at position 253.
+The protein's natural variant, known as in strain: cv. Di-0 and cv. Kil-0, features a modification of the amino acid from K to R at position 263.
+The protein's natural variant, known as in strain: cv. Cl-0, features a modification of the amino acid from K to E at position 271.
+The protein's natural variant, known as in strain: cv. Yo-0, features a modification of the amino acid from V to D at position 280.
+The protein's natural variant, known as in strain: cv. Kil-0, features a modification of the amino acid from K to E at position 290.
+The protein's natural variant, known as in strain: cv. Yo-0, features a modification of the amino acid from L to I at position 301.
+The protein's natural variant, known as in strain: cv. Ba-1, features a modification of the amino acid from QPAD to SLQI at position 311.
+The protein's natural variant, known as in strain: cv. En-2, features a modification of the amino acid from A to S at position 310.
+The protein's natural variant, known as in strain: cv. Oy-0, features a modification of the amino acid from D to V at position 311.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to H at position 719.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from A to T at position 1130.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation, features a modification of the amino acid from L to I at position 422.
+The protein's natural variant, known as in a glioma low grade oligodendroglioma sample; somatic mutation;, features a modification of the amino acid from R to Q at position 781.
+The protein's natural variant, known as in a bladder transitional cell carcinoma sample; somatic mutation, features a modification of the amino acid from L to V at position 1061.
+The protein's natural variant, known as in allele asgC767; unable to produce the A-signal, otherwise growth is unaffected, features a modification of the amino acid from E to K at position 598.
+The protein's natural variant, known as in IFD;, features a modification of the amino acid from S to L at position 46.
+The protein's natural variant, known as in strain: cv. Cranbrook, cv. Empraba, cv. ET8 and cv. Tasman, features a modification of the amino acid from V to M at position 140.
+The protein's natural variant, known as in strain: cv. Maringa, features a modification of the amino acid from L to I at position 208.
+The protein's natural variant, known as in strain: cv. Cranbrook, cv. Empraba, cv. ET8 and cv. Tasman, features a modification of the amino acid from S to F at position 260.
+The protein's natural variant, known as in strain: CAST, MAI, MBT and PWK, features a modification of the amino acid from V to A at position 700.
+The protein's natural variant, known as in strain: CAST, MAI, MBT and PWK, features a modification of the amino acid from S to L at position 716.
+The protein's natural variant, known as in MGFSL-3NEU, features a modification of the amino acid from N to S at position 122.
+The natural variant of this protein is characterized by an amino acid alteration from L to P at position 193.
+The natural variant of this protein is characterized by an amino acid alteration from A to S at position 207.
+The protein's natural variant, known as in cervical cancer; somatic mutation, features a modification of the amino acid from E to K at position 14.
+The protein's natural variant, known as in PJS, features a modification of the amino acid from E to G at position 16.
+The protein's natural variant, known as in melanoma; sporadic malignant; somatic mutation;, features a modification of the amino acid from Y to D at position 49.
+The protein's natural variant, known as in cervical carcinoma; somatic mutation;, features a modification of the amino acid from V to M at position 66.
+The protein's natural variant, known as in PJS; abolishes kinase activity, leading to loss of autophosphorylation;, features a modification of the amino acid from L to P at position 67.
+The protein's natural variant, known as in sporadic cancer; somatic mutation; no effect on kinase activity nor in heterotrimeric complex assembly with STRADA and CAB39;, features a modification of the amino acid from R to G at position 86.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation;, features a modification of the amino acid from R to K at position 87.
+The protein's natural variant, known as in sporadic cancer; somatic mutation; no effect on kinase activity nor in heterotrimeric complex assembly with STRADA and CAB39;, features a modification of the amino acid from Q to R at position 123.
+The protein's natural variant, known as in melanoma; sporadic malignant; somatic mutation;, features a modification of the amino acid from G to R at position 135.
+The protein's natural variant, known as in sporadic cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39, features a modification of the amino acid from F to S at position 157.
+The protein's natural variant, known as in cervical cancer; somatic mutation, features a modification of the amino acid from L to P at position 160.
+The protein's natural variant, known as in PJS, features a modification of the amino acid from DGL to NDM at position 164.
+The protein's natural variant, known as in TGCT; a tumor with seminoma and teratoma components; associated with severely impaired but detectable kinase activity; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39; predominantly nuclear localization;, features a modification of the amino acid from G to D at position 163.
+The protein's natural variant, known as in sporadic cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39, features a modification of the amino acid from Q to P at position 170.
+The protein's natural variant, known as in colorectal cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39;, features a modification of the amino acid from G to S at position 171.
+The protein's natural variant, known as in sporadic cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39, features a modification of the amino acid from H to R at position 174.
+The protein's natural variant, known as in PJS; loss of kinase activity, leading to greatly reduced autophosphorylation; fails to phosphorylate PTEN in vitro; no significant effect on nucleocytoplasmic localization;, features a modification of the amino acid from D to N at position 176.
+The protein's natural variant, known as in sporadic cancer; somatic mutation; Loss of kinase activity, features a modification of the amino acid from D to Y at position 176.
+The protein's natural variant, known as in sporadic cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39;, features a modification of the amino acid from I to N at position 177.
+The protein's natural variant, known as in sporadic cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39; requires 2 nucleotide substitutions;, features a modification of the amino acid from N to E at position 181.
+The protein's natural variant, known as in PJS;, features a modification of the amino acid from D to N at position 194.
+The protein's natural variant, known as in lung cancer; somatic mutation;, features a modification of the amino acid from D to V at position 194.
+The protein's natural variant, known as in melanoma; sporadic malignant; somatic mutation;, features a modification of the amino acid from D to Y at position 194.
+The protein's natural variant, known as in colorectal cancer; somatic mutation; impaired kinase activity;, features a modification of the amino acid from E to K at position 199.
+The protein's natural variant, known as in sporadic cancer; somatic mutation; does not affect kinase activity, features a modification of the amino acid from E to Q at position 199.
+The protein's natural variant, known as in sporadic cancer; somatic mutation; no effect heterotrimeric complex assembly with STRADA and CAB39;, features a modification of the amino acid from A to T at position 205.
+The protein's natural variant, known as in colorectal cancer; somatic mutation; no effect heterotrimeric complex assembly with STRADA and CAB39;, features a modification of the amino acid from D to N at position 208.
+The protein's natural variant, known as in colorectal cancer; somatic mutation;, features a modification of the amino acid from G to D at position 215.
+The protein's natural variant, known as in sporadic cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39;, features a modification of the amino acid from S to F at position 216.
+The protein's natural variant, known as in sporadic cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39, features a modification of the amino acid from E to V at position 223.
+The protein's natural variant, known as in sporadic cancer; somatic mutation; no effect heterotrimeric complex assembly with STRADA and CAB39, features a modification of the amino acid from T to P at position 230.
+The protein's natural variant, known as in cervical cancer; somatic mutation;, features a modification of the amino acid from F to L at position 231.
+The protein's natural variant, known as in sporadic cancer; somatic mutation; no effect heterotrimeric complex assembly with STRADA and CAB39, features a modification of the amino acid from S to P at position 232.
+The protein's natural variant, known as in PJS; late onset suggests reduced penetrance;, features a modification of the amino acid from W to C at position 239.
+The protein's natural variant, known as in sporadic cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39, features a modification of the amino acid from L to R at position 245.
+The protein's natural variant, known as in sporadic cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39, features a modification of the amino acid from T to P at position 250.
+The protein's natural variant, known as in sporadic cancer; somatic mutation; no effect on kinase activity nor in heterotrimeric complex assembly with STRADA and CAB39, features a modification of the amino acid from Y to H at position 272.
+The protein's natural variant, known as in sporadic cancer; somatic mutation; no effect on kinase activity nor in heterotrimeric complex assembly with STRADA and CAB39, features a modification of the amino acid from D to Y at position 277.
+The protein's natural variant, known as in ovarian carcinoma; somatic mutation;, features a modification of the amino acid from P to L at position 281.
+The protein's natural variant, known as in sporadic cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39, features a modification of the amino acid from L to Q at position 285.
+The protein's natural variant, known as in PJS;, features a modification of the amino acid from R to K at position 297.
+The protein's natural variant, known as in PJS, features a modification of the amino acid from IRQH to N at position 306.
+The protein's natural variant, known as in PJS; abolishes kinase activity, leading to loss of autophosphorylation;, features a modification of the amino acid from W to C at position 308.
+The protein's natural variant, known as in colorectal cancer; no effect heterotrimeric complex assembly with STRADA and CAB39, features a modification of the amino acid from P to H at position 314.
+The protein's natural variant, known as in PJS; pathogenicity uncertain; no effect heterotrimeric complex assembly with STRADA and CAB39;, features a modification of the amino acid from P to S at position 315.
+The protein's natural variant, known as in gastric carcinoma; no effect heterotrimeric complex assembly with STRADA and CAB39;, features a modification of the amino acid from P to L at position 324.
+The protein's natural variant, known as in colorectal cancer; somatic mutation;, features a modification of the amino acid from F to L at position 354.
+The protein's natural variant, known as in colorectal cancer; somatic mutation;, features a modification of the amino acid from T to M at position 367.
+The protein's natural variant, known as in DYT4;, features a modification of the amino acid from R to G at position 2.
+The protein's natural variant, known as in HLD6;, features a modification of the amino acid from D to N at position 249.
+The protein's natural variant, known as in MDDGB1;, features a modification of the amino acid from G to R at position 65.
+The protein's natural variant, known as in MDDGA1;, features a modification of the amino acid from G to R at position 76.
+The protein's natural variant, known as in MDDGA1; severe Walker-Warburg syndrome;, features a modification of the amino acid from R to C at position 105.
+The protein's natural variant, known as in MDDGA1; severe Walker-Warburg syndrome;, features a modification of the amino acid from R to H at position 105.
+The protein's natural variant, known as in MDDGC1; a common founder mutation;, features a modification of the amino acid from A to P at position 200.
+The protein's natural variant, known as in MDDGA1; severe Walker-Warburg syndrome, features a modification of the amino acid from G to V at position 207.
+The protein's natural variant, known as requires 2 nucleotide substitutions;, features a modification of the amino acid from Q to W at position 251.
+The protein's natural variant, known as in MDDGA1, features a modification of the amino acid from V to D at position 428.
+The protein's natural variant, known as in MDDGA1 and MDDGB1; likely benign variant;, features a modification of the amino acid from S to R at position 537.
+The protein's natural variant, known as in MDDGB1;, features a modification of the amino acid from W to C at position 582.
+The protein's natural variant, known as in MDDGB1;, features a modification of the amino acid from Q to H at position 590.
+The protein's natural variant, known as in MDDGB1;, features a modification of the amino acid from A to T at position 669.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 20.
+The protein's natural variant, known as abolishes activation by propionate;, features a modification of the amino acid from R to W at position 174.
+The protein's natural variant, known as in mutant COP41, features a modification of the amino acid from T to I at position 108.
+The protein's natural variant, known as in mutant COP50, features a modification of the amino acid from P to S at position 113.
+The protein's natural variant, known as in mutants TS22 and TRCOP21, features a modification of the amino acid from T to I at position 138.
+The protein's natural variant, known as in mutants COP21 and TRCOP21, features a modification of the amino acid from A to S at position 162.
+The protein's natural variant, known as in 30% of egg-white and yolk, features a modification of the amino acid from N to K at position 31.
+The protein's natural variant, known as in NDMSCA; unknown pathological significance;, features a modification of the amino acid from L to F at position 885.
+The protein's natural variant, known as in NDMSCA; unknown pathological significance;, features a modification of the amino acid from R to Q at position 1058.
+The natural variant of this protein is characterized by an amino acid alteration from D to N at position 64.
+The protein's natural variant, known as found in patients with progressive myoclonus epilepsy and dementia; unknown pathological significance;, features a modification of the amino acid from A to V at position 85.
+The protein's natural variant, known as in strain: HW00, HW09, NC37, NC48, TT00 and TT01, features a modification of the amino acid from I to M at position 26.
+The protein's natural variant, known as in strain: HW00, HW09, NC37, NC48, TT00 and TT01, features a modification of the amino acid from M to I at position 32.
+The protein's natural variant, known as in strain: AU023, C167, DSR, DSW, KY007, KY201, KY215, MD106, MD225, RU35 and SC00, features a modification of the amino acid from N to D at position 34.
+The protein's natural variant, known as in SDS1; unknown pathological significance;, features a modification of the amino acid from N to K at position 8.
+The protein's natural variant, known as in SDS1;, features a modification of the amino acid from K to T at position 33.
+The protein's natural variant, known as in SDS1; unknown pathological significance;, features a modification of the amino acid from E to G at position 44.
+The protein's natural variant, known as in SDS1; unknown pathological significance;, features a modification of the amino acid from K to E at position 67.
+The protein's natural variant, known as in SDS1; unknown pathological significance;, features a modification of the amino acid from I to S at position 87.
+The protein's natural variant, known as in SDS1; strongly reduced release of EIF6 from pre-60S ribosome subunits;, features a modification of the amino acid from R to T at position 126.
+The protein's natural variant, known as in SDS1; unknown pathological significance;, features a modification of the amino acid from R to C at position 169.
+The protein's natural variant, known as in strain: AS-P-78, features a modification of the amino acid from I to Y at position 195.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from V to I at position 265.
+The protein's natural variant, known as found in a patient with developmental delay with seizures and mild developmental delay; unknown pathological significance, features a modification of the amino acid from M to R at position 191.
+The protein's natural variant, known as in RTTCV;, features a modification of the amino acid from F to L at position 215.
+The protein's natural variant, known as probable disease-associated variant found in a patient with developmental delay, features a modification of the amino acid from N to S at position 232.
+The protein's natural variant, known as in RTTCV; the mutant protein extensively, although not fully, localizes in nuclear speckles, while the wild-type is more widely dispersed throughout the nucleus;, features a modification of the amino acid from R to C at position 244.
+The protein's natural variant, known as in OKS;, features a modification of the amino acid from R to W at position 961.
+The protein's natural variant, known as in MRXSLF;, features a modification of the amino acid from N to S at position 1007.
+The protein's natural variant, known as in OHDOX;, features a modification of the amino acid from R to H at position 1148.
+The protein's natural variant, known as in OHDOX;, features a modification of the amino acid from S to P at position 1165.
+The protein's natural variant, known as in OHDOX;, features a modification of the amino acid from H to N at position 1729.
+The protein's natural variant, known as found in a family with X-linked intellectual disability; unknown pathological significance;, features a modification of the amino acid from Q to H at position 1974.
+The protein's natural variant, known as in plastocyanin B, features a modification of the amino acid from E to D at position 53.
+The protein's natural variant, known as in NEDHCS;, features a modification of the amino acid from E to G at position 366.
+The protein's natural variant, known as in HGPPS1;, features a modification of the amino acid from L to P at position 5.
+The protein's natural variant, known as in HGPPS1;, features a modification of the amino acid from I to L at position 66.
+The protein's natural variant, known as in HGPPS1;, features a modification of the amino acid from E to K at position 319.
+The protein's natural variant, known as in HGPPS1;, features a modification of the amino acid from G to E at position 361.
+The protein's natural variant, known as in HGPPS1;, features a modification of the amino acid from R to P at position 703.
+The protein's natural variant, known as in HGPPS1;, features a modification of the amino acid from S to P at position 705.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from K to N at position 336.
+The protein's natural variant, known as in CSS11; unknown pathological significance; does not affect the interaction with SMARCC1 and SMARCA4;, features a modification of the amino acid from D to E at position 330.
+The protein's natural variant, known as in CSS11;, features a modification of the amino acid from R to G at position 446.
+The protein's natural variant, known as in CSS11; does not affect the interaction with SMARCC1 and SMARCA4;, features a modification of the amino acid from F to L at position 495.
+The protein's natural variant, known as in THMD4; affects function as shown by complementation studies in yeast;, features a modification of the amino acid from G to S at position 125.
+The protein's natural variant, known as in MCPHA; diminishes thiamine pyrophosphate transmembrane transporter activity by 70%;, features a modification of the amino acid from G to A at position 177.
+The protein's natural variant, known as in THMD4; reduced protein expression, features a modification of the amino acid from Q to H at position 192.
+The protein's natural variant, known as in strain: 1094, features a modification of the amino acid from A to K at position 249.
+The protein's natural variant, known as found in a patient with intellectual disability; unknown pathological significance;, features a modification of the amino acid from R to W at position 40.
+The protein's natural variant, known as found in patients with intellectual disability; unknown pathological significance;, features a modification of the amino acid from R to Q at position 336.
+The protein's natural variant, known as found in a patient with intellectual disability; unknown pathological significance;, features a modification of the amino acid from V to F at position 731.
+The natural variant of this protein is characterized by an amino acid alteration from D to E at position 29.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 120.
+The protein's natural variant, known as found in patients with obliterative portal venopathy; unknown pathological significance;, features a modification of the amino acid from G to R at position 595.
+The protein's natural variant, known as found in a patient with obliterative portal venopathy; unknown pathological significance;, features a modification of the amino acid from F to S at position 1415.
+The protein's natural variant, known as found in patients with obliterative portal venopathy; unknown pathological significance, features a modification of the amino acid from T to I at position 1632.
+The protein's natural variant, known as in DFNB84A, features a modification of the amino acid from R to G at position 281.
+The protein's natural variant, known as in MDS; somatic mutation; affects alternative splicing of target sequences resulting in increased splicing efficiency, exon skipping and alternative splice site utilization; no effect on localization to nuclear speckles;, features a modification of the amino acid from S to F at position 34.
+The protein's natural variant, known as in MDS; somatic mutation; affects alternative splicing of target sequences;, features a modification of the amino acid from S to Y at position 34.
+The protein's natural variant, known as in MDS; somatic mutation; affects alternative splicing of target sequences;, features a modification of the amino acid from Q to R at position 157.
+The protein's natural variant, known as in strain: RM 7004, features a modification of the amino acid from V to I at position 42.
+The protein's natural variant, known as in strain: RM 7004, features a modification of the amino acid from D to G at position 46.
+The protein's natural variant, known as in strain: RM 7004, features a modification of the amino acid from D to E at position 58.
+The protein's natural variant, known as in strain: RM 7004, features a modification of the amino acid from N to K at position 113.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from S to R at position 146.
+The protein's natural variant, known as in strain: Isolate CM-3, features a modification of the amino acid from M to I at position 39.
+The protein's natural variant, known as in a lung squamous cell carcinoma sample; somatic mutation;, features a modification of the amino acid from V to M at position 68.
+The natural variant of this protein is characterized by an amino acid alteration from T to S at position 139.
+The protein's natural variant, known as in FH; recessive, features a modification of the amino acid from R to C at position 84.
+The protein's natural variant, known as in CMS11;, features a modification of the amino acid from L to P at position 14.
+The protein's natural variant, known as in CMS11; reduced coclustering with acetylcholine receptor;, features a modification of the amino acid from V to M at position 45.
+The protein's natural variant, known as in CMS11;, features a modification of the amino acid from N to K at position 88.
+The protein's natural variant, known as in FADS2;, features a modification of the amino acid from F to S at position 139.
+The protein's natural variant, known as in CMS11; reduced coclustering with acetylcholine receptor;, features a modification of the amino acid from E to K at position 162.
+The protein's natural variant, known as in CMS11; reduced coclustering with acetylcholine receptor;, features a modification of the amino acid from R to C at position 164.
+The protein's natural variant, known as in FADS2;, features a modification of the amino acid from A to V at position 189.
+The protein's natural variant, known as in CMS11; reduced coclustering with acetylcholine receptor;, features a modification of the amino acid from L to P at position 283.
+The protein's natural variant, known as in SMDCF; the mutant is not secreted;, features a modification of the amino acid from C to F at position 87.
+The protein's natural variant, known as in SMDCF;, features a modification of the amino acid from C to R at position 123.
+The protein's natural variant, known as in SMDCF;, features a modification of the amino acid from C to W at position 225.
+The protein's natural variant, known as in SMDCF; the mutant is not secreted;, features a modification of the amino acid from Y to D at position 240.
+The protein's natural variant, known as in SMDCF; the mutant is not secreted;, features a modification of the amino acid from C to G at position 260.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from D to N at position 940.
+The protein's natural variant, known as in GFND2;, features a modification of the amino acid from Y to C at position 973.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from R to P at position 1120.
+The protein's natural variant, known as in GFND2; reduced binding to heparin, endothelial cells and podocytes; impaired capability to induce stress-fiber formation;, features a modification of the amino acid from W to R at position 1925.
+The protein's natural variant, known as in GFND2; reduced binding to heparin, endothelial cells and podocytes; impaired capability to induce stress-fiber formation;, features a modification of the amino acid from L to R at position 1974.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from D to N at position 2471.
+The protein's natural variant, known as in HAE5; decreased oligomerization; decreased interaction with TEK; fails to form proper cell-cell adhesions in an in vitro model of endothelial cell barrier;, features a modification of the amino acid from A to S at position 119.
+The protein's natural variant, known as in HAE5; unknown pathological significance; does not affect oligomerization; does not affect interaction with TEK;, features a modification of the amino acid from R to C at position 225.
+The protein's natural variant, known as in HAE5; unknown pathological significance; does not affect oligomerization; does not affect interaction with TEK;, features a modification of the amino acid from R to Q at position 494.
+The protein's natural variant, known as in HYC5; associated with disease susceptibility;, features a modification of the amino acid from H to P at position 526.
+The protein's natural variant, known as in HYC5; associated with disease susceptibility, features a modification of the amino acid from R to C at position 652.
+The protein's natural variant, known as in COXPD12;, features a modification of the amino acid from R to H at position 55.
+The protein's natural variant, known as in COXPD12;, features a modification of the amino acid from K to E at position 65.
+The protein's natural variant, known as in COXPD12;, features a modification of the amino acid from E to K at position 96.
+The protein's natural variant, known as in COXPD12;, features a modification of the amino acid from R to C at position 107.
+The protein's natural variant, known as in COXPD12;, features a modification of the amino acid from R to H at position 107.
+The protein's natural variant, known as in COXPD12;, features a modification of the amino acid from R to W at position 108.
+The protein's natural variant, known as in COXPD12;, features a modification of the amino acid from G to S at position 110.
+The protein's natural variant, known as in COXPD12;, features a modification of the amino acid from C to Y at position 167.
+The protein's natural variant, known as in COXPD12;, features a modification of the amino acid from R to G at position 168.
+The protein's natural variant, known as in COXPD12;, features a modification of the amino acid from G to S at position 204.
+The protein's natural variant, known as in COXPD12;, features a modification of the amino acid from G to S at position 224.
+The protein's natural variant, known as in COXPD12;, features a modification of the amino acid from G to C at position 317.
+The protein's natural variant, known as in COXPD12, features a modification of the amino acid from TR to L at position 427.
+The protein's natural variant, known as in COXPD12;, features a modification of the amino acid from R to Q at position 489.
+The protein's natural variant, known as in COXPD12;, features a modification of the amino acid from R to Q at position 516.
+The protein's natural variant, known as in strain: BID, DHA, MPR, features a modification of the amino acid from A to S at position 36.
+The protein's natural variant, known as in strain: MBT/Pas, PWD/Phj, features a modification of the amino acid from S to F at position 45.
+The protein's natural variant, known as in strain: DHA, features a modification of the amino acid from R to Q at position 47.
+The protein's natural variant, known as in strain: DHA, features a modification of the amino acid from V to G at position 50.
+The protein's natural variant, known as in strain: BID, DHA, MPR, MBT/Pas, PWD/Phj, features a modification of the amino acid from G to C at position 63.
+The protein's natural variant, known as in strain: BALB/c, BID, C57BL/6J, C3H/He, MBT/Pas, PWD/Phj, features a modification of the amino acid from T to A at position 65.
+The protein's natural variant, known as in strain: BID, DHA, MPR, MBT/Pas, PWD/Phj, features a modification of the amino acid from S to Y at position 83.
+The protein's natural variant, known as in strain: DHA, features a modification of the amino acid from Q to R at position 90.
+The protein's natural variant, known as in strain: MBT/Pas, PWD/Phj, features a modification of the amino acid from C to Y at position 103.
+The protein's natural variant, known as in strain: DHA, features a modification of the amino acid from V to I at position 105.
+The protein's natural variant, known as in strain: MPR, DHA, MBT/Pas, PWD/Phj, features a modification of the amino acid from C to F at position 111.
+The protein's natural variant, known as in strain: MPR, MBT/Pas, PWD/Phj, features a modification of the amino acid from H to Q at position 118.
+The protein's natural variant, known as in strain: BID, MPR, features a modification of the amino acid from L to V at position 151.
+The protein's natural variant, known as in strain: MBT/Pas, PWD/Phj, features a modification of the amino acid from P to L at position 176.
+The protein's natural variant, known as in strain: DHA, features a modification of the amino acid from K to E at position 181.
+The protein's natural variant, known as in strain: BID, MBT/Pas, PWD/Phj, features a modification of the amino acid from S to L at position 183.
+The protein's natural variant, known as in strain: BID, DHA, MBT/Pas, PWD/Phj, features a modification of the amino acid from I to T at position 184.
+The protein's natural variant, known as in strain: BALB/c, C57BL/6J, C3H/He, features a modification of the amino acid from R to Q at position 190.
+The protein's natural variant, known as in strain: MBT/Pas, PWD/Phj, features a modification of the amino acid from R to H at position 206.
+The protein's natural variant, known as in strain: BID, C3H/RV, DHA, MPR, MBT/Pas, PWD/Phj, features a modification of the amino acid from Q to R at position 266.
+The protein's natural variant, known as in strain: BID, features a modification of the amino acid from H to L at position 277.
+The protein's natural variant, known as in strain: DHA, features a modification of the amino acid from Q to P at position 278.
+The protein's natural variant, known as in strain: DHA, features a modification of the amino acid from D to V at position 291.
+The protein's natural variant, known as in strain: MPR, features a modification of the amino acid from A to V at position 299.
+The protein's natural variant, known as in strain: MPR, features a modification of the amino acid from I to V at position 305.
+The protein's natural variant, known as in strain: C3H/RV, features a modification of the amino acid from A to T at position 322.
+The protein's natural variant, known as in strain: C3H/RV, DHA, MPR, MBT/Pas, PWD/Phj, features a modification of the amino acid from S to P at position 336.
+The protein's natural variant, known as in strain: DHA, MBT/Pas, PWD/Phj, features a modification of the amino acid from G to A at position 347.
+The protein's natural variant, known as in strain: BID, DHA, MBT/Pas, PWD/Phj, features a modification of the amino acid from M to T at position 350.
+The protein's natural variant, known as in strain: BID, C3H/RV, DHA, MPR, MBT/Pas, PWD/Phj, features a modification of the amino acid from L to F at position 354.
+The protein's natural variant, known as in strain: MPR, features a modification of the amino acid from F to L at position 368.
+The protein's natural variant, known as in pnuP*144, features a modification of the amino acid from V to G at position 151.
+The protein's natural variant, known as in LIPT1D;, features a modification of the amino acid from S to F at position 71.
+The protein's natural variant, known as in LIPT1D;, features a modification of the amino acid from R to G at position 98.
+The protein's natural variant, known as in LIPT1D;, features a modification of the amino acid from T to A at position 179.
+The protein's natural variant, known as in BTH, features a modification of the amino acid from M to K at position 412.
+The protein's natural variant, known as in EPM8; unknown pathological significance, features a modification of the amino acid from L to M at position 68.
+The protein's natural variant, known as in EPM8; expressed and localized properly to the ER; impaired ceramide synthase activity;, features a modification of the amino acid from H to Q at position 183.
+The protein's natural variant, known as in DEE28;, features a modification of the amino acid from P to R at position 47.
+The protein's natural variant, known as in SCAR12;, features a modification of the amino acid from P to T at position 47.
+The protein's natural variant, known as in a Burkitt lymphoma cell line;, features a modification of the amino acid from T to S at position 111.
+The protein's natural variant, known as in a primary colorectal tumor and a histiocytic lymphoma cell line;, features a modification of the amino acid from R to W at position 120.
+The protein's natural variant, known as found in a esophageal cancer sample; somatic mutation;, features a modification of the amino acid from L to P at position 291.
+The protein's natural variant, known as in SCAR12;, features a modification of the amino acid from G to R at position 372.
+The protein's natural variant, known as in SCN3;, features a modification of the amino acid from L to R at position 130.
+The protein's natural variant, known as in SCN3; mild form;, features a modification of the amino acid from F to L at position 141.
+The protein's natural variant, known as in SCN3; likely benign variant;, features a modification of the amino acid from V to I at position 172.
+The protein's natural variant, known as in strain: cv. M9, features a modification of the amino acid from V to A at position 347.
+The protein's natural variant, known as in strain: Showa, features a modification of the amino acid from T to A at position 71.
+The natural variant of this protein is characterized by an amino acid alteration from M to V at position 247.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from H to Y at position 152.
+The natural variant of this protein is characterized by an amino acid alteration from S to P at position 225.
+The protein's natural variant, known as in CHDED;, features a modification of the amino acid from L to W at position 299.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation, features a modification of the amino acid from P to S at position 585.
+The protein's natural variant, known as in CHDED;, features a modification of the amino acid from G to R at position 592.
+The protein's natural variant, known as in a lung bronchoalveolar carcinoma sample; somatic mutation, features a modification of the amino acid from R to M at position 677.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from E to K at position 857.
+The protein's natural variant, known as in strain: DEC 1a, features a modification of the amino acid from K to T at position 37.
+The protein's natural variant, known as in strain: DEC 1a, features a modification of the amino acid from R to H at position 52.
+The protein's natural variant, known as in strain: DEC 1a, features a modification of the amino acid from I to T at position 70.
+The protein's natural variant, known as in strain: DEC 1a, features a modification of the amino acid from M to T at position 124.
+The protein's natural variant, known as in PGBM1, features a modification of the amino acid from A to P at position 18.
+The protein's natural variant, known as in PGBM1;, features a modification of the amino acid from N to S at position 387.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from D to N at position 50.
+The protein's natural variant, known as in PNH1;, features a modification of the amino acid from R to W at position 19.
+The protein's natural variant, known as in PNH1, features a modification of the amino acid from D to H at position 40.
+The protein's natural variant, known as in PNH1, features a modification of the amino acid from G to A at position 48.
+The protein's natural variant, known as in PNH1, features a modification of the amino acid from G to D at position 48.
+The protein's natural variant, known as in PNH1, features a modification of the amino acid from G to V at position 48.
+The protein's natural variant, known as in MCAHS2;, features a modification of the amino acid from R to L at position 77.
+The protein's natural variant, known as in NEDEPH; does not fully rescue defective HAMP expression in PIGA-deficient cells overexpressing HJV, suggesting decreased function in GPI anchor biosynthesis and absent or reduced HJV anchorage at the cell membrane, features a modification of the amino acid from R to Q at position 77.
+The protein's natural variant, known as in MCAHS2;, features a modification of the amino acid from P to L at position 93.
+The protein's natural variant, known as in MCAHS2;, features a modification of the amino acid from R to W at position 119.
+The protein's natural variant, known as in NEDEPH; unknown pathological significance, features a modification of the amino acid from S to L at position 127.
+The protein's natural variant, known as in PNH1, features a modification of the amino acid from H to R at position 128.
+The protein's natural variant, known as probable disease-associated variant found in a patient with infantile onset epileptic encephalopathy with dyskinesia and microcephaly, features a modification of the amino acid from A to V at position 135.
+The protein's natural variant, known as in PNH1, features a modification of the amino acid from S to F at position 155.
+The protein's natural variant, known as in MCAHS2;, features a modification of the amino acid from I to F at position 206.
+The protein's natural variant, known as in PNH1, features a modification of the amino acid from G to R at position 239.
+The protein's natural variant, known as in PNH1, features a modification of the amino acid from N to D at position 297.
+The protein's natural variant, known as in NEDEPH; does not fully rescue defective HAMP expression in PIGA-deficient cells overexpressing HJV, suggesting decreased function in GPI anchor biosynthesis and absent or reduced HJV anchorage at the cell membrane, features a modification of the amino acid from L to P at position 344.
+The protein's natural variant, known as in MCAHS2; unknown pathological significance, features a modification of the amino acid from L to S at position 355.
+The protein's natural variant, known as in SPGF64; unknown pathological significance, features a modification of the amino acid from E to G at position 98.
+The protein's natural variant, known as in SPGF64; unknown pathological significance, features a modification of the amino acid from G to A at position 149.
+The protein's natural variant, known as in SPGF64; unknown pathological significance, features a modification of the amino acid from I to L at position 250.
+The protein's natural variant, known as in SPGF64; unknown pathological significance, features a modification of the amino acid from E to G at position 594.
+The protein's natural variant, known as in SPGF64; unknown pathological significance;, features a modification of the amino acid from G to D at position 664.
+The protein's natural variant, known as in RP46;, features a modification of the amino acid from L to P at position 132.
+The protein's natural variant, known as in GPIBD18; partial loss of function; when tested in PIGS-knockout cells, mediates partial restoration of GPI-anchored protein expression at the cell surface;, features a modification of the amino acid from L to P at position 34.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from M to I at position 159.
+The protein's natural variant, known as in GPIBD18;, features a modification of the amino acid from E to G at position 308.
+The protein's natural variant, known as in GPIBD18; unknown pathological significance, features a modification of the amino acid from TTTLTSLAQLLGK to RLL at position 451.
+The protein's natural variant, known as in CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit, features a modification of the amino acid from S to N at position 9.
+The protein's natural variant, known as in CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit;, features a modification of the amino acid from R to C at position 74.
+The protein's natural variant, known as in CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit, features a modification of the amino acid from R to S at position 146.
+The protein's natural variant, known as in ACRDYS1; reduces PKA activity; decreases cAMP binding, features a modification of the amino acid from Y to C at position 175.
+The protein's natural variant, known as in CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit, features a modification of the amino acid from D to Y at position 183.
+The protein's natural variant, known as in CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit; reduces protein degradation;, features a modification of the amino acid from A to D at position 213.
+The protein's natural variant, known as in ACRDYS1; reduces PKA activity; decreases cAMP binding; reduces protein degradation, features a modification of the amino acid from A to T at position 213.
+The natural variant of this protein is characterized by an amino acid alteration from D to N at position 227.
+The protein's natural variant, known as in ACRDYS1; impairs response of PKA to c-AMP, features a modification of the amino acid from T to A at position 239.
+The protein's natural variant, known as in ACRDYS1; reduces PKA activity; decreases cAMP binding;, features a modification of the amino acid from Q to R at position 285.
+The protein's natural variant, known as in ACRDYS1; reduces PKA activity; decreases cAMP binding; reduces protein degradation, features a modification of the amino acid from G to E at position 289.
+The protein's natural variant, known as in CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit; accelerates protein degradation, features a modification of the amino acid from G to W at position 289.
+The protein's natural variant, known as in ACRDYS1;, features a modification of the amino acid from I to T at position 327.
+The protein's natural variant, known as in ACRDYS1; disrupts cAMP binding, features a modification of the amino acid from A to V at position 328.
+The protein's natural variant, known as in ACRDYS1; disrupts cAMP binding, features a modification of the amino acid from R to L at position 335.
+The protein's natural variant, known as in ACRDYS1;, features a modification of the amino acid from R to P at position 335.
+The protein's natural variant, known as in ACRDYS1, features a modification of the amino acid from Y to C at position 373.
+The protein's natural variant, known as in ACRDYS1;, features a modification of the amino acid from Y to H at position 373.
+The protein's natural variant, known as in XP-A, features a modification of the amino acid from P to L at position 94.
+The protein's natural variant, known as in XP-A; severe form;, features a modification of the amino acid from C to F at position 108.
+The protein's natural variant, known as in XP-A;, features a modification of the amino acid from R to K at position 130.
+The protein's natural variant, known as in XP-A;, features a modification of the amino acid from Q to H at position 185.
+The protein's natural variant, known as in XP-A; mild form;, features a modification of the amino acid from H to R at position 244.
+The protein's natural variant, known as in strain: BALB/cJ, features a modification of the amino acid from T to A at position 164.
+The protein's natural variant, known as in SCN6;, features a modification of the amino acid from G to S at position 14.
+The protein's natural variant, known as in SCN6;, features a modification of the amino acid from R to Q at position 20.
+The protein's natural variant, known as in SCN6;, features a modification of the amino acid from E to D at position 21.
+The protein's natural variant, known as in SCN6;, features a modification of the amino acid from H to Y at position 44.
+The protein's natural variant, known as in SCN6;, features a modification of the amino acid from Q to R at position 162.
+The protein's natural variant, known as in CILD2;, features a modification of the amino acid from L to P at position 61.
+The protein's natural variant, known as in EPM6 and MYOS; no effect on protein stability; loss of localization to the cis-Golgi network membrane; loss of function; unable to rescue the yeast strain lacking the ortholog Bos1;, features a modification of the amino acid from G to W at position 144.
+The protein's natural variant, known as in PULAM;, features a modification of the amino acid from G to R at position 106.
+The protein's natural variant, known as in strain: Eagan, features a modification of the amino acid from V to A at position 21.
+The protein's natural variant, known as in strain: Eagan, features a modification of the amino acid from T to A at position 276.
+The natural variant of this protein is characterized by an amino acid alteration from K to T at position 11.
+The natural variant of this protein is characterized by an amino acid alteration from R to K at position 40.
+The natural variant of this protein is characterized by an amino acid alteration from T to S at position 55.
+The protein's natural variant, known as in NPHP16;, features a modification of the amino acid from A to P at position 312.
+The protein's natural variant, known as in NPHP16;, features a modification of the amino acid from Q to R at position 441.
+The protein's natural variant, known as in allele DTC24; dorsalized embryos, features a modification of the amino acid from T to I at position 429.
+The protein's natural variant, known as requires 2 nucleotide substitutions, features a modification of the amino acid from G to P at position 193.
+The protein's natural variant, known as in fraction 5 and in 10% of fraction 2, features a modification of the amino acid from I to T at position 19.
+The protein's natural variant, known as in fraction 5 and in 10% of fraction 2, features a modification of the amino acid from L to F at position 25.
+The protein's natural variant, known as in 90% of fraction 2, 20% of fraction 3 and 78% of fraction 4, features a modification of the amino acid from L to K at position 25.
+The protein's natural variant, known as in fraction 5, features a modification of the amino acid from K to R at position 33.
+The protein's natural variant, known as probable disease-associated variant found in a patient with limb-girdle muscular dystrophy;, features a modification of the amino acid from D to A at position 43.
+The protein's natural variant, known as in BTHLM1;, features a modification of the amino acid from K to R at position 121.
+The protein's natural variant, known as in BTHLM1;, features a modification of the amino acid from G to D at position 272.
+The protein's natural variant, known as in BTHLM1;, features a modification of the amino acid from P to L at position 274.
+The protein's natural variant, known as in BTHLM1;, features a modification of the amino acid from G to R at position 275.
+The protein's natural variant, known as in UCMD1;, features a modification of the amino acid from G to R at position 281.
+The protein's natural variant, known as in UCMD1; fibroblasts with the mutation assembled and secreted normal collagen VI microfibrils; cell adhesion of heterozygous Arg-284 fibroblasts is markedly decreased but can be rescued by the addition of normal collagen VI;, features a modification of the amino acid from G to R at position 284.
+The protein's natural variant, known as in BTHLM1 and UCMD1;, features a modification of the amino acid from G to R at position 290.
+The protein's natural variant, known as in BTHLM1, features a modification of the amino acid from G to V at position 305.
+The protein's natural variant, known as in BTHLM1;, features a modification of the amino acid from G to D at position 341.
+The protein's natural variant, known as in BTHLM1;, features a modification of the amino acid from G to V at position 341.
+The protein's natural variant, known as in BTHLM1;, features a modification of the amino acid from K to T at position 571.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from KH to NQ at position 28.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from I to V at position 48.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from S to G at position 66.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from KAEVFC to RAAVFY at position 78.
+The protein's natural variant, known as in plasmid pCP301, features a modification of the amino acid from K to R at position 73.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from R to Q at position 97.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from N to D at position 107.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from H to N at position 110.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from TK to SE at position 137.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from D to N at position 144.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from GPV to EPI at position 154.
+The protein's natural variant, known as in plasmid pCP301, features a modification of the amino acid from N to D at position 155.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from SHH to NYN at position 161.
+The protein's natural variant, known as in plasmid pCP301 and plasmid pINV_F6_M1382, features a modification of the amino acid from S to G at position 166.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from RD to SK at position 201.
+The protein's natural variant, known as in plasmid pCP301, features a modification of the amino acid from R to S at position 200.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from V to A at position 252.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from P to Q at position 260.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from S to K at position 300.
+The protein's natural variant, known as in plasmid pCP301, features a modification of the amino acid from S to N at position 300.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from G to E at position 304.
+The protein's natural variant, known as in plasmid pCP301 and plasmid pINV_F6_M1382, features a modification of the amino acid from G to E at position 311.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from K to Q at position 325.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from S to K at position 328.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from D to G at position 359.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from VNN to LNK at position 407.
+The protein's natural variant, known as in plasmid pCP301, features a modification of the amino acid from NN to TK at position 407.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from VT to MA at position 425.
+The protein's natural variant, known as in plasmid pCP301, features a modification of the amino acid from V to M at position 424.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from S to A at position 519.
+The protein's natural variant, known as in second chain, features a modification of the amino acid from A to T at position 130.
+The protein's natural variant, known as in MTDPS16; decreased function in mitochondrial DNA replication; decreased protein stability; no effect on DNA binding;, features a modification of the amino acid from R to W at position 182.
+The protein's natural variant, known as no functional deficit;, features a modification of the amino acid from G to A at position 416.
+The protein's natural variant, known as in MTDPS16B; decreased DNA polymerase processivity factor activity; results in decreased stability; affects the secondary structure as shown by circular dichroism spectroscopy, features a modification of the amino acid from D to Y at position 433.
+The protein's natural variant, known as in PEOA4; affects stimulation of the catalytic subunit;, features a modification of the amino acid from G to E at position 451.
+The protein's natural variant, known as in CATIFA; patient cells contain normally spliced transcripts corresponding to protein variant P-1265 but also transcripts that fail to splice due to intron 24 retention leading to a stop codon at position 1266; loss-of-function variant affecting procollagen secretion, features a modification of the amino acid from R to P at position 1265.
+The protein's natural variant, known as in Co(A-B-) antigen; non functional AQP1; red cells show low osmotic water permeability;, features a modification of the amino acid from P to L at position 38.
+The protein's natural variant, known as in Co(A-B+) antigen;, features a modification of the amino acid from A to V at position 45.
+The natural variant of this protein is characterized by an amino acid alteration from Q to QQQQQQ at position 80.
+The protein's natural variant, known as in ZLS3; gain-of-function variant leading to increased channel sensitivity to calcium and faster channel activation; does not affect interaction with CALM1;, features a modification of the amino acid from K to E at position 269.
+The protein's natural variant, known as in ZLS3; gain-of-function variant leading to increased channel sensitivity to calcium and faster channel activation; does not affect interaction with CALM1;, features a modification of the amino acid from G to D at position 350.
+The protein's natural variant, known as in ZLS3; gain-of-function variant leading to increased channel sensitivity to calcium and faster channel activation; does not affect interaction with CALM1;, features a modification of the amino acid from S to C at position 436.
+The protein's natural variant, known as found in a family with non-cirrhotic portal hypertension; unknown pathological significance; gain-of-function variant leading to constitutive activity with very low calcium levels; does not affect interaction with CALM1, features a modification of the amino acid from V to L at position 450.
+The protein's natural variant, known as in strain: Isolate USNM_575170, features a modification of the amino acid from I to V at position 238.
+The protein's natural variant, known as found in a patient with bipolar disorder; has no significant effect on monoamine vesicular uptake;, features a modification of the amino acid from Q to R at position 10.
+The protein's natural variant, known as found in patients with bipolar disorder; increases the vesicular uptake of noradrenaline and dopamine;, features a modification of the amino acid from F to S at position 84.
+The protein's natural variant, known as found in a patient with bipolar disorder; decreases the vesicular uptake of noradrenaline, dopamine and serotonin;, features a modification of the amino acid from A to P at position 101.
+The protein's natural variant, known as decreases the vesicular uptake of noradrenaline, dopamine and serotonin; may predispose carriers to a increased cortical response to negative stimuli and reduced threat-related amygdala reactivity;, features a modification of the amino acid from I to T at position 136.
+The protein's natural variant, known as found in patients with bipolar disorder; decreases the vesicular uptake of noradrenaline, dopamine and serotonin;, features a modification of the amino acid from R to L at position 138.
+The protein's natural variant, known as decreases the vesicular uptake of noradrenaline and dopamine;, features a modification of the amino acid from L to V at position 392.
+The protein's natural variant, known as in CDG1C;, features a modification of the amino acid from Y to H at position 131.
+The protein's natural variant, known as in CDG1C, features a modification of the amino acid from S to I at position 170.
+The protein's natural variant, known as in CDG1C;, features a modification of the amino acid from G to E at position 227.
+The protein's natural variant, known as may act as disease modifier and exacerbate clinical severity in patients with a congenital disorder of glycosylation; slightly decreased function as shown by rescue experiments of defective glycosylation in an alg6-deficient S.cerevisiae strain;, features a modification of the amino acid from S to F at position 304.
+The protein's natural variant, known as in CDG1C, features a modification of the amino acid from S to R at position 308.
+The protein's natural variant, known as in CDG1C;, features a modification of the amino acid from A to V at position 333.
+The protein's natural variant, known as in CDG1C;, features a modification of the amino acid from S to P at position 478.
+The protein's natural variant, known as in strain: EC47, EC49, EC50 and RT272, features a modification of the amino acid from D to N at position 71.
+The protein's natural variant, known as in strain: ECOR 27 and RT082, features a modification of the amino acid from A to S at position 106.
+The protein's natural variant, known as in strain: MB001D, features a modification of the amino acid from A to P at position 209.
+The protein's natural variant, known as in strain: A8190, E2666-74, E830587, E851819, E3406, EC10, EC14, EC32, EC35, EC38, EC40, EC44, EC46, EC47, EC49, EC50, EC52, EC58, E64 and EC70, features a modification of the amino acid from A to R at position 218.
+The protein's natural variant, known as in strain: ECOR37, features a modification of the amino acid from A to T at position 232.
+The protein's natural variant, known as in strain: RT083, features a modification of the amino acid from V to I at position 249.
+The protein's natural variant, known as in strain: EC35, EC38, EC40, EC44, EC46, EC47 and RT272, features a modification of the amino acid from Q to K at position 289.
+The protein's natural variant, known as in strain: E2666-74, ECOR 27, ECOR 45, RL012A, RT104 and RT174, features a modification of the amino acid from N to S at position 290.
+The protein's natural variant, known as in strain: EC35, features a modification of the amino acid from A to S at position 291.
+The protein's natural variant, known as in strain: ECOR 45, features a modification of the amino acid from G to A at position 294.
+The protein's natural variant, known as in strain: E830587, features a modification of the amino acid from D to N at position 297.
+The protein's natural variant, known as in SRTD19;, features a modification of the amino acid from L to F at position 29.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from E to D at position 23.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from T to M at position 205.
+The protein's natural variant, known as in ECTD12; unknown pathological significance;, features a modification of the amino acid from F to L at position 251.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to H at position 312.
+The natural variant of this protein is characterized by an amino acid alteration from P to R at position 542.
+The protein's natural variant, known as in ATFB11;, features a modification of the amino acid from V to I at position 85.
+The protein's natural variant, known as in ATRST1; somatic;, features a modification of the amino acid from P to S at position 88.
+The protein's natural variant, known as in ATRST1;, features a modification of the amino acid from A to S at position 96.
+The protein's natural variant, known as in ATFB11;, features a modification of the amino acid from L to I at position 221.
+The protein's natural variant, known as in ATFB11;, features a modification of the amino acid from L to M at position 229.
+The natural variant of this protein is characterized by an amino acid alteration from R to K at position 15.
+The natural variant of this protein is characterized by an amino acid alteration from P to F at position 20.
+The protein's natural variant, known as in FANCT; abolishes FANCD2 monoubiquitination; abolishes interaction with FANCL;, features a modification of the amino acid from Q to E at position 2.
+The protein's natural variant, known as detected in a patient with mitochondrial complex I deficiency; uncertain pathological significance;, features a modification of the amino acid from P to S at position 96.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from F to L at position 606.
+The protein's natural variant, known as in IMGT allele IGKV1-5*01; requires 2 nucleotide substitutions, features a modification of the amino acid from K to D at position 72.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from A to G at position 147.
+The protein's natural variant, known as in MYONRI; affects regulation of muscle contraction, features a modification of the amino acid from D to Y at position 34.
+The protein's natural variant, known as in MYONRI; affects regulation of muscle contraction, features a modification of the amino acid from M to I at position 79.
+The natural variant of this protein is characterized by an amino acid alteration from M to T at position 57.
+The protein's natural variant, known as in CHIME;, features a modification of the amino acid from L to P at position 167.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from P to S at position 927.
+The protein's natural variant, known as in NEDLIB; unknown pathological significance; decreased localization to cell membrane, features a modification of the amino acid from G to E at position 47.
+The protein's natural variant, known as in NEDLIB; severe decrease of ionotropic glutamate receptor activity;, features a modification of the amino acid from D to G at position 302.
+The protein's natural variant, known as in NEDLIB;, features a modification of the amino acid from P to T at position 528.
+The protein's natural variant, known as in NEDLIB; homomeric channels show increased ionotropic glutamate receptor activity; decreased localization to cell membrane, features a modification of the amino acid from Q to E at position 607.
+The protein's natural variant, known as in RNA edited version;, features a modification of the amino acid from Q to R at position 607.
+The protein's natural variant, known as in NEDLIB; loss of ionotropic glutamate receptor activity; no effect on localization to cell membrane;, features a modification of the amino acid from G to R at position 609.
+The protein's natural variant, known as in NEDLIB;, features a modification of the amino acid from D to N at position 611.
+The protein's natural variant, known as in NEDLIB; reduced ionotropic glutamate receptor activity; decreased localization to cell membrane;, features a modification of the amino acid from A to S at position 639.
+The protein's natural variant, known as in NEDLIB; reduced ionotropic glutamate receptor activity, features a modification of the amino acid from F to L at position 644.
+The protein's natural variant, known as in NEDLIB; reduced ionotropic glutamate receptor activity, features a modification of the amino acid from T to N at position 646.
+The protein's natural variant, known as in NEDLIB, features a modification of the amino acid from V to L at position 647.
+The protein's natural variant, known as in NEDLIB, features a modification of the amino acid from E to D at position 776.
+The protein's natural variant, known as in NEDLIB, features a modification of the amino acid from W to L at position 788.
+The protein's natural variant, known as in NEDLIB, features a modification of the amino acid from G to V at position 792.
+The protein's natural variant, known as in NEDLIB, features a modification of the amino acid from A to V at position 807.
+The protein's natural variant, known as in NEDLIB, features a modification of the amino acid from N to S at position 812.
+The protein's natural variant, known as in strain: 2.6.1 / French, features a modification of the amino acid from S to P at position 42.
+The protein's natural variant, known as confers susceptibility to neuroblastoma; found as germline mutation in a neuroblastoma family;, features a modification of the amino acid from R to L at position 100.
+The protein's natural variant, known as in CCHS1;, features a modification of the amino acid from R to Q at position 141.
+The protein's natural variant, known as in CCHS1, features a modification of the amino acid from Q to R at position 143.
+The protein's natural variant, known as confers susceptibility to neuroblastoma;, features a modification of the amino acid from G to D at position 197.
+The protein's natural variant, known as in CCHS1, features a modification of the amino acid from A to AAAAAAAAAAA at position 241.
+The protein's natural variant, known as rare variant found in a patient with microphthalmia with limb anomalies; unknown pathological significance;, features a modification of the amino acid from T to M at position 228.
+The protein's natural variant, known as in strain: 65, 66 and D, features a modification of the amino acid from F to V at position 90.
+The protein's natural variant, known as in SGMRT2; results in constitutive activation and enhanced interferon-mediated signaling;, features a modification of the amino acid from C to F at position 268.
+The protein's natural variant, known as in SGMRT2; results in constitutive activation and enhanced interferon-mediated signaling;, features a modification of the amino acid from E to A at position 373.
+The protein's natural variant, known as in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type, features a modification of the amino acid from L to F at position 35.
+The protein's natural variant, known as in MPS3B; decreases the enzyme activity markedly;, features a modification of the amino acid from R to W at position 38.
+The protein's natural variant, known as in MPS3B;, features a modification of the amino acid from F to C at position 48.
+The protein's natural variant, known as in MPS3B; associated with a partially degraded polypeptide in a 16-hour chase experiment suggesting that L-48 NAGLU affects the processing and stability of the gene; some L-48 NAGLU is being correctly sorted to the lysosomal compartment;, features a modification of the amino acid from F to L at position 48.
+The protein's natural variant, known as in MPS3B, features a modification of the amino acid from G to S at position 69.
+The protein's natural variant, known as in MPS3B; decreases the enzyme activity markedly;, features a modification of the amino acid from V to G at position 77.
+The protein's natural variant, known as in MPS3B, features a modification of the amino acid from G to C at position 79.
+The protein's natural variant, known as in MPS3B;, features a modification of the amino acid from G to S at position 79.
+The protein's natural variant, known as in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type;, features a modification of the amino acid from G to D at position 82.
+The protein's natural variant, known as in MPS3B;, features a modification of the amino acid from Y to H at position 92.
+The protein's natural variant, known as in MPS3B, features a modification of the amino acid from H to R at position 100.
+The protein's natural variant, known as in MPS3B;, features a modification of the amino acid from P to S at position 115.
+The protein's natural variant, known as in MPS3B; does not yield active enzyme, features a modification of the amino acid from R to C at position 130.
+The protein's natural variant, known as in MPS3B;, features a modification of the amino acid from Y to C at position 140.
+The protein's natural variant, known as in MPS3B, features a modification of the amino acid from E to K at position 153.
+The protein's natural variant, known as in MPS3B; does not yield active enzyme;, features a modification of the amino acid from I to R at position 154.
+The protein's natural variant, known as in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type, features a modification of the amino acid from W to C at position 156.
+The protein's natural variant, known as in MPS3B;, features a modification of the amino acid from H to P at position 227.
+The protein's natural variant, known as in MPS3B;, features a modification of the amino acid from R to C at position 234.
+The protein's natural variant, known as in MPS3B, features a modification of the amino acid from V to M at position 241.
+The protein's natural variant, known as in MPS3B; no enzyme activity, features a modification of the amino acid from L to P at position 242.
+The protein's natural variant, known as in MPS3B, features a modification of the amino acid from P to L at position 243.
+The protein's natural variant, known as in MPS3B; produces 12.7% residual enzyme activity, features a modification of the amino acid from A to P at position 246.
+The protein's natural variant, known as in MPS3B;, features a modification of the amino acid from H to R at position 248.
+The protein's natural variant, known as in MPS3B, features a modification of the amino acid from W to R at position 268.
+The protein's natural variant, known as in MPS3B, features a modification of the amino acid from C to F at position 277.
+The protein's natural variant, known as in MPS3B;, features a modification of the amino acid from L to P at position 280.
+The protein's natural variant, known as in MPS3B;, features a modification of the amino acid from G to R at position 292.
+The protein's natural variant, known as in MPS3B; does not yield active enzyme;, features a modification of the amino acid from Y to C at position 309.
+The protein's natural variant, known as in MPS3B;, features a modification of the amino acid from F to L at position 314.
+The protein's natural variant, known as in MPS3B;, features a modification of the amino acid from V to F at position 334.
+The protein's natural variant, known as in MPS3B; decreases the enzyme activity markedly;, features a modification of the amino acid from Y to C at position 335.
+The protein's natural variant, known as in MPS3B;, features a modification of the amino acid from P to L at position 358.
+The protein's natural variant, known as in CMT2V;, features a modification of the amino acid from I to T at position 403.
+The protein's natural variant, known as in MPS3B;, features a modification of the amino acid from F to S at position 410.
+The protein's natural variant, known as in MPS3B; does not yield active enzyme, features a modification of the amino acid from G to E at position 412.
+The protein's natural variant, known as in MPS3B; no enzyme activity;, features a modification of the amino acid from H to R at position 414.
+The protein's natural variant, known as in MPS3B, features a modification of the amino acid from T to I at position 437.
+The protein's natural variant, known as in MPS3B; no enzyme activity;, features a modification of the amino acid from E to K at position 446.
+The protein's natural variant, known as in MPS3B;, features a modification of the amino acid from E to K at position 452.
+The protein's natural variant, known as in MPS3B;, features a modification of the amino acid from Y to C at position 455.
+The protein's natural variant, known as in MPS3B, features a modification of the amino acid from W to G at position 474.
+The protein's natural variant, known as in MPS3B; no enzyme activity;, features a modification of the amino acid from R to Q at position 482.
+The protein's natural variant, known as in MPS3B;, features a modification of the amino acid from R to W at position 482.
+The protein's natural variant, known as in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type, features a modification of the amino acid from V to G at position 501.
+The protein's natural variant, known as in MPS3B; no enzyme activity;, features a modification of the amino acid from P to L at position 516.
+The protein's natural variant, known as in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type;, features a modification of the amino acid from R to W at position 520.
+The protein's natural variant, known as in MPS3B; accounts for approximately 6% of mutations in Australasian patients with MPS3B;, features a modification of the amino acid from P to L at position 521.
+The protein's natural variant, known as in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type, features a modification of the amino acid from S to Y at position 534.
+The protein's natural variant, known as in MPS3B; unknown pathological significance, features a modification of the amino acid from L to P at position 550.
+The protein's natural variant, known as in MPS3B, features a modification of the amino acid from L to P at position 560.
+The protein's natural variant, known as in MPS3B, features a modification of the amino acid from L to R at position 561.
+The protein's natural variant, known as in MPS3B; does not yield active enzyme;, features a modification of the amino acid from R to P at position 565.
+The protein's natural variant, known as in MPS3B;, features a modification of the amino acid from R to Q at position 565.
+The protein's natural variant, known as in MPS3B; accounts for approximately 6% of the mutant alleles in Australasian patients with MPS3B;, features a modification of the amino acid from R to W at position 565.
+The protein's natural variant, known as in MPS3B;, features a modification of the amino acid from L to P at position 591.
+The protein's natural variant, known as in MPS3B;, features a modification of the amino acid from S to G at position 612.
+The protein's natural variant, known as in MPS3B;, features a modification of the amino acid from L to F at position 617.
+The protein's natural variant, known as in MPS3B; accounts for approximately 20% of MPS3B alleles in a Dutch patient group;, features a modification of the amino acid from R to C at position 643.
+The protein's natural variant, known as in MPS3B;, features a modification of the amino acid from R to H at position 643.
+The protein's natural variant, known as in MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type, features a modification of the amino acid from W to C at position 649.
+The protein's natural variant, known as in MPS3B;, features a modification of the amino acid from G to E at position 650.
+The protein's natural variant, known as in MPS3B, features a modification of the amino acid from Y to F at position 658.
+The protein's natural variant, known as in MPS3B;, features a modification of the amino acid from A to V at position 664.
+The protein's natural variant, known as in MPS3B;, features a modification of the amino acid from R to C at position 674.
+The protein's natural variant, known as in MPS3B;, features a modification of the amino acid from R to H at position 674.
+The protein's natural variant, known as in MPS3B, features a modification of the amino acid from R to P at position 676.
+The protein's natural variant, known as in MPS3B, features a modification of the amino acid from L to R at position 682.
+The protein's natural variant, known as in MPS3B;, features a modification of the amino acid from E to K at position 705.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from K to R at position 100.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from T to R at position 441.
+The protein's natural variant, known as in H42, features a modification of the amino acid from N to K at position 49.
+The protein's natural variant, known as in MRXSP; unknown pathological significance, features a modification of the amino acid from F to S at position 47.
+The protein's natural variant, known as in MRXSP; mutant channels show severely decreased sensitivity to glycine and are unable to respond to physiological glycine levels; results in reduced protein expression; reduced localization to the cell membrane;, features a modification of the amino acid from N to S at position 136.
+The protein's natural variant, known as in MRXSP; fails to rescue abnormal outgrowth of spinal motor neuron axons in zebrafish morphants; mutant channels show severely decreased sensitivity to glycine and are unable to respond to physiological glycine levels; results in reduced protein expression; reduced localization to the cell membrane, features a modification of the amino acid from R to Q at position 153.
+The protein's natural variant, known as in MRXSP; unknown pathological significance;, features a modification of the amino acid from R to C at position 252.
+The protein's natural variant, known as in MRXSP; unknown pathological significance, features a modification of the amino acid from I to M at position 259.
+The protein's natural variant, known as in MRXSP; unknown pathological significance, features a modification of the amino acid from A to T at position 288.
+The protein's natural variant, known as in MRXSP;, features a modification of the amino acid from T to M at position 296.
+The protein's natural variant, known as in MRXSP; affects channel activity; results in slower channel closing and increased conductance consistent with a gain-of-function effect; results in prolonged inhibitory post-synaptic currents, features a modification of the amino acid from R to L at position 350.
+The protein's natural variant, known as in MRXSP; unknown pathological significance;, features a modification of the amino acid from P to T at position 396.
+The protein's natural variant, known as in MRXSP; unknown pathological significance;, features a modification of the amino acid from P to L at position 400.
+The protein's natural variant, known as in MRXSP; unknown pathological significance;, features a modification of the amino acid from R to Q at position 445.
+The protein's natural variant, known as in LICAS; unknown pathological significance, features a modification of the amino acid from W to S at position 305.
+The protein's natural variant, known as in FANCD2;, features a modification of the amino acid from S to G at position 126.
+The protein's natural variant, known as in FANCD2;, features a modification of the amino acid from R to W at position 302.
+The protein's natural variant, known as in FANCD2; no effect on ubiquitination;, features a modification of the amino acid from R to H at position 1236.
+The protein's natural variant, known as in AHC2;, features a modification of the amino acid from S to F at position 137.
+The protein's natural variant, known as in AHC2; strong decrease in ATPase activity;, features a modification of the amino acid from S to Y at position 137.
+The protein's natural variant, known as in AHC2;, features a modification of the amino acid from Q to L at position 140.
+The protein's natural variant, known as in AHC2; no effect on ATPase activity;, features a modification of the amino acid from D to N at position 220.
+The protein's natural variant, known as in AHC2; strong decrease in ATPase activity;, features a modification of the amino acid from I to N at position 274.
+The protein's natural variant, known as in DYT12;, features a modification of the amino acid from I to T at position 274.
+The protein's natural variant, known as in DYT12;, features a modification of the amino acid from E to K at position 277.
+The protein's natural variant, known as in DEE99; decreased affinity for sodium ions; decreased affinity for potassium ions, features a modification of the amino acid from L to R at position 292.
+The protein's natural variant, known as in DEE99; decreased affinity for sodium ions; decreased affinity for potassium ions, features a modification of the amino acid from G to V at position 316.
+The protein's natural variant, known as probable disease-associated variant found in a patient with tonic-clonic seizures associated with profound developmental delay and paroxysmal movement disorder;, features a modification of the amino acid from A to T at position 320.
+The protein's natural variant, known as in AHC2;, features a modification of the amino acid from V to D at position 322.
+The protein's natural variant, known as in AHC2; decreased ATPase activity;, features a modification of the amino acid from C to F at position 333.
+The protein's natural variant, known as in DEE99, features a modification of the amino acid from S to P at position 361.
+The protein's natural variant, known as in AHC2;, features a modification of the amino acid from L to P at position 371.
+The protein's natural variant, known as in DEE99, features a modification of the amino acid from D to Y at position 609.
+The protein's natural variant, known as in DYT12;, features a modification of the amino acid from T to M at position 613.
+The protein's natural variant, known as in AHC2;, features a modification of the amino acid from G to C at position 755.
+The protein's natural variant, known as in AHC2;, features a modification of the amino acid from G to S at position 755.
+The protein's natural variant, known as in DYT12;, features a modification of the amino acid from I to S at position 758.
+The protein's natural variant, known as in AHC2;, features a modification of the amino acid from S to R at position 772.
+The protein's natural variant, known as in AHC2;, features a modification of the amino acid from N to I at position 773.
+The protein's natural variant, known as in AHC2;, features a modification of the amino acid from N to S at position 773.
+The protein's natural variant, known as in DEE99, features a modification of the amino acid from P to R at position 775.
+The protein's natural variant, known as in DYT12;, features a modification of the amino acid from F to L at position 780.
+The protein's natural variant, known as in AHC2 and DEE99; strong decrease in ATPase activity;, features a modification of the amino acid from D to N at position 801.
+The protein's natural variant, known as in DYT12;, features a modification of the amino acid from D to Y at position 801.
+The protein's natural variant, known as in AHC2;, features a modification of the amino acid from M to R at position 806.
+The protein's natural variant, known as in AHC2;, features a modification of the amino acid from I to S at position 810.
+The protein's natural variant, known as in AHC2; decreased ATPase activity;, features a modification of the amino acid from S to P at position 811.
+The protein's natural variant, known as in AHC2; strong decrease in ATPase activity;, features a modification of the amino acid from E to K at position 815.
+The protein's natural variant, known as in CAPOS;, features a modification of the amino acid from E to K at position 818.
+The protein's natural variant, known as in DEE99; decreased sodium/potassium-exchanging ATPase activity, features a modification of the amino acid from D to Y at position 887.
+The protein's natural variant, known as in DEE99, features a modification of the amino acid from L to P at position 888.
+The protein's natural variant, known as in DEE99, features a modification of the amino acid from G to W at position 893.
+The protein's natural variant, known as in DYT12;, features a modification of the amino acid from D to N at position 923.
+The protein's natural variant, known as in AHC2;, features a modification of the amino acid from D to Y at position 923.
+The protein's natural variant, known as in DEE99;, features a modification of the amino acid from L to P at position 924.
+The protein's natural variant, known as in AHC2;, features a modification of the amino acid from C to Y at position 927.
+The protein's natural variant, known as in AHC2; strong decrease in ATPase activity;, features a modification of the amino acid from G to R at position 947.
+The protein's natural variant, known as in AHC2;, features a modification of the amino acid from A to D at position 955.
+The protein's natural variant, known as in AHC2;, features a modification of the amino acid from D to Y at position 992.
+The protein's natural variant, known as in DYT12; there is a drastic 40- to 50-fold reduction in Na(+) affinity in the mutant protein, features a modification of the amino acid from Y to YY at position 1013.
+The protein's natural variant, known as in atrazine-resistant cell line, features a modification of the amino acid from S to T at position 264.
+The protein's natural variant, known as in JBTS20;, features a modification of the amino acid from D to N at position 209.
+The protein's natural variant, known as in MKS11;, features a modification of the amino acid from Q to P at position 272.
+The protein's natural variant, known as in MC1DN3;, features a modification of the amino acid from V to M at position 122.
+The protein's natural variant, known as found in a patient with Leigh syndrome; unknown pathological significance; decrease in enzyme activity;, features a modification of the amino acid from R to H at position 145.
+The protein's natural variant, known as in strain: Taka5, features a modification of the amino acid from F to L at position 2.
+The protein's natural variant, known as in MC4DN10;, features a modification of the amino acid from M to I at position 19.
+The protein's natural variant, known as in AOS5;, features a modification of the amino acid from C to R at position 429.
+The protein's natural variant, known as in AOS5;, features a modification of the amino acid from C to Y at position 1496.
+The protein's natural variant, known as in AOS5;, features a modification of the amino acid from D to N at position 1989.
+The protein's natural variant, known as in plasmid Rts1 and strain X, features a modification of the amino acid from K to R at position 27.
+The protein's natural variant, known as in plasmid Rts1 and strain X, features a modification of the amino acid from E to A at position 77.
+The protein's natural variant, known as in plasmid Rts1, features a modification of the amino acid from V to A at position 126.
+The protein's natural variant, known as in plasmid Rts1, features a modification of the amino acid from A to T at position 150.
+The protein's natural variant, known as in plasmid Rts1, features a modification of the amino acid from L to F at position 247.
+The protein's natural variant, known as in plasmid Rts1, features a modification of the amino acid from Q to Y at position 249.
+The natural variant of this protein is characterized by an amino acid alteration from H to Q at position 35.
+The natural variant of this protein is characterized by an amino acid alteration from R to Y at position 51.
+The protein's natural variant, known as in strain: S-521F, features a modification of the amino acid from G to S at position 12.
+The protein's natural variant, known as in strain: F-96S, F-775F, S-26F, S-438S, S-483F, S-510S, S-521S, S-549S, S-565F, S-968F and US-255F, features a modification of the amino acid from A to G at position 71.
+The protein's natural variant, known as in strain: S-5F, features a modification of the amino acid from Y to N at position 173.
+The protein's natural variant, known as in strain: S-255S, features a modification of the amino acid from P to A at position 238.
+The protein's natural variant, known as in FECD1;, features a modification of the amino acid from R to Q at position 304.
+The protein's natural variant, known as in FECD1; unknown pathological significance;, features a modification of the amino acid from G to R at position 357.
+The protein's natural variant, known as in FECD1;, features a modification of the amino acid from R to H at position 434.
+The protein's natural variant, known as in FECD1 and PPCD2;, features a modification of the amino acid from Q to K at position 455.
+The protein's natural variant, known as in FECD1; unknown pathological significance;, features a modification of the amino acid from P to L at position 575.
+The protein's natural variant, known as found in a tumor sample; unknown pathological significance; abolished localization to endosomes, features a modification of the amino acid from A to P at position 114.
+The protein's natural variant, known as found in a tumor sample; unknown pathological significance; abolished ability to regulate protein trafficking and localization, features a modification of the amino acid from C to Y at position 243.
+The protein's natural variant, known as in DEE73; gain-of-function variant; increased ER stress-induced apoptosis, features a modification of the amino acid from L to S at position 311.
+The protein's natural variant, known as in DEE73, features a modification of the amino acid from L to P at position 312.
+The protein's natural variant, known as in HIGM2, features a modification of the amino acid from F to L at position 15.
+The protein's natural variant, known as in HIGM2; completely abolishes nuclear import and interaction with CTNNBL1, diminishes interaction with KPNA1 and abolishes immunoglobulin class switching;, features a modification of the amino acid from R to W at position 24.
+The protein's natural variant, known as in HIGM2, features a modification of the amino acid from Y to H at position 31.
+The protein's natural variant, known as in HIGM2; unknown pathological significance; loss of mutagenic activity, features a modification of the amino acid from H to Y at position 56.
+The protein's natural variant, known as in HIGM2;, features a modification of the amino acid from W to R at position 80.
+The protein's natural variant, known as in HIGM2; unknown pathological significance;, features a modification of the amino acid from C to R at position 87.
+The protein's natural variant, known as in HIGM2;, features a modification of the amino acid from L to P at position 106.
+The protein's natural variant, known as in HIGM2; slightly decreased mutagenic activity, features a modification of the amino acid from H to P at position 130.
+The protein's natural variant, known as in HIGM2;, features a modification of the amino acid from M to V at position 139.
+The protein's natural variant, known as in HIGM2;, features a modification of the amino acid from F to S at position 151.
+The protein's natural variant, known as in HIGM2; unknown pathological significance, features a modification of the amino acid from R to S at position 174.
+The protein's natural variant, known as in NEDFASB; decreased histone acetyltransferase activity;, features a modification of the amino acid from R to H at position 53.
+The protein's natural variant, known as in NEDFASB; decreased histone acetyltransferase activity, features a modification of the amino acid from C to S at position 369.
+The protein's natural variant, known as in NEDFASB; decreased histone acetyltransferase activity;, features a modification of the amino acid from S to A at position 413.
+The protein's natural variant, known as in strain: azole-resistant isolates, features a modification of the amino acid from K to E at position 97.
+The protein's natural variant, known as in strain: azole-resistant isolates, features a modification of the amino acid from D to G at position 147.
+The protein's natural variant, known as in strain: azole-resistant isolates, features a modification of the amino acid from L to P at position 193.
+The protein's natural variant, known as in strain: azole-resistant isolates, features a modification of the amino acid from V to A at position 237.
+The protein's natural variant, known as in strain: azole-resistant isolates, features a modification of the amino acid from H to N at position 243.
+The protein's natural variant, known as in strain: azole-resistant isolates, features a modification of the amino acid from T to A at position 330.
+The protein's natural variant, known as in strain: azole-resistant isolates, features a modification of the amino acid from A to T at position 353.
+The protein's natural variant, known as in SPAX2;, features a modification of the amino acid from R to W at position 169.
+The protein's natural variant, known as in strain: FVB/N, features a modification of the amino acid from N to S at position 64.
+The protein's natural variant, known as in strain: FVB/N, features a modification of the amino acid from H to Q at position 91.
+The protein's natural variant, known as in strain: FVB/N, features a modification of the amino acid from S to G at position 94.
+The protein's natural variant, known as in strain: C57BL/6, features a modification of the amino acid from P to T at position 157.
+The protein's natural variant, known as in strain: FVB/N, features a modification of the amino acid from P to L at position 164.
+The protein's natural variant, known as in strain: FVB/N, features a modification of the amino acid from E to A at position 229.
+The protein's natural variant, known as in SPGF60; unknown pathological significance, features a modification of the amino acid from A to V at position 79.
+The protein's natural variant, known as in SPGF60; unknown pathological significance, features a modification of the amino acid from E to G at position 326.
+The protein's natural variant, known as in a family affected by Crohn disease; decreases secretion thereby reducing the anti-inflammatory effect;, features a modification of the amino acid from G to R at position 15.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from A to V at position 312.
+The protein's natural variant, known as in ALS; impaired proteasome efficiency leading to accumulation of CTNNB1;, features a modification of the amino acid from D to A at position 90.
+The protein's natural variant, known as in allele KIR2DL4*0501, features a modification of the amino acid from DAA to MLL at position 273.
+The natural variant of this protein is characterized by an amino acid alteration from D to N at position 271.
+The protein's natural variant, known as in strain: HN/FCC-1, features a modification of the amino acid from S to P at position 295.
+The protein's natural variant, known as in strain: HN/FCC-1, features a modification of the amino acid from T to P at position 388.
+The protein's natural variant, known as in AN66; inactive protein, features a modification of the amino acid from G to R at position 452.
+The protein's natural variant, known as in CABAC;, features a modification of the amino acid from T to K at position 101.
+The protein's natural variant, known as in CABAC; decreased interaction with EXOSC3, EXOSC9 and EXOSC10, when assayed in a heterologous system;, features a modification of the amino acid from T to I at position 114.
+The protein's natural variant, known as in CABAC; unknown pathological significance; no detectable effect on interaction with EXOSC3, EXOSC9 and EXOSC10, when assayed in a heterologous system;, features a modification of the amino acid from M to T at position 148.
+The protein's natural variant, known as in CABAC; strongly decreased interaction with EXOSC3, EXOSC9 and EXOSC10, when assayed in a heterologous system, features a modification of the amino acid from L to H at position 206.
+The protein's natural variant, known as in SSS2; results in a significant reduction of current density compared to wild-type;, features a modification of the amino acid from A to V at position 485.
+The protein's natural variant, known as in EIG18; associated with disease susceptibility; alters the channel kinetics by causing a leftward shift in the voltage dependence of the channel activation curve; neurons expressing mutant channels present lower current thresholds to firing and higher firing rates;, features a modification of the amino acid from R to C at position 550.
+The protein's natural variant, known as in SSS2;, features a modification of the amino acid from D to N at position 553.
+The protein's natural variant, known as in SSS2; results in decreased affinity for cAMP but does not abolish channel activation; shifts the current activation range to hyperpolarized voltages; slows channel opening and speeds up channel closure;, features a modification of the amino acid from S to R at position 672.
+The protein's natural variant, known as in strain: S4; confers macrolide resistance, features a modification of the amino acid from G to GGT at position 63.
+The protein's natural variant, known as in strain: S39; confers macrolide resistance, features a modification of the amino acid from T to K at position 64.
+The protein's natural variant, known as in strain: S27 and S47; confers macrolide resistance, features a modification of the amino acid from G to D at position 65.
+The protein's natural variant, known as in strain: S50; confers macrolide resistance, features a modification of the amino acid from A to S at position 69.
+The protein's natural variant, known as in strain: S54; confers macrolide resistance, features a modification of the amino acid from T to I at position 82.
+The protein's natural variant, known as in strain: cv. Po-1 and cv. Zu-0, features a modification of the amino acid from I to V at position 48.
+The protein's natural variant, known as in strain: cv. BG-4, cv. KNO2, cv. Po-1, cv. Wu-0 and cv. Zu-0, features a modification of the amino acid from Y to C at position 104.
+The protein's natural variant, known as in strain: cv. Pog-0, features a modification of the amino acid from S to Y at position 154.
+The protein's natural variant, known as in strain: cv. BG-4, cv. KNO2, cv. Po-1, cv. Wu-0 and cv. Zu-0, features a modification of the amino acid from S to P at position 419.
+The protein's natural variant, known as in strain: cv. BG-4, cv. KNO2, cv. Po-1, cv. Wu-0 and cv. Zu-0, features a modification of the amino acid from H to N at position 439.
+The protein's natural variant, known as in strain: cv. BG-4, cv. KNO2, cv. Po-1 and cv. Zu-0, features a modification of the amino acid from H to Y at position 472.
+The protein's natural variant, known as in strain: cv. Yo-0, features a modification of the amino acid from V to A at position 515.
+The protein's natural variant, known as in strain: cv. Ang-0, cv. Mt-0 and cv. RLD, features a modification of the amino acid from V to L at position 515.
+The protein's natural variant, known as in strain: cv. Ab-7, cv. Fm-17, cv. Gr-6 and cv. Hs-12, features a modification of the amino acid from P to H at position 527.
+The protein's natural variant, known as in strain: cv. Wu-0, features a modification of the amino acid from S to R at position 544.
+The protein's natural variant, known as in strain: cv. BG-4, cv. KNO2, cv. Po-1, cv. Wu-0 and cv. Zu-0, features a modification of the amino acid from S to Y at position 545.
+The protein's natural variant, known as in strain: cv. BG-4, KNO2, cv. Po-1, cv. Wu-0 and cv. Zu-0, features a modification of the amino acid from E to G at position 644.
+The protein's natural variant, known as in strain: cv. Wu-0, features a modification of the amino acid from G to E at position 649.
+The protein's natural variant, known as in strain: cv. BG-4, cv. KNO2, cv. Po-1 and cv. Zu-0, features a modification of the amino acid from G to Q at position 649.
+The protein's natural variant, known as in strain: cv. BG-4, cv. KNO2, cv. Po-1, cv. Wu-0 and cv. Zu-0, features a modification of the amino acid from A to V at position 653.
+The protein's natural variant, known as in strain: cv. Yo-0, features a modification of the amino acid from E to D at position 699.
+The protein's natural variant, known as in strain: cv. Ang-0, cv. BG-4, cv. Bur-0, cv. Co-1, cv. Ct-1, cv. D2-9, cv. G2-1, cv. Kas-1, cv. KNO2, cv. Mt-0, cv. Po-1, cv. Pog-0, cv. Pu-8, cv. RLD, cv. Tamm-17, cv. Tsu-0, cv. Wu-0, cv. Yo-0 and cv. Zu-0, features a modification of the amino acid from E to D at position 703.
+The protein's natural variant, known as in strain: cv. D2-9, cv. G2-1 and cv. Tsu-0, features a modification of the amino acid from N to K at position 778.
+The protein's natural variant, known as in strain: cv. Wu-0, features a modification of the amino acid from L to V at position 785.
+The protein's natural variant, known as in strain: cv. BG-4, cv. Ct-1, cv. Cvi-0, cv. D2-9, cv. G2-1, cv. Kas-1, cv. KNO2, cv. Po-1, cv. Pu-8, cv. Tsu-0, cv. Wu-0 and cv. Zu-0, features a modification of the amino acid from R to T at position 833.
+The protein's natural variant, known as in allele 2, features a modification of the amino acid from A to AA at position 33.
+The protein's natural variant, known as in allele 2, features a modification of the amino acid from T to I at position 120.
+The protein's natural variant, known as in allele 2, features a modification of the amino acid from D to G at position 219.
+The natural variant of this protein is characterized by an amino acid alteration from G to R at position 98.
+The protein's natural variant, known as in CAMRQ4; abolishes ATPase activity. No effect on interaction with TMEM30A;, features a modification of the amino acid from I to M at position 376.
+The protein's natural variant, known as in CAMRQ4; unknown pathological significance; abolishes ATPase activity. No effect on interaction with TMEM30A;, features a modification of the amino acid from K to M at position 429.
+The protein's natural variant, known as in CAMRQ4; unknown pathological significance; abolishes ATPase activity and results in protein misfolding and proteasomal degradation. No effect on interaction with TMEM30A, features a modification of the amino acid from K to N at position 429.
+The protein's natural variant, known as in CAMRQ4; unknown pathological significance; results in protein misfolding and proteasomal degradation, features a modification of the amino acid from A to P at position 544.
+The protein's natural variant, known as in CAMRQ4; unknown pathological significance; results in protein misfolding and proteasomal degradation;, features a modification of the amino acid from R to W at position 625.
+The protein's natural variant, known as in CAMRQ4; unknown pathological significance; results in protein misfolding and proteasomal degradation, features a modification of the amino acid from W to R at position 702.
+The protein's natural variant, known as in CAMRQ4; unknown pathological significance;, features a modification of the amino acid from N to D at position 917.
+The protein's natural variant, known as in PRLTS6; decreased protein abundance; reduced assembly of the mitochondrial ribosomal small subunit;, features a modification of the amino acid from N to I at position 236.
+The natural variant of this protein is characterized by an amino acid alteration from I to L at position 2.
+The natural variant of this protein is characterized by an amino acid alteration from C to N at position 6.
+The protein's natural variant, known as in strain: CCUG 17874; streptomycin resistant, features a modification of the amino acid from K to R at position 43.
+The protein's natural variant, known as in GLYS;, features a modification of the amino acid from N to S at position 654.
+The natural variant of this protein is characterized by an amino acid alteration from IS to L at position 105.
+The protein's natural variant, known as in AIMAH2; loss of function in promoting apoptosis, features a modification of the amino acid from C to R at position 139.
+The protein's natural variant, known as in AIMAH2;, features a modification of the amino acid from L to F at position 156.
+The protein's natural variant, known as in AIMAH2;, features a modification of the amino acid from R to Q at position 315.
+The protein's natural variant, known as in AIMAH2; loss of function in promoting apoptosis, features a modification of the amino acid from R to W at position 315.
+The protein's natural variant, known as in AIMAH2; unknown pathological significance;, features a modification of the amino acid from L to V at position 318.
+The protein's natural variant, known as in AIMAH2; unknown pathological significance;, features a modification of the amino acid from G to A at position 323.
+The protein's natural variant, known as in AIMAH2; loss of function in promoting apoptosis, features a modification of the amino acid from L to P at position 331.
+The protein's natural variant, known as in AIMAH2; loss of function in promoting apoptosis, features a modification of the amino acid from R to L at position 362.
+The protein's natural variant, known as in AIMAH2;, features a modification of the amino acid from R to W at position 362.
+The protein's natural variant, known as in AIMAH2;, features a modification of the amino acid from L to P at position 365.
+The protein's natural variant, known as in AIMAH2; unknown pathological significance, features a modification of the amino acid from L to P at position 394.
+The protein's natural variant, known as in AIMAH2; loss of function in promoting apoptosis; unknown pathological significance;, features a modification of the amino acid from L to P at position 548.
+The protein's natural variant, known as in AIMAH2; unknown pathological significance, features a modification of the amino acid from L to P at position 580.
+The protein's natural variant, known as in AIMAH2;, features a modification of the amino acid from R to W at position 593.
+The protein's natural variant, known as in AIMAH2; unknown pathological significance;, features a modification of the amino acid from T to M at position 643.
+The protein's natural variant, known as in AIMAH2; loss of function in promoting apoptosis, features a modification of the amino acid from C to R at position 657.
+The protein's natural variant, known as in AIMAH2, features a modification of the amino acid from C to W at position 657.
+The protein's natural variant, known as in AIMAH2; loss of function in promoting apoptosis, features a modification of the amino acid from I to S at position 664.
+The protein's natural variant, known as in AIMAH2;, features a modification of the amino acid from P to R at position 731.
+The protein's natural variant, known as in AIMAH2; loss of function in promoting apoptosis, features a modification of the amino acid from Y to S at position 736.
+The protein's natural variant, known as in AIMAH2; loss of function in promoting apoptosis, features a modification of the amino acid from L to P at position 754.
+The protein's natural variant, known as in AIMAH2, features a modification of the amino acid from H to P at position 808.
+The protein's natural variant, known as in AIMAH2; unknown pathological significance, features a modification of the amino acid from P to T at position 826.
+The protein's natural variant, known as in AIMAH2; loss of function in promoting apoptosis;, features a modification of the amino acid from R to W at position 898.
+The protein's natural variant, known as in allele MC1R-delta-15, features a modification of the amino acid from LEAGTL to T at position 106.
+The protein's natural variant, known as in Va-J, features a modification of the amino acid from I to T at position 362.
+The protein's natural variant, known as in Va and Va-J; constitutive active cation channel localized to plasma membrane, features a modification of the amino acid from A to P at position 419.
+The protein's natural variant, known as in DEE104; unknown pathological significance, features a modification of the amino acid from S to P at position 477.
+The protein's natural variant, known as in NEDEBA; unknown pathological significance;, features a modification of the amino acid from R to W at position 495.
+The protein's natural variant, known as in NEDEBA; impaired acidification of endolysosomal compartments; when tested in transgenic mice, homozygosity leads to body weights lower than in wild-type animals, impaired motor function, defects in the neuronal development and synapse formation and eventually death at about 2 weeks of age, features a modification of the amino acid from A to P at position 505.
+The protein's natural variant, known as in NEDEBA; unknown pathological significance; impaired acidification of endolysosomal compartments;, features a modification of the amino acid from N to D at position 527.
+The protein's natural variant, known as in DEE104; unknown pathological significance, features a modification of the amino acid from G to E at position 551.
+The protein's natural variant, known as in DEE104; impaired acidification of endolysosomal compartments; when tested in transgenic mice, homozygosity leads to embryonic death at 5 to 6 dpc;, features a modification of the amino acid from R to Q at position 740.
+The protein's natural variant, known as in DEE104, features a modification of the amino acid from R to H at position 804.
+The protein's natural variant, known as in strain: 212, features a modification of the amino acid from G to R at position 126.
+The protein's natural variant, known as in strain: 212, features a modification of the amino acid from N to D at position 227.
+The protein's natural variant, known as in strain: 212, features a modification of the amino acid from V to I at position 264.
+The protein's natural variant, known as in strain: 212, features a modification of the amino acid from D to A at position 289.
+The protein's natural variant, known as in strain: 212, features a modification of the amino acid from D to S at position 304.
+The protein's natural variant, known as in strain: 212, features a modification of the amino acid from E to P at position 310.
+The protein's natural variant, known as in strain: 212, features a modification of the amino acid from NV to KL at position 371.
+The protein's natural variant, known as in strain: 212, features a modification of the amino acid from P to A at position 424.
+The protein's natural variant, known as in strain: 212, features a modification of the amino acid from T to A at position 480.
+The protein's natural variant, known as in plasmid pBP201, features a modification of the amino acid from K to E at position 8.
+The protein's natural variant, known as in plasmid pBP201, features a modification of the amino acid from E to Q at position 15.
+The protein's natural variant, known as in slaty; decreased DOPAchrome tautomerase activity, features a modification of the amino acid from R to Q at position 194.
+The protein's natural variant, known as in slaty-2j, features a modification of the amino acid from P to L at position 434.
+The protein's natural variant, known as in slaty-lt, features a modification of the amino acid from G to R at position 486.
+The protein's natural variant, known as in IMD40;, features a modification of the amino acid from R to S at position 751.
+The protein's natural variant, known as in IMD40;, features a modification of the amino acid from R to W at position 1104.
+The protein's natural variant, known as in isoform E, features a modification of the amino acid from K to E at position 80.
+The protein's natural variant, known as associated with reduced disease susceptibility; has a protective effect against Crohn disease and psoriasis;, features a modification of the amino acid from R to Q at position 381.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from T to N at position 32.
+The natural variant of this protein is characterized by an amino acid alteration from S to A at position 54.
+The natural variant of this protein is characterized by an amino acid alteration from D to E at position 87.
+The natural variant of this protein is characterized by an amino acid alteration from A to T at position 122.
+The protein's natural variant, known as may act as disease modifier for Duchenne muscular dystrophy being associated with earlier loss of ambulation;, features a modification of the amino acid from E to D at position 49.
+The natural variant of this protein is characterized by an amino acid alteration from I to T at position 123.
+The protein's natural variant, known as in CTRCT20; unknown pathological significance, features a modification of the amino acid from FY to LN at position 11.
+The protein's natural variant, known as in CTRCT20;, features a modification of the amino acid from G to V at position 18.
+The protein's natural variant, known as in CTRCT20; unknown pathological significance;, features a modification of the amino acid from D to G at position 26.
+The protein's natural variant, known as in CTRCT20; unknown pathological significance;, features a modification of the amino acid from S to C at position 39.
+The protein's natural variant, known as in IDDFSDA; unknown pathological significance;, features a modification of the amino acid from Y to C at position 186.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from V to M at position 523.
+The protein's natural variant, known as in Lp, features a modification of the amino acid from D to E at position 255.
+The protein's natural variant, known as in Lp, features a modification of the amino acid from S to N at position 464.
+The protein's natural variant, known as in temperature-sensitive FT20 cell line; defective activity, features a modification of the amino acid from S to F at position 1180.
+The protein's natural variant, known as in allele SAA2.1;, features a modification of the amino acid from R to H at position 89.
+The protein's natural variant, known as in strain: MOLF/Ei, features a modification of the amino acid from G to D at position 226.
+The protein's natural variant, known as in strain: MOLF/Ei, features a modification of the amino acid from A to T at position 399.
+The protein's natural variant, known as in strain: MOLF/Ei, features a modification of the amino acid from P to T at position 470.
+The protein's natural variant, known as in strain: MOLF/Ei, features a modification of the amino acid from T to A at position 482.
+The protein's natural variant, known as in strain: MOLF/Ei, features a modification of the amino acid from V to M at position 609.
+The protein's natural variant, known as in strain: MOLF/Ei, features a modification of the amino acid from G to A at position 619.
+The protein's natural variant, known as in strain: MOLF/Ei, features a modification of the amino acid from G to E at position 835.
+The protein's natural variant, known as in strain: MOLF/Ei, features a modification of the amino acid from G to A at position 843.
+The protein's natural variant, known as in IFN-tau2C, features a modification of the amino acid from E to D at position 106.
+The protein's natural variant, known as in IFN-tau2B, features a modification of the amino acid from E to K at position 130.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from E to A at position 230.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from G to R at position 865.
+The protein's natural variant, known as in IMD99; when expressed in a B lymphocyte cell line, leads to decreased frequencies of somatic hypermutations, a process involved in the production of isotype-switched high-affinity antibodies, the defect that can be rescued by the wild-type protein; decrease interaction with AICDA, hence impairs AICDA nuclear localization; may decrease protein stability; no effect on interaction with CDC5L;, features a modification of the amino acid from M to V at position 466.
+The protein's natural variant, known as found in a renal cell carcinoma sample; somatic mutation, features a modification of the amino acid from F to I at position 223.
+The protein's natural variant, known as in microcytic anemia; impairs metal ion transport, features a modification of the amino acid from G to R at position 185.
+The protein's natural variant, known as in SPGF2; unknown pathological significance, features a modification of the amino acid from G to S at position 82.
+The protein's natural variant, known as in SPGF2, features a modification of the amino acid from P to L at position 638.
+The protein's natural variant, known as in SPGF2 and POF20, features a modification of the amino acid from S to L at position 754.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from Q to R at position 1093.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from S to G at position 1117.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from Q to R at position 1121.
+The protein's natural variant, known as in beta-2, features a modification of the amino acid from N to H at position 53.
+The protein's natural variant, known as in beta-2, features a modification of the amino acid from N to S at position 57.
+The protein's natural variant, known as in beta-2, features a modification of the amino acid from S to N at position 77.
+The protein's natural variant, known as in beta-2, features a modification of the amino acid from I to V at position 113.
+The protein's natural variant, known as in DA2B1;, features a modification of the amino acid from R to Q at position 174.
+The natural variant of this protein is characterized by an amino acid alteration from L to P at position 2.
+The natural variant of this protein is characterized by an amino acid alteration from S to SDTLPRDVT at position 156.
+The protein's natural variant, known as in CDP-GPAPP;, features a modification of the amino acid from D to N at position 177.
+The protein's natural variant, known as in CDP-GPAPP;, features a modification of the amino acid from T to P at position 183.
+The protein's natural variant, known as in CLN5; retained in the endoplasmic reticulum rather than reaching the lysosome;, features a modification of the amino acid from R to H at position 63.
+The protein's natural variant, known as in CLN5; Retained in the endoplasmic reticulum rather than reaching the lysosome;, features a modification of the amino acid from R to P at position 63.
+The protein's natural variant, known as in CLN5;, features a modification of the amino acid from C to Y at position 77.
+The protein's natural variant, known as in CLN5; loss of glycosylation; effectively transported to the lysosome;, features a modification of the amino acid from N to S at position 143.
+The protein's natural variant, known as in CLN5;, features a modification of the amino acid from L to P at position 149.
+The protein's natural variant, known as in CLN5;, features a modification of the amino acid from P to S at position 156.
+The protein's natural variant, known as in CLN5;, features a modification of the amino acid from W to R at position 158.
+The protein's natural variant, known as in CLN5;, features a modification of the amino acid from W to S at position 158.
+The protein's natural variant, known as in CLN5;, features a modification of the amino acid from Y to D at position 209.
+The protein's natural variant, known as in CLN5; creates a new N-glycosylation site; retained in the endoplasmic reticulum rather than reaching the lysosome;, features a modification of the amino acid from D to N at position 230.
+The protein's natural variant, known as in CLN5;, features a modification of the amino acid from Y to C at position 325.
+The protein's natural variant, known as in CLN5; retained in the endoplasmic reticulum rather than reaching the lysosome;, features a modification of the amino acid from W to C at position 330.
+The protein's natural variant, known as found in a patient with non-obstructive azoospermia; unknown pathological significance, features a modification of the amino acid from L to F at position 309.
+The protein's natural variant, known as found in a patient with non-obstructive azoospermia; unknown pathological significance, features a modification of the amino acid from T to M at position 363.
+The protein's natural variant, known as found in patients with non-obstructive azoospermia; unknown pathological significance;, features a modification of the amino acid from T to R at position 408.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from E to K at position 143.
+The protein's natural variant, known as in GCLEB;, features a modification of the amino acid from T to A at position 338.
+The protein's natural variant, known as in KCS2; enhanced autocatalytic cleavage;, features a modification of the amino acid from Y to H at position 511.
+The protein's natural variant, known as in GCLEB;, features a modification of the amino acid from P to T at position 527.
+The protein's natural variant, known as in GCLEB; enhanced autocatalytic cleavage;, features a modification of the amino acid from D to G at position 528.
+The protein's natural variant, known as in KCS2; enhanced autocatalytic cleavage;, features a modification of the amino acid from R to H at position 569.
+The protein's natural variant, known as in DEE26; reduces sensitivity and cooperativity of the voltage sensor for channel opening and greatly suppresses repetitive firing in cultured cortical neurons;, features a modification of the amino acid from R to C at position 306.
+The protein's natural variant, known as in DEE26; inhibits ion selectivity and gain of a depolarizing inward cation conductance; trafficks normally to the cell surface;, features a modification of the amino acid from S to R at position 347.
+The protein's natural variant, known as in DEE26; inhibits ion selectivity and gain of a depolarizing inward cation conductance; trafficks normally to the cell surface;, features a modification of the amino acid from T to I at position 374.
+The protein's natural variant, known as in DEE26; change in the ion selectivity from potassium-selective to nonselective cation channels and significant decrease in cell membrane localization, features a modification of the amino acid from V to A at position 378.
+The protein's natural variant, known as in DEE26; inhibits ion selectivity and gain of a depolarizing inward cation conductance; trafficks normally to the cell surface;, features a modification of the amino acid from G to R at position 379.
+The protein's natural variant, known as in DEE26; dominant-negative mutation resulting in loss of endogenous channel currents and greatly suppresses repetitive firing in cultured cortical neurons, features a modification of the amino acid from G to R at position 401.
+The protein's natural variant, known as in allele VN1R5*3;, features a modification of the amino acid from R to C at position 350.
+The natural variant of this protein is characterized by an amino acid alteration from E to G at position 84.
+The natural variant of this protein is characterized by an amino acid alteration from E to D at position 146.
+The natural variant of this protein is characterized by an amino acid alteration from Q to R at position 261.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 509.
+The protein's natural variant, known as in TS20; resistant to sulfonamide and temperature-sensitive, features a modification of the amino acid from F to I at position 28.
+The protein's natural variant, known as in strain: DBVPG6044, SK1 and YPS128, features a modification of the amino acid from L to V at position 149.
+The protein's natural variant, known as in strain: DBVPG1853, features a modification of the amino acid from S to L at position 301.
+The protein's natural variant, known as in strain: DBVPG6044, SK1 and YPS128, features a modification of the amino acid from N to D at position 349.
+The protein's natural variant, known as in strain: DBVPG1853, features a modification of the amino acid from G to D at position 499.
+The protein's natural variant, known as in strain: DBVPG6044, SK1 and YPS128, features a modification of the amino acid from E to A at position 518.
+The protein's natural variant, known as in strain: DBVPG1853, features a modification of the amino acid from T to A at position 528.
+The protein's natural variant, known as in strain: DBVPG6763, features a modification of the amino acid from I to S at position 585.
+The protein's natural variant, known as in strain: GQ212, KoQ229, SQ217, features a modification of the amino acid from Q to E at position 20.
+The protein's natural variant, known as in strain: TK-1, features a modification of the amino acid from E to V at position 32.
+The protein's natural variant, known as in strain: GQ212, features a modification of the amino acid from V to A at position 33.
+The protein's natural variant, known as in strain: GQ212, KoQ229, MAN, ME, Priscilla, SQ217, features a modification of the amino acid from A to T at position 52.
+The protein's natural variant, known as in strain: ME, features a modification of the amino acid from V to A at position 63.
+The protein's natural variant, known as in strain: SQ217, features a modification of the amino acid from V to A at position 87.
+The protein's natural variant, known as in strain: California 76 VR 614, features a modification of the amino acid from E to G at position 100.
+The protein's natural variant, known as in strain: 605, features a modification of the amino acid from E to G at position 104.
+The protein's natural variant, known as in strain: Priscilla, features a modification of the amino acid from V to M at position 183.
+The protein's natural variant, known as in strain: Bangui VR 730, features a modification of the amino acid from G to R at position 271.
+The protein's natural variant, known as in strain: Bangui VR 730, features a modification of the amino acid from Y to C at position 306.
+The protein's natural variant, known as in strain: El Tayeb RSA 342, features a modification of the amino acid from W to R at position 379.
+The protein's natural variant, known as in strain: GQ212, KoQ229, SQ217, features a modification of the amino acid from T to A at position 415.
+The protein's natural variant, known as in strain: GQ212, KoQ229, SQ217, features a modification of the amino acid from G to A at position 419.
+The natural variant of this protein is characterized by an amino acid alteration from S to F at position 316.
+The natural variant of this protein is characterized by an amino acid alteration from I to L at position 117.
+The natural variant of this protein is characterized by an amino acid alteration from L to M at position 124.
+The natural variant of this protein is characterized by an amino acid alteration from D to E at position 639.
+The protein's natural variant, known as in SPGF40; unknown pathological significance, features a modification of the amino acid from N to K at position 1007.
+The protein's natural variant, known as in SPGF40; unknown pathological significance, features a modification of the amino acid from L to R at position 1016.
+The natural variant of this protein is characterized by an amino acid alteration from I to F at position 1240.
+The protein's natural variant, known as in strain: CD-1, features a modification of the amino acid from I to M at position 29.
+The protein's natural variant, known as in strain: CD-1, features a modification of the amino acid from I to M at position 145.
+The protein's natural variant, known as in strain: CD-1, features a modification of the amino acid from FGAFHHDIQ to SVLFIMIFK at position 304.
+The protein's natural variant, known as in strain: CD-1, features a modification of the amino acid from V to I at position 361.
+The protein's natural variant, known as in strain: CD-1, features a modification of the amino acid from V to A at position 377.
+The protein's natural variant, known as in strain: CD-1, features a modification of the amino acid from P to A at position 456.
+The protein's natural variant, known as does not affect enzyme activity;, features a modification of the amino acid from L to P at position 3.
+The protein's natural variant, known as does not affect enzyme activity;, features a modification of the amino acid from L to V at position 3.
+The protein's natural variant, known as in FD; loss of enzyme activity;, features a modification of the amino acid from A to D at position 20.
+The protein's natural variant, known as in FD; atypical; loss of enzyme activity;, features a modification of the amino acid from A to P at position 20.
+The protein's natural variant, known as in FD; loss of enzyme activity;, features a modification of the amino acid from L to P at position 21.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from A to V at position 31.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from L to P at position 32.
+The protein's natural variant, known as in FD; unknown pathological significance; decreased enzyme activity;, features a modification of the amino acid from D to G at position 33.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from N to S at position 34.
+The protein's natural variant, known as in FD; unknown pathological significance; decreased enzyme activity;, features a modification of the amino acid from G to E at position 35.
+The protein's natural variant, known as in FD, features a modification of the amino acid from G to R at position 35.
+The protein's natural variant, known as in FD; loss of enzyme activity;, features a modification of the amino acid from L to W at position 36.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from P to L at position 40.
+The protein's natural variant, known as in FD; loss of enzyme activity;, features a modification of the amino acid from P to S at position 40.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from M to L at position 42.
+The protein's natural variant, known as in FD; loss of enzyme activity;, features a modification of the amino acid from M to T at position 42.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from M to V at position 42.
+The protein's natural variant, known as in FD, features a modification of the amino acid from G to R at position 43.
+The protein's natural variant, known as in FD, features a modification of the amino acid from LH to RS at position 46.
+The protein's natural variant, known as in FD; loss of enzyme activity, features a modification of the amino acid from L to P at position 45.
+The protein's natural variant, known as in FD; has 36% of wild-type activity, features a modification of the amino acid from H to P at position 46.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from H to R at position 46.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from H to Y at position 46.
+The protein's natural variant, known as in FD; decreased alpha-galactosidase activity, features a modification of the amino acid from W to G at position 47.
+The protein's natural variant, known as in FD; decreased alpha-galactosidase activity, features a modification of the amino acid from W to R at position 47.
+The protein's natural variant, known as in FD; loss of enzyme activity;, features a modification of the amino acid from E to D at position 48.
+The protein's natural variant, known as in FD, features a modification of the amino acid from R to L at position 49.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from R to P at position 49.
+The protein's natural variant, known as in FD, features a modification of the amino acid from R to S at position 49.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from C to R at position 52.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from C to S at position 52.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from C to F at position 56.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from C to G at position 56.
+The protein's natural variant, known as in FD; loss of enzyme activity;, features a modification of the amino acid from C to Y at position 56.
+The protein's natural variant, known as in FD, features a modification of the amino acid from E to K at position 59.
+The protein's natural variant, known as in FD; unknown pathological significance; decreased enzyme activity;, features a modification of the amino acid from P to L at position 60.
+The protein's natural variant, known as in FD; loss of enzyme activity;, features a modification of the amino acid from I to F at position 64.
+The protein's natural variant, known as in FD; does not affect enzyme function;, features a modification of the amino acid from S to T at position 65.
+The protein's natural variant, known as in FD; has 52% of wild-type activity;, features a modification of the amino acid from E to Q at position 66.
+The protein's natural variant, known as does not affect enzyme activity;, features a modification of the amino acid from E to G at position 71.
+The protein's natural variant, known as in FD; atypical, features a modification of the amino acid from M to V at position 72.
+The protein's natural variant, known as in FD; unknown pathological significance; decreased enzyme activity;, features a modification of the amino acid from G to D at position 80.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from G to D at position 85.
+The protein's natural variant, known as in FD, features a modification of the amino acid from Y to C at position 86.
+The protein's natural variant, known as in FD; loss of enzyme activity;, features a modification of the amino acid from Y to H at position 86.
+The protein's natural variant, known as in FD, features a modification of the amino acid from L to P at position 89.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from L to R at position 89.
+The protein's natural variant, known as in FD; loss of enzyme activity;, features a modification of the amino acid from I to N at position 91.
+The protein's natural variant, known as in FD; mild; loss of enzyme activity;, features a modification of the amino acid from I to T at position 91.
+The protein's natural variant, known as in FD, features a modification of the amino acid from D to H at position 92.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from D to Y at position 92.
+The protein's natural variant, known as in FD, features a modification of the amino acid from D to G at position 93.
+The protein's natural variant, known as in FD; has no enzyme activity;, features a modification of the amino acid from D to N at position 93.
+The protein's natural variant, known as in FD; loss of enzyme activity, features a modification of the amino acid from C to S at position 94.
+The protein's natural variant, known as in FD; loss of enzyme activity;, features a modification of the amino acid from C to Y at position 94.
+The protein's natural variant, known as in FD, features a modification of the amino acid from W to S at position 95.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from A to V at position 97.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from R to K at position 100.
+The protein's natural variant, known as in FD, features a modification of the amino acid from R to T at position 100.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from R to C at position 112.
+The protein's natural variant, known as in FD; mild;, features a modification of the amino acid from R to H at position 112.
+The protein's natural variant, known as in FD, features a modification of the amino acid from R to S at position 112.
+The protein's natural variant, known as in FD; unknown pathological significance; decreased enzyme activity;, features a modification of the amino acid from F to I at position 113.
+The protein's natural variant, known as in FD; mild;, features a modification of the amino acid from F to L at position 113.
+The protein's natural variant, known as in FD, features a modification of the amino acid from F to S at position 113.
+The protein's natural variant, known as in FD, features a modification of the amino acid from LA to PT at position 121.
+The protein's natural variant, known as in FD; has 42% of wild-type activity, features a modification of the amino acid from L to V at position 120.
+The protein's natural variant, known as in FD; unknown pathological significance; decreased enzyme activity;, features a modification of the amino acid from A to T at position 121.
+The protein's natural variant, known as in FD, features a modification of the amino acid from G to E at position 128.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from L to P at position 131.
+The protein's natural variant, known as in FD, features a modification of the amino acid from Y to S at position 134.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from A to V at position 135.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from G to R at position 138.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from C to R at position 142.
+The protein's natural variant, known as in FD, features a modification of the amino acid from C to Y at position 142.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from A to P at position 143.
+The protein's natural variant, known as in FD; unknown pathological significance;, features a modification of the amino acid from A to T at position 143.
+The protein's natural variant, known as in FD, features a modification of the amino acid from G to V at position 144.
+The protein's natural variant, known as in FD; mild;, features a modification of the amino acid from P to S at position 146.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from S to N at position 148.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from S to R at position 148.
+The protein's natural variant, known as does not affect enzyme activity;, features a modification of the amino acid from I to T at position 154.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from A to T at position 156.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from A to V at position 156.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from W to C at position 162.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from W to R at position 162.
+The protein's natural variant, known as in FD, features a modification of the amino acid from G to V at position 163.
+The protein's natural variant, known as in FD; loss of enzyme activity, features a modification of the amino acid from V to G at position 164.
+The protein's natural variant, known as in FD; unknown pathological significance; decreased enzyme activity;, features a modification of the amino acid from V to L at position 164.
+The protein's natural variant, known as in FD, features a modification of the amino acid from D to V at position 165.
+The protein's natural variant, known as in FD, features a modification of the amino acid from L to V at position 166.
+The protein's natural variant, known as in FD; loss of enzyme activity, features a modification of the amino acid from L to Q at position 167.
+The protein's natural variant, known as in FD, features a modification of the amino acid from D to V at position 170.
+The protein's natural variant, known as in FD, features a modification of the amino acid from G to D at position 171.
+The protein's natural variant, known as in FD, features a modification of the amino acid from C to R at position 172.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from C to Y at position 172.
+The protein's natural variant, known as in FD; unknown pathological significance; decreased enzyme activity;, features a modification of the amino acid from L to F at position 180.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from G to D at position 183.
+The protein's natural variant, known as in FD; loss of enzyme activity;, features a modification of the amino acid from M to I at position 187.
+The protein's natural variant, known as in FD; decreased enzyme activity;, features a modification of the amino acid from M to V at position 187.
+The protein's natural variant, known as in FD; unknown pathological significance; decreased enzyme activity;, features a modification of the amino acid from R to S at position 196.
+The protein's natural variant, known as in FD; unknown pathological significance; decreased enzyme activity;, features a modification of the amino acid from I to T at position 198.
+The protein's natural variant, known as in FD, features a modification of the amino acid from S to F at position 201.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from C to W at position 202.
+The protein's natural variant, known as in FD; loss of enzyme activity;, features a modification of the amino acid from C to Y at position 202.
+The protein's natural variant, known as in FD; loss of enzyme activity;, features a modification of the amino acid from W to R at position 204.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from P to T at position 205.
+The protein's natural variant, known as in FD; unknown pathological significance; decreased enzyme activity;, features a modification of the amino acid from K to R at position 213.
+The protein's natural variant, known as in FD; unknown pathological significance; decreased enzyme activity;, features a modification of the amino acid from P to L at position 214.
+The protein's natural variant, known as in FD; mild;, features a modification of the amino acid from N to S at position 215.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from Y to D at position 216.
+The protein's natural variant, known as in FD; unknown pathological significance; decreased enzyme activity;, features a modification of the amino acid from I to M at position 219.
+The protein's natural variant, known as in FD, features a modification of the amino acid from I to N at position 219.
+The protein's natural variant, known as in FD; has 46% of wild-type activity, features a modification of the amino acid from I to T at position 219.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from C to G at position 223.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from N to D at position 224.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from N to S at position 224.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from W to R at position 226.
+The protein's natural variant, known as in FD; loss of enzyme activity;, features a modification of the amino acid from R to P at position 227.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from R to Q at position 227.
+The protein's natural variant, known as in FD; unknown pathological significance; decreased enzyme activity;, features a modification of the amino acid from N to S at position 228.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from A to T at position 230.
+The protein's natural variant, known as in FD, features a modification of the amino acid from D to N at position 231.
+The protein's natural variant, known as in FD, features a modification of the amino acid from D to E at position 234.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from S to C at position 235.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from W to C at position 236.
+The protein's natural variant, known as in FD, features a modification of the amino acid from W to L at position 236.
+The protein's natural variant, known as in FD, features a modification of the amino acid from I to N at position 242.
+The protein's natural variant, known as in FD; unknown pathological significance; decreased enzyme activity;, features a modification of the amino acid from I to V at position 242.
+The protein's natural variant, known as in FD; unknown pathological significance; decreased enzyme activity;, features a modification of the amino acid from L to F at position 243.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from D to H at position 244.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from D to N at position 244.
+The protein's natural variant, known as in FD; loss of enzyme activity;, features a modification of the amino acid from S to P at position 247.
+The protein's natural variant, known as in FD, features a modification of the amino acid from S to SWTS at position 247.
+The protein's natural variant, known as in FD; unknown pathological significance; decreased enzyme activity, features a modification of the amino acid from N to K at position 249.
+The protein's natural variant, known as in FD; unknown pathological significance; decreased enzyme activity;, features a modification of the amino acid from I to T at position 253.
+The protein's natural variant, known as in FD; unknown pathological significance; decreased enzyme activity;, features a modification of the amino acid from V to A at position 254.
+The protein's natural variant, known as in FD, features a modification of the amino acid from G to R at position 258.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from P to L at position 259.
+The protein's natural variant, known as in FD; decreased enzyme activity;, features a modification of the amino acid from P to R at position 259.
+The protein's natural variant, known as in FD, features a modification of the amino acid from G to A at position 260.
+The protein's natural variant, known as in FD, features a modification of the amino acid from G to D at position 261.
+The protein's natural variant, known as in FD; loss of enzyme activity;, features a modification of the amino acid from W to R at position 262.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from N to S at position 263.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from D to V at position 264.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from D to Y at position 264.
+The protein's natural variant, known as in FD, features a modification of the amino acid from P to R at position 265.
+The protein's natural variant, known as in FD, features a modification of the amino acid from D to H at position 266.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from D to N at position 266.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from D to V at position 266.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from M to I at position 267.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from V to A at position 269.
+The protein's natural variant, known as in FD; loss of enzyme activity;, features a modification of the amino acid from V to G at position 269.
+The protein's natural variant, known as in FD, features a modification of the amino acid from N to K at position 272.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from N to S at position 272.
+The protein's natural variant, known as in FD; loss of enzyme activity;, features a modification of the amino acid from S to G at position 276.
+The protein's natural variant, known as in FD; mild; does not significantly affect the enzyme activity but the mutant protein levels are decreased presumably in the ER of the cells;, features a modification of the amino acid from Q to E at position 279.
+The protein's natural variant, known as in FD, features a modification of the amino acid from Q to H at position 279.
+The protein's natural variant, known as in FD, features a modification of the amino acid from Q to H at position 280.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from M to T at position 284.
+The protein's natural variant, known as in FD, features a modification of the amino acid from A to P at position 285.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from W to C at position 287.
+The protein's natural variant, known as in FD, features a modification of the amino acid from W to G at position 287.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from A to D at position 288.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from I to F at position 289.
+The protein's natural variant, known as decreased enzyme activity;, features a modification of the amino acid from I to V at position 289.
+The protein's natural variant, known as in FD; atypical;, features a modification of the amino acid from M to I at position 296.
+The protein's natural variant, known as in FD; mild;, features a modification of the amino acid from M to V at position 296.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from S to F at position 297.
+The protein's natural variant, known as in FD, features a modification of the amino acid from N to H at position 298.
+The protein's natural variant, known as in FD, features a modification of the amino acid from N to K at position 298.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from N to S at position 298.
+The protein's natural variant, known as in FD, features a modification of the amino acid from L to F at position 300.
+The protein's natural variant, known as in FD; mild; does not significantly affect the enzyme activity but the mutant protein levels are decreased presumably in the ER of the cells;, features a modification of the amino acid from R to Q at position 301.
+The protein's natural variant, known as in FD; unknown pathological significance; decreased enzyme activity;, features a modification of the amino acid from A to V at position 309.
+The protein's natural variant, known as does not affect enzyme activity;, features a modification of the amino acid from D to N at position 313.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from D to Y at position 313.
+The protein's natural variant, known as in FD; unknown pathological significance; decreased enzyme activity;, features a modification of the amino acid from D to N at position 315.
+The protein's natural variant, known as in FD; unknown pathological significance; decreased enzyme activity;, features a modification of the amino acid from V to A at position 316.
+The protein's natural variant, known as in FD, features a modification of the amino acid from V to E at position 316.
+The protein's natural variant, known as in FD; loss of enzyme activity;, features a modification of the amino acid from I to S at position 317.
+The protein's natural variant, known as in FD, features a modification of the amino acid from N to K at position 320.
+The protein's natural variant, known as in FD; loss of enzyme activity, features a modification of the amino acid from N to Y at position 320.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from Q to E at position 321.
+The protein's natural variant, known as in FD; unknown pathological significance; decreased enzyme activity;, features a modification of the amino acid from P to R at position 323.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from Q to K at position 327.
+The protein's natural variant, known as in FD; loss of enzyme activity;, features a modification of the amino acid from Q to L at position 327.
+The protein's natural variant, known as in FD; loss of enzyme activity;, features a modification of the amino acid from Q to R at position 327.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from G to A at position 328.
+The protein's natural variant, known as in FD; loss of enzyme activity;, features a modification of the amino acid from G to R at position 328.
+The protein's natural variant, known as in FD, features a modification of the amino acid from G to V at position 328.
+The protein's natural variant, known as in FD; unknown pathological significance; decreased enzyme activity;, features a modification of the amino acid from Q to R at position 330.
+The protein's natural variant, known as in FD, features a modification of the amino acid from E to K at position 338.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from W to R at position 340.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from E to K at position 341.
+The protein's natural variant, known as in FD; loss of enzyme activity, features a modification of the amino acid from R to P at position 342.
+The protein's natural variant, known as in FD; severe;, features a modification of the amino acid from R to Q at position 342.
+The protein's natural variant, known as in FD; unknown pathological significance; decreased enzyme activity;, features a modification of the amino acid from A to G at position 352.
+The protein's natural variant, known as in FD; loss of enzyme activity;, features a modification of the amino acid from R to P at position 356.
+The protein's natural variant, known as in FD; has 15% of wild-type activity;, features a modification of the amino acid from R to Q at position 356.
+The protein's natural variant, known as in FD; severe;, features a modification of the amino acid from R to W at position 356.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from E to A at position 358.
+The protein's natural variant, known as in FD; loss of enzyme activity;, features a modification of the amino acid from E to K at position 358.
+The protein's natural variant, known as in FD; has 6% of wild-type activity;, features a modification of the amino acid from G to C at position 360.
+The protein's natural variant, known as in FD; loss of enzyme activity, features a modification of the amino acid from G to S at position 360.
+The protein's natural variant, known as in FD; severe;, features a modification of the amino acid from G to R at position 361.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from R to H at position 363.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from G to D at position 373.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from G to S at position 373.
+The protein's natural variant, known as in FD; unknown pathological significance; decreased enzyme activity;, features a modification of the amino acid from G to A at position 375.
+The protein's natural variant, known as in FD, features a modification of the amino acid from A to D at position 377.
+The protein's natural variant, known as in FD, features a modification of the amino acid from C to Y at position 378.
+The protein's natural variant, known as in FD; unknown pathological significance; decreased enzyme activity;, features a modification of the amino acid from R to S at position 392.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from F to Y at position 396.
+The protein's natural variant, known as in FD; unknown pathological significance; decreased enzyme activity;, features a modification of the amino acid from W to S at position 399.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from P to A at position 409.
+The protein's natural variant, known as in FD, features a modification of the amino acid from P to T at position 409.
+The protein's natural variant, known as in FD; mild;, features a modification of the amino acid from T to A at position 410.
+The protein's natural variant, known as in FD;, features a modification of the amino acid from L to S at position 414.
+The protein's natural variant, known as in CILD24;, features a modification of the amino acid from G to D at position 103.
+The protein's natural variant, known as may be associated with a reduced risk for age-related macular degeneration;, features a modification of the amino acid from L to H at position 9.
+The protein's natural variant, known as in allele FA; requires 2 nucleotide substitutions, features a modification of the amino acid from W to Q at position 28.
+The protein's natural variant, known as in allele S, features a modification of the amino acid from W to R at position 28.
+The protein's natural variant, known as in allele S; may be associated with a reduced risk for age-related macular degeneration;, features a modification of the amino acid from R to Q at position 32.
+The protein's natural variant, known as in AHUS4, features a modification of the amino acid from S to P at position 166.
+The protein's natural variant, known as in AHUS4;, features a modification of the amino acid from R to Q at position 203.
+The protein's natural variant, known as in AHUS4;, features a modification of the amino acid from I to L at position 242.
+The protein's natural variant, known as in AHUS4; gain-of-function mutation that results in enhanced formation of the C3bBb;, features a modification of the amino acid from F to L at position 286.
+The protein's natural variant, known as in AHUS4; gain-of-function mutation that results in enhanced formation of the C3bBb;, features a modification of the amino acid from K to E at position 323.
+The protein's natural variant, known as in AHUS4, features a modification of the amino acid from K to Q at position 323.
+The protein's natural variant, known as in AHUS4;, features a modification of the amino acid from M to I at position 458.
+The protein's natural variant, known as in AHUS4; benign variant;, features a modification of the amino acid from K to R at position 533.
+The protein's natural variant, known as in allele FA, features a modification of the amino acid from A to S at position 736.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from T to N at position 77.
+The protein's natural variant, known as found in patients with large intestine cancer; unknown pathological significance; does not affect interaction with METTL14; abolished RNA methyltransferase activity in vitro, features a modification of the amino acid from Y to C at position 406.
+The protein's natural variant, known as in STHAG7; impairs Wnt signaling; prevents transport to plasma membrane location;, features a modification of the amino acid from A to V at position 19.
+The protein's natural variant, known as in ADCAD2;, features a modification of the amino acid from R to H at position 360.
+The protein's natural variant, known as in ADCAD2;, features a modification of the amino acid from N to S at position 433.
+The protein's natural variant, known as in ADCAD2; impairs Wnt signaling;, features a modification of the amino acid from R to Q at position 473.
+The protein's natural variant, known as in ADCAD2; impairs Wnt signaling in vitro;, features a modification of the amino acid from R to C at position 611.
+The protein's natural variant, known as found in a patient with congenital hydrocephalus; unknown pathological significance, features a modification of the amino acid from V to F at position 1415.
+The protein's natural variant, known as in HRFTC;, features a modification of the amino acid from T to I at position 30.
+The protein's natural variant, known as in NBIA3;, features a modification of the amino acid from A to T at position 96.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from Q to R at position 471.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from K to R at position 1455.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from N to S at position 1587.
+The protein's natural variant, known as in PPH5, features a modification of the amino acid from R to C at position 743.
+The protein's natural variant, known as in PPH5; unknown pathological significance, features a modification of the amino acid from V to M at position 855.
+The protein's natural variant, known as in Pax6(4Neu); defective, features a modification of the amino acid from S to P at position 259.
+The protein's natural variant, known as in strain: Isolate Palo-Alto, features a modification of the amino acid from A to V at position 16.
+The natural variant of this protein is characterized by an amino acid alteration from N to I at position 51.
+The protein's natural variant, known as in strain: Isolate FCR-3, Isolate Gambia and Isolate Palo-Alto, features a modification of the amino acid from R to C at position 59.
+The protein's natural variant, known as in strain: Isolate FCR-3, Isolate Gambia and Isolate Palo-Alto, features a modification of the amino acid from N to T at position 108.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from R to Q at position 145.
+The natural variant of this protein is characterized by an amino acid alteration from R to W at position 13.
+The protein's natural variant, known as in CLN1;, features a modification of the amino acid from W to C at position 38.
+The protein's natural variant, known as in CLN1;, features a modification of the amino acid from H to Q at position 39.
+The protein's natural variant, known as in CLN1;, features a modification of the amino acid from G to E at position 42.
+The protein's natural variant, known as in CLN1;, features a modification of the amino acid from C to Y at position 45.
+The protein's natural variant, known as in CLN1; juvenile onset;, features a modification of the amino acid from T to P at position 75.
+The protein's natural variant, known as in CLN1; juvenile onset;, features a modification of the amino acid from D to G at position 79.
+The protein's natural variant, known as in CLN1; onset in adulthood; retained in the endoplasmic reticulum rather than reaching the lysosome;, features a modification of the amino acid from G to R at position 108.
+The protein's natural variant, known as in CLN1; late infantile form;, features a modification of the amino acid from Y to D at position 109.
+The protein's natural variant, known as in CLN1; retained in the endoplasmic reticulum rather than reaching the lysosome;, features a modification of the amino acid from R to W at position 122.
+The protein's natural variant, known as in CLN1;, features a modification of the amino acid from S to L at position 138.
+The protein's natural variant, known as in CLN1;, features a modification of the amino acid from C to Y at position 152.
+The protein's natural variant, known as in CLN1; late infantile form;, features a modification of the amino acid from Q to E at position 177.
+The protein's natural variant, known as in CLN1;, features a modification of the amino acid from V to L at position 181.
+The protein's natural variant, known as in CLN1; late infantile form;, features a modification of the amino acid from V to M at position 181.
+The protein's natural variant, known as in CLN1;, features a modification of the amino acid from H to R at position 187.
+The protein's natural variant, known as in CLN1;, features a modification of the amino acid from P to R at position 189.
+The protein's natural variant, known as in CLN1; juvenile onset;, features a modification of the amino acid from L to Q at position 219.
+The protein's natural variant, known as in CLN1; late infantile form;, features a modification of the amino acid from L to P at position 222.
+The protein's natural variant, known as in CLN1;, features a modification of the amino acid from V to G at position 228.
+The protein's natural variant, known as in CLN1;, features a modification of the amino acid from Y to H at position 247.
+The protein's natural variant, known as in CLN1;, features a modification of the amino acid from G to V at position 250.
+The protein's natural variant, known as in CLN1;, features a modification of the amino acid from W to R at position 296.
+The protein's natural variant, known as in CLN1;, features a modification of the amino acid from L to P at position 305.
+The protein's natural variant, known as likely benign variant; found in a patient with congenital anomalies of the kidney and urinary tract; no effect on localization to the nucleus; no effect on transcriptional repression activity, features a modification of the amino acid from E to A at position 126.
+The protein's natural variant, known as likely benign variant; found in a patient with congenital anomalies of the kidney and urinary tract; no effect on localization to the nucleus; no effect on transcriptional repression activity, features a modification of the amino acid from I to V at position 387.
+The protein's natural variant, known as likely benign variant; found in a patient with congenital anomalies of the kidney and urinary tract; no effect on localization to the nucleus; no effect on transcriptional repression activity, features a modification of the amino acid from K to R at position 649.
+The protein's natural variant, known as likely benign variant; found in a patient with congenital anomalies of the kidney and urinary tract; no effect on localization to the nucleus; no effect on transcriptional repression activity, features a modification of the amino acid from Y to H at position 763.
+The protein's natural variant, known as likely benign variant; found in a patient with congenital anomalies of the kidney and urinary tract; requires 2 nucleotide substitutions; no effect on localization to the nucleus, features a modification of the amino acid from Y to L at position 763.
+The protein's natural variant, known as likely benign variant; found in a patient with congenital anomalies of the kidney and urinary tract; no effect on localization to the nucleus; no effect on transcriptional repression activity, features a modification of the amino acid from G to E at position 775.
+The protein's natural variant, known as likely benign variant; found in a patient with congenital anomalies of the kidney and urinary tract; no effect on localization to the nucleus; no effect on transcriptional repression activity, features a modification of the amino acid from E to K at position 1031.
+The protein's natural variant, known as in MACTHC1;, features a modification of the amino acid from R to W at position 318.
+The protein's natural variant, known as in Tc(b) antigen;, features a modification of the amino acid from R to L at position 52.
+The protein's natural variant, known as in Tc(c) antigen;, features a modification of the amino acid from R to P at position 52.
+The protein's natural variant, known as in WES(a) antigen;, features a modification of the amino acid from L to R at position 82.
+The protein's natural variant, known as in Dr(a-) antigen;, features a modification of the amino acid from S to L at position 199.
+The protein's natural variant, known as in Cr(a-) antigen;, features a modification of the amino acid from A to P at position 227.
+The protein's natural variant, known as in GUTI(-) antigen;, features a modification of the amino acid from R to H at position 240.
+The protein's natural variant, known as in CHAPLE; increased complement activation;, features a modification of the amino acid from C to S at position 267.
+The natural variant of this protein is characterized by an amino acid alteration from R to T at position 26.
+The protein's natural variant, known as in colon cancer;, features a modification of the amino acid from R to W at position 175.
+The protein's natural variant, known as in colon cancer;, features a modification of the amino acid from L to V at position 215.
+The protein's natural variant, known as in strain: NV, features a modification of the amino acid from A to T at position 25.
+The protein's natural variant, known as in strain: NV, features a modification of the amino acid from ST to ASS at position 31.
+The protein's natural variant, known as in strain: NV, features a modification of the amino acid from S to N at position 102.
+The protein's natural variant, known as in strain: NV, features a modification of the amino acid from A to V at position 120.
+The protein's natural variant, known as in strain: NV, features a modification of the amino acid from D to G at position 202.
+The protein's natural variant, known as in strain: NV, features a modification of the amino acid from S to G at position 205.
+The protein's natural variant, known as in strain: NV, features a modification of the amino acid from N to S at position 221.
+The protein's natural variant, known as in strain: NV, features a modification of the amino acid from VM to GVK at position 226.
+The protein's natural variant, known as in strain: NV, features a modification of the amino acid from NTR to TTS at position 244.
+The protein's natural variant, known as in strain: NV, features a modification of the amino acid from S to A at position 280.
+The protein's natural variant, known as in strain: NV, features a modification of the amino acid from G to A at position 313.
+The protein's natural variant, known as in strain: 314-448A, features a modification of the amino acid from A to ATA at position 67.
+The protein's natural variant, known as found in patients with fifth finger camptodactyly syndrome; unknown pathological significance;, features a modification of the amino acid from S to L at position 339.
+The protein's natural variant, known as in COXPD22;, features a modification of the amino acid from Y to C at position 321.
+The protein's natural variant, known as in MC5DN4;, features a modification of the amino acid from R to C at position 329.
+The protein's natural variant, known as in strain: NEM1126, features a modification of the amino acid from A to T at position 48.
+The protein's natural variant, known as in strain: NEM1126, features a modification of the amino acid from E to D at position 95.
+The protein's natural variant, known as in strain: NEM1222, features a modification of the amino acid from A to T at position 98.
+The protein's natural variant, known as in alpha-2, features a modification of the amino acid from D to A at position 6.
+The natural variant of this protein is characterized by an amino acid alteration from L to R at position 9.
+The protein's natural variant, known as in strain: IS58, features a modification of the amino acid from A to R at position 2.
+The protein's natural variant, known as in strain: IS58, features a modification of the amino acid from T to Q at position 10.
+The protein's natural variant, known as in strain: IS58, features a modification of the amino acid from T to I at position 13.
+The protein's natural variant, known as found in a patient with hypertrophic cardiomyopathy; unknown pathological significance;, features a modification of the amino acid from K to R at position 82.
+The protein's natural variant, known as in CMH13; increases calcium sensitivity of the myofilaments;, features a modification of the amino acid from A to V at position 8.
+The protein's natural variant, known as in CMH13; impairs protein kinase A dependent signaling from cardiac troponin I to troponin C;, features a modification of the amino acid from L to Q at position 29.
+The protein's natural variant, known as in CMH13; increases calcium sensitivity of the myofilaments;, features a modification of the amino acid from C to Y at position 84.
+The protein's natural variant, known as in CMH13; no changes in calcium sensitivity of the myofilaments;, features a modification of the amino acid from E to D at position 134.
+The protein's natural variant, known as in CMH13; increases calcium sensitivity of the myofilaments;, features a modification of the amino acid from D to E at position 145.
+The protein's natural variant, known as in CMD1Z;, features a modification of the amino acid from G to D at position 159.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from R to S at position 124.
+The protein's natural variant, known as in IBGC5; loss of protein expression, features a modification of the amino acid from L to R at position 9.
+The protein's natural variant, known as in IBGC5; loss of protein expression;, features a modification of the amino acid from L to P at position 119.
+The protein's natural variant, known as in strain: CCUG 4165A, features a modification of the amino acid from GV to AL at position 6.
+The protein's natural variant, known as in strain: CCUG 4165A, features a modification of the amino acid from S to T at position 14.
+The protein's natural variant, known as in strain: NCTC 11050, features a modification of the amino acid from V to I at position 45.
+The protein's natural variant, known as in strain: CCUG 4165A, features a modification of the amino acid from RYA to CYP at position 53.
+The protein's natural variant, known as in strain: CCUG 4557, features a modification of the amino acid from R to C at position 51.
+The protein's natural variant, known as in strain: CCUG 4165A, features a modification of the amino acid from L to F at position 75.
+The protein's natural variant, known as in strain: NCTC 11050, features a modification of the amino acid from S to C at position 81.
+The protein's natural variant, known as in strain: CCUG 4165A and CCUG 4557, features a modification of the amino acid from P to T at position 84.
+The protein's natural variant, known as in strain: NHITCC 2376, features a modification of the amino acid from V to I at position 93.
+The protein's natural variant, known as in strain: NCTC 11050, features a modification of the amino acid from EDPQ to DNPK at position 151.
+The protein's natural variant, known as in strain: CCUG 4165A, CCUG 4557 and NHITCC 2376, features a modification of the amino acid from ED to DN at position 149.
+The protein's natural variant, known as in strain: CCUG 4165A, CCUG 4557, NHITCC 2376 and NCTC 11050, features a modification of the amino acid from H to Q at position 176.
+The protein's natural variant, known as in strain: NHITCC 2376, features a modification of the amino acid from V to F at position 187.
+The protein's natural variant, known as in alpha-2, features a modification of the amino acid from D to A at position 12.
+The protein's natural variant, known as in strain: 388, features a modification of the amino acid from C to G at position 40.
+The protein's natural variant, known as in strain: 388, features a modification of the amino acid from H to R at position 43.
+The protein's natural variant, known as in strain: G52 and BG1, features a modification of the amino acid from H to Q at position 411.
+The protein's natural variant, known as in strain: CVI 47459, features a modification of the amino acid from F to Y at position 853.
+The protein's natural variant, known as in strain: 60190, features a modification of the amino acid from S to F at position 5.
+The protein's natural variant, known as in strain: 60190, features a modification of the amino acid from K to R at position 110.
+The protein's natural variant, known as in strain: 60190, features a modification of the amino acid from S to T at position 162.
+The protein's natural variant, known as in EvgS1; constitutively active, features a modification of the amino acid from F to S at position 577.
+The protein's natural variant, known as in EvgS4; constitutively active, features a modification of the amino acid from E to G at position 701.
+The protein's natural variant, known as in IMD32A; impairs transcriptional activity by disrupting the interaction between IRF8 and DNA;, features a modification of the amino acid from T to A at position 80.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from R to K at position 81.
+The protein's natural variant, known as in IMD32B; in resting macrophages, no effect on cytoplasmic subcellular localization; loss of nuclear subcellular localization upon IFN-gamma induction; decreased protein abundance; increased proteasome-dependent degradation; increased ubiquitination and sumoylation; loss of transcriptional repressor activity; loss of IRF1-dependent transcriptional repressor activity; loss of IRF1-dependent transcriptional activator activity; impairs transcriptional activity by disrupting the interaction between IRF8 and DNA;, features a modification of the amino acid from K to E at position 108.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from A to T at position 197.
+The natural variant of this protein is characterized by an amino acid alteration from I to F at position 519.
+The natural variant of this protein is characterized by an amino acid alteration from Y to C at position 788.
+The natural variant of this protein is characterized by an amino acid alteration from R to G at position 97.
+The protein's natural variant, known as in leukemia;, features a modification of the amino acid from G to C at position 12.
+The protein's natural variant, known as in KNEN and JMML;, features a modification of the amino acid from G to D at position 12.
+The protein's natural variant, known as in RALD and JMML;, features a modification of the amino acid from G to D at position 13.
+The protein's natural variant, known as in CMNS and colorectal cancer; somatic mutation;, features a modification of the amino acid from G to R at position 13.
+The protein's natural variant, known as in KNEN;, features a modification of the amino acid from P to L at position 34.
+The protein's natural variant, known as in NS6; hypermorphic mutation;, features a modification of the amino acid from T to I at position 50.
+The protein's natural variant, known as in NS6; hypermorphic mutation;, features a modification of the amino acid from G to E at position 60.
+The protein's natural variant, known as in CMNS and NCMS; somatic mutation;, features a modification of the amino acid from Q to K at position 61.
+The protein's natural variant, known as in CMNS, NCMS, KNEN and NMTC2; also found in lung carcinoma cell and melanoma; impaired GTP hydrolysis activity, trapping NRAS in a constitutive GTP-bound active conformation; promotes melanomagenesis;, features a modification of the amino acid from Q to R at position 61.
+The protein's natural variant, known as in alpha-2, features a modification of the amino acid from N to T at position 68.
+The protein's natural variant, known as in alpha-2, features a modification of the amino acid from A to V at position 70.
+The protein's natural variant, known as in alpha-2, features a modification of the amino acid from A to P at position 120.
+The protein's natural variant, known as found in a patient with isolated coloboma; unknown pathological significance, features a modification of the amino acid from V to G at position 130.
+The protein's natural variant, known as in Ra6A, features a modification of the amino acid from S to P at position 27.
+The protein's natural variant, known as in Ra6B, features a modification of the amino acid from T to A at position 32.
+The natural variant of this protein is characterized by an amino acid alteration from T to D at position 32.
+The protein's natural variant, known as in Ra6A, features a modification of the amino acid from I to N at position 36.
+The natural variant of this protein is characterized by an amino acid alteration from K to P at position 67.
+The natural variant of this protein is characterized by an amino acid alteration from V to M at position 71.
+The natural variant of this protein is characterized by an amino acid alteration from M to V at position 91.
+The natural variant of this protein is characterized by an amino acid alteration from L to F at position 111.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from L to F at position 27.
+The protein's natural variant, known as in 11-beta-3, features a modification of the amino acid from A to V at position 30.
+The protein's natural variant, known as in 11-beta-3, features a modification of the amino acid from S to G at position 60.
+The protein's natural variant, known as in 11-beta-3, features a modification of the amino acid from H to R at position 106.
+The protein's natural variant, known as in plasmid pCTT1, features a modification of the amino acid from E to V at position 168.
+The protein's natural variant, known as in plasmid pCHL1, features a modification of the amino acid from S to P at position 190.
+The protein's natural variant, known as in plasmid pCHL1 and plasmid pCTT1, features a modification of the amino acid from F to L at position 264.
+The protein's natural variant, known as in strain: Serotype A1 / PH101, features a modification of the amino acid from Q to T at position 112.
+The protein's natural variant, known as in strain: Serotype A1 / PH101 and Serotype A1 / PH8, features a modification of the amino acid from S to A at position 340.
+The protein's natural variant, known as in strain: Serotype A1 /PH101, features a modification of the amino acid from SS to FI at position 367.
+The protein's natural variant, known as in strain: Serotype A1 / PH8, features a modification of the amino acid from V to I at position 576.
+The protein's natural variant, known as in strain: Serotype A1 / PH101, features a modification of the amino acid from N to T at position 597.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation, features a modification of the amino acid from Y to H at position 53.
+The protein's natural variant, known as in strain: ATCC 6633, features a modification of the amino acid from Q to L at position 91.
+The protein's natural variant, known as in strain: ATCC 6633, features a modification of the amino acid from I to V at position 96.
+The protein's natural variant, known as in strain: ATCC 6633, features a modification of the amino acid from GNRASRHTIT to ENQSTRHAIN at position 108.
+The protein's natural variant, known as in strain: ATCC 6633, features a modification of the amino acid from T to A at position 214.
+The protein's natural variant, known as in strain: ATCC 6633, features a modification of the amino acid from V to I at position 232.
+The protein's natural variant, known as in strain: ATCC 6633, features a modification of the amino acid from D to N at position 309.
+The protein's natural variant, known as in strain: ATCC 6633, features a modification of the amino acid from HV to NI at position 323.
+The protein's natural variant, known as in strain: ATCC 6633, features a modification of the amino acid from G to S at position 412.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from D to N at position 200.
+The natural variant of this protein is characterized by an amino acid alteration from E to Q at position 109.
+The protein's natural variant, known as in COXPD30; decreased protein abundance; impaired mitochondrial tRNA processing; has no effect on steady-state mitochondrial-mRNA and mitochondrial-tRNA levels but indirectly impairs mitochondrial translation;, features a modification of the amino acid from R to L at position 181.
+The protein's natural variant, known as in COXPD30; decreased protein abundance; impaired mitochondrial tRNA processing; has no effect on steady-state mitochondrial-mRNA and mitochondrial-tRNA levels but indirectly impairs mitochondrial translation;, features a modification of the amino acid from T to A at position 272.
+The natural variant of this protein is characterized by an amino acid alteration from M to I at position 260.
+The natural variant of this protein is characterized by an amino acid alteration from F to S at position 356.
+The natural variant of this protein is characterized by an amino acid alteration from I to M at position 367.
+The protein's natural variant, known as in IDDSAPN; unknown pathological significance, features a modification of the amino acid from I to T at position 553.
+The protein's natural variant, known as associated with low plasma triglyceride level; fails to suppress LPL activity in vitro;, features a modification of the amino acid from K to T at position 63.
+The protein's natural variant, known as associated with low plasma triglyceride level; fails to suppress LPL activity in vitro;, features a modification of the amino acid from E to G at position 91.
+The protein's natural variant, known as associated with low plasma triglyceride level; fails to suppress LPL activity in vitro;, features a modification of the amino acid from L to F at position 164.
+The protein's natural variant, known as associated with low plasma triglyceride level; fails to suppress LPL activity in vitro; no effect on protein secretion;, features a modification of the amino acid from N to S at position 173.
+The protein's natural variant, known as common allele in African americans; associated with low plasma triglyceride level; fails to suppress LPL activity in vitro; no effect on protein folding;, features a modification of the amino acid from M to T at position 259.
+The protein's natural variant, known as abolishes protein secretion; associated with low plasma triglyceride level;, features a modification of the amino acid from R to Q at position 288.
+The protein's natural variant, known as abolishes protein secretion; associated with low plasma triglyceride level;, features a modification of the amino acid from S to P at position 292.
+The protein's natural variant, known as abolishes protein secretion; associated with low plasma triglyceride level;, features a modification of the amino acid from Y to S at position 344.
+The protein's natural variant, known as abolishes protein secretion; associated with low plasma triglyceride level;, features a modification of the amino acid from E to K at position 375.
+The protein's natural variant, known as abolishes protein secretion; associated with low plasma triglyceride level;, features a modification of the amino acid from Y to C at position 417.
+The natural variant of this protein is characterized by an amino acid alteration from T to I at position 156.
+The natural variant of this protein is characterized by an amino acid alteration from E to D at position 172.
+The protein's natural variant, known as in sh-1, features a modification of the amino acid from R to P at position 241.
+The protein's natural variant, known as in sh-1, features a modification of the amino acid from R to P at position 502.
+The protein's natural variant, known as in PARK7; unknown pathological significance, features a modification of the amino acid from L to P at position 10.
+The protein's natural variant, known as in PARK7; does not affect protein stability and degradation; does not interfere with homodimerization; decreased detoxification activity on methylglyocal-adducted CoA;, features a modification of the amino acid from M to I at position 26.
+The protein's natural variant, known as probable disease-associated variant found in early-onset Parkinson disease with digenic inheritance; no effect on detoxification activity on methylglyocal-adducted CoA; the patient also carries PINK1 mutation L-399;, features a modification of the amino acid from A to S at position 39.
+The protein's natural variant, known as in PARK7; no apparent effect on protein stability; impaired mitochondrial morphology; no effect on detoxification activity on methylglyocal-adducted CoA;, features a modification of the amino acid from E to D at position 64.
+The protein's natural variant, known as in PARK7; loss of protection against metal cytotoxicity; decreased detoxification activity on methylglyocal-adducted CoA;, features a modification of the amino acid from A to T at position 104.
+The protein's natural variant, known as in PARK7; loss of protection against metal cytotoxicity; decreased detoxification activity on methylglyocal-adducted CoA;, features a modification of the amino acid from D to A at position 149.
+The protein's natural variant, known as unknown pathological significance; no effect on detoxification activity on methylglyocal-adducted CoA;, features a modification of the amino acid from E to K at position 163.
+The protein's natural variant, known as in PARK7; strongly decreases enzymatic activity; reduces protein stability and leads to increased degradation; ubiquitinated by PRKN leading to its recognition by HDAC6 and targeting to aggresome where is degraded; interferes with homodimerization; abolishes interaction with PIAS2; reduced localization in lipid rafts; almost abolished detoxification activity on methylglyocal-adducted CoA;, features a modification of the amino acid from L to P at position 166.
+The protein's natural variant, known as in NEDMIBA; loss-of-function variant; does not rescue neurodevelopmental defects in zebrafish morphants, features a modification of the amino acid from Y to C at position 247.
+The protein's natural variant, known as likely benign variant; can rescue neurodevelopmental defects in zebrafish morphants;, features a modification of the amino acid from P to A at position 516.
+The protein's natural variant, known as in STY56I, features a modification of the amino acid from V to I at position 429.
+The protein's natural variant, known as in isoform B2, features a modification of the amino acid from VA to GS at position 16.
+The protein's natural variant, known as in clone 11, features a modification of the amino acid from K to N at position 178.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from A to G at position 99.
+The protein's natural variant, known as in BRGDA4; unknown pathological significance; affects channel activity;, features a modification of the amino acid from S to L at position 535.
+The natural variant of this protein is characterized by an amino acid alteration from Y to C at position 129.
+The natural variant of this protein is characterized by an amino acid alteration from R to G at position 301.
+The protein's natural variant, known as in DSKOD; increases cAMP production upon activation of ADRB1;, features a modification of the amino acid from R to W at position 418.
+The protein's natural variant, known as in DSKOR, features a modification of the amino acid from D to N at position 588.
+The natural variant of this protein is characterized by an amino acid alteration from A to V at position 706.
+The protein's natural variant, known as in DSKOD; increases cAMP production upon activation of ADRB1;, features a modification of the amino acid from A to T at position 726.
+The protein's natural variant, known as in DSKOR;, features a modification of the amino acid from R to C at position 1013.
+The protein's natural variant, known as in DSKOR, features a modification of the amino acid from R to W at position 1238.
+The protein's natural variant, known as in AAT6;, features a modification of the amino acid from R to H at position 39.
+The protein's natural variant, known as in AAT6, features a modification of the amino acid from N to T at position 117.
+The protein's natural variant, known as in AAT6;, features a modification of the amino acid from R to Q at position 118.
+The protein's natural variant, known as in AAT6;, features a modification of the amino acid from Y to H at position 135.
+The protein's natural variant, known as in AAT6, features a modification of the amino acid from Y to C at position 145.
+The protein's natural variant, known as in AAT6;, features a modification of the amino acid from R to C at position 149.
+The protein's natural variant, known as in AAT6;, features a modification of the amino acid from V to A at position 154.
+The protein's natural variant, known as in MSMDS, features a modification of the amino acid from R to C at position 179.
+The protein's natural variant, known as in MYMY5 and MSMDS; disease phenotype include smooth muscle cells dysfunction in organs throughout the body with decreased contractile function in the iris, bladder and gastrointestinal tract;, features a modification of the amino acid from R to H at position 179.
+The protein's natural variant, known as in AAT6;, features a modification of the amino acid from R to Q at position 185.
+The protein's natural variant, known as in AAT6;, features a modification of the amino acid from R to Q at position 212.
+The protein's natural variant, known as in AAT6;, features a modification of the amino acid from R to C at position 258.
+The protein's natural variant, known as in AAT6;, features a modification of the amino acid from R to H at position 258.
+The protein's natural variant, known as in AAT6, features a modification of the amino acid from R to G at position 292.
+The protein's natural variant, known as in AAT6;, features a modification of the amino acid from T to N at position 326.
+The protein's natural variant, known as in AAT6, features a modification of the amino acid from T to N at position 353.
+The protein's natural variant, known as in strain: A+, features a modification of the amino acid from A to S at position 85.
+The protein's natural variant, known as in COXPD25;, features a modification of the amino acid from R to W at position 142.
+The protein's natural variant, known as in V-II-3, features a modification of the amino acid from N to K at position 36.
+The protein's natural variant, known as probably protective against leprosy when associated with A-399 and F-407;, features a modification of the amino acid from G to S at position 396.
+The natural variant of this protein is characterized by an amino acid alteration from G to D at position 286.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from H to R at position 315.
+The protein's natural variant, known as in PBD5B; infantile Refsum disease;, features a modification of the amino acid from E to K at position 55.
+The protein's natural variant, known as in PBD5A, features a modification of the amino acid from C to R at position 247.
+The protein's natural variant, known as in a glioblastoma multiforme sample; somatic mutation, features a modification of the amino acid from G to D at position 139.
+The protein's natural variant, known as in CMH22 and CMD1KK; perturbs MYPN nuclear shuttling and leads to disruption of intercalated disks;, features a modification of the amino acid from Y to C at position 20.
+The protein's natural variant, known as in CMH22;, features a modification of the amino acid from K to R at position 153.
+The protein's natural variant, known as in CMD1KK;, features a modification of the amino acid from I to V at position 213.
+The protein's natural variant, known as in CMH22;, features a modification of the amino acid from A to E at position 217.
+The protein's natural variant, known as in CMD1KK;, features a modification of the amino acid from Y to F at position 339.
+The protein's natural variant, known as in CMH22;, features a modification of the amino acid from V to A at position 410.
+The protein's natural variant, known as in CMD1KK;, features a modification of the amino acid from A to T at position 611.
+The protein's natural variant, known as in CMH22;, features a modification of the amino acid from P to T at position 841.
+The protein's natural variant, known as in CMD1KK;, features a modification of the amino acid from A to T at position 882.
+The protein's natural variant, known as in CMD1KK;, features a modification of the amino acid from F to L at position 954.
+The protein's natural variant, known as in CMD1KK; unknown pathological significance;, features a modification of the amino acid from R to W at position 955.
+The protein's natural variant, known as in CMD1KK;, features a modification of the amino acid from P to L at position 961.
+The protein's natural variant, known as in CMD1KK;, features a modification of the amino acid from R to H at position 1088.
+The protein's natural variant, known as in CMD1KK and CMH22; results in sarcomere disorganization and premature cell death;, features a modification of the amino acid from P to L at position 1112.
+The protein's natural variant, known as in CMD1KK; results in sarcomere disorganization and premature cell death;, features a modification of the amino acid from V to M at position 1195.
+The protein's natural variant, known as in CMH22;, features a modification of the amino acid from A to P at position 1265.
+The protein's natural variant, known as in strain: C57BL/6J, features a modification of the amino acid from T to I at position 103.
+The protein's natural variant, known as in strain: C57BL/6J, features a modification of the amino acid from F to L at position 348.
+The protein's natural variant, known as in strain: C57BL/6J, features a modification of the amino acid from L to P at position 354.
+The protein's natural variant, known as loss of retinol/retinal dehydrogenase activity; does not affect localization to lipid droplets;, features a modification of the amino acid from P to S at position 260.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from I to T at position 527.
+The protein's natural variant, known as associated with high triglyceride levels and low fasting plasma glucose levels; associated with a reduced risk for type 2 diabetes; the mutant protein is less efficiently regulated by physiological concentrations of fructose-6 phosphate;, features a modification of the amino acid from P to L at position 446.
+The protein's natural variant, known as in SEMDSP; unknown pathological significance;, features a modification of the amino acid from R to H at position 42.
+The protein's natural variant, known as in SEMDSP; decreased function in double-strand break repair via homologous recombination, features a modification of the amino acid from S to N at position 174.
+The protein's natural variant, known as in SEMDSP; disease phenotype includes immunologic and hematologic abnormalities;, features a modification of the amino acid from E to K at position 199.
+The protein's natural variant, known as in SEMDSP; unknown pathological significance; decreased function in double-strand break repair via homologous recombination, features a modification of the amino acid from D to H at position 364.
+The protein's natural variant, known as in SEMDSP; unknown pathological significance; genomic instability; when associated with R-1090;, features a modification of the amino acid from Q to R at position 430.
+The protein's natural variant, known as in SEMDSP; unknown pathological significance;, features a modification of the amino acid from E to K at position 487.
+The protein's natural variant, known as in SEMDSP; unknown pathological significance;, features a modification of the amino acid from E to K at position 494.
+The protein's natural variant, known as in SEMDSP; decreased function in double-strand break repair via homologous recombination;, features a modification of the amino acid from E to K at position 539.
+The protein's natural variant, known as in SEMDSP; decreased function in double-strand break repair via homologous recombination; decreased protein amount in patient cells;, features a modification of the amino acid from R to Q at position 558.
+The protein's natural variant, known as in SEMDSP; disease phenotype includes immunologic and hematologic abnormalities; unknown pathological significance;, features a modification of the amino acid from V to L at position 613.
+The protein's natural variant, known as in SEMDSP; disease phenotype includes primary aphakia and absent pupils;, features a modification of the amino acid from T to M at position 653.
+The protein's natural variant, known as in SEMDSP; decreased function in double-strand break repair via homologous recombination;, features a modification of the amino acid from R to W at position 934.
+The protein's natural variant, known as in SEMDSP; decreased function in double-strand break repair via homologous recombination;, features a modification of the amino acid from G to R at position 973.
+The protein's natural variant, known as in SEMDSP; unknown pathological significance; genomic instability; when associated with R-430;, features a modification of the amino acid from L to R at position 1090.
+The protein's natural variant, known as in SEMDSP;, features a modification of the amino acid from S to P at position 1197.
+The protein's natural variant, known as in SEMDSP; unknown pathological significance;, features a modification of the amino acid from E to Q at position 1288.
+The protein's natural variant, known as in variant D, features a modification of the amino acid from S to K at position 33.
+The protein's natural variant, known as in variant H, features a modification of the amino acid from R to C at position 40.
+The protein's natural variant, known as in variant E, features a modification of the amino acid from E to K at position 51.
+The protein's natural variant, known as in variant C, features a modification of the amino acid from E to K at position 52.
+The protein's natural variant, known as in variants A1, B, C, F and G, features a modification of the amino acid from P to H at position 82.
+The protein's natural variant, known as in variant H, features a modification of the amino acid from L to I at position 103.
+The natural variant of this protein is characterized by an amino acid alteration from M to L at position 108.
+The protein's natural variant, known as in variant A3, features a modification of the amino acid from H to Q at position 121.
+The protein's natural variant, known as in variants A1 and G, features a modification of the amino acid from E to Q at position 132.
+The protein's natural variant, known as in variant B, features a modification of the amino acid from S to R at position 137.
+The protein's natural variant, known as in variants A1 and H, features a modification of the amino acid from L to P at position 152.
+The protein's natural variant, known as in variants A1, G and H, features a modification of the amino acid from P to L at position 153.
+The protein's natural variant, known as in variant F, features a modification of the amino acid from P to L at position 167.
+The protein's natural variant, known as in variants A1 and G, features a modification of the amino acid from Q to E at position 190.
+The protein's natural variant, known as found in 37.5% of the Asian population, in 30% of the Caucasian population and in 16.3% of the African-American population; reduced adenylyl cyclase activity in response to stimulation of the beta-adregnergic receptor by Mn(2+) agonists isoproteronol and NaF; increased albuterol-stimulated adenylyl cyclase activity in the presence of corticosteroid;, features a modification of the amino acid from I to M at position 772.
+The protein's natural variant, known as found in prostate cancer samples; somatic mutation; does not up-regulates CDKN1A in a p53-independent manner and significantly reduces cell proliferation;, features a modification of the amino acid from W to R at position 64.
+The protein's natural variant, known as found in prostate cancer samples; somatic mutation; does not up-regulates CDKN1A in a p53-independent manner and significantly reduces cell proliferation;, features a modification of the amino acid from S to P at position 116.
+The protein's natural variant, known as found in prostate cancer samples; somatic mutation; does not up-regulates CDKN1A in a p53-independent manner and significantly reduces cell proliferation;, features a modification of the amino acid from A to D at position 123.
+The protein's natural variant, known as found in gastric cancer samples; somatic mutation;, features a modification of the amino acid from S to R at position 155.
+The protein's natural variant, known as found in prostate cancer samples; somatic mutation; does not up-regulates CDKN1A in a p53-independent manner and significantly reduces cell proliferation;, features a modification of the amino acid from L to P at position 169.
+The protein's natural variant, known as found in gastric cancer samples; somatic mutation, features a modification of the amino acid from P to T at position 172.
+The protein's natural variant, known as found in gastric cancer samples; somatic mutation;, features a modification of the amino acid from S to L at position 180.
+The protein's natural variant, known as found in gastric cancer samples; somatic mutation, features a modification of the amino acid from R to K at position 198.
+The protein's natural variant, known as in strain: HI1388, features a modification of the amino acid from I to V at position 18.
+The protein's natural variant, known as in strain: E1a, features a modification of the amino acid from IA to LT at position 28.
+The protein's natural variant, known as in strain: HI689, features a modification of the amino acid from S to F at position 54.
+The protein's natural variant, known as in strain: SJL/J, features a modification of the amino acid from E to Q at position 591.
+The protein's natural variant, known as in strain: PS178D4, features a modification of the amino acid from G to A at position 237.
+The protein's natural variant, known as in strain: PS178D4, features a modification of the amino acid from T to A at position 477.
+The protein's natural variant, known as in strain: PS178D4, features a modification of the amino acid from Q to K at position 586.
+The protein's natural variant, known as in strain: PS178D4, features a modification of the amino acid from ASD to HVT at position 994.
+The protein's natural variant, known as in strain: PS178D4, features a modification of the amino acid from G to D at position 1016.
+The protein's natural variant, known as in strain: PS178D4, features a modification of the amino acid from L to F at position 1050.
+The protein's natural variant, known as found in a patient with Sertoli cell-only syndrome; unknown pathological significance;, features a modification of the amino acid from R to H at position 545.
+The protein's natural variant, known as in strain: F24.1, MT32 and MT68, features a modification of the amino acid from G to C at position 32.
+The protein's natural variant, known as in strain: Z74, features a modification of the amino acid from T to N at position 80.
+The protein's natural variant, known as in strain: F23.3, MT41, Z3, Z5, Z11, Z16, Z21, Z27, Z42, Z55, Z64, Z74 and Berkeley, features a modification of the amino acid from L to P at position 382.
+The protein's natural variant, known as lover plasma LDL-cholesterol and HDL-cholesterol levels;, features a modification of the amino acid from R to W at position 59.
+The natural variant of this protein is characterized by an amino acid alteration from SGS to RAF at position 237.
+The natural variant of this protein is characterized by an amino acid alteration from F to C at position 507.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from V to M at position 45.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from D to N at position 119.
+The protein's natural variant, known as in PMNDS, features a modification of the amino acid from R to Q at position 193.
+The protein's natural variant, known as in PMNDS, features a modification of the amino acid from R to W at position 193.
+The protein's natural variant, known as in PMNDS; unknown pathological significance, features a modification of the amino acid from A to V at position 272.
+The protein's natural variant, known as in PMNDS, features a modification of the amino acid from E to K at position 427.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from R to G at position 667.
+The protein's natural variant, known as in PMNDS, features a modification of the amino acid from S to F at position 912.
+The protein's natural variant, known as in PMNDS, features a modification of the amino acid from D to N at position 1084.
+The protein's natural variant, known as in PMNDS, features a modification of the amino acid from P to L at position 1124.
+The protein's natural variant, known as in PMNDS, features a modification of the amino acid from R to H at position 1136.
+The protein's natural variant, known as in PMNDS, features a modification of the amino acid from N to I at position 1140.
+The protein's natural variant, known as in PMNDS, features a modification of the amino acid from I to M at position 1419.
+The protein's natural variant, known as in PMNDS, features a modification of the amino acid from D to V at position 1488.
+The protein's natural variant, known as in PMNDS, features a modification of the amino acid from E to G at position 1714.
+The protein's natural variant, known as in strain: NOD, features a modification of the amino acid from S to N at position 291.
+The protein's natural variant, known as in strain: CIP 102503T and NEM1250, features a modification of the amino acid from D to A at position 119.
+The protein's natural variant, known as in GSD-Ia, features a modification of the amino acid from M to I at position 121.
+The protein's natural variant, known as in strain: L2/434/Bu, features a modification of the amino acid from AGI to RGT at position 263.
+The protein's natural variant, known as in strain: L2/434/Bu, features a modification of the amino acid from R to K at position 334.
+The protein's natural variant, known as in strain: L2/434/Bu, features a modification of the amino acid from R to H at position 373.
+The protein's natural variant, known as in BFLS; Loss of interaction with UBTF;, features a modification of the amino acid from C to Y at position 45.
+The protein's natural variant, known as in BFLS; Loss of interaction with UBTF;, features a modification of the amino acid from C to F at position 99.
+The protein's natural variant, known as in BFLS;, features a modification of the amino acid from H to R at position 229.
+The protein's natural variant, known as in BFLS;, features a modification of the amino acid from K to E at position 234.
+The protein's natural variant, known as in BFLS;, features a modification of the amino acid from R to G at position 257.
+The protein's natural variant, known as in BFLS;, features a modification of the amino acid from C to F at position 305.
+The protein's natural variant, known as no effect on activity;, features a modification of the amino acid from P to T at position 8.
+The protein's natural variant, known as in CCDS2;, features a modification of the amino acid from W to S at position 20.
+The protein's natural variant, known as no effect on activity;, features a modification of the amino acid from Y to H at position 27.
+The protein's natural variant, known as no effect on enzymatic activity;, features a modification of the amino acid from R to L at position 44.
+The protein's natural variant, known as in CCDS2; loss of activity;, features a modification of the amino acid from W to R at position 45.
+The protein's natural variant, known as in CCDS2; retains no significant activity;, features a modification of the amino acid from M to L at position 50.
+The protein's natural variant, known as in CCDS2; retains no significant activity, features a modification of the amino acid from H to P at position 51.
+The protein's natural variant, known as in CCDS2; loss of activity;, features a modification of the amino acid from A to P at position 54.
+The protein's natural variant, known as in CCDS2; retains no significant activity;, features a modification of the amino acid from G to C at position 68.
+The protein's natural variant, known as no effect on enzymatic activity;, features a modification of the amino acid from M to V at position 71.
+The protein's natural variant, known as in CCDS2; retains no significant activity;, features a modification of the amino acid from A to V at position 75.
+The protein's natural variant, known as no effect on enzymatic activity;, features a modification of the amino acid from S to L at position 76.
+The protein's natural variant, known as in CCDS2, features a modification of the amino acid from V to E at position 78.
+The protein's natural variant, known as no effect on enzymatic activity;, features a modification of the amino acid from V to M at position 78.
+The protein's natural variant, known as no effect on enzymatic activity;, features a modification of the amino acid from V to I at position 95.
+The protein's natural variant, known as no effect on enzymatic activity;, features a modification of the amino acid from R to Q at position 105.
+The protein's natural variant, known as disrupts enzymatic activity;, features a modification of the amino acid from Q to P at position 106.
+The protein's natural variant, known as in CCDS2; retains no significant activity;, features a modification of the amino acid from V to F at position 110.
+The protein's natural variant, known as in CCDS2;, features a modification of the amino acid from D to N at position 135.
+The protein's natural variant, known as no effect on enzymatic activity;, features a modification of the amino acid from T to R at position 146.
+The protein's natural variant, known as in CCDS2; retains no significant activity;, features a modification of the amino acid from H to Y at position 147.
+The protein's natural variant, known as disrupts enzymatic activity;, features a modification of the amino acid from A to D at position 156.
+The protein's natural variant, known as no effect on enzymatic activity;, features a modification of the amino acid from F to L at position 157.
+The protein's natural variant, known as in CCDS2; loss of activity, features a modification of the amino acid from L to P at position 159.
+The protein's natural variant, known as in CCDS2;, features a modification of the amino acid from G to D at position 164.
+The protein's natural variant, known as in CCDS2; loss of activity;, features a modification of the amino acid from L to P at position 166.
+The protein's natural variant, known as disrupts enzymatic activity;, features a modification of the amino acid from T to I at position 167.
+The protein's natural variant, known as in CCDS2;, features a modification of the amino acid from C to R at position 169.
+The protein's natural variant, known as in CCDS2; retains no significant activity;, features a modification of the amino acid from C to Y at position 169.
+The protein's natural variant, known as no effect on enzymatic activity;, features a modification of the amino acid from A to T at position 196.
+The protein's natural variant, known as no effect on enzymatic activity;, features a modification of the amino acid from A to V at position 196.
+The protein's natural variant, known as in CCDS2; loss of activity, features a modification of the amino acid from L to P at position 197.
+The protein's natural variant, known as in CCDS2; retains no significant activity;, features a modification of the amino acid from R to P at position 208.
+The protein's natural variant, known as no effect on enzymatic activity;, features a modification of the amino acid from A to T at position 224.
+The protein's natural variant, known as in TCS4; unknown pathological significance;, features a modification of the amino acid from S to R at position 682.
+The natural variant of this protein is characterized by an amino acid alteration from H to R at position 887.
+The protein's natural variant, known as in TCS4;, features a modification of the amino acid from R to C at position 1003.
+The protein's natural variant, known as in TCS4, features a modification of the amino acid from R to S at position 1003.
+The protein's natural variant, known as probable disease-associated variant found in a patient with non-syndromic sensorineural hearing loss;, features a modification of the amino acid from I to V at position 502.
+The protein's natural variant, known as in MRFACD; unknown pathological significance;, features a modification of the amino acid from E to G at position 251.
+The protein's natural variant, known as in a patient with dextro-looped transposition of the great arteries; unknown pathological significance;, features a modification of the amino acid from R to H at position 1872.
+The protein's natural variant, known as in a patient with dextro-looped transposition of the great arteries; unknown pathological significance;, features a modification of the amino acid from D to G at position 2023.
+The protein's natural variant, known as in strain: M31, features a modification of the amino acid from K to N at position 2.
+The protein's natural variant, known as in strain: M31, features a modification of the amino acid from V to I at position 50.
+The protein's natural variant, known as in strain: 950 and 5026, features a modification of the amino acid from R to Y at position 43.
+The natural variant of this protein is characterized by an amino acid alteration from R to Q at position 297.
+The protein's natural variant, known as in IECEE1;, features a modification of the amino acid from H to R at position 92.
+The protein's natural variant, known as in IECEE1, features a modification of the amino acid from N to I at position 150.
+The protein's natural variant, known as in IECEE1, features a modification of the amino acid from D to E at position 234.
+The protein's natural variant, known as in IECEE1;, features a modification of the amino acid from H to Q at position 281.
+The protein's natural variant, known as in IECEE1;, features a modification of the amino acid from E to K at position 282.
+The protein's natural variant, known as in IECEE1; unknown pathological significance;, features a modification of the amino acid from A to T at position 447.
+The protein's natural variant, known as in ACCIID;, features a modification of the amino acid from F to L at position 470.
+The protein's natural variant, known as in ACCIID;, features a modification of the amino acid from A to T at position 473.
+The protein's natural variant, known as in CPHD4; has impaired activity on CGA, POU1F1 and TSHB promoters but exhibits normal DNA binding to the CGA pituitary glycoprotein basal element (PGBE) and interaction with the POU1F1 protein;, features a modification of the amino acid from R to C at position 84.
+The protein's natural variant, known as in CPHD4; the mutant protein is inactive in DNA binding and pituitary gene activation assays;, features a modification of the amino acid from L to R at position 190.
+The protein's natural variant, known as in CPHD4; the mutant protein is inactive in DNA binding and pituitary gene activation assays;, features a modification of the amino acid from A to P at position 210.
+The protein's natural variant, known as in CPHD4;, features a modification of the amino acid from P to T at position 389.
+The protein's natural variant, known as in LYNCH2;, features a modification of the amino acid from R to C at position 18.
+The protein's natural variant, known as in LYNCH2; unknown pathological significance;, features a modification of the amino acid from I to F at position 19.
+The protein's natural variant, known as in LYNCH2;, features a modification of the amino acid from A to V at position 21.
+The protein's natural variant, known as in LYNCH2;, features a modification of the amino acid from I to F at position 25.
+The protein's natural variant, known as in LYNCH2; loss of protein expression; normal interaction with PMS2 and EXO1; decreased mismatch repair activity; no effect on nuclear localization;, features a modification of the amino acid from P to L at position 28.
+The protein's natural variant, known as in LYNCH2; unknown pathological significance; acts functionally like the wild-type protein;, features a modification of the amino acid from A to S at position 29.
+The protein's natural variant, known as in LYNCH2; requires 2 nucleotide substitutions; decreased mismatch repair activity;, features a modification of the amino acid from A to C at position 31.
+The protein's natural variant, known as in LYNCH2; unknown pathological significance, features a modification of the amino acid from M to K at position 35.
+The protein's natural variant, known as in MMRCS1; requires 2 nucleotide substitutions;, features a modification of the amino acid from M to N at position 35.
+The protein's natural variant, known as in LYNCH2;, features a modification of the amino acid from M to R at position 35.
+The protein's natural variant, known as found in an endometrial cancer sample; somatic mutation, features a modification of the amino acid from E to ELNH at position 37.
+The protein's natural variant, known as in LYNCH2; decreased mismatch repair activity; loss of nuclear localization;, features a modification of the amino acid from E to K at position 37.
+The protein's natural variant, known as in LYNCH2; decreased mismatch repair activity; no effect on nuclear localization;, features a modification of the amino acid from N to H at position 38.
+The protein's natural variant, known as in LYNCH2; decreased mismatch repair activity; no effect on nuclear localization;, features a modification of the amino acid from N to K at position 38.
+The protein's natural variant, known as in LYNCH2;, features a modification of the amino acid from D to G at position 41.
+The protein's natural variant, known as associated with LYNCH2; no effect on MLH1 splicing;, features a modification of the amino acid from D to H at position 41.
+The protein's natural variant, known as in LYNCH2; no effect on MLH1 splicing; loss of mismatch repair activity;, features a modification of the amino acid from S to F at position 44.
+The protein's natural variant, known as in LYNCH2; decreased mismatch repair activity; loss of protein expression; loss of nuclear localization, features a modification of the amino acid from TSI to CF at position 47.
+The protein's natural variant, known as in CRC; sporadic; somatic mutation; unknown pathological significance;, features a modification of the amino acid from G to E at position 54.
+The protein's natural variant, known as in LYNCH2; decreased mismatch repair activity;, features a modification of the amino acid from Q to K at position 62.
+The protein's natural variant, known as in LYNCH2; decreased mismatch repair activity; loss of protein expression; loss of nuclear localization;, features a modification of the amino acid from D to E at position 63.
+The protein's natural variant, known as in LYNCH2;, features a modification of the amino acid from N to S at position 64.
+The protein's natural variant, known as in CRC;, features a modification of the amino acid from G to E at position 67.
+The protein's natural variant, known as in LYNCH2; no effect on MLH1 splicing; decreased mismatch repair activity; loss of protein expression; loss of nuclear localization;, features a modification of the amino acid from G to R at position 67.
+The protein's natural variant, known as in LYNCH2;, features a modification of the amino acid from G to W at position 67.
+The protein's natural variant, known as in LYNCH2; decreased mismatch repair activity;, features a modification of the amino acid from I to N at position 68.
+The protein's natural variant, known as in LYNCH2; decreased mismatch repair activity;, features a modification of the amino acid from R to K at position 69.
+The protein's natural variant, known as in LYNCH2; decreased mismatch repair activity; loss of nuclear localization; normal interaction with PMS2;, features a modification of the amino acid from C to R at position 77.
+The protein's natural variant, known as in CRC; sporadic; early onset;, features a modification of the amino acid from C to Y at position 77.
+The protein's natural variant, known as in LYNCH2; decreased mismatch repair activity;, features a modification of the amino acid from F to V at position 80.
+The protein's natural variant, known as in LYNCH2; decreased mismatch repair activity;, features a modification of the amino acid from K to E at position 84.
+The protein's natural variant, known as normal interaction with PMS2; no decrease in mismatch repair activity; no effect on nuclear localization;, features a modification of the amino acid from S to G at position 93.
+The protein's natural variant, known as associated with LYNCH2; no effect on MLH1 splicing;, features a modification of the amino acid from G to S at position 98.
+The protein's natural variant, known as in LYNCH2; no effect on MLH1 splicing;, features a modification of the amino acid from G to D at position 101.
+The protein's natural variant, known as associated with LYNCH2; no effect on MLH1 splicing;, features a modification of the amino acid from G to S at position 101.
+The protein's natural variant, known as in LYNCH2; unknown pathological significance;, features a modification of the amino acid from E to K at position 102.
+The protein's natural variant, known as in gastric cancer; unknown pathological significance;, features a modification of the amino acid from S to R at position 106.
+The protein's natural variant, known as in LYNCH2; decreased mismatch repair activity; normal interaction with PMS2; loss of protein expression; loss of nuclear localization;, features a modification of the amino acid from I to R at position 107.
+The protein's natural variant, known as in LYNCH2; decreased mismatch repair activity; no effect on nuclear localization;, features a modification of the amino acid from H to P at position 109.
+The protein's natural variant, known as in gastric cancer; unknown pathological significance;, features a modification of the amino acid from H to Q at position 109.
+The protein's natural variant, known as in LYNCH2; decreased mismatch repair activity;, features a modification of the amino acid from A to P at position 111.
+The protein's natural variant, known as in LYNCH2; unknown pathological significance;, features a modification of the amino acid from A to V at position 111.
+The protein's natural variant, known as associated with LYNCH2; no effect on MLH1 splicing;, features a modification of the amino acid from T to K at position 116.
+The protein's natural variant, known as no effect on protein expression;, features a modification of the amino acid from T to R at position 116.
+The protein's natural variant, known as in LYNCH2; decreased mismatch repair activity; no effect on MLH1 splicing; fails to interact with PMS2 and EXO1; loss of nuclear localization;, features a modification of the amino acid from T to M at position 117.
+The protein's natural variant, known as in LYNCH2; decreased mismatch repair activity;, features a modification of the amino acid from T to R at position 117.
+The protein's natural variant, known as associated with LYNCH2; no effect on MLH1 splicing;, features a modification of the amino acid from Y to N at position 126.
+The protein's natural variant, known as in LYNCH2;, features a modification of the amino acid from A to P at position 128.
+The protein's natural variant, known as in CRC; sporadic; susceptibility to; ATPase function attenuated but not eliminated;, features a modification of the amino acid from D to H at position 132.
+The protein's natural variant, known as in LYNCH2; decreased mismatch repair activity; loss of protein expression; loss of nuclear localization;, features a modification of the amino acid from L to R at position 155.
+The protein's natural variant, known as in LYNCH2; incomplete;, features a modification of the amino acid from R to G at position 182.
+The protein's natural variant, known as in LYNCH2;, features a modification of the amino acid from R to K at position 182.
+The protein's natural variant, known as in LYNCH2; decreased mismatch repair activity; loss of protein expression; loss of nuclear localization; no effect on MLH1 splicing;, features a modification of the amino acid from V to G at position 185.
+The protein's natural variant, known as in LYNCH2; unknown pathological significance;, features a modification of the amino acid from V to L at position 185.
+The protein's natural variant, known as in LYNCH2;, features a modification of the amino acid from S to P at position 193.
+The protein's natural variant, known as no effect on protein expression;, features a modification of the amino acid from V to L at position 213.
+The protein's natural variant, known as no effect on MLH1 splicing;, features a modification of the amino acid from V to M at position 213.
+The protein's natural variant, known as associated with LYNCH2; no effect on MLH1 splicing;, features a modification of the amino acid from N to S at position 215.
+The protein's natural variant, known as associated with LYNCH2; no effect on MLH1 splicing;, features a modification of the amino acid from I to S at position 216.
+The protein's natural variant, known as in LYNCH2; unknown pathological significance; no decrease in mismatch repair activity;, features a modification of the amino acid from R to C at position 217.
+The natural variant of this protein is characterized by an amino acid alteration from R to G at position 217.
+The protein's natural variant, known as no decrease in mismatch repair activity; no effect on nuclear localization;, features a modification of the amino acid from I to V at position 219.
+The protein's natural variant, known as in LYNCH2;, features a modification of the amino acid from R to L at position 226.
+The protein's natural variant, known as in LYNCH2; unknown pathological significance;, features a modification of the amino acid from E to G at position 234.
+The protein's natural variant, known as in LYNCH2; decreased mismatch repair activity;, features a modification of the amino acid from G to D at position 244.
+The protein's natural variant, known as in CRC; sporadic; somatic mutation; unknown pathological significance;, features a modification of the amino acid from G to V at position 244.
+The protein's natural variant, known as in LYNCH2; decreased mismatch repair activity; loss of protein expression; loss of nuclear localization;, features a modification of the amino acid from S to P at position 247.
+The protein's natural variant, known as in LYNCH2; unknown pathological significance; no effect on MLH1 splicing;, features a modification of the amino acid from L to F at position 260.
+The protein's natural variant, known as in CRC;, features a modification of the amino acid from L to R at position 260.
+The protein's natural variant, known as no effect on protein expression;, features a modification of the amino acid from H to L at position 264.
+The protein's natural variant, known as in LYNCH2;, features a modification of the amino acid from H to Y at position 264.
+The protein's natural variant, known as in LYNCH2; results in partial MLH1 exon 10 skipping on ex vivo splicing assay; decreased mismatch repair activity; no effect on nuclear localization;, features a modification of the amino acid from R to C at position 265.
+The protein's natural variant, known as associated with LYNCH2; results in partial MLH1 exon 10 skipping on ex vivo splicing assay; decreased mismatch repair activity;, features a modification of the amino acid from R to H at position 265.
+The protein's natural variant, known as in LYNCH2; decreased mismatch repair activity;, features a modification of the amino acid from R to S at position 265.
+The protein's natural variant, known as in CRC;, features a modification of the amino acid from E to G at position 268.
+The protein's natural variant, known as in LYNCH2;, features a modification of the amino acid from A to G at position 282.
+The protein's natural variant, known as in LYNCH2; unknown pathological significance;, features a modification of the amino acid from L to P at position 292.
+The protein's natural variant, known as in LYNCH2;, features a modification of the amino acid from S to T at position 295.
+The protein's natural variant, known as in LYNCH2;, features a modification of the amino acid from D to V at position 304.
+The protein's natural variant, known as associated with LYNCH2; no effect on MLH1 splicing;, features a modification of the amino acid from E to D at position 320.
+The protein's natural variant, known as in LYNCH2; unknown pathological significance;, features a modification of the amino acid from S to I at position 321.
+The protein's natural variant, known as in CRC; sporadic; somatic mutation; unknown pathological significance;, features a modification of the amino acid from R to Q at position 325.
+The protein's natural variant, known as in LYNCH2; no decrease in mismatch repair activity;, features a modification of the amino acid from V to A at position 326.
+The protein's natural variant, known as in LYNCH2; loss of protein expression; loss of nuclear localization;, features a modification of the amino acid from H to P at position 329.
+The protein's natural variant, known as in LYNCH2;, features a modification of the amino acid from N to S at position 338.
+The protein's natural variant, known as in LYNCH2;, features a modification of the amino acid from Y to C at position 379.
+The protein's natural variant, known as can be associated with HNPCC in some populations;, features a modification of the amino acid from V to D at position 384.
+The protein's natural variant, known as in LYNCH2; unknown pathological significance;, features a modification of the amino acid from R to C at position 385.
+The protein's natural variant, known as in LYNCH2; unknown pathological significance;, features a modification of the amino acid from R to P at position 385.
+The protein's natural variant, known as in LYNCH2; unknown pathological significance; no effect on nuclear localization; normal interaction with PMS2 and EXO1;, features a modification of the amino acid from R to W at position 389.
+The protein's natural variant, known as no decrease in mismatch repair activity; no effect on nuclear localization;, features a modification of the amino acid from P to S at position 403.
+The protein's natural variant, known as no decrease in mismatch repair activity; no effect on nuclear localization;, features a modification of the amino acid from S to N at position 406.
+The protein's natural variant, known as no effect on protein expression;, features a modification of the amino acid from R to T at position 423.
+The protein's natural variant, known as in LYNCH2;, features a modification of the amino acid from A to T at position 441.
+The protein's natural variant, known as in LYNCH2; unknown pathological significance; no decrease in mismatch repair activity; no effect on nuclear localization;, features a modification of the amino acid from K to Q at position 443.
+The protein's natural variant, known as in LYNCH2; unknown pathological significance;, features a modification of the amino acid from E to A at position 460.
+The protein's natural variant, known as in CRC; unknown pathological significance;, features a modification of the amino acid from R to I at position 472.
+The protein's natural variant, known as in LYNCH2; unknown pathological significance;, features a modification of the amino acid from R to Q at position 474.
+The protein's natural variant, known as associated with LYNCH2; no effect on MLH1 splicing;, features a modification of the amino acid from R to W at position 474.
+The protein's natural variant, known as in LYNCH2;, features a modification of the amino acid from D to E at position 485.
+The protein's natural variant, known as in LYNCH2; unknown pathological significance;, features a modification of the amino acid from D to H at position 485.
+The protein's natural variant, known as in LYNCH2; also found in sporadic colorectal cancer;, features a modification of the amino acid from A to T at position 492.
+The protein's natural variant, known as in LYNCH2;, features a modification of the amino acid from V to A at position 506.
+The protein's natural variant, known as associated with LYNCH2; no effect on MLH1 splicing;, features a modification of the amino acid from A to D at position 539.
+The protein's natural variant, known as in LYNCH2; type II; decreased mismatch repair activity;, features a modification of the amino acid from Q to L at position 542.
+The protein's natural variant, known as in LYNCH2;, features a modification of the amino acid from Q to P at position 542.
+The protein's natural variant, known as in LYNCH2; no effect on MLH1 splicing;, features a modification of the amino acid from L to P at position 549.
+The protein's natural variant, known as in LYNCH2; decreased mismatch repair activity; defective in interaction with PMS2 and EXO1; loss of protein expression; may lose nuclear localization;, features a modification of the amino acid from L to P at position 550.
+The protein's natural variant, known as in LYNCH2; no effect on MLH1 splicing;, features a modification of the amino acid from N to T at position 551.
+The protein's natural variant, known as in LYNCH2;, features a modification of the amino acid from L to R at position 559.
+The protein's natural variant, known as in LYNCH2;, features a modification of the amino acid from I to F at position 565.
+The protein's natural variant, known as in LYNCH2; type I; abrogates interaction with EXO1;, features a modification of the amino acid from L to P at position 574.
+The protein's natural variant, known as in LYNCH2 and CRC; unknown pathological significance; no decrease in mismatch repair activity; no effect on nuclear localization;, features a modification of the amino acid from E to G at position 578.
+The protein's natural variant, known as in LYNCH2; decreased mismatch repair activity; no effect on nuclear localization;, features a modification of the amino acid from L to F at position 582.
+The protein's natural variant, known as in LYNCH2; type II;, features a modification of the amino acid from L to V at position 582.
+The protein's natural variant, known as associated with LYNCH2; no effect on MLH1 splicing;, features a modification of the amino acid from L to R at position 585.
+The protein's natural variant, known as in LYNCH2;, features a modification of the amino acid from A to P at position 586.
+The protein's natural variant, known as in LYNCH2;, features a modification of the amino acid from L to P at position 588.
+The protein's natural variant, known as in LYNCH2; decreased mismatch repair activity; loss of interaction with PMS2 and EXO1; loss of protein expression; may lose nuclear localization;, features a modification of the amino acid from A to D at position 589.
+The protein's natural variant, known as in CRC; unknown pathological significance;, features a modification of the amino acid from D to G at position 601.
+The protein's natural variant, known as in LYNCH2; unknown pathological significance; no effect on MLH1 splicing;, features a modification of the amino acid from P to R at position 603.
+The protein's natural variant, known as in LYNCH2; unknown pathological significance; also found in lobular carcinoma in situ of the breast; no effect on MLH1 splicing;, features a modification of the amino acid from L to H at position 607.
+The protein's natural variant, known as in LYNCH2; unknown pathological significance; requires 2 nucleotide substitutions; interacts weakly with PMS2; no decrease in mismatch repair activity; no effect on nuclear localization;, features a modification of the amino acid from K to A at position 618.
+The protein's natural variant, known as in CRC;, features a modification of the amino acid from K to R at position 618.
+The protein's natural variant, known as in LYNCH2; type II; loss of nuclear localization;, features a modification of the amino acid from K to T at position 618.
+The protein's natural variant, known as associated with LYNCH2; no effect on MLH1 splicing;, features a modification of the amino acid from A to P at position 619.
+The protein's natural variant, known as in LYNCH2;, features a modification of the amino acid from L to H at position 622.
+The protein's natural variant, known as in LYNCH2; unknown pathological significance;, features a modification of the amino acid from A to P at position 623.
+The protein's natural variant, known as in LYNCH2, features a modification of the amino acid from FS to ST at position 627.
+The protein's natural variant, known as in LYNCH2; unknown pathological significance;, features a modification of the amino acid from D to A at position 631.
+The protein's natural variant, known as in gastric cancer; unknown pathological significance;, features a modification of the amino acid from N to K at position 635.
+The protein's natural variant, known as in LYNCH2;, features a modification of the amino acid from L to P at position 636.
+The protein's natural variant, known as associated with LYNCH2; no effect on MLH1 splicing;, features a modification of the amino acid from P to L at position 640.
+The protein's natural variant, known as in LYNCH2; no effect on MLH1 splicing;, features a modification of the amino acid from P to S at position 640.
+The protein's natural variant, known as in LYNCH2; defective in interaction with PMS2 and EXO1; no decrease in mismatch repair activity;, features a modification of the amino acid from Y to C at position 646.
+The protein's natural variant, known as in LYNCH2; unknown pathological significance; defective in interaction with PMS2 and EXO1; may lose nuclear localization; loss of protein expression; no decrease in mismatch repair activity;, features a modification of the amino acid from P to L at position 648.
+The protein's natural variant, known as in LYNCH2; the protein is unstable; loss of nuclear localization; loss of protein expression; no decrease in mismatch repair activity;, features a modification of the amino acid from P to S at position 648.
+The protein's natural variant, known as in LYNCH2; decreased mismatch repair activity; defective in interaction with PMS2 and EXO1; loss of protein expression; may lose nuclear localization;, features a modification of the amino acid from P to L at position 654.
+The protein's natural variant, known as in LYNCH2; also found in an endometrial cancer sample; no effect on MLH1 splicing;, features a modification of the amino acid from I to V at position 655.
+The protein's natural variant, known as in LYNCH2; no effect on MLH1 splicing;, features a modification of the amino acid from F to S at position 656.
+The protein's natural variant, known as in LYNCH2;, features a modification of the amino acid from R to L at position 659.
+The protein's natural variant, known as in LYNCH2; interacts only very weakly with PMS2; abrogates interaction with EXO1; decreased mismatch repair activity; may lose nuclear localization;, features a modification of the amino acid from R to P at position 659.
+The protein's natural variant, known as in LYNCH2; unknown pathological significance;, features a modification of the amino acid from R to Q at position 659.
+The protein's natural variant, known as in LYNCH2; unknown pathological significance;, features a modification of the amino acid from T to P at position 662.
+The protein's natural variant, known as in LYNCH2; unknown pathological significance; no effect on MLH1 splicing;, features a modification of the amino acid from W to R at position 666.
+The protein's natural variant, known as in LYNCH2 and CRC; abrogates interaction with EXO1; no decrease in mismatch repair activity;, features a modification of the amino acid from A to T at position 681.
+The protein's natural variant, known as in LYNCH2; unknown pathological significance;, features a modification of the amino acid from R to W at position 687.
+The protein's natural variant, known as in HNPCC; unknown pathological significance;, features a modification of the amino acid from Q to R at position 689.
+The protein's natural variant, known as no decrease in mismatch repair activity; no effect on nuclear localization;, features a modification of the amino acid from V to M at position 716.
+The protein's natural variant, known as in LYNCH2; unknown pathological significance;, features a modification of the amino acid from H to Y at position 718.
+The protein's natural variant, known as in LYNCH2, features a modification of the amino acid from I to INVFHI at position 719.
+The protein's natural variant, known as in LYNCH2;, features a modification of the amino acid from L to M at position 724.
+The protein's natural variant, known as reduces by 60% protein expression;, features a modification of the amino acid from R to H at position 725.
+The protein's natural variant, known as in CRC;, features a modification of the amino acid from L to P at position 749.
+The protein's natural variant, known as in LYNCH2; unknown pathological significance;, features a modification of the amino acid from K to R at position 751.
+The protein's natural variant, known as in HNPCC; incomplete;, features a modification of the amino acid from R to W at position 755.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from Q to H at position 9.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from T to A at position 23.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from D to H at position 28.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from D to Y at position 28.
+The protein's natural variant, known as in GALAC1; mild;, features a modification of the amino acid from I to N at position 32.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from R to H at position 33.
+The protein's natural variant, known as in GALAC1, features a modification of the amino acid from R to P at position 33.
+The protein's natural variant, known as in GALAC1; affects protein stability;, features a modification of the amino acid from Y to N at position 34.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from Q to P at position 38.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from V to L at position 44.
+The protein's natural variant, known as in GALAC1; reduced enzyme activity;, features a modification of the amino acid from V to M at position 44.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from S to L at position 45.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from R to L at position 51.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from R to Q at position 51.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from G to C at position 55.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from R to C at position 67.
+The protein's natural variant, known as in GALAC1; reduced enzyme activity;, features a modification of the amino acid from L to P at position 74.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from A to T at position 81.
+The protein's natural variant, known as in GALAC1, features a modification of the amino acid from G to V at position 83.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from Y to H at position 89.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from N to S at position 97.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from D to N at position 98.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from Q to R at position 103.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from S to R at position 112.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from D to N at position 113.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from H to L at position 114.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from F to S at position 117.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from Q to H at position 118.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from R to G at position 123.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from R to Q at position 123.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from V to A at position 125.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from K to E at position 127.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from M to T at position 129.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from C to Y at position 130.
+The protein's natural variant, known as in GALAC1; affects protein stability;, features a modification of the amino acid from H to Q at position 132.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from H to Y at position 132.
+The protein's natural variant, known as in GALAC1; about 5% of normal galactose uridylyltransferase activity;, features a modification of the amino acid from S to L at position 135.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from S to W at position 135.
+The protein's natural variant, known as in GALAC1; mild;, features a modification of the amino acid from T to M at position 138.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from L to P at position 139.
+The protein's natural variant, known as in GALAC1; 4% of normal activity;, features a modification of the amino acid from M to K at position 142.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from M to T at position 142.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from M to V at position 142.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from S to L at position 143.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from R to G at position 148.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from R to Q at position 148.
+The protein's natural variant, known as in GALAC1; unstable protein;, features a modification of the amino acid from R to W at position 148.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from V to L at position 150.
+The protein's natural variant, known as in GALAC1; approximately 3% of normal activity;, features a modification of the amino acid from V to A at position 151.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from W to G at position 154.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from P to A at position 166.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from W to R at position 167.
+The protein's natural variant, known as in GALAC1; loss of activity;, features a modification of the amino acid from V to L at position 168.
+The protein's natural variant, known as in GALAC1; loss of activity;, features a modification of the amino acid from I to T at position 170.
+The protein's natural variant, known as in GALAC1; reduced enzyme activity;, features a modification of the amino acid from F to S at position 171.
+The protein's natural variant, known as in GALAC1; strongly reduces galactose uridylyltransferase activity;, features a modification of the amino acid from G to D at position 175.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from G to D at position 179.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from S to A at position 181.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from S to F at position 181.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from P to T at position 183.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from H to Q at position 184.
+The protein's natural variant, known as in GALAC1; loss of activity;, features a modification of the amino acid from P to H at position 185.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from P to L at position 185.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from P to S at position 185.
+The protein's natural variant, known as in GALAC1; most common mutation; 10% of normal galactose uridylyltransferase activity; impairs protein folding;, features a modification of the amino acid from Q to R at position 188.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from S to G at position 192.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from S to N at position 192.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from F to L at position 194.
+The protein's natural variant, known as in GALAC1; no enzymatic activity;, features a modification of the amino acid from L to P at position 195.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from I to M at position 198.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from I to T at position 198.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from A to T at position 199.
+The protein's natural variant, known as in GALAC1; 2-fold decrease in activity;, features a modification of the amino acid from R to C at position 201.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from R to H at position 201.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from E to K at position 203.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from R to P at position 204.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from Y to C at position 209.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from Y to S at position 209.
+The protein's natural variant, known as in GALAC1, features a modification of the amino acid from Q to H at position 212.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from L to P at position 217.
+The protein's natural variant, known as in GALAC1; 3-fold decrease in activity;, features a modification of the amino acid from E to K at position 220.
+The protein's natural variant, known as in GALAC1; 3-fold decrease in activity;, features a modification of the amino acid from R to S at position 223.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from L to P at position 226.
+The protein's natural variant, known as in GALAC1; results in no detectable protein in the soluble fraction;, features a modification of the amino acid from L to P at position 227.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from K to N at position 229.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from R to C at position 231.
+The protein's natural variant, known as in GALAC1; 15% of normal activity;, features a modification of the amino acid from R to H at position 231.
+The protein's natural variant, known as in GALAC1, features a modification of the amino acid from P to S at position 244.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from W to R at position 249.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from Y to C at position 251.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from Y to S at position 251.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from Q to H at position 252.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from R to C at position 258.
+The protein's natural variant, known as in GALAC1; loss of activity;, features a modification of the amino acid from R to Q at position 259.
+The protein's natural variant, known as in GALAC1; mild;, features a modification of the amino acid from R to W at position 259.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from R to P at position 262.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from P to A at position 265.
+The protein's natural variant, known as in GALAC1, features a modification of the amino acid from L to R at position 267.
+The protein's natural variant, known as in GALAC1, features a modification of the amino acid from L to V at position 267.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from E to D at position 271.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from R to G at position 272.
+The protein's natural variant, known as in GALAC1; 18-fold decrease in activity;, features a modification of the amino acid from I to N at position 278.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from L to V at position 282.
+The protein's natural variant, known as in GALAC1; severe; impairs protein folding; nearly abolishes enzyme activity;, features a modification of the amino acid from K to N at position 285.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from K to R at position 285.
+The protein's natural variant, known as in GALAC1; 3-fold decrease in activity;, features a modification of the amino acid from L to F at position 289.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from L to R at position 289.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from E to K at position 291.
+The protein's natural variant, known as in GALAC1; 2-fold decrease in activity;, features a modification of the amino acid from E to V at position 291.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from F to Y at position 294.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from E to K at position 308.
+The protein's natural variant, known as in GALAC1; allele Duarte; exists as allelic variants Duarte-1 and Duarte-2; Duarte-1 has normal or increased activity; Duarte-2 has activity reduced to about 35-45% of normal;, features a modification of the amino acid from N to D at position 314.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from Q to H at position 317.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from Q to R at position 317.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from H to Q at position 319.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from A to T at position 320.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from Y to D at position 323.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from Y to H at position 323.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from P to S at position 324.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from P to L at position 325.
+The protein's natural variant, known as in GALAC1; results in no detectable protein in the soluble fraction;, features a modification of the amino acid from L to P at position 327.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from R to H at position 328.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from S to F at position 329.
+The protein's natural variant, known as in GALAC1; mild;, features a modification of the amino acid from A to V at position 330.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from R to G at position 333.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from R to L at position 333.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from R to Q at position 333.
+The protein's natural variant, known as in GALAC1; no enzymatic activity;, features a modification of the amino acid from R to W at position 333.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from K to R at position 334.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from M to L at position 336.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from L to I at position 342.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from Q to K at position 344.
+The protein's natural variant, known as in GALAC1;, features a modification of the amino acid from A to D at position 345.
+The protein's natural variant, known as in GALAC1; mild;, features a modification of the amino acid from T to A at position 350.
+The protein's natural variant, known as in GLM; non-brain stem pediatric glioblastoma and diffuse intrinsic pontine glioma; somatic mutation; results in a global decrease of H3K27me3 levels;, features a modification of the amino acid from K to M at position 28.
+The protein's natural variant, known as probable disease-associated variant found in pediatric undifferentiated soft tissue sarcoma samples; somatic mutation; results in global decrease of H3K36me2 and H3K36me3 levels and increased H3K27me3 levels, features a modification of the amino acid from K to I at position 37.
+The protein's natural variant, known as probable disease-associated variant found in pediatric undifferentiated soft tissue sarcoma samples; somatic mutation; also found in a subset of human papillomavirus-negative head and neck squamous cell carcinomas; results in global decrease of H3K36me2 and H3K36me3 levels and increased H3K27me3 levels, features a modification of the amino acid from K to M at position 37.
+The protein's natural variant, known as in CTRCT5; sporadic; decreased binding to the DNASE2B promoter and decreased DNASE2B expression; impaired RAD51 induction and UVC-induced DNA damage repair;, features a modification of the amino acid from A to D at position 19.
+The protein's natural variant, known as in CTRCT5; decreased binding to the DNASE2B promoter and decreased DNASE2B expression; impaired RAD51 induction and UVC-induced DNA damage repair, features a modification of the amino acid from R to H at position 73.
+The protein's natural variant, known as in CTRCT5; sporadic;, features a modification of the amino acid from I to V at position 86.
+The protein's natural variant, known as in CTRCT5; decreased binding to the DNASE2B promoter and decreased DNASE2B expression; impaired RAD51 induction;, features a modification of the amino acid from L to P at position 114.
+The protein's natural variant, known as in CTRCT5; unknown pathological significance; decreased binding to the DNASE2B promoter and decreased DNASE2B expression; impaired RAD51 induction and UVC-induced DNA damage repair;, features a modification of the amino acid from R to C at position 119.
+The protein's natural variant, known as in THC4; increases the pro-apoptotic function by triggering caspase activation more efficiently than wild-type; does not affect the redox function;, features a modification of the amino acid from G to S at position 42.
+The natural variant of this protein is characterized by an amino acid alteration from M to L at position 66.
+The protein's natural variant, known as in HAE7; unknown pathological significance;, features a modification of the amino acid from R to S at position 217.
+The protein's natural variant, known as webb (WB) antigen;, features a modification of the amino acid from N to S at position 8.
+The protein's natural variant, known as duch (DH(a)) antigen;, features a modification of the amino acid from L to F at position 14.
+The protein's natural variant, known as ahonen (AN(a)) antigen;, features a modification of the amino acid from A to S at position 23.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from G to S at position 454.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from M to I at position 476.
+The natural variant of this protein is characterized by an amino acid alteration from A to P at position 202.
+The natural variant of this protein is characterized by an amino acid alteration from I to T at position 213.
+The natural variant of this protein is characterized by an amino acid alteration from R to G at position 344.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from G to E at position 56.
+The protein's natural variant, known as in strain: G130 and G140, features a modification of the amino acid from I to M at position 71.
+The protein's natural variant, known as in strain: G125, G130 and G140, features a modification of the amino acid from K to P at position 87.
+The protein's natural variant, known as in strain: G02, G125, G130 and G140, features a modification of the amino acid from T to P at position 135.
+The protein's natural variant, known as in strain: G02, G130 and G140, features a modification of the amino acid from P to T at position 143.
+The protein's natural variant, known as in strain: G125, features a modification of the amino acid from H to Q at position 149.
+The protein's natural variant, known as in GPIBD11; reduced protein abundance; decreased function in GPI-anchored protein transport;, features a modification of the amino acid from T to P at position 71.
+The protein's natural variant, known as in GPIBD11; no effect on protein abundance; loss of function in GPI-anchored protein transport;, features a modification of the amino acid from M to V at position 167.
+The protein's natural variant, known as does not affect plasma membrane expression. Does not affect TEA and metformin transport;, features a modification of the amino acid from V to L at position 10.
+The protein's natural variant, known as decreases plasma membrane expression. Transport of TEA and metformin are reduced by at least 90%, features a modification of the amino acid from G to D at position 64.
+The protein's natural variant, known as does not affect plasma membrane expression. Decreases TEA and metformin transport. Vmax value for TEA transport is decreased. Km value for TEA is increased;, features a modification of the amino acid from A to V at position 310.
+The protein's natural variant, known as decreases plasma membrane expression. Decreases TEA and metformin transport. Vmax value for TEA transport is decreased;, features a modification of the amino acid from D to A at position 328.
+The protein's natural variant, known as does not affect plasma membrane localization. Decreases TEA transport. Km value for TEA is increased. Does not affect metformin transport;, features a modification of the amino acid from N to S at position 474.
+The protein's natural variant, known as found in a child with sporadic epilepsy; unknown pathological significance;, features a modification of the amino acid from R to C at position 604.
+The protein's natural variant, known as in RDEOP;, features a modification of the amino acid from E to K at position 79.
+The protein's natural variant, known as in MCOPS5;, features a modification of the amino acid from R to G at position 89.
+The protein's natural variant, known as in MCOPS5; does not affect the expression or nuclear localization of the protein but inhibits its DNA-binding activity as well as its transactivation capability; the protein is non-functional, features a modification of the amino acid from R to S at position 90.
+The protein's natural variant, known as in MCOPS5;, features a modification of the amino acid from P to T at position 133.
+The protein's natural variant, known as in MCOPS5;, features a modification of the amino acid from P to A at position 134.
+The protein's natural variant, known as in CPHD6; unknown pathological significance; loss of transcriptional activity, when tested on bicoid binding sites; decreases transactivation mediated by the wild-type protein, when tested on bicoid binding sites; no effect on DNA-binding;, features a modification of the amino acid from P to R at position 134.
+The protein's natural variant, known as in CPHD6; acts as a dominant inhibitor of the HESX1 gene;, features a modification of the amino acid from N to S at position 225.
+The protein's natural variant, known as in strain: 35, features a modification of the amino acid from Q to L at position 25.
+The protein's natural variant, known as in strain: 7, features a modification of the amino acid from K to R at position 33.
+The protein's natural variant, known as in strain: 77 25 and Praslin, features a modification of the amino acid from S to F at position 36.
+The protein's natural variant, known as in strain: 7, features a modification of the amino acid from T to M at position 37.
+The protein's natural variant, known as in strain: 7, features a modification of the amino acid from K to N at position 38.
+The protein's natural variant, known as in strain: 7, features a modification of the amino acid from S to I at position 39.
+The protein's natural variant, known as in strain: 7, features a modification of the amino acid from L to F at position 117.
+The protein's natural variant, known as in strain: 7, features a modification of the amino acid from I to V at position 207.
+The protein's natural variant, known as in strain: 11, features a modification of the amino acid from G to W at position 244.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from P to T at position 244.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from R to W at position 1174.
+The protein's natural variant, known as found in a CNS cancer cell line;, features a modification of the amino acid from T to I at position 87.
+The natural variant of this protein is characterized by an amino acid alteration from E to Q at position 606.
+The protein's natural variant, known as found in a CNS cancer cell line, features a modification of the amino acid from K to T at position 1059.
+The protein's natural variant, known as found in prostate and ovarian cancer cell lines; abolishes ability to interact with CRK and to activate Rap1, features a modification of the amino acid from P to L at position 1718.
+The protein's natural variant, known as found in colorectal cancer cell line, features a modification of the amino acid from S to P at position 1755.
+The protein's natural variant, known as found in a prostate cancer cell line;, features a modification of the amino acid from V to M at position 1884.
+The natural variant of this protein is characterized by an amino acid alteration from K to Q at position 32.
+The natural variant of this protein is characterized by an amino acid alteration from G to S at position 107.
+The natural variant of this protein is characterized by an amino acid alteration from T to I at position 108.
+The protein's natural variant, known as in allele K4A1;, features a modification of the amino acid from A to V at position 72.
+The protein's natural variant, known as in alleles K4A1 and K4A2, features a modification of the amino acid from T to TGGFGAGGFGAGFGT at position 82.
+The protein's natural variant, known as in WSN1, features a modification of the amino acid from E to EQ at position 139.
+The protein's natural variant, known as in WSN1;, features a modification of the amino acid from E to K at position 435.
+The protein's natural variant, known as in RP71; represents a null allele;, features a modification of the amino acid from L to P at position 257.
+The protein's natural variant, known as in SRTD10;, features a modification of the amino acid from R to W at position 296.
+The protein's natural variant, known as in SRTD10;, features a modification of the amino acid from I to N at position 411.
+The protein's natural variant, known as in BBS20; unknown pathological significance, features a modification of the amino acid from L to R at position 493.
+The protein's natural variant, known as in BBS20; unknown pathological significance;, features a modification of the amino acid from H to Y at position 719.
+The protein's natural variant, known as in SRTD10;, features a modification of the amino acid from L to P at position 1536.
+The protein's natural variant, known as in SRTD10;, features a modification of the amino acid from R to C at position 1544.
+The protein's natural variant, known as in BBS20; hypomorphic mutation;, features a modification of the amino acid from H to Q at position 1567.
+The protein's natural variant, known as in RP71; hypomorphic mutation;, features a modification of the amino acid from D to E at position 1605.
+The protein's natural variant, known as in SRTD10;, features a modification of the amino acid from C to R at position 1727.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from T to N at position 195.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from A to T at position 282.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from R to K at position 361.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from R to K at position 386.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from S to L at position 395.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from H to Q at position 398.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from E to K at position 408.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from G to D at position 420.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from T to N at position 442.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from RTT to KTS at position 453.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from S to N at position 477.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from H to L at position 480.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from F to L at position 503.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from R to K at position 506.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from L to V at position 522.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from I to T at position 567.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from V to I at position 579.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from I to M at position 583.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from P to L at position 600.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from R to Q at position 605.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from I to M at position 618.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from A to E at position 708.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from Y to F at position 741.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from G to R at position 773.
+The protein's natural variant, known as in an ovarian mucinous carcinoma sample; somatic mutation;, features a modification of the amino acid from T to M at position 460.
+The protein's natural variant, known as in strain: Isolate MSB 53282/NK 7980, features a modification of the amino acid from I to V at position 61.
+The protein's natural variant, known as in strain: Isolate MSB 53282/NK 7980, features a modification of the amino acid from I to V at position 123.
+The protein's natural variant, known as in allele 2, features a modification of the amino acid from V to I at position 231.
+The protein's natural variant, known as decreased cytoprotective action;, features a modification of the amino acid from T to I at position 13.
+The protein's natural variant, known as in MAHCJ; does not affect ATPase activity. Loss of cobalamin transport activity. Decreases interaction with LMBD1. Does not affect lysosomal subcellular location;, features a modification of the amino acid from N to K at position 141.
+The protein's natural variant, known as in MAHCJ; strong decrease of ATPase activity. Strong decrease of cobalamin transport activity;, features a modification of the amino acid from Y to C at position 319.
+The protein's natural variant, known as in MAHCJ; decreases interaction with LMBD1. Does not affect lysosomal subcellular location. Decreases ATPase activity;, features a modification of the amino acid from R to Q at position 432.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to Q at position 397.
+The protein's natural variant, known as in HPS3; mild;, features a modification of the amino acid from R to W at position 397.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from T to A at position 354.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from L to M at position 785.
+The protein's natural variant, known as in FANCV; drastically reduced protein abundance;, features a modification of the amino acid from V to E at position 85.
+The protein's natural variant, known as in strain: 10536, CZ, 18323 and B6, features a modification of the amino acid from D to E at position 68.
+The protein's natural variant, known as in strain: CS, features a modification of the amino acid from N to S at position 129.
+The protein's natural variant, known as in strain: CZ and 18323, features a modification of the amino acid from S to P at position 196.
+The protein's natural variant, known as in strain: 287, Al1561, B572, CHANG and HAV, features a modification of the amino acid from M to I at position 228.
+The protein's natural variant, known as in strain: CZ and 18323, features a modification of the amino acid from I to M at position 232.
+The protein's natural variant, known as in strain: 10536 and B6, features a modification of the amino acid from I to V at position 232.
+The protein's natural variant, known as in strain: S1 / subtype 2, features a modification of the amino acid from L to P at position 38.
+The protein's natural variant, known as in strain: L2, features a modification of the amino acid from D to G at position 245.
+The protein's natural variant, known as in strain: S1 / subtype 2, features a modification of the amino acid from S to P at position 308.
+The protein's natural variant, known as in strain: S1 / subtype 2, L2, RJL1 and JL, features a modification of the amino acid from I to S at position 371.
+The protein's natural variant, known as in strain: S1 / subtype 2, features a modification of the amino acid from F to S at position 391.
+The protein's natural variant, known as in strain: RJL1, features a modification of the amino acid from W to R at position 392.
+The protein's natural variant, known as in SPG75; unknown pathological significance;, features a modification of the amino acid from R to H at position 118.
+The protein's natural variant, known as in SPG75; alters proper folding; impairs N-glycosylation; retained in the endoplasmic reticulum; increased proteasome-dependent degradation;, features a modification of the amino acid from S to R at position 133.
+The protein's natural variant, known as in SPG75; unknown pathological significance;, features a modification of the amino acid from C to G at position 430.
+The protein's natural variant, known as in WS4C; loss of DNA binding and transactivation capacity, features a modification of the amino acid from R to W at position 106.
+The protein's natural variant, known as found in a patient with Kallmann syndrome, features a modification of the amino acid from M to T at position 108.
+The protein's natural variant, known as found in a patient with Kallmann syndrome, features a modification of the amino acid from F to V at position 111.
+The protein's natural variant, known as in WS2E and PCWH; increased DNA binding capacity, features a modification of the amino acid from M to I at position 112.
+The protein's natural variant, known as in PCWH; reduced DNA binding capacity, features a modification of the amino acid from N to H at position 131.
+The protein's natural variant, known as found in a patient with Kallmann syndrome, features a modification of the amino acid from S to G at position 135.
+The protein's natural variant, known as in WS2E; without neurologic involvement;, features a modification of the amino acid from S to T at position 135.
+The protein's natural variant, known as in WS4C; loss of DNA binding and transactivation capacity, features a modification of the amino acid from L to P at position 145.
+The protein's natural variant, known as in PCWH; loss of DNA binding and transactivation capacity, features a modification of the amino acid from K to N at position 150.
+The protein's natural variant, known as found in a patient with Kallmann syndrome;, features a modification of the amino acid from R to C at position 151.
+The protein's natural variant, known as in WS4C; loss of DNA binding and transactivation capacity;, features a modification of the amino acid from A to V at position 157.
+The protein's natural variant, known as found in a patient with Kallmann syndrome, features a modification of the amino acid from R to C at position 161.
+The protein's natural variant, known as in WS2E; reduced DNA binding capacity;, features a modification of the amino acid from R to H at position 161.
+The protein's natural variant, known as in WS4C, features a modification of the amino acid from R to RLR at position 161.
+The protein's natural variant, known as in PCWH; without Hirschsprung disease; reduced DNA binding capacity;, features a modification of the amino acid from Q to P at position 174.
+The protein's natural variant, known as in PCWH; reduced DNA binding capacity, features a modification of the amino acid from P to A at position 175.
+The protein's natural variant, known as in PCWH; reduced DNA binding capacity, features a modification of the amino acid from P to L at position 175.
+The protein's natural variant, known as in PCWH; reduced DNA binding capacity, features a modification of the amino acid from P to R at position 175.
+The protein's natural variant, known as in PCWH, features a modification of the amino acid from G to R at position 321.
+The protein's natural variant, known as in IIAE11; requires 2 nucleotide substitutions; decreased protein abundance; decreased RNA lariat debranching enzyme activity, features a modification of the amino acid from L to G at position 13.
+The protein's natural variant, known as in IIAE11; decreased protein abundance; decreased RNA lariat debranching enzyme activity, features a modification of the amino acid from Y to H at position 17.
+The protein's natural variant, known as in IIAE11; decreased protein abundance; decreased RNA lariat debranching enzyme activity, features a modification of the amino acid from I to T at position 120.
+The protein's natural variant, known as in allele beta-I, features a modification of the amino acid from S to T at position 49.
+The protein's natural variant, known as in allele beta-I, features a modification of the amino acid from H to N at position 116.
+The protein's natural variant, known as in allele beta-I, features a modification of the amino acid from V to A at position 134.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from A to V at position 375.
+The natural variant of this protein is characterized by an amino acid alteration from G to D at position 167.
+The natural variant of this protein is characterized by an amino acid alteration from I to N at position 86.
+The natural variant of this protein is characterized by an amino acid alteration from R to M at position 32.
+The natural variant of this protein is characterized by an amino acid alteration from A to S at position 73.
+The natural variant of this protein is characterized by an amino acid alteration from K to R at position 77.
+The natural variant of this protein is characterized by an amino acid alteration from Q to R at position 81.
+The natural variant of this protein is characterized by an amino acid alteration from H to Q at position 87.
+The natural variant of this protein is characterized by an amino acid alteration from Q to H at position 89.
+The natural variant of this protein is characterized by an amino acid alteration from G to Q at position 91.
+The natural variant of this protein is characterized by an amino acid alteration from E to M at position 97.
+The natural variant of this protein is characterized by an amino acid alteration from R to S at position 99.
+The natural variant of this protein is characterized by an amino acid alteration from T to K at position 106.
+The natural variant of this protein is characterized by an amino acid alteration from N to Q at position 123.
+The natural variant of this protein is characterized by an amino acid alteration from K to G at position 124.
+The natural variant of this protein is characterized by an amino acid alteration from M to V at position 126.
+The protein's natural variant, known as in DFNB107;, features a modification of the amino acid from A to T at position 160.
+The protein's natural variant, known as in DFNB107; unknown pathological significance;, features a modification of the amino acid from M to L at position 163.
+The protein's natural variant, known as in DFNB107; unknown pathological significance;, features a modification of the amino acid from A to V at position 224.
+The protein's natural variant, known as found in a patient with left-sided obstructive cardiac lesions; unknown pathological significance;, features a modification of the amino acid from R to H at position 46.
+The protein's natural variant, known as found in a patient with left-sided obstructive cardiac lesions; unknown pathological significance;, features a modification of the amino acid from R to H at position 47.
+The protein's natural variant, known as found in a patient with left-sided obstructive cardiac lesions; unknown pathological significance;, features a modification of the amino acid from A to T at position 60.
+The protein's natural variant, known as found in a patient with left-sided obstructive cardiac lesions; unknown pathological significance; alters Ca(2+)-binding affinity;, features a modification of the amino acid from G to D at position 203.
+The protein's natural variant, known as found in a patient with left-sided obstructive cardiac lesions; unknown pathological significance; alters Ca(2+)-binding affinity;, features a modification of the amino acid from Y to C at position 235.
+The protein's natural variant, known as found in a patient with left-sided obstructive cardiac lesions; unknown pathological significance;, features a modification of the amino acid from V to I at position 475.
+The protein's natural variant, known as found in a patient with left-sided obstructive cardiac lesions; unknown pathological significance;, features a modification of the amino acid from A to V at position 695.
+The protein's natural variant, known as in CMT2T; unknown pathological significance, features a modification of the amino acid from D to A at position 12.
+The protein's natural variant, known as in SCA43;, features a modification of the amino acid from C to Y at position 143.
+The protein's natural variant, known as in CMT2T; results in reduction of neprilysin activity;, features a modification of the amino acid from Y to C at position 347.
+The protein's natural variant, known as in CMT2T; unknown pathological significance;, features a modification of the amino acid from A to P at position 348.
+The protein's natural variant, known as in CMT2T; late-onset form; results in reduction of neprilysin activity;, features a modification of the amino acid from A to D at position 422.
+The protein's natural variant, known as in CMT2T; decrease of protein expression;, features a modification of the amino acid from C to R at position 621.
+The natural variant of this protein is characterized by an amino acid alteration from F to L at position 7.
+The natural variant of this protein is characterized by an amino acid alteration from Q to K at position 23.
+The protein's natural variant, known as in strain: cv. Q903; susceptibility to pathogens, features a modification of the amino acid from D to H at position 285.
+The protein's natural variant, known as in CNA2;, features a modification of the amino acid from T to K at position 215.
+The protein's natural variant, known as in CNA2;, features a modification of the amino acid from N to S at position 247.
+The protein's natural variant, known as in BDPLT20; the mutation results in strongly reduced protein stability;, features a modification of the amino acid from K to E at position 218.
+The protein's natural variant, known as in BDPLT20; the mutation results in strongly reduced protein stability;, features a modification of the amino acid from K to N at position 219.
+The protein's natural variant, known as in BDPLT20; the mutation results in weakly reduced protein stability;, features a modification of the amino acid from V to D at position 220.
+The protein's natural variant, known as in BDPLT20;, features a modification of the amino acid from R to W at position 223.
+The protein's natural variant, known as in NPHP2, features a modification of the amino acid from P to R at position 482.
+The protein's natural variant, known as in NPHP2; impairs ability to target DVL1 for degradation;, features a modification of the amino acid from L to S at position 493.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to W at position 141.
+The protein's natural variant, known as in STL2, features a modification of the amino acid from G to V at position 565.
+The protein's natural variant, known as in STL2;, features a modification of the amino acid from G to V at position 625.
+The protein's natural variant, known as in STL2; overlapping phenotype with Marshall syndrome;, features a modification of the amino acid from G to R at position 676.
+The protein's natural variant, known as in FBCG1, features a modification of the amino acid from G to R at position 796.
+The protein's natural variant, known as in STL2, features a modification of the amino acid from G to R at position 1027.
+The protein's natural variant, known as in FBCG1, features a modification of the amino acid from G to R at position 1042.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from A to V at position 1326.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from Q to K at position 1328.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from Q to L at position 1328.
+The protein's natural variant, known as in STL2;, features a modification of the amino acid from G to D at position 1513.
+The protein's natural variant, known as in STL2; overlapping phenotype with Marshall syndrome;, features a modification of the amino acid from G to V at position 1516.
+The protein's natural variant, known as in strain: Isolate MVZ 152779, features a modification of the amino acid from A to V at position 238.
+The protein's natural variant, known as in strain: Isolate MVZ 152779, features a modification of the amino acid from T to I at position 241.
+The protein's natural variant, known as in strain: Isolate MVZ 152779, features a modification of the amino acid from V to I at position 306.
+The protein's natural variant, known as in IBD10; has no effect on the stability of the protein under normal conditions; enhances the cleavage and the degradation mediated by activated CASP3; results in reduced autophagy and defective clearance of intestinal pathogens; impairs interaction with TMEM59; slows TMEM59 intracellular trafficking; increases production of type IIFNs;, features a modification of the amino acid from T to A at position 300.
+The protein's natural variant, known as in IBGC7;, features a modification of the amino acid from M to V at position 35.
+The protein's natural variant, known as in IBGC7; unknown pathological significance;, features a modification of the amino acid from G to E at position 64.
+The protein's natural variant, known as in IBGC7; unknown pathological significance;, features a modification of the amino acid from L to R at position 113.
+The protein's natural variant, known as in IBGC7, features a modification of the amino acid from R to RLAFR at position 116.
+The protein's natural variant, known as in IBGC7; unknown pathological significance;, features a modification of the amino acid from W to C at position 229.
+The protein's natural variant, known as in IBGC7; unknown pathological significance;, features a modification of the amino acid from S to L at position 232.
+The protein's natural variant, known as in IBGC7; unknown pathological significance, features a modification of the amino acid from A to AA at position 236.
+The protein's natural variant, known as in IBGC7; unknown pathological significance;, features a modification of the amino acid from W to C at position 249.
+The protein's natural variant, known as in IBGC7; unknown pathological significance, features a modification of the amino acid from R to L at position 261.
+The protein's natural variant, known as in IBGC7; unknown pathological significance;, features a modification of the amino acid from A to D at position 373.
+The protein's natural variant, known as in IBGC7; unknown pathological significance;, features a modification of the amino acid from D to H at position 434.
+The protein's natural variant, known as in IBGC7;, features a modification of the amino acid from R to G at position 441.
+The protein's natural variant, known as in IBGC7; unknown pathological significance;, features a modification of the amino acid from T to N at position 476.
+The protein's natural variant, known as in IBGC7; unknown pathological significance;, features a modification of the amino acid from R to W at position 611.
+The protein's natural variant, known as in IBGC7; unknown pathological significance;, features a modification of the amino acid from L to P at position 622.
+The protein's natural variant, known as in IBGC7; unknown pathological significance;, features a modification of the amino acid from I to T at position 656.
+The protein's natural variant, known as in IBGC7; unknown pathological significance;, features a modification of the amino acid from L to Q at position 660.
+The protein's natural variant, known as in HRCDF; unknown pathological significance, features a modification of the amino acid from C to W at position 204.
+The protein's natural variant, known as in HRCDF; almost complete loss of ciliary localization;, features a modification of the amino acid from R to H at position 408.
+The natural variant of this protein is characterized by an amino acid alteration from Q to R at position 79.
+The natural variant of this protein is characterized by an amino acid alteration from E to G at position 153.
+The natural variant of this protein is characterized by an amino acid alteration from M to V at position 169.
+The protein's natural variant, known as in non-Hodgkin lymphoma; somatic mutation;, features a modification of the amino acid from A to T at position 25.
+The protein's natural variant, known as in ALPS1A; associated with autoimmune hepatitis type 2, features a modification of the amino acid from T to A at position 28.
+The protein's natural variant, known as in ALPS1A, features a modification of the amino acid from C to R at position 82.
+The protein's natural variant, known as in squamous cell carcinoma; burn-scar related; somatic mutation;, features a modification of the amino acid from N to S at position 118.
+The protein's natural variant, known as in ALPS1A;, features a modification of the amino acid from R to W at position 121.
+The protein's natural variant, known as in squamous cell carcinoma; burn-scar related; somatic mutation;, features a modification of the amino acid from C to R at position 178.
+The protein's natural variant, known as in non-Hodgkin lymphoma; somatic mutation, features a modification of the amino acid from L to F at position 180.
+The protein's natural variant, known as in non-Hodgkin lymphoma; somatic mutation;, features a modification of the amino acid from P to L at position 183.
+The protein's natural variant, known as in non-Hodgkin lymphoma; somatic mutation, features a modification of the amino acid from T to I at position 198.
+The protein's natural variant, known as in ALPS1A; no effect on interaction with FADD;, features a modification of the amino acid from Y to C at position 232.
+The protein's natural variant, known as in ALPS1A;, features a modification of the amino acid from T to K at position 241.
+The protein's natural variant, known as in ALPS1A;, features a modification of the amino acid from T to P at position 241.
+The protein's natural variant, known as in ALPS1A, features a modification of the amino acid from V to L at position 249.
+The protein's natural variant, known as in ALPS1A;, features a modification of the amino acid from R to P at position 250.
+The protein's natural variant, known as in ALPS1A; no effect on interaction with FADD, features a modification of the amino acid from R to Q at position 250.
+The protein's natural variant, known as in ALPS1A, features a modification of the amino acid from G to D at position 253.
+The protein's natural variant, known as in ALPS1A, features a modification of the amino acid from G to S at position 253.
+The protein's natural variant, known as in squamous cell carcinoma; burn-scar related; somatic mutation;, features a modification of the amino acid from N to D at position 255.
+The protein's natural variant, known as in ALPS1A; loss of interaction with FADD;, features a modification of the amino acid from A to D at position 257.
+The protein's natural variant, known as in ALPS1A, features a modification of the amino acid from I to R at position 259.
+The protein's natural variant, known as in ALPS1A, features a modification of the amino acid from D to G at position 260.
+The protein's natural variant, known as in ALPS1A; also found in non-Hodgkin lymphoma; somatic mutation; loss of interaction with FADD;, features a modification of the amino acid from D to V at position 260.
+The protein's natural variant, known as in ALPS1A; loss of interaction with FADD;, features a modification of the amino acid from D to Y at position 260.
+The protein's natural variant, known as in ALPS1A, features a modification of the amino acid from I to S at position 262.
+The protein's natural variant, known as in non-Hodgkin lymphoma; somatic mutation, features a modification of the amino acid from N to K at position 264.
+The protein's natural variant, known as in ALPS1A;, features a modification of the amino acid from T to I at position 270.
+The protein's natural variant, known as in ALPS1A; loss of interaction with FADD, features a modification of the amino acid from T to K at position 270.
+The protein's natural variant, known as in ALPS1A, features a modification of the amino acid from E to G at position 272.
+The protein's natural variant, known as in ALPS1A; also found in non-Hodgkin lymphoma; somatic mutation; loss of interaction with FADD, features a modification of the amino acid from E to K at position 272.
+The protein's natural variant, known as in non-Hodgkin lymphoma; somatic mutation, features a modification of the amino acid from L to F at position 278.
+The protein's natural variant, known as in non-Hodgkin lymphoma; somatic mutation, features a modification of the amino acid from K to N at position 299.
+The protein's natural variant, known as in ALPS1A, features a modification of the amino acid from I to S at position 310.
+The protein's natural variant, known as in strain: cv. Karhumaeki, features a modification of the amino acid from AKRVPGRTDN to NSQKSTGKNR at position 104.
+The protein's natural variant, known as no effect on transactivation activity; not statistically significant decrease of nuclear location;, features a modification of the amino acid from R to L at position 44.
+The protein's natural variant, known as in POF5; unknown pathological significance; decreased transactivation activity; decreased nuclear location; intranuclear and cytosolic aggregates;, features a modification of the amino acid from G to W at position 91.
+The protein's natural variant, known as in POF5; unknown pathological significance; loss of transactivation activity; intranuclear and cytosolic aggregates; not statistically significant decrease of nuclear location;, features a modification of the amino acid from G to R at position 111.
+The protein's natural variant, known as in POF5; unknown pathological significance; decreased transactivation activity;, features a modification of the amino acid from R to W at position 117.
+The protein's natural variant, known as in POF5; unknown pathological significance; decreased nuclear location; intranuclear and cytosolic aggregates;, features a modification of the amino acid from G to R at position 152.
+The protein's natural variant, known as in POF5;, features a modification of the amino acid from S to T at position 342.
+The protein's natural variant, known as in POF5;, features a modification of the amino acid from V to L at position 350.
+The protein's natural variant, known as in POF5;, features a modification of the amino acid from R to H at position 355.
+The protein's natural variant, known as in POF5; unknown pathological significance; decreased transactivation activity;, features a modification of the amino acid from K to T at position 371.
+The protein's natural variant, known as in POF5; likely benign variant; decreased nuclear location; intranuclear and cytosolic aggregates;, features a modification of the amino acid from D to N at position 452.
+The protein's natural variant, known as no effect on transactivation activity;, features a modification of the amino acid from P to L at position 619.
+The protein's natural variant, known as in allele: CaO19.11814, features a modification of the amino acid from A to V at position 4.
+The protein's natural variant, known as in allele: CaO19.11814, features a modification of the amino acid from G to S at position 102.
+The protein's natural variant, known as in plasmid PCHL1 and plasmid pCTT1, features a modification of the amino acid from Q to E at position 12.
+The protein's natural variant, known as in plasmid PCHL1 and plasmid pCTT1, features a modification of the amino acid from P to S at position 61.
+The protein's natural variant, known as in plasmid pCTT1, features a modification of the amino acid from D to N at position 86.
+The protein's natural variant, known as in plasmid pCHL1 and plasmid pCTT1, features a modification of the amino acid from G to D at position 90.
+The protein's natural variant, known as in plasmid pCHL1, features a modification of the amino acid from T to K at position 109.
+The protein's natural variant, known as in plasmid pCHL1 and plasmid pCTT1, features a modification of the amino acid from R to S at position 138.
+The protein's natural variant, known as in plasmid pCTT1, features a modification of the amino acid from K to N at position 189.
+The protein's natural variant, known as in plasmid pCHL1 and plasmid pCTT1, features a modification of the amino acid from Y to C at position 191.
+The protein's natural variant, known as in plasmid pCHL1, features a modification of the amino acid from V to I at position 201.
+The protein's natural variant, known as in plasmid pCHL1 and plasmid pCTT1, features a modification of the amino acid from R to S at position 210.
+The protein's natural variant, known as in plasmid pCHL1 and plasmid pCTT1, features a modification of the amino acid from I to T at position 212.
+The natural variant of this protein is characterized by an amino acid alteration from L to P at position 152.
+The natural variant of this protein is characterized by an amino acid alteration from R to Q at position 173.
+The protein's natural variant, known as in ANIB12; loss of function in endothelial cell-matrix adhesion; undetectable protein expression;, features a modification of the amino acid from L to F at position 5.
+The protein's natural variant, known as in LMPHM13; unknown pathological significance, features a modification of the amino acid from C to Y at position 206.
+The protein's natural variant, known as in ANIB12; unknown pathological significance; decreased function in endothelial cell-matrix adhesion; decreased interaction with TLN1;, features a modification of the amino acid from R to W at position 460.
+The protein's natural variant, known as in ANIB12; unknown pathological significance; loss of function in endothelial cell-matrix adhesion; decreased interaction with TLN1;, features a modification of the amino acid from E to G at position 466.
+The protein's natural variant, known as in ANIB12; unknown pathological significance; loss of function in endothelial cell-matrix adhesion; decreased interaction with TLN1;, features a modification of the amino acid from G to E at position 600.
+The protein's natural variant, known as in ANIB12; decreased function in endothelial cell-matrix adhesion; decreased interaction with TLN1;, features a modification of the amino acid from P to L at position 639.
+The protein's natural variant, known as in ANIB12; unknown pathological significance; loss of function in endothelial cell-matrix adhesion; decreased interaction with TLN1;, features a modification of the amino acid from T to I at position 653.
+The protein's natural variant, known as in ANIB12; unknown pathological significance; loss of function in endothelial cell-matrix adhesion; decreased interaction with TLN1;, features a modification of the amino acid from S to P at position 775.
+The protein's natural variant, known as in strain: Isolate AF 7052, features a modification of the amino acid from T to M at position 237.
+The protein's natural variant, known as in strain: Isolate AF 3130, features a modification of the amino acid from T to A at position 293.
+The protein's natural variant, known as in strain: Isolate AF 3130, features a modification of the amino acid from I to V at position 327.
+The protein's natural variant, known as in allele 6M1-10*02;, features a modification of the amino acid from Q to R at position 234.
+The natural variant of this protein is characterized by an amino acid alteration from M to L at position 32.
+The natural variant of this protein is characterized by an amino acid alteration from S to R at position 135.
+The protein's natural variant, known as in a patient with primary open angle glaucoma;, features a modification of the amino acid from A to V at position 318.
+The protein's natural variant, known as in a patient with normal tension glaucoma, features a modification of the amino acid from R to T at position 363.
+The protein's natural variant, known as found in a patient with LCA6;, features a modification of the amino acid from S to F at position 432.
+The protein's natural variant, known as in CORD13;, features a modification of the amino acid from A to S at position 547.
+The protein's natural variant, known as does not affect the interaction with NPHP4;, features a modification of the amino acid from Q to H at position 589.
+The protein's natural variant, known as found in patients with primary open angle glaucoma and juvenile open angle glaucoma; affects the interaction with NPHP4;, features a modification of the amino acid from R to Q at position 598.
+The protein's natural variant, known as found in a patient with LCA6;, features a modification of the amino acid from S to W at position 601.
+The natural variant of this protein is characterized by an amino acid alteration from C to S at position 603.
+The protein's natural variant, known as in LCA6, features a modification of the amino acid from H to P at position 631.
+The protein's natural variant, known as in a patient with normal tension glaucoma and a patient with primary open angle glaucoma; affects the interaction with NPHP4;, features a modification of the amino acid from A to G at position 635.
+The protein's natural variant, known as in LCA6;, features a modification of the amino acid from G to E at position 746.
+The protein's natural variant, known as does not affect the interaction with NPHP4;, features a modification of the amino acid from A to V at position 764.
+The protein's natural variant, known as in a patient with primary open angle glaucoma who also carries variant K-352 in MYOC; affects the interaction with NPHP4;, features a modification of the amino acid from T to I at position 806.
+The protein's natural variant, known as does not affect the interaction with NPHP4, features a modification of the amino acid from R to H at position 812.
+The protein's natural variant, known as in CORD13;, features a modification of the amino acid from R to L at position 827.
+The protein's natural variant, known as in a patient with primary open angle glaucoma and a patient with juvenile open angle glaucoma; affects the interaction with NPHP4;, features a modification of the amino acid from A to G at position 837.
+The protein's natural variant, known as in a patient with normal tension glaucoma and a patient with primary open angle glaucoma; affects the interaction with NPHP4;, features a modification of the amino acid from I to V at position 838.
+The natural variant of this protein is characterized by an amino acid alteration from A to T at position 841.
+The protein's natural variant, known as impairs interaction with NPHP4;, features a modification of the amino acid from D to G at position 876.
+The natural variant of this protein is characterized by an amino acid alteration from G to D at position 883.
+The protein's natural variant, known as found in a patient associated with LCA6;, features a modification of the amino acid from H to L at position 1057.
+The protein's natural variant, known as in LCA6; no effect on interaction with RPGR;, features a modification of the amino acid from D to G at position 1114.
+The protein's natural variant, known as found in a patient with LCA6, features a modification of the amino acid from E to Q at position 1130.
+The protein's natural variant, known as in LCA6, features a modification of the amino acid from V to E at position 1211.
+The protein's natural variant, known as in allele beta-II;, features a modification of the amino acid from R to H at position 51.
+The protein's natural variant, known as in allele beta-II;, features a modification of the amino acid from D to G at position 52.
+The protein's natural variant, known as in allele beta-II;, features a modification of the amino acid from R to P at position 53.
+The protein's natural variant, known as increases the binding for cholesterol; increases high density lipoprotein (HDL)- and low density lipoprotein (LDL)-mediated cholesterol uptake;, features a modification of the amino acid from T to A at position 94.
+The protein's natural variant, known as in strain: Taihe silkies, features a modification of the amino acid from H to R at position 27.
+The natural variant of this protein is characterized by an amino acid alteration from T to S at position 29.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 142.
+The natural variant of this protein is characterized by an amino acid alteration from I to M at position 404.
+The natural variant of this protein is characterized by an amino acid alteration from A to V at position 413.
+The natural variant of this protein is characterized by an amino acid alteration from T to A at position 435.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from A to S at position 562.
+The natural variant of this protein is characterized by an amino acid alteration from H to N at position 1921.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from G to S at position 2003.
+The protein's natural variant, known as in NMTC2; somatic mutation;, features a modification of the amino acid from S to L at position 41.
+The protein's natural variant, known as in PCH16; loss of enzymatic activity, features a modification of the amino acid from Y to D at position 53.
+The protein's natural variant, known as in PCH16; unknown pathological significance;, features a modification of the amino acid from F to L at position 228.
+The protein's natural variant, known as in NMTC2;, features a modification of the amino acid from Q to R at position 270.
+The protein's natural variant, known as in PCH16; unknown pathological significance, features a modification of the amino acid from A to D at position 284.
+The protein's natural variant, known as in PCH16; unknown pathological significance, features a modification of the amino acid from I to S at position 331.
+The protein's natural variant, known as in PCH16; unknown pathological significance;, features a modification of the amino acid from R to Q at position 401.
+The protein's natural variant, known as in PCH16; unknown pathological significance; contary to wild-type, does not rescue normal growth in a MINPP1 knockout cell line, features a modification of the amino acid from E to K at position 486.
+The protein's natural variant, known as in plasmid pMYSH6000, plasmid pCP301 and plasmid pINV_F6_M1382, features a modification of the amino acid from I to V at position 168.
+The protein's natural variant, known as in NPHS10; decreased amount of CAV1;, features a modification of the amino acid from F to L at position 7.
+The protein's natural variant, known as in NPHS10; decreased amount of CAV1;, features a modification of the amino acid from A to T at position 10.
+The protein's natural variant, known as in LIGOWS; no effect on protein expression; no effect on MSL complex assembly; decreased histone acetyltransferase activity, features a modification of the amino acid from Y to C at position 90.
+The protein's natural variant, known as in LIGOWS; no effect on protein expression; no effect on MSL complex assembly; decreased histone acetyltransferase activity, features a modification of the amino acid from R to Q at position 98.
+The protein's natural variant, known as in LIGOWS; no effect on protein expression; no effect on MSL complex assembly; decreased histone acetyltransferase activity, features a modification of the amino acid from R to Q at position 99.
+The protein's natural variant, known as in LIGOWS; unknown pathological significance; no effect on protein expression; no effect on MSL complex assembly; decreased histone acetyltransferase activity, features a modification of the amino acid from A to V at position 165.
+The protein's natural variant, known as in LIGOWS; no effect on protein expression; no effect on MSL complex assembly; decreased histone acetyltransferase activity, features a modification of the amino acid from K to E at position 175.
+The protein's natural variant, known as in LIGOWS; unknown pathological significance; no effect on protein expression; no effect on MSL complex assembly; decreased histone acetyltransferase activity, features a modification of the amino acid from K to N at position 181.
+The protein's natural variant, known as found in a severe neurodevelopmental disorder similar to Li-Ghorbani-Weisz-Hubshman syndrome with apparently autosomal recessive inheritance; unknown pathological significance; no effect on protein expression; no effect on localization to the nucleus; no effect on MSL complex assembly; decreased histone acetyltransferase activity, features a modification of the amino acid from R to C at position 325.
+The natural variant of this protein is characterized by an amino acid alteration from L to F at position 11.
+The protein's natural variant, known as may play a role in obesity in an age-dependent manner; apparently no effect on activity;, features a modification of the amino acid from A to T at position 67.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from R to P at position 10.
+The protein's natural variant, known as in a glioblastoma multiforme sample; somatic mutation;, features a modification of the amino acid from G to D at position 568.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation, features a modification of the amino acid from K to R at position 1052.
+The protein's natural variant, known as in a lung squamous cell carcinoma sample; somatic mutation, features a modification of the amino acid from E to D at position 1055.
+The protein's natural variant, known as in strain: Apxo, features a modification of the amino acid from T to A at position 28.
+The protein's natural variant, known as in strain: Apxo, features a modification of the amino acid from N to I at position 222.
+The protein's natural variant, known as in strain: Oregon-2 and Oregon-R, features a modification of the amino acid from K to R at position 286.
+The protein's natural variant, known as in strain: Apxo, features a modification of the amino acid from A to D at position 415.
+The protein's natural variant, known as in strain: bIf and Berkeley, features a modification of the amino acid from E to K at position 478.
+The protein's natural variant, known as in strain: bIf and Berkeley, features a modification of the amino acid from K to E at position 489.
+The protein's natural variant, known as in HOMGSMR1; results in reduced protein membrane expression;, features a modification of the amino acid from E to K at position 122.
+The protein's natural variant, known as in HOMGSMR1; results in reduced protein membrane expression; decreases cellular uptake of magnesium;, features a modification of the amino acid from S to W at position 269.
+The protein's natural variant, known as in HOMGSMR1, features a modification of the amino acid from L to F at position 330.
+The protein's natural variant, known as in HOMGSMR1; results in decreased cellular uptake of magnesium;, features a modification of the amino acid from E to K at position 357.
+The protein's natural variant, known as in HOMG6; reduced activity; electrophysiological analysis shows that magnesium-sensitive sodium currents are significantly diminished and are blocked by increased extracellular magnesium concentrations;, features a modification of the amino acid from T to I at position 568.
+The protein's natural variant, known as in CMRD, features a modification of the amino acid from G to D at position 11.
+The protein's natural variant, known as in CMRD; loss of GDP/GTP-binding;, features a modification of the amino acid from G to R at position 37.
+The protein's natural variant, known as in CMRD;, features a modification of the amino acid from D to G at position 75.
+The protein's natural variant, known as in CMRD; reduced affinity for GDP/GTP;, features a modification of the amino acid from D to N at position 137.
+The protein's natural variant, known as in CMRD; loss of GDP/GTP-binding;, features a modification of the amino acid from S to R at position 179.
+The protein's natural variant, known as in strain: NRRLY-552, features a modification of the amino acid from I to V at position 46.
+The protein's natural variant, known as in strain: NRRLY-553, features a modification of the amino acid from I to V at position 247.
+The protein's natural variant, known as in strain: NRRLY-553, features a modification of the amino acid from F to Y at position 355.
+The protein's natural variant, known as in strain: NRRLY-553, features a modification of the amino acid from K to R at position 391.
+The protein's natural variant, known as in strain: NRRLY-553, features a modification of the amino acid from A to S at position 439.
+The protein's natural variant, known as in strain: NRRLY-552, features a modification of the amino acid from N to D at position 484.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation, features a modification of the amino acid from R to K at position 563.
+The protein's natural variant, known as in strain: FGSC 541, features a modification of the amino acid from Q to K at position 44.
+The protein's natural variant, known as in strain: FGSC 541, features a modification of the amino acid from L to V at position 50.
+The protein's natural variant, known as in strain: FGSC 541, features a modification of the amino acid from L to P at position 410.
+The protein's natural variant, known as in strain: FGSC 541, features a modification of the amino acid from D to N at position 708.
+The protein's natural variant, known as in strain: FGSC 541, features a modification of the amino acid from T to M at position 726.
+The protein's natural variant, known as in CDD; affects protein secretion;, features a modification of the amino acid from V to L at position 21.
+The protein's natural variant, known as in CDD; de novo mutation; affects protein secretion;, features a modification of the amino acid from V to M at position 21.
+The protein's natural variant, known as in SOST1; leads to retention of the mutant protein in the endoplasmic reticulum; leads to a complete loss of function of the protein, features a modification of the amino acid from C to R at position 167.
+The protein's natural variant, known as in strain: cv. Irene, features a modification of the amino acid from D to V at position 633.
+The protein's natural variant, known as in strain: cv. Irene, features a modification of the amino acid from L to F at position 1322.
+The protein's natural variant, known as in strain: cv. Irene, features a modification of the amino acid from S to L at position 1658.
+The protein's natural variant, known as in strain: cv. Irene, features a modification of the amino acid from KS to NW at position 1693.
+The protein's natural variant, known as in strain: cv. Irene, features a modification of the amino acid from AC to LS at position 1778.
+The protein's natural variant, known as in strain: cv. Irene, features a modification of the amino acid from RAEPS to GRTK at position 1795.
+The protein's natural variant, known as in strain: cv. Irene, features a modification of the amino acid from EA to DG at position 1848.
+The natural variant of this protein is characterized by an amino acid alteration from F to K at position 35.
+The protein's natural variant, known as increased urate transport;, features a modification of the amino acid from T to I at position 269.
+The protein's natural variant, known as in NEDMIAL; changed localization to stress granules; decreased RNA-binding; no effect on RNA-dependent ATPase activity; by inducing the formation of stress granules probably indirectly decreases global protein synthesis;, features a modification of the amino acid from R to H at position 493.
+The protein's natural variant, known as in NEDMIAL; changed localization to stress granules; decreased RNA-dependent ATPase activity; by inducing the formation of stress granules probably indirectly decreases global protein synthesis;, features a modification of the amino acid from H to R at position 562.
+The protein's natural variant, known as in NEDMIAL; changed localization to stress granules; decreased RNA-dependent ATPase activity; by inducing the formation of stress granules probably indirectly decreases global protein synthesis;, features a modification of the amino acid from G to D at position 781.
+The protein's natural variant, known as in NEDMIAL; changed localization to stress granules; decreased RNA-dependent ATPase activity; by inducing the formation of stress granules probably indirectly decreases global protein synthesis;, features a modification of the amino acid from R to W at position 782.
+The protein's natural variant, known as in NEDMIAL; changed localization to stress granules; decreased RNA-dependent ATPase activity; by inducing the formation of stress granules probably indirectly decreases global protein synthesis;, features a modification of the amino acid from R to C at position 785.
+The protein's natural variant, known as in NEDMIAL; changed localization to stress granules; decreased RNA-dependent ATPase activity; by inducing the formation of stress granules probably indirectly decreases global protein synthesis;, features a modification of the amino acid from R to H at position 785.
+The protein's natural variant, known as in a1, features a modification of the amino acid from L to R at position 3.
+The protein's natural variant, known as in b1, features a modification of the amino acid from H to Q at position 54.
+The protein's natural variant, known as in b1 and b2, features a modification of the amino acid from EATR to GAKS at position 115.
+The protein's natural variant, known as in HEMB, features a modification of the amino acid from G to E at position 418.
+The protein's natural variant, known as in strain: Isolate MNFS 436, features a modification of the amino acid from F to L at position 109.
+The protein's natural variant, known as in strain: Isolate MNFS 436, features a modification of the amino acid from A to T at position 238.
+The protein's natural variant, known as in allele CYP4A22*2 and CYP4A22*3;, features a modification of the amino acid from R to C at position 11.
+The protein's natural variant, known as in allele CYP4A22*8, allele CYP4A22*9, allele CYP4A22*11, allele CYP4A22*12, allele CYP4A22*13, allele CYP4A22*14 and allele CYP4A22*15;, features a modification of the amino acid from R to W at position 126.
+The protein's natural variant, known as in allele CYP4A22*4, allele CYP4A22*10, allele CYP4A22*12, allele CYP4A22*13, allele CYP4A22*14 and allele CYP4A22*15;, features a modification of the amino acid from G to S at position 130.
+The protein's natural variant, known as in allele CYP4A22*2, allele CYP4A22*3, allele CYP4A22*4, allele CYP4A22*5, allele CYP4A22*6, allele CYP4A22*7, allele CYP4A22*8, allele CYP4A22*9, allele CYP4A22*10, allele CYP4A22*11, allele CYP4A22*12, allele CYP4A22*13, allele CYP4A22*14 and allele CYP4A22*15;, features a modification of the amino acid from N to Y at position 152.
+The protein's natural variant, known as in allele CYP4A22*10, allele CYP4A22*11, allele CYP4A22*12, allele CYP4A22*13, allele CYP4A22*14 and allele CYP4A22*15;, features a modification of the amino acid from V to F at position 185.
+The protein's natural variant, known as allele CYP4A22*2, allele CYP4A22*3, allele CYP4A22*4, allele CYP4A22*5, allele CYP4A22*6, allele CYP4A22*7, allele CYP4A22*8, allele CYP4A22*9, allele CYP4A22*10, allele CYP4A22*11, allele CYP4A22*12, allele CYP4A22*13, allele CYP4A22*14 and allele CYP4A22*15;, features a modification of the amino acid from C to R at position 231.
+The protein's natural variant, known as in allele CYP4A22*8, allele CYP4A22*11, allele CYP4A22*14 and allele CYP4A22*15;, features a modification of the amino acid from K to T at position 276.
+The protein's natural variant, known as in allele CYP4A22*6, allele CYP4A22*9, allele CYP4A22*10, allele CYP4A22*12, allele CYP4A22*13 and allele CYP4A22*15;, features a modification of the amino acid from L to P at position 428.
+The protein's natural variant, known as in allele CYP4A22*7, allele CYP4A22*10, allele CYP4A22*11, allele CYP4A22*13, allele CYP4A22*14 and allele CYP4A22*15;, features a modification of the amino acid from L to F at position 509.
+The protein's natural variant, known as in HYCX, features a modification of the amino acid from W to S at position 9.
+The natural variant of this protein is characterized by an amino acid alteration from H to N at position 30.
+The protein's natural variant, known as probable disease-associated variant found in L1 syndrome; loss of localization at the cell surface; retention in the endoplasmic reticulum; loss of homophilic interactions at the cell surface, features a modification of the amino acid from I to N at position 37.
+The protein's natural variant, known as no effect on localization at the cell surface;, features a modification of the amino acid from T to M at position 38.
+The protein's natural variant, known as no effect on axon guidance activity, nor on synapse formation, when assayed in a heterologous system;, features a modification of the amino acid from L to V at position 120.
+The protein's natural variant, known as in HYCX, features a modification of the amino acid from G to S at position 121.
+The protein's natural variant, known as probable disease-associated variant found in a patient with L1 syndrome; loss of homophilic interactions at the cell surface; no effect on the localization at the cell surface, features a modification of the amino acid from M to I at position 172.
+The protein's natural variant, known as in HYCX and MASA;, features a modification of the amino acid from I to S at position 179.
+The protein's natural variant, known as probable disease-associated variant found in L1 syndrome, features a modification of the amino acid from R to G at position 184.
+The protein's natural variant, known as in HYCX; severe; reduced axon arborization; partial loss of localization at the cell surface; retention in the endoplasmic reticulum; in neurons, restricted to cell bodies and proximal segments of processes; loss of axon guidance and of proper synapse formation, when assayed in a heterologous system;, features a modification of the amino acid from R to Q at position 184.
+The protein's natural variant, known as in HYCX, features a modification of the amino acid from R to W at position 184.
+The protein's natural variant, known as in HYCX, features a modification of the amino acid from Y to C at position 194.
+The protein's natural variant, known as in MASA; loss of homophilic interactions at the cell surface; no effect on localization at the cell surface, features a modification of the amino acid from D to Y at position 202.
+The protein's natural variant, known as in MASA; decrease in cell-matrix adhesion; decreased cell migration; loss of axon guidance and of proper synapse formation, when assayed in a heterologous system; no effect on the localization at the cell surface; no effect on cell proliferation, when transfected in pheochromocytoma PC12 cells; no effect on neurite outgrowth, when assayed in NGF-treated pheochromocytoma PC12 cells;, features a modification of the amino acid from H to Q at position 210.
+The protein's natural variant, known as in HYCX; decrease in cell-matrix adhesion; decreased cell migration; no effect on the localization at the cell surface; no effect on cell proliferation, when transfected in pheochromocytoma PC12 cells; no effect on neurite outgrowth, when assayed in NGF-treated pheochromocytoma PC12 cells, features a modification of the amino acid from I to T at position 219.
+The protein's natural variant, known as in HYCX and ACCPX;, features a modification of the amino acid from P to L at position 240.
+The protein's natural variant, known as probable disease-associated variant found in L1 syndrome, features a modification of the amino acid from A to D at position 254.
+The protein's natural variant, known as in HYCX; severe; loss of localization to the cell surface; retention in the endoplasmic reticulum; loss of axon guidance, when assayed in a heterologous system;, features a modification of the amino acid from C to Y at position 264.
+The protein's natural variant, known as in MASA, features a modification of the amino acid from G to D at position 268.
+The protein's natural variant, known as probable disease-associated variant found in L1 syndrome;, features a modification of the amino acid from W to R at position 276.
+The protein's natural variant, known as in MASA; decrease in neurite outgrowth, when assayed in NGF-treated pheochromocytoma PC12 cells; decrease in cell-matrix adhesion; decreased cell migration; no effect on axon guidance, on subcellular location to synaptic terminals, nor on proper synapse formation, when assayed in a heterologous system; no effect on the localization at the cell surface; no effect on cell proliferation, when transfected in pheochromocytoma PC12 cells;, features a modification of the amino acid from E to K at position 309.
+The protein's natural variant, known as probable disease-associated variant found in L1 syndrome, features a modification of the amino acid from L to P at position 313.
+The protein's natural variant, known as in HYCX, features a modification of the amino acid from W to C at position 335.
+The protein's natural variant, known as in HYCX and MASA; also in a patient with hydrocephalus and Hirschsprung disease, features a modification of the amino acid from W to R at position 335.
+The protein's natural variant, known as probable disease-associated variant found in L1 syndrome, features a modification of the amino acid from N to K at position 369.
+The protein's natural variant, known as in HYCX and MASA;, features a modification of the amino acid from G to R at position 370.
+The protein's natural variant, known as in HYCX;, features a modification of the amino acid from R to C at position 386.
+The protein's natural variant, known as in HYCX, features a modification of the amino acid from N to I at position 408.
+The protein's natural variant, known as in HYCX, features a modification of the amino acid from A to P at position 415.
+The protein's natural variant, known as in HYCX, features a modification of the amino acid from V to D at position 421.
+The protein's natural variant, known as in MASA, features a modification of the amino acid from A to D at position 426.
+The protein's natural variant, known as in HYCX; severe;, features a modification of the amino acid from G to R at position 452.
+The protein's natural variant, known as in HYCX and MASA;, features a modification of the amino acid from R to C at position 473.
+The protein's natural variant, known as probable disease-associated variant found in L1 syndrome, features a modification of the amino acid from G to R at position 480.
+The protein's natural variant, known as in MASA;, features a modification of the amino acid from L to P at position 482.
+The protein's natural variant, known as in HYCX, features a modification of the amino acid from C to Y at position 497.
+The protein's natural variant, known as found in a patient with L1 syndrome; unknown pathological significance;, features a modification of the amino acid from D to N at position 516.
+The protein's natural variant, known as found in a patient with L1 syndrome; unknown pathological significance, features a modification of the amino acid from D to Y at position 516.
+The protein's natural variant, known as found in a patient with L1 syndrome; unknown pathological significance;, features a modification of the amino acid from R to H at position 525.
+The protein's natural variant, known as in HYCX, features a modification of the amino acid from S to P at position 542.
+The protein's natural variant, known as in MASA;, features a modification of the amino acid from D to N at position 598.
+The protein's natural variant, known as in MASA, features a modification of the amino acid from R to P at position 632.
+The protein's natural variant, known as probable disease-associated variant found in L1 syndrome; loss of localization at the cell surface; retention in the endoplasmic reticulum; loss of transport into axons; loss of neurite outgrowth; loss of cell-cell adhesion, features a modification of the amino acid from W to C at position 635.
+The protein's natural variant, known as probable disease-associated variant found in L1 syndrome; requires 2 nucleotide substitutions, features a modification of the amino acid from I to P at position 645.
+The protein's natural variant, known as in HYCX;, features a modification of the amino acid from K to E at position 655.
+The protein's natural variant, known as in MASA; associated with callosal agenesis, features a modification of the amino acid from S to C at position 674.
+The protein's natural variant, known as in MASA; associated with callosal agenesis, features a modification of the amino acid from A to D at position 691.
+The protein's natural variant, known as in HYCX, features a modification of the amino acid from A to T at position 691.
+The protein's natural variant, known as in HYCX and MASA; associated with callosal agenesis; also found in a patient affected by hydrocephalus with Hirschsprung disease;, features a modification of the amino acid from G to R at position 698.
+The protein's natural variant, known as probable disease-associated variant found in L1 syndrome, features a modification of the amino acid from P to S at position 714.
+The protein's natural variant, known as in HYCX;, features a modification of the amino acid from M to T at position 741.
+The protein's natural variant, known as in HYCX, features a modification of the amino acid from R to P at position 751.
+The protein's natural variant, known as in HYCX and MASA; also found in a patient with the diagnosis of L1 syndrome; also in a patient with hydrocephalus and Hirschsprung disease;, features a modification of the amino acid from V to M at position 752.
+The protein's natural variant, known as probable disease-associated variant found in L1 syndrome, features a modification of the amino acid from W to R at position 754.
+The protein's natural variant, known as in HYCX, features a modification of the amino acid from V to F at position 768.
+The protein's natural variant, known as decreased cell-cell adhesion; no effect on subcellular localization; no effect on neurite outgrowth;, features a modification of the amino acid from V to I at position 768.
+The protein's natural variant, known as in MASA; associated with callosal agenesis;, features a modification of the amino acid from D to N at position 770.
+The protein's natural variant, known as in HYCX;, features a modification of the amino acid from Y to C at position 784.
+The protein's natural variant, known as in HYCX, features a modification of the amino acid from L to P at position 935.
+The protein's natural variant, known as in HYCX and MASA; decrease in neurite outgrowth, when assayed in NGF-treated pheochromocytoma PC12 cells; decrease in cell-matrix adhesion; decreased cell migration; no effect on the localization at the cell surface; no effect on cell proliferation, when transfected in pheochromocytoma PC12 cells, features a modification of the amino acid from P to L at position 941.
+The protein's natural variant, known as in HYCX; partial loss of localization at the cell surface; retention in the endoplasmic reticulum; in neurons, partial loss of localization to axons, but enriched on proximal dendrites, features a modification of the amino acid from W to L at position 1036.
+The protein's natural variant, known as in HYCX; partial loss of axon guidance and loss of proper synapse formation, when assayed in a heterologous system, features a modification of the amino acid from Y to C at position 1070.
+The protein's natural variant, known as probable disease-associated variant found in L1 syndrome, features a modification of the amino acid from L to Q at position 1080.
+The protein's natural variant, known as in HYCX and MASA;, features a modification of the amino acid from S to L at position 1194.
+The protein's natural variant, known as in HYCX, features a modification of the amino acid from S to L at position 1224.
+The natural variant of this protein is characterized by an amino acid alteration from G to E at position 1239.
+The protein's natural variant, known as in CCDS3; unknown pathological significance; reduces glycine amidinotransferase activity;, features a modification of the amino acid from R to Q at position 23.
+The protein's natural variant, known as in CCDS3; unknown pathological significance; reduces glycine amidinotransferase activity;, features a modification of the amino acid from I to V at position 93.
+The protein's natural variant, known as in CCDS3; unknown pathological significance; reduces glycine amidinotransferase activity;, features a modification of the amino acid from K to N at position 102.
+The protein's natural variant, known as in CCDS3; loss of glycine amidinotransferase activity;, features a modification of the amino acid from P to L at position 105.
+The protein's natural variant, known as in CCDS3; loss of glycine amidinotransferase activity;, features a modification of the amino acid from E to K at position 181.
+The protein's natural variant, known as in CCDS3; decreases glycine amidinotransferase activity, features a modification of the amino acid from A to P at position 185.
+The protein's natural variant, known as in CCDS3; loss of glycine amidinotransferase activity;, features a modification of the amino acid from R to C at position 189.
+The protein's natural variant, known as in CCDS3; loss of glycine amidinotransferase activity;, features a modification of the amino acid from Y to S at position 203.
+The protein's natural variant, known as in CCDS3; loss of glycine amidinotransferase activity;, features a modification of the amino acid from A to T at position 208.
+The protein's natural variant, known as decreases glycine amidinotransferase activity;, features a modification of the amino acid from S to C at position 231.
+The protein's natural variant, known as decreases glycine amidinotransferase activity;, features a modification of the amino acid from D to G at position 234.
+The protein's natural variant, known as in CCDS3; decreases glycine amidinotransferase activity;, features a modification of the amino acid from R to H at position 282.
+The protein's natural variant, known as in FRTS1; results in GATM protein aggregation; GATM deposits affect mitochondrial morphology leading to abnormal and elongated mitochondria;, features a modification of the amino acid from P to S at position 320.
+The protein's natural variant, known as in CCDS3; decreases glycine amidinotransferase activity;, features a modification of the amino acid from L to V at position 329.
+The protein's natural variant, known as in FRTS1; results in GATM protein aggregation; GATM deposits affect mitochondrial morphology leading to abnormal and elongated mitochondria;, features a modification of the amino acid from T to A at position 336.
+The protein's natural variant, known as in FRTS1; results in GATM protein aggregation; GATM deposits affect mitochondrial morphology and are associated with increased ROS production, activation of the NLRP3 inflammasome and enhanced expression of the profibrotic cytokine IL-18, features a modification of the amino acid from T to I at position 336.
+The protein's natural variant, known as in FRTS1; results in GATM protein aggregation; GATM deposits affect mitochondrial morphology leading to abnormal and elongated mitochondria;, features a modification of the amino acid from P to L at position 341.
+The protein's natural variant, known as in CCDS3; decreases glycine amidinotransferase activity;, features a modification of the amino acid from P to L at position 346.
+The protein's natural variant, known as in CCDS3; loss of glycine amidinotransferase activity;, features a modification of the amino acid from R to Q at position 413.
+The protein's natural variant, known as in CCDS3; loss of glycine amidinotransferase activity;, features a modification of the amino acid from R to W at position 413.
+The protein's natural variant, known as in CCDS3; unknown pathological significance; reduces glycine amidinotransferase activity;, features a modification of the amino acid from R to Q at position 415.
+The protein's natural variant, known as in gentamicin resistant strain: GS50-15, features a modification of the amino acid from RRPEPYKGKGVRYADEVVRTKEAKKK to AL at position 177.
+The protein's natural variant, known as in gentamicin resistant strain: GS20-8, features a modification of the amino acid from KGKGVRYADEVVRTKEAKKK to TL at position 177.
+The protein's natural variant, known as in TDH1;, features a modification of the amino acid from G to R at position 93.
+The natural variant of this protein is characterized by an amino acid alteration from A to P at position 102.
+The protein's natural variant, known as in TDH1;, features a modification of the amino acid from Q to E at position 267.
+The protein's natural variant, known as in TDH1;, features a modification of the amino acid from T to P at position 354.
+The protein's natural variant, known as in TDH1;, features a modification of the amino acid from G to R at position 395.
+The protein's natural variant, known as requires 2 nucleotide substitutions, features a modification of the amino acid from T to Q at position 536.
+The protein's natural variant, known as in TDH1;, features a modification of the amino acid from G to E at position 543.
+The protein's natural variant, known as requires 2 nucleotide substitutions, features a modification of the amino acid from S to Q at position 556.
+The natural variant of this protein is characterized by an amino acid alteration from Q to P at position 384.
+The protein's natural variant, known as in strain: 65, features a modification of the amino acid from S to N at position 59.
+The protein's natural variant, known as in strain: KSA8, features a modification of the amino acid from A to V at position 26.
+The protein's natural variant, known as in strain: KSA8, features a modification of the amino acid from S to L at position 335.
+The protein's natural variant, known as in strain: KSA8, features a modification of the amino acid from E to Q at position 692.
+The protein's natural variant, known as in strain: P1, features a modification of the amino acid from NN to KH at position 11.
+The protein's natural variant, known as in strain: P1, features a modification of the amino acid from N to D at position 18.
+The protein's natural variant, known as in strain: P1, features a modification of the amino acid from A to V at position 46.
+The protein's natural variant, known as in strain: P1, features a modification of the amino acid from E to G at position 48.
+The protein's natural variant, known as in strain: P1, features a modification of the amino acid from EE to GQ at position 73.
+The protein's natural variant, known as in strain: P1, features a modification of the amino acid from G to V at position 76.
+The protein's natural variant, known as in strain: P1, features a modification of the amino acid from R to H at position 79.
+The protein's natural variant, known as in strain: P1, features a modification of the amino acid from Y to Q at position 84.
+The protein's natural variant, known as in strain: P1, features a modification of the amino acid from D to G at position 108.
+The protein's natural variant, known as in strain: P1, features a modification of the amino acid from SK to NN at position 120.
+The protein's natural variant, known as in strain: P1, features a modification of the amino acid from M to L at position 169.
+The protein's natural variant, known as in strain: P1, features a modification of the amino acid from K to N at position 177.
+The protein's natural variant, known as in strain: P1, features a modification of the amino acid from S to N at position 181.
+The protein's natural variant, known as in strain: P1, features a modification of the amino acid from E to K at position 206.
+The protein's natural variant, known as in strain: P1, features a modification of the amino acid from A to T at position 233.
+The protein's natural variant, known as in strain: P1, features a modification of the amino acid from S to G at position 258.
+The protein's natural variant, known as in strain: P1, features a modification of the amino acid from A to T at position 304.
+The natural variant of this protein is characterized by an amino acid alteration from L to Q at position 170.
+The protein's natural variant, known as in allele tw[1], features a modification of the amino acid from T to GS at position 59.
+The protein's natural variant, known as in AML, features a modification of the amino acid from S to A at position 854.
+The protein's natural variant, known as in ACML; somatic mutation in ACML and other myeloid malignancies;, features a modification of the amino acid from E to K at position 858.
+The protein's natural variant, known as in SGMFS;, features a modification of the amino acid from D to A at position 868.
+The protein's natural variant, known as in myeloid malignancies, features a modification of the amino acid from D to G at position 868.
+The protein's natural variant, known as in SGMFS, ACML, JMML and MDS; also found in other myeloid malignancies; somatic mutation;, features a modification of the amino acid from D to N at position 868.
+The protein's natural variant, known as in myeloid malignancies, features a modification of the amino acid from D to Y at position 868.
+The protein's natural variant, known as in MDS and myeloid malignancies, features a modification of the amino acid from S to N at position 869.
+The protein's natural variant, known as in myeloid malignancies, features a modification of the amino acid from S to R at position 869.
+The protein's natural variant, known as in SGMFS;, features a modification of the amino acid from G to D at position 870.
+The protein's natural variant, known as in AML, features a modification of the amino acid from G to R at position 870.
+The protein's natural variant, known as in SGMFS, ACML, MDS and AML; somatic mutation in ACML and other myeloid malignancies; results in higher protein levels; cells expressing this mutant exhibit higher proliferation rates than those expressing the wild-type protein;, features a modification of the amino acid from G to S at position 870.
+The protein's natural variant, known as in myeloid malignancies, features a modification of the amino acid from G to V at position 870.
+The protein's natural variant, known as in AML;, features a modification of the amino acid from I to S at position 871.
+The protein's natural variant, known as in SGMFS and ACML; somatic mutation in ACML and other myeloid malignancies;, features a modification of the amino acid from I to T at position 871.
+The protein's natural variant, known as in MDS and myeloid malignancies, features a modification of the amino acid from T to R at position 873.
+The protein's natural variant, known as in myeloid malignancies, features a modification of the amino acid from D to N at position 874.
+The protein's natural variant, known as in myeloid malignancies, features a modification of the amino acid from D to A at position 880.
+The protein's natural variant, known as in myeloid malignancies, features a modification of the amino acid from D to E at position 880.
+The protein's natural variant, known as in myeloid malignancies, features a modification of the amino acid from D to N at position 880.
+The protein's natural variant, known as in myeloid malignancies;, features a modification of the amino acid from D to N at position 908.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to W at position 1162.
+The natural variant of this protein is characterized by an amino acid alteration from I to N at position 101.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from P to A at position 326.
+The protein's natural variant, known as - phenotype, features a modification of the amino acid from MQS to IQKCYA at position 3.
+The protein's natural variant, known as ++++ phenotype, features a modification of the amino acid from M to MNTKMLCN at position 1.
+The protein's natural variant, known as in OFD1;, features a modification of the amino acid from S to F at position 74.
+The protein's natural variant, known as in OFD1;, features a modification of the amino acid from A to T at position 79.
+The protein's natural variant, known as in OFD1;, features a modification of the amino acid from G to S at position 138.
+The protein's natural variant, known as in OFD1;, features a modification of the amino acid from M to R at position 141.
+The protein's natural variant, known as in JBTS10; unknown pathological significance, features a modification of the amino acid from V to D at position 307.
+The protein's natural variant, known as in OFD1, features a modification of the amino acid from KDD to FSY at position 360.
+The protein's natural variant, known as in OFD1;, features a modification of the amino acid from S to R at position 435.
+The protein's natural variant, known as in IMD64; no effect on protein expression; decreased T cell activation;, features a modification of the amino acid from T to I at position 214.
+The protein's natural variant, known as in strain: 1479, features a modification of the amino acid from R to H at position 51.
+The protein's natural variant, known as in strain: 1479, features a modification of the amino acid from M to T at position 110.
+The protein's natural variant, known as in strain: 1479, features a modification of the amino acid from I to V at position 177.
+The protein's natural variant, known as in strain: 1479, features a modification of the amino acid from G to V at position 208.
+The protein's natural variant, known as may be associated with low RHD expression, resulting in a weak D phenotype, features a modification of the amino acid from S to C at position 3.
+The protein's natural variant, known as may be associated with low RHD expression, resulting in a weak D phenotype, features a modification of the amino acid from R to Q at position 10.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from S to C at position 103.
+The protein's natural variant, known as in Tar antigen;, features a modification of the amino acid from L to P at position 110.
+The protein's natural variant, known as may be associated with low RHD expression, resulting in a weak D phenotype, features a modification of the amino acid from A to D at position 149.
+The protein's natural variant, known as may be associated with low RHD expression, resulting in a weak D phenotype, features a modification of the amino acid from S to T at position 182.
+The protein's natural variant, known as may be associated with low RHD expression, resulting in a weak D phenotype, features a modification of the amino acid from K to N at position 198.
+The protein's natural variant, known as may be associated with low RHD expression, resulting in a weak D phenotype;, features a modification of the amino acid from T to R at position 201.
+The protein's natural variant, known as may be associated with low RHD expression, resulting in a weak D phenotype, features a modification of the amino acid from W to R at position 220.
+The protein's natural variant, known as found in RhDVa(FK) and RhDVa(TT); may be associated with low RHD expression, resulting in a weak D phenotype;, features a modification of the amino acid from F to V at position 223.
+The protein's natural variant, known as found in RhDVa(FK), RhDVa(TO), RhDVa(TT) and RhDYo;, features a modification of the amino acid from E to Q at position 233.
+The protein's natural variant, known as found in RhDVa(TO) and RhDVa(TT);, features a modification of the amino acid from V to M at position 238.
+The protein's natural variant, known as found in RhDVa(TT);, features a modification of the amino acid from V to L at position 245.
+The protein's natural variant, known as may be associated with low RHD expression, resulting in a weak D phenotype, features a modification of the amino acid from V to G at position 270.
+The protein's natural variant, known as may be associated with low RHD expression, resulting in a weak D phenotype, features a modification of the amino acid from A to P at position 276.
+The protein's natural variant, known as may be associated with low RHD expression, resulting in a weak D phenotype, features a modification of the amino acid from G to E at position 277.
+The protein's natural variant, known as may be associated with low RHD expression, resulting in a weak D phenotype, features a modification of the amino acid from G to D at position 282.
+The protein's natural variant, known as may be associated with moderate decrease in RHD expression, resulting in DHMi phenotype, features a modification of the amino acid from T to I at position 283.
+The protein's natural variant, known as may be associated with low RHD expression, resulting in a weak D phenotype, features a modification of the amino acid from A to P at position 294.
+The protein's natural variant, known as may be associated with low RHD expression, resulting in a weak D phenotype, features a modification of the amino acid from M to I at position 295.
+The protein's natural variant, known as may be associated with low RHD expression, resulting in a weak D phenotype, features a modification of the amino acid from G to R at position 307.
+The protein's natural variant, known as may be associated with low RHD expression, resulting in a weak D phenotype, features a modification of the amino acid from G to E at position 339.
+The protein's natural variant, known as may be associated with low RHD expression, resulting in a weak D phenotype, features a modification of the amino acid from G to A at position 385.
+The protein's natural variant, known as may be associated with low RHD expression, resulting in a weak D phenotype, features a modification of the amino acid from W to R at position 393.
+The protein's natural variant, known as in DBA10;, features a modification of the amino acid from D to N at position 33.
+The protein's natural variant, known as in DBA10, features a modification of the amino acid from M to T at position 115.
+The protein's natural variant, known as in CMS20; decreased choline transmembrane transporter activity; no effect on localization at plasma membrane;, features a modification of the amino acid from D to G at position 48.
+The protein's natural variant, known as in CMS20; loss of choline transmembrane transporter activity; no effect on localization at plasma membrane;, features a modification of the amino acid from G to E at position 65.
+The protein's natural variant, known as 40% reduction in choline uptake rate; found in 0.06 of Ashkenazi Jews;, features a modification of the amino acid from I to V at position 89.
+The protein's natural variant, known as in CMS20; decreased choline transmembrane transporter activity; no effect on localization at plasma membrane;, features a modification of the amino acid from P to S at position 105.
+The protein's natural variant, known as in CMS20; no effect on localization at plasma membrane, features a modification of the amino acid from Y to H at position 111.
+The protein's natural variant, known as in CMS20; unknown pathological significance;, features a modification of the amino acid from Y to C at position 175.
+The protein's natural variant, known as in CMS20; unknown pathological significance;, features a modification of the amino acid from I to T at position 291.
+The protein's natural variant, known as in CMS20; unknown pathological significance, features a modification of the amino acid from V to L at position 344.
+The protein's natural variant, known as in CMS20; decreased choline transmembrane transporter activity; no effect on localization at plasma membrane;, features a modification of the amino acid from R to Q at position 361.
+The protein's natural variant, known as in CMS20; unknown pathological significance, features a modification of the amino acid from F to V at position 418.
+The protein's natural variant, known as in CMS20; decreased choline transmembrane transporter activity; no effect on localization at plasma membrane, features a modification of the amino acid from R to G at position 446.
+The protein's natural variant, known as decreased plasma membrane expression; loss of homodimerization and dipeptidyl peptidase activity; mislocalized with the calnexin in the endoplasmic reticulum; causes induction of the unfolded protein response (UPR);, features a modification of the amino acid from S to L at position 363.
+The protein's natural variant, known as found in a patient with schizophrenia; unknown pathological significance;, features a modification of the amino acid from D to N at position 200.
+The protein's natural variant, known as rare variant found in patients with X-linked intellectual disability; unknown pathological significance;, features a modification of the amino acid from G to V at position 21.
+The protein's natural variant, known as rare variant found in patients with X-linked intellectual disability; unknown pathological significance;, features a modification of the amino acid from R to Q at position 324.
+The protein's natural variant, known as rare variant found in patients with X-linked intellectual disability; unknown pathological significance;, features a modification of the amino acid from I to V at position 337.
+The protein's natural variant, known as decreased IFNB induction upon Sendai virus infection, features a modification of the amino acid from N to K at position 146.
+The protein's natural variant, known as no effect on IFNB induction upon Sendai virus infection, features a modification of the amino acid from R to Q at position 227.
+The protein's natural variant, known as in IIAE7; loss of viral infection-induced phosphorylation at S-386; loss of viral infection-induced homodimerization; loss of viral infection-induced transcription factor activity; unable to activate interferon transcription in response to viral infection; decreased IFNB induction upon Sendai virus infection;, features a modification of the amino acid from R to Q at position 285.
+The protein's natural variant, known as no effect on IFNB induction upon Sendai virus infection, features a modification of the amino acid from L to V at position 401.
+The protein's natural variant, known as in DEE55; reduced GPI-anchor biosynthetic process; may affect expression of isoform A;, features a modification of the amino acid from M to T at position 25.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from K to T at position 278.
+The protein's natural variant, known as in HAE1; phenotype consistent with hereditary angioedema type 1, features a modification of the amino acid from L to R at position 11.
+The protein's natural variant, known as in HAE1;, features a modification of the amino acid from T to A at position 118.
+The protein's natural variant, known as in HAE1; phenotype consistent with hereditary angioedema type 1, features a modification of the amino acid from C to Y at position 130.
+The protein's natural variant, known as in HAE1;, features a modification of the amino acid from Y to C at position 154.
+The protein's natural variant, known as in HAE1;, features a modification of the amino acid from S to F at position 170.
+The protein's natural variant, known as in HAE1;, features a modification of the amino acid from G to R at position 184.
+The protein's natural variant, known as in HAE1;, features a modification of the amino acid from L to P at position 230.
+The protein's natural variant, known as in HAE1;, features a modification of the amino acid from I to K at position 232.
+The protein's natural variant, known as in HAE1, features a modification of the amino acid from W to R at position 265.
+The protein's natural variant, known as in HAE1; phenotype consistent with hereditary angioedema type 2, features a modification of the amino acid from I to V at position 274.
+The protein's natural variant, known as in HAE1;, features a modification of the amino acid from W to R at position 299.
+The protein's natural variant, known as in HAE1; phenotype consistent with hereditary angioedema type 1, features a modification of the amino acid from G to R at position 345.
+The protein's natural variant, known as in HAE1; phenotype consistent with hereditary angioedema type 1, features a modification of the amino acid from T to P at position 394.
+The protein's natural variant, known as in HAE1; phenotype consistent with hereditary angioedema type 1, features a modification of the amino acid from D to V at position 408.
+The protein's natural variant, known as in HAE1; phenotype consistent with hereditary angioedema type 2, features a modification of the amino acid from G to R at position 429.
+The protein's natural variant, known as in HAE1;, features a modification of the amino acid from L to Q at position 430.
+The protein's natural variant, known as in HAE1;, features a modification of the amino acid from M to T at position 441.
+The protein's natural variant, known as in HAE1;, features a modification of the amino acid from L to P at position 447.
+The protein's natural variant, known as in HAE1; phenotype consistent with hereditary angioedema type 2;, features a modification of the amino acid from V to E at position 454.
+The protein's natural variant, known as in HAE1; phenotype consistent with hereditary angioedema type 2, features a modification of the amino acid from A to E at position 456.
+The protein's natural variant, known as in HAE1; phenotype consistent with hereditary angioedema type 2;, features a modification of the amino acid from A to T at position 458.
+The protein's natural variant, known as in HAE1; phenotype consistent with hereditary angioedema type 2, features a modification of the amino acid from A to V at position 458.
+The protein's natural variant, known as in HAE1; phenotype consistent with hereditary angioedema type 2;, features a modification of the amino acid from A to V at position 465.
+The protein's natural variant, known as in HAE1; phenotype consistent with hereditary angioedema type 2;, features a modification of the amino acid from R to C at position 466.
+The protein's natural variant, known as in HAE1; phenotype consistent with hereditary angioedema type 2;, features a modification of the amino acid from R to H at position 466.
+The protein's natural variant, known as in HAE1; phenotype consistent with hereditary angioedema type 2;, features a modification of the amino acid from R to L at position 466.
+The protein's natural variant, known as in HAE1; phenotype consistent with hereditary angioedema type 2;, features a modification of the amino acid from R to S at position 466.
+The protein's natural variant, known as in HAE1; phenotype consistent with hereditary angioedema type 2, features a modification of the amino acid from T to P at position 467.
+The protein's natural variant, known as in HAE1; phenotype consistent with hereditary angioedema type 1, features a modification of the amino acid from V to E at position 473.
+The protein's natural variant, known as in HAE1;, features a modification of the amino acid from V to G at position 473.
+The protein's natural variant, known as in HAE1; phenotype consistent with hereditary angioedema type 2, features a modification of the amino acid from V to M at position 473.
+The natural variant of this protein is characterized by an amino acid alteration from Q to E at position 474.
+The protein's natural variant, known as in HAE1; phenotype consistent with hereditary angioedema type 2, features a modification of the amino acid from F to S at position 477.
+The protein's natural variant, known as in HAE1; phenotype consistent with hereditary angioedema type 2, features a modification of the amino acid from L to P at position 481.
+The protein's natural variant, known as in HAE1; phenotype consistent with hereditary angioedema type 2, features a modification of the amino acid from L to R at position 481.
+The protein's natural variant, known as in HAE1; phenotype consistent with hereditary angioedema type 2, features a modification of the amino acid from P to R at position 489.
+The protein's natural variant, known as in HAE1; phenotype consistent with hereditary angioedema type 1, features a modification of the amino acid from G to E at position 493.
+The protein's natural variant, known as in HAE1; phenotype consistent with hereditary angioedema type 2, features a modification of the amino acid from G to R at position 493.
+The protein's natural variant, known as in HAE1;, features a modification of the amino acid from D to G at position 497.
+The protein's natural variant, known as in HAE1; phenotype consistent with hereditary angioedema type 1, features a modification of the amino acid from P to R at position 498.
+The protein's natural variant, known as in HAE1; phenotype consistent with hereditary angioedema type 2, features a modification of the amino acid from P to S at position 498.
+The protein's natural variant, known as in HAE6, features a modification of the amino acid from M to K at position 379.
+The protein's natural variant, known as in HAE6; unknown pathological significance, features a modification of the amino acid from P to A at position 574.
+The protein's natural variant, known as in strain: B4, features a modification of the amino acid from R to G at position 190.
+The protein's natural variant, known as in strain: B4, features a modification of the amino acid from G to S at position 237.
+The protein's natural variant, known as in strain: B4, features a modification of the amino acid from T to A at position 280.
+The protein's natural variant, known as in strain: B2 and B3, features a modification of the amino acid from D to N at position 281.
+The protein's natural variant, known as in strain: D1, features a modification of the amino acid from G to D at position 285.
+The protein's natural variant, known as in strain: B3 and B4, features a modification of the amino acid from S to N at position 286.
+The protein's natural variant, known as in strain: B2, B3 and B4, features a modification of the amino acid from E to K at position 296.
+The protein's natural variant, known as in pt, features a modification of the amino acid from H to Q at position 37.
+The protein's natural variant, known as in strain: S1, features a modification of the amino acid from D to A at position 111.
+The protein's natural variant, known as linked to long incubation time, features a modification of the amino acid from L to F at position 108.
+The protein's natural variant, known as linked to long incubation time; requires 2 nucleotide substitutions, features a modification of the amino acid from T to V at position 189.
+The protein's natural variant, known as in RB, features a modification of the amino acid from E to Q at position 72.
+The protein's natural variant, known as in RB; unilateral form;, features a modification of the amino acid from E to D at position 137.
+The natural variant of this protein is characterized by an amino acid alteration from Y to H at position 173.
+The protein's natural variant, known as in RB, features a modification of the amino acid from I to T at position 185.
+The protein's natural variant, known as in RB; unknown pathological significance;, features a modification of the amino acid from G to E at position 310.
+The protein's natural variant, known as in RB, features a modification of the amino acid from R to G at position 358.
+The protein's natural variant, known as in RB;, features a modification of the amino acid from R to Q at position 358.
+The protein's natural variant, known as in RB, features a modification of the amino acid from K to Q at position 447.
+The protein's natural variant, known as in RB, features a modification of the amino acid from M to R at position 457.
+The protein's natural variant, known as in RB, features a modification of the amino acid from R to G at position 500.
+The protein's natural variant, known as in RB;, features a modification of the amino acid from K to R at position 530.
+The protein's natural variant, known as in RB;, features a modification of the amino acid from H to Y at position 549.
+The protein's natural variant, known as in RB;, features a modification of the amino acid from S to L at position 567.
+The protein's natural variant, known as in RB, features a modification of the amino acid from K to E at position 616.
+The protein's natural variant, known as in RB, features a modification of the amino acid from A to P at position 635.
+The protein's natural variant, known as in RB, features a modification of the amino acid from V to E at position 654.
+The protein's natural variant, known as in RB, features a modification of the amino acid from L to P at position 657.
+The protein's natural variant, known as in RB; mild form;, features a modification of the amino acid from R to W at position 661.
+The protein's natural variant, known as in RB, features a modification of the amino acid from L to P at position 662.
+The protein's natural variant, known as in RB, features a modification of the amino acid from H to P at position 673.
+The protein's natural variant, known as in RB, features a modification of the amino acid from Q to P at position 685.
+The protein's natural variant, known as in RB, features a modification of the amino acid from C to Y at position 706.
+The protein's natural variant, known as in RB;, features a modification of the amino acid from C to R at position 712.
+The protein's natural variant, known as in RB, features a modification of the amino acid from N to K at position 803.
+The protein's natural variant, known as in SMDP4;, features a modification of the amino acid from G to R at position 196.
+The protein's natural variant, known as found in patients with Bardet-Biedl syndrome carrying mutations in other BBS genes; uncertain pathological role;, features a modification of the amino acid from E to K at position 61.
+The protein's natural variant, known as in BBS4, features a modification of the amino acid from N to H at position 165.
+The protein's natural variant, known as in BBS4;, features a modification of the amino acid from R to P at position 295.
+The protein's natural variant, known as in BBS4, features a modification of the amino acid from L to P at position 327.
+The protein's natural variant, known as in BBS4, features a modification of the amino acid from L to R at position 351.
+The protein's natural variant, known as in BBS4;, features a modification of the amino acid from A to E at position 364.
+The protein's natural variant, known as in BBS4;, features a modification of the amino acid from D to G at position 368.
+The protein's natural variant, known as in a patient with Bardet-Biedl syndrome compound heterozygote for mutations in BBS1; uncertain pathological role;, features a modification of the amino acid from E to D at position 412.
+The protein's natural variant, known as in BBS4, features a modification of the amino acid from S to I at position 457.
+The protein's natural variant, known as in BBS4;, features a modification of the amino acid from M to V at position 472.
+The protein's natural variant, known as in a patient with Bardet-Biedl syndrome homozygous for a mutation in BBS12; uncertain pathological role;, features a modification of the amino acid from T to K at position 488.
+The protein's natural variant, known as in BBS4;, features a modification of the amino acid from P to L at position 503.
+The protein's natural variant, known as in FA2D; Shanghai, features a modification of the amino acid from E to G at position 72.
+The protein's natural variant, known as confirmed at protein level;, features a modification of the amino acid from T to M at position 165.
+The protein's natural variant, known as in FA2D; prothrombin type 3; variant confirmed at protein level;, features a modification of the amino acid from E to K at position 200.
+The protein's natural variant, known as in FA2D; Barcelona/Madrid;, features a modification of the amino acid from R to C at position 314.
+The protein's natural variant, known as in FA2D; Padua-1;, features a modification of the amino acid from R to H at position 314.
+The protein's natural variant, known as in FA2D; Himi-1;, features a modification of the amino acid from M to T at position 380.
+The protein's natural variant, known as confirmed at protein level;, features a modification of the amino acid from P to T at position 386.
+The protein's natural variant, known as in FA2D; Quick-1;, features a modification of the amino acid from R to C at position 425.
+The protein's natural variant, known as in FA2D; Himi-2;, features a modification of the amino acid from R to H at position 431.
+The protein's natural variant, known as in FA2D; Tokushima;, features a modification of the amino acid from R to W at position 461.
+The protein's natural variant, known as in FA2D; Salakta/Frankfurt, features a modification of the amino acid from E to A at position 509.
+The natural variant of this protein is characterized by an amino acid alteration from E to Q at position 532.
+The protein's natural variant, known as in FA2D; Quick-2;, features a modification of the amino acid from G to V at position 601.
+The protein's natural variant, known as in D11 marker, features a modification of the amino acid from T to M at position 104.
+The protein's natural variant, known as in E15 marker, features a modification of the amino acid from T to A at position 185.
+The protein's natural variant, known as in USH1B;, features a modification of the amino acid from G to R at position 25.
+The protein's natural variant, known as in USH1B;, features a modification of the amino acid from A to E at position 26.
+The protein's natural variant, known as in USH1B;, features a modification of the amino acid from V to M at position 67.
+The protein's natural variant, known as in USH1B, features a modification of the amino acid from R to P at position 90.
+The protein's natural variant, known as in USH1B; unknown pathological significance;, features a modification of the amino acid from H to D at position 133.
+The protein's natural variant, known as in USH1B;, features a modification of the amino acid from I to N at position 134.
+The protein's natural variant, known as found in patients with retinitis pigmentosa; unknown pathological significance;, features a modification of the amino acid from G to R at position 158.
+The protein's natural variant, known as in USH1B;, features a modification of the amino acid from G to R at position 163.
+The protein's natural variant, known as in USH1B, features a modification of the amino acid from K to R at position 164.
+The protein's natural variant, known as in USH1B;, features a modification of the amino acid from T to M at position 165.
+The protein's natural variant, known as found in a patient with Leber congenital amaurosis; unknown pathological significance;, features a modification of the amino acid from T to I at position 193.
+The protein's natural variant, known as in USH1B; is predicted to alter the normal splicing of exon 6, features a modification of the amino acid from A to T at position 198.
+The protein's natural variant, known as in USH1B, features a modification of the amino acid from T to A at position 204.
+The protein's natural variant, known as in USH1B;, features a modification of the amino acid from R to C at position 212.
+The protein's natural variant, known as in USH1B;, features a modification of the amino acid from R to H at position 212.
+The protein's natural variant, known as in USH1B;, features a modification of the amino acid from G to R at position 214.
+The protein's natural variant, known as in USH1B;, features a modification of the amino acid from R to C at position 241.
+The protein's natural variant, known as in USH1B, features a modification of the amino acid from R to S at position 241.
+The protein's natural variant, known as in DFNB2;, features a modification of the amino acid from R to P at position 244.
+The protein's natural variant, known as in USH1B;, features a modification of the amino acid from A to D at position 397.
+The protein's natural variant, known as in USH1B;, features a modification of the amino acid from E to Q at position 450.
+The protein's natural variant, known as in USH1B;, features a modification of the amino acid from A to V at position 457.
+The protein's natural variant, known as in DFNA11;, features a modification of the amino acid from N to I at position 458.
+The protein's natural variant, known as in USH1B, features a modification of the amino acid from H to HQ at position 468.
+The protein's natural variant, known as in USH1B, features a modification of the amino acid from P to L at position 503.
+The protein's natural variant, known as in USH1B;, features a modification of the amino acid from G to D at position 519.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 597.
+The protein's natural variant, known as in DFNB2;, features a modification of the amino acid from M to I at position 599.
+The protein's natural variant, known as in USH1B; atypical;, features a modification of the amino acid from L to P at position 651.
+The protein's natural variant, known as in DFNB2, features a modification of the amino acid from C to R at position 652.
+The protein's natural variant, known as in DFNA11, features a modification of the amino acid from G to R at position 722.
+The protein's natural variant, known as in USH1B;, features a modification of the amino acid from R to W at position 756.
+The protein's natural variant, known as in USH1B;, features a modification of the amino acid from A to T at position 826.
+The protein's natural variant, known as in DFNA11; disturb calmodulin/MYO7A binding, features a modification of the amino acid from R to C at position 853.
+The protein's natural variant, known as in USH1B;, features a modification of the amino acid from M to R at position 946.
+The protein's natural variant, known as in USH1B;, features a modification of the amino acid from G to S at position 955.
+The protein's natural variant, known as in USH1B;, features a modification of the amino acid from E to D at position 968.
+The protein's natural variant, known as in USH1B;, features a modification of the amino acid from L to P at position 1087.
+The protein's natural variant, known as in USH1B;, features a modification of the amino acid from E to K at position 1170.
+The protein's natural variant, known as in USH1B;, features a modification of the amino acid from R to Q at position 1240.
+The protein's natural variant, known as in USH1B, features a modification of the amino acid from E to K at position 1248.
+The protein's natural variant, known as in USH1B;, features a modification of the amino acid from A to P at position 1288.
+The protein's natural variant, known as in USH1B;, features a modification of the amino acid from E to K at position 1327.
+The protein's natural variant, known as in USH1B;, features a modification of the amino acid from R to S at position 1343.
+The protein's natural variant, known as in USH1B; atypical;, features a modification of the amino acid from R to Q at position 1602.
+The protein's natural variant, known as in USH1B, features a modification of the amino acid from A to S at position 1628.
+The natural variant of this protein is characterized by an amino acid alteration from S to G at position 1666.
+The protein's natural variant, known as in USH1B;, features a modification of the amino acid from R to W at position 1743.
+The protein's natural variant, known as in USH1B;, features a modification of the amino acid from E to K at position 1812.
+The protein's natural variant, known as in USH1B;, features a modification of the amino acid from L to P at position 1858.
+The protein's natural variant, known as in USH1B;, features a modification of the amino acid from R to W at position 1873.
+The protein's natural variant, known as in USH1B;, features a modification of the amino acid from R to Q at position 1883.
+The protein's natural variant, known as in USH1B;, features a modification of the amino acid from P to L at position 1887.
+The protein's natural variant, known as in USH1B;, features a modification of the amino acid from G to E at position 2137.
+The protein's natural variant, known as in USH1B;, features a modification of the amino acid from G to S at position 2163.
+The protein's natural variant, known as in USH1B;, features a modification of the amino acid from G to D at position 2187.
+The protein's natural variant, known as in NS11; constitutively active form; increased GTPase activity, features a modification of the amino acid from G to V at position 23.
+The protein's natural variant, known as in NS11, features a modification of the amino acid from T to I at position 68.
+The protein's natural variant, known as in NS11, features a modification of the amino acid from Q to R at position 71.
+The protein's natural variant, known as in about 20% of the molecules, features a modification of the amino acid from A to P at position 3.
+The protein's natural variant, known as in NHEJ1-SCID; fails to translocate to the nucleus;, features a modification of the amino acid from R to G at position 57.
+The protein's natural variant, known as in NHEJ1-SCID;, features a modification of the amino acid from C to R at position 123.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to H at position 46.
+The protein's natural variant, known as in strain: NTHi TN106, features a modification of the amino acid from S to A at position 45.
+The protein's natural variant, known as in strain: NTHi TN106, features a modification of the amino acid from V to I at position 97.
+The protein's natural variant, known as in strain: NTHi TN106, features a modification of the amino acid from S to A at position 209.
+The protein's natural variant, known as in strain: NTHi TN106, features a modification of the amino acid from R to K at position 350.
+The protein's natural variant, known as in strain: NTHi TN106, features a modification of the amino acid from S to A at position 356.
+The protein's natural variant, known as in strain: CLIB 219, features a modification of the amino acid from H to R at position 90.
+The protein's natural variant, known as in strain: CLIB 630, features a modification of the amino acid from M to T at position 117.
+The protein's natural variant, known as in strain: CLIB 219, features a modification of the amino acid from K to T at position 157.
+The protein's natural variant, known as in strain: CLIB 630, features a modification of the amino acid from G to S at position 161.
+The protein's natural variant, known as in strain: CLIB 630, features a modification of the amino acid from T to I at position 165.
+The protein's natural variant, known as in strain: CLIB 630, features a modification of the amino acid from D to N at position 171.
+The protein's natural variant, known as in strain: CLIB 382, features a modification of the amino acid from Q to L at position 189.
+The protein's natural variant, known as in strain: CLIB 413 haplotype Ha2, features a modification of the amino acid from I to M at position 210.
+The protein's natural variant, known as in strain: CLIB 556, features a modification of the amino acid from E to K at position 249.
+The protein's natural variant, known as in strain: Sigma 1278B, features a modification of the amino acid from S to R at position 253.
+The protein's natural variant, known as in strain: CLIB 219, features a modification of the amino acid from S to N at position 325.
+The protein's natural variant, known as in strain: R12, features a modification of the amino acid from G to S at position 355.
+The protein's natural variant, known as in strain: CLIB 219, features a modification of the amino acid from S to L at position 384.
+The protein's natural variant, known as in strain: CLIB 410, CLIB 413 and Sigma 1278B, features a modification of the amino acid from L to M at position 409.
+The protein's natural variant, known as in Niq CART2 and Niq CART3, features a modification of the amino acid from Q to R at position 91.
+The protein's natural variant, known as in allele VN1R4*3;, features a modification of the amino acid from A to V at position 52.
+The protein's natural variant, known as in allele VN1R4*4;, features a modification of the amino acid from R to L at position 58.
+The protein's natural variant, known as in allele VN1R4*2 and allele VN1R4*3;, features a modification of the amino acid from D to N at position 220.
+The protein's natural variant, known as in a lung squamous cell carcinoma sample; somatic mutation, features a modification of the amino acid from S to A at position 496.
+The protein's natural variant, known as in NOC;, features a modification of the amino acid from R to W at position 1169.
+The protein's natural variant, known as in NOC, features a modification of the amino acid from L to P at position 1970.
+The protein's natural variant, known as in EDSCL2, features a modification of the amino acid from G to R at position 228.
+The protein's natural variant, known as in EDSCL2;, features a modification of the amino acid from G to R at position 963.
+The protein's natural variant, known as in strain: 14021-0231.6, features a modification of the amino acid from R to M at position 94.
+The natural variant of this protein is characterized by an amino acid alteration from P to A at position 213.
+The protein's natural variant, known as in PGL7; unknown pathological significance; not changed dihydrolipoyllysine-residue succinyltransferase activity;, features a modification of the amino acid from R to Q at position 231.
+The protein's natural variant, known as not changed dihydrolipoyllysine-residue succinyltransferase activity;, features a modification of the amino acid from D to N at position 304.
+The protein's natural variant, known as in PGL7; decreased dihydrolipoyllysine-residue succinyltransferase activity;, features a modification of the amino acid from G to E at position 374.
+The natural variant of this protein is characterized by an amino acid alteration from P to T at position 384.
+The protein's natural variant, known as in PGL7; unknown pathological significance; not changed dihydrolipoyllysine-residue succinyltransferase activity;, features a modification of the amino acid from Y to C at position 422.
+The protein's natural variant, known as in 66% of the molecules, features a modification of the amino acid from C to S at position 28.
+The protein's natural variant, known as in strain: Isolate DAO1Cds98/8/21-1Aomori, features a modification of the amino acid from A to T at position 23.
+The protein's natural variant, known as in strain: Isolate SO2Kmisc100 and Isolate SO2Kmisc101, features a modification of the amino acid from T to I at position 158.
+The protein's natural variant, known as in strain: Isolate SO2Kmisc100, features a modification of the amino acid from P to L at position 258.
+The protein's natural variant, known as in strain: Isolate SO2Kmisc101, features a modification of the amino acid from A to G at position 302.
+The protein's natural variant, known as in strain: Isolate HS1296, Isolate HS1297 and Isolate HSO960926-1, features a modification of the amino acid from H to Y at position 345.
+The protein's natural variant, known as in strain: Isolate HA6134, Isolate HS1237, Isolate HS1295, Isolate HS1296, Isolate HS1297, Isolate HSO960926-1, Isolate SO2Kmisc100 and Isolate SO2Kmisc101, features a modification of the amino acid from M to T at position 360.
+The protein's natural variant, known as in strain: Isolate HA6134, Isolate SO2Kmisc100 and Isolate SO2Kmisc101, features a modification of the amino acid from I to V at position 365.
+The protein's natural variant, known as in strain: S1; confers macrolide resistance, features a modification of the amino acid from D to DDEGPSM at position 77.
+The protein's natural variant, known as in strain: S26; confers macrolide resistance, features a modification of the amino acid from R to RRAKG at position 88.
+The protein's natural variant, known as in strain: S2 and S3; confers macrolide resistance, features a modification of the amino acid from G to D at position 91.
+The protein's natural variant, known as in strain: S49; confers macrolide resistance, features a modification of the amino acid from G to GKG at position 91.
+The protein's natural variant, known as in strain: S60; confers macrolide resistance, features a modification of the amino acid from G to GRADR at position 91.
+The protein's natural variant, known as in strain: S58; confers macrolide resistance, features a modification of the amino acid from G to GRAG at position 91.
+The protein's natural variant, known as in MC4DN6;, features a modification of the amino acid from R to W at position 217.
+The protein's natural variant, known as in MC4DN6;, features a modification of the amino acid from S to P at position 344.
+The protein's natural variant, known as found in patients with severe progressive myoclonic epilepsy; unknown pathological significance; results in increased protein activity when associated with I-153; less active in stimulating calcium release when associated with I-153;, features a modification of the amino acid from R to H at position 148.
+The protein's natural variant, known as found in patients with severe progressive myoclonic epilepsy; unknown pathological significance; results in increased protein activity when associated with H-148; less active in stimulating calcium release when associated with H-148;, features a modification of the amino acid from V to I at position 153.
+The protein's natural variant, known as found in a patient with myoclonic epilepsy; unknown pathological significance; results in decreased protein activity; less active in stimulating calcium release compared to wild-type;, features a modification of the amino acid from V to F at position 605.
+The protein's natural variant, known as found in a patient with autism spectrum disorder; unknown pathological significance; induces response to endoplasmic reticulum stress; negative regulation of dendrite morphogenesis, features a modification of the amino acid from M to T at position 152.
+The protein's natural variant, known as found in a patient with autism spectrum disorder; unknown pathological significance; induces response to endoplasmic reticulum stress; negative regulation of dendrite morphogenesis, features a modification of the amino acid from V to L at position 221.
+The protein's natural variant, known as impairs the ability to induce NF-kappa-B activation;, features a modification of the amino acid from L to V at position 128.
+The protein's natural variant, known as impairs the ability to induce NF-kappa-B activation;, features a modification of the amino acid from L to P at position 194.
+The protein's natural variant, known as impairs the ability to induce NF-kappa-B activation;, features a modification of the amino acid from A to V at position 474.
+The protein's natural variant, known as impairs the ability to induce NF-kappa-B activation;, features a modification of the amino acid from N to T at position 690.
+The protein's natural variant, known as impairs the ability to induce NF-kappa-B activation;, features a modification of the amino acid from Q to H at position 708.
+The natural variant of this protein is characterized by an amino acid alteration from E to EVEVVAE at position 79.
+The natural variant of this protein is characterized by an amino acid alteration from P to R at position 195.
+The natural variant of this protein is characterized by an amino acid alteration from I to F at position 216.
+The protein's natural variant, known as in allele A, features a modification of the amino acid from P to S at position 82.
+The protein's natural variant, known as in allele A, features a modification of the amino acid from K to E at position 93.
+The protein's natural variant, known as in allele A, features a modification of the amino acid from S to G at position 101.
+The natural variant of this protein is characterized by an amino acid alteration from E to D at position 412.
+The protein's natural variant, known as in strain: 8-6, features a modification of the amino acid from E to K at position 48.
+The protein's natural variant, known as in strain: 8-6, features a modification of the amino acid from V to I at position 56.
+The protein's natural variant, known as in strain: 8-6, features a modification of the amino acid from V to T at position 76.
+The protein's natural variant, known as in strain: 8-6 and NCIB 10662, features a modification of the amino acid from C to G at position 109.
+The protein's natural variant, known as in strain: 8-6, features a modification of the amino acid from G to S at position 149.
+The protein's natural variant, known as in strain: 8-6, features a modification of the amino acid from R to K at position 171.
+The protein's natural variant, known as in strain: NCIB 10662, features a modification of the amino acid from E to D at position 201.
+The protein's natural variant, known as in strain: NCIB 10662, features a modification of the amino acid from DN to KS at position 221.
+The protein's natural variant, known as in strain: 8-6, features a modification of the amino acid from D to N at position 220.
+The protein's natural variant, known as in strain: 8-6, features a modification of the amino acid from N to S at position 332.
+The protein's natural variant, known as in strain: NCIB 10662, features a modification of the amino acid from T to A at position 347.
+The protein's natural variant, known as in strain: NCIB 10662, features a modification of the amino acid from D to N at position 481.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from E to G at position 92.
+The protein's natural variant, known as in Ag5.1 negative strains, features a modification of the amino acid from D to G at position 136.
+The protein's natural variant, known as in strain: Palo Alto17 and 3D7, features a modification of the amino acid from P to T at position 160.
+The protein's natural variant, known as in SPD1, features a modification of the amino acid from A to AAAAAAAAAA at position 57.
+The protein's natural variant, known as in SPD1; decreases the transcriptional activator activity;, features a modification of the amino acid from R to G at position 306.
+The protein's natural variant, known as in SPD1; decreases the transcriptional activator activity;, features a modification of the amino acid from R to Q at position 306.
+The protein's natural variant, known as in SPD1;, features a modification of the amino acid from R to W at position 306.
+The protein's natural variant, known as in SPD1; disrupts interaction with DNA;, features a modification of the amino acid from T to R at position 313.
+The protein's natural variant, known as in BDE1 and BDD;, features a modification of the amino acid from S to C at position 316.
+The protein's natural variant, known as in BDE1; decreases the transcriptional activator activity;, features a modification of the amino acid from I to L at position 322.
+The protein's natural variant, known as in BDSDO;, features a modification of the amino acid from Q to K at position 325.
+The protein's natural variant, known as in SDTY5; impairs capacity to transactivate EPHA7 promoter;, features a modification of the amino acid from Q to R at position 325.
+The protein's natural variant, known as in BCS2;, features a modification of the amino acid from Y to C at position 107.
+The protein's natural variant, known as in strain: C.AKR, features a modification of the amino acid from M to V at position 105.
+The protein's natural variant, known as in strain: CHAU1, features a modification of the amino acid from T to A at position 374.
+The protein's natural variant, known as in clone HYA-2, features a modification of the amino acid from D to S at position 371.
+The protein's natural variant, known as found in a renal cell carcinoma sample; somatic mutation;, features a modification of the amino acid from T to I at position 214.
+The protein's natural variant, known as in HDBSCC; normal location at the cell membrane;, features a modification of the amino acid from E to K at position 116.
+The protein's natural variant, known as in HDBSCC; the mutant is retained in the endoplasmic reticulum;, features a modification of the amino acid from C to Y at position 219.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from Q to R at position 770.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from C to G at position 878.
+The protein's natural variant, known as in strain: VT847, features a modification of the amino acid from S to G at position 51.
+The protein's natural variant, known as in strain: VT847, features a modification of the amino acid from V to L at position 53.
+The protein's natural variant, known as in strain: VT847, features a modification of the amino acid from C to W at position 66.
+The protein's natural variant, known as in strain: ED3032 and ED3036, features a modification of the amino acid from V to F at position 86.
+The protein's natural variant, known as in strain: VT847, features a modification of the amino acid from V to I at position 90.
+The protein's natural variant, known as in strain: EG4181, features a modification of the amino acid from T to A at position 98.
+The protein's natural variant, known as in strain: ED3092 and ED3101, features a modification of the amino acid from V to I at position 168.
+The protein's natural variant, known as in GSD6;, features a modification of the amino acid from N to S at position 339.
+The protein's natural variant, known as in GSD6;, features a modification of the amino acid from N to K at position 377.
+The protein's natural variant, known as in CBAS2; decreases protein level; accumulates in inclusion bodies; acks of 5-beta-reductase activity;, features a modification of the amino acid from L to F at position 106.
+The protein's natural variant, known as in CBAS2; highly reduced KM and Vmax with cortisone as substrate. Increases KM and decreases kcat with testosterone as substrate. No change in NADPH affinity. More thermolabile in the absence of NADPH. Reduces 5-beta-reductase activity;, features a modification of the amino acid from P to R at position 133.
+The protein's natural variant, known as in CBAS2; decreases protein level; accumulates in inclusion bodies; decreases 5-beta-reductase activity;, features a modification of the amino acid from P to L at position 198.
+The protein's natural variant, known as in CBAS2; decreases protein level; accumulates in inclusion bodies; decreases 5-beta-reductase activity;, features a modification of the amino acid from G to E at position 223.
+The protein's natural variant, known as in CBAS2; decreases protein level; accumulates in inclusion bodies; lacks of 5-beta-reductase activity;, features a modification of the amino acid from R to C at position 261.
+The protein's natural variant, known as in DFNB57; unknown pathological significance;, features a modification of the amino acid from R to L at position 66.
+The protein's natural variant, known as in DFNB57;, features a modification of the amino acid from G to R at position 103.
+The protein's natural variant, known as in DFNB57;, features a modification of the amino acid from G to R at position 228.
+The protein's natural variant, known as in DFNB57;, features a modification of the amino acid from M to R at position 285.
+The protein's natural variant, known as in EPM1;, features a modification of the amino acid from G to R at position 4.
+The protein's natural variant, known as found in a family diagnosed with inherited Brugada syndrome; unknown pathological significance; does not affect nuclear membrane localization. Reduces cardiomyocyte cell surface expression of SCN5A. Decreases in Na(+) current in cardiomyocytes, features a modification of the amino acid from R to Q at position 539.
+The protein's natural variant, known as in OIEDS2; decreased N-terminal propeptide processing;, features a modification of the amino acid from G to D at position 109.
+The protein's natural variant, known as in OI4;, features a modification of the amino acid from G to S at position 193.
+The protein's natural variant, known as in OIEDS2, features a modification of the amino acid from G to V at position 196.
+The protein's natural variant, known as in OI4;, features a modification of the amino acid from G to R at position 202.
+The protein's natural variant, known as in OI1;, features a modification of the amino acid from G to D at position 211.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from R to C at position 234.
+The protein's natural variant, known as in OI1, features a modification of the amino acid from G to R at position 247.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to D at position 253.
+The protein's natural variant, known as in OI4;, features a modification of the amino acid from G to V at position 256.
+The protein's natural variant, known as in OI2, features a modification of the amino acid from G to R at position 283.
+The protein's natural variant, known as in OI1;, features a modification of the amino acid from G to R at position 319.
+The protein's natural variant, known as in OI4;, features a modification of the amino acid from G to E at position 325.
+The protein's natural variant, known as in OI1, OI3 and OI4;, features a modification of the amino acid from G to S at position 328.
+The protein's natural variant, known as in OI3;, features a modification of the amino acid from G to D at position 331.
+The protein's natural variant, known as in OI2, features a modification of the amino acid from G to C at position 334.
+The protein's natural variant, known as in OI3;, features a modification of the amino acid from G to C at position 337.
+The protein's natural variant, known as in OI3;, features a modification of the amino acid from G to S at position 337.
+The protein's natural variant, known as in OI3;, features a modification of the amino acid from G to C at position 349.
+The protein's natural variant, known as in OI3;, features a modification of the amino acid from G to S at position 358.
+The protein's natural variant, known as in OI2, features a modification of the amino acid from G to E at position 397.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to V at position 409.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to E at position 433.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to C at position 454.
+The protein's natural variant, known as in OI2; requires 2 nucleotide substitutions, features a modification of the amino acid from G to L at position 457.
+The protein's natural variant, known as in OI3;, features a modification of the amino acid from G to S at position 460.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to D at position 511.
+The protein's natural variant, known as in OI3;, features a modification of the amino acid from G to R at position 517.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to E at position 526.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to R at position 547.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to C at position 562.
+The protein's natural variant, known as in OI2, features a modification of the amino acid from G to V at position 562.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to R at position 586.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to S at position 592.
+The protein's natural variant, known as in OI;, features a modification of the amino acid from G to S at position 601.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to D at position 625.
+The protein's natural variant, known as in OI4;, features a modification of the amino acid from G to V at position 634.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to D at position 637.
+The protein's natural variant, known as in OI2, features a modification of the amino acid from G to S at position 640.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to D at position 670.
+The protein's natural variant, known as in OI3;, features a modification of the amino acid from G to D at position 676.
+The protein's natural variant, known as in OI3 and OI4;, features a modification of the amino acid from G to V at position 676.
+The protein's natural variant, known as found in a patient with a variant form of Marfan syndrome; unknown pathological significance;, features a modification of the amino acid from R to Q at position 708.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to D at position 715.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to C at position 730.
+The protein's natural variant, known as in OI1;, features a modification of the amino acid from G to C at position 733.
+The protein's natural variant, known as in OI1; mild;, features a modification of the amino acid from G to C at position 736.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to R at position 739.
+The protein's natural variant, known as in OI2, features a modification of the amino acid from G to V at position 748.
+The protein's natural variant, known as in OI4;, features a modification of the amino acid from G to S at position 751.
+The protein's natural variant, known as in OI4;, features a modification of the amino acid from G to C at position 754.
+The protein's natural variant, known as in OI2, features a modification of the amino acid from G to R at position 754.
+The protein's natural variant, known as in OI4;, features a modification of the amino acid from G to V at position 766.
+The protein's natural variant, known as in OI3;, features a modification of the amino acid from G to S at position 778.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to R at position 784.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to C at position 787.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to D at position 790.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to S at position 796.
+The protein's natural variant, known as in OI2, features a modification of the amino acid from P to PP at position 798.
+The protein's natural variant, known as in OI4, features a modification of the amino acid from G to GPPG at position 811.
+The protein's natural variant, known as in OI3;, features a modification of the amino acid from G to S at position 820.
+The protein's natural variant, known as in OI3, features a modification of the amino acid from G to C at position 835.
+The protein's natural variant, known as in OI1;, features a modification of the amino acid from G to S at position 835.
+The protein's natural variant, known as in OI3, features a modification of the amino acid from G to R at position 856.
+The protein's natural variant, known as in OI2, features a modification of the amino acid from G to V at position 856.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to C at position 877.
+The protein's natural variant, known as in OI3 and OI4;, features a modification of the amino acid from G to D at position 892.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to D at position 895.
+The protein's natural variant, known as in OI3; moderate;, features a modification of the amino acid from G to S at position 949.
+The protein's natural variant, known as in OI2, features a modification of the amino acid from G to D at position 955.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to S at position 955.
+The protein's natural variant, known as in OI3;, features a modification of the amino acid from G to V at position 973.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to D at position 982.
+The protein's natural variant, known as in OI4, features a modification of the amino acid from P to PVGP at position 989.
+The protein's natural variant, known as in OI3;, features a modification of the amino acid from G to V at position 991.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to D at position 997.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to D at position 1003.
+The protein's natural variant, known as in OI3 and OI4; moderate;, features a modification of the amino acid from G to S at position 1012.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to E at position 1027.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to D at position 1066.
+The protein's natural variant, known as in OI2, features a modification of the amino acid from G to C at position 1078.
+The protein's natural variant, known as in OI3;, features a modification of the amino acid from G to D at position 1087.
+The protein's natural variant, known as in OI3;, features a modification of the amino acid from G to A at position 1096.
+The natural variant of this protein is characterized by an amino acid alteration from P to L at position 1101.
+The protein's natural variant, known as in OI4;, features a modification of the amino acid from G to R at position 1102.
+The protein's natural variant, known as found in a patient with mild osteogenesis imperfecta associated with increased bone mineral density; results in defective type I procollagen processing; incorporation of the immature procollagen into the matrix leads to increased bone matrix mineralization and altered collagen fibril structure, features a modification of the amino acid from A to T at position 1119.
+The protein's natural variant, known as in OI3;, features a modification of the amino acid from T to P at position 1148.
+The protein's natural variant, known as in OI1;, features a modification of the amino acid from C to Y at position 1195.
+The natural variant of this protein is characterized by an amino acid alteration from M to V at position 198.
+The protein's natural variant, known as found in an individual with overgrowth, learning disability and dysmorphic features; unknown pathological significance;, features a modification of the amino acid from R to H at position 286.
+The natural variant of this protein is characterized by an amino acid alteration from F to R at position 65.
+The natural variant of this protein is characterized by an amino acid alteration from H to D at position 709.
+The protein's natural variant, known as in AGS5; loss of oligomerization; decreased ability to restrict LINE-1 retrotransposon activity;, features a modification of the amino acid from H to P at position 123.
+The protein's natural variant, known as in AGS5; loss of oligomerization;, features a modification of the amino acid from R to C at position 143.
+The protein's natural variant, known as in AGS5; loss of oligomerization; decreased ability to restrict LINE-1 retrotransposon activity;, features a modification of the amino acid from R to H at position 143.
+The protein's natural variant, known as in AGS5; loss of oligomerization; decreased ability to restrict LINE-1 retrotransposon activity;, features a modification of the amino acid from R to Q at position 145.
+The protein's natural variant, known as in AGS5; loss of function in defense response to virus; loss of oligomerization; decreased ability to restrict LINE-1 retrotransposon activity, features a modification of the amino acid from H to Y at position 167.
+The protein's natural variant, known as in AGS5 and CHBL2; loss of function in defense response to virus; decreased oligomerization; decreased ability to restrict LINE-1 retrotransposon activity;, features a modification of the amino acid from I to N at position 201.
+The protein's natural variant, known as in AGS5; does not affect oligomerization; decreased ability to restrict LINE-1 retrotransposon activity; does not affect localization to nucleus;, features a modification of the amino acid from G to S at position 209.
+The protein's natural variant, known as in AGS5; loss of function in defense response to virus; does not affect oligomerization; decreased ability to restrict LINE-1 retrotransposon activity;, features a modification of the amino acid from M to V at position 254.
+The protein's natural variant, known as in AGS5; loss of oligomerization; decreased ability to restrict LINE-1 retrotransposon activity;, features a modification of the amino acid from R to H at position 290.
+The protein's natural variant, known as in AGS5; loss of function in defense response to virus; decreased oligomerization;, features a modification of the amino acid from L to S at position 369.
+The protein's natural variant, known as in AGS5; loss of function in defense response to virus; loss of oligomerization;, features a modification of the amino acid from M to V at position 385.
+The protein's natural variant, known as in AGS5; loss of function in defense response to virus; decreased oligomerization; does not affect localization to nucleus; novel localization to the cytoplasm;, features a modification of the amino acid from I to T at position 448.
+The protein's natural variant, known as in strain: cv. Uk-2, features a modification of the amino acid from T to S at position 310.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from I to V at position 400.
+The protein's natural variant, known as in OA1; results in altered glycosylation pattern and subcellular localization consistent with protein retention in the endoplasmic reticulum; lacks G protein-activation abilities;, features a modification of the amino acid from R to C at position 5.
+The protein's natural variant, known as in OA1; results in altered glycosylation pattern and subcellular localization consistent with protein retention in the endoplasmic reticulum;, features a modification of the amino acid from G to D at position 35.
+The protein's natural variant, known as in OA1;, features a modification of the amino acid from L to R at position 39.
+The protein's natural variant, known as in OA1; results in altered glycosylation pattern and subcellular localization consistent with protein retention in the endoplasmic reticulum;, features a modification of the amino acid from D to N at position 78.
+The protein's natural variant, known as in OA1;, features a modification of the amino acid from D to V at position 78.
+The protein's natural variant, known as in OA1, features a modification of the amino acid from G to V at position 81.
+The protein's natural variant, known as in OA1; results in altered glycosylation pattern and subcellular localization consistent with protein retention in the endoplasmic reticulum;, features a modification of the amino acid from G to D at position 84.
+The protein's natural variant, known as in OA1;, features a modification of the amino acid from G to R at position 84.
+The protein's natural variant, known as in NYS6;, features a modification of the amino acid from S to F at position 89.
+The protein's natural variant, known as in OA1, features a modification of the amino acid from C to G at position 116.
+The protein's natural variant, known as in OA1;, features a modification of the amino acid from C to R at position 116.
+The protein's natural variant, known as in OA1; results in altered glycosylation pattern and subcellular localization consistent with protein retention in the endoplasmic reticulum;, features a modification of the amino acid from C to S at position 116.
+The protein's natural variant, known as in OA1, features a modification of the amino acid from C to W at position 116.
+The protein's natural variant, known as in OA1; results in altered glycosylation pattern and subcellular localization consistent with protein retention in the endoplasmic reticulum;, features a modification of the amino acid from G to E at position 118.
+The protein's natural variant, known as in OA1;, features a modification of the amino acid from Q to R at position 124.
+The protein's natural variant, known as in OA1, features a modification of the amino acid from W to R at position 132.
+The protein's natural variant, known as in OA1; results in altered glycosylation pattern and subcellular localization consistent with protein retention in the endoplasmic reticulum;, features a modification of the amino acid from W to R at position 133.
+The protein's natural variant, known as in OA1, features a modification of the amino acid from L to P at position 134.
+The protein's natural variant, known as in OA1;, features a modification of the amino acid from A to V at position 138.
+The protein's natural variant, known as in OA1;, features a modification of the amino acid from S to N at position 152.
+The protein's natural variant, known as in OA1, features a modification of the amino acid from T to N at position 166.
+The protein's natural variant, known as in OA1; results in altered glycosylation pattern and subcellular localization consistent with protein retention in the endoplasmic reticulum;, features a modification of the amino acid from A to D at position 173.
+The protein's natural variant, known as in OA1, features a modification of the amino acid from E to K at position 185.
+The protein's natural variant, known as in OA1, features a modification of the amino acid from R to P at position 186.
+The protein's natural variant, known as in OA1;, features a modification of the amino acid from R to W at position 186.
+The protein's natural variant, known as in OA1; not delivered at the cell surface of melanocytic and non-melanocytic cells;, features a modification of the amino acid from G to V at position 229.
+The protein's natural variant, known as in OA1; abnormal distribution of melanosomes; Not delivered at the cell surface of melanocytic and non-melanocytic cells;, features a modification of the amino acid from T to K at position 232.
+The protein's natural variant, known as in OA1;, features a modification of the amino acid from E to K at position 233.
+The protein's natural variant, known as in OA1; not delivered at the cell surface of melanocytic and non-melanocytic cells, features a modification of the amino acid from E to K at position 235.
+The protein's natural variant, known as in OA1; not delivered at the cell surface of melanocytic and non-melanocytic cells;, features a modification of the amino acid from I to V at position 244.
+The protein's natural variant, known as in OA1; results in altered glycosylation pattern and subcellular localization consistent with protein retention in the endoplasmic reticulum, features a modification of the amino acid from I to N at position 261.
+The protein's natural variant, known as in OA1;, features a modification of the amino acid from E to G at position 271.
+The protein's natural variant, known as in OA1;, features a modification of the amino acid from W to C at position 292.
+The protein's natural variant, known as in OA1; results in altered glycosylation pattern and subcellular localization consistent with protein retention in the endoplasmic reticulum;, features a modification of the amino acid from W to G at position 292.
+The protein's natural variant, known as in DRTA2; disruption of V-ATPase assembly resulting in loss of enzyme activity; impaired trafficking of V-ATPase to apical cell membrane; impaired renal proton secretion;, features a modification of the amino acid from L to P at position 81.
+The protein's natural variant, known as in DRTA2;, features a modification of the amino acid from G to V at position 123.
+The protein's natural variant, known as in DRTA2; disruption of V-ATPase assembly resulting in loss of enzyme activity; impaired trafficking of V-ATPase to apical cell membrane; impaired renal proton secretion;, features a modification of the amino acid from R to W at position 124.
+The protein's natural variant, known as in DRTA2;, features a modification of the amino acid from R to C at position 157.
+The protein's natural variant, known as in DRTA2; disruption of V-ATPase assembly resulting in loss of enzyme activity; impaired trafficking of V-ATPase to apical cell membrane; impaired renal proton secretion, features a modification of the amino acid from M to R at position 174.
+The protein's natural variant, known as in DRTA2; disruption of V-ATPase assembly resulting in loss of enzyme activity; impaired trafficking of V-ATPase to apical cell membrane; impaired renal proton secretion;, features a modification of the amino acid from T to P at position 275.
+The protein's natural variant, known as in DRTA2; disruption of V-ATPase assembly resulting in loss of enzyme activity; impaired trafficking of V-ATPase to apical cell membrane; impaired renal proton secretion;, features a modification of the amino acid from G to E at position 316.
+The protein's natural variant, known as in DRTA2; disruption of V-ATPase assembly resulting in loss of enzyme activity; impaired trafficking of V-ATPase to apical cell membrane; impaired renal proton secretion;, features a modification of the amino acid from P to R at position 346.
+The protein's natural variant, known as in DRTA2; disruption of V-ATPase assembly resulting in loss of enzyme activity; impaired trafficking of V-ATPase to apical cell membrane; impaired renal proton secretion, features a modification of the amino acid from G to S at position 364.
+The protein's natural variant, known as in NPHS20; rescues only partially glomerular filtration defects in tbc1d8b knockout fish; defective vesicular trafficking in podocytes;, features a modification of the amino acid from Q to H at position 246.
+The protein's natural variant, known as in NPHS20; exhibits intracellular vesicular localization; rescues only partially glomerular filtration defects in tbc1d8b knockout fish; reduced podocyte migration; defective vesicular trafficking in podocytes;, features a modification of the amino acid from F to S at position 291.
+The protein's natural variant, known as in strain: CBS 789 and CLIB 381, features a modification of the amino acid from M to V at position 39.
+The protein's natural variant, known as in strain: CLIB 660, features a modification of the amino acid from M to L at position 46.
+The protein's natural variant, known as in strain: CBS 789 and CLIB 381, features a modification of the amino acid from M to I at position 51.
+The protein's natural variant, known as in strain: CBS 789 and CLIB 381, features a modification of the amino acid from V to I at position 106.
+The protein's natural variant, known as in strain: CBS 789 and CLIB 381, features a modification of the amino acid from M to I at position 179.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from Q to H at position 286.
+The protein's natural variant, known as in MAHCD; cblD variant 2, features a modification of the amino acid from S to SLAEPLS at position 108.
+The protein's natural variant, known as in MAHCD; cblD variant 1; impairs interaction with MMACHC;, features a modification of the amino acid from T to N at position 182.
+The protein's natural variant, known as in MAHCD; cblD variant 1;, features a modification of the amino acid from Y to C at position 249.
+The protein's natural variant, known as in MAHCD; cblD variant 1; decreases methylcobalamin levels and increases adenosylcobalamin levels; no effect on interaction with MMACHC;, features a modification of the amino acid from L to P at position 259.
+The protein's natural variant, known as in ROSAH, features a modification of the amino acid from T to M at position 237.
+The protein's natural variant, known as in an ovarian mucinous carcinoma sample; somatic mutation, features a modification of the amino acid from K to E at position 339.
+The protein's natural variant, known as in variant copia-related, features a modification of the amino acid from STTGYLFKMFDFNLICWNTKRQNS to VQQGIYSKCLILISFVGIQRDRTQ at position 1288.
+The protein's natural variant, known as in MOWS, features a modification of the amino acid from R to G at position 953.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from D to N at position 983.
+The protein's natural variant, known as in MOWS;, features a modification of the amino acid from Q to R at position 1119.
+The protein's natural variant, known as in Ly-6E.1, features a modification of the amino acid from D to G at position 63.
+The protein's natural variant, known as in Ly-6E.1, features a modification of the amino acid from V to A at position 106.
+The protein's natural variant, known as probable disease-associated variant found in a patient with idiopathic childhood epilepsy; de novo mutation; loss of function in increasing sodium channel activity;, features a modification of the amino acid from D to N at position 25.
+The protein's natural variant, known as in ATFB13; the mutant results in highly reduced sodium currents and altered channel gating when coexpressed with SCN5A in a heterologous expression system;, features a modification of the amino acid from R to H at position 85.
+The protein's natural variant, known as probable disease-associated variant found in a patient with non-specific cardiac conduction defects;, features a modification of the amino acid from E to Q at position 87.
+The protein's natural variant, known as in DEE52; unknown pathological significance, features a modification of the amino acid from I to T at position 106.
+The protein's natural variant, known as in GEFSP1; can rescue the loss of function and defective trafficking to cell membrane phenotype of the SCN1A variant Thr-1852;, features a modification of the amino acid from C to W at position 121.
+The protein's natural variant, known as in DEE52; severely decreased channel localization at the cell membrane;, features a modification of the amino acid from R to C at position 125.
+The protein's natural variant, known as in GEFSP1;, features a modification of the amino acid from R to L at position 125.
+The protein's natural variant, known as in ATFB13; the mutant results in reduced sodium currents when coexpressed with SCN5A in a heterologous expression system;, features a modification of the amino acid from D to N at position 153.
+The protein's natural variant, known as in AOMS3; expression of glucose-6-phosphatase is significantly higher than wild-type;, features a modification of the amino acid from H to P at position 90.
+The protein's natural variant, known as in AOMS3; accumulation of intracellular lipid is significantly greater than with wild-type protein; cells expressing the variant are able to transform into mature adipocytes without requiring adipogenic medium; expression levels of CEBPA, PPARG forms 1 and 2 and PPARGC1A are higher and those of GLI1 and CDKN1B are lower in cells transfected with the mutant protein compared to wild-type; WNT1 signaling activity is lower in mutant cells compared to wild-type;, features a modification of the amino acid from R to C at position 102.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation, features a modification of the amino acid from Q to R at position 275.
+The natural variant of this protein is characterized by an amino acid alteration from V to L at position 161.
+The protein's natural variant, known as in plasmid pYVa127/90, features a modification of the amino acid from I to V at position 34.
+The protein's natural variant, known as in plasmid pYVa127/90, features a modification of the amino acid from A to S at position 99.
+The protein's natural variant, known as in plasmid pYVa127/90, features a modification of the amino acid from A to T at position 152.
+The protein's natural variant, known as in plasmid pYVa127/90, features a modification of the amino acid from G to C at position 228.
+The protein's natural variant, known as in a breast infiltrating ductal carcinoma sample; somatic mutation, features a modification of the amino acid from E to Q at position 30.
+The protein's natural variant, known as in a breast infiltrating ductal carcinoma sample; somatic mutation;, features a modification of the amino acid from A to S at position 78.
+The protein's natural variant, known as in a lung squamous cell carcinoma sample; somatic mutation, features a modification of the amino acid from H to L at position 217.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation, features a modification of the amino acid from S to I at position 116.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from K to I at position 212.
+The protein's natural variant, known as in plasmid pCP301 and plasmid pINV_F6_M1382, features a modification of the amino acid from S to I at position 2.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from I to V at position 30.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from E to A at position 66.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from N to K at position 76.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from A to V at position 94.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from R to K at position 105.
+The protein's natural variant, known as in plasmid pWR100, features a modification of the amino acid from R to A at position 116.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from R to S at position 116.
+The protein's natural variant, known as in plasmid pCP301 and plasmid pINV_F6_M1382, features a modification of the amino acid from E to D at position 202.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from H to Y at position 269.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from K to Q at position 285.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from D to N at position 336.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from T to S at position 434.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from E to G at position 443.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from E to V at position 450.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from I to T at position 458.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from I to V at position 482.
+The protein's natural variant, known as displays higher channel activity and enhanced chloride-bicarbonate ion exchange;, features a modification of the amino acid from Y to N at position 70.
+The protein's natural variant, known as results in smaller halide currents but not for thiocyanate ion;, features a modification of the amino acid from T to N at position 127.
+The protein's natural variant, known as decreased plasma membrane expression which partially accounts for decreased whole cell currents; transport is reduced to about 50%;, features a modification of the amino acid from V to L at position 622.
+The protein's natural variant, known as decreased plasma membrane expression which partially accounts for decreased whole cell currents;, features a modification of the amino acid from V to M at position 744.
+The protein's natural variant, known as in allele AHSG*1;, features a modification of the amino acid from M to T at position 248.
+The protein's natural variant, known as in allele AHSG*1;, features a modification of the amino acid from S to T at position 256.
+The protein's natural variant, known as in allele AHSG*5;, features a modification of the amino acid from D to N at position 276.
+The protein's natural variant, known as in allele AHSG*3;, features a modification of the amino acid from R to C at position 317.
+The protein's natural variant, known as in APMR1; unknown pathological significance;, features a modification of the amino acid from R to H at position 317.
+The protein's natural variant, known as in EVR5;, features a modification of the amino acid from T to M at position 49.
+The protein's natural variant, known as in EVR5;, features a modification of the amino acid from L to H at position 101.
+The protein's natural variant, known as in EVR5;, features a modification of the amino acid from Y to C at position 138.
+The protein's natural variant, known as in EVR5;, features a modification of the amino acid from G to R at position 188.
+The protein's natural variant, known as in EVR5, features a modification of the amino acid from M to R at position 210.
+The protein's natural variant, known as in EVR5, features a modification of the amino acid from L to P at position 223.
+The protein's natural variant, known as in EVR5;, features a modification of the amino acid from A to P at position 237.
+The protein's natural variant, known as found in aldosterone-producing adrenal adenoma samples; somatic mutation, features a modification of the amino acid from E to Q at position 145.
+The protein's natural variant, known as in HALD3; results in a profound alteration of channel function with loss of channel selectivity and membrane depolarization;, features a modification of the amino acid from G to E at position 151.
+The protein's natural variant, known as in HALD3; detected as germline mutation in a kindred with severe primary aldosteronism and adrenocortical hyperplasia; also found as somatic mutation in aldosterone-producing adrenal adenoma samples; results in loss of channel selectivity and membrane depolarization;, features a modification of the amino acid from G to R at position 151.
+The protein's natural variant, known as in HALD3; results in alteration of channel function with reduced channel selectivity and membrane depolarization; increases expression of CYP11B2 and its transcriptional regulator NR4A2, features a modification of the amino acid from Y to C at position 152.
+The protein's natural variant, known as in HALD3; loss of channel selectivity;, features a modification of the amino acid from I to S at position 157.
+The protein's natural variant, known as in HALD3; also found in aldosterone-producing adrenal adenoma samples; results in loss of channel selectivity and membrane depolarization; increases expression of CYP11B2 and its transcriptional regulators NR4A2 and ATF2; increases aldosterone and hybrid steroids 18-oxocortisol and 18-hydroxycortisol synthesis; increases STAR expression and phosphorylation;, features a modification of the amino acid from T to A at position 158.
+The protein's natural variant, known as found in aldosterone-producing adrenal adenoma samples; somatic mutation; results in loss of channel selectivity and membrane depolarization;, features a modification of the amino acid from L to R at position 168.
+The protein's natural variant, known as found in patients with hypertension with ACTH-dependent aldosterone hypersecretion; unknown pathological significance; no effect on channel function;, features a modification of the amino acid from V to M at position 259.
+The protein's natural variant, known as probable disease-associated variant found in patients with hypertension with ACTH-dependent aldosterone hypersecretion; loss of channel selectivity, features a modification of the amino acid from Y to N at position 348.
+The protein's natural variant, known as in LQT13;, features a modification of the amino acid from G to R at position 387.
+The protein's natural variant, known as in strain: ISP 5236, features a modification of the amino acid from SGS to ERI at position 146.
+The protein's natural variant, known as in strain: ISP 5236, features a modification of the amino acid from G to R at position 329.
+The protein's natural variant, known as in strain: ISP 5236, features a modification of the amino acid from TAR to RPL at position 342.
+The protein's natural variant, known as in strain: 3610, features a modification of the amino acid from M to A at position 69.
+The protein's natural variant, known as in strain: Berkeley, JP-5, JP-35, JP-55, JP-75, KN-12 and Oregon-R, features a modification of the amino acid from A to S at position 11.
+The protein's natural variant, known as in strain: 1420#1, JP-169, JP-186, JP-190, KO123, KN-3, KN-9, KN-10, TN22 and TN256, features a modification of the amino acid from S to R at position 71.
+The protein's natural variant, known as in strain: JP-55, features a modification of the amino acid from D to E at position 121.
+The protein's natural variant, known as in strain: 1420#1, JP-190, JP-169, JP-186, KO123, TN22 and TN256, features a modification of the amino acid from D to G at position 121.
+The protein's natural variant, known as in strain: KN-10, KN-3 and KN-9, features a modification of the amino acid from D to N at position 121.
+The protein's natural variant, known as in strain: JP-75, KN-17, KN-21, KN-22 and L16, features a modification of the amino acid from S to T at position 138.
+The protein's natural variant, known as in strain: 1420#1, JP-169, JP-186, JP-190, KO123, KN-3, KN-9, KN-10, TN22 and TN256, features a modification of the amino acid from S to R at position 156.
+The protein's natural variant, known as in strain: 1420#1, AO168, J87, JP-60, JP-169, JP-186, JP-190, KO123, KN-3, KN-9, KN-10, TN22 and TN256, features a modification of the amino acid from D to N at position 278.
+The protein's natural variant, known as in strain: KN-15, features a modification of the amino acid from T to I at position 288.
+The protein's natural variant, known as in strain: Berkeley, JP-5, JP-35, JP-55, JP-60, JP-65, JP-70, JP-75, JP-169, JP-186, JP-190, KN-3, KN-9, KN-10, KN-12, KN-17, KN-21 and KN-23, features a modification of the amino acid from T to A at position 398.
+The protein's natural variant, known as in strain: Berkeley, JP-5, JP-35, JP-55, JP-65, JP-70, KN-12 and KN-21, features a modification of the amino acid from S to L at position 401.
+The protein's natural variant, known as in strain: 1420#1, AO168, J87, JP-60, JP-169, JP-186, JP-190, KO123, KN-3, KN-9, KN-10, TN22 and TN256, features a modification of the amino acid from E to A at position 403.
+The protein's natural variant, known as in strain: Berkeley, JP-5, JP-35, JP-55, JP-65 and KN-12, features a modification of the amino acid from N to S at position 410.
+The protein's natural variant, known as in strain: JP-1, JP-15, JP-84, KO140 and KN-27, features a modification of the amino acid from V to I at position 465.
+The protein's natural variant, known as in strain: 1420#1, AO168, J87, JP-1, JP-15, JP-55, JP-60, JP-75, JP-84, JP-169, JP-186, JP-190, KO123, KO140, KN-3, KN-9, KN-10, KN-15, KN-17, KN-21, KN-22, KN-23, KN-27, L16, TN22 and TN256, features a modification of the amino acid from Y to N at position 476.
+The protein's natural variant, known as in strain: KN-21, features a modification of the amino acid from G to A at position 478.
+The protein's natural variant, known as found in patients with type 2 diabetes; unknown pathological significance, features a modification of the amino acid from F to S at position 635.
+The protein's natural variant, known as found in patients with type 2 diabetes; unknown pathological significance, features a modification of the amino acid from Q to P at position 649.
+The protein's natural variant, known as found in patients with type 2 diabetes; unknown pathological significance, features a modification of the amino acid from R to C at position 650.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from V to I at position 190.
+The protein's natural variant, known as in strain: Isolate 95/8/19-1, features a modification of the amino acid from L to F at position 82.
+The protein's natural variant, known as in strain: Isolate #696, features a modification of the amino acid from A to V at position 84.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from A to T at position 23.
+The protein's natural variant, known as can be associated with lower folate and higher homocysteine levels;, features a modification of the amino acid from H to Y at position 475.
+The protein's natural variant, known as in NTD; protein interactions not affected by the mutation; shows reduced protein localization to the cell membrane;, features a modification of the amino acid from P to S at position 454.
+The protein's natural variant, known as in NTD; protein interactions not affected by the mutation; shows reduced protein localization to the cell membrane;, features a modification of the amino acid from R to Q at position 1535.
+The protein's natural variant, known as in strain: Isolate SMG-7470, features a modification of the amino acid from V to I at position 115.
+The protein's natural variant, known as in strain: Isolate SMG-7470, features a modification of the amino acid from A to T at position 190.
+The protein's natural variant, known as in strain: Isolate SMG-7470, features a modification of the amino acid from I to M at position 241.
+The protein's natural variant, known as in strain: Isolate SMG-7470, features a modification of the amino acid from Y to H at position 345.
+The protein's natural variant, known as in strain: Isolate SMG-7470, features a modification of the amino acid from I to V at position 368.
+The protein's natural variant, known as in allele DEC-1-FC3, features a modification of the amino acid from M to V at position 627.
+The protein's natural variant, known as in allele DEC-1-FC4, features a modification of the amino acid from Q to H at position 644.
+The protein's natural variant, known as in allele DEC-1-FC3, features a modification of the amino acid from Q to H at position 690.
+The protein's natural variant, known as in isoform B, features a modification of the amino acid from V to A at position 61.
+The protein's natural variant, known as in isoform B, features a modification of the amino acid from I to V at position 64.
+The protein's natural variant, known as in isoform B, features a modification of the amino acid from A to V at position 89.
+The protein's natural variant, known as in VWM;, features a modification of the amino acid from D to V at position 62.
+The protein's natural variant, known as in VWM;, features a modification of the amino acid from L to S at position 68.
+The protein's natural variant, known as in VWM;, features a modification of the amino acid from V to G at position 73.
+The protein's natural variant, known as in VWM;, features a modification of the amino acid from A to T at position 74.
+The protein's natural variant, known as in VWM;, features a modification of the amino acid from T to A at position 91.
+The protein's natural variant, known as in VWM;, features a modification of the amino acid from L to F at position 106.
+The protein's natural variant, known as in VWM;, features a modification of the amino acid from R to C at position 113.
+The protein's natural variant, known as in VWM; with ovarian failure;, features a modification of the amino acid from R to H at position 113.
+The protein's natural variant, known as in VWM; with ovarian failure;, features a modification of the amino acid from R to C at position 195.
+The protein's natural variant, known as in VWM; Cree leukoencephalopathy type;, features a modification of the amino acid from R to H at position 195.
+The protein's natural variant, known as in VWM;, features a modification of the amino acid from R to G at position 269.
+The protein's natural variant, known as in VWM;, features a modification of the amino acid from R to Q at position 269.
+The protein's natural variant, known as in VWM;, features a modification of the amino acid from D to H at position 270.
+The protein's natural variant, known as in VWM;, features a modification of the amino acid from R to H at position 299.
+The protein's natural variant, known as in VWM;, features a modification of the amino acid from C to F at position 310.
+The protein's natural variant, known as in VWM;, features a modification of the amino acid from R to C at position 315.
+The protein's natural variant, known as in VWM;, features a modification of the amino acid from R to G at position 315.
+The protein's natural variant, known as in VWM;, features a modification of the amino acid from R to H at position 315.
+The protein's natural variant, known as in VWM;, features a modification of the amino acid from C to R at position 335.
+The protein's natural variant, known as in VWM, features a modification of the amino acid from C to S at position 335.
+The protein's natural variant, known as in VWM;, features a modification of the amino acid from R to P at position 339.
+The protein's natural variant, known as in VWM;, features a modification of the amino acid from R to Q at position 339.
+The protein's natural variant, known as in VWM;, features a modification of the amino acid from R to W at position 339.
+The protein's natural variant, known as in VWM, features a modification of the amino acid from N to D at position 376.
+The protein's natural variant, known as in VWM;, features a modification of the amino acid from G to V at position 386.
+The protein's natural variant, known as in VWM;, features a modification of the amino acid from V to A at position 430.
+The protein's natural variant, known as in VWM;, features a modification of the amino acid from S to L at position 447.
+The protein's natural variant, known as in VWM;, features a modification of the amino acid from W to R at position 628.
+The protein's natural variant, known as in VWM;, features a modification of the amino acid from E to K at position 650.
+The protein's natural variant, known as in strain: 0101.3, 0101.4, 0101.5, 0101.7, 0101.9, MSH22, MA28, MA32, MSH38, SP138, SP235 and SP295, features a modification of the amino acid from V to L at position 13.
+The protein's natural variant, known as in strain: 0101.3, 0101.4, 0101.5, 0101.7, 0101.9, MSH22, MA28, MA32, MSH38, SP138, SP235 and SP295, features a modification of the amino acid from P to Q at position 29.
+The protein's natural variant, known as in strain: 0101.3, 0101.4, 0101.5, 0101.7, 0101.9, MSH22, MA28, MA32, MSH38, SP138, SP235 and SP295, features a modification of the amino acid from V to I at position 47.
+The protein's natural variant, known as in strain: SP235, features a modification of the amino acid from F to Y at position 52.
+The protein's natural variant, known as in strain: 0101.5, features a modification of the amino acid from D to H at position 53.
+The protein's natural variant, known as in strain: MSH22, features a modification of the amino acid from L to F at position 56.
+The protein's natural variant, known as in strain: 0101.3, 0101.4, 0101.5, 0101.7, 0101.9, MSH22, MA28, MA32, MSH38, SP138, SP235 and SP295, features a modification of the amino acid from A to V at position 129.
+The natural variant of this protein is characterized by an amino acid alteration from V to L at position 62.
+The natural variant of this protein is characterized by an amino acid alteration from F to A at position 90.
+The natural variant of this protein is characterized by an amino acid alteration from F to L at position 136.
+The natural variant of this protein is characterized by an amino acid alteration from S to D at position 146.
+The natural variant of this protein is characterized by an amino acid alteration from KI to QT at position 173.
+The protein's natural variant, known as probable disease-associated variant found in a patient with apparently autosomal dominant severe congenital neutropenia; affects CSF3 mediated proliferation and survival of myeloid cells; abrogates receptor signaling by altering ligand binding; dominant negative effect;, features a modification of the amino acid from P to H at position 229.
+The protein's natural variant, known as in SCN7; decreases localization to plasma membrane; decreases receptor signaling;, features a modification of the amino acid from R to C at position 308.
+The protein's natural variant, known as in neutrophilia;, features a modification of the amino acid from T to N at position 640.
+The protein's natural variant, known as in strain: DBA/2, NZB and NZW, in vitro decreases nuclease activity against free DNA by approximately twofold and decreases activity to establish a barrier to liposomal gene transfection by eightfold, features a modification of the amino acid from T to I at position 89.
+The protein's natural variant, known as in strain: NMRI, features a modification of the amino acid from T to A at position 212.
+The protein's natural variant, known as in strain: NMRI, features a modification of the amino acid from Q to R at position 240.
+The protein's natural variant, known as in strain: NMRI; requires 2 nucleotide substitutions, features a modification of the amino acid from L to C at position 422.
+The protein's natural variant, known as in strain: NMRI, features a modification of the amino acid from G to V at position 485.
+The protein's natural variant, known as in strain: NMRI, features a modification of the amino acid from V to A at position 603.
+The protein's natural variant, known as in strain: NMRI, features a modification of the amino acid from V to I at position 675.
+The protein's natural variant, known as in strain: NMRI, features a modification of the amino acid from E to Q at position 925.
+The protein's natural variant, known as found in Vel-negative population; unknown pathological significance; heterozygous with the 17-nucleotide frameshift deletion;, features a modification of the amino acid from M to K at position 51.
+The protein's natural variant, known as found in Vel-negative population; unknown pathological significance; heterozygous with the 17-nucleotide frameshift deletion, features a modification of the amino acid from M to R at position 51.
+The protein's natural variant, known as in HLD10; severe decrease of protein amount; does not affect mitochondrial localization;, features a modification of the amino acid from R to C at position 119.
+The protein's natural variant, known as in HLD10; mild decrease of homodimerization; does not affect mitochondrial localization;, features a modification of the amino acid from R to C at position 251.
+The protein's natural variant, known as in strain: cv. Chi-1, features a modification of the amino acid from S to P at position 85.
+The protein's natural variant, known as in strain: cv. Bla-1, features a modification of the amino acid from M to T at position 93.
+The protein's natural variant, known as in strain: cv. Chi-1, features a modification of the amino acid from K to R at position 99.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from A to T at position 100.
+The protein's natural variant, known as in strain: cv. Jl-1, features a modification of the amino acid from M to V at position 120.
+The protein's natural variant, known as in strain: cv. Bla-1, features a modification of the amino acid from L to P at position 125.
+The protein's natural variant, known as in strain: cv. Jl-1, features a modification of the amino acid from S to G at position 166.
+The protein's natural variant, known as in strain: cv. Chi-1, features a modification of the amino acid from L to P at position 212.
+The protein's natural variant, known as in strain: cv. Co-1, features a modification of the amino acid from A to V at position 233.
+The protein's natural variant, known as in LGMDR27; unknown pathological significance, features a modification of the amino acid from C to S at position 74.
+The protein's natural variant, known as in LGMDR27; unknown pathological significance;, features a modification of the amino acid from T to A at position 95.
+The protein's natural variant, known as in LGMDR27; unknown pathological significance, features a modification of the amino acid from E to K at position 164.
+The protein's natural variant, known as in LGMDR27; unknown pathological significance, features a modification of the amino acid from A to D at position 243.
+The protein's natural variant, known as in LGMDR27; unknown pathological significance, features a modification of the amino acid from N to I at position 358.
+The protein's natural variant, known as in LGMDR27; unknown pathological significance;, features a modification of the amino acid from P to S at position 682.
+The protein's natural variant, known as in LGMDR27; unknown pathological significance, features a modification of the amino acid from R to C at position 712.
+The protein's natural variant, known as in LGMDR27; unknown pathological significance;, features a modification of the amino acid from R to C at position 825.
+The protein's natural variant, known as in LGMDR27;, features a modification of the amino acid from G to R at position 839.
+The protein's natural variant, known as in LGMDR27; unknown pathological significance, features a modification of the amino acid from F to S at position 977.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to C at position 41.
+The protein's natural variant, known as in an ovarian mucinous carcinoma sample; somatic mutation, features a modification of the amino acid from K to E at position 92.
+The natural variant of this protein is characterized by an amino acid alteration from A to S at position 261.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from V to M at position 155.
+The protein's natural variant, known as found in a patient with autosomal recessive osteopetrosis; unknown pathological significance; reduced chloride:bicarbonate antiporter activity; impaired dynamic organization of podosome in osteoclasts; failure to rescue impaired osteoclast differentiation when expressed in a Slc4a2-knockdown mouse macrophage cell line RAW 264.7, features a modification of the amino acid from A to T at position 186.
+The protein's natural variant, known as found in a patient with autosomal recessive osteopetrosis; unknown pathological significance; reduced chloride:bicarbonate antiporter activity; impaired dynamic organization of podosome in osteoclasts; failure to rescue impaired osteoclast differentiation when expressed in a Slc4a2-knockdown mouse macrophage cell line RAW 264.7, features a modification of the amino acid from V to A at position 553.
+The protein's natural variant, known as in plastocyanin A", features a modification of the amino acid from S to P at position 58.
+The protein's natural variant, known as in strain: G187, features a modification of the amino acid from T to I at position 11.
+The protein's natural variant, known as in strain: G136, features a modification of the amino acid from L to H at position 14.
+The protein's natural variant, known as in strain: G179, features a modification of the amino acid from S to F at position 18.
+The protein's natural variant, known as in strain: PAK12085 and SB33, features a modification of the amino acid from D to A at position 24.
+The protein's natural variant, known as in strain: TN106, features a modification of the amino acid from T to A at position 37.
+The protein's natural variant, known as in strain: PAK12085 and SB33, features a modification of the amino acid from T to V at position 37.
+The protein's natural variant, known as in strain: TN106, features a modification of the amino acid from E to A at position 59.
+The protein's natural variant, known as in strain: TN106, features a modification of the amino acid from Q to K at position 103.
+The protein's natural variant, known as in strain: TN106, features a modification of the amino acid from I to V at position 119.
+The protein's natural variant, known as in strain: TN106, features a modification of the amino acid from A to V at position 284.
+The protein's natural variant, known as in strain: TN106, features a modification of the amino acid from I to T at position 323.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from N to S at position 1059.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from TG to KD at position 1854.
+The protein's natural variant, known as in MASPD; found in a patient suffering from frequent infections and chronic inflammatory disease; strongly decreases affinity for MBL2 and FCN2;, features a modification of the amino acid from D to G at position 120.
+The protein's natural variant, known as in MASPD;, features a modification of the amino acid from P to L at position 126.
+The protein's natural variant, known as in MASPD, features a modification of the amino acid from C to CHNH at position 156.
+The protein's natural variant, known as associated with reduced MASP2 levels in plasma; no effect on catalytic activity;, features a modification of the amino acid from V to A at position 377.
+The protein's natural variant, known as in OCNDS;, features a modification of the amino acid from R to Q at position 47.
+The protein's natural variant, known as in OCNDS;, features a modification of the amino acid from Y to S at position 50.
+The protein's natural variant, known as in OCNDS;, features a modification of the amino acid from D to G at position 175.
+The protein's natural variant, known as in OCNDS;, features a modification of the amino acid from K to R at position 198.
+The protein's natural variant, known as in DFNA12, features a modification of the amino acid from D to N at position 197.
+The protein's natural variant, known as in DFNA12, features a modification of the amino acid from F to S at position 211.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from R to H at position 284.
+The protein's natural variant, known as in DFNA12, features a modification of the amino acid from V to E at position 317.
+The protein's natural variant, known as in DFNA12;, features a modification of the amino acid from S to C at position 362.
+The protein's natural variant, known as in DFNA12, features a modification of the amino acid from N to K at position 465.
+The protein's natural variant, known as in DFNA12;, features a modification of the amino acid from T to M at position 562.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from I to N at position 771.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from N to T at position 813.
+The protein's natural variant, known as in DFNA12;, features a modification of the amino acid from T to M at position 815.
+The protein's natural variant, known as in DFNA12;, features a modification of the amino acid from N to S at position 886.
+The protein's natural variant, known as in DFNA12;, features a modification of the amino acid from C to Y at position 1036.
+The protein's natural variant, known as in DFNA12; progressive deafness with late onset;, features a modification of the amino acid from C to S at position 1057.
+The protein's natural variant, known as in DFNA12;, features a modification of the amino acid from A to V at position 1098.
+The protein's natural variant, known as in DFNA12;, features a modification of the amino acid from D to H at position 1136.
+The protein's natural variant, known as in DFNA12;, features a modification of the amino acid from P to L at position 1248.
+The protein's natural variant, known as in DFNA12, features a modification of the amino acid from C to G at position 1509.
+The protein's natural variant, known as in DFNA12, features a modification of the amino acid from C to R at position 1517.
+The protein's natural variant, known as in DFNA12;, features a modification of the amino acid from C to S at position 1619.
+The protein's natural variant, known as in DFNA12;, features a modification of the amino acid from P to R at position 1791.
+The protein's natural variant, known as in DFNA12; prelingual and stable deafness;, features a modification of the amino acid from L to F at position 1820.
+The protein's natural variant, known as in DFNA12; prelingual and stable deafness;, features a modification of the amino acid from G to D at position 1824.
+The protein's natural variant, known as in DFNA12; postlingual and progressive;, features a modification of the amino acid from C to G at position 1837.
+The protein's natural variant, known as in DFNA12;, features a modification of the amino acid from C to R at position 1837.
+The protein's natural variant, known as in DFNA12;, features a modification of the amino acid from T to M at position 1866.
+The protein's natural variant, known as in DFNA12, features a modification of the amino acid from H to R at position 1867.
+The protein's natural variant, known as in DFNA12; prelingual and stable deafness;, features a modification of the amino acid from Y to C at position 1870.
+The protein's natural variant, known as in DFNA12;, features a modification of the amino acid from R to C at position 1890.
+The protein's natural variant, known as in DFNA12, features a modification of the amino acid from C to R at position 1898.
+The protein's natural variant, known as in DFNA12;, features a modification of the amino acid from R to C at position 1947.
+The protein's natural variant, known as in DFNA12, features a modification of the amino acid from I to T at position 2009.
+The protein's natural variant, known as in DFNA12; prelingual and stable deafness;, features a modification of the amino acid from R to H at position 2021.
+The natural variant of this protein is characterized by an amino acid alteration from S to T at position 2100.
+The protein's natural variant, known as in penicillin-resistant isolates, features a modification of the amino acid from H to Y at position 105.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from V to F at position 214.
+The protein's natural variant, known as in CMD1HH;, features a modification of the amino acid from R to W at position 71.
+The protein's natural variant, known as in MFM6; interferes with the differentiation of skeletal muscle cells; does not cause functional alterations in cardiomyocyte cells;, features a modification of the amino acid from P to L at position 209.
+The protein's natural variant, known as in CMD1HH; interferes with the assembly of Z-disks; increases stress-induced apoptosis;, features a modification of the amino acid from R to W at position 218.
+The protein's natural variant, known as no functional consequences;, features a modification of the amino acid from R to W at position 258.
+The protein's natural variant, known as in CMD1HH;, features a modification of the amino acid from E to K at position 455.
+The protein's natural variant, known as in CMD1HH; interferes with the assembly of Z-disks; increases stress-induced apoptosis;, features a modification of the amino acid from L to P at position 462.
+The protein's natural variant, known as in CMD1HH, features a modification of the amino acid from V to M at position 468.
+The protein's natural variant, known as in CMD1HH;, features a modification of the amino acid from R to H at position 477.
+The protein's natural variant, known as found in patients with melanomas; decreased protein phosphatase activity, leading to increased phosphorylation of STING1, features a modification of the amino acid from H to Y at position 55.
+The protein's natural variant, known as found in patients with melanomas; decreased protein phosphatase activity, leading to increased phosphorylation of STING1, features a modification of the amino acid from H to Y at position 114.
+The protein's natural variant, known as found in patients with melanomas; decreased protein phosphatase activity, leading to increased phosphorylation of STING1, features a modification of the amino acid from G to R at position 189.
+The protein's natural variant, known as in CDCBM4;, features a modification of the amino acid from Y to C at position 92.
+The protein's natural variant, known as in CDCBM4;, features a modification of the amino acid from T to P at position 331.
+The protein's natural variant, known as in CDCBM4; the chaperonin-dependent folding and hence the yield of monomeric gamma-tubulin is compromised;, features a modification of the amino acid from L to P at position 387.
+The protein's natural variant, known as in prostate cancer;, features a modification of the amino acid from R to H at position 199.
+The protein's natural variant, known as in prostate cancer;, features a modification of the amino acid from A to S at position 279.
+The natural variant of this protein is characterized by an amino acid alteration from C to G at position 289.
+The protein's natural variant, known as in prostate cancer;, features a modification of the amino acid from V to A at position 650.
+The protein's natural variant, known as in prostate cancer, features a modification of the amino acid from H to N at position 679.
+The protein's natural variant, known as in BDPLT22;, features a modification of the amino acid from R to C at position 745.
+The protein's natural variant, known as in prostate cancer;, features a modification of the amino acid from M to V at position 883.
+The protein's natural variant, known as in prostate cancer, features a modification of the amino acid from I to M at position 909.
+The protein's natural variant, known as in ALL; unknown pathological significance; somatic mutation, features a modification of the amino acid from K to R at position 2.
+The protein's natural variant, known as in ALL; unknown pathological significance; somatic mutation, features a modification of the amino acid from E to G at position 19.
+The protein's natural variant, known as in ALL; unknown pathological significance; somatic mutation;, features a modification of the amino acid from P to S at position 226.
+The protein's natural variant, known as in ALL; unknown pathological significance; somatic mutation;, features a modification of the amino acid from V to I at position 267.
+The protein's natural variant, known as in ALL; unknown pathological significance; somatic mutation, features a modification of the amino acid from S to P at position 470.
+The protein's natural variant, known as found in a patient with autism; unknown pathological significance;, features a modification of the amino acid from Y to C at position 488.
+The protein's natural variant, known as in ALL; unknown pathological significance; somatic mutation, features a modification of the amino acid from T to A at position 499.
+The protein's natural variant, known as in ALL; unknown pathological significance; somatic mutation;, features a modification of the amino acid from M to I at position 761.
+The protein's natural variant, known as in AML; unknown pathological significance; somatic mutation;, features a modification of the amino acid from S to N at position 800.
+The protein's natural variant, known as in ALL; unknown pathological significance; somatic mutation, features a modification of the amino acid from S to P at position 1076.
+The protein's natural variant, known as in ALL; unknown pathological significance; somatic mutation, features a modification of the amino acid from S to G at position 1093.
+The protein's natural variant, known as in ALL; unknown pathological significance; somatic mutation;, features a modification of the amino acid from T to A at position 1171.
+The protein's natural variant, known as in ALL; unknown pathological significance; somatic mutation, features a modification of the amino acid from D to G at position 1351.
+The protein's natural variant, known as in ALL; unknown pathological significance; somatic mutation, features a modification of the amino acid from G to E at position 1365.
+The protein's natural variant, known as in AML; unknown pathological significance; somatic mutation;, features a modification of the amino acid from D to G at position 1397.
+The protein's natural variant, known as in ALL; unknown pathological significance; somatic mutation, features a modification of the amino acid from D to N at position 1453.
+The protein's natural variant, known as in ALL; unknown pathological significance; somatic mutation, features a modification of the amino acid from D to N at position 1493.
+The protein's natural variant, known as in ALL; unknown pathological significance; somatic mutation, features a modification of the amino acid from L to P at position 1609.
+The protein's natural variant, known as in ALL; unknown pathological significance; somatic mutation, features a modification of the amino acid from K to Q at position 1654.
+The protein's natural variant, known as in ALL; unknown pathological significance; somatic mutation;, features a modification of the amino acid from T to M at position 1663.
+The protein's natural variant, known as in RCC; defects in recruitment of the MutS alpha complex, features a modification of the amino acid from N to D at position 1733.
+The protein's natural variant, known as in MRD70, features a modification of the amino acid from R to Q at position 1740.
+The protein's natural variant, known as in RAPAS, features a modification of the amino acid from R to W at position 1740.
+The protein's natural variant, known as in RCC; defects in recruitment of the MutS alpha complex, features a modification of the amino acid from S to P at position 1769.
+The protein's natural variant, known as in AML; unknown pathological significance; somatic mutation, features a modification of the amino acid from L to S at position 1804.
+The protein's natural variant, known as in LLS; unknown pathological significance;, features a modification of the amino acid from L to W at position 1815.
+The protein's natural variant, known as in ALL; unknown pathological significance; somatic mutation, features a modification of the amino acid from L to P at position 1821.
+The protein's natural variant, known as in ALL; unknown pathological significance; somatic mutation, features a modification of the amino acid from V to A at position 1915.
+The protein's natural variant, known as in ALL; unknown pathological significance; somatic mutation, features a modification of the amino acid from E to V at position 1920.
+The protein's natural variant, known as in AML; unknown pathological significance; somatic mutation, features a modification of the amino acid from R to W at position 2122.
+The protein's natural variant, known as in ALL; unknown pathological significance; somatic mutation, features a modification of the amino acid from T to A at position 2214.
+The protein's natural variant, known as in ALL; unknown pathological significance; somatic mutation, features a modification of the amino acid from P to S at position 2361.
+The protein's natural variant, known as in AML; Impairs interaction with hyperphosphorylated POLR2A; unknown pathological significance; somatic mutation, features a modification of the amino acid from F to L at position 2505.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from V to L at position 7.
+The protein's natural variant, known as in strain: cv. Lemont; increases copper transport activity, features a modification of the amino acid from V to A at position 914.
+The natural variant of this protein is characterized by an amino acid alteration from H to R at position 28.
+The protein's natural variant, known as in AOS3; shows decreased binding to the HES1 promoter compared to wild-type;, features a modification of the amino acid from E to G at position 63.
+The protein's natural variant, known as in AOS3; shows decreased binding to the HES1 promoter compared to wild-type;, features a modification of the amino acid from K to E at position 169.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to C at position 342.
+The natural variant of this protein is characterized by an amino acid alteration from E to A at position 1.
+The protein's natural variant, known as in strain: DSR 2, features a modification of the amino acid from I to T at position 25.
+The protein's natural variant, known as in strain: DSR 1, features a modification of the amino acid from T to A at position 208.
+The protein's natural variant, known as in strain: DSR 3, features a modification of the amino acid from F to L at position 286.
+The protein's natural variant, known as in strain: DSR 1, features a modification of the amino acid from N to S at position 358.
+The protein's natural variant, known as in strain: DSR 2, features a modification of the amino acid from I to T at position 483.
+The protein's natural variant, known as in strain: DSR 3, features a modification of the amino acid from A to T at position 617.
+The protein's natural variant, known as in XPV;, features a modification of the amino acid from R to P at position 93.
+The protein's natural variant, known as in XPV;, features a modification of the amino acid from R to H at position 111.
+The protein's natural variant, known as in XPV;, features a modification of the amino acid from T to P at position 122.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from G to D at position 153.
+The protein's natural variant, known as in XPV; impairs translesion synthesis;, features a modification of the amino acid from G to V at position 263.
+The protein's natural variant, known as in XPV, features a modification of the amino acid from V to D at position 266.
+The protein's natural variant, known as in XPV, features a modification of the amino acid from G to R at position 295.
+The protein's natural variant, known as in XPV, features a modification of the amino acid from R to S at position 361.
+The protein's natural variant, known as in XPV;, features a modification of the amino acid from K to E at position 535.
+The protein's natural variant, known as in XPV;, features a modification of the amino acid from K to T at position 589.
+The protein's natural variant, known as in XPV;, features a modification of the amino acid from T to A at position 692.
+The protein's natural variant, known as in strain: cv. H599, features a modification of the amino acid from L to I at position 92.
+The protein's natural variant, known as resistance to rhizoxin, features a modification of the amino acid from N to I at position 100.
+The protein's natural variant, known as in PXEL-MCFD;, features a modification of the amino acid from F to S at position 299.
+The protein's natural variant, known as in VKCFD1; affects glutamate binding;, features a modification of the amino acid from L to R at position 394.
+The protein's natural variant, known as in PXEL-MCFD;, features a modification of the amino acid from R to C at position 476.
+The protein's natural variant, known as in PXEL-MCFD;, features a modification of the amino acid from R to H at position 476.
+The protein's natural variant, known as in VKCFD1;, features a modification of the amino acid from R to P at position 485.
+The protein's natural variant, known as in PXEL-MCFD;, features a modification of the amino acid from W to S at position 493.
+The protein's natural variant, known as in VKCFD1;, features a modification of the amino acid from W to S at position 501.
+The protein's natural variant, known as in PXEL-MCFD;, features a modification of the amino acid from G to R at position 558.
+The protein's natural variant, known as in strain: CLBrenner, features a modification of the amino acid from G to S at position 160.
+The protein's natural variant, known as in strain: Colombiana, features a modification of the amino acid from N to D at position 192.
+The protein's natural variant, known as in strain: Colombiana, features a modification of the amino acid from K to R at position 196.
+The protein's natural variant, known as in shaking pup, features a modification of the amino acid from H to P at position 37.
+The protein's natural variant, known as in CDLS5;, features a modification of the amino acid from H to R at position 180.
+The protein's natural variant, known as in CDLS5;, features a modification of the amino acid from T to M at position 311.
+The protein's natural variant, known as in CDLS5;, features a modification of the amino acid from G to R at position 320.
+The protein's natural variant, known as in CDLS5;, features a modification of the amino acid from H to R at position 334.
+The protein's natural variant, known as in 50% of the molecules, features a modification of the amino acid from W to R at position 257.
+The protein's natural variant, known as in GPIBD15; results in low amounts of GPI-anchored proteins on cell surface;, features a modification of the amino acid from S to L at position 51.
+The protein's natural variant, known as in GPIBD15; unknown pathological significance; requires 2 nucleotide substitutions;, features a modification of the amino acid from A to N at position 54.
+The protein's natural variant, known as in GPIBD15; results in low amounts of GPI-anchored proteins on cell surface;, features a modification of the amino acid from W to S at position 176.
+The protein's natural variant, known as in GPIBD15;, features a modification of the amino acid from L to P at position 290.
+The protein's natural variant, known as in GPIBD15; results in low amounts of GPI-anchored proteins on cell surface;, features a modification of the amino acid from L to P at position 291.
+The protein's natural variant, known as in GPIBD15;, features a modification of the amino acid from A to P at position 389.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from E to G at position 26.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from S to R at position 39.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from N to D at position 79.
+The natural variant of this protein is characterized by an amino acid alteration from R to H at position 94.
+The protein's natural variant, known as in allele ALDH4A1*4;, features a modification of the amino acid from P to L at position 16.
+The protein's natural variant, known as in HYRPRO2; allele ALDH4A1*3; loss of enzyme activity;, features a modification of the amino acid from S to L at position 352.
+The protein's natural variant, known as in strain: NCTC 12882, features a modification of the amino acid from V to I at position 32.
+The protein's natural variant, known as in strain: NCTC 12882, features a modification of the amino acid from S to T at position 120.
+The natural variant of this protein is characterized by an amino acid alteration from F to V at position 324.
+The protein's natural variant, known as in CORD21;, features a modification of the amino acid from Y to H at position 27.
+The protein's natural variant, known as in CORD21;, features a modification of the amino acid from S to N at position 44.
+The protein's natural variant, known as in CORD21;, features a modification of the amino acid from H to L at position 121.
+The protein's natural variant, known as in strain: Isolate A-0V-2-A and Isolate A-0V-3-A, features a modification of the amino acid from V to M at position 60.
+The protein's natural variant, known as in strain: Isolate A-0V-3-A, features a modification of the amino acid from V to M at position 98.
+The protein's natural variant, known as in strain: Isolate A-0V-2-A, features a modification of the amino acid from Y to H at position 109.
+The protein's natural variant, known as found in patients with large intestine cancer; abolished methyltransferase activity, features a modification of the amino acid from G to C at position 110.
+The protein's natural variant, known as in GA2B; decreased protein stability;, features a modification of the amino acid from D to N at position 128.
+The protein's natural variant, known as in GA2B; reduced electron transfer activity;, features a modification of the amino acid from R to Q at position 164.
+The protein's natural variant, known as in AUNB1;, features a modification of the amino acid from Q to H at position 255.
+The protein's natural variant, known as in DFNB9;, features a modification of the amino acid from P to Q at position 490.
+The protein's natural variant, known as in DFNB9 and AUNB1; temperature sensitive AUNB1 phenotype with severe hearing loss during febrile illness;, features a modification of the amino acid from I to T at position 515.
+The natural variant of this protein is characterized by an amino acid alteration from R to S at position 773.
+The protein's natural variant, known as in DFNB9;, features a modification of the amino acid from R to H at position 794.
+The protein's natural variant, known as in AUNB1;, features a modification of the amino acid from A to E at position 964.
+The protein's natural variant, known as in AUNB1 and DFNB9;, features a modification of the amino acid from L to P at position 1011.
+The protein's natural variant, known as in AUNB1;, features a modification of the amino acid from L to P at position 1138.
+The protein's natural variant, known as in DFNB9;, features a modification of the amino acid from R to Q at position 1157.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from E to K at position 1323.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from I to V at position 1547.
+The natural variant of this protein is characterized by an amino acid alteration from T to K at position 1688.
+The protein's natural variant, known as in AUNB1;, features a modification of the amino acid from F to C at position 1795.
+The protein's natural variant, known as in DFNB9;, features a modification of the amino acid from P to A at position 1825.
+The protein's natural variant, known as in AUNB1;, features a modification of the amino acid from R to Q at position 1939.
+The protein's natural variant, known as in AUNB1;, features a modification of the amino acid from P to R at position 1987.
+The natural variant of this protein is characterized by an amino acid alteration from K to Q at position 34.
+The natural variant of this protein is characterized by an amino acid alteration from F to L at position 91.
+The natural variant of this protein is characterized by an amino acid alteration from E to K at position 178.
+The natural variant of this protein is characterized by an amino acid alteration from N to H at position 273.
+The natural variant of this protein is characterized by an amino acid alteration from G to K at position 275.
+The protein's natural variant, known as in MPS1S;, features a modification of the amino acid from L to P at position 18.
+The protein's natural variant, known as in MPS1H;, features a modification of the amino acid from G to D at position 51.
+The protein's natural variant, known as in MPS1H;, features a modification of the amino acid from A to T at position 75.
+The protein's natural variant, known as in MPS1S;, features a modification of the amino acid from Y to C at position 76.
+The protein's natural variant, known as in MPS1H/S; reduction of activity and protein levels;, features a modification of the amino acid from A to V at position 79.
+The protein's natural variant, known as in MPS1H/S;, features a modification of the amino acid from H to P at position 82.
+The protein's natural variant, known as reduction of protein levels;, features a modification of the amino acid from H to Q at position 82.
+The protein's natural variant, known as in MPS1H/S, features a modification of the amino acid from G to R at position 84.
+The protein's natural variant, known as in MPS1S;, features a modification of the amino acid from R to Q at position 89.
+The protein's natural variant, known as in MPS1S;, features a modification of the amino acid from R to W at position 89.
+The protein's natural variant, known as in MPS1H; uncertain pathological role, features a modification of the amino acid from T to P at position 103.
+The protein's natural variant, known as in MPS1H;, features a modification of the amino acid from M to I at position 133.
+The protein's natural variant, known as in MPS1H/S;, features a modification of the amino acid from E to K at position 178.
+The protein's natural variant, known as in MPS1H;, features a modification of the amino acid from E to K at position 182.
+The protein's natural variant, known as in MPS1H/S; associated with R-423, features a modification of the amino acid from F to L at position 188.
+The protein's natural variant, known as in MPS1H;, features a modification of the amino acid from G to D at position 208.
+The protein's natural variant, known as in MPS1H;, features a modification of the amino acid from L to P at position 218.
+The protein's natural variant, known as in MPS1S;, features a modification of the amino acid from G to E at position 219.
+The protein's natural variant, known as in MPS1H/S;, features a modification of the amino acid from L to Q at position 238.
+The protein's natural variant, known as in MPS1H/S, features a modification of the amino acid from S to F at position 260.
+The protein's natural variant, known as in MPS1H/S;, features a modification of the amino acid from G to R at position 265.
+The protein's natural variant, known as in MPS1H/S and MPS1S, features a modification of the amino acid from E to K at position 276.
+The natural variant of this protein is characterized by an amino acid alteration from V to A at position 279.
+The protein's natural variant, known as in IDUA pseudodeficiency;, features a modification of the amino acid from A to T at position 300.
+The protein's natural variant, known as in MPS1S, features a modification of the amino acid from W to L at position 306.
+The protein's natural variant, known as in MPS1H; loss of function; undetectable enzyme activity, features a modification of the amino acid from D to Y at position 315.
+The protein's natural variant, known as in MPS1H; MPS1H/S;, features a modification of the amino acid from A to P at position 327.
+The protein's natural variant, known as in MPS1H/S; 0.4% of normal activity;, features a modification of the amino acid from L to R at position 346.
+The protein's natural variant, known as in MPS1S;, features a modification of the amino acid from N to K at position 348.
+The protein's natural variant, known as in MPS1H;, features a modification of the amino acid from D to N at position 349.
+The protein's natural variant, known as in MPS1H, features a modification of the amino acid from D to Y at position 349.
+The protein's natural variant, known as in MPS1S, features a modification of the amino acid from N to I at position 350.
+The protein's natural variant, known as in MPS1H/S; loss of activity;, features a modification of the amino acid from R to C at position 363.
+The protein's natural variant, known as in MPS1H;, features a modification of the amino acid from T to P at position 366.
+The protein's natural variant, known as in MPS1H/S and MPS1S;, features a modification of the amino acid from Q to R at position 380.
+The protein's natural variant, known as in MPS1S; 2-3% of normal activity;, features a modification of the amino acid from R to H at position 383.
+The protein's natural variant, known as in MPS1H;, features a modification of the amino acid from P to R at position 385.
+The protein's natural variant, known as in MPS1H;, features a modification of the amino acid from T to R at position 388.
+The protein's natural variant, known as in MPS1H, features a modification of the amino acid from L to LALL at position 396.
+The protein's natural variant, known as in MPS1H/S, features a modification of the amino acid from L to P at position 396.
+The protein's natural variant, known as in MPS1H;, features a modification of the amino acid from G to R at position 409.
+The protein's natural variant, known as in MPS1S and MPS1H/S; associated with L-188 in a patient with MPS1H/S; significant reduction of activity and protein levels;, features a modification of the amino acid from S to R at position 423.
+The protein's natural variant, known as in MPS1H/S, features a modification of the amino acid from A to P at position 436.
+The protein's natural variant, known as in MPS1H, features a modification of the amino acid from R to P at position 489.
+The protein's natural variant, known as in MPS1H/S and MPS1S;, features a modification of the amino acid from L to P at position 490.
+The protein's natural variant, known as in MPS1S;, features a modification of the amino acid from R to P at position 492.
+The protein's natural variant, known as in MPS1H/S;, features a modification of the amino acid from P to L at position 496.
+The protein's natural variant, known as in MPS1H/S;, features a modification of the amino acid from P to R at position 496.
+The protein's natural variant, known as in MPS1H/S, features a modification of the amino acid from M to T at position 504.
+The protein's natural variant, known as in MPS1H and MPS1H/S; in 3% of the MPS1H patients; reduces catalytic activity and protein stability;, features a modification of the amino acid from P to R at position 533.
+The protein's natural variant, known as in MPS1H/S, features a modification of the amino acid from L to F at position 535.
+The protein's natural variant, known as in MPS1H/S; reduction of activity and protein levels, features a modification of the amino acid from F to I at position 602.
+The protein's natural variant, known as in MPS1H/S; 1.5% of normal activity;, features a modification of the amino acid from R to G at position 619.
+The protein's natural variant, known as in MPS1H; loss of function; undetectable enzyme activity, features a modification of the amino acid from V to F at position 620.
+The protein's natural variant, known as in MPS1H/S;, features a modification of the amino acid from W to R at position 626.
+The protein's natural variant, known as in MPS1H/S;, features a modification of the amino acid from R to P at position 628.
+The protein's natural variant, known as in plasmid pCP301, features a modification of the amino acid from R to K at position 17.
+The protein's natural variant, known as in PERRS;, features a modification of the amino acid from W to R at position 299.
+The protein's natural variant, known as in strain: 137c and CC-503, features a modification of the amino acid from L to P at position 46.
+The protein's natural variant, known as in strain: Czech II, features a modification of the amino acid from L to P at position 203.
+The protein's natural variant, known as in strain: Czech II, features a modification of the amino acid from A to V at position 642.
+The protein's natural variant, known as in Don Q cell line; low level of activity, features a modification of the amino acid from G to D at position 116.
+The protein's natural variant, known as in SG14 mutant; lower apparent affinities for substrates, fructose-1,6-bisphosphate and AMP, features a modification of the amino acid from A to T at position 44.
+The protein's natural variant, known as in CL1136 mutant; less dependent on the allosteric activator, fructose-1,6-bisphosphate, for activity and less sensitive to inhibition by AMP, features a modification of the amino acid from R to C at position 67.
+The protein's natural variant, known as in SG5 mutant, features a modification of the amino acid from P to S at position 295.
+The protein's natural variant, known as in 618 mutant; causes lowered affinity for AMP, features a modification of the amino acid from G to D at position 336.
+The protein's natural variant, known as found in patients with cancer; loss of auto-inhibition, leading to constitutive ATP-dependent chromatin remodeler activity, features a modification of the amino acid from R to H at position 842.
+The protein's natural variant, known as found in patients with cancer; loss of auto-inhibition, leading to constitutive ATP-dependent chromatin remodeler activity;, features a modification of the amino acid from W to C at position 852.
+The protein's natural variant, known as found in patients with cancer; loss of auto-inhibition, leading to constitutive ATP-dependent chromatin remodeler activity;, features a modification of the amino acid from R to Q at position 857.
+The protein's natural variant, known as found in patients with cancer; loss of auto-inhibition, leading to constitutive ATP-dependent chromatin remodeler activity;, features a modification of the amino acid from R to W at position 860.
+The protein's natural variant, known as in LGMDD2;, features a modification of the amino acid from R to P at position 818.
+The protein's natural variant, known as in LGMDD2, features a modification of the amino acid from RLFR to GCFDSSHSCTVPVTQECLF at position 923.
+The protein's natural variant, known as in LGMDD2, features a modification of the amino acid from R to DSSHSCTVPVTQECLF at position 923.
+The protein's natural variant, known as in LGMDD2; induces relocalization to nuclear periphery; impaired ability to transport target proteins into the nucleus; induces resistance to HIV-1 infection;, features a modification of the amino acid from R to RCSHSCTVPVTQECLF at position 923.
+The natural variant of this protein is characterized by an amino acid alteration from V to E at position 257.
+The protein's natural variant, known as in NEDMISS; unable to rescue intra-Golgi vesicle-mediated transport defects in gene-null cells, features a modification of the amino acid from P to L at position 929.
+The protein's natural variant, known as in HYPT7 and ARWH2;, features a modification of the amino acid from W to R at position 108.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from D to N at position 445.
+The natural variant of this protein is characterized by an amino acid alteration from Y to C at position 21.
+The protein's natural variant, known as in CMH25;, features a modification of the amino acid from R to W at position 70.
+The protein's natural variant, known as found in a patient with dilated cardiomyopathy; unknown pathological significance;, features a modification of the amino acid from R to Q at position 87.
+The protein's natural variant, known as in CMH25; unknown pathological significance;, features a modification of the amino acid from P to L at position 90.
+The protein's natural variant, known as probable disease-associated variant found in a patient with dilated cardiomyopathy; impairs the interaction with CSRP3, TTN and MYOZ2;, features a modification of the amino acid from E to Q at position 132.
+The protein's natural variant, known as in CMH25; increased interaction with TTN and MYOZ2;, features a modification of the amino acid from T to I at position 137.
+The protein's natural variant, known as in CMH25;, features a modification of the amino acid from R to H at position 153.
+The protein's natural variant, known as in strain: Vedros M1801, features a modification of the amino acid from R to G at position 32.
+The protein's natural variant, known as in strain: Vedros M1801, features a modification of the amino acid from Y to F at position 48.
+The protein's natural variant, known as in strain: Vedros M1801, features a modification of the amino acid from G to D at position 97.
+The protein's natural variant, known as in strain: Vedros M1801, features a modification of the amino acid from T to V at position 103.
+The protein's natural variant, known as in strain: Vedros M1801, features a modification of the amino acid from G to A at position 123.
+The protein's natural variant, known as in strain: Vedros M1801, features a modification of the amino acid from T to S at position 137.
+The protein's natural variant, known as in strain: Vedros M1801, features a modification of the amino acid from VARAR to IETVQ at position 149.
+The protein's natural variant, known as in strain: Vedros M1801, features a modification of the amino acid from E to K at position 153.
+The protein's natural variant, known as in strain: Vedros M1801, features a modification of the amino acid from K to R at position 158.
+The protein's natural variant, known as in strain: Vedros M1801, features a modification of the amino acid from E to Q at position 166.
+The protein's natural variant, known as in strain: Vedros M1801, features a modification of the amino acid from VSG to AAE at position 211.
+The protein's natural variant, known as in ECTD9; unknown pathological significance;, features a modification of the amino acid from Q to R at position 271.
+The protein's natural variant, known as in strain: HW00, HW09, NC37, NC48, TT00 and TT01, features a modification of the amino acid from L to I at position 28.
+The protein's natural variant, known as in strain: HW00, HW09, NC37, NC48, TT00 and TT01, features a modification of the amino acid from L to M at position 115.
+The protein's natural variant, known as in strain: C167, features a modification of the amino acid from I to F at position 119.
+The protein's natural variant, known as in strain: HW00, HW09, NC37, NC48, TT00 and TT01, features a modification of the amino acid from I to V at position 137.
+The protein's natural variant, known as in strain: HW09, features a modification of the amino acid from V to I at position 187.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 295.
+The protein's natural variant, known as in strain: IL1403, features a modification of the amino acid from A to V at position 145.
+The protein's natural variant, known as in strain: IL1403, features a modification of the amino acid from H to N at position 159.
+The protein's natural variant, known as in strain: IL1403, features a modification of the amino acid from S to A at position 188.
+The natural variant of this protein is characterized by an amino acid alteration from N to D at position 209.
+The protein's natural variant, known as in ATS2;, features a modification of the amino acid from G to E at position 297.
+The protein's natural variant, known as in ATS2;, features a modification of the amino acid from G to R at position 407.
+The protein's natural variant, known as in ATS2;, features a modification of the amino acid from G to D at position 532.
+The protein's natural variant, known as in ATS2; unknown pathological significance;, features a modification of the amino acid from G to V at position 631.
+The protein's natural variant, known as in ATS2;, features a modification of the amino acid from G to R at position 640.
+The protein's natural variant, known as in ATS2;, features a modification of the amino acid from G to R at position 739.
+The protein's natural variant, known as in ATS2;, features a modification of the amino acid from G to R at position 853.
+The protein's natural variant, known as in BFH;, features a modification of the amino acid from G to V at position 985.
+The protein's natural variant, known as in BFH;, features a modification of the amino acid from G to E at position 1015.
+The protein's natural variant, known as in ATS3; in isolated microhematuria at heterozygosity;, features a modification of the amino acid from G to R at position 1167.
+The protein's natural variant, known as in ATS2; in isolated microhematuria at heterozygosity;, features a modification of the amino acid from G to E at position 1207.
+The protein's natural variant, known as in ATS2; unknown pathological significance;, features a modification of the amino acid from R to Q at position 1215.
+The protein's natural variant, known as in ATS2, features a modification of the amino acid from G to R at position 1216.
+The protein's natural variant, known as in ATS2;, features a modification of the amino acid from G to S at position 1277.
+The protein's natural variant, known as in ATS2; unknown pathological significance;, features a modification of the amino acid from I to T at position 1330.
+The protein's natural variant, known as in ATS2;, features a modification of the amino acid from G to E at position 1334.
+The protein's natural variant, known as in ATS2; unknown pathological significance;, features a modification of the amino acid from D to E at position 1347.
+The protein's natural variant, known as in ATS2; unknown pathological significance;, features a modification of the amino acid from R to C at position 1661.
+The protein's natural variant, known as in IMD63;, features a modification of the amino acid from L to P at position 77.
+The protein's natural variant, known as rare variant; unknown pathological significance; decreased down-regulation of angiotensin-activated signaling pathway; decreased RGS2 protein abundance;, features a modification of the amino acid from Q to L at position 2.
+The protein's natural variant, known as likely benign variant; no effect on down-regulation of angiotensin-activated signaling pathway;, features a modification of the amino acid from Q to R at position 2.
+The protein's natural variant, known as likely benign variant; no effect on down-regulation of angiotensin-activated signaling pathway;, features a modification of the amino acid from S to G at position 3.
+The protein's natural variant, known as likely benign variant; no effect on down-regulation of angiotensin-activated signaling pathway;, features a modification of the amino acid from A to V at position 4.
+The protein's natural variant, known as likely benign variant; no effect on down-regulation of angiotensin-activated signaling pathway;, features a modification of the amino acid from M to V at position 5.
+The protein's natural variant, known as likely benign variant; no effect on down-regulation of angiotensin-activated signaling pathway;, features a modification of the amino acid from K to N at position 18.
+The protein's natural variant, known as likely benign variant; no effect on down-regulation of angiotensin-activated signaling pathway;, features a modification of the amino acid from G to D at position 23.
+The protein's natural variant, known as unknown pathological significance; decreased down-regulation of angiotensin-activated signaling pathway; reduced localization at the cell membrane;, features a modification of the amino acid from D to Y at position 40.
+The protein's natural variant, known as unknown pathological significance; decreased down-regulation of angiotensin-activated signaling pathway; reduced localization at the cell membrane;, features a modification of the amino acid from R to H at position 44.
+The protein's natural variant, known as likely benign variant; no effect on down-regulation of angiotensin-activated signaling pathway;, features a modification of the amino acid from Q to K at position 50.
+The protein's natural variant, known as likely benign variant; no effect on down-regulation of angiotensin-activated signaling pathway;, features a modification of the amino acid from P to L at position 55.
+The protein's natural variant, known as likely benign variant; no effect on down-regulation of angiotensin-activated signaling pathway, features a modification of the amino acid from Q to H at position 78.
+The protein's natural variant, known as likely benign variant; no effect on down-regulation of angiotensin-activated signaling pathway;, features a modification of the amino acid from A to G at position 99.
+The protein's natural variant, known as likely benign variant; no effect on down-regulation of angiotensin-activated signaling pathway;, features a modification of the amino acid from I to V at position 110.
+The protein's natural variant, known as rare variant; unknown pathological significance; decreased down-regulation of angiotensin-activated signaling pathway; reduced interaction with GNAQ;, features a modification of the amino acid from R to H at position 188.
+The protein's natural variant, known as likely benign variant; no effect on down-regulation of angiotensin-activated signaling pathway;, features a modification of the amino acid from Q to R at position 196.
+The natural variant of this protein is characterized by an amino acid alteration from I to L at position 161.
+The protein's natural variant, known as probable disease-associated variant found in a patient with congenital heart defect; significant loss of interaction with HDAC1; fails to rescue the abnormal cardiac phenotypes defects in zebrafish morphants;, features a modification of the amino acid from G to D at position 345.
+The protein's natural variant, known as found in a patient with congenital heart defect;, features a modification of the amino acid from R to Q at position 579.
+The protein's natural variant, known as found in a renal cell carcinoma sample; somatic mutation, features a modification of the amino acid from A to P at position 601.
+The protein's natural variant, known as in SNIBFIS; no effect on nuclear location; decreased transcriptional activation function; no effect on homodimerization, features a modification of the amino acid from R to L at position 362.
+The protein's natural variant, known as in SNIBFIS; no effect on nuclear location; no effect on transcriptional activation function; no effect on homodimerization, features a modification of the amino acid from R to G at position 407.
+The protein's natural variant, known as in SNIBFIS; no effect on nuclear location; increased transcriptional activation function; no effect on homodimerization, features a modification of the amino acid from R to L at position 407.
+The protein's natural variant, known as in SNIBFIS; no effect on nuclear location; decreased transcriptional activation function; slightly decreased homodimerization, features a modification of the amino acid from N to S at position 456.
+The protein's natural variant, known as in HPANBH4; decreased protein levels in patient cells;, features a modification of the amino acid from R to P at position 72.
+The protein's natural variant, known as in SCA26; compromises the mechanics of translocation;, features a modification of the amino acid from P to H at position 596.
+The protein's natural variant, known as in SPG31; impairs normal ER-targeting, features a modification of the amino acid from P to L at position 19.
+The protein's natural variant, known as in SPG31; impairs normal ER-targeting;, features a modification of the amino acid from P to R at position 19.
+The protein's natural variant, known as in SPG31; loss of function mutation; shows severely altered localization to numerous punctate small structures throughout the cytoplasm; does not localize to the endoplasmic reticulum; impairs normal ER targeting;, features a modification of the amino acid from A to E at position 20.
+The protein's natural variant, known as in SPG31; impairs normal ER-targeting, features a modification of the amino acid from S to F at position 23.
+The protein's natural variant, known as in SPG31 and DSMA6; impairs normal ER-targeting, features a modification of the amino acid from W to R at position 42.
+The protein's natural variant, known as in SPG31; unknown pathological significance; does not impair normal ER-targeting;, features a modification of the amino acid from T to K at position 55.
+The protein's natural variant, known as in SPG31; unknown pathological significance; does not impair normal ER-targeting;, features a modification of the amino acid from D to N at position 56.
+The protein's natural variant, known as in SPG31, features a modification of the amino acid from L to P at position 107.
+The protein's natural variant, known as in HINCONS; decreased GTPase activity; decreased RALA effector binding, features a modification of the amino acid from V to L at position 25.
+The protein's natural variant, known as in HINCONS; decreased GTPase activity; decreased RALA effector binding;, features a modification of the amino acid from V to M at position 25.
+The protein's natural variant, known as in HINCONS, features a modification of the amino acid from K to R at position 128.
+The protein's natural variant, known as in HINCONS; decreased GTPase activity; decreased RALA effector binding, features a modification of the amino acid from D to G at position 130.
+The protein's natural variant, known as in HINCONS; decreased GTPase activity; increased RALA effector binding, features a modification of the amino acid from S to A at position 157.
+The protein's natural variant, known as in variant 2, features a modification of the amino acid from NFTLPA to T at position 592.
+The protein's natural variant, known as in AM; Galloway cattle, features a modification of the amino acid from R to H at position 221.
+The protein's natural variant, known as in AM; Angus cattle, features a modification of the amino acid from F to L at position 321.
+The protein's natural variant, known as found in a patient with features of hypogonadotropic hypogonadism and Kabuki syndrome also carrying a KMT2D variant; unknown pathological significance; reduced transactivation activity on KISS1 promoter; requires 2 nucleotide substitutions, features a modification of the amino acid from A to L at position 9.
+The protein's natural variant, known as in HH27; the patient also carries KISS1 and PROKR2 variants; unknown pathological significance, features a modification of the amino acid from V to M at position 31.
+The protein's natural variant, known as in HH27; unknown pathological significance; severely reduced binding to MC4R promoter; reduced transactivation activity on KISS1 promoter, features a modification of the amino acid from R to C at position 79.
+The protein's natural variant, known as in strain: IS58, features a modification of the amino acid from A to S at position 14.
+The protein's natural variant, known as associated with altered expression of E antigen, features a modification of the amino acid from W to C at position 16.
+The protein's natural variant, known as in C(X)/Rh9 antigen;, features a modification of the amino acid from A to T at position 36.
+The protein's natural variant, known as in C(W)/Rh8 antigen;, features a modification of the amino acid from Q to R at position 41.
+The protein's natural variant, known as in C/Rh2 antigen;, features a modification of the amino acid from P to S at position 103.
+The protein's natural variant, known as found in antigen RhEKH, features a modification of the amino acid from R to T at position 154.
+The protein's natural variant, known as in E/Rh5 antigen;, features a modification of the amino acid from P to A at position 226.
+The protein's natural variant, known as found in antigen RhEFM;, features a modification of the amino acid from Q to E at position 233.
+The protein's natural variant, known as found in antigen RhEFM;, features a modification of the amino acid from M to V at position 238.
+The protein's natural variant, known as in VS antigen;, features a modification of the amino acid from L to V at position 245.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from A to V at position 92.
+The natural variant of this protein is characterized by an amino acid alteration from L to F at position 164.
+The protein's natural variant, known as in DFNA85; unknown pathological significance; decreased deubiquitinase activity, features a modification of the amino acid from G to R at position 406.
+The protein's natural variant, known as in DFNA85; unknown pathological significance; requires 2 nucleotide substitutions; decreased deubiquitinase activity, features a modification of the amino acid from T to L at position 739.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from N to D at position 91.
+The protein's natural variant, known as in CGD4;, features a modification of the amino acid from G to R at position 24.
+The protein's natural variant, known as in CGD4;, features a modification of the amino acid from G to D at position 25.
+The protein's natural variant, known as in CGD4;, features a modification of the amino acid from G to V at position 25.
+The protein's natural variant, known as in CGD4;, features a modification of the amino acid from L to P at position 52.
+The protein's natural variant, known as in CGD4;, features a modification of the amino acid from E to V at position 53.
+The protein's natural variant, known as in CGD4;, features a modification of the amino acid from R to Q at position 90.
+The protein's natural variant, known as in CGD4;, features a modification of the amino acid from R to W at position 90.
+The protein's natural variant, known as in CGD4;, features a modification of the amino acid from H to R at position 94.
+The protein's natural variant, known as in CGD4;, features a modification of the amino acid from S to R at position 118.
+The protein's natural variant, known as in CGD4;, features a modification of the amino acid from A to V at position 124.
+The protein's natural variant, known as in CGD4;, features a modification of the amino acid from A to T at position 125.
+The protein's natural variant, known as in CGD4;, features a modification of the amino acid from P to Q at position 156.
+The protein's natural variant, known as in strain: 5E78-1, features a modification of the amino acid from T to A at position 13.
+The protein's natural variant, known as in strain: 5E78-1, features a modification of the amino acid from V to A at position 23.
+The protein's natural variant, known as in strain: 5E78-1, features a modification of the amino acid from NT to DN at position 31.
+The protein's natural variant, known as in strain: 5E78-1, features a modification of the amino acid from S to N at position 40.
+The protein's natural variant, known as in strain: 5E78-1, features a modification of the amino acid from E to K at position 58.
+The protein's natural variant, known as in strain: 5E78-1, features a modification of the amino acid from E to A at position 88.
+The protein's natural variant, known as in strain: 5E78-1, features a modification of the amino acid from V to T at position 119.
+The protein's natural variant, known as in strain: 5E78-1, features a modification of the amino acid from S to T at position 123.
+The protein's natural variant, known as in strain: 5E78-1, features a modification of the amino acid from Q to E at position 126.
+The protein's natural variant, known as in strain: 5E78-1, features a modification of the amino acid from H to N at position 224.
+The protein's natural variant, known as in strain: 5E78-1, features a modification of the amino acid from I to V at position 235.
+The protein's natural variant, known as in strain: 5E78-1, features a modification of the amino acid from K to E at position 257.
+The protein's natural variant, known as in strain: 5E78-1, features a modification of the amino acid from V to A at position 283.
+The protein's natural variant, known as in strain: 5E78-1, features a modification of the amino acid from T to A at position 286.
+The protein's natural variant, known as in BCARD; generates a new glycosylation site; decreases protein stability; strongly decreases lysyl hydroxylase activity and nearly abolishes glycosyltransferase activity;, features a modification of the amino acid from N to S at position 223.
+The protein's natural variant, known as increases cell surface expression;, features a modification of the amino acid from C to Y at position 529.
+The protein's natural variant, known as in allele W3, features a modification of the amino acid from V to I at position 8.
+The protein's natural variant, known as in allele W4, features a modification of the amino acid from H to Q at position 54.
+The protein's natural variant, known as in allele W3, features a modification of the amino acid from K to E at position 64.
+The protein's natural variant, known as in allele W2, features a modification of the amino acid from R to T at position 101.
+The protein's natural variant, known as in allele A, features a modification of the amino acid from A to D at position 105.
+The protein's natural variant, known as in allele W2, W4 and W5, features a modification of the amino acid from A to V at position 105.
+The protein's natural variant, known as in strain: AP213, features a modification of the amino acid from E to D at position 35.
+The protein's natural variant, known as in strain: AP213, features a modification of the amino acid from G to D at position 40.
+The protein's natural variant, known as in strain: AP213, features a modification of the amino acid from I to V at position 199.
+The protein's natural variant, known as in strain: AP213, features a modification of the amino acid from F to Y at position 218.
+The protein's natural variant, known as in strain: AP213, features a modification of the amino acid from D to E at position 250.
+The protein's natural variant, known as in strain: AP213, features a modification of the amino acid from I to V at position 319.
+The protein's natural variant, known as in strain: AP213, features a modification of the amino acid from G to V at position 373.
+The protein's natural variant, known as in strain: AP213, features a modification of the amino acid from P to S at position 523.
+The protein's natural variant, known as in CORD7;, features a modification of the amino acid from R to H at position 820.
+The protein's natural variant, known as may increase breast cancer risk, features a modification of the amino acid from R to W at position 275.
+The protein's natural variant, known as in DFNB99;, features a modification of the amino acid from R to Q at position 510.
+The protein's natural variant, known as found in a patient with congenital central hypoventilation syndrome; unknown pathological significance;, features a modification of the amino acid from T to I at position 2.
+The protein's natural variant, known as strongly associated with susceptibility to eating disorders such as anorexia nervosa and bulimia nervosa; associated with poorer episodic memory; may have a protective effect in obsessive-compulsive disorder; impairs localization to secretory granules or synapses; decreases density of dendritic mushroom spines and synapses;, features a modification of the amino acid from V to M at position 66.
+The protein's natural variant, known as found in a small consanguineous family with intellectual disability; unknown pathological significance;, features a modification of the amino acid from M to T at position 122.
+The protein's natural variant, known as in NEDBASS; unknown pathological significance;, features a modification of the amino acid from R to Q at position 232.
+The protein's natural variant, known as in NEDBASS; unknown pathological significance;, features a modification of the amino acid from M to V at position 302.
+The protein's natural variant, known as in NEDBASS; unknown pathological significance;, features a modification of the amino acid from R to W at position 431.
+The protein's natural variant, known as in NEDBASS;, features a modification of the amino acid from P to L at position 532.
+The protein's natural variant, known as in NEDBASS; when associated in cis with H-1017; unknown pathological significance;, features a modification of the amino acid from K to R at position 583.
+The protein's natural variant, known as in NEDBASS, features a modification of the amino acid from N to K at position 634.
+The protein's natural variant, known as in NEDBASS; unknown pathological significance;, features a modification of the amino acid from P to L at position 829.
+The protein's natural variant, known as in NEDBASS; unknown pathological significance;, features a modification of the amino acid from H to Y at position 894.
+The protein's natural variant, known as in NEDBASS; unknown pathological significance;, features a modification of the amino acid from Q to R at position 916.
+The protein's natural variant, known as in NEDBASS; when associated in cis with R-583; unknown pathological significance;, features a modification of the amino acid from Q to H at position 1017.
+The protein's natural variant, known as in NEDBASS; unknown pathological significance;, features a modification of the amino acid from E to K at position 1250.
+The protein's natural variant, known as in NEDBASS; unknown pathological significance;, features a modification of the amino acid from R to L at position 1332.
+The natural variant of this protein is characterized by an amino acid alteration from E to V at position 468.
+The natural variant of this protein is characterized by an amino acid alteration from T to A at position 474.
+The protein's natural variant, known as in CMT2DD; no effect on Na(+)-dependent currents;, features a modification of the amino acid from L to R at position 48.
+The protein's natural variant, known as in HOMGSMR2; results in altered sodium and potassium transport as shown by in vitro functional expression of the homologous rat variant, features a modification of the amino acid from L to R at position 302.
+The protein's natural variant, known as in HOMGSMR2; results in altered sodium and potassium transport as shown by in vitro functional expression of the homologous rat variant;, features a modification of the amino acid from G to R at position 303.
+The protein's natural variant, known as in CMT2DD; unknown pathological significance;, features a modification of the amino acid from I to T at position 592.
+The protein's natural variant, known as in CMT2DD; unknown pathological significance, features a modification of the amino acid from A to T at position 597.
+The protein's natural variant, known as in CMT2DD; shows fewer Na(+)-dependent currents than wild-type protein;, features a modification of the amino acid from P to A at position 600.
+The protein's natural variant, known as in CMT2DD; unknown pathological significance;, features a modification of the amino acid from P to T at position 600.
+The protein's natural variant, known as in CMT2DD; unknown pathological significance; requires 2 nucleotide substitutions, features a modification of the amino acid from D to F at position 601.
+The protein's natural variant, known as in CMT2DD; shows fewer Na(+)-dependent currents than wild-type protein;, features a modification of the amino acid from D to A at position 811.
+The protein's natural variant, known as in HOMGSMR2; results in altered sodium and potassium transport as shown by in vitro functional expression of the homologous rat variant;, features a modification of the amino acid from M to R at position 859.
+The protein's natural variant, known as in ATFB17;, features a modification of the amino acid from V to G at position 162.
+The protein's natural variant, known as in ATFB17;, features a modification of the amino acid from I to L at position 166.
+The protein's natural variant, known as in LQT10; increase in late sodium current;, features a modification of the amino acid from L to F at position 179.
+The protein's natural variant, known as in strain: D273-10B/A1, features a modification of the amino acid from S to I at position 207.
+The protein's natural variant, known as in allele ATP3a, features a modification of the amino acid from S to F at position 308.
+The protein's natural variant, known as in SPGF38; unknown pathological significance;, features a modification of the amino acid from I to N at position 760.
+The natural variant of this protein is characterized by an amino acid alteration from H to R at position 136.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation;, features a modification of the amino acid from E to K at position 311.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from R to Q at position 732.
+The protein's natural variant, known as causes malformations in the distal reproductive tract development in both female and male, features a modification of the amino acid from G to E at position 102.
+The protein's natural variant, known as in Pendred syndrome/deafness individuals;, features a modification of the amino acid from R to G at position 24.
+The protein's natural variant, known as in PDS and DFNB4;, features a modification of the amino acid from S to R at position 28.
+The protein's natural variant, known as in PDS;, features a modification of the amino acid from E to Q at position 29.
+The protein's natural variant, known as in PDS, features a modification of the amino acid from Y to C at position 78.
+The protein's natural variant, known as in DFNB4;, features a modification of the amino acid from S to L at position 90.
+The protein's natural variant, known as in PDS; fails to localize to cell membrane; abolishes iodide transport;, features a modification of the amino acid from G to R at position 102.
+The protein's natural variant, known as in Pendred syndrome/deafness individuals;, features a modification of the amino acid from A to V at position 104.
+The protein's natural variant, known as in PDS;, features a modification of the amino acid from Y to C at position 105.
+The protein's natural variant, known as in PDS, features a modification of the amino acid from A to D at position 106.
+The protein's natural variant, known as in DFNB4 and PDS; does not affect protein localization to cell membrane; does not affect iodide transport;, features a modification of the amino acid from L to F at position 117.
+The protein's natural variant, known as in DFNB4;, features a modification of the amino acid from P to S at position 123.
+The protein's natural variant, known as in DFNB4;, features a modification of the amino acid from T to I at position 132.
+The protein's natural variant, known as in PDS;, features a modification of the amino acid from S to T at position 133.
+The protein's natural variant, known as in PDS;, features a modification of the amino acid from S to P at position 137.
+The protein's natural variant, known as in PDS; fails to localize to cell membrane; abolishes iodide transport;, features a modification of the amino acid from V to F at position 138.
+The protein's natural variant, known as in PDS, features a modification of the amino acid from G to A at position 139.
+The protein's natural variant, known as found at heterozygosity in a patient with non-syndromic deafness; uncertain pathological significance;, features a modification of the amino acid from V to A at position 144.
+The protein's natural variant, known as in DFNB4;, features a modification of the amino acid from M to V at position 147.
+The protein's natural variant, known as in DFNB4; also found at heterozygosity in a patient with non-syndromic deafness; uncertain pathological significance; loss of cell membrane localization, loss of chloride tranport, chloride-bicarbonate exchanger and chloride-iodide exchanger activities;, features a modification of the amino acid from R to T at position 185.
+The protein's natural variant, known as in PDS;, features a modification of the amino acid from T to I at position 193.
+The protein's natural variant, known as in DFNB4 and PDS; severely reduces iodide transport without affecting protein localization to cell membrane;, features a modification of the amino acid from G to V at position 209.
+The protein's natural variant, known as in DFNB4, features a modification of the amino acid from A to P at position 227.
+The protein's natural variant, known as in PDS and DFNB4; common mutation; fails to localize to cell membrane; abolishes iodide transport;, features a modification of the amino acid from L to P at position 236.
+The protein's natural variant, known as in PDS and DFNB4;, features a modification of the amino acid from V to D at position 239.
+The protein's natural variant, known as in DFNB4;, features a modification of the amino acid from S to P at position 252.
+The protein's natural variant, known as in PDS, features a modification of the amino acid from D to H at position 271.
+The protein's natural variant, known as in DFNB4;, features a modification of the amino acid from V to I at position 281.
+The protein's natural variant, known as in PDS and DFNB4;, features a modification of the amino acid from F to L at position 335.
+The protein's natural variant, known as in DFNB4;, features a modification of the amino acid from K to E at position 369.
+The protein's natural variant, known as in DFNB4;, features a modification of the amino acid from A to V at position 372.
+The protein's natural variant, known as in PDS; also found at heterozygosity in a patient with hearing loss and unilateral enlargement of the vestibular aqueduct; uncertain pathological significance;, features a modification of the amino acid from E to G at position 384.
+The protein's natural variant, known as in PDS, features a modification of the amino acid from S to N at position 391.
+The protein's natural variant, known as in DFNB4;, features a modification of the amino acid from N to Y at position 392.
+The protein's natural variant, known as in PDS and DFNB4;, features a modification of the amino acid from V to M at position 402.
+The protein's natural variant, known as in PDS;, features a modification of the amino acid from R to H at position 409.
+The protein's natural variant, known as in DFNB4;, features a modification of the amino acid from R to P at position 409.
+The protein's natural variant, known as in DFNB4 and PDS; fails to localize to cell membrane; abolishes iodide transport;, features a modification of the amino acid from T to M at position 410.
+The protein's natural variant, known as in PDS;, features a modification of the amino acid from A to P at position 411.
+The protein's natural variant, known as in PDS and DFNB4; common mutation;, features a modification of the amino acid from T to P at position 416.
+The protein's natural variant, known as in Pendred syndrome/deafness individuals;, features a modification of the amino acid from Q to R at position 421.
+The protein's natural variant, known as in PDS and DFNB4; also found at heterozygosity in a patient with hearing loss and unilateral enlargement of the vestibular aqueduct; uncertain pathological significance;, features a modification of the amino acid from L to W at position 445.
+The protein's natural variant, known as in DFNB4 and PDS; fails to localize to cell membrane; abolishes iodide transport;, features a modification of the amino acid from Q to R at position 446.
+The protein's natural variant, known as in DFNB4;, features a modification of the amino acid from N to K at position 457.
+The protein's natural variant, known as in PDS; retains residual transport function, features a modification of the amino acid from V to D at position 480.
+The protein's natural variant, known as in DFNB4;, features a modification of the amino acid from I to L at position 490.
+The protein's natural variant, known as in DFNB4;, features a modification of the amino acid from G to S at position 497.
+The protein's natural variant, known as in PDS, features a modification of the amino acid from T to N at position 508.
+The protein's natural variant, known as in PDS;, features a modification of the amino acid from Q to R at position 514.
+The protein's natural variant, known as in PDS;, features a modification of the amino acid from Y to H at position 530.
+The protein's natural variant, known as in PDS and DFNB4;, features a modification of the amino acid from Y to S at position 530.
+The protein's natural variant, known as in PDS, features a modification of the amino acid from S to I at position 552.
+The protein's natural variant, known as in PDS and DFNB4; partially affects protein localization to cell membrane; abolishes iodide transport;, features a modification of the amino acid from Y to C at position 556.
+The protein's natural variant, known as in PDS, features a modification of the amino acid from Y to H at position 556.
+The protein's natural variant, known as in DFNB4, features a modification of the amino acid from N to K at position 558.
+The protein's natural variant, known as in PDS;, features a modification of the amino acid from C to Y at position 565.
+The protein's natural variant, known as found at heterozygosity in a patient with hearing loss and unilateral enlargement of the vestibular aqueduct; uncertain pathological significance;, features a modification of the amino acid from L to S at position 597.
+The protein's natural variant, known as in PDS; retains residual transport function;, features a modification of the amino acid from V to A at position 653.
+The protein's natural variant, known as in DFNB4;, features a modification of the amino acid from S to F at position 666.
+The protein's natural variant, known as in PDS;, features a modification of the amino acid from F to C at position 667.
+The protein's natural variant, known as in PDS; partially affects protein localization to cell membrane; abolishes iodide transport;, features a modification of the amino acid from G to E at position 672.
+The protein's natural variant, known as in DFNB4;, features a modification of the amino acid from L to Q at position 676.
+The protein's natural variant, known as in Pendred syndrome/deafness individuals;, features a modification of the amino acid from F to S at position 683.
+The protein's natural variant, known as in PDS;, features a modification of the amino acid from S to P at position 694.
+The protein's natural variant, known as in DFNB4 and PDS;, features a modification of the amino acid from T to M at position 721.
+The protein's natural variant, known as in DFNB4 and PDS; common mutation in Korea and Japan;, features a modification of the amino acid from H to R at position 723.
+The protein's natural variant, known as in PDS;, features a modification of the amino acid from D to N at position 724.
+The protein's natural variant, known as found at heterozygosity in a patient with hearing loss and unilateral enlargement of the vestibular aqueduct; requires 2 nucleotide substitutions; uncertain pathological significance, features a modification of the amino acid from M to C at position 775.
+The protein's natural variant, known as in PDS and DFNB4;, features a modification of the amino acid from M to T at position 775.
+The protein's natural variant, known as found at heterozygosity in a patient with hearing loss and unilateral enlargement of the vestibular aqueduct; unknown pathological significance; retains its ability to transport iodide in vitro;, features a modification of the amino acid from R to C at position 776.
+The protein's natural variant, known as in ADTKD1, features a modification of the amino acid from C to W at position 52.
+The protein's natural variant, known as in ADTKD1; results in defective trafficking of mutant protein to the plasma membrane; the mutant is retained in the ER, features a modification of the amino acid from D to A at position 59.
+The protein's natural variant, known as in ADTKD1;, features a modification of the amino acid from C to Y at position 77.
+The protein's natural variant, known as in ADTKD1, features a modification of the amino acid from VCPEG to AASC at position 97.
+The protein's natural variant, known as in ADTKD1;, features a modification of the amino acid from G to C at position 103.
+The protein's natural variant, known as in ADTKD1; causes a delay in protein export to the plasma membrane due to a longer retention time in the ER;, features a modification of the amino acid from V to E at position 109.
+The protein's natural variant, known as in ADTKD1, features a modification of the amino acid from C to R at position 112.
+The protein's natural variant, known as in ADTKD1; serum levels severely reduced;, features a modification of the amino acid from C to G at position 120.
+The protein's natural variant, known as in ADTKD1;, features a modification of the amino acid from C to R at position 126.
+The protein's natural variant, known as in ADTKD1; results in defective trafficking of mutant protein to the plasma membrane; the mutant is retained in the ER;, features a modification of the amino acid from N to S at position 128.
+The protein's natural variant, known as in ADTKD1, features a modification of the amino acid from C to S at position 135.
+The protein's natural variant, known as in ADTKD1; phenotype overlapping with medullary cystic kidney disease; causes a delay in protein export to the plasma membrane due to a longer retention time in the ER, features a modification of the amino acid from C to W at position 148.
+The protein's natural variant, known as in ADTKD1;, features a modification of the amino acid from C to Y at position 148.
+The protein's natural variant, known as in ADTKD1; phenotype overlapping with medullary cystic kidney disease; causes a delay in protein export to the plasma membrane due to a longer retention time in the ER; results is abnormal intracellular polymerization of the mutant protein, features a modification of the amino acid from C to S at position 150.
+The protein's natural variant, known as probable-disease association mutation found in a patient with cystic kidney disease; results in mutant retention in the ER; results is abnormal intracellular polymerization of the mutant protein, features a modification of the amino acid from C to R at position 155.
+The protein's natural variant, known as in ADTKD1, features a modification of the amino acid from C to Y at position 170.
+The protein's natural variant, known as in ADTKD1, features a modification of the amino acid from R to S at position 185.
+The protein's natural variant, known as in ADTKD1, features a modification of the amino acid from C to F at position 195.
+The protein's natural variant, known as in ADTKD1, features a modification of the amino acid from W to S at position 202.
+The protein's natural variant, known as in ADTKD1; results in defective trafficking of mutant protein to the plasma membrane; the mutant is retained in the ER, features a modification of the amino acid from R to G at position 204.
+The protein's natural variant, known as in ADTKD1;, features a modification of the amino acid from C to G at position 217.
+The protein's natural variant, known as in ADTKD1; results in defective trafficking of mutant protein to the plasma membrane; the mutant is retained in the ER;, features a modification of the amino acid from C to R at position 217.
+The protein's natural variant, known as in ADTKD1, features a modification of the amino acid from R to P at position 222.
+The protein's natural variant, known as in ADTKD1, features a modification of the amino acid from C to Y at position 223.
+The protein's natural variant, known as in ADTKD1; results in defective trafficking of mutant protein to the plasma membrane; the mutant is retained in the ER, features a modification of the amino acid from T to K at position 225.
+The protein's natural variant, known as in ADTKD1, features a modification of the amino acid from T to M at position 225.
+The protein's natural variant, known as in ADTKD1, features a modification of the amino acid from W to R at position 230.
+The protein's natural variant, known as in ADTKD1;, features a modification of the amino acid from P to L at position 236.
+The protein's natural variant, known as in ADTKD1; causes a delay in protein export to the plasma membrane due to a longer retention time in the ER, features a modification of the amino acid from P to Q at position 236.
+The protein's natural variant, known as in ADTKD1; results in defective trafficking of mutant protein to the plasma membrane; the mutant is retained in the ER, features a modification of the amino acid from P to R at position 236.
+The protein's natural variant, known as in ADTKD1; causes a delay in protein export to the plasma membrane due to a longer retention time in the ER;, features a modification of the amino acid from C to W at position 248.
+The protein's natural variant, known as in ADTKD1;, features a modification of the amino acid from C to Y at position 255.
+The protein's natural variant, known as in ADTKD1, features a modification of the amino acid from C to R at position 282.
+The protein's natural variant, known as in ADTKD1;, features a modification of the amino acid from C to G at position 300.
+The protein's natural variant, known as in ADTKD1; causes a delay in protein export to the plasma membrane due to a longer retention time in the ER;, features a modification of the amino acid from C to R at position 315.
+The protein's natural variant, known as in ADTKD1;, features a modification of the amino acid from Q to P at position 316.
+The protein's natural variant, known as in ADTKD1; phenotype overlapping with medullary cystic kidney disease; causes a delay in protein export to the plasma membrane due to a longer retention time in the ER, features a modification of the amino acid from C to Y at position 317.
+The protein's natural variant, known as in ADTKD1; causes a delay in protein export to the plasma membrane due to a longer retention time in the ER, features a modification of the amino acid from C to G at position 347.
+The protein's natural variant, known as in ADTKD1, features a modification of the amino acid from A to E at position 461.
+The protein's natural variant, known as in COFG; unknown pathological significance;, features a modification of the amino acid from Q to P at position 233.
+The protein's natural variant, known as in MCAHS1;, features a modification of the amino acid from R to Q at position 709.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from A to V at position 20.
+The protein's natural variant, known as in PDIL; loss of function in DNA replication initiation; contrary to the wild type, the mutant does not rescue reduced cell proliferation, prolonged S-phase and impaired DNA replication when transfected in patient cells, features a modification of the amino acid from C to R at position 301.
+The protein's natural variant, known as found in a patient with nephrotic syndrome; unknown pathological significance; no effect on protein localization;, features a modification of the amino acid from E to K at position 454.
+The natural variant of this protein is characterized by an amino acid alteration from S to P at position 636.
+The protein's natural variant, known as in an ovarian mucinous carcinoma sample; somatic mutation, features a modification of the amino acid from E to D at position 434.
+The protein's natural variant, known as in PHA2B; impaired interaction with KLHL3;, features a modification of the amino acid from E to K at position 562.
+The protein's natural variant, known as in PHA2B; impaired interaction with KLHL3;, features a modification of the amino acid from D to A at position 564.
+The protein's natural variant, known as in PHA2B; impaired interaction with KLHL3;, features a modification of the amino acid from Q to E at position 565.
+The natural variant of this protein is characterized by an amino acid alteration from P to L at position 813.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation, features a modification of the amino acid from P to S at position 992.
+The natural variant of this protein is characterized by an amino acid alteration from L to P at position 1013.
+The protein's natural variant, known as in PHA2B;, features a modification of the amino acid from R to C at position 1185.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from W to S at position 44.
+The protein's natural variant, known as in hyperproinsulinemia obese fat/fat mice; reduced activity, features a modification of the amino acid from S to P at position 244.
+The protein's natural variant, known as in strain: Isolate I539, features a modification of the amino acid from PQ to RK at position 6.
+The protein's natural variant, known as in strain: Isolate I539, features a modification of the amino acid from S to W at position 31.
+The protein's natural variant, known as in strain: Isolate I539, features a modification of the amino acid from L to I at position 45.
+The protein's natural variant, known as in strain: Isolate I539, features a modification of the amino acid from V to I at position 117.
+The protein's natural variant, known as in strain: Isolate I539, features a modification of the amino acid from I to M at position 218.
+The protein's natural variant, known as in strain: Isolate I539, features a modification of the amino acid from L to M at position 307.
+The protein's natural variant, known as in strain: Isolate I539, features a modification of the amino acid from N to Y at position 374.
+The natural variant of this protein is characterized by an amino acid alteration from V to L at position 66.
+The protein's natural variant, known as in strain: Serotype T10 / PH252, features a modification of the amino acid from P to S at position 351.
+The protein's natural variant, known as in SGS;, features a modification of the amino acid from L to R at position 21.
+The protein's natural variant, known as in SGS, features a modification of the amino acid from S to T at position 28.
+The protein's natural variant, known as in SGS, features a modification of the amino acid from S to L at position 31.
+The protein's natural variant, known as in SGS, features a modification of the amino acid from L to P at position 32.
+The protein's natural variant, known as in SGS;, features a modification of the amino acid from L to V at position 32.
+The protein's natural variant, known as in SGS, features a modification of the amino acid from G to A at position 34.
+The protein's natural variant, known as in SGS;, features a modification of the amino acid from G to C at position 34.
+The protein's natural variant, known as in SGS;, features a modification of the amino acid from G to D at position 34.
+The protein's natural variant, known as in SGS;, features a modification of the amino acid from G to S at position 34.
+The protein's natural variant, known as in SGS;, features a modification of the amino acid from G to V at position 34.
+The protein's natural variant, known as in SGS;, features a modification of the amino acid from P to Q at position 35.
+The protein's natural variant, known as in SGS;, features a modification of the amino acid from P to S at position 35.
+The protein's natural variant, known as in SGS;, features a modification of the amino acid from G to E at position 116.
+The protein's natural variant, known as in SGS;, features a modification of the amino acid from G to R at position 117.
+The protein's natural variant, known as increased kinase activity;, features a modification of the amino acid from I to V at position 57.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation; reduces interaction with TPX2, features a modification of the amino acid from S to R at position 155.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation; constitutively enhanced kinase activity, features a modification of the amino acid from V to M at position 174.
+The protein's natural variant, known as in variant H17, features a modification of the amino acid from E to K at position 7.
+The protein's natural variant, known as in GAMOS3; strongly reduced formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs;, features a modification of the amino acid from I to F at position 14.
+The protein's natural variant, known as in GAMOS3;, features a modification of the amino acid from K to E at position 78.
+The protein's natural variant, known as in GAMOS3;, features a modification of the amino acid from V to M at position 107.
+The protein's natural variant, known as in GAMOS3; strongly reduced formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs;, features a modification of the amino acid from C to R at position 110.
+The protein's natural variant, known as in GAMOS3; strongly reduced formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs;, features a modification of the amino acid from I to T at position 111.
+The protein's natural variant, known as in GAMOS3;, features a modification of the amino acid from I to T at position 139.
+The protein's natural variant, known as in GAMOS3;, features a modification of the amino acid from G to A at position 177.
+The protein's natural variant, known as in GAMOS3; reduced formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs, features a modification of the amino acid from K to R at position 198.
+The protein's natural variant, known as in GAMOS3; reduced formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs;, features a modification of the amino acid from R to Q at position 247.
+The protein's natural variant, known as in GAMOS3;, features a modification of the amino acid from R to C at position 280.
+The protein's natural variant, known as in GAMOS3;, features a modification of the amino acid from R to H at position 280.
+The protein's natural variant, known as in GAMOS3; reduced formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs;, features a modification of the amino acid from R to L at position 280.
+The protein's natural variant, known as in GAMOS3; reduced formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs;, features a modification of the amino acid from R to Q at position 325.
+The protein's natural variant, known as in GAMOS3;, features a modification of the amino acid from R to W at position 325.
+The protein's natural variant, known as in strain: 5E78-1, features a modification of the amino acid from L to V at position 124.
+The protein's natural variant, known as in strain: 5E78-1, features a modification of the amino acid from D to G at position 171.
+The protein's natural variant, known as in strain: 5E78-1, features a modification of the amino acid from P to R at position 175.
+The protein's natural variant, known as in strain: 5E78-1, features a modification of the amino acid from T to N at position 186.
+The protein's natural variant, known as in strain: 5E78-1, features a modification of the amino acid from P to S at position 217.
+The protein's natural variant, known as in strain: 5E78-1, features a modification of the amino acid from L to M at position 258.
+The protein's natural variant, known as in strain: 5E78-1, features a modification of the amino acid from N to S at position 284.
+The protein's natural variant, known as in strain: 5E78-1, features a modification of the amino acid from I to C at position 290.
+The protein's natural variant, known as in LOP, features a modification of the amino acid from A to P at position 51.
+The protein's natural variant, known as in MRT51; no effect on protein abundance; no effect on protein localization to the cytoplasm; decreased thermal stability; decreased ligand affinity for S-adenosyl-L-methionine; loss of histamine N-methyltransferase activity;, features a modification of the amino acid from G to D at position 60.
+The protein's natural variant, known as in MRT51; loss of protein solubility; increased aggregation in the cytoplasm;, features a modification of the amino acid from L to P at position 208.
+The protein's natural variant, known as in strain: CLIB 556 haplotype Ha2 and CLIB 630 haplotype Ha2, features a modification of the amino acid from I to V at position 48.
+The protein's natural variant, known as in strain: CLIB 556 haplotype Ha1, features a modification of the amino acid from S to R at position 172.
+The protein's natural variant, known as in strain: CLIB 95, CLIB 382, CLIB 388, CLIB 556 haplotype Ha2, CLIB 630, K1, R12, R13, YIIc12 haplotype Ha2 and YIIc17 haplotype Ha1, features a modification of the amino acid from S to F at position 212.
+The natural variant of this protein is characterized by an amino acid alteration from I to L at position 6.
+The natural variant of this protein is characterized by an amino acid alteration from V to S at position 19.
+The natural variant of this protein is characterized by an amino acid alteration from L to Y at position 23.
+The natural variant of this protein is characterized by an amino acid alteration from V to L at position 31.
+The natural variant of this protein is characterized by an amino acid alteration from T to G at position 49.
+The natural variant of this protein is characterized by an amino acid alteration from H to G at position 50.
+The protein's natural variant, known as in OCA2;, features a modification of the amino acid from R to W at position 10.
+The protein's natural variant, known as in OCA2;, features a modification of the amino acid from G to R at position 27.
+The protein's natural variant, known as in OCA2;, features a modification of the amino acid from S to R at position 86.
+The protein's natural variant, known as in OCA2;, features a modification of the amino acid from C to F at position 112.
+The protein's natural variant, known as in OCA2;, features a modification of the amino acid from P to L at position 198.
+The protein's natural variant, known as in OCA2;, features a modification of the amino acid from P to L at position 211.
+The protein's natural variant, known as in OCA2;, features a modification of the amino acid from NW to KV at position 274.
+The protein's natural variant, known as in OCA2;, features a modification of the amino acid from R to G at position 290.
+The protein's natural variant, known as associated with nonblue eye color; could be a biomarker of cutaneous cancer risk;, features a modification of the amino acid from R to W at position 305.
+The protein's natural variant, known as in OCA2;, features a modification of the amino acid from A to V at position 334.
+The protein's natural variant, known as in unclassified OCA;, features a modification of the amino acid from V to M at position 350.
+The protein's natural variant, known as in OCA2;, features a modification of the amino acid from A to V at position 368.
+The protein's natural variant, known as in unclassified OCA;, features a modification of the amino acid from I to T at position 370.
+The protein's natural variant, known as in OCA2; severe;, features a modification of the amino acid from F to I at position 385.
+The protein's natural variant, known as in OCA2;, features a modification of the amino acid from M to I at position 394.
+The protein's natural variant, known as in OCA2; severe;, features a modification of the amino acid from M to L at position 395.
+The protein's natural variant, known as in OCA2;, features a modification of the amino acid from T to M at position 404.
+The protein's natural variant, known as associated with green/hazel eye color;, features a modification of the amino acid from R to Q at position 419.
+The protein's natural variant, known as in OCA2;, features a modification of the amino acid from R to W at position 419.
+The natural variant of this protein is characterized by an amino acid alteration from L to H at position 440.
+The protein's natural variant, known as in OCA2; reduced flow of chloride ions; no effect on subcellular location; slightly increased luminal pH;, features a modification of the amino acid from V to I at position 443.
+The protein's natural variant, known as in OCA2; mild; AROA form;, features a modification of the amino acid from M to V at position 446.
+The protein's natural variant, known as in OCA2, features a modification of the amino acid from I to S at position 473.
+The protein's natural variant, known as in OCA2, features a modification of the amino acid from N to D at position 476.
+The protein's natural variant, known as in OCA2;, features a modification of the amino acid from A to T at position 481.
+The protein's natural variant, known as in OCA2; mild/severe;, features a modification of the amino acid from N to D at position 489.
+The protein's natural variant, known as in OCA2, features a modification of the amino acid from H to Q at position 549.
+The protein's natural variant, known as in OCA2;, features a modification of the amino acid from T to I at position 592.
+The protein's natural variant, known as in OCA2; no effect on flow of chloride ions; no effect on subcellular location; no effect on luminal pH, features a modification of the amino acid from K to E at position 614.
+The protein's natural variant, known as in OCA2, features a modification of the amino acid from K to N at position 614.
+The protein's natural variant, known as in OCA2;, features a modification of the amino acid from I to L at position 617.
+The protein's natural variant, known as in OCA2;, features a modification of the amino acid from V to I at position 633.
+The protein's natural variant, known as in OCA2;, features a modification of the amino acid from W to R at position 652.
+The protein's natural variant, known as in unclassified OCA, features a modification of the amino acid from E to K at position 678.
+The protein's natural variant, known as in OCA2;, features a modification of the amino acid from W to C at position 679.
+The protein's natural variant, known as in OCA2; severe;, features a modification of the amino acid from W to R at position 679.
+The protein's natural variant, known as in OCA2;, features a modification of the amino acid from F to C at position 684.
+The protein's natural variant, known as in unclassified OCA, features a modification of the amino acid from L to F at position 688.
+The protein's natural variant, known as in OCA2;, features a modification of the amino acid from R to C at position 720.
+The protein's natural variant, known as in OCA2, features a modification of the amino acid from A to P at position 724.
+The protein's natural variant, known as in OCA2;, features a modification of the amino acid from S to L at position 736.
+The protein's natural variant, known as in OCA2 and unclassified OCA;, features a modification of the amino acid from P to L at position 743.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from A to T at position 773.
+The protein's natural variant, known as in OCA2, features a modification of the amino acid from G to R at position 775.
+The protein's natural variant, known as in OCA2;, features a modification of the amino acid from A to V at position 787.
+The protein's natural variant, known as in OCA2, features a modification of the amino acid from G to R at position 795.
+The protein's natural variant, known as in OCA2, features a modification of the amino acid from Q to H at position 799.
+The protein's natural variant, known as in OCA2;, features a modification of the amino acid from Y to H at position 827.
+The protein's natural variant, known as in strain: K69 / isolate 8844 and K91 /isolate 8756; rifampicin resistant, features a modification of the amino acid from S to P at position 537.
+The protein's natural variant, known as in strain: K69 / isolate 8751, K69 / isolate 8752, K69 / isolate 8840-43 and K69 / isolate 8845-49; rifampicin resistant, features a modification of the amino acid from H to Y at position 541.
+The protein's natural variant, known as in strain: K91 / isolate 8755; rifampicin resistant, features a modification of the amino acid from R to H at position 544.
+The protein's natural variant, known as requires 2 nucleotide substitutions;, features a modification of the amino acid from E to N at position 141.
+The protein's natural variant, known as in POF11; weaker cellular response to DNA damage as indicated by delayed recruitment of mutant protein to DNA damaged sites, compared to ERCC6 isoform 1; no effect on interaction with RNA polymerase II either after UV or H(2)O(2) damage, features a modification of the amino acid from G to D at position 746.
+The protein's natural variant, known as in POF11; weaker cellular response to DNA damage as indicated by delayed recruitment of mutant protein to DNA damaged sites, compared to ERCC6 isoform 1; no effect on interaction with RNA polymerase II either after UV or H(2)O(2) damage, features a modification of the amino acid from V to I at position 1056.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from T to P at position 833.
+The protein's natural variant, known as in strain: HFL23, HFL5, VT10, VT6 and HFL2, features a modification of the amino acid from F to L at position 284.
+The protein's natural variant, known as in strain: VT37, HFL15 and HFL3, features a modification of the amino acid from F to V at position 284.
+The protein's natural variant, known as in strain: ATCC 35471, features a modification of the amino acid from I to M at position 153.
+The protein's natural variant, known as in strain: Isolate NK 4504, features a modification of the amino acid from P to H at position 154.
+The protein's natural variant, known as in strain: Isolate NK 4504, features a modification of the amino acid from T to S at position 203.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from P to R at position 351.
+The protein's natural variant, known as in MC1DN20;, features a modification of the amino acid from F to I at position 44.
+The protein's natural variant, known as in MC1DN20, features a modification of the amino acid from R to K at position 127.
+The protein's natural variant, known as in MC1DN20; unknown pathological significance;, features a modification of the amino acid from R to W at position 193.
+The protein's natural variant, known as in MC1DN20, features a modification of the amino acid from A to V at position 220.
+The protein's natural variant, known as in MC1DN20; unknown pathological significance, features a modification of the amino acid from S to F at position 234.
+The protein's natural variant, known as in MC1DN20;, features a modification of the amino acid from R to Q at position 266.
+The protein's natural variant, known as in MC1DN20, features a modification of the amino acid from C to G at position 271.
+The protein's natural variant, known as in MC1DN20; unknown pathological significance;, features a modification of the amino acid from G to S at position 303.
+The protein's natural variant, known as in MC1DN20; unknown pathological significance;, features a modification of the amino acid from A to T at position 326.
+The protein's natural variant, known as in MC1DN20;, features a modification of the amino acid from V to M at position 384.
+The protein's natural variant, known as in MC1DN20; unknown pathological significance;, features a modification of the amino acid from E to K at position 413.
+The protein's natural variant, known as in MC1DN20;, features a modification of the amino acid from R to C at position 414.
+The protein's natural variant, known as in MC1DN20;, features a modification of the amino acid from R to C at position 417.
+The protein's natural variant, known as in MC1DN20;, features a modification of the amino acid from R to W at position 469.
+The protein's natural variant, known as in MC1DN20;, features a modification of the amino acid from R to H at position 518.
+The protein's natural variant, known as in MC1DN20;, features a modification of the amino acid from R to W at position 532.
+The protein's natural variant, known as in MC1DN20, features a modification of the amino acid from L to H at position 606.
+The protein's natural variant, known as in allele Ddc-R6, allele Ddc-R9, allele Ddc-R16, allele Ddc-R20, allele Ddc-R25 and allele Ddc-R30, features a modification of the amino acid from T to P at position 12.
+The protein's natural variant, known as in allele Ddc-R9, features a modification of the amino acid from K to N at position 197.
+The protein's natural variant, known as in allele Ddc-R11 and allele Ddc-R18, features a modification of the amino acid from V to M at position 264.
+The protein's natural variant, known as in allele Ddc-Ore, features a modification of the amino acid from R to M at position 390.
+The protein's natural variant, known as in allele Ddc-R33, features a modification of the amino acid from S to F at position 428.
+The protein's natural variant, known as in allele Ddc-2b, features a modification of the amino acid from S to A at position 489.
+The protein's natural variant, known as in strain: Sprague-Dawley, features a modification of the amino acid from A to P at position 21.
+The protein's natural variant, known as in strain: Sprague-Dawley, features a modification of the amino acid from C to S at position 126.
+The protein's natural variant, known as in LDS5; hypomorphic mutation; results in impaired TGF-beta signaling;, features a modification of the amino acid from C to Y at position 409.
+The protein's natural variant, known as in MMIHS5; interferes with proper polymerization into thin filaments;, features a modification of the amino acid from R to C at position 40.
+The protein's natural variant, known as in VSCM1 and MMIHS5;, features a modification of the amino acid from R to H at position 40.
+The protein's natural variant, known as in VSCM1; unknown pathological significance, features a modification of the amino acid from H to Q at position 41.
+The protein's natural variant, known as in VSCM1;, features a modification of the amino acid from M to T at position 45.
+The protein's natural variant, known as in VSCM1;, features a modification of the amino acid from R to G at position 63.
+The protein's natural variant, known as in MMIHS5; interferes with proper polymerization into thin filaments, features a modification of the amino acid from R to Q at position 63.
+The protein's natural variant, known as in VSCM1, features a modification of the amino acid from P to L at position 110.
+The protein's natural variant, known as in MMIHS5;, features a modification of the amino acid from Y to N at position 134.
+The protein's natural variant, known as in VSCM1, features a modification of the amino acid from L to F at position 143.
+The protein's natural variant, known as in VSCM1, features a modification of the amino acid from R to L at position 148.
+The protein's natural variant, known as in VSCM1; interferes with proper polymerization into thin filaments;, features a modification of the amino acid from R to S at position 148.
+The protein's natural variant, known as in VSCM1, features a modification of the amino acid from T to R at position 149.
+The protein's natural variant, known as in MMIHS5; interferes with proper polymerization into thin filaments leading to impaired contractility of the smooth muscle;, features a modification of the amino acid from R to C at position 178.
+The protein's natural variant, known as in MMIHS5; interferes with proper polymerization into thin filaments;, features a modification of the amino acid from R to H at position 178.
+The protein's natural variant, known as in MMIHS5; interferes with proper polymerization into thin filaments leading to impaired contractility of the smooth muscle;, features a modification of the amino acid from R to L at position 178.
+The protein's natural variant, known as in VSCM1, features a modification of the amino acid from T to I at position 195.
+The protein's natural variant, known as in VSCM1, features a modification of the amino acid from E to D at position 196.
+The protein's natural variant, known as in VSCM1;, features a modification of the amino acid from G to D at position 198.
+The protein's natural variant, known as in MMIHS5 and VSCM1;, features a modification of the amino acid from R to C at position 257.
+The protein's natural variant, known as in MMIHS5, features a modification of the amino acid from R to H at position 257.
+The protein's natural variant, known as found in a severe infantile gastrointestinal motility disorder; unknown pathological significance, features a modification of the amino acid from R to W at position 336.
+The protein's natural variant, known as in strain: BALB/c and SJL/J, features a modification of the amino acid from R to K at position 69.
+The protein's natural variant, known as in strain: BALB/c and SJL/J, features a modification of the amino acid from V to M at position 200.
+The protein's natural variant, known as in allele 1.31 and allele 1.32;, features a modification of the amino acid from L to F at position 56.
+The protein's natural variant, known as in allele 2.21, allele 2.22 and allele 2.23;, features a modification of the amino acid from S to N at position 150.
+The protein's natural variant, known as in allele 1.11, allele 1.21, allele 1.31, allele 1.32, allele 1.51, allele 1.52, allele 2.11, allele 2.21, allele 2.22 and allele 2.23;, features a modification of the amino acid from S to F at position 202.
+The protein's natural variant, known as in allele 1.21;, features a modification of the amino acid from S to G at position 401.
+The protein's natural variant, known as in allele 1.51;, features a modification of the amino acid from S to A at position 408.
+The protein's natural variant, known as in allele 2.11, allele 2.21, allele 2.22 and allele 2.23;, features a modification of the amino acid from S to L at position 410.
+The protein's natural variant, known as in allele 2.21, allele 2.22 and allele 2.23;, features a modification of the amino acid from D to N at position 527.
+The protein's natural variant, known as in strain: O29, features a modification of the amino acid from A to G at position 263.
+The protein's natural variant, known as in strain: cv. Jl-1, features a modification of the amino acid from S to R at position 8.
+The protein's natural variant, known as in strain: cv. Ita-0, features a modification of the amino acid from G to D at position 78.
+The natural variant of this protein is characterized by an amino acid alteration from M to V at position 160.
+The protein's natural variant, known as in NIDDM;, features a modification of the amino acid from G to S at position 464.
+The protein's natural variant, known as found in a patient with schizophrenia; unknown pathological significance; does not impair synaptogenesis; no effect on localization to cell membrane;, features a modification of the amino acid from V to M at position 89.
+The protein's natural variant, known as found in a patient with schizophrenia; unknown pathological significance; does not impair synaptogenesis; no effect on localization to cell membrane;, features a modification of the amino acid from S to F at position 549.
+The protein's natural variant, known as does not affect synaptogenesis; no effect on localization to cell membrane;, features a modification of the amino acid from S to P at position 601.
+The protein's natural variant, known as in SSS4; leads to a sustained activation of cardiac G protein-coupled inwardly-rectifying potassium (GIRK) channels, which is likely to hyperpolarize the myocellular membrane potential and reduce their spontaneous activity; does not affect protein levels, subcellular location, nor interaction with GNAI2 and GNG2, features a modification of the amino acid from R to L at position 52.
+The protein's natural variant, known as in NEDHYDF, features a modification of the amino acid from A to T at position 73.
+The protein's natural variant, known as in NEDHYDF, features a modification of the amino acid from G to R at position 77.
+The protein's natural variant, known as in NEDHYDF, features a modification of the amino acid from G to W at position 77.
+The protein's natural variant, known as in NEDHYDF, features a modification of the amino acid from K to E at position 89.
+The protein's natural variant, known as in NEDHYDF, features a modification of the amino acid from K to T at position 89.
+The protein's natural variant, known as in NEDHYDF, features a modification of the amino acid from S to L at position 147.
+The protein's natural variant, known as in SCAR16; reduces protein level; does not reduce ubiquitin ligase activity and autoubiquitination, features a modification of the amino acid from E to K at position 28.
+The protein's natural variant, known as found in a patient with progressive myoclonus epilepsy; unknown pathological significance, features a modification of the amino acid from P to S at position 57.
+The protein's natural variant, known as in SCAR16; reduces protein level; reduces ubiquitin ligase activity; does not change autoubiquitination;, features a modification of the amino acid from N to S at position 65.
+The protein's natural variant, known as in SCAR16;, features a modification of the amino acid from A to D at position 79.
+The protein's natural variant, known as in SCAR16;, features a modification of the amino acid from A to T at position 79.
+The protein's natural variant, known as in SCAR16;, features a modification of the amino acid from L to V at position 123.
+The protein's natural variant, known as in SCAR16;, features a modification of the amino acid from N to I at position 130.
+The protein's natural variant, known as in SCAR16;, features a modification of the amino acid from K to Q at position 145.
+The protein's natural variant, known as in SCAR16;, features a modification of the amino acid from W to C at position 147.
+The protein's natural variant, known as in SCAR16;, features a modification of the amino acid from L to F at position 165.
+The protein's natural variant, known as in SCAR16, features a modification of the amino acid from S to T at position 236.
+The protein's natural variant, known as in SCAR16;, features a modification of the amino acid from M to T at position 240.
+The protein's natural variant, known as in SCAR16; inhibits ubiquitin ligase activity and autoubiquitination;, features a modification of the amino acid from T to M at position 246.
+The protein's natural variant, known as in DENT1, features a modification of the amino acid from R to RH at position 100.
+The protein's natural variant, known as in DENT1; alters targeting to endosomes;, features a modification of the amino acid from G to V at position 127.
+The protein's natural variant, known as in DENT1; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional, features a modification of the amino acid from G to D at position 249.
+The protein's natural variant, known as in DENT1; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional;, features a modification of the amino acid from L to R at position 270.
+The protein's natural variant, known as in DENT1; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional, features a modification of the amino acid from S to L at position 273.
+The protein's natural variant, known as in DENT1; trafficks normally to the cell surface and to early endosomes; endergoes complex glycosylation at the cell surface like wild-type protein but exhibits significant reductions in outwardly rectifying ion currents, features a modification of the amino acid from G to A at position 282.
+The protein's natural variant, known as in DENT1; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional, features a modification of the amino acid from C to R at position 289.
+The protein's natural variant, known as in DENT1; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional, features a modification of the amino acid from C to R at position 291.
+The protein's natural variant, known as in DENT1; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional;, features a modification of the amino acid from L to P at position 295.
+The protein's natural variant, known as in XLRHR; trafficks normally to the cell surface and to early endosomes; displays complex glycosylation at the cell surface like wild-type protein; exhibits reduced current;, features a modification of the amino acid from S to L at position 314.
+The protein's natural variant, known as in DENT1; delayed in processing of the protein and decrease in the stability of the mature complex glycosylated form causing lower cell surface expression; the early endosome distribution is normal; shows abolished current at the plasma membrane;, features a modification of the amino acid from G to V at position 330.
+The protein's natural variant, known as in DENT1, features a modification of the amino acid from E to A at position 337.
+The protein's natural variant, known as in DENT1, features a modification of the amino acid from S to G at position 340.
+The protein's natural variant, known as in DENT1; retained in the endoplasmic reticulum; alters protein stability; associated with an abolition of chloride current, features a modification of the amino acid from S to R at position 340.
+The protein's natural variant, known as in DENT1; trafficks normally to the cell surface and to early endosomes and displays complex glycosylation at the cell surface like wild-type protein; exhibits no current;, features a modification of the amino acid from Y to C at position 342.
+The protein's natural variant, known as in DENT1, features a modification of the amino acid from F to L at position 343.
+The protein's natural variant, known as in DENT1; associated with a marked reduction to about 30% of wild-type chloride currents; no significant differences between the expression of the mutated and wild-type protein;, features a modification of the amino acid from L to F at position 348.
+The protein's natural variant, known as in LMWPHN; 70% reduction in chloride transport activity and alters targeting to endosomes;, features a modification of the amino acid from R to P at position 350.
+The protein's natural variant, known as in DENT1; unknown pathological significance, features a modification of the amino acid from G to R at position 403.
+The protein's natural variant, known as in DENT1; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional;, features a modification of the amino acid from N to K at position 410.
+The protein's natural variant, known as in DENT1, features a modification of the amino acid from G to D at position 532.
+The protein's natural variant, known as in DENT1; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional, features a modification of the amino acid from L to P at position 539.
+The protein's natural variant, known as in XRN;, features a modification of the amino acid from G to E at position 576.
+The protein's natural variant, known as in DENT1; abolishes the chloride currents, features a modification of the amino acid from G to R at position 582.
+The protein's natural variant, known as in DENT1; causes retention in the endoplasmic reticulum and alters protein stability; total loss of function, features a modification of the amino acid from G to E at position 583.
+The protein's natural variant, known as in DENT1;, features a modification of the amino acid from G to R at position 583.
+The protein's natural variant, known as in DENT1; causes retention in the endoplasmic reticulum and alters protein stability; total loss of function;, features a modification of the amino acid from R to W at position 586.
+The protein's natural variant, known as in DENT1;, features a modification of the amino acid from S to P at position 590.
+The protein's natural variant, known as in LMWPHN; causes retention in the endoplasmic reticulum and alters protein stability; total loss of function, features a modification of the amino acid from I to K at position 594.
+The protein's natural variant, known as in DENT1; abolishes the chloride currents; total loss of function, features a modification of the amino acid from E to D at position 597.
+The protein's natural variant, known as in DENT1, features a modification of the amino acid from S to N at position 615.
+The protein's natural variant, known as in DENT1; delayed in processing of the protein and decrease in the stability of the mature complex glycosylated form causing lower cell surface expression; the early endosome distribution is normal; shows abolished current at the plasma membrane, features a modification of the amino acid from K to E at position 616.
+The protein's natural variant, known as in DENT1; delayed in processing of the protein and decrease in the stability of the mature complex glycosylated form causing lower cell surface expression; the early endosome distribution is normal; shows reduced current at the plasma membrane;, features a modification of the amino acid from W to G at position 617.
+The protein's natural variant, known as in DENT1;, features a modification of the amino acid from T to S at position 727.
+The protein's natural variant, known as found in a patient with intractable epileptic encephalopathy, developmental delay and additional multi-organ symptoms; unknown pathological significance;, features a modification of the amino acid from G to R at position 425.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from A to P at position 907.
+The natural variant of this protein is characterized by an amino acid alteration from P to L at position 118.
+The protein's natural variant, known as in MEDS1;, features a modification of the amino acid from V to G at position 21.
+The protein's natural variant, known as in MEDS1;, features a modification of the amino acid from L to P at position 78.
+The protein's natural variant, known as in allele CYP2C9*7;, features a modification of the amino acid from L to I at position 19.
+The protein's natural variant, known as in allele CYP2C9*35;, features a modification of the amino acid from R to H at position 125.
+The protein's natural variant, known as in allele CYP2C9*14;, features a modification of the amino acid from R to L at position 125.
+The protein's natural variant, known as in allele CYP2C9*2;, features a modification of the amino acid from R to C at position 144.
+The protein's natural variant, known as in allele CYP2C9*8;, features a modification of the amino acid from R to H at position 150.
+The protein's natural variant, known as in allele CYP2C9*57, features a modification of the amino acid from N to H at position 204.
+The protein's natural variant, known as in allele CYP2C9*9;, features a modification of the amino acid from H to R at position 251.
+The protein's natural variant, known as in allele CYP2C9*10;, features a modification of the amino acid from E to G at position 272.
+The protein's natural variant, known as in allele CYP2C9*11;, features a modification of the amino acid from R to W at position 335.
+The protein's natural variant, known as in allele CYP2C9*3; responsible for the tolbutamide poor metabolizer phenotype;, features a modification of the amino acid from I to L at position 359.
+The protein's natural variant, known as in allele CYP2C9*4;, features a modification of the amino acid from I to T at position 359.
+The protein's natural variant, known as in allele CYP2C9*5; increases the K(m) value for substrates tested;, features a modification of the amino acid from D to E at position 360.
+The natural variant of this protein is characterized by an amino acid alteration from G to D at position 417.
+The protein's natural variant, known as in allele CYP2C9*59; produces warfarin hypersensitivity; increases affinity but highly decreases enzymatic activity for tolbutamide; no effect on affinity but decreases enzymatic activity for diclofenac; decreases affinity and highly decreases enzymatic activity for losartan, features a modification of the amino acid from I to F at position 434.
+The protein's natural variant, known as in allele CYP2C9*12;, features a modification of the amino acid from P to S at position 489.
+The protein's natural variant, known as in allele RPS12-R43; confers streptomycin resistance, features a modification of the amino acid from K to R at position 43.
+The protein's natural variant, known as in PMS2, features a modification of the amino acid from N to S at position 159.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from W to R at position 127.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from E to K at position 454.
+The protein's natural variant, known as in IMDDHH;, features a modification of the amino acid from G to R at position 31.
+The protein's natural variant, known as in IMDDHH;, features a modification of the amino acid from E to K at position 79.
+The protein's natural variant, known as in IMDDHH; increased protein abundance; increased positive regulation of transcription of target genes; changed cell redox homeostasis;, features a modification of the amino acid from T to K at position 80.
+The protein's natural variant, known as in IMDDHH;, features a modification of the amino acid from G to S at position 81.
+The protein's natural variant, known as in CMH2;, features a modification of the amino acid from A to V at position 38.
+The protein's natural variant, known as in CMH2;, features a modification of the amino acid from F to L at position 80.
+The protein's natural variant, known as in CMH2;, features a modification of the amino acid from I to N at position 89.
+The protein's natural variant, known as in CMH2;, features a modification of the amino acid from R to L at position 102.
+The protein's natural variant, known as in CMH2;, features a modification of the amino acid from R to Q at position 102.
+The protein's natural variant, known as in CMH2;, features a modification of the amino acid from R to W at position 102.
+The protein's natural variant, known as in CMH2;, features a modification of the amino acid from R to L at position 104.
+The protein's natural variant, known as in CMH2;, features a modification of the amino acid from A to V at position 114.
+The protein's natural variant, known as in CMH2;, features a modification of the amino acid from F to I at position 120.
+The protein's natural variant, known as in CMH2;, features a modification of the amino acid from F to V at position 120.
+The protein's natural variant, known as in CMH2;, features a modification of the amino acid from R to C at position 140.
+The protein's natural variant, known as in CMD1D;, features a modification of the amino acid from R to W at position 141.
+The protein's natural variant, known as in CMD1D;, features a modification of the amino acid from R to W at position 151.
+The protein's natural variant, known as in CMH2, features a modification of the amino acid from E to K at position 173.
+The protein's natural variant, known as in CMH2;, features a modification of the amino acid from S to F at position 189.
+The protein's natural variant, known as in CMD1D;, features a modification of the amino acid from R to L at position 215.
+The protein's natural variant, known as in CMH2;, features a modification of the amino acid from E to D at position 254.
+The protein's natural variant, known as in CMH2;, features a modification of the amino acid from N to I at position 281.
+The protein's natural variant, known as in CMH2;, features a modification of the amino acid from R to C at position 288.
+The protein's natural variant, known as in CMH2;, features a modification of the amino acid from R to P at position 288.
+The protein's natural variant, known as in CMH2;, features a modification of the amino acid from R to C at position 296.
+The protein's natural variant, known as in a patient with diffuse leukoencephalopathy with spheroids; unknown pathological significance;, features a modification of the amino acid from S to L at position 27.
+The protein's natural variant, known as in NSC; loss of localization to the cilium axoneme;, features a modification of the amino acid from K to N at position 17.
+The protein's natural variant, known as in DFNB66; results in ciliary abnormalities including increased ciliary length;, features a modification of the amino acid from Q to P at position 424.
+The protein's natural variant, known as in globin-2A, features a modification of the amino acid from S to D at position 64.
+The protein's natural variant, known as in strain: TMH16, features a modification of the amino acid from A to G at position 50.
+The protein's natural variant, known as in strain: TMH16, features a modification of the amino acid from K to N at position 121.
+The protein's natural variant, known as in strain: TMH16, features a modification of the amino acid from F to S at position 136.
+The protein's natural variant, known as in ESCR;, features a modification of the amino acid from G to S at position 480.
+The protein's natural variant, known as in ALXDRD; affects intermediate filaments formation yielding protein aggregates;, features a modification of the amino acid from K to Q at position 63.
+The protein's natural variant, known as in ALXDRD;, features a modification of the amino acid from R to Q at position 66.
+The protein's natural variant, known as in ALXDRD;, features a modification of the amino acid from R to Q at position 70.
+The protein's natural variant, known as in ALXDRD;, features a modification of the amino acid from R to W at position 70.
+The protein's natural variant, known as in ALXDRD;, features a modification of the amino acid from E to K at position 72.
+The protein's natural variant, known as in ALXDRD;, features a modification of the amino acid from M to K at position 73.
+The protein's natural variant, known as in ALXDRD;, features a modification of the amino acid from M to R at position 73.
+The protein's natural variant, known as in ALXDRD;, features a modification of the amino acid from M to T at position 73.
+The protein's natural variant, known as in ALXDRD;, features a modification of the amino acid from M to T at position 74.
+The protein's natural variant, known as in ALXDRD;, features a modification of the amino acid from L to F at position 76.
+The protein's natural variant, known as in ALXDRD;, features a modification of the amino acid from L to V at position 76.
+The protein's natural variant, known as in ALXDRD, features a modification of the amino acid from N to K at position 77.
+The protein's natural variant, known as in ALXDRD;, features a modification of the amino acid from N to S at position 77.
+The protein's natural variant, known as in ALXDRD;, features a modification of the amino acid from N to Y at position 77.
+The protein's natural variant, known as in ALXDRD; adult form;, features a modification of the amino acid from D to E at position 78.
+The protein's natural variant, known as in ALXDRD;, features a modification of the amino acid from D to N at position 78.
+The protein's natural variant, known as in ALXDRD;, features a modification of the amino acid from R to C at position 79.
+The protein's natural variant, known as in ALXDRD;, features a modification of the amino acid from R to G at position 79.
+The protein's natural variant, known as in ALXDRD;, features a modification of the amino acid from R to H at position 79.
+The protein's natural variant, known as in ALXDRD;, features a modification of the amino acid from R to L at position 79.
+The protein's natural variant, known as in ALXDRD;, features a modification of the amino acid from R to P at position 79.
+The protein's natural variant, known as in ALXDRD;, features a modification of the amino acid from Y to H at position 83.
+The protein's natural variant, known as in ALXDRD;, features a modification of the amino acid from K to E at position 86.
+The protein's natural variant, known as in ALXDRD;, features a modification of the amino acid from R to C at position 88.
+The protein's natural variant, known as in ALXDRD;, features a modification of the amino acid from R to S at position 88.
+The protein's natural variant, known as in ALXDRD;, features a modification of the amino acid from L to P at position 90.
+The protein's natural variant, known as in ALXDRD;, features a modification of the amino acid from L to P at position 97.
+The protein's natural variant, known as in ALXDRD;, features a modification of the amino acid from L to P at position 101.
+The protein's natural variant, known as does not affect intermediate filaments formation;, features a modification of the amino acid from V to I at position 115.
+The protein's natural variant, known as in ALXDRD;, features a modification of the amino acid from E to K at position 207.
+The protein's natural variant, known as in ALXDRD;, features a modification of the amino acid from E to Q at position 207.
+The protein's natural variant, known as in ALXDRD; affects intermediate filaments formation;, features a modification of the amino acid from E to K at position 210.
+The protein's natural variant, known as in ALXDRD;, features a modification of the amino acid from L to P at position 235.
+The protein's natural variant, known as in ALXDRD;, features a modification of the amino acid from K to T at position 236.
+The protein's natural variant, known as in ALXDRD;, features a modification of the amino acid from R to C at position 239.
+The protein's natural variant, known as in ALXDRD;, features a modification of the amino acid from R to H at position 239.
+The protein's natural variant, known as in ALXDRD;, features a modification of the amino acid from R to L at position 239.
+The protein's natural variant, known as in ALXDRD;, features a modification of the amino acid from R to P at position 239.
+The protein's natural variant, known as in ALXDRD;, features a modification of the amino acid from Y to D at position 242.
+The protein's natural variant, known as in ALXDRD; unknown pathological significance; does not affect intermediate filaments formation;, features a modification of the amino acid from A to V at position 244.
+The protein's natural variant, known as in ALXDRD; affects intermediate filaments formation yielding protein aggregates;, features a modification of the amino acid from A to G at position 253.
+The protein's natural variant, known as in ALXDRD; impairs filaments formation;, features a modification of the amino acid from Y to C at position 257.
+The protein's natural variant, known as in ALXDRD;, features a modification of the amino acid from R to P at position 258.
+The protein's natural variant, known as in ALXDRD;, features a modification of the amino acid from A to P at position 267.
+The protein's natural variant, known as in ALXDRD;, features a modification of the amino acid from R to L at position 276.
+The protein's natural variant, known as in ALXDRD;, features a modification of the amino acid from K to E at position 279.
+The protein's natural variant, known as in ALXDRD; associated with Lys-332;, features a modification of the amino acid from R to G at position 330.
+The protein's natural variant, known as in ALXDRD; associated with Gly-330;, features a modification of the amino acid from E to K at position 332.
+The protein's natural variant, known as in ALXDRD;, features a modification of the amino acid from L to P at position 352.
+The protein's natural variant, known as in ALXDRD;, features a modification of the amino acid from L to P at position 359.
+The protein's natural variant, known as in ALXDRD;, features a modification of the amino acid from L to V at position 359.
+The protein's natural variant, known as in ALXDRD;, features a modification of the amino acid from E to D at position 362.
+The protein's natural variant, known as in ALXDRD;, features a modification of the amino acid from A to P at position 364.
+The protein's natural variant, known as in ALXDRD;, features a modification of the amino acid from Y to H at position 366.
+The protein's natural variant, known as in ALXDRD;, features a modification of the amino acid from E to Q at position 371.
+The protein's natural variant, known as in ALXDRD;, features a modification of the amino acid from E to V at position 371.
+The protein's natural variant, known as in ALXDRD, features a modification of the amino acid from E to D at position 373.
+The protein's natural variant, known as in ALXDRD;, features a modification of the amino acid from E to K at position 373.
+The protein's natural variant, known as in ALXDRD;, features a modification of the amino acid from E to Q at position 373.
+The protein's natural variant, known as in ALXDRD;, features a modification of the amino acid from E to G at position 374.
+The protein's natural variant, known as in ALXDRD, features a modification of the amino acid from E to Q at position 374.
+The protein's natural variant, known as in ALXDRD;, features a modification of the amino acid from R to G at position 376.
+The protein's natural variant, known as in ALXDRD;, features a modification of the amino acid from S to F at position 385.
+The protein's natural variant, known as in ALXDRD;, features a modification of the amino acid from R to W at position 416.
+The protein's natural variant, known as in COXPD40; highly decreased glutaminyl-tRNAGln biosynthesis via transamidation;, features a modification of the amino acid from G to E at position 117.
+The protein's natural variant, known as in COXPD40; highly decreased glutaminyl-tRNAGln biosynthesis via transamidation;, features a modification of the amino acid from G to V at position 133.
+The protein's natural variant, known as in COXPD40; unknown pathological significance, features a modification of the amino acid from TRNP to NKNH at position 199.
+The protein's natural variant, known as in COXPD40; requires 2 nucleotide substitutions; unknown pathological significance;, features a modification of the amino acid from A to L at position 427.
+The protein's natural variant, known as in DFNA79; unknown pathological significance;, features a modification of the amino acid from W to S at position 209.
+The protein's natural variant, known as in HGCH-3, features a modification of the amino acid from G to D at position 15.
+The protein's natural variant, known as in DRD;, features a modification of the amino acid from P to L at position 23.
+The protein's natural variant, known as in DRD, features a modification of the amino acid from L to Q at position 71.
+The protein's natural variant, known as in DRD, features a modification of the amino acid from A to V at position 74.
+The protein's natural variant, known as found in patients with DRD; unknown pathological significance, features a modification of the amino acid from Y to C at position 75.
+The protein's natural variant, known as in DRD, features a modification of the amino acid from L to P at position 79.
+The protein's natural variant, known as in DRD, features a modification of the amino acid from G to A at position 83.
+The protein's natural variant, known as in DRD, features a modification of the amino acid from R to P at position 88.
+The protein's natural variant, known as in DRD;, features a modification of the amino acid from R to W at position 88.
+The protein's natural variant, known as in DRD, features a modification of the amino acid from G to V at position 90.
+The natural variant of this protein is characterized by an amino acid alteration from A to V at position 98.
+The protein's natural variant, known as in DRD, features a modification of the amino acid from M to K at position 102.
+The protein's natural variant, known as in DRD, features a modification of the amino acid from M to R at position 102.
+The protein's natural variant, known as in DRD, features a modification of the amino acid from T to I at position 106.
+The protein's natural variant, known as in HPABH4B; intermediate phenotype presenting with dystonia and motor delay;, features a modification of the amino acid from G to D at position 108.
+The protein's natural variant, known as in DRD;, features a modification of the amino acid from D to N at position 115.
+The protein's natural variant, known as in DRD;, features a modification of the amino acid from D to V at position 134.
+The protein's natural variant, known as in DRD;, features a modification of the amino acid from I to K at position 135.
+The natural variant of this protein is characterized by an amino acid alteration from I to T at position 135.
+The protein's natural variant, known as in DRD, features a modification of the amino acid from C to R at position 141.
+The protein's natural variant, known as in DRD, features a modification of the amino acid from C to W at position 141.
+The protein's natural variant, known as in DRD;, features a modification of the amino acid from H to P at position 144.
+The protein's natural variant, known as in DRD, features a modification of the amino acid from H to P at position 153.
+The protein's natural variant, known as in DRD, features a modification of the amino acid from L to R at position 163.
+The protein's natural variant, known as in DRD, features a modification of the amino acid from S to T at position 176.
+The protein's natural variant, known as in DRD, features a modification of the amino acid from R to S at position 178.
+The protein's natural variant, known as in DRD, features a modification of the amino acid from Q to R at position 180.
+The protein's natural variant, known as in HPABH4B; severe hyperphenylalaninemia;, features a modification of the amino acid from R to H at position 184.
+The protein's natural variant, known as in DRD, features a modification of the amino acid from T to K at position 186.
+The protein's natural variant, known as in DRD;, features a modification of the amino acid from V to I at position 191.
+The protein's natural variant, known as in DRD, features a modification of the amino acid from P to L at position 199.
+The protein's natural variant, known as in DRD;, features a modification of the amino acid from G to E at position 201.
+The protein's natural variant, known as in DRD;, features a modification of the amino acid from G to R at position 203.
+The protein's natural variant, known as in HPABH4B; severe hyperphenylalaninemia;, features a modification of the amino acid from M to I at position 211.
+The protein's natural variant, known as in DRD, features a modification of the amino acid from M to V at position 211.
+The protein's natural variant, known as in DRD;, features a modification of the amino acid from M to V at position 213.
+The protein's natural variant, known as in HPABH4B; intermediate phenotype presenting with dystonia and motor delay;, features a modification of the amino acid from M to T at position 221.
+The protein's natural variant, known as in HPABH4B and DRD; phenotype presenting with dystonia and myoclonus;, features a modification of the amino acid from K to R at position 224.
+The protein's natural variant, known as in DRD, features a modification of the amino acid from F to S at position 234.
+The protein's natural variant, known as in DRD;, features a modification of the amino acid from R to W at position 241.
+The protein's natural variant, known as in DRD;, features a modification of the amino acid from R to S at position 249.
+The natural variant of this protein is characterized by an amino acid alteration from A to V at position 103.
+The natural variant of this protein is characterized by an amino acid alteration from I to T at position 403.
+The natural variant of this protein is characterized by an amino acid alteration from F to S at position 558.
+The protein's natural variant, known as in a gastric adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from D to N at position 306.
+The protein's natural variant, known as found in a clear cell renal carcinoma case; somatic mutation, features a modification of the amino acid from A to T at position 367.
+The protein's natural variant, known as detected in mice with the buff mutation; leads to melanocytes with a reduced number of undermelanized melanosomes, features a modification of the amino acid from D to E at position 251.
+The protein's natural variant, known as in BWCNS; studies in fibroblasts show a dramatically reduced level of EMG1 protein in a BWCNS-affected patient compared to normal fibroblasts although patient fibroblasts do not have complete EMG1 deficiency; the mutation increases dimerization of EMG1 subunits suggesting that aggregation of EMG1 leads to reduced levels of the protein;, features a modification of the amino acid from D to G at position 86.
+The protein's natural variant, known as in a spontaneous PAS-resistant mutant strain; complementation with wild-type folC restores PAS susceptibility, confirmimg that this mutation confers high level resistance to PAS, features a modification of the amino acid from E to A at position 40.
+The protein's natural variant, known as in clinical isolates: Q274 and 501063; PAS-resistant; complementation with wild-type folC restores PAS susceptibility, features a modification of the amino acid from E to G at position 40.
+The protein's natural variant, known as in clinical isolate: Q36; PAS-resistant; complementation with wild-type folC restores PAS susceptibility, features a modification of the amino acid from I to A at position 43.
+The protein's natural variant, known as in clinical isolates: Q449 and 1314; PAS-resistant; complementation with wild-type folC restores PAS susceptibility; 7-fold reduction in DHFS activity relative to wild-type; loss of the ability to glutaminate H2PtePAS, features a modification of the amino acid from I to T at position 43.
+The protein's natural variant, known as in a spontaneous PAS-resistant mutant strain, features a modification of the amino acid from N to S at position 73.
+The protein's natural variant, known as in a spontaneous PAS-resistant mutant strain; complementation with wild-type folC restores PAS susceptibility, features a modification of the amino acid from S to G at position 150.
+The protein's natural variant, known as in a spontaneous PAS-resistant mutant strain; complementation with wild-type folC restores PAS susceptibility, features a modification of the amino acid from F to S at position 152.
+The protein's natural variant, known as in a spontaneous PAS-resistant mutant strain; complementation with wild-type folC restores PAS susceptibility; 5-fold reduction in DHFS activity relative to wild-type; loss of the ability to glutaminate H2PtePAS, features a modification of the amino acid from E to A at position 153.
+The protein's natural variant, known as in a spontaneous PAS-resistant mutant strain; complementation with wild-type folC restores PAS susceptibility, features a modification of the amino acid from E to G at position 153.
+The protein's natural variant, known as in RD, features a modification of the amino acid from N to Y at position 83.
+The protein's natural variant, known as in RD, features a modification of the amino acid from P to S at position 173.
+The protein's natural variant, known as in RD, features a modification of the amino acid from H to R at position 175.
+The protein's natural variant, known as in RD;, features a modification of the amino acid from Q to K at position 176.
+The protein's natural variant, known as in RD; total loss of activity;, features a modification of the amino acid from D to G at position 177.
+The protein's natural variant, known as in RD, features a modification of the amino acid from A to AA at position 192.
+The protein's natural variant, known as in RD, features a modification of the amino acid from W to R at position 193.
+The protein's natural variant, known as in RD, features a modification of the amino acid from E to Q at position 197.
+The protein's natural variant, known as in RD, features a modification of the amino acid from I to F at position 199.
+The protein's natural variant, known as in RD; total loss of activity;, features a modification of the amino acid from G to S at position 204.
+The protein's natural variant, known as in RD;, features a modification of the amino acid from H to Y at position 220.
+The protein's natural variant, known as in RD;, features a modification of the amino acid from F to S at position 257.
+The protein's natural variant, known as in RD;, features a modification of the amino acid from N to H at position 269.
+The protein's natural variant, known as in RD; total loss of activity;, features a modification of the amino acid from R to Q at position 275.
+The protein's natural variant, known as in RD; total loss of activity;, features a modification of the amino acid from R to W at position 275.
+The protein's natural variant, known as in HHT1;, features a modification of the amino acid from L to P at position 8.
+The protein's natural variant, known as in HHT1, features a modification of the amino acid from A to D at position 11.
+The protein's natural variant, known as in HHT1;, features a modification of the amino acid from V to F at position 49.
+The protein's natural variant, known as in HHT1; impairs protein folding; abolishes expression at the cell surface, features a modification of the amino acid from G to V at position 52.
+The protein's natural variant, known as in HHT1; impairs protein folding; abolishes expression at the cell surface, features a modification of the amino acid from C to R at position 53.
+The protein's natural variant, known as in HHT1;, features a modification of the amino acid from V to D at position 105.
+The protein's natural variant, known as in HHT1, features a modification of the amino acid from L to R at position 107.
+The protein's natural variant, known as in HHT1; impairs protein folding; nearly abolishes expression at the cell surface;, features a modification of the amino acid from W to C at position 149.
+The protein's natural variant, known as found in a family with hereditary hemorrhagic talagiectasia; unknown pathological significance, features a modification of the amino acid from A to P at position 150.
+The protein's natural variant, known as in HHT1, features a modification of the amino acid from A to D at position 160.
+The protein's natural variant, known as in HHT1, features a modification of the amino acid from A to E at position 175.
+The protein's natural variant, known as in HHT1, features a modification of the amino acid from TL to VLQ at position 194.
+The natural variant of this protein is characterized by an amino acid alteration from R to P at position 205.
+The protein's natural variant, known as in HHT1;, features a modification of the amino acid from I to T at position 220.
+The protein's natural variant, known as in HHT1; impairs protein folding; strongly reduces expression at the cell surface;, features a modification of the amino acid from L to P at position 221.
+The protein's natural variant, known as in HHT1, features a modification of the amino acid from L to Q at position 221.
+The protein's natural variant, known as found in a patient with hereditary hemorrhagic talagiectasia; unknown pathological significance;, features a modification of the amino acid from V to M at position 236.
+The protein's natural variant, known as in HHT1;, features a modification of the amino acid from V to E at position 238.
+The protein's natural variant, known as in HHT1, features a modification of the amino acid from I to S at position 263.
+The protein's natural variant, known as in HHT1, features a modification of the amino acid from I to T at position 263.
+The protein's natural variant, known as in HHT1, features a modification of the amino acid from M to R at position 269.
+The protein's natural variant, known as in HHT1, features a modification of the amino acid from L to P at position 306.
+The protein's natural variant, known as in HHT1, features a modification of the amino acid from A to D at position 308.
+The protein's natural variant, known as found in a family with hereditary hemorrhagic talagiectasia; unknown pathological significance;, features a modification of the amino acid from V to M at position 315.
+The protein's natural variant, known as in HHT1;, features a modification of the amino acid from C to S at position 363.
+The protein's natural variant, known as found in a patient with hereditary hemorrhagic talagiectasia; unknown pathological significance, features a modification of the amino acid from K to E at position 374.
+The protein's natural variant, known as in HHT1;, features a modification of the amino acid from C to Y at position 394.
+The protein's natural variant, known as in HHT1, features a modification of the amino acid from C to S at position 412.
+The protein's natural variant, known as in HHT1;, features a modification of the amino acid from G to V at position 413.
+The protein's natural variant, known as found in a patient with hereditary hemorrhagic talagiectasia; unknown pathological significance, features a modification of the amino acid from M to R at position 414.
+The protein's natural variant, known as in HHT1;, features a modification of the amino acid from R to W at position 437.
+The protein's natural variant, known as in HHT1;, features a modification of the amino acid from L to S at position 490.
+The protein's natural variant, known as in HHT1;, features a modification of the amino acid from V to M at position 504.
+The protein's natural variant, known as in HHT1;, features a modification of the amino acid from R to H at position 529.
+The protein's natural variant, known as in HHT1, features a modification of the amino acid from R to P at position 529.
+The protein's natural variant, known as in HHT1, features a modification of the amino acid from G to D at position 545.
+The protein's natural variant, known as in HHT1, features a modification of the amino acid from L to P at position 547.
+The protein's natural variant, known as found in a patient with hereditary hemorrhagic talagiectasia; unknown pathological significance;, features a modification of the amino acid from C to Y at position 549.
+The protein's natural variant, known as in HHT1;, features a modification of the amino acid from G to R at position 603.
+The protein's natural variant, known as in HHT1, features a modification of the amino acid from A to D at position 604.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from E to D at position 64.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from RN to KK at position 102.
+The protein's natural variant, known as in plasmid pMYSH6000 and plasmid pCP301, features a modification of the amino acid from N to H at position 102.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from DQ to YE at position 127.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from A to D at position 136.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from N to K at position 140.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from N to K at position 193.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from KALEE to DELTK at position 201.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from Q to K at position 220.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from Q to E at position 239.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from S to N at position 247.
+The protein's natural variant, known as in allele DPB1*09:02;, features a modification of the amino acid from T to M at position 16.
+The protein's natural variant, known as in allele DPB1*75:01, features a modification of the amino acid from R to P at position 30.
+The protein's natural variant, known as in allele DPB1*75:01; requires 2 nucleotide substitutions, features a modification of the amino acid from A to L at position 31.
+The protein's natural variant, known as in allele DPB1*75:01, features a modification of the amino acid from T to P at position 32.
+The protein's natural variant, known as in allele DPB1*75:01, features a modification of the amino acid from P to A at position 33.
+The protein's natural variant, known as in allele DPB1*01:01, allele DPB1*03:01, allele DPB1*05:02, allele DPB1*06:01, allele DPB1*09:01, allele DPB1*09:02, allele DPB1*10:01, allele DPB1*11:01, allele DPB1*11:02, allele DPB1*13:01, allele DPB1*13:02, allele DPB1*14:01, allele DPB1*14:02, allele DPB1*15:01, allele DPB1*16:02, allele DPB1*17:01, allele DPB1*17:02, allele DPB1*18:01, allele DPB1*20:02, allele DPB1*21:01, allele DPB1*21:02, allele DPB1*20:01, allele DPB1*22:02, allele DPB1*25:01, allele DPB1*25:02, allele DPB1*26:01, allele DPB1*27:01, allele DPB1*29:01, allele DPB1*30:01, allele DPB1*35:01, allele DPB1*36:01, allele DPB1*37:01, allele DPB1*44:01, allele DPB1*45:01, allele DPB1*50:01, allele DPB1*52:01, allele DPB1*54:01, allele DPB1*55:01, allele DPB1*56:01, allele DPB1*58:01, allele DPB1*66:01, allele DPB1*67:01, allele DPB1*69:01, allele DPB1*70:01, allele DPB1*74:01, allele DPB1*76:01, allele DPB1*78:01, allele DPB1*79:01, allele DPB1*85:01, allele DPB1*86:01, allele DPB1*87:01, allele DPB1*88:01, allele DPB1*89:01, allele DPB1*90:01, allele DPB1*91:01, allele DPB1*92:01, allele DPB1*93:01 and allele DPB1*98:01;, features a modification of the amino acid from L to V at position 37.
+The protein's natural variant, known as in allele DPB1*70:01; requires 2 nucleotide substitutions, features a modification of the amino acid from F to D at position 38.
+The protein's natural variant, known as in allele DPB1*09:01, allele DPB1*10:01, allele DPB1*14:01, allele DPB1*16:02, allele DPB1*17:01, allele DPB1*22:02, allele DPB1*30:01, allele DPB1*35:01, allele DPB1*45:01, allele DPB1*54:01, allele DPB1*55:01, allele DPB1*58:01, allele DPB1*66:01, allele DPB1*67:01, allele DPB1*76:01, allele DPB1*86:01, allele DPB1*91:01 and allele DPB1*98:01; requires 2 nucleotide substitutions, features a modification of the amino acid from F to H at position 38.
+The protein's natural variant, known as in allele DPB1*01:01, allele DPB1*03:01, allele DPB1*05:02, allele DPB1*06:01, allele DPB1*09:02, allele DPB1*11:01, allele DPB1*11:02, allele DPB1*13:01, allele DPB1*13:02, allele DPB1*14:02, allele DPB1*15:01, allele DPB1*17:02, allele DPB1*18:01, allele DPB1*20:02, allele DPB1*21:01, allele DPB1*21:02, allele DPB1*20:01, allele DPB1*25:01, allele DPB1*25:02, allele DPB1*26:01, allele DPB1*27:01, allele DPB1*29:01, allele DPB1*36:01, allele DPB1*37:01, allele DPB1*44:01, allele DPB1*50:01, allele DPB1*52:01, allele DPB1*56:01, allele DPB1*69:01, allele DPB1*74:01, allele DPB1*78:01, allele DPB1*79:01, allele DPB1*85:01, allele DPB1*87:01, allele DPB1*88:01, allele DPB1*89:01, allele DPB1*90:01, allele DPB1*92:01 and allele DPB1*93:01;, features a modification of the amino acid from F to Y at position 38.
+The protein's natural variant, known as in allele DPB1*03:01, allele DPB1*05:02, allele DPB1*06:01, allele DPB1*09:01, allele DPB1*09:02, allele DPB1*10:01, allele DPB1*11:01, allele DPB1*11:02, allele DPB1*13:01, allele DPB1*13:02, allele DPB1*14:01, allele DPB1*14:02, allele DPB1*16:02, allele DPB1*17:01, allele DPB1*17:02, allele DPB1*20:02, allele DPB1*21:01, allele DPB1*20:01, allele DPB1*22:02, allele DPB1*25:01, allele DPB1*26:01, allele DPB1*27:01, allele DPB1*29:01, allele DPB1*30:01, allele DPB1*35:01, allele DPB1*36:01, allele DPB1*37:01, allele DPB1*44:01, allele DPB1*45:01, allele DPB1*52:01, allele DPB1*54:01, allele DPB1*55:01, allele DPB1*56:01, allele DPB1*58:01, allele DPB1*66:01, allele DPB1*67:01, allele DPB1*69:01, allele DPB1*70:01, allele DPB1*74:01, allele DPB1*76:01, allele DPB1*78:01, allele DPB1*79:01, allele DPB1*85:01, allele DPB1*86:01, allele DPB1*87:01, allele DPB1*88:01, allele DPB1*91:01, allele DPB1*92:01, allele DPB1*93:01 and allele DPB1*98:01; requires 2 nucleotide substitutions;, features a modification of the amino acid from G to L at position 40.
+The protein's natural variant, known as in allele DPB1*77:01;, features a modification of the amino acid from R to L at position 41.
+The protein's natural variant, known as in allele DPB1*26:02;, features a modification of the amino acid from C to G at position 44.
+The protein's natural variant, known as in allele DPB1*38:01;, features a modification of the amino acid from A to P at position 46.
+The protein's natural variant, known as in allele DPB1*18:02;, features a modification of the amino acid from A to T at position 46.
+The protein's natural variant, known as in allele DPB1*99:01;, features a modification of the amino acid from Y to D at position 57.
+The protein's natural variant, known as in allele DPB1*14:02 and allele DPB1*21:02;, features a modification of the amino acid from R to P at position 61.
+The protein's natural variant, known as ind allele DPB1*11:01, allele DPB1*15:01 and allele DPB1*74:01;, features a modification of the amino acid from E to Q at position 62.
+The protein's natural variant, known as in allele DPB1*02:02, allele DPB1*02:03, allele DPB1*05:01, allele DPB1*15:02, allele DPB1*17:02, allele DPB1*19:02, allele DPB1*21:01, allele DPB1*21:01, allele DPB1*22:01, allele DPB1*34:01, allele DPB1*36:01, allele DPB1*38:01, allele DPB1*44:01, allele DPB1*48:01, allele DPB1*58:01, allele DPB1*62:01, allele DPB1*63:01, allele DPB1*95:01 and allele DPB1*97:01;, features a modification of the amino acid from F to L at position 64.
+The protein's natural variant, known as in allele DPB1*01:01, allele DPB1*01:02, allele DPB1*09:02, allele DPB1*11:01, allele DPB1*13:01, allele DPB1*15:01, allele DPB1*20:02, allele DPB1*21:02, allele DPB1*25:02, allele DPB1*26:01, allele DPB1*27:01, allele DPB1*39:01, allele DPB1*40:01, allele DPB1*49:01, allele DPB1*53:01, allele DPB1*65:01, allele DPB1*74:01, allele DPB1*85:01, allele DPB1*89:01 and allele DPB1*96:01;, features a modification of the amino acid from F to Y at position 64.
+The protein's natural variant, known as in allele DPB1*01:02, allele DPB1*02:01, allele DPB1*02:02, allele DPB1*02:03, allele DPB1*03:01, allele DPB1*04:02, allele DPB1*04:03, allele DPB1*05:01, allele DPB1*05:02, allele DPB1*06:01, allele DPB1*06:02, allele DPB1*08:01, allele DPB1*08:02, allele DPB1*09:01, allele DPB1*10:01, allele DPB1*10:02, allele DPB1*11:02, allele DPB1*14:01, allele DPB1*14:02, allele DPB1*15:02, allele DPB1*16:01, allele DPB1*16:02, allele DPB1*17:01, allele DPB1*17:02, allele DPB1*18:01, allele DPB1*18:02, allele DPB1*19:01, allele DPB1*19:02, allele DPB1*21:01, allele DPB1*20:01, allele DPB1*22:01, allele DPB1*22:02, allele DPB1*23:01, allele DPB1*25:01, allele DPB1*26:02, allele DPB1*29:01, allele DPB1*30:01, allele DPB1*32:01, allele DPB1*34:01, allele DPB1*35:01, allele DPB1*36:01, allele DPB1*37:01, allele DPB1*38:01, allele DPB1*41:01, allele DPB1*44:01, allele DPB1*45:01, allele DPB1*46:01, allele DPB1*47:01, allele DPB1*48:01, allele DPB1*50:01, allele DPB1*52:01, allele DPB1*54:01, allele DPB1*55:01, allele DPB1*57:01, allele DPB1*58:01, allele DPB1*59:01, allele DPB1*60:01, allele DPB1*62:01, allele DPB1*63:01, allele DPB1*67:01, allele DPB1*68:01, allele DPB1*69:01, allele DPB1*70:01, allele DPB1*71:01, allele DPB1*73:01, allele DPB1*75:01, allele DPB1*77:01, allele DPB1*78:01, allele DPB1*79:01, allele DPB1*80:01, allele DPB1*82:01, allele DPB1*83:01, allele DPB1*84:01, allele DPB1*86:01, allele DPB1*87:01, allele DPB1*88:01, allele DPB1*91:01, allele DPB1*93:01, allele DPB1*94:01, allele DPB1*95:01, allele DPB1*97:01 and allele DPB1*98:01;, features a modification of the amino acid from A to V at position 65.
+The protein's natural variant, known as in allele DPB1*24:02;, features a modification of the amino acid from D to Y at position 68.
+The protein's natural variant, known as in allele DPB1*97:01;, features a modification of the amino acid from G to W at position 72.
+The protein's natural variant, known as in allele DPB1*02:01, allele DPB1*03:01, allele DPB1*04:02, allele DPB1*05:02, allele DPB1*06:01, allele DPB1*06:02, allele DPB1*08:01, allele DPB1*09:01, allele DPB1*10:01, allele DPB1*10:02, allele DPB1*11:02, allele DPB1*14:01, allele DPB1*14:02, allele DPB1*16:01, allele DPB1*16:02, allele DPB1*17:01, allele DPB1*18:01, allele DPB1*18:01, allele DPB1*18:02, allele DPB1*19:02, allele DPB1*20:01, allele DPB1*22:02, allele DPB1*25:01, allele DPB1*25:02, allele DPB1*26:02, allele DPB1*28:01, allele DPB1*29:01, allele DPB1*32:01, allele DPB1*35:01, allele DPB1*37:01, allele DPB1*41:01, allele DPB1*44:01, allele DPB1*45:01, allele DPB1*46:01, allele DPB1*48:01, allele DPB1*49:01, allele DPB1*50:01, allele DPB1*51:01, allele DPB1*53:01, allele DPB1*57:01, allele DPB1*59:01, allele DPB1*60:01, allele DPB1*68:01, allele DPB1*69:01, allele DPB1*70:01, allele DPB1*73:01, allele DPB1*75:01, allele DPB1*76:01, allele DPB1*77:01, allele DPB1*78:01, allele DPB1*79:01, allele DPB1*80:01, allele DPB1*81:01, allele DPB1*82:01, allele DPB1*83:01, allele DPB1*86:01, allele DPB1*88:01, allele DPB1*91:01, allele DPB1*92:01, allele DPB1*93:01, allele DPB1*94:01 and allele DPB1*98:01;, features a modification of the amino acid from A to D at position 84.
+The protein's natural variant, known as in allele DPB1*01:02, allele DPB1*02:02, allele DPB1*02:03, allele DPB1*05:01, allele DPB1*08:02, allele DPB1*17:02, allele DPB1*19:01, allele DPB1*21:01, allele DPB1*22:01, allele DPB1*24:01, allele DPB1*30:01, allele DPB1*36:01, allele DPB1*38:01, allele DPB1*47:01, allele DPB1*54:01, allele DPB1*84:01 and allele DPB1*97:01;, features a modification of the amino acid from A to E at position 84.
+The protein's natural variant, known as in allele DPB1*02:01, allele DPB1*03:01, allele DPB1*04:02, allele DPB1*05:02, allele DPB1*06:01, allele DPB1*06:02, allele DPB1*08:01, allele DPB1*09:01, allele DPB1*10:01, allele DPB1*10:02, allele DPB1*11:02, allele DPB1*14:01, allele DPB1*14:02, allele DPB1*16:01, allele DPB1*16:02, allele DPB1*17:01, allele DPB1*18:01, allele DPB1*18:02, allele DPB1*19:02, allele DPB1*20:01, allele DPB1*22:02, allele DPB1*25:01, allele DPB1*25:02, allele DPB1*26:02, allele DPB1*28:01, allele DPB1*29:01, allele DPB1*32:01, allele DPB1*35:01, allele DPB1*37:01, allele DPB1*41:01, allele DPB1*44:01, allele DPB1*45:01, allele DPB1*46:01, allele DPB1*48:01, allele DPB1*49:01, allele DPB1*50:01, allele DPB1*51:01, allele DPB1*53:01, allele DPB1*57:01, allele DPB1*59:01, allele DPB1*60:01, allele DPB1*68:01, allele DPB1*69:01, allele DPB1*70:01, allele DPB1*73:01, allele DPB1*75:01, allele DPB1*76:01, allele DPB1*77:01, allele DPB1*78:01, allele DPB1*79:01, allele DPB1*80:01, allele DPB1*81:01, allele DPB1*82:01, allele DPB1*83:01, allele DPB1*84:01, allele DPB1*86:01, allele DPB1*88:01, allele DPB1*91:01, allele DPB1*92:01, allele DPB1*93:01, allele DPB1*94:01 and allele DPB1*98:01;, features a modification of the amino acid from A to E at position 85.
+The protein's natural variant, known as in allele DPB1*03:01, allele DPB1*05:02, allele DPB1*06:01, allele DPB1*09:01, allele DPB1*10:02, allele DPB1*14:01, allele DPB1*14:02, allele DPB1*17:01, allele DPB1*20:01, allele DPB1*22:02, allele DPB1*29:01, allele DPB1*35:01, allele DPB1*44:01, allele DPB1*46:01, allele DPB1*50:01, allele DPB1*57:01, allele DPB1*69:01, allele DPB1*70:01, allele DPB1*76:01, allele DPB1*78:01, allele DPB1*80:01, allele DPB1*86:01, allele DPB1*88:01, allele DPB1*91:01, allele DPB1*92:01 and allele DPB1*98:01;, features a modification of the amino acid from E to D at position 86.
+The protein's natural variant, known as in allele DPB1*32:01;, features a modification of the amino acid from E to V at position 86.
+The protein's natural variant, known as in allele DPB1*02:03;, features a modification of the amino acid from N to H at position 89.
+The protein's natural variant, known as in allele DPB1*96:01;, features a modification of the amino acid from D to H at position 93.
+The protein's natural variant, known as allele DPB1*41:01 and allele DPB1*83:01;, features a modification of the amino acid from I to F at position 94.
+The protein's natural variant, known as in allele DPB1*03:01, allele DPB1*03:02, allele DPB1*05:02, allele DPB1*06:01, allele DPB1*10:02, allele DPB1*11:01, allele DPB1*14:01, allele DPB1*14:02, allele DPB1*15:01, allele DPB1*17:02, allele DPB1*20:01, allele DPB1*22:02, allele DPB1*25:01, allele DPB1*28:01, allele DPB1*29:01, allele DPB1*31:01, allele DPB1*34:01, allele DPB1*44:01, allele DPB1*45:01, allele DPB1*50:01, allele DPB1*52:01, allele DPB1*56:01, allele DPB1*57:01, allele DPB1*59:01, allele DPB1*67:01, allele DPB1*69:01, allele DPB1*70:01, allele DPB1*72:01, allele DPB1*73:01, allele DPB1*74:01, allele DPB1*76:01, allele DPB1*78:01, allele DPB1*87:01, allele DPB1*91:01, allele DPB1*92:01 and allele DPB1*95:01;, features a modification of the amino acid from I to L at position 94.
+The protein's natural variant, known as in allele DPB1*60:01;, features a modification of the amino acid from I to N at position 94.
+The protein's natural variant, known as in allele DPB1*02:01, allele DPB1*02:02, allele DPB1*02:03, allele DPB1*04:03, allele DPB1*06:01, allele DPB1*08:01, allele DPB1*08:02, allele DPB1*09:01, allele DPB1*09:02, allele DPB1*10:01, allele DPB1*11:02, allele DPB1*13:01, allele DPB1*13:02, allele DPB1*16:01, allele DPB1*16:02, allele DPB1*17:01, allele DPB1*18:02, allele DPB1*19:01, allele DPB1*20:02, allele DPB1*21:01, allele DPB1*22:01, allele DPB1*26:02, allele DPB1*29:01, allele DPB1*30:01, allele DPB1*32:01, allele DPB1*33:01, allele DPB1*37:01, allele DPB1*41:01, allele DPB1*44:01, allele DPB1*46:01, allele DPB1*47:01, allele DPB1*48:01, allele DPB1*54:01, allele DPB1*55:01, allele DPB1*58:01, allele DPB1*71:01, allele DPB1*81:01, allele DPB1*86:01, allele DPB1*88:01, allele DPB1*93:01 and allele DPB1*95:01;, features a modification of the amino acid from K to E at position 98.
+The protein's natural variant, known as in allele DPB1*11:01, allele DPB1*15:01, allele DPB1*69:01 and allele DPB1*74:01;, features a modification of the amino acid from K to R at position 98.
+The protein's natural variant, known as in allele DPB1*94:01;, features a modification of the amino acid from R to W at position 99.
+The protein's natural variant, known as in allele DPB1*31:01 and allele DPB1*34:01;, features a modification of the amino acid from V to L at position 101.
+The protein's natural variant, known as in allele DPB1*78:01;, features a modification of the amino acid from P to L at position 102.
+The protein's natural variant, known as in allele DPB1*08:02, allele DPB1*09:02, allele DPB1*13:01, allele DPB1*13:02 and allele DPB1*19:01;, features a modification of the amino acid from M to I at position 105.
+The protein's natural variant, known as in allele DPB1*01:01, allele DPB1*03:01, allele DPB1*05:02, allele DPB1*08:01, allele DPB1*09:01, allele DPB1*10:01, allele DPB1*14:01, allele DPB1*14:02, allele DPB1*17:02, allele DPB1*21:02, allele DPB1*22:02, allele DPB1*25:01, allele DPB1*25:02, allele DPB1*26:01, allele DPB1*29:01, allele DPB1*35:01, allele DPB1*37:01, allele DPB1*44:01, allele DPB1*45:01, allele DPB1*50:01, allele DPB1*52:01, allele DPB1*54:01, allele DPB1*56:01, allele DPB1*57:01, allele DPB1*65:01, allele DPB1*67:01, allele DPB1*68:01, allele DPB1*70:01, allele DPB1*73:01, allele DPB1*75:01, allele DPB1*76:01, allele DPB1*78:01, allele DPB1*79:01, allele DPB1*84:01, allele DPB1*88:01, allele DPB1*90:01 and allele DPB1*92:01;, features a modification of the amino acid from M to V at position 105.
+The protein's natural variant, known as in allele DPB1*01:01, allele DPB1*03:01, allele DPB1*03:02, allele DPB1*04:03, allele DPB1*05:01, allele DPB1*05:02, allele DPB1*06:01, allele DPB1*08:01, allele DPB1*08:02, allele DPB1*09:01, allele DPB1*09:02, allele DPB1*10:01, allele DPB1*11:01, allele DPB1*11:01, allele DPB1*13:01, allele DPB1*13:02, allele DPB1*13:02, allele DPB1*14:01, allele DPB1*14:02, allele DPB1*16:01, allele DPB1*17:01, allele DPB1*17:02, allele DPB1*19:01, allele DPB1*21:01, allele DPB1*21:01, allele DPB1*21:02, allele DPB1*21:02, allele DPB1*20:01, allele DPB1*22:01, allele DPB1*25:01, allele DPB1*25:02, allele DPB1*26:01, allele DPB1*27:01, allele DPB1*29:01, allele DPB1*30:01, allele DPB1*31:01, allele DPB1*35:01, allele DPB1*36:01, allele DPB1*37:01, allele DPB1*38:01, allele DPB1*44:01, allele DPB1*45:01, allele DPB1*50:01, allele DPB1*52:01, allele DPB1*54:01, allele DPB1*55:01, allele DPB1*56:01, allele DPB1*57:01, allele DPB1*58:01, allele DPB1*63:01, allele DPB1*65:01, allele DPB1*67:01, allele DPB1*68:01, allele DPB1*69:01, allele DPB1*70:01, allele DPB1*76:01, allele DPB1*78:01, allele DPB1*79:01, allele DPB1*84:01, allele DPB1*85:01, allele DPB1*87:01, allele DPB1*88:01, allele DPB1*89:01, allele DPB1*90:01, allele DPB1*91:01, allele DPB1*92:01, allele DPB1*93:01, allele DPB1*97:01 and allele DPB1*98:01;, features a modification of the amino acid from G to D at position 113.
+The protein's natural variant, known as in allele DPB1*22:02; requires 2 nucleotide substitutions, features a modification of the amino acid from G to N at position 113.
+The protein's natural variant, known as in allele DPB1*15:01, allele DPB1*18:01, allele DPB1*28:01, allele DPB1*34:01, allele DPB1*40:01, allele DPB1*53:01, allele DPB1*62:01 and allele DPB1*74:01;, features a modification of the amino acid from G to V at position 113.
+The protein's natural variant, known as in allele DPB1*01:01, allele DPB1*03:01, allele DPB1*03:02, allele DPB1*04:03, allele DPB1*05:01, allele DPB1*05:02, allele DPB1*06:01, allele DPB1*08:01, allele DPB1*08:02, allele DPB1*09:01, allele DPB1*09:02, allele DPB1*10:01, allele DPB1*11:01, allele DPB1*13:01, allele DPB1*13:02, allele DPB1*14:01, allele DPB1*14:02, allele DPB1*16:01, allele DPB1*17:01, allele DPB1*17:02, allele DPB1*19:01, allele DPB1*21:01, allele DPB1*21:02, allele DPB1*20:01, allele DPB1*22:01, allele DPB1*22:02, allele DPB1*25:01, allele DPB1*25:02, allele DPB1*26:01, allele DPB1*27:01, allele DPB1*29:01, allele DPB1*30:01, allele DPB1*31:01, allele DPB1*35:01, allele DPB1*36:01, allele DPB1*37:01, allele DPB1*38:01, allele DPB1*44:01, allele DPB1*45:01, allele DPB1*50:01, allele DPB1*52:01, allele DPB1*54:01, allele DPB1*55:01, allele DPB1*56:01, allele DPB1*57:01, allele DPB1*58:01, allele DPB1*63:01, allele DPB1*65:01, allele DPB1*67:01, allele DPB1*68:01, allele DPB1*69:01, allele DPB1*70:01, allele DPB1*76:01, allele DPB1*78:01, allele DPB1*79:01, allele DPB1*84:01, allele DPB1*85:01, allele DPB1*87:01, allele DPB1*88:01, allele DPB1*89:01, allele DPB1*90:01, allele DPB1*91:01, allele DPB1*92:01, allele DPB1*93:01, allele DPB1*97:01 and allele DPB1*98:01;, features a modification of the amino acid from G to E at position 114.
+The protein's natural variant, known as in allele DPB1*01:01, allele DPB1*03:01, allele DPB1*03:02, allele DPB1*04:03, allele DPB1*05:01, allele DPB1*05:02, allele DPB1*06:01, allele DPB1*08:01, allele DPB1*08:02, allele DPB1*09:01, allele DPB1*09:02, allele DPB1*10:01, allele DPB1*11:01, allele DPB1*13:01, allele DPB1*13:02, allele DPB1*14:01, allele DPB1*14:02, allele DPB1*16:01, allele DPB1*17:01, allele DPB1*17:02, allele DPB1*19:01, allele DPB1*21:01, allele DPB1*21:02, allele DPB1*20:01, allele DPB1*22:01, allele DPB1*22:02, allele DPB1*25:01, allele DPB1*25:02, allele DPB1*26:01, allele DPB1*27:01, allele DPB1*29:01, allele DPB1*30:01, allele DPB1*31:01, allele DPB1*35:01, allele DPB1*36:01, allele DPB1*37:01, allele DPB1*38:01, allele DPB1*44:01, allele DPB1*45:01, allele DPB1*50:01, allele DPB1*52:01, allele DPB1*54:01, allele DPB1*55:01, allele DPB1*56:01, allele DPB1*57:01, allele DPB1*58:01, allele DPB1*63:01, allele DPB1*65:01, allele DPB1*67:01, allele DPB1*68:01, allele DPB1*69:01, allele DPB1*70:01, allele DPB1*76:01, allele DPB1*78:01, allele DPB1*79:01, allele DPB1*84:01, allele DPB1*85:01, allele DPB1*87:01, allele DPB1*88:01, allele DPB1*89:01, allele DPB1*90:01, allele DPB1*91:01, allele DPB1*92:01, allele DPB1*93:01, allele DPB1*97:01 and allele DPB1*98:01;, features a modification of the amino acid from P to A at position 115.
+The protein's natural variant, known as in allele DPB1*01:01, allele DPB1*03:01, allele DPB1*03:02, allele DPB1*04:03, allele DPB1*05:01, allele DPB1*05:02, allele DPB1*06:01, allele DPB1*08:01, allele DPB1*08:02, allele DPB1*09:01, allele DPB1*09:02, allele DPB1*10:01, allele DPB1*11:01, allele DPB1*13:01, allele DPB1*13:02, allele DPB1*14:01, allele DPB1*14:02, allele DPB1*16:01, allele DPB1*17:01, allele DPB1*17:02, allele DPB1*19:01, allele DPB1*21:01, allele DPB1*21:02, allele DPB1*20:01, allele DPB1*22:01, allele DPB1*22:02, allele DPB1*25:01, allele DPB1*25:02, allele DPB1*26:01, allele DPB1*27:01, allele DPB1*29:01, allele DPB1*30:01, allele DPB1*31:01, allele DPB1*35:01, allele DPB1*36:01, allele DPB1*37:01, allele DPB1*38:01, allele DPB1*44:01, allele DPB1*45:01, allele DPB1*50:01, allele DPB1*52:01, allele DPB1*54:01, allele DPB1*55:01, allele DPB1*56:01, allele DPB1*58:01, allele DPB1*63:01, allele DPB1*65:01, allele DPB1*67:01, allele DPB1*68:01, allele DPB1*69:01, allele DPB1*70:01, allele DPB1*76:01, allele DPB1*78:01, allele DPB1*79:01, allele DPB1*84:01, allele DPB1*85:01, allele DPB1*87:01, allele DPB1*88:01, allele DPB1*89:01, allele DPB1*90:01, allele DPB1*91:01, allele DPB1*92:01, allele DPB1*93:01, allele DPB1*97:01 and allele DPB1*98:01;, features a modification of the amino acid from M to V at position 116.
+The protein's natural variant, known as in allele DPB1*82:01 and allele DPB1*85:01;, features a modification of the amino acid from R to H at position 120.
+The protein's natural variant, known as in allele DPB1*01:01, allele DPB1*03:01, allele DPB1*05:01, allele DPB1*05:02, allele DPB1*06:01, allele DPB1*09:01, allele DPB1*09:02, allele DPB1*13:01, allele DPB1*14:01, allele DPB1*15:01, allele DPB1*18:01, allele DPB1*19:01, allele DPB1*20:01, allele DPB1*26:01, allele DPB1*45:01 and allele DPB1*85:01;, features a modification of the amino acid from R to K at position 125.
+The protein's natural variant, known as in allele DPB1*01:01, allele DPB1*03:01, allele DPB1*05:01, allele DPB1*05:02, allele DPB1*06:01, allele DPB1*09:01, allele DPB1*09:02, allele DPB1*13:01, allele DPB1*14:01, allele DPB1*15:01, allele DPB1*18:01, allele DPB1*19:01, allele DPB1*20:01, allele DPB1*26:01, allele DPB1*45:01 and allele DPB1*85:01;, features a modification of the amino acid from T to I at position 199.
+The protein's natural variant, known as in allele DPB1*04:02;, features a modification of the amino acid from L to M at position 207.
+The protein's natural variant, known as in allele DPB1*01:01;, features a modification of the amino acid from R to Q at position 223.
+The protein's natural variant, known as in allele DPB1*05:01 and allele DPB1*19:01;, features a modification of the amino acid from V to M at position 234.
+The protein's natural variant, known as in allele DPB1*15:01;, features a modification of the amino acid from I to T at position 244.
+The natural variant of this protein is characterized by an amino acid alteration from E to K at position 56.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from R to Q at position 633.
+The protein's natural variant, known as in ALUNC; affects binding to thyroid hormone receptor; Markedly diminished histone demethylase activity;, features a modification of the amino acid from D to N at position 1012.
+The protein's natural variant, known as in ALUNC;, features a modification of the amino acid from T to A at position 1022.
+The protein's natural variant, known as in ALUNC;, features a modification of the amino acid from V to D at position 1136.
+The protein's natural variant, known as in GEFSP9; loss of function mutation;, features a modification of the amino acid from V to E at position 216.
+The protein's natural variant, known as in GEFSP9;, features a modification of the amino acid from G to R at position 226.
+The protein's natural variant, known as in EPVB6D;, features a modification of the amino acid from P to L at position 87.
+The protein's natural variant, known as in EPVB6D; decreased expression at the mRNA level; undetectable at the protein level in patient's fibroblasts;, features a modification of the amino acid from L to P at position 175.
+The protein's natural variant, known as in EPVB6D;, features a modification of the amino acid from R to Q at position 241.
+The protein's natural variant, known as in HMLR2; unknown pathological significance;, features a modification of the amino acid from V to G at position 92.
+The protein's natural variant, known as in HMLR2; unknown pathological significance;, features a modification of the amino acid from R to L at position 99.
+The protein's natural variant, known as in HMLR2; unknown pathological significance;, features a modification of the amino acid from F to L at position 218.
+The protein's natural variant, known as in HMLR2; results in severe functional decrease in peroxisome biogenesis;, features a modification of the amino acid from P to L at position 274.
+The protein's natural variant, known as in PBD-CG4; disease phenotype includes hearing loss, visual impairment, enamel dysplasia microcephaly with deep white matter changes and developmental delay;, features a modification of the amino acid from G to V at position 413.
+The protein's natural variant, known as in PBD-CG4;, features a modification of the amino acid from L to P at position 534.
+The protein's natural variant, known as in HMLR2;, features a modification of the amino acid from T to I at position 572.
+The protein's natural variant, known as in HMLR2; unknown pathological significance; results in mild functional decrease in peroxisome biogenesis;, features a modification of the amino acid from R to Q at position 601.
+The protein's natural variant, known as in HMLR2; results in mild functional decrease in peroxisome biogenesis;, features a modification of the amino acid from R to W at position 644.
+The protein's natural variant, known as in PBD4A;, features a modification of the amino acid from R to Q at position 812.
+The protein's natural variant, known as in PBD4A; atypical;, features a modification of the amino acid from R to W at position 812.
+The protein's natural variant, known as in PBD-CG4;, features a modification of the amino acid from N to T at position 849.
+The protein's natural variant, known as in PBD-CG4;, features a modification of the amino acid from R to Q at position 860.
+The protein's natural variant, known as in PBD-CG4;, features a modification of the amino acid from R to W at position 860.
+The protein's natural variant, known as in HMLR2;, features a modification of the amino acid from C to F at position 905.
+The protein's natural variant, known as in YOBELN; unknown pathological significance;, features a modification of the amino acid from R to W at position 244.
+The protein's natural variant, known as in YOBELN; unknown pathological significance, features a modification of the amino acid from R to G at position 299.
+The protein's natural variant, known as in YOBELN; unknown pathological significance;, features a modification of the amino acid from A to V at position 327.
+The protein's natural variant, known as in YOBELN; unknown pathological significance;, features a modification of the amino acid from D to V at position 491.
+The protein's natural variant, known as in YOBELN; unknown pathological significance;, features a modification of the amino acid from R to Q at position 673.
+The protein's natural variant, known as in YOBELN; unknown pathological significance; fails to rescue knockdown-induced defects of neuronal function in a Drosophila model system;, features a modification of the amino acid from S to L at position 778.
+The protein's natural variant, known as in YOBELN; unknown pathological significance, features a modification of the amino acid from P to A at position 852.
+The protein's natural variant, known as in microcytic anemia, features a modification of the amino acid from G to R at position 185.
+The protein's natural variant, known as in clone ADES3/2, features a modification of the amino acid from E to D at position 126.
+The protein's natural variant, known as in clone ADES3/2, features a modification of the amino acid from S to G at position 129.
+The protein's natural variant, known as in minor form, features a modification of the amino acid from E to V at position 115.
+The protein's natural variant, known as in minor form, features a modification of the amino acid from K to A at position 172.
+The protein's natural variant, known as in minor form, features a modification of the amino acid from K to I at position 185.
+The protein's natural variant, known as in minor form, features a modification of the amino acid from LG to RA at position 236.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from P to S at position 152.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from C to S at position 243.
+The protein's natural variant, known as found in a renal cell carcinoma sample; somatic mutation, features a modification of the amino acid from H to L at position 590.
+The protein's natural variant, known as in OL78, features a modification of the amino acid from Q to E at position 23.
+The protein's natural variant, known as in OL78, features a modification of the amino acid from D to E at position 48.
+The protein's natural variant, known as in FODH;, features a modification of the amino acid from G to R at position 60.
+The protein's natural variant, known as in FODH, features a modification of the amino acid from S to F at position 136.
+The protein's natural variant, known as in FODH;, features a modification of the amino acid from G to R at position 168.
+The protein's natural variant, known as in a patient with focal dermal hypoplasia also carrying a frameshift mutation; uncertain pathological significance;, features a modification of the amino acid from R to C at position 228.
+The protein's natural variant, known as in FODH, features a modification of the amino acid from H to Y at position 252.
+The protein's natural variant, known as in FODH, features a modification of the amino acid from V to E at position 258.
+The protein's natural variant, known as in FODH, features a modification of the amino acid from S to L at position 297.
+The protein's natural variant, known as in FODH, features a modification of the amino acid from L to R at position 331.
+The protein's natural variant, known as in FODH, features a modification of the amino acid from H to L at position 341.
+The protein's natural variant, known as in FODH, features a modification of the amino acid from E to V at position 361.
+The protein's natural variant, known as in FODH, features a modification of the amino acid from R to G at position 365.
+The protein's natural variant, known as in FODH, features a modification of the amino acid from R to Q at position 365.
+The protein's natural variant, known as in FODH, features a modification of the amino acid from A to P at position 374.
+The protein's natural variant, known as in FODH, features a modification of the amino acid from C to R at position 385.
+The protein's natural variant, known as in FODH, features a modification of the amino acid from C to Y at position 385.
+The protein's natural variant, known as in FODH, features a modification of the amino acid from W to R at position 439.
+The natural variant of this protein is characterized by an amino acid alteration from N to K at position 169.
+The natural variant of this protein is characterized by an amino acid alteration from G to R at position 465.
+The natural variant of this protein is characterized by an amino acid alteration from T to M at position 512.
+The protein's natural variant, known as in a renal chromophobe sample; somatic mutation, features a modification of the amino acid from V to L at position 105.
+The protein's natural variant, known as in IGF1RES; has decreased IGF1R function;, features a modification of the amino acid from R to Q at position 138.
+The protein's natural variant, known as in IGF1RES; has decreased IGF1R function;, features a modification of the amino acid from K to N at position 145.
+The protein's natural variant, known as in IGF1RES; significant decrease in IGF1-induced DNA synthesis and AKT1 phosphorylation in patient fibroblasts, features a modification of the amino acid from N to Y at position 359.
+The protein's natural variant, known as in IGF1RES; leads to failure of processing of the IGF1R proreceptor to mature IGF1R;, features a modification of the amino acid from R to Q at position 739.
+The protein's natural variant, known as in IGF1RES; significant decrease in IGF1-induced DNA synthesis and AKT1 phosphorylation in patient fibroblasts, features a modification of the amino acid from Y to C at position 865.
+The protein's natural variant, known as in IGF1RES; significant decrease in IGF1-induced DNA synthesis and AKT1 phosphorylation in patient fibroblasts, features a modification of the amino acid from R to S at position 1256.
+The protein's natural variant, known as in IGF1RES; unknown pathological significance; significant decrease in IGF1-induced DNA synthesis; significant increase in IGF1-induced AKT1 phosphorylation in patient fibroblasts;, features a modification of the amino acid from R to C at position 1337.
+The protein's natural variant, known as in a lung squamous cell carcinoma sample; somatic mutation, features a modification of the amino acid from A to V at position 1347.
+The protein's natural variant, known as in NPHP20; unknown pathological significance; no effect on localization at the spindle pole; no effect on interaction with WDR62; no effect on interaction with MAPK9;, features a modification of the amino acid from R to Q at position 544.
+The protein's natural variant, known as in PTORCH1;, features a modification of the amino acid from F to S at position 219.
+The natural variant of this protein is characterized by an amino acid alteration from R to Q at position 66.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 143.
+The natural variant of this protein is characterized by an amino acid alteration from T to I at position 187.
+The natural variant of this protein is characterized by an amino acid alteration from I to T at position 201.
+The natural variant of this protein is characterized by an amino acid alteration from V to A at position 8.
+The protein's natural variant, known as in ALGS2;, features a modification of the amino acid from C to Y at position 444.
+The protein's natural variant, known as in strain: Isolate 5294, features a modification of the amino acid from H to G at position 15.
+The protein's natural variant, known as in allotype T61, features a modification of the amino acid from K to N at position 88.
+The protein's natural variant, known as in allotype T61, features a modification of the amino acid from D to E at position 94.
+The protein's natural variant, known as in allotype T61, features a modification of the amino acid from TVDQLTQN to YLNRLSQS at position 108.
+The protein's natural variant, known as in allotype T63, features a modification of the amino acid from S to T at position 110.
+The protein's natural variant, known as in MRD50; unknown pathological significance;, features a modification of the amino acid from D to N at position 112.
+The protein's natural variant, known as in MRD50; unknown pathological significance;, features a modification of the amino acid from K to E at position 450.
+The protein's natural variant, known as in MRD50; unknown pathological significance;, features a modification of the amino acid from A to V at position 475.
+The protein's natural variant, known as in NS12; increased MAPK signaling;, features a modification of the amino acid from G to V at position 23.
+The protein's natural variant, known as in NS12; increased MAPK signaling, features a modification of the amino acid from G to GGGG at position 24.
+The protein's natural variant, known as in NS12; increased MAPK signaling; results in craniofacial patterning defects when expressed in zebrafish, features a modification of the amino acid from G to GGVG at position 26.
+The protein's natural variant, known as in NS12; decreased GAP-stimulated GTPase activity leading to an accumulation of RRAS2 in its GTP-bound active state; increased MAPK signaling; loss of interaction with RASSF5;, features a modification of the amino acid from A to T at position 70.
+The protein's natural variant, known as in NS12; associated in cis with C-75; increased MAPK signaling; results in craniofacial patterning defects when expressed in zebrafish; results in craniofacial patterning defects in zebrafish when associated with C-75, features a modification of the amino acid from Q to H at position 72.
+The protein's natural variant, known as in NS12; also found as somatic mutation in ovarian cancer; increased MAPK signaling; results in craniofacial patterning defects when expressed in zebrafish;, features a modification of the amino acid from Q to L at position 72.
+The protein's natural variant, known as likely benign variant; associated in cis with H-72 in a patient with Noonan syndrome; has no effect on MAPK signaling; has no effect on craniofacial patterning when expressed in zebrafish; results in craniofacial patterning defects in zebrafish when associated with H-72, features a modification of the amino acid from F to C at position 75.
+The protein's natural variant, known as in allele 14B; temperature sensitive, features a modification of the amino acid from E to K at position 241.
+The protein's natural variant, known as in allele 33B; temperature sensitive, features a modification of the amino acid from V to M at position 431.
+The protein's natural variant, known as in strain: W, features a modification of the amino acid from G to E at position 47.
+The protein's natural variant, known as in strain: W, features a modification of the amino acid from N to H at position 76.
+The protein's natural variant, known as in strain: W, features a modification of the amino acid from E to Q at position 106.
+The protein's natural variant, known as in DIDDF; unknown pathological significance, features a modification of the amino acid from E to K at position 644.
+The protein's natural variant, known as in DIDDF; unknown pathological significance, features a modification of the amino acid from R to Q at position 788.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from E to D at position 22.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from L to V at position 15.
+The protein's natural variant, known as in allele HERV-K18.1 and allele HERV-K18.3, features a modification of the amino acid from C to Y at position 97.
+The protein's natural variant, known as in allele HERV-K18.3, features a modification of the amino acid from V to I at position 272.
+The protein's natural variant, known as in allele HERV-K18.3, features a modification of the amino acid from V to I at position 348.
+The protein's natural variant, known as in allele HERV-K18.3, features a modification of the amino acid from V to I at position 534.
+The protein's natural variant, known as in SD; frequent variant in Finland; alters intracellular localization, only partially targeted to lysosomes and mainly detected in LAMP1-negative vesicles and in the Golgi apparatus; completely devoid of L-aspartate and L-glutamate transport activity, but retains appreciable H(+)-coupled sialic acid and nitrate transporter activity;, features a modification of the amino acid from R to C at position 39.
+The protein's natural variant, known as in SD; alters intracellular localization, only partially targeted to lysosomes and mainly detected in LAMP1-negative vesicles and in the Golgi apparatus; completely devoid of L-aspartate and L-glutamate transporter activity, but retains appreciable H(+)-coupled sialic acid transporter activity;, features a modification of the amino acid from K to E at position 136.
+The protein's natural variant, known as in ISSD; alters intracellular localization, only partially targeted to lysosomes and mainly detected in LAMP1-negative vesicles and in the Golgi apparatus; abolishes H(+)-coupled sialic acid transporter activity; has normal L-aspartate and L-glutamate transporter activity;, features a modification of the amino acid from H to R at position 183.
+The protein's natural variant, known as in ISSD; some patients may manifest a milder phenotype consistent with Salla disease; markedly decreases H(+)-coupled sialic acid transporter activity; abolishes L-aspartate and L-glutamate transporter activity;, features a modification of the amino acid from G to E at position 328.
+The protein's natural variant, known as in ISSD; does not affect intracellular localization, targeted to lysosomes; abolishes H(+)-coupled sialic acid transporter activity; abolishes L-aspartate and L-glutamate transporter activity;, features a modification of the amino acid from P to R at position 334.
+The protein's natural variant, known as in ISSD; abolishes H(+)-coupled sialic acid transporter activity; abolishes L-aspartate and L-glutamate transporter activity;, features a modification of the amino acid from G to V at position 371.
+The protein's natural variant, known as in strain: Isolate 3, features a modification of the amino acid from I to T at position 17.
+The protein's natural variant, known as in strain: Isolate 3, features a modification of the amino acid from W to G at position 43.
+The protein's natural variant, known as in strain: Isolate 3, features a modification of the amino acid from Q to E at position 55.
+The protein's natural variant, known as in strain: Isolate 3, features a modification of the amino acid from M to L at position 100.
+The protein's natural variant, known as in strain: Isolate 3, features a modification of the amino acid from L to V at position 140.
+The protein's natural variant, known as in strain: Isolate 3, features a modification of the amino acid from H to R at position 153.
+The protein's natural variant, known as in strain: Isolate 3, features a modification of the amino acid from I to V at position 165.
+The protein's natural variant, known as in strain: Isolate 3, features a modification of the amino acid from M to V at position 199.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from N to S at position 203.
+The protein's natural variant, known as in MDDGA11; affects subcellular localization;, features a modification of the amino acid from G to E at position 247.
+The protein's natural variant, known as in MDDGA11;, features a modification of the amino acid from V to G at position 252.
+The protein's natural variant, known as in MDDGA11; affects subcellular localization;, features a modification of the amino acid from V to M at position 268.
+The protein's natural variant, known as in MDDGA11; does not affect subcellular localization;, features a modification of the amino acid from R to P at position 292.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from D to H at position 415.
+The protein's natural variant, known as in MMDS5; unknown pathological significance;, features a modification of the amino acid from E to K at position 87.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from H to Q at position 19.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from P to S at position 21.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from C to Y at position 36.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from D to G at position 42.
+The protein's natural variant, known as in OCA1A, features a modification of the amino acid from S to G at position 44.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from S to R at position 44.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from G to D at position 47.
+The protein's natural variant, known as in OCA1A, features a modification of the amino acid from G to V at position 47.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from S to L at position 50.
+The protein's natural variant, known as in OCA1;, features a modification of the amino acid from R to I at position 52.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from C to Y at position 55.
+The protein's natural variant, known as in OCA1A, features a modification of the amino acid from Q to H at position 68.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from R to Q at position 77.
+The protein's natural variant, known as in OCA1A, features a modification of the amino acid from R to RR at position 77.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from R to W at position 77.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from S to L at position 79.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from W to R at position 80.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from P to L at position 81.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from C to R at position 89.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from C to Y at position 91.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from G to R at position 97.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from G to R at position 109.
+The protein's natural variant, known as in OCA1B;, features a modification of the amino acid from P to S at position 152.
+The protein's natural variant, known as in OCA1A, features a modification of the amino acid from T to S at position 155.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from F to I at position 176.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from V to F at position 177.
+The protein's natural variant, known as in OCA1A, features a modification of the amino acid from M to L at position 179.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from H to N at position 180.
+The protein's natural variant, known as associated with SHEP3; light/dark skin;, features a modification of the amino acid from S to Y at position 192.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from I to T at position 198.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from D to N at position 199.
+The protein's natural variant, known as in OCA1A, features a modification of the amino acid from A to S at position 201.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from P to T at position 205.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from A to T at position 206.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from L to M at position 216.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from R to G at position 217.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from R to Q at position 217.
+The protein's natural variant, known as in OCA1A, features a modification of the amino acid from R to S at position 217.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from R to W at position 217.
+The protein's natural variant, known as in OCA1A, features a modification of the amino acid from W to L at position 236.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from W to S at position 236.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from R to W at position 239.
+The protein's natural variant, known as in OCA1A, features a modification of the amino acid from D to V at position 240.
+The protein's natural variant, known as in OCA1A, features a modification of the amino acid from K to T at position 243.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from G to R at position 253.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from H to Y at position 256.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from W to C at position 272.
+The protein's natural variant, known as in OCA1B and OCA1A;, features a modification of the amino acid from V to F at position 275.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from L to S at position 288.
+The protein's natural variant, known as in OCA1A, features a modification of the amino acid from C to G at position 289.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from C to R at position 289.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from E to G at position 294.
+The protein's natural variant, known as in OCA1A and OCA1B;, features a modification of the amino acid from E to K at position 294.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from R to W at position 298.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from R to H at position 299.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from R to S at position 299.
+The protein's natural variant, known as in OCA1;, features a modification of the amino acid from L to V at position 312.
+The protein's natural variant, known as in OCA1;, features a modification of the amino acid from P to R at position 313.
+The protein's natural variant, known as in OCA1A, features a modification of the amino acid from V to E at position 318.
+The protein's natural variant, known as in OCA1B;, features a modification of the amino acid from T to A at position 325.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from E to Q at position 328.
+The protein's natural variant, known as in OCA1A, features a modification of the amino acid from S to P at position 329.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from M to T at position 332.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from S to G at position 339.
+The protein's natural variant, known as in OCA1;, features a modification of the amino acid from F to L at position 340.
+The protein's natural variant, known as in OCA1A, features a modification of the amino acid from E to G at position 345.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from G to E at position 346.
+The protein's natural variant, known as in OCA1A, features a modification of the amino acid from A to E at position 355.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from A to P at position 355.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from A to V at position 355.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from S to R at position 361.
+The protein's natural variant, known as in OCA1A, features a modification of the amino acid from N to H at position 364.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from H to Y at position 367.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from M to T at position 370.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from N to T at position 371.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from N to Y at position 371.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from T to K at position 373.
+The protein's natural variant, known as in OCA1A, features a modification of the amino acid from Q to K at position 378.
+The protein's natural variant, known as in OCA1B;, features a modification of the amino acid from S to P at position 380.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from N to K at position 382.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from D to N at position 383.
+The protein's natural variant, known as in OCA1A, features a modification of the amino acid from P to A at position 384.
+The protein's natural variant, known as in OCA1B;, features a modification of the amino acid from H to D at position 390.
+The protein's natural variant, known as in OCA1A, features a modification of the amino acid from V to F at position 393.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from S to N at position 395.
+The protein's natural variant, known as in OCA1A, features a modification of the amino acid from S to R at position 395.
+The protein's natural variant, known as in OCA1A, features a modification of the amino acid from E to A at position 398.
+The protein's natural variant, known as in OCA1A, features a modification of the amino acid from E to V at position 398.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from W to L at position 400.
+The protein's natural variant, known as in OCA1B, features a modification of the amino acid from R to G at position 402.
+The protein's natural variant, known as in OCA1A, features a modification of the amino acid from R to L at position 402.
+The protein's natural variant, known as in OCA1A and OCA1B;, features a modification of the amino acid from R to S at position 403.
+The protein's natural variant, known as in OCA1A, features a modification of the amino acid from H to N at position 404.
+The protein's natural variant, known as in OCA-I;, features a modification of the amino acid from H to P at position 404.
+The protein's natural variant, known as in OCA1A, features a modification of the amino acid from R to L at position 405.
+The protein's natural variant, known as in OCA1A and OCA1B;, features a modification of the amino acid from P to L at position 406.
+The protein's natural variant, known as in OCA1A, features a modification of the amino acid from Q to H at position 408.
+The protein's natural variant, known as in OCA1A, features a modification of the amino acid from E to D at position 409.
+The protein's natural variant, known as in OCA1A, features a modification of the amino acid from A to S at position 416.
+The protein's natural variant, known as in OCA1A, features a modification of the amino acid from P to H at position 417.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from G to R at position 419.
+The protein's natural variant, known as in OCA1A and OCA1B; temperature sensitive variant;, features a modification of the amino acid from R to Q at position 422.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from S to F at position 424.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from M to K at position 426.
+The protein's natural variant, known as in OCA1A, features a modification of the amino acid from V to G at position 427.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from P to L at position 431.
+The protein's natural variant, known as in OCA1A, features a modification of the amino acid from R to I at position 434.
+The protein's natural variant, known as in OCA1A, features a modification of the amino acid from N to D at position 435.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from F to V at position 439.
+The protein's natural variant, known as in OCA1A, features a modification of the amino acid from D to G at position 444.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from G to S at position 446.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from D to N at position 448.
+The protein's natural variant, known as in OCA1A;, features a modification of the amino acid from A to D at position 490.
+The protein's natural variant, known as in strain: Isolate HS1224, features a modification of the amino acid from IL to NI at position 4.
+The protein's natural variant, known as in strain: Isolate HS1224, features a modification of the amino acid from Y to N at position 15.
+The protein's natural variant, known as in strain: Isolate HS1224, features a modification of the amino acid from T to S at position 67.
+The protein's natural variant, known as in strain: Isolate MFL-CHI1, features a modification of the amino acid from Y to H at position 107.
+The protein's natural variant, known as in strain: Isolate HS1224, features a modification of the amino acid from M to T at position 108.
+The protein's natural variant, known as in strain: Isolate HS1224, features a modification of the amino acid from A to T at position 122.
+The protein's natural variant, known as in strain: Isolate MFL-CHI1, features a modification of the amino acid from I to H at position 153.
+The protein's natural variant, known as in strain: Isolate HS1224, features a modification of the amino acid from N to T at position 158.
+The protein's natural variant, known as in F5F8D2;, features a modification of the amino acid from D to H at position 81.
+The protein's natural variant, known as in F5F8D2; interferes with protein folding;, features a modification of the amino acid from D to E at position 129.
+The protein's natural variant, known as in F5F8D2;, features a modification of the amino acid from Y to N at position 135.
+The protein's natural variant, known as in F5F8D2; interferes with protein folding;, features a modification of the amino acid from I to T at position 136.
+The protein's natural variant, known as in isozyme 2A, features a modification of the amino acid from A to T at position 3.
+The protein's natural variant, known as in isozyme 1 and isozyme 3, features a modification of the amino acid from V to I at position 5.
+The protein's natural variant, known as in isozyme 2C, features a modification of the amino acid from Q to K at position 17.
+The protein's natural variant, known as in isozyme 2D, features a modification of the amino acid from N to S at position 45.
+The protein's natural variant, known as in isozyme 1, features a modification of the amino acid from S to G at position 66.
+The protein's natural variant, known as in isozyme 1, features a modification of the amino acid from D to E at position 106.
+The protein's natural variant, known as in isozyme 1, features a modification of the amino acid from H to Q at position 116.
+The protein's natural variant, known as in isozyme 3, features a modification of the amino acid from E to Q at position 143.
+The natural variant of this protein is characterized by an amino acid alteration from S to T at position 7.
+The protein's natural variant, known as may confer susceptibility to obesity; reduces the ability to activate melanocortin receptor 4;, features a modification of the amino acid from R to G at position 236.
+The natural variant of this protein is characterized by an amino acid alteration from R to Q at position 236.
+The protein's natural variant, known as in ARCND2;, features a modification of the amino acid from N to T at position 329.
+The protein's natural variant, known as in ARCND2;, features a modification of the amino acid from R to C at position 621.
+The protein's natural variant, known as in ARCND2;, features a modification of the amino acid from R to H at position 621.
+The protein's natural variant, known as in ARCND2;, features a modification of the amino acid from Y to C at position 623.
+The protein's natural variant, known as in ARCND2;, features a modification of the amino acid from N to H at position 650.
+The protein's natural variant, known as in strain: C57BL/6J, features a modification of the amino acid from A to V at position 4.
+The protein's natural variant, known as in strain: C57BL/6J, features a modification of the amino acid from Y to F at position 6.
+The protein's natural variant, known as in strain: C57BL/6J, features a modification of the amino acid from C to F at position 7.
+The natural variant of this protein is characterized by an amino acid alteration from T to M at position 25.
+The protein's natural variant, known as in strain: BALB/cByJ and C57BL/6J; requires 2 nucleotide substitutions, features a modification of the amino acid from Q to T at position 64.
+The natural variant of this protein is characterized by an amino acid alteration from N to S at position 518.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from S to C at position 7.
+The natural variant of this protein is characterized by an amino acid alteration from S to A at position 19.
+The natural variant of this protein is characterized by an amino acid alteration from E to Q at position 41.
+The natural variant of this protein is characterized by an amino acid alteration from L to N at position 51.
+The natural variant of this protein is characterized by an amino acid alteration from P to A at position 903.
+The protein's natural variant, known as found in a renal cell carcinoma case; somatic mutation, features a modification of the amino acid from L to H at position 63.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from I to L at position 332.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from L to F at position 445.
+The protein's natural variant, known as in ALS; unknown pathological significance;, features a modification of the amino acid from R to P at position 133.
+The protein's natural variant, known as in ALS; unknown pathological significance; leads to filamentous aggregate formation;, features a modification of the amino acid from D to Y at position 141.
+The protein's natural variant, known as in Lec3 cell glycosylation mutants; loss of epimerase activity, features a modification of the amino acid from G to E at position 135.
+The natural variant of this protein is characterized by an amino acid alteration from K to R at position 274.
+The natural variant of this protein is characterized by an amino acid alteration from F to L at position 171.
+The natural variant of this protein is characterized by an amino acid alteration from L to S at position 187.
+The natural variant of this protein is characterized by an amino acid alteration from G to E at position 202.
+The natural variant of this protein is characterized by an amino acid alteration from C to S at position 295.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to H at position 200.
+The protein's natural variant, known as in SPG17 and HMN5C; does not affect protein subcellular location;, features a modification of the amino acid from N to S at position 88.
+The protein's natural variant, known as in SPG17 and HMN5C; also found in patients with hereditary motor and sensory neuropathy type 2; does not affect the function in lipid storage;, features a modification of the amino acid from S to L at position 90.
+The protein's natural variant, known as in CGL2; increases localization to nuclear envelope; no effect on its interaction with LDAF1; no rescue of aberrant lipid droplet formation in BSCL2-knockdown cells;, features a modification of the amino acid from A to P at position 212.
+The protein's natural variant, known as in Strain: Iowa) (CH-E6, features a modification of the amino acid from Q to R at position 132.
+The protein's natural variant, known as in allele ULBP6*01 and allele ULBP6*04;, features a modification of the amino acid from R to G at position 26.
+The protein's natural variant, known as in allele ULBP6*01, allele ULBP6*02 and allele ULBP6*04;, features a modification of the amino acid from M to T at position 85.
+The protein's natural variant, known as in allele ULBP6*01; affects KLRK1-binding affinity and KLRK1-mediated cytotoxic response;, features a modification of the amino acid from L to R at position 106.
+The protein's natural variant, known as in allele ULBP6*01; no effect on KLRK1-binding affinity;, features a modification of the amino acid from T to I at position 147.
+The protein's natural variant, known as in strain: 5Az; confers macrolide resistance. Grows slowly at 35 degrees Celsius and dies at 25 degrees Celsius, features a modification of the amino acid from Q to QSQ at position 67.
+The protein's natural variant, known as in 12 Bulgarian and 4 Slovakian strains; confers high resistance to erythromycin, azithromycin and josamycin and lower resistance to clarithromycin and penicillin G, features a modification of the amino acid from GTG to TPS at position 71.
+The protein's natural variant, known as in strain: 4Az; confers macrolide resistance, features a modification of the amino acid from G to C at position 69.
+The protein's natural variant, known as in strain: BM4418; confers moderate resistance to macrolides and high resistance to the ketolide telithromycin. Grows slowly, features a modification of the amino acid from G to GRQKGTG at position 71.
+The protein's natural variant, known as in CMTDIC; partial loss of activity;, features a modification of the amino acid from G to R at position 41.
+The protein's natural variant, known as in IMNEPD2; hypomorphic variant in yeast complementation assays; decreased homodimerization; does not affect localization to the cytoplasm, features a modification of the amino acid from P to T at position 167.
+The protein's natural variant, known as in CMTDIC; partial loss of activity;, features a modification of the amino acid from E to K at position 196.
+The protein's natural variant, known as in IMNEPD2; unknown pathological significance;, features a modification of the amino acid from P to L at position 213.
+The protein's natural variant, known as in IMNEPD2; unknown pathological significance, features a modification of the amino acid from F to S at position 269.
+The protein's natural variant, known as found in a patient with hereditary motor and sensory neuropathy; unknown pathological significance;, features a modification of the amino acid from E to K at position 274.
+The protein's natural variant, known as found in a patient with proximal-predominant motor neuropathy; probable disease-associated variant; loss of function, features a modification of the amino acid from D to Y at position 308.
+The protein's natural variant, known as in IMNEPD2; unknown pathological significance, features a modification of the amino acid from G to R at position 525.
+The protein's natural variant, known as in strain: DL42, features a modification of the amino acid from KA to NS at position 49.
+The protein's natural variant, known as in strain: DL42, features a modification of the amino acid from T to N at position 181.
+The protein's natural variant, known as in strain: DL42, features a modification of the amino acid from H to N at position 240.
+The protein's natural variant, known as in strain: DL42, features a modification of the amino acid from T to I at position 343.
+The protein's natural variant, known as in strain: DL42, features a modification of the amino acid from A to V at position 375.
+The protein's natural variant, known as in MC4DN3;, features a modification of the amino acid from T to K at position 196.
+The protein's natural variant, known as in MC4DN3;, features a modification of the amino acid from N to K at position 204.
+The protein's natural variant, known as in MC4DN3;, features a modification of the amino acid from P to L at position 225.
+The protein's natural variant, known as in MC4DN3;, features a modification of the amino acid from G to R at position 288.
+The protein's natural variant, known as in MC4DN3;, features a modification of the amino acid from D to G at position 336.
+The protein's natural variant, known as in MC4DN3;, features a modification of the amino acid from D to V at position 336.
+The protein's natural variant, known as in MC4DN3;, features a modification of the amino acid from P to L at position 420.
+The protein's natural variant, known as in IMD71; unknown pathological significance, features a modification of the amino acid from A to V at position 105.
+The protein's natural variant, known as in IMD71; unknown pathological significance;, features a modification of the amino acid from A to T at position 238.
+The protein's natural variant, known as in EL2; Lograno, features a modification of the amino acid from I to S at position 24.
+The protein's natural variant, known as in EL2;, features a modification of the amino acid from R to C at position 28.
+The protein's natural variant, known as in EL2; Corbeil;, features a modification of the amino acid from R to H at position 28.
+The protein's natural variant, known as in EL2;, features a modification of the amino acid from R to L at position 28.
+The protein's natural variant, known as in EL2;, features a modification of the amino acid from R to S at position 28.
+The protein's natural variant, known as in EL2; Marseille;, features a modification of the amino acid from V to A at position 31.
+The protein's natural variant, known as in EL2; Genova;, features a modification of the amino acid from R to W at position 34.
+The protein's natural variant, known as in EL2; Tunis;, features a modification of the amino acid from R to W at position 41.
+The protein's natural variant, known as in EL2; Clichy;, features a modification of the amino acid from R to S at position 45.
+The protein's natural variant, known as in EL2; Anastasia, features a modification of the amino acid from R to T at position 45.
+The protein's natural variant, known as in EL2; Culoz;, features a modification of the amino acid from G to V at position 46.
+The protein's natural variant, known as in HPP;, features a modification of the amino acid from K to R at position 48.
+The protein's natural variant, known as in EL2; Lyon;, features a modification of the amino acid from L to F at position 49.
+The protein's natural variant, known as in EL2; Ponte de Sor;, features a modification of the amino acid from G to D at position 151.
+The protein's natural variant, known as in EL2, features a modification of the amino acid from L to LL at position 154.
+The protein's natural variant, known as in EL2 and HPP; Saint-Louis;, features a modification of the amino acid from L to P at position 207.
+The protein's natural variant, known as in EL2; Nigerian;, features a modification of the amino acid from L to P at position 260.
+The protein's natural variant, known as in EL2;, features a modification of the amino acid from S to P at position 261.
+The protein's natural variant, known as in EL2; Barcelona, features a modification of the amino acid from H to P at position 469.
+The protein's natural variant, known as in EL2;, features a modification of the amino acid from Q to P at position 471.
+The protein's natural variant, known as in EL2; Jendouba;, features a modification of the amino acid from D to E at position 791.
+The protein's natural variant, known as in Cagliari, features a modification of the amino acid from A to G at position 2025.
+The protein's natural variant, known as in allele Lyt-3A, features a modification of the amino acid from R to S at position 98.
+The protein's natural variant, known as in SPAX4;, features a modification of the amino acid from N to D at position 478.
+The natural variant of this protein is characterized by an amino acid alteration from E to D at position 72.
+The natural variant of this protein is characterized by an amino acid alteration from R to K at position 115.
+The protein's natural variant, known as in NEDBAVC; unknown pathological significance;, features a modification of the amino acid from R to Q at position 93.
+The protein's natural variant, known as in NEDBAVC; unknown pathological significance; requires 2 nucleotide substitutions, features a modification of the amino acid from E to S at position 167.
+The protein's natural variant, known as in SRXY11;, features a modification of the amino acid from T to M at position 304.
+The protein's natural variant, known as in SRXY11;, features a modification of the amino acid from R to Q at position 308.
+The protein's natural variant, known as in SRXY11; unknown pathological significance, features a modification of the amino acid from R to L at position 334.
+The protein's natural variant, known as in SRXY11; unknown pathological significance, features a modification of the amino acid from R to W at position 334.
+The protein's natural variant, known as in NEDBAVC; unknown pathological significance;, features a modification of the amino acid from D to G at position 382.
+The protein's natural variant, known as in NEDBAVC; unknown pathological significance;, features a modification of the amino acid from N to K at position 419.
+The protein's natural variant, known as in NEDBAVC; unknown pathological significance;, features a modification of the amino acid from L to V at position 467.
+The protein's natural variant, known as in NEDBAVC; unknown pathological significance;, features a modification of the amino acid from R to H at position 487.
+The protein's natural variant, known as in SRXY11;, features a modification of the amino acid from S to F at position 595.
+The protein's natural variant, known as in SRXY11; unknown pathological significance, features a modification of the amino acid from S to L at position 626.
+The protein's natural variant, known as in SRXY11;, features a modification of the amino acid from R to Q at position 674.
+The protein's natural variant, known as in SRXY11;, features a modification of the amino acid from R to W at position 674.
+The protein's natural variant, known as in NEDBAVC; unknown pathological significance;, features a modification of the amino acid from V to M at position 731.
+The protein's natural variant, known as in SRXY11; unknown pathological significance;, features a modification of the amino acid from G to E at position 1030.
+The protein's natural variant, known as in NEDBAVC; unknown pathological significance;, features a modification of the amino acid from T to M at position 1094.
+The protein's natural variant, known as found in patients with recurrent kidney stones formation; unknown pathological significance; no effect on protein abundance; no effect on stability; decreased adenyl nucleotide antiporter activity; no effect on transporter activity regulation by calcium;, features a modification of the amino acid from Q to H at position 315.
+The protein's natural variant, known as in 50% of the molecules, features a modification of the amino acid from K to R at position 47.
+The protein's natural variant, known as in LISX1, features a modification of the amino acid from T to I at position 42.
+The protein's natural variant, known as in LISX1;, features a modification of the amino acid from L to S at position 43.
+The protein's natural variant, known as in LISX1 and SBHX;, features a modification of the amino acid from S to R at position 47.
+The protein's natural variant, known as in SBHX;, features a modification of the amino acid from K to N at position 50.
+The protein's natural variant, known as in SBHX;, features a modification of the amino acid from R to H at position 59.
+The protein's natural variant, known as in LISX1 and SBHX;, features a modification of the amino acid from R to L at position 59.
+The protein's natural variant, known as in LISX1, features a modification of the amino acid from N to D at position 60.
+The protein's natural variant, known as in LISX1 and SBHX;, features a modification of the amino acid from D to N at position 62.
+The protein's natural variant, known as in SBHX, features a modification of the amino acid from G to E at position 67.
+The protein's natural variant, known as in LISX1;, features a modification of the amino acid from A to S at position 71.
+The protein's natural variant, known as in SBH;, features a modification of the amino acid from R to H at position 78.
+The protein's natural variant, known as in SBHX;, features a modification of the amino acid from R to L at position 78.
+The protein's natural variant, known as in SBHX, features a modification of the amino acid from D to H at position 86.
+The protein's natural variant, known as in SBHX; mild;, features a modification of the amino acid from R to G at position 89.
+The protein's natural variant, known as in SBHX;, features a modification of the amino acid from L to R at position 97.
+The protein's natural variant, known as in LISX1 and SBHX, features a modification of the amino acid from G to A at position 100.
+The protein's natural variant, known as in LISX1, features a modification of the amino acid from R to S at position 102.
+The protein's natural variant, known as in SBHX, features a modification of the amino acid from I to T at position 104.
+The protein's natural variant, known as in SBHX, features a modification of the amino acid from Y to D at position 125.
+The protein's natural variant, known as in LISX1 and SBHX;, features a modification of the amino acid from Y to H at position 125.
+The protein's natural variant, known as in SBHX;, features a modification of the amino acid from R to C at position 178.
+The protein's natural variant, known as in SBHX;, features a modification of the amino acid from R to L at position 178.
+The protein's natural variant, known as in SBHX;, features a modification of the amino acid from R to C at position 186.
+The protein's natural variant, known as in SBHX, features a modification of the amino acid from P to L at position 191.
+The protein's natural variant, known as in SBHX;, features a modification of the amino acid from P to R at position 191.
+The protein's natural variant, known as in LISX1 and SBHX;, features a modification of the amino acid from R to W at position 192.
+The protein's natural variant, known as in LISX1;, features a modification of the amino acid from R to H at position 196.
+The protein's natural variant, known as in epilepsy; resistant partial seizures; related to 'cryptogenic' epilepsy;, features a modification of the amino acid from R to S at position 196.
+The protein's natural variant, known as in SBHX, features a modification of the amino acid from N to I at position 200.
+The protein's natural variant, known as in SBHX, features a modification of the amino acid from N to K at position 200.
+The protein's natural variant, known as in SBHX;, features a modification of the amino acid from T to A at position 203.
+The protein's natural variant, known as in LISX1 and SBHX;, features a modification of the amino acid from T to R at position 203.
+The protein's natural variant, known as in SBHX;, features a modification of the amino acid from I to T at position 214.
+The protein's natural variant, known as in SBHX, features a modification of the amino acid from T to I at position 222.
+The protein's natural variant, known as in SBHX, features a modification of the amino acid from G to E at position 223.
+The protein's natural variant, known as in SBHX, features a modification of the amino acid from G to V at position 223.
+The protein's natural variant, known as in SBHX;, features a modification of the amino acid from V to I at position 236.
+The protein's natural variant, known as in LISX1, features a modification of the amino acid from F to L at position 243.
+The protein's natural variant, known as in SBHX, features a modification of the amino acid from I to N at position 250.
+The protein's natural variant, known as in SBHX, features a modification of the amino acid from I to T at position 250.
+The protein's natural variant, known as in SBHX;, features a modification of the amino acid from A to S at position 251.
+The protein's natural variant, known as in SBHX, features a modification of the amino acid from A to V at position 251.
+The protein's natural variant, known as in SBHX, features a modification of the amino acid from G to D at position 253.
+The protein's natural variant, known as in LISX1 and SBHX; decreased tubulin binding;, features a modification of the amino acid from D to G at position 262.
+The protein's natural variant, known as in strain: Sonesta, Polder, Paloma, Laureat, Baby Bop, Hystyle and Midnight. In strain: GN 1140, Black Knight, Amanda, Imuna, Clipper and CY-10 S4, alleles PveIF4E(3) and cyv. In strain: Jolanda, Imuna and Evolutie, allele desc. In strain: IVT 7214, B/RRIL 105-25, USWK-6 and USWKH x HS4, allele bc-3, features a modification of the amino acid from S to T at position 6.
+The protein's natural variant, known as in strain: USLK1, USCR8 and USCR7. In strain: Imuna, Clipper and CY-10 S4, alleles PveIF4E(3) and cyv. In strain: Jolanda, Imuna and Evolutie, allele desc. In strain: Raven, allele PveIF4E(2). In strain: IVT 7214, B/RRIL 105-25, USWK-6 and USWKH x HS4, allele bc-3, features a modification of the amino acid from N to K at position 53.
+The protein's natural variant, known as in strain: USLK1, USCR8 and USCR7. In strain: Imuna, Clipper and CY-10 S4, alleles PveIF4E(3) and cyv. In strain: Imuna and Evolutie, allele desc. In strain: Raven, allele PveIF4E(2). In strain: IVT 7214, B/RRIL 105-25, USWK-6 and USWKH x HS4, allele bc-3, features a modification of the amino acid from F to Y at position 65.
+The protein's natural variant, known as in strain: USLK1, USCR8, USCR7, Sonesta, Polder, Paloma, Laureat and Baby Bop, allele PveIF4E(4). In strain: GN 1140, Black Knight, Amanda, Imuna, Clipper and CY-10 S4, alleles PveIF4E(3) and cyv. In strain: Jolanda, Imuna and Evolutie, allele desc. In strain: Raven, allele PveIF4E(2). In strain: IVT 7214, B/RRIL 105-25, USWK-6 and USWKH x HS4, allele bc-3, features a modification of the amino acid from A to E at position 76.
+The protein's natural variant, known as in strain: USLK1, USCR8 and USCR7. In strain: IVT 7214, B/RRIL 105-25, USWK-6 and USWKH x HS4, allele bc-3, features a modification of the amino acid from D to G at position 111.
+The protein's natural variant, known as in strain: Sonesta, Polder, Paloma, Laureat, Baby Bop, Hystyle and Midnight. In strain, GN 1140, Black Knight, Amanda, Imuna, Clipper and CY-10 S4, alleles PveIF4E(3) and cyv. In strain: Jolanda, Imuna and Evolutie, allele desc. In strain: IVT 7214, B/RRIL 105-25, USWK-6 and USWKH x HS4, allele bc-3, features a modification of the amino acid from AI to VV at position 230.
+The protein's natural variant, known as in DEE45; no effect on localization to the plasma membrane; increased GABA-gated chloride ion channel activity; increased single channel burst duration;, features a modification of the amino acid from F to S at position 246.
+The protein's natural variant, known as in DEE45;, features a modification of the amino acid from T to I at position 287.
+The protein's natural variant, known as found in 1.1% of population and in some schizophrenic patients;, features a modification of the amino acid from H to Q at position 421.
+The protein's natural variant, known as in allele HERV-H19, features a modification of the amino acid from V to L at position 81.
+The protein's natural variant, known as in allele HERV-H19, features a modification of the amino acid from F to L at position 150.
+The protein's natural variant, known as in strain: CWL029 and TW-183, features a modification of the amino acid from S to F at position 163.
+The protein's natural variant, known as in strain: EH15, features a modification of the amino acid from P to S at position 2.
+The protein's natural variant, known as in strain: EH15, features a modification of the amino acid from N to P at position 39.
+The protein's natural variant, known as in strain: EH15, features a modification of the amino acid from T to V at position 235.
+The protein's natural variant, known as in strain: EH15, features a modification of the amino acid from EA to DD at position 300.
+The protein's natural variant, known as in strain: EH15, features a modification of the amino acid from L to S at position 442.
+The protein's natural variant, known as in strain: EH15, features a modification of the amino acid from N to S at position 449.
+The protein's natural variant, known as in strain: EH15, features a modification of the amino acid from D to N at position 514.
+The protein's natural variant, known as in strain: EH15, features a modification of the amino acid from L to V at position 527.
+The protein's natural variant, known as in strain: NBRC 1060, features a modification of the amino acid from E to EE at position 409.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from E to D at position 50.
+The natural variant of this protein is characterized by an amino acid alteration from R to C at position 112.
+The protein's natural variant, known as found in infertile men; unknown pathological significance; no effect on induction of target genes expression;, features a modification of the amino acid from R to H at position 172.
+The protein's natural variant, known as in XP-E; impairs DNA-binding of the UV-DDB complex;, features a modification of the amino acid from K to E at position 244.
+The protein's natural variant, known as in XP-E; impairs interaction with DDB1 and CUL4A;, features a modification of the amino acid from R to H at position 273.
+The protein's natural variant, known as in du; variant allele entla, features a modification of the amino acid from E to EIYKDNRNLFEVQENEPQKLVEKVAGDIESLLDRKVQALK at position 99.
+The protein's natural variant, known as in HKLLS1;, features a modification of the amino acid from C to S at position 75.
+The protein's natural variant, known as in HKLLS1;, features a modification of the amino acid from C to S at position 102.
+The protein's natural variant, known as in HKLLS1;, features a modification of the amino acid from R to C at position 158.
+The protein's natural variant, known as in HKLLS1;, features a modification of the amino acid from C to R at position 174.
+The protein's natural variant, known as in HKLLS1;, features a modification of the amino acid from G to R at position 327.
+The protein's natural variant, known as in strain: Line W1, features a modification of the amino acid from N to K at position 228.
+The protein's natural variant, known as in CMM10; complete abolition of POT1-DNA complex formation, thus disrupting the interaction with telomeres and leading to elongated telomeres;, features a modification of the amino acid from Y to C at position 89.
+The protein's natural variant, known as in CMM10; complete abolition of POT1-DNA complex formation, thus disrupting the interaction with telomeres and leading to elongated telomeres;, features a modification of the amino acid from Q to E at position 94.
+The protein's natural variant, known as in GLM9;, features a modification of the amino acid from G to C at position 95.
+The protein's natural variant, known as in CMM10; increased telomere intensity signals and telomere fragility;, features a modification of the amino acid from R to H at position 137.
+The protein's natural variant, known as in CMM10;, features a modification of the amino acid from D to N at position 224.
+The protein's natural variant, known as in CMM10; significantly increased telomere length and numbers of fragile telomeres;, features a modification of the amino acid from S to N at position 270.
+The protein's natural variant, known as in CMM10; complete abolition of POT1-DNA complex formation, thus disrupting the interaction with telomeres and leading to elongated telomeres;, features a modification of the amino acid from R to L at position 273.
+The protein's natural variant, known as in CMM10;, features a modification of the amino acid from A to P at position 532.
+The protein's natural variant, known as in CMM10; increased telomere intensity signals and telomere fragility;, features a modification of the amino acid from Q to H at position 623.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from L to H at position 929.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from R to K at position 1634.
+The protein's natural variant, known as in variant Michigan-1; confers enhanced esterase activity and an additional zinc binding site;, features a modification of the amino acid from H to R at position 68.
+The protein's natural variant, known as in Guam;, features a modification of the amino acid from G to R at position 254.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from L to V at position 416.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from C to Y at position 490.
+The protein's natural variant, known as in a gastric adenocarcinoma sample; somatic mutation, features a modification of the amino acid from E to V at position 1010.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 1200.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from E to K at position 34.
+The protein's natural variant, known as in strain: Isolate TK 135728, features a modification of the amino acid from L to I at position 3.
+The protein's natural variant, known as in HH13; significantly reduced efficacy as well as potency, features a modification of the amino acid from N to K at position 115.
+The protein's natural variant, known as in PPNAD3; shows significantly higher cyclic AMP levels after transfection with the mutant protein than after transfection with the wild-type, indicating an impaired ability of the mutant protein to degrade cAMP;, features a modification of the amino acid from H to P at position 305.
+The protein's natural variant, known as associated with P2(k) phenotype;, features a modification of the amino acid from E to A at position 266.
+The protein's natural variant, known as associated with P1(k) phenotype;, features a modification of the amino acid from G to R at position 271.
+The protein's natural variant, known as found in 29% of the population; associated with increased plasma insulin concentration, increased fat oxidation and insulin resistance; 2-fold greater affinity for long-chain fatty acids;, features a modification of the amino acid from A to T at position 55.
+The protein's natural variant, known as in strain: 417RIB/A1, features a modification of the amino acid from GG to EE at position 8.
+The protein's natural variant, known as in strain: 205RIB/A2, 208RIB/A2, 209RIB/A2, 211RIB/A2 and 240RIB/AST, features a modification of the amino acid from I to V at position 9.
+The protein's natural variant, known as in strain: 201RIB/A1, features a modification of the amino acid from N to H at position 155.
+The protein's natural variant, known as in strain: 200RIB/A1, 201RIB/A1, 203RIB/A1, 233RIB/A1, 238RIB/AST, 332RIB/A1, 358RIB/A1, 394RIB/A1, 417RIB/A1 and 441RIB/A1, features a modification of the amino acid from I to V at position 163.
+The protein's natural variant, known as in strain: 200RIB/A1, 201RIB/A1, 203RIB/A1, 233RIB/A1, 238RIB/AST, 332RIB/A1, 358RIB/A1, 394RIB/A1, 417RIB/A1 and 441RIB/A1, features a modification of the amino acid from A to T at position 167.
+The protein's natural variant, known as in strain: 200RIB/A1, 238RIB/AST, 358RIB/A1, 340RIB/A1, 394RIB/A1 and 441RIB/A1, features a modification of the amino acid from S to N at position 198.
+The protein's natural variant, known as in strain: 240RIB/Ast, features a modification of the amino acid from T to S at position 262.
+The protein's natural variant, known as in strain: 205RIB/A2, features a modification of the amino acid from D to N at position 323.
+The protein's natural variant, known as in strain: 200RIB/A1, 201RIB/A1, 203RIB/A1, 233RIB/A1, 332RIB/A1, 340RIB/A1, 358RIB/A1, 394RIB/A1, 441RIB/A1 and 417RIB/A1, features a modification of the amino acid from P to S at position 451.
+The protein's natural variant, known as in strain: 206RIB/AST, features a modification of the amino acid from G to S at position 476.
+The protein's natural variant, known as in strain: 211RIB/A2, features a modification of the amino acid from I to V at position 480.
+The protein's natural variant, known as in IMD28; encodes misfolded protein with abnormal glycosylation; affects receptor trafficking to the cell surface; reduces response to IFNG;, features a modification of the amino acid from R to C at position 114.
+The protein's natural variant, known as in IMD28; encodes misfolded protein with abnormal glycosylation; affects receptor trafficking to the cell surface; reduces response to IFNG, features a modification of the amino acid from S to F at position 124.
+The protein's natural variant, known as in IMD28; encodes misfolded protein with abnormal glycosylation; affects receptor trafficking to the cell surface; reduces response to IFNG;, features a modification of the amino acid from G to R at position 141.
+The protein's natural variant, known as in IMD28; does not affect receptor trafficking to the cell surface; loss of function due to gain of N-glycosylation;, features a modification of the amino acid from T to N at position 168.
+The protein's natural variant, known as in IMD28; encodes misfolded protein with abnormal glycosylation; affects receptor trafficking to the cell surface; reduces response to IFNG, features a modification of the amino acid from G to R at position 227.
+The protein's natural variant, known as in NPHLOP1; causes hypophosphatemic urolithiasis; requires 2 nucleotide substitutions; results in lower phosphate current, decreases affinity for phosphate and decreases phosphate uptake compared to wild-type; shows a dominant-negative effect;, features a modification of the amino acid from A to F at position 48.
+The protein's natural variant, known as in NPHLOP1; causes hypophosphatemic osteoporosis; results in lower phosphate current, decreases affinity for phosphate and decreases phosphate uptake compared to wild-type; shows a dominant-negative effect;, features a modification of the amino acid from V to M at position 147.
+The protein's natural variant, known as in HCINF2; loss of phosphate transport activity; loss of localization to apical plasma membrane; display a complete intracellular retention and no detectable actin colocalization;, features a modification of the amino acid from G to A at position 153.
+The protein's natural variant, known as in HCINF2; loss of phosphate transport activity; loss of localization to apical plasma membrane; display a complete intracellular retention and no detectable actin colocalization;, features a modification of the amino acid from G to V at position 153.
+The protein's natural variant, known as in HCINF2; loss of phosphate transport activity; loss of localization to apical plasma membrane; display a complete intracellular retention and no detectable actin colocalization;, features a modification of the amino acid from L to P at position 155.
+The protein's natural variant, known as in FRTS2; loss of function in the homozygous state; loss of localization to cell membrane, features a modification of the amino acid from V to VILVTVLV at position 160.
+The protein's natural variant, known as in HCINF2;, features a modification of the amino acid from R to W at position 215.
+The protein's natural variant, known as in HCINF2; loss of phosphate transport activity; loss of localization to apical plasma membrane; display a complete intracellular retention and no detectable actin colocalization;, features a modification of the amino acid from C to G at position 336.
+The protein's natural variant, known as in HCINF2; loss of phosphate transport activity; loss of localization to apical plasma membrane; a complete intracellular retention and no detectable actin colocalization;, features a modification of the amino acid from V to E at position 408.
+The protein's natural variant, known as in HCINF2; loss of phosphate transport activity; loss of localization to apical plasma membrane; display a complete intracellular retention and no detectable actin colocalization, features a modification of the amino acid from W to R at position 488.
+The protein's natural variant, known as in strain: C57BL/6 and C57BL/6 XBALB/c, features a modification of the amino acid from S to N at position 2.
+The protein's natural variant, known as in strain: A/Sn, BALB/c, C57BL/6, C57BL/6 XBALB/c, C57BL/6 XCBA, CB-17/SCID and NZB, features a modification of the amino acid from L to Q at position 22.
+The protein's natural variant, known as in strain: C57BL/6, C57BL/6 XBALB/c and NZB, features a modification of the amino acid from V to A at position 34.
+The protein's natural variant, known as in strain: C57BL/6 XBALB/c, NZB and C57BL/6, features a modification of the amino acid from AP to VS at position 42.
+The protein's natural variant, known as in strain: C57BL/6, C57BL/6 XBALB/c and NZB, features a modification of the amino acid from T to I at position 60.
+The protein's natural variant, known as in strain: C57BL/6, C57BL/6 XBALB/c and NZB, features a modification of the amino acid from AV to TI at position 66.
+The protein's natural variant, known as in strain: C57BL/6, C57BL/6 XBALB/c and NZB, features a modification of the amino acid from N to S at position 72.
+The protein's natural variant, known as in strain: C57BL/6, C57BL/6 XBALB/c and NZB, features a modification of the amino acid from H to Y at position 85.
+The protein's natural variant, known as in strain: A/Sn, BALB/c, C57BL/6, C57BL/6 XBALB/c, C57BL/6 XCBA, CB-17/SCID and NZB, features a modification of the amino acid from RA to SD at position 94.
+The protein's natural variant, known as in strain: C57BL/6, C57BL/6 XBALB/c and NZB; requires 2 nucleotide substitutions, features a modification of the amino acid from T to L at position 115.
+The protein's natural variant, known as in strain: C57BL/6 and C57BL/6 XBALB/c, features a modification of the amino acid from E to D at position 117.
+The protein's natural variant, known as in strain: C57BL/6 and C57BL/6 XBALB/c, features a modification of the amino acid from D to N at position 127.
+The protein's natural variant, known as in strain: C57BL/6, C57BL/6 XBALB/c and NZB, features a modification of the amino acid from K to E at position 129.
+The protein's natural variant, known as in strain: NZB, features a modification of the amino acid from K to N at position 131.
+The protein's natural variant, known as in strain: NZB, features a modification of the amino acid from V to I at position 133.
+The protein's natural variant, known as in strain: C57BL/6 and C57BL/6 XBALB/c, features a modification of the amino acid from Y to H at position 146.
+The protein's natural variant, known as in strain: C57BL/6, C57BL/6 XBALB/c and NZB, features a modification of the amino acid from S to G at position 151.
+The protein's natural variant, known as in strain: A/Sn, BALB/c, C57BL/6, C57BL/6 XBALB/c, C57BL/6 XCBA, CB-17/SCID and NZB, features a modification of the amino acid from Y to F at position 174.
+The protein's natural variant, known as in strain: C57BL/6, C57BL/6 XBALB/c and NZB, features a modification of the amino acid from L to V at position 179.
+The protein's natural variant, known as in strain: NZB, features a modification of the amino acid from F to S at position 189.
+The protein's natural variant, known as in strain: C57BL/6, C57BL/6 XBALB/c and NZB, features a modification of the amino acid from N to S at position 198.
+The protein's natural variant, known as in strain: C57BL/6, C57BL/6 XBALB/c and NZB, features a modification of the amino acid from P to Q at position 219.
+The protein's natural variant, known as in strain: C57BL/6, C57BL/6 XBALB/c and NZB, features a modification of the amino acid from I to T at position 226.
+The protein's natural variant, known as in strain: NZB, features a modification of the amino acid from K to T at position 232.
+The protein's natural variant, known as in strain: C57BL/6, C57BL/6 XBALB/c and NZB, features a modification of the amino acid from I to T at position 247.
+The protein's natural variant, known as in strain: NZB, features a modification of the amino acid from I to T at position 251.
+The protein's natural variant, known as in strain: NZB, features a modification of the amino acid from K to R at position 260.
+The protein's natural variant, known as in 30% of the molecules, features a modification of the amino acid from L to V at position 153.
+The protein's natural variant, known as in MCCPD; unknown pathological significance;, features a modification of the amino acid from G to R at position 115.
+The protein's natural variant, known as in MCCPD;, features a modification of the amino acid from H to Q at position 173.
+The protein's natural variant, known as in MCCPD;, features a modification of the amino acid from Y to C at position 244.
+The natural variant of this protein is characterized by an amino acid alteration from T to D at position 15.
+The natural variant of this protein is characterized by an amino acid alteration from F to V at position 24.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from Q to K at position 319.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from G to E at position 189.
+The natural variant of this protein is characterized by an amino acid alteration from A to V at position 348.
+The natural variant of this protein is characterized by an amino acid alteration from W to G at position 524.
+The protein's natural variant, known as in strain: B, features a modification of the amino acid from E to A at position 312.
+The protein's natural variant, known as in isozyme 2, features a modification of the amino acid from D to N at position 66.
+The protein's natural variant, known as in isozyme 2, features a modification of the amino acid from N to D at position 88.
+The protein's natural variant, known as in isozyme 2, features a modification of the amino acid from D to A at position 90.
+The protein's natural variant, known as in isozyme 2, features a modification of the amino acid from T to A at position 94.
+The protein's natural variant, known as in isozyme 2, features a modification of the amino acid from G to H at position 117.
+The protein's natural variant, known as in MPSPS; may induce lysosome hyperacidification; does not affect the interaction with VPS16 and STX17; does not affect intracellular trafficking, lipid trafficking, nor cathepsin D processing;, features a modification of the amino acid from R to W at position 498.
+The protein's natural variant, known as in alpha-2, features a modification of the amino acid from V to L at position 30.
+The protein's natural variant, known as in alpha-2, features a modification of the amino acid from FT to LS at position 50.
+The protein's natural variant, known as in HTX6; unknown pathological significance;, features a modification of the amino acid from R to G at position 158.
+The protein's natural variant, known as in TOC;, features a modification of the amino acid from I to T at position 186.
+The protein's natural variant, known as in TOC;, features a modification of the amino acid from P to L at position 189.
+The protein's natural variant, known as in SPGF49; unknown pathological significance, features a modification of the amino acid from S to L at position 108.
+The protein's natural variant, known as in SPGF49; unknown pathological significance;, features a modification of the amino acid from R to W at position 619.
+The protein's natural variant, known as in SPGF49; unknown pathological significance, features a modification of the amino acid from Y to C at position 628.
+The protein's natural variant, known as in SPGF49; unknown pathological significance, features a modification of the amino acid from A to S at position 674.
+The protein's natural variant, known as in DEE56; unknown pathological significance;, features a modification of the amino acid from E to A at position 15.
+The protein's natural variant, known as found in an individual with autism; unknown pathological significance;, features a modification of the amino acid from K to Q at position 50.
+The protein's natural variant, known as in DEE56;, features a modification of the amino acid from D to E at position 129.
+The protein's natural variant, known as in DEE56;, features a modification of the amino acid from R to C at position 132.
+The protein's natural variant, known as probable disease-associated variant found in an individual with neurodevelopmental disorder;, features a modification of the amino acid from Y to S at position 133.
+The protein's natural variant, known as in DUH1;, features a modification of the amino acid from S to A at position 507.
+The protein's natural variant, known as in DUH1; increased interaction with GNAS; increased interaction with IQGAP1; increased protein levels; increased protein stability;, features a modification of the amino acid from E to K at position 509.
+The protein's natural variant, known as in DUH1; unknown pathological significance;, features a modification of the amino acid from S to R at position 513.
+The protein's natural variant, known as in DUH1; affects the regulation of cell mobility resulting in increased melanocyte migration; increased interaction with GNAS; increased interaction with IQGAP1; increased protein levels; increased protein stability;, features a modification of the amino acid from L to P at position 515.
+The protein's natural variant, known as in DUH1;, features a modification of the amino acid from S to N at position 519.
+The protein's natural variant, known as in DUH1; affects the regulation of cell mobility resulting in increased melanocyte migration; increased interaction with GNAS; increased interaction with IQGAP1; increased protein levels; increased protein stability;, features a modification of the amino acid from Y to D at position 551.
+The protein's natural variant, known as in DUH1;, features a modification of the amino acid from Y to H at position 551.
+The protein's natural variant, known as in DUH1; unknown pathological significance;, features a modification of the amino acid from M to T at position 595.
+The protein's natural variant, known as in CAPOK; affects the regulation of cell mobility; patient fibroblasts migrate better than control fibroblasts;, features a modification of the amino acid from E to K at position 617.
+The protein's natural variant, known as in ASNSD; dramatic reduction in protein abundance;, features a modification of the amino acid from A to E at position 6.
+The protein's natural variant, known as in ASNSD; dramatic reduction in protein abundance;, features a modification of the amino acid from F to V at position 362.
+The protein's natural variant, known as in ASNSD; increases level of protein abundance;, features a modification of the amino acid from R to C at position 550.
+The protein's natural variant, known as associated with elevated mean fasting plasma glucose level;, features a modification of the amino acid from A to G at position 148.
+The protein's natural variant, known as in IMD102; decreased protein abundance; patient T cells show decreased proliferation and cell cycle progression and increased apoptosis; functional signaling defects of the T cell receptor, features a modification of the amino acid from R to C at position 347.
+The protein's natural variant, known as renders the protein unstable and disrupts its cytoplasmic localization;, features a modification of the amino acid from D to G at position 59.
+The natural variant of this protein is characterized by an amino acid alteration from N to K at position 396.
+The protein's natural variant, known as in CILD33; the same mutation in the mouse sequence shows a moderate decrease in cilia motility;, features a modification of the amino acid from A to V at position 391.
+The protein's natural variant, known as in strain: CNTC 1/82, features a modification of the amino acid from V to I at position 115.
+The protein's natural variant, known as in AGM2;, features a modification of the amino acid from P to L at position 142.
+The protein's natural variant, known as does not affect NF-kappa-B activation and TNF production;, features a modification of the amino acid from A to P at position 9.
+The protein's natural variant, known as does not affect NF-kappa-B activation and TNF production;, features a modification of the amino acid from R to W at position 13.
+The protein's natural variant, known as does not affect NF-kappa-B activation and TNF production;, features a modification of the amino acid from S to N at position 55.
+The protein's natural variant, known as hypomorphic variant resulting in impaired NF-kappa-B activation and TNF production; loss of interaction with MYD88;, features a modification of the amino acid from D to N at position 96.
+The protein's natural variant, known as the functional impact of this variant is unclear; it has been reported both to affect interaction with TLR2, hence attenuating TLR2 signal transduction and to have no effect on NF-kappa-B activation and TNF production;, features a modification of the amino acid from S to L at position 180.
+The protein's natural variant, known as does not affect NF-kappa-B activation and TNF production;, features a modification of the amino acid from V to I at position 197.
+The protein's natural variant, known as in JBTS37; loss of interaction with ARMC9, features a modification of the amino acid from R to W at position 368.
+The protein's natural variant, known as in JBTS37; unknown pathological significance;, features a modification of the amino acid from A to D at position 371.
+The protein's natural variant, known as in JBTS37; loss of interaction with ARMC9;, features a modification of the amino acid from L to P at position 375.
+The protein's natural variant, known as in JBTS37; affects ciliogenesis resulting in shorter cilia; does not affect the interaction with ARMC9;, features a modification of the amino acid from R to C at position 1311.
+The protein's natural variant, known as in VETD; unknown pathological significance; decreased transcriptional regulatory activity; no effect on localization to the nucleus;, features a modification of the amino acid from R to Q at position 20.
+The protein's natural variant, known as in VETD; de novo variant; decreased transcriptional regulatory activity; no effect on localization to the nucleus;, features a modification of the amino acid from R to H at position 305.
+The protein's natural variant, known as in CDG2R; increases degradation rate via the ER-associated degradation pathway; loss of interaction with ATP6AP1;, features a modification of the amino acid from R to H at position 71.
+The protein's natural variant, known as in CDG2R; impairs export from the ER and cleavage, increases N-glycosylation post-translational modification which targets the misfolded protein to degradation via the ER-associated degradation pathway, results in loss of interaction with ATP6AP1, features a modification of the amino acid from L to S at position 98.
+The natural variant of this protein is characterized by an amino acid alteration from M to V at position 133.
+The natural variant of this protein is characterized by an amino acid alteration from T to S at position 169.
+The natural variant of this protein is characterized by an amino acid alteration from V to A at position 227.
+The natural variant of this protein is characterized by an amino acid alteration from A to R at position 309.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation, features a modification of the amino acid from G to E at position 107.
+The protein's natural variant, known as in strain: cv. Dzit Bacal, features a modification of the amino acid from S to G at position 9.
+The protein's natural variant, known as in strain: cv. D940Y and cv. M37W, features a modification of the amino acid from A to T at position 48.
+The protein's natural variant, known as in strain: cv. CML247, features a modification of the amino acid from V to A at position 70.
+The protein's natural variant, known as in strain: cv. Missouri 17, features a modification of the amino acid from D to G at position 75.
+The protein's natural variant, known as in strain: cv. I29, cv. Illinois 101, cv. Illinois 14H, cv. P39 and cv. Tennessee 8, features a modification of the amino acid from P to T at position 88.
+The protein's natural variant, known as in strain: cv. Nal-tel, features a modification of the amino acid from S to P at position 102.
+The protein's natural variant, known as in strain: cv. Costeno, features a modification of the amino acid from S to R at position 119.
+The protein's natural variant, known as in strain: cv. CML61, features a modification of the amino acid from S to T at position 167.
+The protein's natural variant, known as in strain: cv. CML247, features a modification of the amino acid from D to G at position 184.
+The protein's natural variant, known as in strain: cv. Assiniboine and cv. Missouri 17, features a modification of the amino acid from S to N at position 187.
+The protein's natural variant, known as in strain: cv. Sabanero, features a modification of the amino acid from P to S at position 197.
+The protein's natural variant, known as in strain: cv. Chapalote, features a modification of the amino acid from R to C at position 214.
+The protein's natural variant, known as in strain: cv. Guirua, features a modification of the amino acid from A to T at position 223.
+The protein's natural variant, known as in strain: cv. Chapalote, features a modification of the amino acid from Q to P at position 242.
+The protein's natural variant, known as in strain: cv. Sabanero, features a modification of the amino acid from M to I at position 266.
+The protein's natural variant, known as in strain: cv. Gehu, features a modification of the amino acid from W to R at position 268.
+The protein's natural variant, known as in strain: cv. A619, cv. B103, cv. F2, cv. H95, cv. H99, cv. Illinois 677A, cv. Moencopi, cv. North Carolina 260, cv. North Carolina 338, cv. Ohio 43, cv. Pioneer Inbred AP9, cv. U267Y, cv. W64A and cv. WF9, features a modification of the amino acid from G to V at position 284.
+The protein's natural variant, known as in strain: cv. Dzit Bacal, features a modification of the amino acid from S to P at position 299.
+The protein's natural variant, known as in strain: cv. Cateto Sulino, features a modification of the amino acid from M to R at position 304.
+The protein's natural variant, known as in strain: cv. Illinois 101, cv. Illinois 14H, cv. MS153, cv. P39 and cv. Tennessee 8, features a modification of the amino acid from A to P at position 320.
+The protein's natural variant, known as in strain: cv. Canilla, features a modification of the amino acid from C to R at position 358.
+The protein's natural variant, known as found in a patient with autism spectrum disorder; unknown pathological significance, features a modification of the amino acid from A to G at position 285.
+The protein's natural variant, known as found in a patient with schizophrenia; unknown pathological significance;, features a modification of the amino acid from R to C at position 336.
+The protein's natural variant, known as found in a patient with schizophrenia; unknown pathological significance;, features a modification of the amino acid from P to L at position 381.
+The protein's natural variant, known as found in a patient with schizophrenia; unknown pathological significance;, features a modification of the amino acid from R to H at position 470.
+The protein's natural variant, known as found in a patient with autism spectrum disorder; unknown pathological significance;, features a modification of the amino acid from L to P at position 472.
+The protein's natural variant, known as found in a patient with autism spectrum disorder; unknown pathological significance;, features a modification of the amino acid from T to M at position 641.
+The protein's natural variant, known as found in a patient with autism spectrum disorder; unknown pathological significance;, features a modification of the amino acid from E to D at position 919.
+The protein's natural variant, known as found in a patient with schizophrenia; unknown pathological significance;, features a modification of the amino acid from A to V at position 948.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from S to L at position 24.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from R to Q at position 27.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from E to Q at position 52.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from G to S at position 67.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from G to S at position 167.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from S to T at position 191.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from RKVNTEK to GQVKTEN at position 205.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from ED to DE at position 214.
+The protein's natural variant, known as in strain: U79, features a modification of the amino acid from S to F at position 748.
+The protein's natural variant, known as in strain: Berkeley, L18, Oregon-R, SP1 and U79, features a modification of the amino acid from T to S at position 762.
+The protein's natural variant, known as in strain: U79, features a modification of the amino acid from A to T at position 846.
+The protein's natural variant, known as in strain: L18 and U79, features a modification of the amino acid from V to A at position 858.
+The protein's natural variant, known as in strain: L18, features a modification of the amino acid from S to P at position 1176.
+The natural variant of this protein is characterized by an amino acid alteration from R to Q at position 5.
+The natural variant of this protein is characterized by an amino acid alteration from V to E at position 14.
+The natural variant of this protein is characterized by an amino acid alteration from T to M at position 110.
+The natural variant of this protein is characterized by an amino acid alteration from V to A at position 232.
+The protein's natural variant, known as in SPG56;, features a modification of the amino acid from C to R at position 262.
+The protein's natural variant, known as in SPG56;, features a modification of the amino acid from D to V at position 316.
+The protein's natural variant, known as in SPG56;, features a modification of the amino acid from E to G at position 380.
+The protein's natural variant, known as in SPG56;, features a modification of the amino acid from R to W at position 488.
+The protein's natural variant, known as in strain: CPN50, features a modification of the amino acid from G to A at position 147.
+The protein's natural variant, known as in strain: CPN50, features a modification of the amino acid from KIQS to EIKN at position 175.
+The protein's natural variant, known as in strain: CPN50, features a modification of the amino acid from V to M at position 250.
+The protein's natural variant, known as in strain: CPN50, features a modification of the amino acid from A to E at position 548.
+The protein's natural variant, known as in strain: CPN50, features a modification of the amino acid from D to E at position 558.
+The protein's natural variant, known as in strain: CPN50, features a modification of the amino acid from G to S at position 614.
+The protein's natural variant, known as in strain: CPN50, features a modification of the amino acid from I to V at position 944.
+The protein's natural variant, known as in strain: CPN50, features a modification of the amino acid from N to S at position 950.
+The protein's natural variant, known as in strain: CPN50, features a modification of the amino acid from T to I at position 979.
+The protein's natural variant, known as in strain: CPN50, features a modification of the amino acid from I to L at position 982.
+The protein's natural variant, known as in strain: CPN50, features a modification of the amino acid from I to F at position 1042.
+The protein's natural variant, known as in BBS1;, features a modification of the amino acid from H to R at position 35.
+The protein's natural variant, known as in BBS1;, features a modification of the amino acid from K to E at position 53.
+The protein's natural variant, known as in BBS1;, features a modification of the amino acid from D to N at position 148.
+The protein's natural variant, known as in BBS1;, features a modification of the amino acid from R to Q at position 160.
+The protein's natural variant, known as in a patient with Bardet-Biedl syndrome;, features a modification of the amino acid from L to V at position 206.
+The protein's natural variant, known as in BBS1;, features a modification of the amino acid from E to K at position 234.
+The protein's natural variant, known as in a patient with Bardet-Biedl syndrome;, features a modification of the amino acid from P to L at position 245.
+The protein's natural variant, known as in BBS1;, features a modification of the amino acid from G to S at position 305.
+The protein's natural variant, known as in BBS1, features a modification of the amino acid from I to T at position 330.
+The protein's natural variant, known as in BBS1;, features a modification of the amino acid from M to R at position 390.
+The protein's natural variant, known as in BBS1, features a modification of the amino acid from Y to S at position 434.
+The protein's natural variant, known as in BBS1;, features a modification of the amino acid from L to H at position 503.
+The protein's natural variant, known as in BBS1;, features a modification of the amino acid from L to P at position 518.
+The protein's natural variant, known as in BBS1, features a modification of the amino acid from L to Q at position 518.
+The protein's natural variant, known as in a patient with Meckel-Gruber like syndrome also carrying L-753 in TTC21B and a variant in CC2D2A;, features a modification of the amino acid from G to D at position 559.
+The natural variant of this protein is characterized by an amino acid alteration from S to M at position 26.
+The natural variant of this protein is characterized by an amino acid alteration from V to A at position 43.
+The natural variant of this protein is characterized by an amino acid alteration from S to Y at position 62.
+The natural variant of this protein is characterized by an amino acid alteration from G to E at position 63.
+The natural variant of this protein is characterized by an amino acid alteration from E to Q at position 64.
+The natural variant of this protein is characterized by an amino acid alteration from F to L at position 75.
+The natural variant of this protein is characterized by an amino acid alteration from F to I at position 119.
+The natural variant of this protein is characterized by an amino acid alteration from D to E at position 140.
+The natural variant of this protein is characterized by an amino acid alteration from V to A at position 143.
+The natural variant of this protein is characterized by an amino acid alteration from G to E at position 165.
+The natural variant of this protein is characterized by an amino acid alteration from Q to P at position 236.
+The protein's natural variant, known as in beta-B chain, features a modification of the amino acid from A to G at position 13.
+The protein's natural variant, known as in beta-B chain, features a modification of the amino acid from F to Y at position 41.
+The protein's natural variant, known as in beta-B chain, features a modification of the amino acid from G to A at position 122.
+The protein's natural variant, known as in beta-B chain, features a modification of the amino acid from K to C at position 143.
+The protein's natural variant, known as in a colorectal cancer, features a modification of the amino acid from F to S at position 74.
+The protein's natural variant, known as in some colorectal cancers, features a modification of the amino acid from A to T at position 209.
+The protein's natural variant, known as in a gastric cancer, features a modification of the amino acid from K to T at position 218.
+The protein's natural variant, known as in a colorectal cancer, features a modification of the amino acid from F to S at position 248.
+The protein's natural variant, known as in a colorectal cancer, features a modification of the amino acid from Y to H at position 280.
+The protein's natural variant, known as in a colorectal cancer, features a modification of the amino acid from I to V at position 395.
+The protein's natural variant, known as in a colorectal cancer, features a modification of the amino acid from Y to F at position 412.
+The protein's natural variant, known as in a gastric cancer;, features a modification of the amino acid from R to C at position 453.
+The protein's natural variant, known as in a colorectal cancer;, features a modification of the amino acid from N to K at position 510.
+The protein's natural variant, known as in a colorectal cancer;, features a modification of the amino acid from T to M at position 605.
+The protein's natural variant, known as in a colorectal cancer, features a modification of the amino acid from V to G at position 648.
+The protein's natural variant, known as in a colorectal cancer, features a modification of the amino acid from A to T at position 707.
+The protein's natural variant, known as in a colorectal cancer, features a modification of the amino acid from A to V at position 707.
+The protein's natural variant, known as in a colorectal cancer, features a modification of the amino acid from L to P at position 708.
+The protein's natural variant, known as in a lung cancer, features a modification of the amino acid from R to I at position 771.
+The protein's natural variant, known as in a colorectal cancer, features a modification of the amino acid from D to G at position 905.
+The protein's natural variant, known as in a colorectal cancer; reduced phosphatase activity, features a modification of the amino acid from Q to K at position 965.
+The protein's natural variant, known as in a colorectal cancer, features a modification of the amino acid from A to P at position 1096.
+The protein's natural variant, known as in a colorectal cancer; reduced phosphatase activity, features a modification of the amino acid from N to I at position 1106.
+The protein's natural variant, known as in a colorectal cancer; reduced phosphatase activity;, features a modification of the amino acid from R to W at position 1190.
+The protein's natural variant, known as in an acute myeloid leukemia sample; somatic mutation, features a modification of the amino acid from P to L at position 1213.
+The protein's natural variant, known as in a colorectal cancer, features a modification of the amino acid from M to L at position 1237.
+The protein's natural variant, known as in a colorectal cancer;, features a modification of the amino acid from V to M at position 1247.
+The protein's natural variant, known as in a lung cancer; reduced phosphatase activity, features a modification of the amino acid from R to L at position 1324.
+The protein's natural variant, known as in a colorectal cancer;, features a modification of the amino acid from Y to F at position 1329.
+The protein's natural variant, known as found in a patient with severe intellectual disability, behavioral problems, microcephaly, congenital cardiac defect and herniation of the abdominal diaphragm; also observed in some colorectal cancers; reduced phosphatase activity; unknown pathological significance;, features a modification of the amino acid from T to M at position 1346.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to G at position 7.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from R to P at position 7.
+The protein's natural variant, known as in CRS4;, features a modification of the amino acid from R to Q at position 65.
+The protein's natural variant, known as in CRS4;, features a modification of the amino acid from R to C at position 86.
+The protein's natural variant, known as in CHYTS;, features a modification of the amino acid from Y to C at position 89.
+The protein's natural variant, known as in strain: Isolate 2, features a modification of the amino acid from I to M at position 194.
+The protein's natural variant, known as in strain: Isolate 2, features a modification of the amino acid from SNN to VKY at position 207.
+The protein's natural variant, known as in strain: MmRL 1635, features a modification of the amino acid from T to S at position 198.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from V to M at position 173.
+The protein's natural variant, known as in alpha-A, features a modification of the amino acid from S to G at position 95.
+The protein's natural variant, known as in alpha A, features a modification of the amino acid from N to D at position 107.
+The protein's natural variant, known as in strain: ECOR 6, ECOR 28, ECOR 35, ECOR 37, ECOR 51, ECOR 58, ECOR 61, ECOR 66 and ECOR 69, features a modification of the amino acid from I to T at position 17.
+The protein's natural variant, known as in strain: ECOR 58, features a modification of the amino acid from A to E at position 51.
+The protein's natural variant, known as in strain: ECOR 28, ECOR 37, ECOR 58 and ECOR 69, features a modification of the amino acid from S to T at position 59.
+The protein's natural variant, known as in strain: ECOR 51, features a modification of the amino acid from Q to R at position 62.
+The protein's natural variant, known as in strain: ECOR 51, ECOR 61 and ECOR 66, features a modification of the amino acid from N to S at position 92.
+The protein's natural variant, known as in strain: Isolate SO-2000/12/21-1, features a modification of the amino acid from S to F at position 246.
+The natural variant of this protein is characterized by an amino acid alteration from Q to L at position 349.
+The natural variant of this protein is characterized by an amino acid alteration from FP to ST at position 359.
+The protein's natural variant, known as in strain: cv. Nd-1, features a modification of the amino acid from I to V at position 108.
+The protein's natural variant, known as in strain: cv. Nd-1, features a modification of the amino acid from R to K at position 113.
+The protein's natural variant, known as in strain: cv. Nd-1, features a modification of the amino acid from E to A at position 167.
+The protein's natural variant, known as in strain: cv. Nd-1, features a modification of the amino acid from E to D at position 181.
+The protein's natural variant, known as in strain: cv. Nd-1, features a modification of the amino acid from R to G at position 209.
+The protein's natural variant, known as in strain: cv. Nd-1, features a modification of the amino acid from E to R at position 213.
+The protein's natural variant, known as in strain: cv. Nd-1, features a modification of the amino acid from R to K at position 238.
+The protein's natural variant, known as in strain: cv. Nd-1, features a modification of the amino acid from K to M at position 253.
+The protein's natural variant, known as in strain: cv. RLD, features a modification of the amino acid from E to D at position 256.
+The protein's natural variant, known as in strain: cv. Nd-1 and cv. RLD, features a modification of the amino acid from Y to H at position 264.
+The protein's natural variant, known as in strain: cv. Nd-1 and cv. RLD, features a modification of the amino acid from D to E at position 286.
+The protein's natural variant, known as in strain: cv. Nd-1, features a modification of the amino acid from V to L at position 314.
+The protein's natural variant, known as in strain: cv. RLD, features a modification of the amino acid from K to N at position 346.
+The protein's natural variant, known as in strain: cv. RLD, features a modification of the amino acid from L to V at position 435.
+The protein's natural variant, known as in strain: cv. Nd-1 and cv. RLD, features a modification of the amino acid from H to R at position 440.
+The protein's natural variant, known as in strain: cv. Nd-1, features a modification of the amino acid from A to S at position 514.
+The protein's natural variant, known as in strain: cv. Nd-1, features a modification of the amino acid from E to Q at position 524.
+The protein's natural variant, known as in strain: cv. Nd-1, features a modification of the amino acid from H to N at position 527.
+The protein's natural variant, known as in strain: cv. Nd-1, features a modification of the amino acid from FKRYSSEKRK to IKRFAR at position 539.
+The protein's natural variant, known as in strain: cv. RLD, features a modification of the amino acid from F to V at position 530.
+The protein's natural variant, known as in strain: cv. RLD, features a modification of the amino acid from Y to N at position 548.
+The protein's natural variant, known as in strain: cv. RLD, features a modification of the amino acid from EFDH to LDN at position 554.
+The protein's natural variant, known as in strain: cv. Nd-1, features a modification of the amino acid from FDHLVGLDFET to LKFLVRLDVEK at position 562.
+The protein's natural variant, known as in strain: cv. RLD, features a modification of the amino acid from L to P at position 558.
+The protein's natural variant, known as in strain: cv. RLD, features a modification of the amino acid from L to T at position 563.
+The protein's natural variant, known as in strain: cv. Nd-1, features a modification of the amino acid from FGSLWLPFKI to LEALLGPFAS at position 580.
+The protein's natural variant, known as in strain: cv. RLD, features a modification of the amino acid from FGSLWLPF to VRRLGFPL at position 578.
+The protein's natural variant, known as in strain: cv. RLD, features a modification of the amino acid from H to P at position 586.
+The protein's natural variant, known as in strain: cv. Nd-1, features a modification of the amino acid from GI to RF at position 592.
+The protein's natural variant, known as in strain: cv. RLD, features a modification of the amino acid from GNSINDFDI to DYSFSDR at position 602.
+The protein's natural variant, known as in strain: cv. Nd-1, features a modification of the amino acid from NSIND to FSLRV at position 599.
+The protein's natural variant, known as in strain: cv. Nd-1, features a modification of the amino acid from L to S at position 609.
+The protein's natural variant, known as in strain: cv. Nd-1, features a modification of the amino acid from FVSDNYFIEE to DADHVCFIYD at position 625.
+The protein's natural variant, known as in strain: cv. RLD, features a modification of the amino acid from FVSDNYFIEE to EVSTYSEYPIYD at position 625.
+The protein's natural variant, known as in strain: cv. Nd-1, features a modification of the amino acid from L to F at position 632.
+The protein's natural variant, known as in strain: cv. Nd-1, features a modification of the amino acid from N to K at position 641.
+The protein's natural variant, known as in strain: cv. RLD, features a modification of the amino acid from N to Q at position 641.
+The protein's natural variant, known as in strain: cv. Nd-1 and cv. RLD, features a modification of the amino acid from FGG to VGE at position 645.
+The protein's natural variant, known as in strain: cv. Nd-1 and cv. RLD, features a modification of the amino acid from V to A at position 651.
+The protein's natural variant, known as in strain: cv. Nd-1 and cv. RLD, features a modification of the amino acid from T to R at position 658.
+The protein's natural variant, known as in strain: cv. RLD, features a modification of the amino acid from S to F at position 659.
+The protein's natural variant, known as in strain: cv. Nd-1 and cv. RLD, features a modification of the amino acid from F to S at position 662.
+The protein's natural variant, known as in strain: cv. Nd-1, features a modification of the amino acid from N to S at position 666.
+The protein's natural variant, known as in strain: cv. Nd-1, features a modification of the amino acid from P to H at position 670.
+The protein's natural variant, known as in strain: cv. Nd-1 and cv. RLD, features a modification of the amino acid from GISEM to EIYEDY at position 684.
+The protein's natural variant, known as in strain: cv. RLD, features a modification of the amino acid from SRSKE to DEDFD at position 689.
+The protein's natural variant, known as in strain: cv. Nd-1, features a modification of the amino acid from SR to NK at position 686.
+The protein's natural variant, known as in strain: cv. Nd-1 and cv. RLD, features a modification of the amino acid from H to T at position 693.
+The protein's natural variant, known as in strain: cv. Nd-1 and cv. RLD, features a modification of the amino acid from E to R at position 703.
+The protein's natural variant, known as in strain: cv. RLD, features a modification of the amino acid from ATPTEVHLS to YYLR at position 719.
+The protein's natural variant, known as in strain: cv. Nd-1, features a modification of the amino acid from ATPTEVH to VADRRY at position 717.
+The protein's natural variant, known as in strain: cv. RLD, features a modification of the amino acid from M to T at position 729.
+The protein's natural variant, known as in strain: cv. RLD, features a modification of the amino acid from R to L at position 734.
+The protein's natural variant, known as in strain: cv. Nd-1, features a modification of the amino acid from R to P at position 734.
+The protein's natural variant, known as in strain: cv. RLD, features a modification of the amino acid from V to E at position 742.
+The protein's natural variant, known as in strain: cv. RLD, features a modification of the amino acid from P to T at position 750.
+The protein's natural variant, known as in strain: cv. Nd-1, features a modification of the amino acid from LLSCNYS to FENCDYWG at position 771.
+The protein's natural variant, known as in strain: cv. RLD, features a modification of the amino acid from S to H at position 767.
+The protein's natural variant, known as in strain: cv. RLD, features a modification of the amino acid from G to GG at position 772.
+The protein's natural variant, known as in strain: cv. Nd-1, features a modification of the amino acid from DLLMRS to KLFINR at position 793.
+The protein's natural variant, known as in strain: cv. RLD, features a modification of the amino acid from DLLMR to QIFIHN at position 792.
+The protein's natural variant, known as in strain: cv. Nd-1, features a modification of the amino acid from EISVSKRETKLII to VVQTDNSKPIASV at position 823.
+The protein's natural variant, known as in strain: cv. RLD, features a modification of the amino acid from EISVSKRET to KITFKEVK at position 819.
+The protein's natural variant, known as in strain: cv. RLD, features a modification of the amino acid from FGQIYC to CMSYES at position 835.
+The natural variant of this protein is characterized by an amino acid alteration from T to A at position 1840.
+The protein's natural variant, known as does not affect D-fructose or D-glucose transport;, features a modification of the amino acid from I to V at position 296.
+The protein's natural variant, known as in CMLP9, features a modification of the amino acid from N to T at position 99.
+The protein's natural variant, known as in strain: O44:K74, features a modification of the amino acid from L to M at position 353.
+The protein's natural variant, known as in strain: B, features a modification of the amino acid from I to M at position 374.
+The protein's natural variant, known as does not affect subcellular localizattion; does not affect the transport of monoglucuronosyl bilirubin, bisglucuronosyl bilirubin, leukotriene C4, dehydroepiandrosterone-3-sulfate and 17-beta-glucuronosyl oestradiol;, features a modification of the amino acid from R to H at position 1297.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from L to V at position 566.
+The protein's natural variant, known as in MATD; abolishes enzyme activity, features a modification of the amino acid from S to N at position 38.
+The protein's natural variant, known as in MATD;, features a modification of the amino acid from A to D at position 55.
+The protein's natural variant, known as in MATD; retains 11% of wild-type activity;, features a modification of the amino acid from R to C at position 199.
+The protein's natural variant, known as in MATD; has virtually no enzymatic activity;, features a modification of the amino acid from R to C at position 264.
+The protein's natural variant, known as in MATD; dominant mutation;, features a modification of the amino acid from R to H at position 264.
+The protein's natural variant, known as in MATD;, features a modification of the amino acid from L to P at position 305.
+The protein's natural variant, known as in MATD; diminishes but do not completely abolishes enzyme activity; 46% of the level of the wild-type enzyme;, features a modification of the amino acid from I to M at position 322.
+The protein's natural variant, known as in MATD; retains significant enzymatic activity; 23% of the level of the wild-type enzyme;, features a modification of the amino acid from G to R at position 336.
+The protein's natural variant, known as in MATD; diminishes but do not completely abolishes enzyme activity; 12% of the level of the wild-type enzyme, features a modification of the amino acid from E to A at position 344.
+The protein's natural variant, known as in MATD;, features a modification of the amino acid from R to Q at position 356.
+The protein's natural variant, known as in MATD;, features a modification of the amino acid from P to L at position 357.
+The protein's natural variant, known as in MATD;, features a modification of the amino acid from G to S at position 378.
+The protein's natural variant, known as in CMM3; somatic and familial; generates a dominant oncogene resistant to inhibition by p16(INK4a);, features a modification of the amino acid from R to C at position 24.
+The protein's natural variant, known as in CMM3;, features a modification of the amino acid from R to H at position 24.
+The protein's natural variant, known as in CMM3; sporadic;, features a modification of the amino acid from N to S at position 41.
+The protein's natural variant, known as in CMS9;, features a modification of the amino acid from D to E at position 38.
+The protein's natural variant, known as in CMS9;, features a modification of the amino acid from P to R at position 344.
+The protein's natural variant, known as in FADS1; reduces agrin-dependent AChR aggregation and tyrosine kinase activity in developing neuromuscular junction;, features a modification of the amino acid from I to T at position 575.
+The protein's natural variant, known as in CMS9; affects interaction with DOK7 and impairs MUSK phosphorylation; altered AChR clustering;, features a modification of the amino acid from M to I at position 605.
+The protein's natural variant, known as in CMS9; affects interaction with DOK7 and impairs MUSK phosphorylation; altered AChR clustering;, features a modification of the amino acid from A to V at position 727.
+The protein's natural variant, known as in CMS9; does not affect catalytic kinase activity; reduces protein expression and stability;, features a modification of the amino acid from V to M at position 790.
+The protein's natural variant, known as in a lung neuroendocrine carcinoma sample; somatic mutation;, features a modification of the amino acid from N to S at position 819.
+The protein's natural variant, known as in CMS9; reduces AChR aggregation in developing neuromuscular junction, features a modification of the amino acid from M to V at position 835.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from G to V at position 75.
+The protein's natural variant, known as in HOMG1; impairs heterodimer formation resulting in intracellular retention;, features a modification of the amino acid from S to L at position 141.
+The protein's natural variant, known as in HOMG1; loss of function; no effect on cell membrane localization, features a modification of the amino acid from L to P at position 708.
+The protein's natural variant, known as in HOMG1; loss of function; no effect on cell membrane localization, features a modification of the amino acid from E to G at position 872.
+The protein's natural variant, known as in a lung large cell carcinoma sample; somatic mutation, features a modification of the amino acid from W to C at position 1007.
+The protein's natural variant, known as in HOMG1; loss of function; no effect on cell membrane localization, features a modification of the amino acid from Y to C at position 1053.
+The protein's natural variant, known as in HOMG1; loss of function; no effect on cell membrane localization, features a modification of the amino acid from L to P at position 1143.
+The protein's natural variant, known as no effect on function or cell membrane localization;, features a modification of the amino acid from Q to R at position 1663.
+The protein's natural variant, known as in HOMG1; loss of function; no effect on cell membrane localization, features a modification of the amino acid from S to N at position 1754.
+The protein's natural variant, known as in PC; rare variant associated with disease susceptibility;, features a modification of the amino acid from G to E at position 84.
+The protein's natural variant, known as found in prostate cancer samples; unknown pathological significance, features a modification of the amino acid from Y to D at position 88.
+The protein's natural variant, known as found in prostate cancer samples; unknown pathological significance, features a modification of the amino acid from L to P at position 144.
+The protein's natural variant, known as found in prostate cancer samples; unknown pathological significance;, features a modification of the amino acid from G to C at position 216.
+The protein's natural variant, known as found in prostate cancer samples; unknown pathological significance;, features a modification of the amino acid from R to G at position 229.
+The natural variant of this protein is characterized by an amino acid alteration from K to W at position 50.
+The protein's natural variant, known as in strain: C57BL/6J-pa mutants, features a modification of the amino acid from T to M at position 14.
+The protein's natural variant, known as in strain: BALB/c, CBA and C57BL/6J-pa mutants, features a modification of the amino acid from T to M at position 32.
+The protein's natural variant, known as in EBS2F;, features a modification of the amino acid from P to L at position 25.
+The protein's natural variant, known as in EBS2B;, features a modification of the amino acid from V to A at position 143.
+The protein's natural variant, known as in EBS2B;, features a modification of the amino acid from V to D at position 143.
+The protein's natural variant, known as probable disease-associated variant found in a patient with EBS with an unspecified subtype;, features a modification of the amino acid from V to F at position 143.
+The protein's natural variant, known as in EBS2C; unknown pathological significance, features a modification of the amino acid from N to Y at position 146.
+The protein's natural variant, known as in EBS2C; unknown pathological significance;, features a modification of the amino acid from L to P at position 149.
+The protein's natural variant, known as in EBS2B; unknown pathological significance;, features a modification of the amino acid from L to P at position 150.
+The protein's natural variant, known as in EBS2C; unknown pathological significance;, features a modification of the amino acid from T to P at position 151.
+The protein's natural variant, known as in EBS2C;, features a modification of the amino acid from P to L at position 152.
+The protein's natural variant, known as in EBS2D; unknown pathological significance;, features a modification of the amino acid from D to N at position 158.
+The protein's natural variant, known as in EBS2C; unknown pathological significance;, features a modification of the amino acid from D to V at position 158.
+The protein's natural variant, known as in DDD1; unknown pathological significance, features a modification of the amino acid from P to L at position 159.
+The protein's natural variant, known as in EBS2C;, features a modification of the amino acid from I to S at position 161.
+The protein's natural variant, known as in EBS2A;, features a modification of the amino acid from R to S at position 165.
+The protein's natural variant, known as in EBS2C;, features a modification of the amino acid from E to K at position 167.
+The protein's natural variant, known as in EBS2B; unknown pathological significance, features a modification of the amino acid from E to D at position 168.
+The protein's natural variant, known as in EBS2A;, features a modification of the amino acid from E to K at position 168.
+The protein's natural variant, known as in EBS2A;, features a modification of the amino acid from R to P at position 169.
+The protein's natural variant, known as in EBS2C; unknown pathological significance;, features a modification of the amino acid from E to G at position 170.
+The protein's natural variant, known as in EBS2C, EBS2B and EBS2D;, features a modification of the amino acid from E to K at position 170.
+The protein's natural variant, known as in EBS2B;, features a modification of the amino acid from K to N at position 173.
+The protein's natural variant, known as in EBS2A;, features a modification of the amino acid from L to F at position 175.
+The protein's natural variant, known as in EBS2A;, features a modification of the amino acid from N to S at position 176.
+The protein's natural variant, known as in EBS2C;, features a modification of the amino acid from N to S at position 177.
+The protein's natural variant, known as in EBS2A;, features a modification of the amino acid from F to S at position 179.
+The protein's natural variant, known as in EBS2B;, features a modification of the amino acid from A to D at position 180.
+The protein's natural variant, known as in EBS2A; unknown pathological significance;, features a modification of the amino acid from A to P at position 180.
+The protein's natural variant, known as in EBS2A; with laryngeal involvement;, features a modification of the amino acid from S to P at position 181.
+The protein's natural variant, known as in EBS2A; unknown pathological significance;, features a modification of the amino acid from I to M at position 183.
+The protein's natural variant, known as in EBS2D;, features a modification of the amino acid from I to T at position 183.
+The protein's natural variant, known as in EBS2C;, features a modification of the amino acid from V to E at position 186.
+The protein's natural variant, known as in EBS2B;, features a modification of the amino acid from V to L at position 186.
+The protein's natural variant, known as in EBS2B; unknown pathological significance;, features a modification of the amino acid from V to M at position 186.
+The protein's natural variant, known as in EBS2C; unknown pathological significance;, features a modification of the amino acid from R to P at position 187.
+The protein's natural variant, known as in EBS2C and in a patient with epidermolysis bullosa simplex with unspecified subtype; unknown pathological significance; requires 2 nucleotide substitutions;, features a modification of the amino acid from E to K at position 190.
+The protein's natural variant, known as in EBS2B and EBS2A; unknown pathological significance;, features a modification of the amino acid from Q to P at position 191.
+The protein's natural variant, known as in EBS2A and EBS2C;, features a modification of the amino acid from N to K at position 193.
+The protein's natural variant, known as in EBS2C; unknown pathological significance;, features a modification of the amino acid from T to S at position 198.
+The protein's natural variant, known as in EBS2C; unknown pathological significance;, features a modification of the amino acid from K to M at position 199.
+The protein's natural variant, known as in EBS2C;, features a modification of the amino acid from K to T at position 199.
+The protein's natural variant, known as found in a patient with epidermolysis bullosa simplex with unspecified subtype; unknown pathological significance, features a modification of the amino acid from L to M at position 203.
+The protein's natural variant, known as in EBS2C;, features a modification of the amino acid from L to P at position 311.
+The protein's natural variant, known as in EBS2C;, features a modification of the amino acid from T to P at position 321.
+The protein's natural variant, known as in EBS2B;, features a modification of the amino acid from V to A at position 323.
+The protein's natural variant, known as in EBS2C, features a modification of the amino acid from V to G at position 323.
+The protein's natural variant, known as in EBS2C;, features a modification of the amino acid from V to D at position 324.
+The protein's natural variant, known as in EBS2C, features a modification of the amino acid from L to F at position 325.
+The protein's natural variant, known as in EBS2B;, features a modification of the amino acid from L to P at position 325.
+The protein's natural variant, known as in EBS2C;, features a modification of the amino acid from M to K at position 327.
+The protein's natural variant, known as in EBS2C;, features a modification of the amino acid from M to T at position 327.
+The protein's natural variant, known as in EBS2C;, features a modification of the amino acid from D to E at position 328.
+The protein's natural variant, known as in EBS2C;, features a modification of the amino acid from D to G at position 328.
+The protein's natural variant, known as in EBS2C;, features a modification of the amino acid from D to H at position 328.
+The protein's natural variant, known as in EBS2C;, features a modification of the amino acid from D to V at position 328.
+The protein's natural variant, known as in EBS2C;, features a modification of the amino acid from N to K at position 329.
+The protein's natural variant, known as in EBS2C;, features a modification of the amino acid from R to C at position 331.
+The protein's natural variant, known as in EBS2C;, features a modification of the amino acid from R to H at position 331.
+The protein's natural variant, known as in EBS2C;, features a modification of the amino acid from R to S at position 352.
+The protein's natural variant, known as in EBS2C; unknown pathological significance;, features a modification of the amino acid from K to E at position 404.
+The protein's natural variant, known as in EBS2D;, features a modification of the amino acid from E to K at position 418.
+The protein's natural variant, known as in EBS2C, features a modification of the amino acid from A to D at position 428.
+The protein's natural variant, known as in EBS2C;, features a modification of the amino acid from A to T at position 428.
+The protein's natural variant, known as in EBS2C and EBS2B; unknown pathological significance;, features a modification of the amino acid from A to D at position 438.
+The protein's natural variant, known as in EBS2C; unknown pathological significance;, features a modification of the amino acid from K to N at position 443.
+The protein's natural variant, known as in EBS2B;, features a modification of the amino acid from L to P at position 463.
+The protein's natural variant, known as in EBS2B; unknown pathological significance;, features a modification of the amino acid from E to D at position 466.
+The protein's natural variant, known as in EBS2A;;, features a modification of the amino acid from I to M at position 467.
+The protein's natural variant, known as in EBS2A;, features a modification of the amino acid from I to T at position 467.
+The protein's natural variant, known as in EBS2A;, features a modification of the amino acid from T to P at position 469.
+The protein's natural variant, known as in EBS2C; unknown pathological significance;, features a modification of the amino acid from R to H at position 471.
+The protein's natural variant, known as in EBS2A;, features a modification of the amino acid from E to G at position 475.
+The protein's natural variant, known as in EBS2B;, features a modification of the amino acid from E to K at position 475.
+The protein's natural variant, known as in EBS2C; unknown pathological significance;, features a modification of the amino acid from G to D at position 476.
+The protein's natural variant, known as found in a patient with epidermolysis bullosa simplex with unspecified subtype; unknown pathological significance;, features a modification of the amino acid from E to G at position 477.
+The protein's natural variant, known as in EBS2A;, features a modification of the amino acid from E to K at position 477.
+The protein's natural variant, known as in EBS2A; unknown pathological significance;, features a modification of the amino acid from E to K at position 478.
+The protein's natural variant, known as in EBS2B;, features a modification of the amino acid from G to D at position 517.
+The protein's natural variant, known as found in a renal cell carcinoma sample; somatic mutation, features a modification of the amino acid from V to L at position 282.
+The protein's natural variant, known as in AVSD2; associated with disease susceptibility;, features a modification of the amino acid from R to H at position 107.
+The protein's natural variant, known as in AVSD2; associated with disease susceptibility;, features a modification of the amino acid from P to A at position 162.
+The protein's natural variant, known as in AVSD2; associated with disease susceptibility;, features a modification of the amino acid from T to I at position 311.
+The protein's natural variant, known as in AVSD2; associated with disease susceptibility;, features a modification of the amino acid from R to C at position 329.
+The protein's natural variant, known as in SEMDIST, features a modification of the amino acid from R to P at position 183.
+The protein's natural variant, known as in PFITS; unknown pathological significance, features a modification of the amino acid from D to N at position 26.
+The protein's natural variant, known as in PFITS; unknown pathological significance, features a modification of the amino acid from G to R at position 121.
+The protein's natural variant, known as in PFITS; unknown pathological significance; almost complete loss of protein expression in peripheral blood mononuclear cells, features a modification of the amino acid from H to Q at position 145.
+The protein's natural variant, known as in PFITS; unknown pathological significance, features a modification of the amino acid from L to V at position 286.
+The protein's natural variant, known as in PFITS; contrary to wild-type, which shows a uniform distribution throughout the cytoplasm, forms cytoplasmic aggregates, which contain pyrin/MEFV, hence might trigger spontaneous inflammasome activation, features a modification of the amino acid from L to F at position 293.
+The protein's natural variant, known as in PFITS; unknown pathological significance, features a modification of the amino acid from V to M at position 424.
+The protein's natural variant, known as in PFITS; unknown pathological significance; almost complete loss of protein expression in peripheral blood mononuclear cells, features a modification of the amino acid from G to S at position 501.
+The protein's natural variant, known as in PFITS; almost complete loss of protein expression in peripheral blood mononuclear cells, features a modification of the amino acid from D to V at position 572.
+The protein's natural variant, known as found in patients with gastrointestinal diffuse large cell lymphoma; impairs inhibitory activity on CARD11-induced NF-kappa-B activation;, features a modification of the amino acid from Q to H at position 249.
+The protein's natural variant, known as found in patients with gastrointestinal diffuse large cell lymphoma; somatic mutation; impairs inhibitory activity on CARD11-induced NF-kappa-B activation and impairs interaction with TNFAIP3;, features a modification of the amino acid from E to K at position 255.
+The protein's natural variant, known as in BRENS; decreased protein abundance; associated with abnormal ciliary structure and function, features a modification of the amino acid from N to S at position 263.
+The protein's natural variant, known as in BRENS; unknown pathological significance, features a modification of the amino acid from P to L at position 444.
+The natural variant of this protein is characterized by an amino acid alteration from R to H at position 573.
+The protein's natural variant, known as in an ovarian Endometrioid carcinoma sample; somatic mutation;, features a modification of the amino acid from S to T at position 14.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation, features a modification of the amino acid from G to S at position 92.
+The protein's natural variant, known as in strain: IBT2303, features a modification of the amino acid from Q to H at position 165.
+The natural variant of this protein is characterized by an amino acid alteration from Q to K at position 51.
+The protein's natural variant, known as in CDS;, features a modification of the amino acid from E to K at position 7.
+The protein's natural variant, known as found in a patient with CDS but without evidence it may cause the disease;, features a modification of the amino acid from H to R at position 82.
+The protein's natural variant, known as in CDS, features a modification of the amino acid from S to G at position 115.
+The protein's natural variant, known as in CDS; loss of PNPLA2-dependent triacylclycerol hydrolysis but no effect on LPA acyltransferase activity;, features a modification of the amino acid from Q to P at position 130.
+The protein's natural variant, known as in CDS; loss of PNPLA2-dependent triacylclycerol hydrolysis but no effect on LPA acyltransferase activity;, features a modification of the amino acid from E to K at position 260.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from A to T at position 617.
+The protein's natural variant, known as in FRTS4;, features a modification of the amino acid from R to W at position 85.
+The protein's natural variant, known as in MODY1;, features a modification of the amino acid from R to W at position 136.
+The protein's natural variant, known as found in a patient with non-insulin-dependent diabetes mellitus; does not affect activity;, features a modification of the amino acid from V to M at position 264.
+The protein's natural variant, known as in MODY1; results in loss of function, features a modification of the amino acid from E to Q at position 285.
+The protein's natural variant, known as in MODY1;, features a modification of the amino acid from M to R at position 373.
+The protein's natural variant, known as in T2D; reduced transactivation activity;, features a modification of the amino acid from V to I at position 402.
+The protein's natural variant, known as in IMGT allele IGHV1-46*02, features a modification of the amino acid from T to N at position 49.
+The protein's natural variant, known as in strain: DI7, Draveil, KY024, KY038, Loua, Monty5, Tahiti and ZW141, features a modification of the amino acid from I to V at position 7.
+The protein's natural variant, known as in strain: DI7, Draveil, KY024, KY038, Loua, Monty5 and ZW141, features a modification of the amino acid from I to V at position 24.
+The protein's natural variant, known as in strain: KY024, KY038 and ZW141, features a modification of the amino acid from A to T at position 72.
+The protein's natural variant, known as in strain: ZW141, features a modification of the amino acid from N to H at position 171.
+The natural variant of this protein is characterized by an amino acid alteration from K to N at position 8.
+The protein's natural variant, known as found in a patient with hereditary hemorrhagic talagiectasia; unknown pathological significance;, features a modification of the amino acid from P to S at position 30.
+The protein's natural variant, known as in HHT2, features a modification of the amino acid from C to Y at position 34.
+The natural variant of this protein is characterized by an amino acid alteration from S to C at position 38.
+The protein's natural variant, known as in HHT2; loss of receptor activity in response to BMP9; predominantly retained in the endoplasmic reticulum, features a modification of the amino acid from C to G at position 41.
+The protein's natural variant, known as in HHT2; loss of receptor activity in response to BMP9; predominantly retained in the endoplasmic reticulum;, features a modification of the amino acid from C to Y at position 41.
+The protein's natural variant, known as in HHT2; loss of receptor activity in response to BMP9; retained in the endoplasmic reticulum, features a modification of the amino acid from C to G at position 46.
+The protein's natural variant, known as in HHT2; loss of receptor activity in response to BMP9; retained in the endoplasmic reticulum;, features a modification of the amino acid from R to P at position 47.
+The protein's natural variant, known as in HHT2;, features a modification of the amino acid from GA to EP at position 49.
+The protein's natural variant, known as in HHT2, features a modification of the amino acid from G to R at position 48.
+The protein's natural variant, known as in HHT2; retained in the endoplasmic reticulum;, features a modification of the amino acid from W to C at position 50.
+The protein's natural variant, known as in HHT2, features a modification of the amino acid from W to G at position 50.
+The protein's natural variant, known as in HHT2;, features a modification of the amino acid from C to Y at position 51.
+The protein's natural variant, known as in HHT2;, features a modification of the amino acid from T to A at position 52.
+The protein's natural variant, known as found in a patient with pulmonary arterial hypertension; unknown pathological significance;, features a modification of the amino acid from E to V at position 59.
+The protein's natural variant, known as in HHT2, features a modification of the amino acid from H to P at position 66.
+The protein's natural variant, known as in HHT2; loss of receptor activity in response to BMP9; retained in the endoplasmic reticulum;, features a modification of the amino acid from H to Y at position 66.
+The protein's natural variant, known as in HHT2; retained in the endoplasmic reticulum;, features a modification of the amino acid from R to Q at position 67.
+The protein's natural variant, known as in HHT2;, features a modification of the amino acid from R to W at position 67.
+The protein's natural variant, known as in HHT2, features a modification of the amino acid from C to R at position 69.
+The protein's natural variant, known as in HHT2; loss of receptor activity in response to BMP9; retained in the endoplasmic reticulum;, features a modification of the amino acid from C to F at position 77.
+The protein's natural variant, known as in HHT2; retained in the endoplasmic reticulum, features a modification of the amino acid from C to W at position 77.
+The protein's natural variant, known as in HHT2, features a modification of the amino acid from N to D at position 96.
+The protein's natural variant, known as in HHT2, features a modification of the amino acid from N to S at position 96.
+The protein's natural variant, known as no loss of receptor activity in response to BMP9; mutant protein is capable of targeting the cell surface appropriately;, features a modification of the amino acid from E to D at position 111.
+The natural variant of this protein is characterized by an amino acid alteration from L to P at position 138.
+The protein's natural variant, known as found in a patient with pulmonary arterial hypertension; unknown pathological significance, features a modification of the amino acid from E to V at position 159.
+The protein's natural variant, known as in HHT2, features a modification of the amino acid from D to Y at position 176.
+The protein's natural variant, known as in HHT2; mutant protein is capable of targeting the cell surface appropriately;, features a modification of the amino acid from D to A at position 179.
+The protein's natural variant, known as in HHT2, features a modification of the amino acid from T to I at position 197.
+The protein's natural variant, known as in HHT2; loss of receptor activity in response to BMP9; retained in the endoplasmic reticulum;, features a modification of the amino acid from G to D at position 211.
+The protein's natural variant, known as in HHT2; loss of receptor activity in response to BMP9; retained in the endoplasmic reticulum, features a modification of the amino acid from G to S at position 211.
+The protein's natural variant, known as in HHT2;, features a modification of the amino acid from E to K at position 215.
+The protein's natural variant, known as in HHT2, features a modification of the amino acid from W to G at position 217.
+The protein's natural variant, known as in HHT2, features a modification of the amino acid from G to D at position 219.
+The protein's natural variant, known as in HHT2, features a modification of the amino acid from G to R at position 223.
+The protein's natural variant, known as found in a patient with pulmonary arterial hypertension; unknown pathological significance, features a modification of the amino acid from S to C at position 225.
+The protein's natural variant, known as in HHT2;, features a modification of the amino acid from V to E at position 226.
+The protein's natural variant, known as in HHT2, features a modification of the amino acid from K to R at position 229.
+The protein's natural variant, known as in HHT2;, features a modification of the amino acid from S to L at position 233.
+The protein's natural variant, known as in HHT2, features a modification of the amino acid from Q to K at position 237.
+The protein's natural variant, known as in HHT2; no loss of receptor activity in response to BMP9; mutant protein is capable of targeting the cell surface appropriately; affects splicing by inducing the creation of a new donor splice site and the loss of the 3' end of exon 6, features a modification of the amino acid from I to V at position 245.
+The protein's natural variant, known as in HHT2, features a modification of the amino acid from I to L at position 260.
+The protein's natural variant, known as in HHT2;, features a modification of the amino acid from T to P at position 265.
+The protein's natural variant, known as found in a patient with hereditary hemorrhagic talagiectasia; unknown pathological significance, features a modification of the amino acid from T to K at position 277.
+The protein's natural variant, known as in HHT2, features a modification of the amino acid from H to R at position 280.
+The protein's natural variant, known as in HHT2;, features a modification of the amino acid from L to F at position 285.
+The protein's natural variant, known as in HHT2, features a modification of the amino acid from L to P at position 289.
+The protein's natural variant, known as in HHT2, features a modification of the amino acid from L to R at position 294.
+The protein's natural variant, known as in HHT2; loss of receptor activity in response to BMP9; retained in the endoplasmic reticulum;, features a modification of the amino acid from A to P at position 306.
+The protein's natural variant, known as in HHT2; loss of receptor activity in response to BMP9; predominantly retained in the endoplasmic reticulum, features a modification of the amino acid from L to V at position 313.
+The protein's natural variant, known as in HHT2; loss of receptor activity in response to BMP9; retained in the endoplasmic reticulum;, features a modification of the amino acid from H to Y at position 314.
+The protein's natural variant, known as in HHT2;, features a modification of the amino acid from H to Q at position 328.
+The protein's natural variant, known as in HHT2; retained in the endoplasmic reticulum;, features a modification of the amino acid from S to I at position 333.
+The protein's natural variant, known as in HHT2, features a modification of the amino acid from N to H at position 335.
+The protein's natural variant, known as in HHT2;, features a modification of the amino acid from L to P at position 337.
+The protein's natural variant, known as in HHT2;, features a modification of the amino acid from C to R at position 344.
+The protein's natural variant, known as in HHT2; retained in the endoplasmic reticulum;, features a modification of the amino acid from C to Y at position 344.
+The protein's natural variant, known as in HHT2, features a modification of the amino acid from A to D at position 347.
+The protein's natural variant, known as in HHT2, features a modification of the amino acid from A to P at position 347.
+The protein's natural variant, known as in HHT2; retained in the endoplasmic reticulum;, features a modification of the amino acid from R to Q at position 374.
+The protein's natural variant, known as in HHT2;, features a modification of the amino acid from R to W at position 374.
+The protein's natural variant, known as in HHT2;, features a modification of the amino acid from M to R at position 376.
+The protein's natural variant, known as in HHT2;, features a modification of the amino acid from M to V at position 376.
+The protein's natural variant, known as in HHT2; retained in the endoplasmic reticulum, features a modification of the amino acid from P to L at position 378.
+The protein's natural variant, known as in HHT2; loss of receptor activity in response to BMP9; retained in the endoplasmic reticulum;, features a modification of the amino acid from P to S at position 378.
+The protein's natural variant, known as in HHT2; loss of receptor activity in response to BMP9; retained in the endoplasmic reticulum, features a modification of the amino acid from E to D at position 379.
+The protein's natural variant, known as in HHT2; loss of receptor activity in response to BMP9; retained in the endoplasmic reticulum;, features a modification of the amino acid from E to K at position 379.
+The protein's natural variant, known as found in patients with pulmonary arterial hypertension; unknown pathological significance, features a modification of the amino acid from T to A at position 396.
+The protein's natural variant, known as in HHT2, features a modification of the amino acid from D to G at position 397.
+The protein's natural variant, known as in HHT2;, features a modification of the amino acid from I to N at position 398.
+The protein's natural variant, known as in HHT2;, features a modification of the amino acid from W to S at position 399.
+The protein's natural variant, known as found in a patient with hereditary hemorrhagic talagiectasia; unknown pathological significance, features a modification of the amino acid from A to T at position 400.
+The protein's natural variant, known as in HHT2, features a modification of the amino acid from L to P at position 403.
+The protein's natural variant, known as in HHT2; loss of receptor activity in response to BMP9; predominantly retained in the endoplasmic reticulum, features a modification of the amino acid from V to G at position 404.
+The protein's natural variant, known as in HHT2;, features a modification of the amino acid from E to D at position 407.
+The protein's natural variant, known as in HHT2;, features a modification of the amino acid from R to P at position 411.
+The protein's natural variant, known as in HHT2; retained in the endoplasmic reticulum;, features a modification of the amino acid from R to Q at position 411.
+The protein's natural variant, known as in HHT2; loss of receptor activity in response to BMP9; predominantly retained in the endoplasmic reticulum;, features a modification of the amino acid from R to W at position 411.
+The protein's natural variant, known as in HHT2, features a modification of the amino acid from G to S at position 416.
+The protein's natural variant, known as no loss of receptor activity in response to BMP9; mutant protein is capable of targeting the cell surface appropriately;, features a modification of the amino acid from I to F at position 417.
+The protein's natural variant, known as in HHT2;, features a modification of the amino acid from P to R at position 424.
+The protein's natural variant, known as in HHT2;, features a modification of the amino acid from P to T at position 424.
+The protein's natural variant, known as in HHT2, features a modification of the amino acid from F to L at position 425.
+The protein's natural variant, known as in HHT2, features a modification of the amino acid from F to V at position 425.
+The protein's natural variant, known as in HHT2, features a modification of the amino acid from Y to C at position 426.
+The protein's natural variant, known as in HHT2, features a modification of the amino acid from P to R at position 433.
+The protein's natural variant, known as in HHT2; retained in the endoplasmic reticulum;, features a modification of the amino acid from V to M at position 441.
+The protein's natural variant, known as in HHT2; retained in the endoplasmic reticulum, features a modification of the amino acid from C to Y at position 443.
+The protein's natural variant, known as in HHT2;, features a modification of the amino acid from P to S at position 449.
+The protein's natural variant, known as in HHT2, features a modification of the amino acid from R to L at position 479.
+The protein's natural variant, known as in HHT2;, features a modification of the amino acid from R to P at position 479.
+The protein's natural variant, known as in HHT2;, features a modification of the amino acid from A to V at position 482.
+The protein's natural variant, known as in HHT2;, features a modification of the amino acid from R to W at position 484.
+The protein's natural variant, known as found in a patient with hereditary hemorrhagic talagiectasia; unknown pathological significance;, features a modification of the amino acid from K to E at position 486.
+The protein's natural variant, known as in HHT2; mutant protein is capable of targeting the cell surface appropriately;, features a modification of the amino acid from K to T at position 487.
+The protein's natural variant, known as in TNORS;, features a modification of the amino acid from M to I at position 112.
+The protein's natural variant, known as in TNORS;, features a modification of the amino acid from S to L at position 163.
+The protein's natural variant, known as in TNORS;, features a modification of the amino acid from R to C at position 174.
+The protein's natural variant, known as in strain: LO28, features a modification of the amino acid from A to P at position 92.
+The protein's natural variant, known as in strain: LO28, features a modification of the amino acid from E to D at position 124.
+The protein's natural variant, known as in strain: EGD5, features a modification of the amino acid from F to L at position 261.
+The protein's natural variant, known as in strain: EGD5, features a modification of the amino acid from C to R at position 375.
+The protein's natural variant, known as in strain: LO28, features a modification of the amino acid from DD to TT at position 381.
+The protein's natural variant, known as found in a renal cell carcinoma sample; somatic mutation, features a modification of the amino acid from E to K at position 236.
+The protein's natural variant, known as in MCOPCB7; unknown pathological significance; hypomorphic mutation;, features a modification of the amino acid from A to T at position 57.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from R to G at position 69.
+The protein's natural variant, known as in DUH3; the protein is retained in the Golgi apparatus;, features a modification of the amino acid from S to G at position 170.
+The protein's natural variant, known as decrease expression; does not affect susbtrate binding; does not affect ATP-binding; loss of plasma membrane expression;, features a modification of the amino acid from R to Q at position 192.
+The protein's natural variant, known as may be a modifier of disease severity in porphyria patients; loss of expression;, features a modification of the amino acid from R to W at position 276.
+The protein's natural variant, known as in DUH3;, features a modification of the amino acid from S to R at position 322.
+The protein's natural variant, known as in DUH3; the protein is retained in the Golgi apparatus;, features a modification of the amino acid from L to P at position 356.
+The protein's natural variant, known as in PSHK2;, features a modification of the amino acid from R to Q at position 375.
+The protein's natural variant, known as in PSHK2;, features a modification of the amino acid from R to W at position 375.
+The protein's natural variant, known as in DUH3, features a modification of the amino acid from Y to H at position 424.
+The protein's natural variant, known as in DUH3, features a modification of the amino acid from A to V at position 453.
+The protein's natural variant, known as may be a modifier of disease severity in porphyria patients; increases expression; does not affect susbtrate binding; impairs ATP-binding; Loss of ATP-dependent coproporphyrin III transport; Highly decrease plasma membrane expression;, features a modification of the amino acid from A to T at position 492.
+The protein's natural variant, known as may be a modifier of disease severity in porphyria patients; loss of expression;, features a modification of the amino acid from T to S at position 521.
+The protein's natural variant, known as in DUH3;, features a modification of the amino acid from Q to K at position 555.
+The protein's natural variant, known as in DUH3; the protein is retained in the Golgi apparatus. Does not affect subcellular location in early melanosome and lysosome. Does not rescue the normal amyloid fibril formation and normal maturation of pigmented melanosomes. Does not influence trafficking of melanosomal proteins.;, features a modification of the amino acid from G to E at position 579.
+The protein's natural variant, known as may be a modifier of disease severity in porphyria patients; loss of expression;, features a modification of the amino acid from G to S at position 588.
+The protein's natural variant, known as may be a modifier of disease severity in porphyria patients; loss of expression;, features a modification of the amino acid from A to T at position 681.
+The protein's natural variant, known as in PSHK2;, features a modification of the amino acid from R to Q at position 723.
+The protein's natural variant, known as in MCOPCB7; hypomorphic mutation;, features a modification of the amino acid from L to V at position 811.
+The protein's natural variant, known as in strain: W, features a modification of the amino acid from L to V at position 143.
+The protein's natural variant, known as in strain: W, features a modification of the amino acid from A to T at position 440.
+The protein's natural variant, known as in strain: W, features a modification of the amino acid from S to N at position 611.
+The protein's natural variant, known as in minor component, features a modification of the amino acid from Q to E at position 64.
+The protein's natural variant, known as in minor component, features a modification of the amino acid from E to D at position 79.
+The natural variant of this protein is characterized by an amino acid alteration from T to G at position 80.
+The protein's natural variant, known as in minor component, features a modification of the amino acid from H to N at position 83.
+The protein's natural variant, known as in minor and major variants, features a modification of the amino acid from S to A at position 97.
+The protein's natural variant, known as in NEDCAFD; unknown pathological significance, features a modification of the amino acid from Y to C at position 210.
+The protein's natural variant, known as in NEDCAFD; unknown pathological significance;, features a modification of the amino acid from A to V at position 231.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from T to A at position 278.
+The protein's natural variant, known as in strain: NVIII-5, NVIII-9, NVIII-46 and NVIII-41, features a modification of the amino acid from S to L at position 20.
+The protein's natural variant, known as in strain: NVIII-1, NVIII-2, NVIII-5, NVIII-9, NVIII-18, NVIII-22, NVIII-24, NVIII-41, NVIII-42, NVIII-46, NVIII-m11, NVIII-m12, NVIII-m13, NVIII-m15 and NVIII-m19, features a modification of the amino acid from Q to H at position 21.
+The protein's natural variant, known as in component C, features a modification of the amino acid from D to I at position 95.
+The protein's natural variant, known as in DFNB53;, features a modification of the amino acid from A to S at position 37.
+The natural variant of this protein is characterized by an amino acid alteration from D to G at position 593.
+The protein's natural variant, known as in DFNB53;, features a modification of the amino acid from P to T at position 621.
+The protein's natural variant, known as in OSMEDB;, features a modification of the amino acid from G to R at position 661.
+The protein's natural variant, known as in DFNA13;, features a modification of the amino acid from G to E at position 808.
+The protein's natural variant, known as in DFNB53;, features a modification of the amino acid from P to T at position 888.
+The protein's natural variant, known as in DFNA13;, features a modification of the amino acid from R to C at position 1034.
+The protein's natural variant, known as in OSMEDA;, features a modification of the amino acid from G to E at position 1441.
+The protein's natural variant, known as found in a patient with infantile-onset inflammatory bowel disease; unknown pathological significance; decreased function in cellular response to hydrogen peroxide; does not affect protein abundance; does not affect interaction with VCP;, features a modification of the amino acid from E to K at position 152.
+The protein's natural variant, known as found in a patient with infantile-onset inflammatory bowel disease; unknown pathological significance; decreased function in cellular response to hydrogen peroxide; decreased protein abundance; does not affect interaction with VCP;, features a modification of the amino acid from R to Q at position 585.
+The natural variant of this protein is characterized by an amino acid alteration from Q to P at position 638.
+The natural variant of this protein is characterized by an amino acid alteration from A to G at position 265.
+The natural variant of this protein is characterized by an amino acid alteration from A to I at position 265.
+The natural variant of this protein is characterized by an amino acid alteration from H to I at position 266.
+The natural variant of this protein is characterized by an amino acid alteration from TYA to RFB at position 273.
+The protein's natural variant, known as in FANCI; benign variant; no effect on ubiquitination and DNA repair;, features a modification of the amino acid from P to L at position 55.
+The protein's natural variant, known as in FANCI, features a modification of the amino acid from H to Y at position 858.
+The protein's natural variant, known as in FANCI; abolishes function in DNA repair;, features a modification of the amino acid from R to Q at position 1285.
+The protein's natural variant, known as in CSS4;, features a modification of the amino acid from T to M at position 859.
+The protein's natural variant, known as in CSS4;, features a modification of the amino acid from R to C at position 885.
+The protein's natural variant, known as in CSS4;, features a modification of the amino acid from L to F at position 921.
+The protein's natural variant, known as in CSS4;, features a modification of the amino acid from M to T at position 1011.
+The protein's natural variant, known as in CSS4;, features a modification of the amino acid from R to G at position 1157.
+The protein's natural variant, known as in strain: cv. Sy-0; causes late flowering phenotype, features a modification of the amino acid from K to E at position 525.
+The protein's natural variant, known as in strain: ZBMEL377, features a modification of the amino acid from T to A at position 105.
+The protein's natural variant, known as in strain: ZBMEL157, features a modification of the amino acid from E to R at position 147.
+The protein's natural variant, known as in strain: ZBMEL157, features a modification of the amino acid from N to R at position 148.
+The protein's natural variant, known as in strain: ZBMEL157, features a modification of the amino acid from V to L at position 149.
+The protein's natural variant, known as in strain: ZBMEL186, features a modification of the amino acid from Q to L at position 214.
+The protein's natural variant, known as in strain: ZBMEL186, features a modification of the amino acid from N to I at position 218.
+The protein's natural variant, known as in strain: FVB/N, features a modification of the amino acid from R to W at position 78.
+The natural variant of this protein is characterized by an amino acid alteration from H to Y at position 25.
+The natural variant of this protein is characterized by an amino acid alteration from V to L at position 33.
+The natural variant of this protein is characterized by an amino acid alteration from P to S at position 276.
+The protein's natural variant, known as in CFD;, features a modification of the amino acid from K to R at position 1103.
+The protein's natural variant, known as in strain: KS3/2, features a modification of the amino acid from L to F at position 18.
+The protein's natural variant, known as in isozyme 3A and isozyme 4A/4B, features a modification of the amino acid from E to K at position 32.
+The protein's natural variant, known as in isozyme 4A/4B, features a modification of the amino acid from G to D at position 37.
+The protein's natural variant, known as in isozyme 3A, features a modification of the amino acid from S to G at position 55.
+The protein's natural variant, known as in isozyme 2A, isozyme 3A and isozyme 4A/4B, features a modification of the amino acid from E to A at position 101.
+The protein's natural variant, known as in isozyme 2A, isozyme 3A and isozyme 4A/4B, features a modification of the amino acid from N to D at position 106.
+The protein's natural variant, known as in isozyme 2A, isozyme 3A and isozyme 4A/4B, features a modification of the amino acid from A to E at position 108.
+The protein's natural variant, known as in isozyme 2A, isozyme 3A and isozyme 4A/4B, features a modification of the amino acid from S to T at position 146.
+The protein's natural variant, known as in strain: cv. Sparkle, features a modification of the amino acid from ITPNV to LTPNL at position 91.
+The protein's natural variant, known as in a lung large cell carcinoma sample; somatic mutation, features a modification of the amino acid from F to L at position 371.
+The protein's natural variant, known as in strain: Isolate IZEA5429, features a modification of the amino acid from V to I at position 98.
+The protein's natural variant, known as in HLASA; decreased leucine-tRNA ligase activity;, features a modification of the amino acid from A to V at position 430.
+The protein's natural variant, known as in PRLTS4 and HLASA; reduced activity; decreased leucine-tRNA ligase activity;, features a modification of the amino acid from T to N at position 522.
+The protein's natural variant, known as in PRLTS4; unknown pathological significance; the mutant is functional in a yeast complementation assay;, features a modification of the amino acid from T to M at position 629.
+The protein's natural variant, known as in IMD23; decreased phosphoacetylglucosamine mutase activity; no effect on protein abundance;, features a modification of the amino acid from L to S at position 83.
+The protein's natural variant, known as in IMD23; decreased phosphoacetylglucosamine mutase activity;, features a modification of the amino acid from D to H at position 239.
+The protein's natural variant, known as in IMD23; loss of phosphoacetylglucosamine mutase activity;, features a modification of the amino acid from N to S at position 246.
+The protein's natural variant, known as in IMD23; decreased phosphoacetylglucosamine mutase activity; decreased protein abundance;, features a modification of the amino acid from D to E at position 297.
+The protein's natural variant, known as in IMD23; decreased phosphoacetylglucosamine mutase activity;, features a modification of the amino acid from Q to R at position 451.
+The protein's natural variant, known as in allele PGM3*2;, features a modification of the amino acid from D to N at position 466.
+The protein's natural variant, known as in IMD23; decreased phosphoacetylglucosamine mutase activity; no effect on protein abundance;, features a modification of the amino acid from E to Q at position 501.
+The protein's natural variant, known as in IMD23; decreased phosphoacetylglucosamine mutase activity; no effect on protein abundance;, features a modification of the amino acid from D to Y at position 502.
+The protein's natural variant, known as in strain: ISS and 129/Ola, features a modification of the amino acid from T to S at position 960.
+The protein's natural variant, known as in strain: ISS and 129/Ola, features a modification of the amino acid from T to M at position 1348.
+The protein's natural variant, known as in strain: S2980 and S2983, features a modification of the amino acid from P to S at position 2.
+The protein's natural variant, known as in strain: S2978 and S2979, features a modification of the amino acid from G to C at position 4.
+The protein's natural variant, known as in strain: S3333, features a modification of the amino acid from Q to R at position 20.
+The protein's natural variant, known as in strain: S2978 and S2979, features a modification of the amino acid from H to Q at position 41.
+The protein's natural variant, known as in strain: S2980 and S2983, features a modification of the amino acid from S to N at position 73.
+The protein's natural variant, known as in strain: S2980, S2983, S3013, S3014, S3015 and S3027, features a modification of the amino acid from D to N at position 77.
+The protein's natural variant, known as in strain: S3041 and S3044, features a modification of the amino acid from DH to EQ at position 147.
+The protein's natural variant, known as in strain: S2980 and S2983, features a modification of the amino acid from P to L at position 151.
+The protein's natural variant, known as in strain: S2978, S2979 and S2993, features a modification of the amino acid from P to S at position 151.
+The protein's natural variant, known as in strain: S3041 and S3044, features a modification of the amino acid from M to V at position 154.
+The protein's natural variant, known as in strain: S3044, features a modification of the amino acid from I to M at position 156.
+The protein's natural variant, known as in strain: S3333, features a modification of the amino acid from R to C at position 163.
+The protein's natural variant, known as in strain: S3015 and S3027, features a modification of the amino acid from Q to L at position 167.
+The protein's natural variant, known as in strain: S3013, S3014, S3015 and S3027, features a modification of the amino acid from S to R at position 170.
+The protein's natural variant, known as in strain: S3041 and S3044, features a modification of the amino acid from R to H at position 174.
+The protein's natural variant, known as in strain: S3015 and S3027, features a modification of the amino acid from T to A at position 181.
+The protein's natural variant, known as in strain: S3015 and S3027, features a modification of the amino acid from T to A at position 183.
+The protein's natural variant, known as in strain: S2980 and S2983, features a modification of the amino acid from T to I at position 183.
+The protein's natural variant, known as in strain: S3041 and S3044, features a modification of the amino acid from L to F at position 184.
+The protein's natural variant, known as in strain: S3041 and S3044, features a modification of the amino acid from EDA to AEG at position 188.
+The protein's natural variant, known as in strain: S3014, features a modification of the amino acid from A to G at position 188.
+The protein's natural variant, known as in strain: S2980, S2983, S3041 and S3044, features a modification of the amino acid from V to L at position 194.
+The protein's natural variant, known as in strain: S3041, features a modification of the amino acid from A to T at position 197.
+The protein's natural variant, known as in strain: S3041 and S3044, features a modification of the amino acid from LT to FI at position 214.
+The protein's natural variant, known as in strain: S2980 and S2983, features a modification of the amino acid from T to A at position 214.
+The protein's natural variant, known as in strain: S3041 and S3044, features a modification of the amino acid from C to G at position 303.
+The protein's natural variant, known as in strain: S3041 and S3044, features a modification of the amino acid from E to N at position 307.
+The protein's natural variant, known as in strain: S3041 and S3044, features a modification of the amino acid from M to V at position 348.
+The protein's natural variant, known as in strain: S3041 and S3044, features a modification of the amino acid from RQ to QR at position 384.
+The protein's natural variant, known as in strain: S2995 and S3057, features a modification of the amino acid from A to T at position 391.
+The protein's natural variant, known as in strain: S2980, S2983, S3041 and S3044, features a modification of the amino acid from R to Q at position 394.
+The protein's natural variant, known as in strain: S2978, S2979, S2993, S2995, S3013, S3014, S3015, S3027, S3041, S3044 and S3057, features a modification of the amino acid from H to Q at position 407.
+The protein's natural variant, known as in strain: S3041 and S3044, features a modification of the amino acid from V to A at position 409.
+The protein's natural variant, known as in strain: S2993, features a modification of the amino acid from R to C at position 411.
+The protein's natural variant, known as in strain: S3041 and S3044, features a modification of the amino acid from V to A at position 429.
+The protein's natural variant, known as in strain: S3041 and S3044, features a modification of the amino acid from N to H at position 486.
+The protein's natural variant, known as in strain: S3044, features a modification of the amino acid from P to T at position 492.
+The protein's natural variant, known as in strain: S2979, features a modification of the amino acid from A to S at position 501.
+The protein's natural variant, known as in strain: S3041 and S3044, features a modification of the amino acid from S to C at position 502.
+The protein's natural variant, known as in strain: S2979, features a modification of the amino acid from PG to RC at position 511.
+The protein's natural variant, known as in strain: S3041 and S3044, features a modification of the amino acid from A to G at position 547.
+The protein's natural variant, known as in strain: S3041 and S3044, features a modification of the amino acid from E to N at position 554.
+The protein's natural variant, known as in strain: S2978, S2979 and S2993, features a modification of the amino acid from V to I at position 557.
+The protein's natural variant, known as in strain: S2978, S2979, S2995 and S3057, features a modification of the amino acid from S to G at position 570.
+The protein's natural variant, known as in strain: S2980 and S2983, features a modification of the amino acid from GAISSTANSS to DIDRRLDKAPAPAGNVCRTA at position 583.
+The protein's natural variant, known as in strain: S3333, features a modification of the amino acid from GAISSTANSS to ETDRRPDKAFAPPSGNVRRA at position 583.
+The protein's natural variant, known as in strain: S2995 and S3057, features a modification of the amino acid from ISSTANSS to KEASPL at position 583.
+The protein's natural variant, known as in strain: S3041 and S3044, features a modification of the amino acid from S to T at position 578.
+The protein's natural variant, known as in strain: S3015, S3027, S3041 and S3044, features a modification of the amino acid from A to V at position 580.
+The protein's natural variant, known as in allele KAP3-v1, features a modification of the amino acid from C to CCCLTTCCRTTCCRPSCCISSCCRPSCCISSCCKPS at position 64.
+The protein's natural variant, known as in IO; associated with disease susceptibility; some patients also carry a HFE variant; decreased function in positive regulation of SMAD protein signal transduction; results in partial activation of hepcidin expression; affects post-translational processing resulting in reduced amount of the mature form; results in impaired secretion, features a modification of the amino acid from P to S at position 95.
+The protein's natural variant, known as in IO; associated with disease susceptibility; some patients also carry a HFE variant; decreased function in positive regulation of SMAD protein signal transduction; results in partial activation of hepcidin expression; affects post-translational processing resulting in reduced amount of the mature form; results in impaired secretion, features a modification of the amino acid from L to P at position 96.
+The protein's natural variant, known as in IO; associated with disease susceptibility, features a modification of the amino acid from E to Q at position 112.
+The protein's natural variant, known as in IO; associated with disease susceptibility; some patients also carry a HFE variant; decreased function in positive regulation of SMAD protein signal transduction; results in partial activation of hepcidin expression; affects post-translational processing resulting in reduced amount of the mature form; results in impaired secretion, features a modification of the amino acid from Q to E at position 113.
+The protein's natural variant, known as in IO; associated with disease susceptibility, features a modification of the amino acid from R to H at position 257.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from A to D at position 343.
+The protein's natural variant, known as in IO; associated with disease susceptibility; results in decreased activation of hepcidin expression in cultured liver cells, features a modification of the amino acid from V to M at position 394.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from P to L at position 476.
+The protein's natural variant, known as in an allele of Droughtmaster cattle; an Australian breed, features a modification of the amino acid from R to Q at position 29.
+The protein's natural variant, known as in CMS14; shows severely reduced expression of the mutant protein;, features a modification of the amino acid from V to G at position 68.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from K to N at position 161.
+The natural variant of this protein is characterized by an amino acid alteration from S to L at position 42.
+The protein's natural variant, known as in CGDX, features a modification of the amino acid from W to C at position 18.
+The protein's natural variant, known as in CGDX;, features a modification of the amino acid from G to R at position 20.
+The protein's natural variant, known as in CGDX;, features a modification of the amino acid from Y to D at position 41.
+The protein's natural variant, known as in CGDX;, features a modification of the amino acid from R to M at position 54.
+The protein's natural variant, known as in CGDX;, features a modification of the amino acid from R to S at position 54.
+The protein's natural variant, known as in CGDX;, features a modification of the amino acid from A to D at position 55.
+The protein's natural variant, known as in CGDX;, features a modification of the amino acid from A to E at position 57.
+The protein's natural variant, known as in CGDX;, features a modification of the amino acid from C to R at position 59.
+The protein's natural variant, known as in CGDX;, features a modification of the amino acid from C to W at position 59.
+The protein's natural variant, known as in CGDX;, features a modification of the amino acid from H to R at position 101.
+The protein's natural variant, known as in CGDX;, features a modification of the amino acid from H to Y at position 101.
+The protein's natural variant, known as in CGDX;, features a modification of the amino acid from H to R at position 119.
+The protein's natural variant, known as in CGDX;, features a modification of the amino acid from A to T at position 156.
+The protein's natural variant, known as in IMD34;, features a modification of the amino acid from T to P at position 178.
+The protein's natural variant, known as in CGDX;, features a modification of the amino acid from G to R at position 179.
+The protein's natural variant, known as in CGDX;, features a modification of the amino acid from S to F at position 193.
+The protein's natural variant, known as in CGDX;, features a modification of the amino acid from F to I at position 205.
+The protein's natural variant, known as in CGDX;, features a modification of the amino acid from H to Q at position 209.
+The protein's natural variant, known as in CGDX;, features a modification of the amino acid from H to R at position 209.
+The protein's natural variant, known as in CGDX;, features a modification of the amino acid from H to Y at position 209.
+The protein's natural variant, known as in CGDX;, features a modification of the amino acid from H to N at position 222.
+The protein's natural variant, known as in CGDX;, features a modification of the amino acid from H to R at position 222.
+The protein's natural variant, known as in CGDX;, features a modification of the amino acid from H to Y at position 222.
+The protein's natural variant, known as in CGDX; requires 2 nucleotide substitutions;, features a modification of the amino acid from G to L at position 223.
+The protein's natural variant, known as in CGDX;, features a modification of the amino acid from A to G at position 224.
+The protein's natural variant, known as in CGDX;, features a modification of the amino acid from E to V at position 225.
+The protein's natural variant, known as in IMD34;, features a modification of the amino acid from Q to P at position 231.
+The protein's natural variant, known as in CGDX;, features a modification of the amino acid from C to R at position 244.
+The protein's natural variant, known as in CGDX;, features a modification of the amino acid from C to S at position 244.
+The protein's natural variant, known as in CGDX;, features a modification of the amino acid from C to Y at position 244.
+The protein's natural variant, known as in CGDX, features a modification of the amino acid from K to N at position 299.
+The protein's natural variant, known as in CGDX; completely inhibits NADPH oxidase activity; NADPH oxidase assembly is abolished;, features a modification of the amino acid from H to N at position 303.
+The protein's natural variant, known as in CGDX; reduces NADPH oxidase activity to 4% of wild-type; translocation to the membrane of the phagosome is only attenuated;, features a modification of the amino acid from P to R at position 304.
+The protein's natural variant, known as in CGDX;, features a modification of the amino acid from T to P at position 307.
+The protein's natural variant, known as in CGDX;, features a modification of the amino acid from E to K at position 309.
+The protein's natural variant, known as in CGDX;, features a modification of the amino acid from G to E at position 322.
+The protein's natural variant, known as in CGDX;, features a modification of the amino acid from I to F at position 325.
+The protein's natural variant, known as in CGDX;, features a modification of the amino acid from S to P at position 333.
+The protein's natural variant, known as in CGDX, features a modification of the amino acid from H to D at position 338.
+The protein's natural variant, known as in CGDX;, features a modification of the amino acid from H to Y at position 338.
+The protein's natural variant, known as in CGDX;, features a modification of the amino acid from P to H at position 339.
+The protein's natural variant, known as in CGDX;, features a modification of the amino acid from L to Q at position 342.
+The protein's natural variant, known as in CGDX;, features a modification of the amino acid from S to F at position 344.
+The protein's natural variant, known as in CGDX;, features a modification of the amino acid from R to P at position 356.
+The protein's natural variant, known as in CGDX;, features a modification of the amino acid from G to A at position 389.
+The protein's natural variant, known as in CGDX;, features a modification of the amino acid from G to E at position 389.
+The protein's natural variant, known as in CGDX;, features a modification of the amino acid from M to R at position 405.
+The protein's natural variant, known as in CGDX;, features a modification of the amino acid from G to E at position 408.
+The protein's natural variant, known as in CGDX;, features a modification of the amino acid from G to R at position 408.
+The protein's natural variant, known as in CGDX, features a modification of the amino acid from A to G at position 409.
+The protein's natural variant, known as in CGDX, features a modification of the amino acid from G to E at position 412.
+The protein's natural variant, known as in CGDX;, features a modification of the amino acid from P to H at position 415.
+The protein's natural variant, known as in CGDX;, features a modification of the amino acid from P to L at position 415.
+The protein's natural variant, known as in CGDX;, features a modification of the amino acid from L to P at position 420.
+The protein's natural variant, known as in CGDX;, features a modification of the amino acid from S to P at position 422.
+The protein's natural variant, known as in CGDX;, features a modification of the amino acid from W to R at position 453.
+The protein's natural variant, known as in CGDX, features a modification of the amino acid from A to D at position 488.
+The protein's natural variant, known as in CGDX, features a modification of the amino acid from D to E at position 500.
+The protein's natural variant, known as in CGDX;, features a modification of the amino acid from D to G at position 500.
+The protein's natural variant, known as in CGDX;, features a modification of the amino acid from L to R at position 505.
+The protein's natural variant, known as in CGDX;, features a modification of the amino acid from W to C at position 516.
+The protein's natural variant, known as in CGDX;, features a modification of the amino acid from W to R at position 516.
+The protein's natural variant, known as in CGDX;, features a modification of the amino acid from V to D at position 534.
+The protein's natural variant, known as in CGDX;, features a modification of the amino acid from C to R at position 537.
+The protein's natural variant, known as in CGDX;, features a modification of the amino acid from L to P at position 546.
+The protein's natural variant, known as in SPGF6;, features a modification of the amino acid from R to Q at position 283.
+The natural variant of this protein is characterized by an amino acid alteration from M to V at position 286.
+The protein's natural variant, known as in strain: HMI/Msf, features a modification of the amino acid from N to S at position 44.
+The protein's natural variant, known as in strain: BLG2/Msf, MSM/Msf, SWN/Msf and NJL/Msf, features a modification of the amino acid from V to A at position 86.
+The protein's natural variant, known as in strain: BLG2/Msf and NJL/Msf, features a modification of the amino acid from P to S at position 88.
+The protein's natural variant, known as in strain: CAST/Ei and HMI/Msf, features a modification of the amino acid from S to T at position 100.
+The protein's natural variant, known as in strain: BLG2/Msf, NJL/Msf, MSM/Msf and SWN/Msf, features a modification of the amino acid from N to D at position 124.
+The protein's natural variant, known as in DIAR5;, features a modification of the amino acid from C to Y at position 66.
+The protein's natural variant, known as in strain: D488 and HB60, features a modification of the amino acid from D to N at position 199.
+The protein's natural variant, known as in strain: D488, features a modification of the amino acid from A to V at position 225.
+The protein's natural variant, known as in strain: D488, features a modification of the amino acid from D to N at position 255.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from A to T at position 45.
+The protein's natural variant, known as in IGHD4;, features a modification of the amino acid from L to H at position 144.
+The protein's natural variant, known as in IGHD4; reduced cAMP response to GHRH;, features a modification of the amino acid from A to V at position 176.
+The protein's natural variant, known as in IGHD4;, features a modification of the amino acid from A to E at position 222.
+The protein's natural variant, known as in IGHD4;, features a modification of the amino acid from F to C at position 242.
+The protein's natural variant, known as in IGHD4;, features a modification of the amino acid from K to E at position 329.
+The protein's natural variant, known as found in a patient with autism; unknown pathological significance;, features a modification of the amino acid from G to V at position 1094.
+The protein's natural variant, known as in strain: H0892/92; INH-resistant, features a modification of the amino acid from W to G at position 300.
+The protein's natural variant, known as in strain: H0181/94, H0452/92, H0948/92 and H0169/93; INH-resistant, features a modification of the amino acid from S to T at position 315.
+The protein's natural variant, known as in strain: H0169/93; INH-resistant, features a modification of the amino acid from R to L at position 463.
+The protein's natural variant, known as in strain: H0948/92; INH-resistant, features a modification of the amino acid from P to A at position 501.
+The protein's natural variant, known as in strain: H0251/90; INH-resistant, features a modification of the amino acid from Q to P at position 525.
+The protein's natural variant, known as in strain: 15726/89; INH-resistant, features a modification of the amino acid from L to P at position 587.
+The protein's natural variant, known as in strain: H0004/93; INH-resistant, features a modification of the amino acid from S to P at position 700.
+The protein's natural variant, known as in allele MtnA-3 and strain: AF6, Highgrove, Indiana, LA20, Taiwan, ZH18, ZH21, ZH27, ZS11, ZS30 and ZS56, features a modification of the amino acid from E to K at position 40.
+The natural variant of this protein is characterized by an amino acid alteration from P to D at position 116.
+The natural variant of this protein is characterized by an amino acid alteration from R to W at position 338.
+The protein's natural variant, known as in MMAM; likely benign variant;, features a modification of the amino acid from I to V at position 69.
+The protein's natural variant, known as in MMAM; mut0 and mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability;, features a modification of the amino acid from P to L at position 86.
+The protein's natural variant, known as in MMAM; mut0;, features a modification of the amino acid from G to E at position 87.
+The protein's natural variant, known as in MMAM; mut0; decreased methylmalonyl-CoA mutase activity;, features a modification of the amino acid from R to H at position 93.
+The protein's natural variant, known as in MMAM; mut0;, features a modification of the amino acid from G to R at position 94.
+The protein's natural variant, known as in MMAM; mut- and mut0;, features a modification of the amino acid from G to V at position 94.
+The protein's natural variant, known as in MMAM; mut0;, features a modification of the amino acid from P to R at position 95.
+The protein's natural variant, known as in MMAM; mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability;, features a modification of the amino acid from Y to C at position 100.
+The protein's natural variant, known as in MMAM; mut0;, features a modification of the amino acid from W to R at position 105.
+The protein's natural variant, known as in MMAM; mut0;, features a modification of the amino acid from R to C at position 108.
+The protein's natural variant, known as in MMAM; mut-, features a modification of the amino acid from R to G at position 108.
+The protein's natural variant, known as in MMAM; mut0;, features a modification of the amino acid from R to H at position 108.
+The protein's natural variant, known as in MMAM; mut0;, features a modification of the amino acid from Q to R at position 109.
+The protein's natural variant, known as in MMAM;, features a modification of the amino acid from Y to C at position 110.
+The protein's natural variant, known as in MMAM;, features a modification of the amino acid from N to K at position 126.
+The protein's natural variant, known as in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity;, features a modification of the amino acid from G to R at position 133.
+The protein's natural variant, known as in MMAM;, features a modification of the amino acid from A to G at position 137.
+The protein's natural variant, known as in MMAM; mut0;, features a modification of the amino acid from A to V at position 137.
+The protein's natural variant, known as in MMAM; unknown pathological significance;, features a modification of the amino acid from D to N at position 139.
+The protein's natural variant, known as in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity, features a modification of the amino acid from L to P at position 140.
+The protein's natural variant, known as in MMAM; decreased protein expression;, features a modification of the amino acid from A to T at position 141.
+The protein's natural variant, known as in MMAM; mut0, features a modification of the amino acid from H to Y at position 143.
+The protein's natural variant, known as in MMAM; mut0, features a modification of the amino acid from G to S at position 145.
+The protein's natural variant, known as in MMAM; mut0;, features a modification of the amino acid from S to L at position 148.
+The protein's natural variant, known as in MMAM; mut-, features a modification of the amino acid from D to N at position 156.
+The protein's natural variant, known as in MMAM;, features a modification of the amino acid from D to V at position 156.
+The protein's natural variant, known as in MMAM; mut0, features a modification of the amino acid from G to V at position 158.
+The protein's natural variant, known as in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity, features a modification of the amino acid from G to R at position 161.
+The protein's natural variant, known as in MMAM; decreased protein expression, features a modification of the amino acid from G to V at position 161.
+The protein's natural variant, known as in MMAM; mut0;, features a modification of the amino acid from F to S at position 174.
+The protein's natural variant, known as in MMAM; mut-;, features a modification of the amino acid from M to V at position 186.
+The protein's natural variant, known as in MMAM; mut0;, features a modification of the amino acid from T to S at position 187.
+The protein's natural variant, known as in MMAM; mut-; decreased protein abundance; decreased methylmalonyl-CoA mutase activity;, features a modification of the amino acid from N to I at position 189.
+The protein's natural variant, known as in MMAM; mut-;, features a modification of the amino acid from N to K at position 189.
+The protein's natural variant, known as in MMAM; mut- and mut0; affects proper folding; reduced protein level; decreased methylmalonyl-CoA mutase activity;, features a modification of the amino acid from A to E at position 191.
+The protein's natural variant, known as in MMAM; mut0, features a modification of the amino acid from A to E at position 197.
+The protein's natural variant, known as in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity;, features a modification of the amino acid from G to R at position 203.
+The protein's natural variant, known as in MMAM; mut- and mut0;, features a modification of the amino acid from G to C at position 215.
+The protein's natural variant, known as in MMAM; mut0;, features a modification of the amino acid from G to S at position 215.
+The protein's natural variant, known as in MMAM; mut0 and mut-; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; alters thermodynamic stability;, features a modification of the amino acid from Q to H at position 218.
+The protein's natural variant, known as in MMAM; mut0; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity;, features a modification of the amino acid from N to Y at position 219.
+The protein's natural variant, known as in MMAM; mut0;, features a modification of the amino acid from R to Q at position 228.
+The protein's natural variant, known as in MMAM; mut-, features a modification of the amino acid from T to I at position 230.
+The protein's natural variant, known as in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity;, features a modification of the amino acid from T to R at position 230.
+The protein's natural variant, known as in MMAM; mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; strong decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability;, features a modification of the amino acid from Y to N at position 231.
+The protein's natural variant, known as in MMAM; mut0, features a modification of the amino acid from S to N at position 262.
+The protein's natural variant, known as in MMAM; mut-, features a modification of the amino acid from H to Y at position 265.
+The protein's natural variant, known as in MMAM; mut-; unknown pathological significance;, features a modification of the amino acid from E to D at position 276.
+The protein's natural variant, known as in MMAM; mut0;, features a modification of the amino acid from L to S at position 281.
+The protein's natural variant, known as in MMAM; mut0;, features a modification of the amino acid from G to E at position 284.
+The protein's natural variant, known as in MMAM; mut0;, features a modification of the amino acid from G to R at position 284.
+The protein's natural variant, known as in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity;, features a modification of the amino acid from S to P at position 288.
+The protein's natural variant, known as in MMAM; mut0, features a modification of the amino acid from G to E at position 291.
+The protein's natural variant, known as in MMAM; mut0, features a modification of the amino acid from Q to P at position 293.
+The protein's natural variant, known as in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity;, features a modification of the amino acid from L to S at position 305.
+The protein's natural variant, known as in MMAM; mut0;, features a modification of the amino acid from S to F at position 306.
+The protein's natural variant, known as in MMAM; decreased protein expression, features a modification of the amino acid from W to G at position 309.
+The protein's natural variant, known as in MMAM; mut0;, features a modification of the amino acid from G to V at position 312.
+The protein's natural variant, known as in MMAM; mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; no decreased affinity for adenosylcob(III)alamin;, features a modification of the amino acid from Y to C at position 316.
+The protein's natural variant, known as in MMAM; mut-;, features a modification of the amino acid from A to T at position 324.
+The protein's natural variant, known as in MMAM;, features a modification of the amino acid from G to D at position 325.
+The protein's natural variant, known as in MMAM; unknown pathological significance;, features a modification of the amino acid from R to K at position 326.
+The protein's natural variant, known as in MMAM; mut0; affects proper folding; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity;, features a modification of the amino acid from L to F at position 328.
+The protein's natural variant, known as in MMAM; mut0;, features a modification of the amino acid from L to P at position 328.
+The protein's natural variant, known as in MMAM; mut-; affects proper folding; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin, features a modification of the amino acid from S to F at position 344.
+The protein's natural variant, known as in MMAM; mut0;, features a modification of the amino acid from L to R at position 347.
+The protein's natural variant, known as in MMAM; mut0;, features a modification of the amino acid from H to Y at position 350.
+The protein's natural variant, known as in MMAM; mut0, features a modification of the amino acid from L to P at position 358.
+The protein's natural variant, known as in MMAM;, features a modification of the amino acid from Y to S at position 364.
+The protein's natural variant, known as in MMAM; mut-; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability;, features a modification of the amino acid from N to S at position 366.
+The protein's natural variant, known as in MMAM, features a modification of the amino acid from V to D at position 368.
+The protein's natural variant, known as in MMAM; mut0;, features a modification of the amino acid from R to C at position 369.
+The protein's natural variant, known as in MMAM; mut- and mut0; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; alters thermodynamic stability;, features a modification of the amino acid from R to H at position 369.
+The protein's natural variant, known as in MMAM; mut0;, features a modification of the amino acid from T to P at position 370.
+The protein's natural variant, known as in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity;, features a modification of the amino acid from A to E at position 377.
+The protein's natural variant, known as in MMAM; mut0, features a modification of the amino acid from Q to H at position 383.
+The protein's natural variant, known as in MMAM; mut0, features a modification of the amino acid from Q to P at position 383.
+The protein's natural variant, known as in MMAM; mut0;, features a modification of the amino acid from H to N at position 386.
+The protein's natural variant, known as in MMAM; mut0;, features a modification of the amino acid from H to R at position 386.
+The protein's natural variant, known as in MMAM; mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability, features a modification of the amino acid from T to I at position 387.
+The protein's natural variant, known as in MMAM; mut0;, features a modification of the amino acid from N to H at position 388.
+The protein's natural variant, known as in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity;, features a modification of the amino acid from N to K at position 388.
+The protein's natural variant, known as in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity;, features a modification of the amino acid from P to L at position 424.
+The protein's natural variant, known as in MMAM; mut-; decreased protein abundance; decreased methylmalonyl-CoA mutase activity;, features a modification of the amino acid from G to E at position 426.
+The protein's natural variant, known as in MMAM; mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; strong decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability;, features a modification of the amino acid from G to R at position 426.
+The protein's natural variant, known as in MMAM; mut0;, features a modification of the amino acid from G to D at position 427.
+The protein's natural variant, known as in MMAM; mut0, features a modification of the amino acid from G to E at position 454.
+The protein's natural variant, known as in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity, features a modification of the amino acid from I to T at position 505.
+The protein's natural variant, known as in MMAM; unknown pathological significance, features a modification of the amino acid from Q to E at position 514.
+The protein's natural variant, known as in MMAM; decreased protein expression, features a modification of the amino acid from Q to K at position 514.
+The protein's natural variant, known as in MMAM; mut0;, features a modification of the amino acid from L to P at position 518.
+The protein's natural variant, known as in MMAM; mut0;, features a modification of the amino acid from A to P at position 535.
+The protein's natural variant, known as in MMAM; unknown pathological significance;, features a modification of the amino acid from A to V at position 552.
+The protein's natural variant, known as in MMAM; mut0;, features a modification of the amino acid from C to Y at position 560.
+The protein's natural variant, known as in MMAM; mut0, features a modification of the amino acid from T to R at position 566.
+The protein's natural variant, known as in MMAM; mut-; affects proper folding; no effect on protein abundance; no effect on methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; does not alter thermodynamic stability;, features a modification of the amino acid from F to S at position 573.
+The protein's natural variant, known as in MMAM; mut-, features a modification of the amino acid from Y to C at position 587.
+The protein's natural variant, known as in MMAM; no changed in protein expression; decreased methylmalonyl-CoA mutase activity;, features a modification of the amino acid from I to R at position 597.
+The protein's natural variant, known as in MMAM; mut0; affects proper folding; reduced strongly protein level, features a modification of the amino acid from P to L at position 615.
+The protein's natural variant, known as in MMAM; mut0;, features a modification of the amino acid from P to R at position 615.
+The protein's natural variant, known as in MMAM; mut0; affects proper folding; reduced strongly protein level; loss of methylmalonyl-CoA mutase activity;, features a modification of the amino acid from P to T at position 615.
+The protein's natural variant, known as in MMAM; mut0;, features a modification of the amino acid from R to C at position 616.
+The protein's natural variant, known as in MMAM; mut0;, features a modification of the amino acid from L to R at position 617.
+The protein's natural variant, known as in MMAM;, features a modification of the amino acid from L to P at position 618.
+The protein's natural variant, known as in MMAM; mut0, features a modification of the amino acid from K to N at position 621.
+The protein's natural variant, known as in MMAM; mut0;, features a modification of the amino acid from G to R at position 623.
+The protein's natural variant, known as in MMAM; no effect on protein abundance;, features a modification of the amino acid from Q to R at position 624.
+The protein's natural variant, known as in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity;, features a modification of the amino acid from D to G at position 625.
+The protein's natural variant, known as in MMAM; mut0; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity, features a modification of the amino acid from D to V at position 625.
+The protein's natural variant, known as in MMAM; mut-;, features a modification of the amino acid from G to C at position 626.
+The protein's natural variant, known as in MMAM; mut0;, features a modification of the amino acid from H to R at position 627.
+The protein's natural variant, known as in MMAM; mut0;, features a modification of the amino acid from G to E at position 630.
+The protein's natural variant, known as in MMAM; mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; does not alter thermodynamic stability;, features a modification of the amino acid from V to G at position 633.
+The protein's natural variant, known as in MMAM; mut-, features a modification of the amino acid from G to E at position 637.
+The protein's natural variant, known as in MMAM; mut0;, features a modification of the amino acid from G to R at position 637.
+The protein's natural variant, known as in MMAM; mut0, features a modification of the amino acid from F to I at position 638.
+The protein's natural variant, known as in MMAM; mut0;, features a modification of the amino acid from D to Y at position 640.
+The protein's natural variant, known as in MMAM; mut-;, features a modification of the amino acid from G to R at position 642.
+The protein's natural variant, known as in MMAM; mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; strong decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability;, features a modification of the amino acid from G to D at position 648.
+The protein's natural variant, known as in MMAM; mut0;, features a modification of the amino acid from V to E at position 669.
+The protein's natural variant, known as in MMAM; decreased protein abundance; decreased methylmalonyl-CoA mutase activity;, features a modification of the amino acid from L to F at position 674.
+The protein's natural variant, known as in MMAM; mut-;, features a modification of the amino acid from H to R at position 678.
+The protein's natural variant, known as in MMAM; mut-, features a modification of the amino acid from E to EL at position 684.
+The protein's natural variant, known as in MMAM; mut-;, features a modification of the amino acid from L to R at position 685.
+The protein's natural variant, known as in MMAM, features a modification of the amino acid from L to P at position 692.
+The protein's natural variant, known as in MMAM; mut-; decreased protein abundance; loss of methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability, features a modification of the amino acid from R to L at position 694.
+The protein's natural variant, known as in MMAM; mut- and mut0; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability;, features a modification of the amino acid from R to W at position 694.
+The protein's natural variant, known as in MMAM; mut-; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability;, features a modification of the amino acid from M to K at position 700.
+The protein's natural variant, known as in MMAM; mut0;, features a modification of the amino acid from G to R at position 703.
+The protein's natural variant, known as in MMAM; mut-; no effect on protein abundance; interfers with the binding of the cofactor to the apoenzyme; decreased methylmalonyl-CoA mutase activity; strong decreased affinity for adenosylcob(III)alamin; decreased thermodynamic stability;, features a modification of the amino acid from G to V at position 717.
+The protein's natural variant, known as in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity;, features a modification of the amino acid from G to D at position 723.
+The protein's natural variant, known as in MMAM;, features a modification of the amino acid from L to F at position 736.
+The protein's natural variant, known as inactive enzyme, features a modification of the amino acid from Y to G at position 27.
+The protein's natural variant, known as in teniposide (VM-26) resistant cells;, features a modification of the amino acid from R to Q at position 450.
+The protein's natural variant, known as in amsacrine resistant cells;, features a modification of the amino acid from R to K at position 487.
+The natural variant of this protein is characterized by an amino acid alteration from K to A at position 232.
+The protein's natural variant, known as in allele DMA*01:03 and allele DMA*01:04, features a modification of the amino acid from H to Q at position 162.
+The protein's natural variant, known as in allele DMA*01:03 and allele DMA*01:04, features a modification of the amino acid from D to H at position 163.
+The protein's natural variant, known as in allele DMA*01:02 and allele DMA*01:04;, features a modification of the amino acid from V to I at position 166.
+The protein's natural variant, known as in allele DMA*01:03;, features a modification of the amino acid from G to A at position 181.
+The protein's natural variant, known as in allele DMA*01:04;, features a modification of the amino acid from R to C at position 210.
+The protein's natural variant, known as in allele DMA*01:03;, features a modification of the amino acid from R to H at position 210.
+The protein's natural variant, known as in a lung neuroendocrine carcinoma sample; somatic mutation;, features a modification of the amino acid from R to W at position 295.
+The protein's natural variant, known as in a gastric adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from R to C at position 499.
+The protein's natural variant, known as found in a patient with features of Robinow syndrome; unknown pathological significance;, features a modification of the amino acid from R to K at position 412.
+The protein's natural variant, known as in strain: MA2, features a modification of the amino acid from A to V at position 80.
+The protein's natural variant, known as in QME;, features a modification of the amino acid from V to D at position 64.
+The protein's natural variant, known as in ARCND3;, features a modification of the amino acid from P to H at position 77.
+The protein's natural variant, known as in ARCND3;, features a modification of the amino acid from K to E at position 91.
+The protein's natural variant, known as associated with HDL cholesterol levels is some populations and in a sex-specific manner;, features a modification of the amino acid from K to N at position 198.
+The protein's natural variant, known as in KTZSL; unknown pathological significance, features a modification of the amino acid from P to L at position 181.
+The protein's natural variant, known as in KTZSL, features a modification of the amino acid from M to V at position 323.
+The protein's natural variant, known as no effect on DNA-binding or transcriptional repression, features a modification of the amino acid from S to L at position 366.
+The protein's natural variant, known as in KTZSL, features a modification of the amino acid from Q to R at position 402.
+The protein's natural variant, known as in KTZSL; stabilized DNA-binding and increased transcriptional repression, features a modification of the amino acid from E to G at position 407.
+The protein's natural variant, known as in KTZSL, features a modification of the amino acid from E to Q at position 407.
+The protein's natural variant, known as in KTZSL, features a modification of the amino acid from E to K at position 413.
+The protein's natural variant, known as in KTZSL; stabilized DNA-binding and increased transcriptional repression, features a modification of the amino acid from Q to R at position 420.
+The protein's natural variant, known as no effect on DNA-binding or transcriptional repression, features a modification of the amino acid from V to L at position 519.
+The protein's natural variant, known as in KTZSL, features a modification of the amino acid from Q to R at position 525.
+The protein's natural variant, known as in KTZSL, features a modification of the amino acid from E to G at position 530.
+The protein's natural variant, known as in KTZSL; stabilized DNA-binding and increased transcriptional repression, features a modification of the amino acid from E to K at position 530.
+The protein's natural variant, known as in KTZSL; stabilized DNA-binding and increased transcriptional repression, features a modification of the amino acid from E to Q at position 530.
+The protein's natural variant, known as in KTZSL; stabilized DNA-binding and increased transcriptional repression, features a modification of the amino acid from E to K at position 547.
+The protein's natural variant, known as no effect on DNA-binding or transcriptional repression, features a modification of the amino acid from A to T at position 573.
+The protein's natural variant, known as in KTZSL, features a modification of the amino acid from H to R at position 577.
+The protein's natural variant, known as in KTZSL; unknown pathological significance, features a modification of the amino acid from Q to R at position 619.
+The protein's natural variant, known as in KTZSL; unknown pathological significance; no effect on DNA-binding or transcriptional repression, features a modification of the amino acid from L to V at position 682.
+The protein's natural variant, known as in strain: D273-10B/A1, features a modification of the amino acid from I to M at position 171.
+The protein's natural variant, known as in strain: D273-10B/A1, features a modification of the amino acid from F to I at position 177.
+The protein's natural variant, known as in strain: D273-10B/A1, features a modification of the amino acid from M to I at position 231.
+The protein's natural variant, known as in strain: D273-10B/A1, features a modification of the amino acid from G to S at position 241.
+The protein's natural variant, known as in strain: D273-10B/A1, features a modification of the amino acid from A to T at position 245.
+The protein's natural variant, known as in strain: D273-10B/A1, features a modification of the amino acid from AV to TL at position 256.
+The protein's natural variant, known as in strain: JA176; unable to grow on galactarate, glucarate and glycerate, features a modification of the amino acid from P to S at position 292.
+The protein's natural variant, known as in an autistic patient, features a modification of the amino acid from S to G at position 82.
+The protein's natural variant, known as in an autistic patient;, features a modification of the amino acid from R to G at position 798.
+The protein's natural variant, known as in a family with an autistic patient;, features a modification of the amino acid from P to T at position 854.
+The protein's natural variant, known as the property of the variant is indistinguishable from the wild-type;, features a modification of the amino acid from L to P at position 36.
+The protein's natural variant, known as the property of the variant is indistinguishable from the wild-type;, features a modification of the amino acid from L to V at position 36.
+The protein's natural variant, known as the property of the variant is indistinguishable from the wild-type;, features a modification of the amino acid from S to Y at position 41.
+The protein's natural variant, known as the property of the variant is indistinguishable from the wild-type;, features a modification of the amino acid from R to C at position 55.
+The protein's natural variant, known as may be associated with susceptibility to bipolar affective disorder; decreases solubility; decreases thermal stability; catalytic activity as the wild type; moderate loss-of-function observed manifested via stability and solubility effect;, features a modification of the amino acid from P to S at position 206.
+The protein's natural variant, known as in ADHD7; has severely reduced solubility; is completely inactive; loss of function may lead to a reduced serotonin synthesis;, features a modification of the amino acid from R to W at position 303.
+The protein's natural variant, known as moderate loss-of-function observed manifested via stability and solubility effect;, features a modification of the amino acid from A to V at position 328.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from R to G at position 433.
+The protein's natural variant, known as linked with susceptibility to major depressive disorder; may be due to a rare RNA editing event; 80% loss of function; decreases solubility; decreases thermal stability; reduces catalytic activity;, features a modification of the amino acid from R to H at position 441.
+The protein's natural variant, known as in RNA edited version;, features a modification of the amino acid from Q to R at position 468.
+The protein's natural variant, known as moderate loss-of-function observed manifested via stability and solubility effect;, features a modification of the amino acid from D to E at position 479.
+The protein's natural variant, known as in LDYT; decrease in enzyme activity;, features a modification of the amino acid from I to M at position 26.
+The protein's natural variant, known as in LHON;, features a modification of the amino acid from G to S at position 36.
+The protein's natural variant, known as in LHON;, features a modification of the amino acid from Y to C at position 59.
+The protein's natural variant, known as in LHON;, features a modification of the amino acid from L to S at position 60.
+The protein's natural variant, known as in LS; decrease in enzyme activity and impaired assembly of complex I;, features a modification of the amino acid from M to V at position 63.
+The protein's natural variant, known as in LHON;, features a modification of the amino acid from M to I at position 64.
+The protein's natural variant, known as in LHON; low severity; up to 50% of vision recovery; results in decreased complex I activity;, features a modification of the amino acid from M to V at position 64.
+The protein's natural variant, known as in LDYT; most severe mutation with no vision recovery;, features a modification of the amino acid from A to V at position 72.
+The protein's natural variant, known as in MELAS;, features a modification of the amino acid from A to V at position 74.
+The protein's natural variant, known as in allele A4, features a modification of the amino acid from L to I at position 22.
+The protein's natural variant, known as in allele A3, features a modification of the amino acid from L to S at position 24.
+The protein's natural variant, known as in allele A2 and allele A3, features a modification of the amino acid from K to R at position 35.
+The protein's natural variant, known as in allele A2 and allele A4, features a modification of the amino acid from I to F at position 36.
+The protein's natural variant, known as in allele A2, features a modification of the amino acid from Q to H at position 37.
+The protein's natural variant, known as in allele A2, features a modification of the amino acid from GG to AV at position 44.
+The protein's natural variant, known as in allele A4, features a modification of the amino acid from T to S at position 46.
+The protein's natural variant, known as in allele A2, allele A3 and allele A4, features a modification of the amino acid from T to M at position 53.
+The protein's natural variant, known as in allele A2, allele A3 and allele A4, features a modification of the amino acid from QK to HE at position 57.
+The protein's natural variant, known as in allele A3 and allele A4, features a modification of the amino acid from A to T at position 65.
+The protein's natural variant, known as in allele A3 and allele A4, features a modification of the amino acid from N to K at position 70.
+The protein's natural variant, known as in allele A4, features a modification of the amino acid from VLT to MLK at position 73.
+The protein's natural variant, known as in allele A2 and allele A3, features a modification of the amino acid from I to T at position 75.
+The protein's natural variant, known as in allele A4, features a modification of the amino acid from L to T at position 106.
+The protein's natural variant, known as in allele A2 and allele A4, features a modification of the amino acid from Q to R at position 107.
+The protein's natural variant, known as in allele A3, features a modification of the amino acid from V to I at position 146.
+The protein's natural variant, known as in allele A2, allele A3 and allele A4, features a modification of the amino acid from S to A at position 152.
+The protein's natural variant, known as in allele A2, allele A3 and allele A4, features a modification of the amino acid from K to R at position 164.
+The protein's natural variant, known as in allele A2, features a modification of the amino acid from H to Y at position 197.
+The protein's natural variant, known as in allele A4, features a modification of the amino acid from G to A at position 205.
+The protein's natural variant, known as in allele A4, features a modification of the amino acid from A to S at position 222.
+The protein's natural variant, known as in allele A4, features a modification of the amino acid from R to S at position 233.
+The protein's natural variant, known as in allele A4, features a modification of the amino acid from R to Q at position 235.
+The protein's natural variant, known as in allele A4, features a modification of the amino acid from P to S at position 245.
+The protein's natural variant, known as in allele A4, features a modification of the amino acid from R to G at position 253.
+The protein's natural variant, known as in allele A2, allele A3 and allele A4, features a modification of the amino acid from V to L at position 270.
+The protein's natural variant, known as in allele A2, allele A3 and allele A4, features a modification of the amino acid from Q to K at position 281.
+The protein's natural variant, known as in allele A4, features a modification of the amino acid from V to L at position 284.
+The protein's natural variant, known as in allele A2 and allele A3, features a modification of the amino acid from Q to K at position 287.
+The protein's natural variant, known as in allele A2 and allele A3, features a modification of the amino acid from H to Y at position 300.
+The protein's natural variant, known as in strain: Dahl salt-resistant, features a modification of the amino acid from R to C at position 127.
+The protein's natural variant, known as in strain: Dahl salt-resistant, features a modification of the amino acid from V to A at position 351.
+The protein's natural variant, known as in strain: Dahl salt-resistant, features a modification of the amino acid from V to L at position 381.
+The protein's natural variant, known as in strain: Dahl salt-resistant, features a modification of the amino acid from I to L at position 384.
+The protein's natural variant, known as in strain: Dahl salt-resistant, features a modification of the amino acid from V to M at position 443.
+The natural variant of this protein is characterized by an amino acid alteration from K to N at position 628.
+The protein's natural variant, known as in bpa; does not rescue the yeast mutant lacking the ortholog erg26, features a modification of the amino acid from V to D at position 53.
+The protein's natural variant, known as in bpa; does not rescue the yeast mutant lacking the ortholog erg26, features a modification of the amino acid from A to T at position 94.
+The protein's natural variant, known as in str; does not rescue the yeast mutant lacking the ortholog erg26, features a modification of the amino acid from P to L at position 98.
+The protein's natural variant, known as in str; rescues the yeast mutant lacking the ortholog erg26, features a modification of the amino acid from V to M at position 109.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from G to A at position 145.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from N to K at position 165.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from P to S at position 569.
+The protein's natural variant, known as in ARCI2;, features a modification of the amino acid from L to P at position 24.
+The protein's natural variant, known as in ARCI2;, features a modification of the amino acid from I to F at position 67.
+The protein's natural variant, known as in ARCI2;, features a modification of the amino acid from R to W at position 114.
+The protein's natural variant, known as in ARCI2;, features a modification of the amino acid from P to S at position 127.
+The protein's natural variant, known as in ARCI2; complete loss of the enzyme activity;, features a modification of the amino acid from F to L at position 195.
+The protein's natural variant, known as in ARCI2, features a modification of the amino acid from Y to C at position 318.
+The protein's natural variant, known as in ARCI2; complete loss of the enzyme activity;, features a modification of the amino acid from K to E at position 382.
+The protein's natural variant, known as in ARCI2;, features a modification of the amino acid from T to M at position 383.
+The protein's natural variant, known as in ARCI2;, features a modification of the amino acid from N to K at position 416.
+The protein's natural variant, known as in ARCI2; complete loss of the enzyme activity;, features a modification of the amino acid from L to P at position 426.
+The protein's natural variant, known as in ARCI2;, features a modification of the amino acid from G to D at position 462.
+The protein's natural variant, known as in ARCI2; complete loss of the enzyme activity;, features a modification of the amino acid from R to H at position 488.
+The protein's natural variant, known as in ARCI2;, features a modification of the amino acid from Y to C at position 521.
+The protein's natural variant, known as in ARCI2;, features a modification of the amino acid from V to M at position 527.
+The protein's natural variant, known as in ARCI2; complete loss of the enzyme activity;, features a modification of the amino acid from H to Q at position 578.
+The protein's natural variant, known as in ARCI2;, features a modification of the amino acid from A to E at position 597.
+The protein's natural variant, known as in ARCI2; complete loss of the enzyme activity, features a modification of the amino acid from A to P at position 664.
+The protein's natural variant, known as in ARCI2;, features a modification of the amino acid from R to L at position 679.
+The protein's natural variant, known as in strain: T2, features a modification of the amino acid from K to Q at position 184.
+The protein's natural variant, known as in strain: T2, features a modification of the amino acid from A to T at position 224.
+The protein's natural variant, known as in strain: T2, features a modification of the amino acid from S to T at position 273.
+The protein's natural variant, known as in DFNA40, features a modification of the amino acid from K to KYNKGT at position 314.
+The protein's natural variant, known as in DFNA40;, features a modification of the amino acid from K to T at position 314.
+The protein's natural variant, known as in plasmid pWR100, plasmid pWR501, plasmid pSF5 and plasmid pINV_F6_M1382, features a modification of the amino acid from P to Q at position 222.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from Q to L at position 474.
+The protein's natural variant, known as in plasmid pWR100 and plasmid pWR501, features a modification of the amino acid from P to F at position 536.
+The protein's natural variant, known as in plasmid pSF5, features a modification of the amino acid from P to S at position 536.
+The protein's natural variant, known as in strain: S108, features a modification of the amino acid from Y to C at position 29.
+The protein's natural variant, known as in strain: FSP2, FSP15, FSP16, FSP19, FSP23, FSP29, RR8, RR11, RR17, RR18, RR35, RR52, S76, SL5_131, SL5_29, T28 and T39, features a modification of the amino acid from P to T at position 165.
+The protein's natural variant, known as in strain: FSP19, RR33 and S108, features a modification of the amino acid from A to V at position 429.
+The protein's natural variant, known as in strain: RR33, S108, T28 and T39, features a modification of the amino acid from A to T at position 452.
+The protein's natural variant, known as in strain: FSP2, FSP3, FSP15, FSP19, FSP23, FSP25, FSP29, RR8, RR11, RR17, RR18, RR33, RR35, RR52, S76, S107, S108, T9, T15, T28, T39 and T41, features a modification of the amino acid from K to R at position 664.
+The protein's natural variant, known as in strain: S103, features a modification of the amino acid from P to S at position 675.
+The protein's natural variant, known as in strain: FSP3, FSP15, FSP19, FSP23, FSP25, RR8, RR11, RR17, RR33, RR35, RR52, S76, S97, S107, S108, T9, T28, T39 and T41, features a modification of the amino acid from L to I at position 676.
+The protein's natural variant, known as in strain: FSP2, FSP3, FSP15, FSP23, FSP25, FSP29, RR8, RR11, RR17, RR18, RR33, RR35, RR52, S108, T9, T15, T28, T39 and T41, features a modification of the amino acid from S to G at position 721.
+The protein's natural variant, known as in strain: FSP2, FSP3, FSP15, FSP16, FSP19, FSP23, FSP25, FSP29, RR8, RR11, RR17, RR18, RR33, RR35, RR52, S76, S97, S103, S107, S108, SL5_131, SL5_29, T9, T15, T28, T39 and T41, features a modification of the amino acid from S to L at position 722.
+The protein's natural variant, known as in strain: FSP3, FSP15, FSP16, FSP23, FSP25, FSP29, RR8, RR11, RR17, RR33, RR35, RR52, S108, T9, T15, T28, T39 and T41, features a modification of the amino acid from C to S at position 744.
+The protein's natural variant, known as in strain: RR8 and T41, features a modification of the amino acid from I to M at position 808.
+The protein's natural variant, known as in strain: FSP19, features a modification of the amino acid from A to V at position 851.
+The protein's natural variant, known as in strain: FSP16, features a modification of the amino acid from A to T at position 873.
+The protein's natural variant, known as in roughened mutants, features a modification of the amino acid from F to L at position 157.
+The protein's natural variant, known as in CDDG2; unknown pathological significance; results in defective processing of free oligosaccharides as shown by complementation assay in MAN2C1-deficient cells;, features a modification of the amino acid from G to R at position 203.
+The protein's natural variant, known as in CDDG2; unknown pathological significance; severely decreased mannosidase activity; results in defective processing of free oligosaccharides as shown by complementation assay in MAN2C1-deficient cells;, features a modification of the amino acid from R to Q at position 768.
+The protein's natural variant, known as in CDDG2; unknown pathological significance; has no effect on processing of free oligosaccharides as shown by complementation assay in MAN2C1-deficient cells;, features a modification of the amino acid from C to S at position 871.
+The protein's natural variant, known as in CILD11;, features a modification of the amino acid from P to S at position 87.
+The protein's natural variant, known as in CILD11; unknown pathological significance;, features a modification of the amino acid from G to E at position 464.
+The protein's natural variant, known as in strain: TREU66, features a modification of the amino acid from A to P at position 192.
+The protein's natural variant, known as in strain: TREU66, features a modification of the amino acid from K to L at position 199.
+The natural variant of this protein is characterized by an amino acid alteration from R to S at position 3.
+The natural variant of this protein is characterized by an amino acid alteration from E to S at position 24.
+The protein's natural variant, known as in RHUC1; unknown pathological significance; reduced urate transport; decreased localization to cell membrane;, features a modification of the amino acid from I to T at position 75.
+The protein's natural variant, known as in RHUC1; strongly reduced urate transport;, features a modification of the amino acid from R to H at position 90.
+The protein's natural variant, known as in RHUC1; strongly reduced urate transport;, features a modification of the amino acid from V to M at position 138.
+The protein's natural variant, known as in RHUC1; reduced urate transport;, features a modification of the amino acid from G to S at position 164.
+The protein's natural variant, known as in RHUC1; strongly reduced urate transport;, features a modification of the amino acid from T to M at position 217.
+The protein's natural variant, known as in some gout patients; uncertain pathological significance, features a modification of the amino acid from R to G at position 284.
+The protein's natural variant, known as in some gout patients; uncertain pathological significance, features a modification of the amino acid from G to C at position 290.
+The protein's natural variant, known as in some gout patients; uncertain pathological significance, features a modification of the amino acid from Q to E at position 297.
+The protein's natural variant, known as in RHUC1; strongly reduced urate transport;, features a modification of the amino acid from E to D at position 298.
+The protein's natural variant, known as in some gout patients; uncertain pathological significance, features a modification of the amino acid from I to S at position 305.
+The natural variant of this protein is characterized by an amino acid alteration from Q to L at position 312.
+The protein's natural variant, known as in RHUC1; unknown pathological significance; reduced urate transport; no effect on its localization to cell membrane;, features a modification of the amino acid from R to S at position 347.
+The protein's natural variant, known as in RHUC1; reduced urate transport; reduced localization at the plasma membrane;, features a modification of the amino acid from G to R at position 366.
+The protein's natural variant, known as in RHUC1; strongly reduced urate transport;, features a modification of the amino acid from Q to L at position 382.
+The protein's natural variant, known as in RHUC1; unknown pathological significance; no effect on urate transport; no effect on its localization to cell membrane;, features a modification of the amino acid from V to M at position 388.
+The protein's natural variant, known as in RHUC1; strongly reduced urate transport;, features a modification of the amino acid from L to R at position 418.
+The protein's natural variant, known as in RHUC1; reduced urate transport;, features a modification of the amino acid from M to T at position 430.
+The protein's natural variant, known as in RHUC1; unknown pathological significance; strongly reduced urate transport; abolishes localization to cell membrane;, features a modification of the amino acid from R to C at position 434.
+The protein's natural variant, known as in RHUC1; unknown pathological significance; reduced urate transport; abolishes localization to cell membrane;, features a modification of the amino acid from R to H at position 434.
+The protein's natural variant, known as in RHUC1;, features a modification of the amino acid from R to H at position 477.
+The protein's natural variant, known as risk factor for drug-induced arrhythmia; impedes activation and increases sensitivity to macrolide antibiotics; may lower current in KCNQ1/KCNE2 channel;, features a modification of the amino acid from Q to E at position 9.
+The protein's natural variant, known as in LQT6; unknown pathological significance;, features a modification of the amino acid from V to I at position 14.
+The protein's natural variant, known as in LQT6; unknown pathological significance;, features a modification of the amino acid from I to N at position 20.
+The protein's natural variant, known as in ATFB4; gain-of-function mutation associated with the initiation and/or maintenance of AF;, features a modification of the amino acid from R to C at position 27.
+The protein's natural variant, known as in LQT6; unknown pathological significance;, features a modification of the amino acid from R to H at position 27.
+The protein's natural variant, known as in LQT6; forms I(KR) channels that deactivate twice as fast as wild type;, features a modification of the amino acid from M to T at position 54.
+The protein's natural variant, known as in LQT6; may affect KCNQ1/KCNE2 channel;, features a modification of the amino acid from I to T at position 57.
+The protein's natural variant, known as in LQT6; unknown pathological significance;, features a modification of the amino acid from F to L at position 60.
+The protein's natural variant, known as in LQT6; unknown pathological significance;, features a modification of the amino acid from V to L at position 65.
+The protein's natural variant, known as in LQT6;, features a modification of the amino acid from V to M at position 65.
+The protein's natural variant, known as in LQT6; unknown pathological significance;, features a modification of the amino acid from R to Q at position 77.
+The protein's natural variant, known as in LQT6;, features a modification of the amino acid from R to W at position 77.
+The protein's natural variant, known as in LQT6; unknown pathological significance;, features a modification of the amino acid from E to G at position 94.
+The protein's natural variant, known as in strain: ATCC 204278, features a modification of the amino acid from S to SSSSSSSSSSISLSSSSSSSSSSSSSSSS at position 264.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from R to K at position 427.
+The protein's natural variant, known as in OGIN; unknown pathological significance, features a modification of the amino acid from S to L at position 613.
+The protein's natural variant, known as in OGIN; unknown pathological significance, features a modification of the amino acid from S to F at position 720.
+The protein's natural variant, known as in OGIN; unknown pathological significance;, features a modification of the amino acid from R to W at position 800.
+The protein's natural variant, known as in OGIN; unknown pathological significance, features a modification of the amino acid from G to S at position 969.
+The protein's natural variant, known as in OGIN; unknown pathological significance, features a modification of the amino acid from R to K at position 1028.
+The protein's natural variant, known as in MGORS6;, features a modification of the amino acid from K to R at position 17.
+The protein's natural variant, known as in CACTD;, features a modification of the amino acid from R to W at position 133.
+The protein's natural variant, known as in CACTD;, features a modification of the amino acid from D to H at position 231.
+The protein's natural variant, known as in CACTD;, features a modification of the amino acid from Q to R at position 238.
+The protein's natural variant, known as in allele A, features a modification of the amino acid from G to S at position 89.
+The protein's natural variant, known as in allele A, features a modification of the amino acid from A to V at position 107.
+The natural variant of this protein is characterized by an amino acid alteration from S to R at position 31.
+The protein's natural variant, known as in ovarian cancer; somatic mutation;, features a modification of the amino acid from P to R at position 95.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from L to P at position 254.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to H at position 622.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from L to F at position 1039.
+The protein's natural variant, known as in MODY3; abolishes interaction with PCBD1 and DNA, features a modification of the amino acid from L to H at position 12.
+The protein's natural variant, known as in MODY3; abolishes interaction with PCBD1 and DNA, features a modification of the amino acid from G to R at position 20.
+The protein's natural variant, known as in MODY3; no effect on interaction with PCBD1 and DNA, features a modification of the amino acid from G to D at position 31.
+The protein's natural variant, known as in T1D20, features a modification of the amino acid from E to K at position 48.
+The protein's natural variant, known as in MODY3, features a modification of the amino acid from L to R at position 107.
+The protein's natural variant, known as in MODY3, features a modification of the amino acid from K to E at position 117.
+The protein's natural variant, known as in MODY3, features a modification of the amino acid from Y to C at position 122.
+The protein's natural variant, known as in a hepatocellular carcinoma sample; somatic mutation, features a modification of the amino acid from N to Y at position 127.
+The protein's natural variant, known as in MODY3, features a modification of the amino acid from I to N at position 128.
+The protein's natural variant, known as in MODY3, features a modification of the amino acid from P to T at position 129.
+The protein's natural variant, known as in MODY3, features a modification of the amino acid from R to Q at position 131.
+The protein's natural variant, known as in MODY3, features a modification of the amino acid from R to W at position 131.
+The protein's natural variant, known as in MODY3, features a modification of the amino acid from V to M at position 133.
+The protein's natural variant, known as in MODY3; reduces transcription activation by about 80%, features a modification of the amino acid from S to F at position 142.
+The protein's natural variant, known as in MODY3, features a modification of the amino acid from H to Y at position 143.
+The protein's natural variant, known as in MODY3, features a modification of the amino acid from K to N at position 158.
+The protein's natural variant, known as in MODY3, features a modification of the amino acid from R to Q at position 159.
+The protein's natural variant, known as in MODY3, features a modification of the amino acid from R to W at position 159.
+The protein's natural variant, known as in MODY3, features a modification of the amino acid from A to T at position 161.
+The protein's natural variant, known as in a hepatocellular carcinoma sample; somatic mutation, features a modification of the amino acid from W to C at position 165.
+The protein's natural variant, known as in late-onset NIDDM, features a modification of the amino acid from G to D at position 191.
+The protein's natural variant, known as in MODY3, features a modification of the amino acid from R to W at position 200.
+The protein's natural variant, known as in MODY3, features a modification of the amino acid from R to C at position 203.
+The protein's natural variant, known as in MODY3, features a modification of the amino acid from R to H at position 203.
+The protein's natural variant, known as in MODY3; reduces transcription activation by about 50%, features a modification of the amino acid from K to Q at position 205.
+The protein's natural variant, known as in a hepatic adenoma sample; somatic mutation, features a modification of the amino acid from W to C at position 206.
+The protein's natural variant, known as in a hepatic adenoma sample; somatic mutation, features a modification of the amino acid from W to L at position 206.
+The protein's natural variant, known as in MODY3, features a modification of the amino acid from R to Q at position 229.
+The protein's natural variant, known as in a hepatic multiple adenoma sample; somatic mutation, features a modification of the amino acid from N to S at position 237.
+The protein's natural variant, known as in T1D20 and MODY3, features a modification of the amino acid from C to G at position 241.
+The protein's natural variant, known as in a hepatic adenoma sample; somatic mutation, features a modification of the amino acid from R to G at position 244.
+The protein's natural variant, known as in a hepatocellular carcinoma sample; somatic mutation, features a modification of the amino acid from Q to P at position 250.
+The protein's natural variant, known as in late-onset NIDDM; low penetrance; unknown pathological significance, features a modification of the amino acid from L to M at position 254.
+The protein's natural variant, known as in MODY3, features a modification of the amino acid from V to D at position 259.
+The protein's natural variant, known as in MODY3, features a modification of the amino acid from T to M at position 260.
+The protein's natural variant, known as in MODY3, features a modification of the amino acid from R to C at position 263.
+The protein's natural variant, known as in a hepatic adenoma sample; somatic mutation, features a modification of the amino acid from F to C at position 268.
+The protein's natural variant, known as in MODY3, features a modification of the amino acid from R to G at position 271.
+The protein's natural variant, known as in MODY3, features a modification of the amino acid from R to W at position 271.
+The protein's natural variant, known as in NIDDM; loss of function in positive regulation of DNA-templated transcription, features a modification of the amino acid from R to C at position 272.
+The protein's natural variant, known as in T1D20 and MODY3, features a modification of the amino acid from R to H at position 272.
+The protein's natural variant, known as in a hepatic adenoma sample; somatic mutation, features a modification of the amino acid from K to E at position 273.
+The protein's natural variant, known as strong association with NIDDM susceptibility; unique to the Canadian Oji-Cree population, features a modification of the amino acid from G to S at position 319.
+The protein's natural variant, known as in T1D20; decreased function in positive regulation of DNA-templated transcription, features a modification of the amino acid from G to R at position 415.
+The protein's natural variant, known as in MODY3, features a modification of the amino acid from S to C at position 432.
+The protein's natural variant, known as in MODY3, features a modification of the amino acid from P to L at position 447.
+The natural variant of this protein is characterized by an amino acid alteration from H to R at position 514.
+The protein's natural variant, known as in MODY3, features a modification of the amino acid from P to L at position 519.
+The protein's natural variant, known as in MODY3; incomplete penetrance, features a modification of the amino acid from T to R at position 537.
+The protein's natural variant, known as in a black African with an atypical form of diabetes; also in an individual with hepatic adenoma and familial early-onset diabetes;, features a modification of the amino acid from G to S at position 574.
+The protein's natural variant, known as in T1D20, features a modification of the amino acid from R to G at position 583.
+The protein's natural variant, known as in late-onset NIDDM; also in an individual with hepatic hyperplasia and familial early-onset diabetes, features a modification of the amino acid from R to Q at position 583.
+The protein's natural variant, known as in MODY3, features a modification of the amino acid from S to I at position 594.
+The protein's natural variant, known as in MODY3, features a modification of the amino acid from I to M at position 618.
+The protein's natural variant, known as in MODY3, features a modification of the amino acid from E to K at position 619.
+The protein's natural variant, known as in MODY3; incomplete penetrance, features a modification of the amino acid from T to I at position 620.
+The protein's natural variant, known as in HALP1; reduced secretion into plasma, features a modification of the amino acid from L to P at position 168.
+The protein's natural variant, known as in HALP1; reduced secretion into plasma;, features a modification of the amino acid from R to C at position 299.
+The protein's natural variant, known as in HALP1;, features a modification of the amino acid from D to G at position 459.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to W at position 480.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from A to V at position 499.
+The protein's natural variant, known as requires 2 nucleotide substitutions;, features a modification of the amino acid from Y to T at position 84.
+The protein's natural variant, known as in SWS; found as somatic mosaic mutation in CMC; also found in melanocytomas sample; somatic mutation; shows significant activation of EPHB2 compared to control;, features a modification of the amino acid from R to Q at position 183.
+The protein's natural variant, known as found in blue naevi and uveal melanoma samples; somatic mutation; constitutive activation;, features a modification of the amino acid from Q to L at position 209.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from V to E at position 368.
+The protein's natural variant, known as in IDDHDF; contrary to the wild-type protein, does not rescue morpholino knockdown phenotype in zebrafish;, features a modification of the amino acid from K to E at position 111.
+The protein's natural variant, known as in motheaten (me), features a modification of the amino acid from EYYTQQQGILQDRDGTIIHLKYP to VPRPHIWRAGGVTAAGQGRALD at position 99.
+The protein's natural variant, known as in CVT; also in Charcot-Marie-Tooth disease-like foot deformities;, features a modification of the amino acid from M to K at position 319.
+The protein's natural variant, known as in strain: Isolate 2, features a modification of the amino acid from I to L at position 82.
+The protein's natural variant, known as in strain: Isolate 2, features a modification of the amino acid from D to G at position 228.
+The protein's natural variant, known as in strain: Breinl, features a modification of the amino acid from S to A at position 10.
+The protein's natural variant, known as in strain: Breinl, features a modification of the amino acid from H to L at position 15.
+The protein's natural variant, known as in strain: Breinl, features a modification of the amino acid from I to L at position 19.
+The protein's natural variant, known as in strain: Breinl, features a modification of the amino acid from D to E at position 96.
+The protein's natural variant, known as in strain: Breinl, features a modification of the amino acid from R to I at position 195.
+The protein's natural variant, known as in strain: Breinl, features a modification of the amino acid from K to R at position 216.
+The protein's natural variant, known as in strain: Breinl, features a modification of the amino acid from K to E at position 256.
+The protein's natural variant, known as in strain: Breinl, features a modification of the amino acid from D to Y at position 273.
+The protein's natural variant, known as in strain: Breinl, features a modification of the amino acid from K to N at position 282.
+The protein's natural variant, known as in strain: Breinl, features a modification of the amino acid from G to S at position 299.
+The protein's natural variant, known as in strain: Breinl, features a modification of the amino acid from L to F at position 310.
+The protein's natural variant, known as in rifampicin resistant mutant, features a modification of the amino acid from R to K at position 546.
+The protein's natural variant, known as in strain: KY038, features a modification of the amino acid from A to T at position 6.
+The protein's natural variant, known as in MRT34;, features a modification of the amino acid from G to R at position 128.
+The protein's natural variant, known as in DPYSD, features a modification of the amino acid from T to R at position 68.
+The protein's natural variant, known as in DPYSD;, features a modification of the amino acid from Q to R at position 334.
+The protein's natural variant, known as in DPYSD;, features a modification of the amino acid from W to R at position 360.
+The protein's natural variant, known as in DPYSD;, features a modification of the amino acid from G to R at position 435.
+The protein's natural variant, known as in DPYSD, features a modification of the amino acid from R to T at position 490.
+The protein's natural variant, known as in NS13; results in increased MAPK signaling; reduced interaction wth DUSP6; no effect on interaction with MAP2K1, features a modification of the amino acid from I to N at position 74.
+The protein's natural variant, known as in NS13; results in increased MAPK signaling; reduced interaction wth DUSP6; no effect on interaction with MAP2K1, features a modification of the amino acid from H to Y at position 80.
+The protein's natural variant, known as in NS13; results in increased MAPK signaling; increased translocation to the nucleus; reduced interaction wth DUSP6; no effect on interaction with MAP2K1, features a modification of the amino acid from A to V at position 174.
+The protein's natural variant, known as in NS13; results in increased MAPK signaling; increased translocation to the nucleus; reduced interaction wth DUSP6; no effect on interaction with MAP2K1, features a modification of the amino acid from D to G at position 318.
+The protein's natural variant, known as in NS13; results in increased MAPK signaling; increased translocation to the nucleus; reduced interaction wth DUSP6; no effect on interaction with MAP2K1, features a modification of the amino acid from D to N at position 318.
+The protein's natural variant, known as in NS13, features a modification of the amino acid from E to Q at position 322.
+The protein's natural variant, known as in NS13; results in increased MAPK signaling; increased translocation to the nucleus; reduced interaction wth DUSP6; no effect on interaction with MAP2K1, features a modification of the amino acid from P to R at position 323.
+The protein's natural variant, known as in NPHS9, features a modification of the amino acid from L to R at position 98.
+The protein's natural variant, known as in NPHS9;, features a modification of the amino acid from R to W at position 178.
+The protein's natural variant, known as in NPHS9;, features a modification of the amino acid from D to G at position 286.
+The protein's natural variant, known as in NPHS9, features a modification of the amino acid from P to L at position 310.
+The protein's natural variant, known as in NPHS9;, features a modification of the amino acid from R to W at position 320.
+The protein's natural variant, known as in NPHS9;, features a modification of the amino acid from R to W at position 343.
+The protein's natural variant, known as in NPHS9;, features a modification of the amino acid from R to Q at position 477.
+The protein's natural variant, known as in NPHS9, features a modification of the amino acid from A to E at position 498.
+The protein's natural variant, known as in DEDBANP; unknown pathological significance, features a modification of the amino acid from Y to C at position 346.
+The protein's natural variant, known as in DEDBANP; decreased G protein-coupled receptor signaling, features a modification of the amino acid from W to R at position 1005.
+The protein's natural variant, known as in DEDBANP; decreased G protein-coupled receptor signaling; decreased cell surface localization, features a modification of the amino acid from M to T at position 1152.
+The protein's natural variant, known as in DEDBANP; decreased G protein-coupled receptor signaling; decreased cell surface localization, features a modification of the amino acid from S to F at position 1164.
+The protein's natural variant, known as associated with an increased risk for coronary heart disease (CHD) in smoker and diabetic mellitus (DM) patients in a Chinese population; higher plasma symmetric (SDMA) dimethylarginine as well as plasma and urinary beta-aminoisobutyrate (BAIB) concentrations; localized to the mitochondrion as the wild-type; reduces alanine-glyoxylate aminotransferase activity;, features a modification of the amino acid from V to I at position 140.
+The protein's natural variant, known as higher plasma and urinary beta-aminoisobutyrate (BAIB) concentrations;, features a modification of the amino acid from V to L at position 498.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from A to T at position 386.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from H to Q at position 387.
+The protein's natural variant, known as in a renal clear cell carcinoma sample; somatic mutation;, features a modification of the amino acid from N to S at position 244.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from L to R at position 474.
+The protein's natural variant, known as in a gastric adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from R to W at position 635.
+The protein's natural variant, known as in a glioblastoma multiforme sample; somatic mutation, features a modification of the amino acid from S to F at position 769.
+The protein's natural variant, known as in an ovarian serous carcinoma sample; somatic mutation;, features a modification of the amino acid from P to L at position 830.
+The protein's natural variant, known as does not affect taurocholate transport activity; does not affect cell surface protein expression;, features a modification of the amino acid from S to L at position 56.
+The protein's natural variant, known as in PFIC2; loss of cell membrane localization; significantly reduces taurocholate transport activity, features a modification of the amino acid from C to Y at position 129.
+The protein's natural variant, known as in BRIC2;, features a modification of the amino acid from E to G at position 186.
+The protein's natural variant, known as impairs taurocholate transport activity; does not affect protein expression; does not affect cell surface protein expression; does not affect cell membrane localization;, features a modification of the amino acid from I to V at position 206.
+The protein's natural variant, known as in PFIC2;, features a modification of the amino acid from G to V at position 238.
+The protein's natural variant, known as in PFIC2, features a modification of the amino acid from V to L at position 284.
+The protein's natural variant, known as in PFIC2 and BRIC2; reduces transport capacity for taurocholate; decreases protein expression; affects maturation of protein in the reticulum endoplasmic; does not affect apical membrane localization; does not affect cell surface expression of the mature form; does not affect transport of taurocholate and glycocholate; enhances ubiquitination susceptibility; reduces transport activity of taurocholate in a low cholesterol environment; increases transport activity of taurocholate in a high cholesterol environment; does not affect protein expression; does not affect cell membrane localization;, features a modification of the amino acid from E to G at position 297.
+The protein's natural variant, known as in PFIC2;, features a modification of the amino acid from C to S at position 336.
+The protein's natural variant, known as in PFIC2; unknown pathological significance, features a modification of the amino acid from Y to H at position 337.
+The protein's natural variant, known as in BRIC2; reduced transport capacity for taurocholate; reduces transport activity of taurocholate in a low cholesterol environment; increases transport activity of taurocholate in a high cholesterol environment;, features a modification of the amino acid from R to T at position 432.
+The protein's natural variant, known as more frequent in patients with drug-induced cholestasis than healthy controls; associated with lower hepatic expression; does not affect transport capacity for taurocholate; increases transport activity of taurocholate in a low cholesterol environment; increases transport activity of taurocholate in a high cholesterol environment; does not affect cell surface protein expression; does not affect protein expression;, features a modification of the amino acid from V to A at position 444.
+The protein's natural variant, known as in PFIC2;, features a modification of the amino acid from K to E at position 461.
+The protein's natural variant, known as in PFIC2;, features a modification of the amino acid from Y to C at position 472.
+The protein's natural variant, known as in PFIC2; decreases protein expression; affects maturation of protein in the reticulum endoplasmic; decreases apical membrane localization; affects cell surface expression; does not affect transport of taurocholate and glycocholate; enhances ubiquitination susceptibility;, features a modification of the amino acid from D to G at position 482.
+The protein's natural variant, known as impairs taurocholate transport activity; does not affect protein expression; does not affect cell surface protein expression; does not affect cell membrane localization;, features a modification of the amino acid from Q to H at position 558.
+The protein's natural variant, known as in BRIC2;, features a modification of the amino acid from A to T at position 570.
+The protein's natural variant, known as in a patient with intrahepatic cholestasis of pregnancy; impairs taurocholate transport activity; does not affect protein expression; does not affect cell surface protein expression; does not affect cell membrane localization;, features a modification of the amino acid from N to S at position 591.
+The protein's natural variant, known as does not affect taurocholate transport activity; does not affect protein expression; does not affect cell surface protein expression;, features a modification of the amino acid from E to Q at position 592.
+The natural variant of this protein is characterized by an amino acid alteration from R to G at position 616.
+The protein's natural variant, known as in fluvastatin-induced cholestasis; does not affect transport capacity for taurocholate, features a modification of the amino acid from D to Y at position 676.
+The protein's natural variant, known as does not affect taurocholate transport activity; does not affect protein expression; does not affect cell surface protein expression;, features a modification of the amino acid from M to V at position 677.
+The protein's natural variant, known as in PFIC2; unknown pathological significance;, features a modification of the amino acid from R to W at position 696.
+The protein's natural variant, known as in ethinylestradiol/gestodene-induced cholestasis; loss of transport capacity for taurocholate, features a modification of the amino acid from G to R at position 855.
+The protein's natural variant, known as might be associated with increased risk of intrahepatic stones; decreases protein expression; deacreases localization to the cell membrane; decreases the trafficking to the plasma membrane;, features a modification of the amino acid from A to V at position 865.
+The protein's natural variant, known as in BRIC2;, features a modification of the amino acid from T to P at position 923.
+The protein's natural variant, known as in BRIC2;, features a modification of the amino acid from A to P at position 926.
+The protein's natural variant, known as in PFIC2; unknown pathological significance, features a modification of the amino acid from Q to P at position 931.
+The protein's natural variant, known as in PFIC2; impairs taurocholate transport activity; significantly reduces protein expression; decreases cell surface protein expression; loss of ell membrane localization;, features a modification of the amino acid from G to R at position 982.
+The protein's natural variant, known as in PFIC2, features a modification of the amino acid from G to D at position 1004.
+The protein's natural variant, known as in BRIC2;, features a modification of the amino acid from R to C at position 1050.
+The protein's natural variant, known as in BRIC2;, features a modification of the amino acid from R to H at position 1128.
+The protein's natural variant, known as in PFIC2, features a modification of the amino acid from D to V at position 1131.
+The protein's natural variant, known as in PFIC2; impairs taurocholate transport activity; significantly reduces protein expression; decreases cell surface protein expression; loss of ell membrane localization;, features a modification of the amino acid from R to C at position 1153.
+The protein's natural variant, known as impairs taurocholate transport activity; does not affect protein expression; decreases cell surface protein expression; reduces plasma membrane localization;, features a modification of the amino acid from E to K at position 1186.
+The protein's natural variant, known as in PFIC2; unknown pathological significance, features a modification of the amino acid from H to R at position 1198.
+The protein's natural variant, known as in PFIC2;, features a modification of the amino acid from R to Q at position 1268.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 113.
+The natural variant of this protein is characterized by an amino acid alteration from Q to R at position 118.
+The protein's natural variant, known as in CDG1WAD; partial loss of function, when tested in a heterologous system; does not affect expression levels, features a modification of the amino acid from H to R at position 46.
+The protein's natural variant, known as in CDG1WAD; partial loss of function, when tested in a heterologous system; does not affect expression levels, features a modification of the amino acid from R to Q at position 160.
+The protein's natural variant, known as in CDG1WAD; unknown pathological significance; partial loss of function, when tested in a heterologous system, features a modification of the amino acid from R to C at position 329.
+The protein's natural variant, known as in CDG1WAD; partial loss of function, when tested in a heterologous system; does not affect expression levels, features a modification of the amino acid from R to C at position 405.
+The protein's natural variant, known as in CDG1WAD, features a modification of the amino acid from R to H at position 405.
+The protein's natural variant, known as in CDG1WAD; unknown pathological significance; partial loss of function, when tested in a heterologous system; does not affect expression levels, features a modification of the amino acid from Y to S at position 530.
+The protein's natural variant, known as in CDG1WAD; unknown pathological significance; partial loss of function, when tested in a heterologous system; does not affect expression levels, features a modification of the amino acid from T to I at position 546.
+The protein's natural variant, known as in CDG1WAR; affects activity resulting in hypoglycosylation of STT3A-specific substrates;, features a modification of the amino acid from V to A at position 626.
+The protein's natural variant, known as in strain: Isolate Pacific ocean, features a modification of the amino acid from A to T at position 193.
+The protein's natural variant, known as in LORD;, features a modification of the amino acid from S to R at position 163.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from C to S at position 558.
+The natural variant of this protein is characterized by an amino acid alteration from L to F at position 131.
+The protein's natural variant, known as reduced transport of inosine and thymidine;, features a modification of the amino acid from G to R at position 367.
+The protein's natural variant, known as lower concentrative capacity and altered sodium binding capacity, features a modification of the amino acid from C to R at position 602.
+The protein's natural variant, known as in HA-GPID; GPIMatsumoto;, features a modification of the amino acid from T to I at position 5.
+The protein's natural variant, known as in HA-GPID; severe form with neurological deficits; GPIHomburg;, features a modification of the amino acid from H to P at position 20.
+The protein's natural variant, known as in HA-GPID; GPIElyria;, features a modification of the amino acid from R to G at position 75.
+The protein's natural variant, known as in HA-GPID;, features a modification of the amino acid from R to W at position 83.
+The protein's natural variant, known as in HA-GPID; GPISarcina;, features a modification of the amino acid from V to M at position 101.
+The protein's natural variant, known as in HA-GPID;, features a modification of the amino acid from G to S at position 159.
+The protein's natural variant, known as in HA-GPID; unknown pathological significance, features a modification of the amino acid from S to P at position 160.
+The protein's natural variant, known as in HA-GPID; GPIBari and Mola;, features a modification of the amino acid from T to I at position 195.
+The protein's natural variant, known as in HA-GPID; GPIIwate;, features a modification of the amino acid from T to M at position 224.
+The protein's natural variant, known as in HA-GPID;, features a modification of the amino acid from R to H at position 273.
+The protein's natural variant, known as in HA-GPID;, features a modification of the amino acid from S to L at position 278.
+The protein's natural variant, known as in HA-GPID;, features a modification of the amino acid from A to P at position 300.
+The protein's natural variant, known as in HA-GPID; severe form with neurological deficits; GPIHomburg;, features a modification of the amino acid from L to P at position 339.
+The protein's natural variant, known as in HA-GPID; GPINarita and Morcone;, features a modification of the amino acid from Q to R at position 343.
+The protein's natural variant, known as in HA-GPID; GPIMount Scopus;, features a modification of the amino acid from R to C at position 347.
+The protein's natural variant, known as in HA-GPID;, features a modification of the amino acid from R to H at position 347.
+The protein's natural variant, known as in HA-GPID; GPIKinki;, features a modification of the amino acid from T to R at position 375.
+The protein's natural variant, known as in HA-GPID; severe form; GPICalden;, features a modification of the amino acid from H to R at position 389.
+The protein's natural variant, known as in HA-GPID; Strongly reduced glucose-6-phosphate isomerase activity;, features a modification of the amino acid from R to C at position 472.
+The protein's natural variant, known as in HA-GPID;, features a modification of the amino acid from R to H at position 472.
+The protein's natural variant, known as in HA-GPID;, features a modification of the amino acid from L to F at position 487.
+The protein's natural variant, known as in HA-GPID;, features a modification of the amino acid from E to K at position 495.
+The protein's natural variant, known as in HA-GPID; severe form; GPICalden, features a modification of the amino acid from L to V at position 517.
+The protein's natural variant, known as in HA-GPID;, features a modification of the amino acid from I to T at position 525.
+The protein's natural variant, known as in HA-GPID; GPIFukuoka and Kinki;, features a modification of the amino acid from D to N at position 539.
+The protein's natural variant, known as in allele TY31A; no midbrain/hindbrain boundary, features a modification of the amino acid from G to V at position 79.
+The protein's natural variant, known as in a patient with late onset Alzheimer disease;, features a modification of the amino acid from E to D at position 665.
+The protein's natural variant, known as in AD1; Swedish mutation; highly increases hydrolysis by BACE1 and amyloid-beta proteins production;, features a modification of the amino acid from KM to NL at position 671.
+The protein's natural variant, known as in AD1;, features a modification of the amino acid from D to N at position 678.
+The protein's natural variant, known as in AD1; Flemish mutation; increases the solubility of processed amyloid-beta peptides and increases the stability of peptide oligomers;, features a modification of the amino acid from A to G at position 692.
+The protein's natural variant, known as in AD1;, features a modification of the amino acid from E to G at position 693.
+The protein's natural variant, known as in CAA-APP; Italian type;, features a modification of the amino acid from E to K at position 693.
+The protein's natural variant, known as in CAA-APP; Dutch type;, features a modification of the amino acid from E to Q at position 693.
+The protein's natural variant, known as in CAA-APP; Iowa type;, features a modification of the amino acid from D to N at position 694.
+The protein's natural variant, known as in CAA-APP; Italian type;, features a modification of the amino acid from L to V at position 705.
+The protein's natural variant, known as in AD1;, features a modification of the amino acid from A to T at position 713.
+The protein's natural variant, known as in one chronic schizophrenia patient; unknown pathological significance;, features a modification of the amino acid from A to V at position 713.
+The protein's natural variant, known as in AD1;, features a modification of the amino acid from T to A at position 714.
+The protein's natural variant, known as in AD1; increased amyloid-beta protein 42/40 ratio;, features a modification of the amino acid from T to I at position 714.
+The protein's natural variant, known as in AD1; decreased amyloid-beta protein 40/total amyloid-beta;, features a modification of the amino acid from V to M at position 715.
+The protein's natural variant, known as in AD1;, features a modification of the amino acid from I to V at position 716.
+The protein's natural variant, known as in AD1; increased amyloid-beta protein 42/40 ratio;, features a modification of the amino acid from V to F at position 717.
+The protein's natural variant, known as in AD1; increased amyloid-beta protein 42/40 ratio;, features a modification of the amino acid from V to G at position 717.
+The protein's natural variant, known as in AD1; increased amyloid-beta protein 42/40 ratio;, features a modification of the amino acid from V to I at position 717.
+The protein's natural variant, known as in AD1;, features a modification of the amino acid from V to L at position 717.
+The protein's natural variant, known as in AD1;, features a modification of the amino acid from L to P at position 723.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from T to M at position 129.
+The protein's natural variant, known as in DFNA4A;, features a modification of the amino acid from S to L at position 120.
+The protein's natural variant, known as in DFNA4A;, features a modification of the amino acid from G to C at position 376.
+The protein's natural variant, known as in DFNA4A;, features a modification of the amino acid from R to S at position 726.
+The protein's natural variant, known as in PNMHH;, features a modification of the amino acid from R to L at position 933.
+The protein's natural variant, known as in DFNA4A;, features a modification of the amino acid from L to F at position 976.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from G to R at position 40.
+The protein's natural variant, known as in oligomycin-resistant mutant, features a modification of the amino acid from F to S at position 127.
+The protein's natural variant, known as in oligomycin-resistant mutant, features a modification of the amino acid from F to Y at position 127.
+The protein's natural variant, known as in oligomycin-resistant mutant, features a modification of the amino acid from F to Y at position 136.
+The protein's natural variant, known as found in a patient with intellectual disability; unknown pathological significance, features a modification of the amino acid from E to K at position 349.
+The protein's natural variant, known as in strain: 45/20, features a modification of the amino acid from DNDGGYTGTTNYH to EDVDNDYT at position 212.
+The protein's natural variant, known as in strain: 45/20, features a modification of the amino acid from D to H at position 219.
+The protein's natural variant, known as in strain: Koala type I, features a modification of the amino acid from V to I at position 6.
+The protein's natural variant, known as in strain: Koala type I, features a modification of the amino acid from N to T at position 183.
+The protein's natural variant, known as in strain: Koala type I, features a modification of the amino acid from R to P at position 201.
+The protein's natural variant, known as in strain: Koala type I, features a modification of the amino acid from T to A at position 234.
+The protein's natural variant, known as in strain: Koala type I, features a modification of the amino acid from I to V at position 249.
+The protein's natural variant, known as in strain: Koala type I, features a modification of the amino acid from VP to TS at position 312.
+The protein's natural variant, known as in strain: Koala type I, features a modification of the amino acid from EL to DV at position 369.
+The protein's natural variant, known as in strain: Koala type I, features a modification of the amino acid from V to M at position 401.
+The protein's natural variant, known as in strain: Koala type I, features a modification of the amino acid from V to L at position 413.
+The protein's natural variant, known as in strain: Isolate Nellis, features a modification of the amino acid from Y to H at position 54.
+The protein's natural variant, known as in strain: Isolate Nellis, features a modification of the amino acid from L to F at position 121.
+The protein's natural variant, known as in ECTDS;, features a modification of the amino acid from Y to H at position 398.
+The protein's natural variant, known as in ECTDS; reduced expression; altered cell morphology; impaired tight junctions; adhesion defects; cytoplasmic translocation;, features a modification of the amino acid from I to K at position 482.
+The protein's natural variant, known as in PSORS15; results in decreased protein levels;, features a modification of the amino acid from F to C at position 4.
+The protein's natural variant, known as in PSORS15; results in decreased TLR3 targeting to the endosomes indicating impaired function;, features a modification of the amino acid from R to W at position 33.
+The natural variant of this protein is characterized by an amino acid alteration from Q to E at position 124.
+The natural variant of this protein is characterized by an amino acid alteration from A to S at position 247.
+The natural variant of this protein is characterized by an amino acid alteration from T to M at position 770.
+The natural variant of this protein is characterized by an amino acid alteration from L to V at position 915.
+The protein's natural variant, known as in HKTD; when coexpressed with KCNJ10 or KCNJ15 in Xenopus oocytes, it results in decreased channel expression at the surface and reduced potassium current amplitude compared to the wild-type, features a modification of the amino acid from T to I at position 64.
+The protein's natural variant, known as in HKTD; when coexpressed with KCNJ10 in Xenopus oocytes, it results in decreased channel expression at the surface and reduced potassium current amplitude compared to the wild-type, features a modification of the amino acid from I to R at position 132.
+The protein's natural variant, known as in HKTD, features a modification of the amino acid from G to A at position 135.
+The protein's natural variant, known as in HKTD; when coexpressed with KCNJ10 or KCNJ15 in Xenopus oocytes, it results in decreased channel expression at the surface and reduced potassium current amplitude compared to the wild-type, features a modification of the amino acid from R to C at position 137.
+The protein's natural variant, known as in HKTD; when coexpressed with KCNJ10 in Xenopus oocytes, it results in decreased channel expression at the surface and reduced potassium current amplitude compared to the wild-type, features a modification of the amino acid from P to L at position 250.
+The protein's natural variant, known as in Jk(null);, features a modification of the amino acid from N to K at position 74.
+The protein's natural variant, known as in Jk(null);, features a modification of the amino acid from M to V at position 167.
+The protein's natural variant, known as in Jk(b);, features a modification of the amino acid from D to N at position 280.
+The protein's natural variant, known as in Jk(null);, features a modification of the amino acid from S to P at position 291.
+The protein's natural variant, known as in Jk(null);, features a modification of the amino acid from G to E at position 299.
+The protein's natural variant, known as in Jk(null);, features a modification of the amino acid from T to M at position 319.
+The protein's natural variant, known as in allele ORM1*S;, features a modification of the amino acid from R to Q at position 38.
+The protein's natural variant, known as in allele ORM1*F2;, features a modification of the amino acid from V to M at position 174.
+The protein's natural variant, known as in XLP2; unknown pathological significance, features a modification of the amino acid from G to E at position 188.
+The protein's natural variant, known as in XLP2; unknown pathological significance, features a modification of the amino acid from I to N at position 194.
+The protein's natural variant, known as in XLP2; unknown pathological significance, features a modification of the amino acid from P to R at position 482.
+The protein's natural variant, known as in GPHYSD3; unknown pathological significance; no effect on TGF-beta secretion;, features a modification of the amino acid from S to C at position 696.
+The protein's natural variant, known as in strain: SHSN-2, features a modification of the amino acid from E to K at position 163.
+The protein's natural variant, known as in strain: Danny/horse/Oregon, features a modification of the amino acid from I to T at position 205.
+The protein's natural variant, known as in strain: Thorenberg/horse/Oregon, features a modification of the amino acid from E to G at position 209.
+The protein's natural variant, known as in strain: Stagnicola/snail/Oregon, features a modification of the amino acid from P to S at position 235.
+The protein's natural variant, known as in strain: Drpepper/horse/California, features a modification of the amino acid from K to N at position 277.
+The protein's natural variant, known as in strain: Stagnicola/snail/Oregon, features a modification of the amino acid from K to R at position 299.
+The protein's natural variant, known as in a patient with Graves disease;, features a modification of the amino acid from D to H at position 36.
+The protein's natural variant, known as in CHNG1, features a modification of the amino acid from C to S at position 41.
+The protein's natural variant, known as does not contribute to the genetic susceptibility to Graves disease;, features a modification of the amino acid from P to T at position 52.
+The protein's natural variant, known as in CHNG1, features a modification of the amino acid from R to Q at position 109.
+The protein's natural variant, known as in CHNG1;, features a modification of the amino acid from P to A at position 162.
+The protein's natural variant, known as in CHNG1, features a modification of the amino acid from I to N at position 167.
+The protein's natural variant, known as in HTFG; enhances receptor response to chorionic gonadotropin, features a modification of the amino acid from K to R at position 183.
+The protein's natural variant, known as in papillary cancer, features a modification of the amino acid from F to I at position 197.
+The protein's natural variant, known as in papillary cancer, features a modification of the amino acid from D to E at position 219.
+The protein's natural variant, known as in CHNG1; displays a low expression at the cell surface and a reduced response to bovine TSH in terms of cAMP production, features a modification of the amino acid from L to P at position 252.
+The protein's natural variant, known as in hyperthyroidism; congenital; due to a toxic adenoma, features a modification of the amino acid from S to I at position 281.
+The protein's natural variant, known as in HTNA; gain of function; found in toxic thyroid nodules and hyperfunctioning thyroid adenomas, features a modification of the amino acid from S to N at position 281.
+The protein's natural variant, known as in hyperthyroidism; associated with hyperfunctioning thyroid adenomas, features a modification of the amino acid from S to T at position 281.
+The protein's natural variant, known as in CHNG1, features a modification of the amino acid from R to C at position 310.
+The protein's natural variant, known as in CHNG1; persistent hypothyroidism and defective thyroid development; abolishes high affinity hormone binding, features a modification of the amino acid from C to W at position 390.
+The protein's natural variant, known as in CHNG1; lack of adenylate cyclase activation, features a modification of the amino acid from D to N at position 410.
+The protein's natural variant, known as found in toxic thyroid nodules; 8 to 9 times higher levels of basal cAMP than wild-type TSHR and similar response to maximal TSH stimulation, features a modification of the amino acid from S to I at position 425.
+The protein's natural variant, known as in HTNA; gain of function; constitutive activation of the G(s)/adenylyl cyclase system, features a modification of the amino acid from G to S at position 431.
+The protein's natural variant, known as in CHNG1; abolishes cell membrane location; abolishes adenylate cyclase-activating G-protein coupled receptor signaling pathway; abolishes phospholipase C-activating G-protein coupled receptor signaling pathway, features a modification of the amino acid from N to D at position 432.
+The protein's natural variant, known as in CHNG1; no effect on cell membrane location; upon TSH stimulation decreases more phospholipase C-activating G-protein coupled receptor signaling pathway than adenylate cyclase-activating G-protein coupled receptor signaling pathway, features a modification of the amino acid from P to L at position 449.
+The protein's natural variant, known as in CHNG1, features a modification of the amino acid from R to H at position 450.
+The protein's natural variant, known as in HTNA; sporadic; found in toxic thyroid nodules and hyperfunctioning thyroid adenomas, features a modification of the amino acid from M to T at position 453.
+The protein's natural variant, known as in HTNA; gain of function, features a modification of the amino acid from M to V at position 463.
+The protein's natural variant, known as in CHNG1, features a modification of the amino acid from L to P at position 467.
+The protein's natural variant, known as in CHNG1; severe hypothyroidism, features a modification of the amino acid from T to I at position 477.
+The protein's natural variant, known as in HTNA; found in thyroid toxic nodules and hyperfunctioning thyroid adenomas; also in hyperfunctioning follicular carcinoma, features a modification of the amino acid from I to F at position 486.
+The protein's natural variant, known as in HTNA; found in hyperfunctioning thyroid adenomas, features a modification of the amino acid from I to M at position 486.
+The protein's natural variant, known as in CHNG1, features a modification of the amino acid from G to S at position 498.
+The protein's natural variant, known as in HTNA; found in toxic thyroid nodules, features a modification of the amino acid from S to N at position 505.
+The protein's natural variant, known as in HTNA; gain of function, features a modification of the amino acid from S to R at position 505.
+The protein's natural variant, known as in HTNA; gain of function, features a modification of the amino acid from V to A at position 509.
+The protein's natural variant, known as found in toxic thyroid nodules; 5 times higher levels of basal cAMP than wild-type TSHR and slightly less response to maximal TSH stimulation, features a modification of the amino acid from L to Q at position 512.
+The protein's natural variant, known as in hyperthyroidism; associated with autonomously functioning thyroid nodules; 3.3-fold increase in basal cAMP level, features a modification of the amino acid from L to R at position 512.
+The protein's natural variant, known as in CHNG1; impairs adenylate cyclase activation, features a modification of the amino acid from F to L at position 525.
+The natural variant of this protein is characterized by an amino acid alteration from R to H at position 528.
+The protein's natural variant, known as in CHNG1; severe hypothyroidism, features a modification of the amino acid from A to T at position 553.
+The protein's natural variant, known as in HTNA; found in thyroid toxic nodules and hyperfunctioning thyroid adenomas, features a modification of the amino acid from I to T at position 568.
+The protein's natural variant, known as in toxic thyroid adenoma; requires 2 nucleotide substitutions; somatic mutation; constitutively activates the cAMP cascade, features a modification of the amino acid from A to N at position 593.
+The protein's natural variant, known as in HTNA; 11-fold increase in specific constitutive activity associated with reduction in receptor protein expression, features a modification of the amino acid from V to F at position 597.
+The protein's natural variant, known as in hyperthyroidism; congenital with severe thyrotoxicosis, features a modification of the amino acid from V to L at position 597.
+The protein's natural variant, known as in CHNG1, features a modification of the amino acid from C to R at position 600.
+The natural variant of this protein is characterized by an amino acid alteration from I to M at position 606.
+The protein's natural variant, known as in hyperthyroidism; found in toxic thyroid nodules; associated with hyperfunctioning thyroid adenomas, features a modification of the amino acid from D to G at position 619.
+The protein's natural variant, known as in hyperthyroidism; associated with hyperfunctioning thyroid adenomas; gain of function; requires 2 nucleotide substitutions, features a modification of the amino acid from A to I at position 623.
+The protein's natural variant, known as in hyperthyroidism; found in toxic thyroid nodules; associated with hyperfunctioning thyroid adenomas; gain of function, features a modification of the amino acid from A to V at position 623.
+The protein's natural variant, known as in HTNA; also in hyperfunctioning thyroid adenomas and non-adenomatous nodules, features a modification of the amino acid from L to F at position 629.
+The protein's natural variant, known as in hyperthyroidism; associated with hyperfunctioning thyroid adenomas, features a modification of the amino acid from I to L at position 630.
+The protein's natural variant, known as in hyperthyroidism; associated with hyperfunctioning thyroid adenomas, features a modification of the amino acid from F to C at position 631.
+The protein's natural variant, known as in HTNA; gain of function; found in toxic thyroid nodules and hyperfunctioning thyroid adenomas, features a modification of the amino acid from F to L at position 631.
+The protein's natural variant, known as in HTNA; found in toxic thyroid nodules and hyperfunctioning non-adenomatous nodules, features a modification of the amino acid from T to A at position 632.
+The protein's natural variant, known as in HTNA; gain of function; found in thyroid toxic nodules and hyperfunctioning thyroid adenomas, features a modification of the amino acid from T to I at position 632.
+The protein's natural variant, known as in hyperthyroidism; associated with hyperfunctioning thyroid adenomas, features a modification of the amino acid from D to A at position 633.
+The protein's natural variant, known as in HTNA; found in thyroid toxic nodules and hyperfunctioning thyroid adenomas, features a modification of the amino acid from D to E at position 633.
+The protein's natural variant, known as in hyperthyroidism; found in toxic thyroid nodules; associated with hyperfunctioning thyroid adenomas; also in hyperfunctioning insular carcinoma; with severe thyrotoxicosis; gain of function;, features a modification of the amino acid from D to H at position 633.
+The protein's natural variant, known as in hyperthyroidism; found in toxic thyroid nodules; associated with hyperfunctioning thyroid adenomas, features a modification of the amino acid from D to Y at position 633.
+The protein's natural variant, known as found in toxic thyroid nodules, features a modification of the amino acid from P to A at position 639.
+The protein's natural variant, known as in HTNA; gain of function, features a modification of the amino acid from P to S at position 639.
+The protein's natural variant, known as in HTNA; found in non-adenomatous hyperfunctioning nodules, features a modification of the amino acid from A to V at position 647.
+The protein's natural variant, known as in HTNA; gain of function, features a modification of the amino acid from N to Y at position 650.
+The protein's natural variant, known as found in toxic thyroid nodules, features a modification of the amino acid from V to F at position 656.
+The protein's natural variant, known as in HTNA; gain of function, features a modification of the amino acid from N to S at position 670.
+The protein's natural variant, known as in HTNA; gain of function, features a modification of the amino acid from C to Y at position 672.
+The protein's natural variant, known as in thyroid carcinoma; with thyrotoxicosis; gain of function, features a modification of the amino acid from L to V at position 677.
+The natural variant of this protein is characterized by an amino acid alteration from A to G at position 703.
+The protein's natural variant, known as in papillary cancer, features a modification of the amino acid from N to D at position 715.
+The natural variant of this protein is characterized by an amino acid alteration from Q to E at position 720.
+The protein's natural variant, known as in papillary cancer, features a modification of the amino acid from K to M at position 723.
+The protein's natural variant, known as may be a predisposing factor in toxic multinodular goiter pathogenesis; activation of the cAMP cascade does not differ from the wild-type;, features a modification of the amino acid from D to E at position 727.
+The protein's natural variant, known as in strain: NOD/MrkTac, features a modification of the amino acid from V to A at position 175.
+The protein's natural variant, known as in strain: NOD/MrkTac, features a modification of the amino acid from E to K at position 296.
+The protein's natural variant, known as in strain: NOD/MrkTac, features a modification of the amino acid from V to A at position 318.
+The protein's natural variant, known as in strain: NOD/MrkTac, features a modification of the amino acid from V to I at position 392.
+The protein's natural variant, known as in strain: NOD/MrkTac, features a modification of the amino acid from D to N at position 451.
+The protein's natural variant, known as in strain: NOD/MrkTac, features a modification of the amino acid from H to D at position 557.
+The protein's natural variant, known as in strain: NOD/MrkTac, features a modification of the amino acid from N to D at position 565.
+The protein's natural variant, known as in strain: NOD/MrkTac, features a modification of the amino acid from R to H at position 620.
+The protein's natural variant, known as in strain: NOD/MrkTac, features a modification of the amino acid from I to M at position 648.
+The protein's natural variant, known as in strain: NOD/MrkTac, features a modification of the amino acid from A to T at position 860.
+The natural variant of this protein is characterized by an amino acid alteration from F to L at position 17.
+The protein's natural variant, known as in strain: cv. Lisse-2, features a modification of the amino acid from D to E at position 138.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation, features a modification of the amino acid from H to Y at position 495.
+The natural variant of this protein is characterized by an amino acid alteration from T to M at position 311.
+The natural variant of this protein is characterized by an amino acid alteration from N to K at position 413.
+The natural variant of this protein is characterized by an amino acid alteration from G to E at position 147.
+The natural variant of this protein is characterized by an amino acid alteration from R to G at position 197.
+The natural variant of this protein is characterized by an amino acid alteration from A to G at position 495.
+The protein's natural variant, known as in NEDBA; unknown pathological significance;, features a modification of the amino acid from G to R at position 400.
+The protein's natural variant, known as in NEDBA;, features a modification of the amino acid from L to P at position 444.
+The protein's natural variant, known as in NEDBA; unknown pathological significance;, features a modification of the amino acid from R to Q at position 525.
+The protein's natural variant, known as in NEDBA; affects axon development when expressed in a heterologous system;, features a modification of the amino acid from R to C at position 578.
+The protein's natural variant, known as in NEDBA; unknown pathological significance;, features a modification of the amino acid from H to Q at position 994.
+The protein's natural variant, known as in NEDBA; affects axon development when expressed in a heterologous system;, features a modification of the amino acid from R to C at position 1146.
+The protein's natural variant, known as found in a patient with autism and Parkinson's disease; unknown pathological significance;, features a modification of the amino acid from R to W at position 208.
+The protein's natural variant, known as in strain: GP204; streptomycin-resistant, features a modification of the amino acid from K to T at position 56.
+The protein's natural variant, known as in EVPLS;, features a modification of the amino acid from R to W at position 126.
+The protein's natural variant, known as in EVPLS;, features a modification of the amino acid from Y to C at position 128.
+The natural variant of this protein is characterized by an amino acid alteration from H to Y at position 184.
+The protein's natural variant, known as in SIDBA4; unknown pathological significance;, features a modification of the amino acid from S to P at position 212.
+The protein's natural variant, known as in SIDBA4; unknown pathological significance, features a modification of the amino acid from G to S at position 388.
+The protein's natural variant, known as in SIDBA4; unknown pathological significance, features a modification of the amino acid from E to K at position 415.
+The natural variant of this protein is characterized by an amino acid alteration from T to K at position 539.
+The protein's natural variant, known as in NEDHISB, features a modification of the amino acid from G to C at position 40.
+The protein's natural variant, known as in NEDHISB, features a modification of the amino acid from G to R at position 40.
+The protein's natural variant, known as in NEDHISB, features a modification of the amino acid from G to D at position 45.
+The protein's natural variant, known as in NEDHISB, features a modification of the amino acid from T to I at position 48.
+The protein's natural variant, known as in NEDHISB, features a modification of the amino acid from T to K at position 48.
+The protein's natural variant, known as in NEDHISB; loss of GTP binding, features a modification of the amino acid from Q to P at position 52.
+The protein's natural variant, known as in NEDHISB, features a modification of the amino acid from D to V at position 173.
+The protein's natural variant, known as in NEDHISB, features a modification of the amino acid from C to Y at position 224.
+The protein's natural variant, known as in NEDHISB, features a modification of the amino acid from K to N at position 270.
+The protein's natural variant, known as in NEDHISB, features a modification of the amino acid from K to R at position 270.
+The protein's natural variant, known as in NEDHISB, features a modification of the amino acid from D to G at position 272.
+The protein's natural variant, known as in NEDHISB, features a modification of the amino acid from A to P at position 326.
+The protein's natural variant, known as in NEDHISB; unknown pathological significance, features a modification of the amino acid from V to E at position 332.
+The protein's natural variant, known as in strain: 951, features a modification of the amino acid from H to Y at position 62.
+The protein's natural variant, known as in strain: VBI-M0894, features a modification of the amino acid from D to T at position 14.
+The protein's natural variant, known as in strain: VBI-M0894, features a modification of the amino acid from C to F at position 21.
+The protein's natural variant, known as in strain: VBI-M0894, features a modification of the amino acid from S to G at position 92.
+The protein's natural variant, known as in strain: VBI-M0894, features a modification of the amino acid from T to I at position 124.
+The protein's natural variant, known as in strain: VBI-M0894, features a modification of the amino acid from I to V at position 150.
+The protein's natural variant, known as in strain: VBI-M0894, features a modification of the amino acid from A to S at position 157.
+The protein's natural variant, known as in strain: VBI-M0894, features a modification of the amino acid from I to F at position 177.
+The protein's natural variant, known as in strain: VBI-M0894, features a modification of the amino acid from F to Y at position 217.
+The protein's natural variant, known as in HIBCHD;, features a modification of the amino acid from Y to C at position 122.
+The protein's natural variant, known as in NSDVS2; dominant-negative, increased BET proteins stability, features a modification of the amino acid from T to A at position 25.
+The protein's natural variant, known as in NSDVS2; dominant-negative, increased BET proteins stability, features a modification of the amino acid from Y to C at position 83.
+The protein's natural variant, known as in NSDVS1; gain-of-function, reduced BET proteins stability, features a modification of the amino acid from R to Q at position 121.
+The protein's natural variant, known as in NSDVS2; dominant-negative, increased BET proteins stability, features a modification of the amino acid from G to V at position 132.
+The protein's natural variant, known as in NSDVS2; dominant-negative, increased BET proteins stability, features a modification of the amino acid from R to C at position 138.
+The protein's natural variant, known as in NSDVS1; gain-of-function, reduced BET proteins stability, features a modification of the amino acid from D to N at position 144.
+The protein's natural variant, known as in strain: PI 247087, allele pot-1, features a modification of the amino acid from L to F at position 48.
+The protein's natural variant, known as in strain: PI 247087, allele pot-1, features a modification of the amino acid from N to K at position 68.
+The protein's natural variant, known as in strain: PI 247087, allele pot-1, features a modification of the amino acid from A to D at position 77.
+The protein's natural variant, known as in strain: PI 247087, allele pot-1, features a modification of the amino acid from M to I at position 109.
+The protein's natural variant, known as in HTX12; unknown pathological significance;, features a modification of the amino acid from S to F at position 31.
+The protein's natural variant, known as in HTX12; unknown pathological significance, features a modification of the amino acid from C to S at position 324.
+The protein's natural variant, known as in HTX12; unknown pathological significance;, features a modification of the amino acid from S to L at position 384.
+The protein's natural variant, known as in HTX12; unknown pathological significance, features a modification of the amino acid from R to I at position 389.
+The protein's natural variant, known as in HTX12; unknown pathological significance, features a modification of the amino acid from L to P at position 469.
+The protein's natural variant, known as in MFM11; mislocated away from the A-band to the Z-disk, features a modification of the amino acid from S to P at position 403.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from D to H at position 496.
+The protein's natural variant, known as in MFM11; unknown pathological significance; mislocated away from the A-band to the Z-disk;, features a modification of the amino acid from C to R at position 514.
+The protein's natural variant, known as in MFM11; mislocated away from the A-band to the Z-disk, features a modification of the amino acid from R to Q at position 754.
+The protein's natural variant, known as in CTRCT43;, features a modification of the amino acid from R to W at position 805.
+The protein's natural variant, known as in a breast infiltrating ductal carcinoma sample; somatic mutation, features a modification of the amino acid from S to C at position 424.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from I to L at position 880.
+The protein's natural variant, known as in SSS3; rare variant predisposing to sick sinus syndrome;, features a modification of the amino acid from R to W at position 721.
+The protein's natural variant, known as in CMH14; late onset;, features a modification of the amino acid from R to Q at position 795.
+The protein's natural variant, known as in ASD3;, features a modification of the amino acid from I to N at position 820.
+The protein's natural variant, known as in CMD1EE;, features a modification of the amino acid from P to L at position 830.
+The protein's natural variant, known as in CMD1EE;, features a modification of the amino acid from A to S at position 1004.
+The protein's natural variant, known as in CMH14;, features a modification of the amino acid from Q to H at position 1065.
+The protein's natural variant, known as in CMD1EE;, features a modification of the amino acid from E to K at position 1457.
+The protein's natural variant, known as in CMD1EE; unknown pathological significance;, features a modification of the amino acid from R to Q at position 1502.
+The protein's natural variant, known as in HISTID;, features a modification of the amino acid from R to T at position 206.
+The protein's natural variant, known as in HISTID;, features a modification of the amino acid from R to L at position 208.
+The protein's natural variant, known as in HISTID;, features a modification of the amino acid from P to L at position 259.
+The protein's natural variant, known as in HISTID;, features a modification of the amino acid from R to P at position 322.
+The natural variant of this protein is characterized by an amino acid alteration from N to S at position 29.
+The natural variant of this protein is characterized by an amino acid alteration from K to R at position 35.
+The protein's natural variant, known as in strain: 129/SvJ, features a modification of the amino acid from T to S at position 12.
+The protein's natural variant, known as in allele CSN3-B, features a modification of the amino acid from Q to R at position 65.
+The protein's natural variant, known as in allele CSN3-B, allele C and allele G, features a modification of the amino acid from V to I at position 86.
+The protein's natural variant, known as in allele E, features a modification of the amino acid from D to G at position 111.
+The protein's natural variant, known as in allele CSN3-B, allele B, allele C, allele E, allele F and allele G, features a modification of the amino acid from V to I at position 140.
+The protein's natural variant, known as in allele C, features a modification of the amino acid from A to V at position 177.
+The protein's natural variant, known as in allele CSN3-B, allele C, allele F and allele G, features a modification of the amino acid from S to P at position 180.
+The protein's natural variant, known as no effect on succinate-semialdehyde dehydrogenase activity;, features a modification of the amino acid from G to R at position 36.
+The protein's natural variant, known as in SSADHD; 3% of activity;, features a modification of the amino acid from C to F at position 93.
+The protein's natural variant, known as in SSADHD; <1% of activity;, features a modification of the amino acid from G to R at position 176.
+The protein's natural variant, known as 83% of activity;, features a modification of the amino acid from H to Y at position 180.
+The protein's natural variant, known as 48% of activity;, features a modification of the amino acid from P to L at position 182.
+The protein's natural variant, known as in SSADHD; 5% of activity;, features a modification of the amino acid from C to Y at position 223.
+The protein's natural variant, known as in SSADHD; 4% of activity;, features a modification of the amino acid from T to M at position 233.
+The protein's natural variant, known as 65% of activity;, features a modification of the amino acid from A to S at position 237.
+The protein's natural variant, known as in SSADHD; 17% of activity;, features a modification of the amino acid from N to S at position 255.
+The protein's natural variant, known as in SSADHD; <1% of activity;, features a modification of the amino acid from G to E at position 268.
+The protein's natural variant, known as in SSADHD; 1% of activity;, features a modification of the amino acid from N to K at position 335.
+The natural variant of this protein is characterized by an amino acid alteration from N to S at position 372.
+The protein's natural variant, known as in SSADHD; 2% of activity, features a modification of the amino acid from P to L at position 382.
+The protein's natural variant, known as in SSADHD, features a modification of the amino acid from P to Q at position 382.
+The protein's natural variant, known as in SSADHD; <1% of activity;, features a modification of the amino acid from G to D at position 409.
+The protein's natural variant, known as in SSADHD, features a modification of the amino acid from V to E at position 487.
+The protein's natural variant, known as in SSADHD; <1% of activity;, features a modification of the amino acid from G to R at position 533.
+The protein's natural variant, known as in strain: Xinghua, features a modification of the amino acid from V to A at position 17.
+The protein's natural variant, known as in strain: Xinghua, features a modification of the amino acid from G to R at position 20.
+The protein's natural variant, known as in PEOA6; the mutant protein has a complete loss of nuclease activity and severely impaired helicase activity; consistent with a loss of function mutation;, features a modification of the amino acid from R to H at position 198.
+The protein's natural variant, known as in PEOA6; the mutant protein has significantly reduced nuclease and helicase activity; consistent with a loss of function mutation;, features a modification of the amino acid from K to E at position 227.
+The protein's natural variant, known as in PEOA6; the mutant protein has decreased nuclease activity (30% of wild-type) and enhanced helicase activity; consistent with a loss of function mutation;, features a modification of the amino acid from V to I at position 637.
+The protein's natural variant, known as in Christchurch-2, Seattle-1 and Ijmuiden;, features a modification of the amino acid from R to C at position 44.
+The protein's natural variant, known as in Ise, features a modification of the amino acid from G to R at position 45.
+The protein's natural variant, known as in Nijmegen;, features a modification of the amino acid from R to C at position 74.
+The protein's natural variant, known as in CAFBN; hypofibrinogenemia; heterozygous; decreased fibrinogen complex assembly; no effect on fibrinogen complex secretion, features a modification of the amino acid from C to R at position 95.
+The protein's natural variant, known as in DYSFIBRIN; fibrinogen Naples and Milano-2; associated with defective thrombin binding and thrombophilia;, features a modification of the amino acid from A to T at position 98.
+The protein's natural variant, known as in CAFBN; fibrinogen Longmont;, features a modification of the amino acid from R to C at position 196.
+The protein's natural variant, known as in CAFBN;, features a modification of the amino acid from L to Q at position 202.
+The protein's natural variant, known as in Pontoise-2;, features a modification of the amino acid from A to T at position 365.
+The protein's natural variant, known as in CAFBN; abolishes fibrinogen secretion;, features a modification of the amino acid from L to R at position 383.
+The protein's natural variant, known as in CAFBN; homozygous; heterozygous; no effect on fibrinogen complex assembly; impaired fibrinogen complex secretion, features a modification of the amino acid from T to K at position 407.
+The protein's natural variant, known as in CAFBN; abolishes fibrinogen secretion;, features a modification of the amino acid from G to D at position 430.
+The protein's natural variant, known as in Baltimore-2;, features a modification of the amino acid from R to K at position 478.
+The protein's natural variant, known as in CAB45A, features a modification of the amino acid from R to K at position 281.
+The natural variant of this protein is characterized by an amino acid alteration from N to S at position 23.
+The natural variant of this protein is characterized by an amino acid alteration from T to A at position 28.
+The natural variant of this protein is characterized by an amino acid alteration from S to L at position 61.
+The natural variant of this protein is characterized by an amino acid alteration from K to R at position 70.
+The natural variant of this protein is characterized by an amino acid alteration from Y to H at position 120.
+The natural variant of this protein is characterized by an amino acid alteration from R to Q at position 125.
+The natural variant of this protein is characterized by an amino acid alteration from E to G at position 127.
+The natural variant of this protein is characterized by an amino acid alteration from R to H at position 129.
+The natural variant of this protein is characterized by an amino acid alteration from M to V at position 132.
+The natural variant of this protein is characterized by an amino acid alteration from S to N at position 145.
+The natural variant of this protein is characterized by an amino acid alteration from L to V at position 153.
+The natural variant of this protein is characterized by an amino acid alteration from N to D at position 203.
+The natural variant of this protein is characterized by an amino acid alteration from G to R at position 261.
+The natural variant of this protein is characterized by an amino acid alteration from F to L at position 302.
+The natural variant of this protein is characterized by an amino acid alteration from F to L at position 316.
+The natural variant of this protein is characterized by an amino acid alteration from G to R at position 337.
+The natural variant of this protein is characterized by an amino acid alteration from S to N at position 367.
+The natural variant of this protein is characterized by an amino acid alteration from Q to L at position 422.
+The natural variant of this protein is characterized by an amino acid alteration from I to F at position 429.
+The natural variant of this protein is characterized by an amino acid alteration from D to E at position 433.
+The protein's natural variant, known as in strain: Swiss Webster, features a modification of the amino acid from V to F at position 146.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from I to V at position 27.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from I to V at position 63.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from I to V at position 66.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from K to R at position 241.
+The protein's natural variant, known as resistant to nodulisporic acid, features a modification of the amino acid from P to S at position 299.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from S to N at position 345.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from Y to C at position 18.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from Y to H at position 18.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from D to N at position 32.
+The protein's natural variant, known as does not affect subcellular location; increases G-protein coupled receptor activity;, features a modification of the amino acid from E to K at position 78.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from T to M at position 82.
+The protein's natural variant, known as does not affect subcellular location; decreases G-protein coupled receptor activity;, features a modification of the amino acid from Y to C at position 85.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from Y to D at position 89.
+The protein's natural variant, known as reduces cell membrane location; decreases G-protein coupled receptor activity;, features a modification of the amino acid from F to L at position 110.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from S to F at position 138.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from G to S at position 140.
+The protein's natural variant, known as does not affect subcellular location; increases G-protein coupled receptor activity;, features a modification of the amino acid from G to D at position 141.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from V to L at position 145.
+The protein's natural variant, known as does not affect subcellular location; decreases G-protein coupled receptor activity;, features a modification of the amino acid from R to W at position 150.
+The protein's natural variant, known as reduces cell membrane location; decreases G-protein coupled receptor activity;, features a modification of the amino acid from W to S at position 174.
+The protein's natural variant, known as reduces cell membrane location; decreases G-protein coupled receptor activity;, features a modification of the amino acid from E to K at position 178.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from V to I at position 184.
+The protein's natural variant, known as reduces cell membrane location; decreases G-protein coupled receptor activity;, features a modification of the amino acid from G to R at position 195.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from R to C at position 199.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from R to H at position 199.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from E to D at position 203.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from V to M at position 209.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from D to N at position 226.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from R to W at position 233.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from A to T at position 241.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from M to T at position 242.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from T to I at position 245.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from T to A at position 257.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from P to Q at position 259.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from S to Y at position 265.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from S to N at position 268.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from V to A at position 270.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from V to M at position 270.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from P to A at position 293.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from G to R at position 294.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from P to S at position 308.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from L to F at position 318.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from S to N at position 349.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from N to S at position 364.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from T to M at position 369.
+The protein's natural variant, known as does not affect subcellular location; increases G-protein coupled receptor activity;, features a modification of the amino acid from F to S at position 383.
+The protein's natural variant, known as does not affect subcellular location; increases G-protein coupled receptor activity;, features a modification of the amino acid from V to M at position 393.
+The protein's natural variant, known as does not affect subcellular location;, features a modification of the amino acid from H to Q at position 397.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from R to C at position 399.
+The protein's natural variant, known as does not affect subcellular location; increases G-protein coupled receptor activity;, features a modification of the amino acid from G to A at position 404.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from Q to P at position 405.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from I to V at position 410.
+The protein's natural variant, known as does not affect subcellular location; increases G-protein coupled receptor activity;, features a modification of the amino acid from P to S at position 411.
+The protein's natural variant, known as does not affect subcellular location; increases G-protein coupled receptor activity;, features a modification of the amino acid from E to K at position 413.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from A to V at position 419.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from G to S at position 425.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from A to T at position 441.
+The protein's natural variant, known as reduces cell membrane location; decreases G-protein coupled receptor activity;, features a modification of the amino acid from A to D at position 448.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from H to R at position 450.
+The protein's natural variant, known as does not affect subcellular location; increases G-protein coupled receptor activity;, features a modification of the amino acid from D to N at position 453.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from C to Y at position 454.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from A to T at position 458.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from S to A at position 464.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from N to S at position 476.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from S to L at position 478.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from T to M at position 484.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from V to I at position 485.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from E to G at position 498.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from A to S at position 499.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from V to M at position 508.
+The protein's natural variant, known as does not change G-protein coupled receptor activity;, features a modification of the amino acid from S to L at position 523.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from N to K at position 524.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from V to A at position 538.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from V to I at position 538.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from R to C at position 540.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from R to H at position 540.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from R to C at position 560.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from R to H at position 560.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from S to L at position 567.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from I to V at position 569.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from A to T at position 589.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from V to M at position 594.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from R to H at position 601.
+The protein's natural variant, known as does not affect subcellular location; decreases G-protein coupled receptor activity;, features a modification of the amino acid from L to M at position 608.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from R to C at position 624.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from E to K at position 626.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from T to I at position 630.
+The protein's natural variant, known as does not affect subcellular location; decreases G-protein coupled receptor activity;, features a modification of the amino acid from S to L at position 667.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from R to H at position 673.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from M to T at position 695.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from G to R at position 699.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from A to V at position 720.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from A to T at position 743.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from H to R at position 749.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from D to E at position 751.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from A to E at position 761.
+The protein's natural variant, known as reduces cell membrane location; decreases G-protein coupled receptor activity;, features a modification of the amino acid from V to M at position 764.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from V to M at position 777.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from A to V at position 779.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from T to M at position 793.
+The protein's natural variant, known as decreases cell surface location; abolishes G-protein coupled receptor activity;, features a modification of the amino acid from N to K at position 795.
+The protein's natural variant, known as reduces cell membrane location; decreases G-protein coupled receptor activity;, features a modification of the amino acid from A to T at position 816.
+The protein's natural variant, known as does not affect subcellular location; increases G-protein coupled receptor activity;, features a modification of the amino acid from T to M at position 827.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from A to T at position 831.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from A to T at position 836.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from A to V at position 836.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from M to T at position 851.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from R to H at position 868.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from V to I at position 869.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from D to N at position 870.
+The protein's natural variant, known as does not affect subcellular location; does not change G-protein coupled receptor activity;, features a modification of the amino acid from V to M at position 874.
+The protein's natural variant, known as found in patients with squamous cell carcinomas; oncogenic, features a modification of the amino acid from Q to E at position 311.
+The protein's natural variant, known as no effect on nuclear localization; complements loss of endogenous DONSON by rescuing the spontaneous fork stalling observed after DONSON depletion;, features a modification of the amino acid from S to R at position 28.
+The protein's natural variant, known as in MISSLA, features a modification of the amino acid from C to R at position 278.
+The protein's natural variant, known as in MISSLA; loss of nuclear localization, features a modification of the amino acid from Y to C at position 282.
+The protein's natural variant, known as in MISSLA; loss of nuclear localization;, features a modification of the amino acid from F to L at position 292.
+The protein's natural variant, known as in MISSLA, features a modification of the amino acid from P to S at position 433.
+The protein's natural variant, known as in MISSLA; reduced protein level; reduced nuclear localization;, features a modification of the amino acid from M to T at position 446.
+The protein's natural variant, known as in MISSLA; unknown pathological significance; reduced protein level; no effect on nuclear localization; does not complement loss of endogenous DONSON when tested for the rescue of the spontaneous fork stalling observed after DONSON depletion;, features a modification of the amino acid from K to T at position 489.
+The protein's natural variant, known as in MISSLA;, features a modification of the amino acid from E to K at position 504.
+The protein's natural variant, known as in MISSLA; reduced nuclear localization, features a modification of the amino acid from Q to QK at position 543.
+The protein's natural variant, known as in strain: NEM895, features a modification of the amino acid from S to L at position 115.
+The protein's natural variant, known as in strain: NEM895, features a modification of the amino acid from L to I at position 135.
+The protein's natural variant, known as rare variant; found in a patient with hypertrophic cardiomyopathy; unknown pathological significance, features a modification of the amino acid from C to Y at position 50.
+The protein's natural variant, known as rare variant; found in a patient with hypertrophic cardiomyopathy; unknown pathological significance;, features a modification of the amino acid from P to A at position 79.
+The protein's natural variant, known as rare variant; found in a patient with hypertrophic cardiomyopathy; unknown pathological significance, features a modification of the amino acid from L to M at position 241.
+The natural variant of this protein is characterized by an amino acid alteration from S to F at position 252.
+The protein's natural variant, known as rare variant; found in a patient with hypertrophic cardiomyopathy; unknown pathological significance;, features a modification of the amino acid from P to T at position 392.
+The natural variant of this protein is characterized by an amino acid alteration from T to I at position 418.
+The protein's natural variant, known as rare variant; found in a patient with hypertrophic cardiomyopathy; unknown pathological significance;, features a modification of the amino acid from K to N at position 452.
+The natural variant of this protein is characterized by an amino acid alteration from P to L at position 458.
+The protein's natural variant, known as rare variant; found in a patient with hypertrophic cardiomyopathy; unknown pathological significance;, features a modification of the amino acid from T to S at position 506.
+The protein's natural variant, known as in brain, features a modification of the amino acid from D to DD at position 8.
+The protein's natural variant, known as in strain: 169-98 / Serotype O22, features a modification of the amino acid from FGFID to LGPIE at position 70.
+The protein's natural variant, known as in strain: MO45 / ATCC 51394 / Serotype O139, features a modification of the amino acid from F to S at position 68.
+The protein's natural variant, known as in strain: 169-98 / Serotype O22, features a modification of the amino acid from D to G at position 161.
+The protein's natural variant, known as in strain: 169-98 / Serotype O22, features a modification of the amino acid from N to H at position 211.
+The protein's natural variant, known as in strain: 169-98 / Serotype O22, features a modification of the amino acid from G to S at position 233.
+The protein's natural variant, known as in strain: 169-98 / Serotype O22, features a modification of the amino acid from D to E at position 271.
+The protein's natural variant, known as in strain: 169-98 / Serotype O22, features a modification of the amino acid from S to T at position 299.
+The natural variant of this protein is characterized by an amino acid alteration from I to L at position 227.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from Q to R at position 607.
+The protein's natural variant, known as in strain: Persimi50, features a modification of the amino acid from V to L at position 82.
+The protein's natural variant, known as in strain: Persimi44, features a modification of the amino acid from R to K at position 185.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from V to L at position 389.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from M to I at position 438.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 95.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from S to L at position 712.
+The protein's natural variant, known as in PRAAS5; unknown pathological significance; impaired autocleavage and maturation, features a modification of the amino acid from F to S at position 14.
+The natural variant of this protein is characterized by an amino acid alteration from P to L at position 22.
+The protein's natural variant, known as in MSA1; associated with disease susceptibility, features a modification of the amino acid from F to L at position 29.
+The protein's natural variant, known as in MSA1; associated with disease susceptibility, features a modification of the amino acid from P to H at position 49.
+The protein's natural variant, known as in MSA1; associated with disease susceptibility, features a modification of the amino acid from S to T at position 57.
+The natural variant of this protein is characterized by an amino acid alteration from R to H at position 69.
+The protein's natural variant, known as in MSA1; associated with disease susceptibility; decreased ubiquinone biosynthesis, features a modification of the amino acid from M to V at position 78.
+The protein's natural variant, known as in COQ10D1; decreased ubiquinone biosynthesis, features a modification of the amino acid from S to N at position 96.
+The protein's natural variant, known as in MSA1; associated with disease susceptibility, features a modification of the amino acid from I to T at position 97.
+The protein's natural variant, known as in MSA1; associated with disease susceptibility, features a modification of the amino acid from P to S at position 107.
+The protein's natural variant, known as in MSA1; associated with disease susceptibility, features a modification of the amino acid from S to F at position 113.
+The protein's natural variant, known as in COQ10D1; decreased ubiquinone biosynthesis, features a modification of the amino acid from M to R at position 132.
+The protein's natural variant, known as in COQ10D1; loss of ubiquinone biosynthesis, features a modification of the amino acid from R to H at position 147.
+The protein's natural variant, known as in COQ10D1; decreased ubiquinone biosynthesis, features a modification of the amino acid from N to S at position 178.
+The protein's natural variant, known as in COQ10D1; decreased 4-hydroxybenzoate decaprenyltransferase activity, features a modification of the amino acid from Y to C at position 247.
+The protein's natural variant, known as in COQ10D1; loss of ubiquinone biosynthesis, features a modification of the amino acid from A to V at position 252.
+The protein's natural variant, known as in MSA1; associated with disease susceptibility, features a modification of the amino acid from T to A at position 267.
+The protein's natural variant, known as in MSA1; associated with disease susceptibility, features a modification of the amino acid from S to C at position 297.
+The natural variant of this protein is characterized by an amino acid alteration from N to H at position 336.
+The protein's natural variant, known as in MSA1; associated with disease susceptibility, features a modification of the amino acid from R to Q at position 337.
+The protein's natural variant, known as in COQ10D1; unknown pathological significance, features a modification of the amino acid from G to A at position 340.
+The protein's natural variant, known as in MSA1; associated with disease susceptibility;, features a modification of the amino acid from V to A at position 343.
+The protein's natural variant, known as probable disease-associated variant found in patients with features of Noonan syndrome;, features a modification of the amino acid from S to T at position 35.
+The protein's natural variant, known as in NS8; results in increased ELK1 transcriptional activation; results in increased MAPK-ERK signaling;, features a modification of the amino acid from A to G at position 57.
+The protein's natural variant, known as in NS8; results in increased ELK1 transcriptional activation;, features a modification of the amino acid from E to G at position 81.
+The protein's natural variant, known as in NS8; results in increased ELK1 transcriptional activation;, features a modification of the amino acid from F to L at position 82.
+The protein's natural variant, known as probable disease-associated variant found in patients with features of Noonan syndrome;, features a modification of the amino acid from F to V at position 82.
+The protein's natural variant, known as probable disease-associated variant found in patients with features of Noonan syndrome;, features a modification of the amino acid from T to P at position 83.
+The protein's natural variant, known as probable disease-associated variant found in patients with features of Noonan syndrome;, features a modification of the amino acid from Y to H at position 89.
+The protein's natural variant, known as in NS8; results in increased MAPK-ERK signaling;, features a modification of the amino acid from M to I at position 90.
+The protein's natural variant, known as in NS8; results in increased ELK1 transcriptional activation;, features a modification of the amino acid from G to A at position 95.
+The protein's natural variant, known as in strain: Sprague-Dawley, features a modification of the amino acid from K to R at position 73.
+The natural variant of this protein is characterized by an amino acid alteration from L to P at position 37.
+The natural variant of this protein is characterized by an amino acid alteration from H to Y at position 61.
+The protein's natural variant, known as in MLASA3;, features a modification of the amino acid from S to N at position 148.
+The protein's natural variant, known as in LS, MC5DM1 and APAO;, features a modification of the amino acid from L to P at position 156.
+The protein's natural variant, known as in NARP and LS;, features a modification of the amino acid from L to R at position 156.
+The protein's natural variant, known as in LHON; possible rate primary mutation;, features a modification of the amino acid from I to T at position 192.
+The protein's natural variant, known as in LS and MIBSN;, features a modification of the amino acid from L to P at position 217.
+The protein's natural variant, known as in LS;, features a modification of the amino acid from L to P at position 220.
+The protein's natural variant, known as found in a family with syndactyly, undescended testes, delayed motor milestones, intellectual disability and signs of brain atrophy; unknown pathological significance;, features a modification of the amino acid from C to F at position 397.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from V to M at position 128.
+The natural variant of this protein is characterized by an amino acid alteration from V to L at position 123.
+The protein's natural variant, known as in a gastric adenocarcinoma sample; somatic mutation, features a modification of the amino acid from C to R at position 61.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from I to V at position 73.
+The protein's natural variant, known as in LDS2;, features a modification of the amino acid from R to H at position 190.
+The protein's natural variant, known as in LDS2;, features a modification of the amino acid from D to V at position 247.
+The protein's natural variant, known as in LDS2, features a modification of the amino acid from Q to HE at position 306.
+The protein's natural variant, known as in LDS2; has a negative effect on TGF-beta signaling;, features a modification of the amino acid from L to P at position 308.
+The protein's natural variant, known as in HNPCC6;, features a modification of the amino acid from T to M at position 315.
+The protein's natural variant, known as in LDS2, features a modification of the amino acid from T to P at position 325.
+The protein's natural variant, known as in a lung neuroendocrine carcinoma sample; somatic mutation, features a modification of the amino acid from H to Y at position 328.
+The protein's natural variant, known as in LDS2;, features a modification of the amino acid from Y to N at position 336.
+The protein's natural variant, known as in LDS2;, features a modification of the amino acid from A to P at position 355.
+The protein's natural variant, known as in LDS2, features a modification of the amino acid from G to R at position 357.
+The protein's natural variant, known as in LDS2;, features a modification of the amino acid from G to W at position 357.
+The protein's natural variant, known as in LDS2;, features a modification of the amino acid from H to R at position 377.
+The protein's natural variant, known as in a breast tumor;, features a modification of the amino acid from V to M at position 387.
+The protein's natural variant, known as in a breast tumor; signaling of TGF-beta significantly inhibited, features a modification of the amino acid from N to S at position 435.
+The protein's natural variant, known as in LDS2;, features a modification of the amino acid from D to N at position 446.
+The protein's natural variant, known as in a breast tumor; signaling of TGF-beta significantly inhibited, features a modification of the amino acid from V to A at position 447.
+The protein's natural variant, known as in LDS2; has a negative effect on TGF-beta signaling;, features a modification of the amino acid from S to F at position 449.
+The protein's natural variant, known as in a breast tumor; signaling of TGF-beta significantly inhibited, features a modification of the amino acid from L to M at position 452.
+The protein's natural variant, known as in LDS2, features a modification of the amino acid from M to K at position 457.
+The protein's natural variant, known as in LDS2;, features a modification of the amino acid from R to C at position 460.
+The protein's natural variant, known as in LDS2;, features a modification of the amino acid from R to H at position 460.
+The protein's natural variant, known as in a gastric adenocarcinoma sample; somatic mutation, features a modification of the amino acid from N to S at position 490.
+The protein's natural variant, known as in LDS2;, features a modification of the amino acid from G to V at position 509.
+The protein's natural variant, known as in LDS2, features a modification of the amino acid from I to F at position 510.
+The protein's natural variant, known as in LDS2, features a modification of the amino acid from I to S at position 510.
+The protein's natural variant, known as in LDS2;, features a modification of the amino acid from C to R at position 514.
+The protein's natural variant, known as in LDS2;, features a modification of the amino acid from W to R at position 521.
+The protein's natural variant, known as in esophageal cancer;, features a modification of the amino acid from E to Q at position 526.
+The protein's natural variant, known as in LDS2;, features a modification of the amino acid from R to C at position 528.
+The protein's natural variant, known as in LDS2;, features a modification of the amino acid from R to H at position 528.
+The protein's natural variant, known as in LDS2, features a modification of the amino acid from T to I at position 530.
+The protein's natural variant, known as in LDS2; has a negative effect on TGF-beta signaling;, features a modification of the amino acid from R to C at position 537.
+The protein's natural variant, known as in COXPD44; unknown pathological significance, features a modification of the amino acid from L to P at position 255.
+The protein's natural variant, known as in HCINF1; complete loss of function;, features a modification of the amino acid from R to Q at position 159.
+The protein's natural variant, known as in HCINF1; complete loss of function;, features a modification of the amino acid from E to K at position 322.
+The protein's natural variant, known as in HCINF1; complete loss of function;, features a modification of the amino acid from R to W at position 396.
+The protein's natural variant, known as in HCINF1; retains small but measurable levels of activity;, features a modification of the amino acid from L to S at position 409.
+The natural variant of this protein is characterized by an amino acid alteration from G to D at position 25.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from F to L at position 9.
+The protein's natural variant, known as in beta-1, features a modification of the amino acid from H to Q at position 2.
+The protein's natural variant, known as in beta-1, features a modification of the amino acid from G to A at position 5.
+The protein's natural variant, known as in beta-1, features a modification of the amino acid from L to V at position 11.
+The protein's natural variant, known as in SCAR30; decreased function in degradation of amyloid-beta protein 40; decreased metalloendopeptidase activity towards different substrates including an amyloid-beta peptide derivative; decreased protein levels in patient tissues; no effect on mitochondrial localization;, features a modification of the amino acid from R to Q at position 183.
+The protein's natural variant, known as in SCAR30; strongly decreased metalloendopeptidase activity towards amyloid-beta protein 40 and amyloid-beta protein 42;, features a modification of the amino acid from T to M at position 931.
+The protein's natural variant, known as found in a patient with unilateral multicystic kidney disease; unknown pathological significance;, features a modification of the amino acid from G to D at position 202.
+The protein's natural variant, known as found in patients with renal adysplasia; unknown pathological significance; normal targeting to the cell surface;, features a modification of the amino acid from P to L at position 273.
+The protein's natural variant, known as in strain: PCI 219, features a modification of the amino acid from E to V at position 10.
+The protein's natural variant, known as in strain: PCI 219, features a modification of the amino acid from G to E at position 43.
+The protein's natural variant, known as in strain: PCI 219, features a modification of the amino acid from N to D at position 253.
+The protein's natural variant, known as in strain: PCI 219, features a modification of the amino acid from F to Y at position 259.
+The protein's natural variant, known as in susceptible haplotype, features a modification of the amino acid from L to V at position 45.
+The protein's natural variant, known as in susceptible haplotype, features a modification of the amino acid from S to A at position 120.
+The protein's natural variant, known as in susceptible haplotype, features a modification of the amino acid from L to S at position 305.
+The protein's natural variant, known as in susceptible haplotype, features a modification of the amino acid from A to S at position 512.
+The protein's natural variant, known as in susceptible haplotype, features a modification of the amino acid from K to E at position 692.
+The protein's natural variant, known as in AMC1;, features a modification of the amino acid from R to P at position 258.
+The protein's natural variant, known as in AMC1;, features a modification of the amino acid from V to D at position 434.
+The protein's natural variant, known as in AD3; unknown pathological significance; decreased protease activity with APP;, features a modification of the amino acid from R to Q at position 35.
+The protein's natural variant, known as in AD3; also found in late-onset Alzheimer disease; impaired protease activity with APP; results in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio; no effect on interaction with GFAP;, features a modification of the amino acid from A to V at position 79.
+The protein's natural variant, known as in AD3; decreased protease activity with APP; no effect on interaction with GFAP;, features a modification of the amino acid from V to L at position 82.
+The protein's natural variant, known as in AD3, features a modification of the amino acid from I to T at position 83.
+The protein's natural variant, known as in AD3; the patient also manifest spastic paraparesis and apraxia; loss of protease activity with APP in vitro; altered amyloid-beta production in cells transfected with the mutant and increased amyloid-beta 42/amyloid-beta 40 ratio;, features a modification of the amino acid from L to P at position 85.
+The protein's natural variant, known as in AD3; decreased protease activity with APP; increased amyloid-beta 42/amyloid-beta 40 ratio;, features a modification of the amino acid from V to L at position 89.
+The protein's natural variant, known as in AD3; loss of protease activity with APP;, features a modification of the amino acid from C to S at position 92.
+The protein's natural variant, known as in AD3; unknown pathological significance; reduced protease activity with APP; no relevant change in amyloid-beta 42/amyloid-beta 40 ratio;, features a modification of the amino acid from V to M at position 94.
+The protein's natural variant, known as in AD3; loss of protease activity with APP;, features a modification of the amino acid from V to F at position 96.
+The protein's natural variant, known as in AD3; unknown pathological significance; slightly reduced protease activity with APP;, features a modification of the amino acid from V to L at position 97.
+The protein's natural variant, known as in AD3;, features a modification of the amino acid from F to L at position 105.
+The protein's natural variant, known as in frontotemporal dementia;, features a modification of the amino acid from L to P at position 113.
+The protein's natural variant, known as in AD3;, features a modification of the amino acid from Y to C at position 115.
+The protein's natural variant, known as in AD3; impaired protease activity with APP and increased amyloid-beta 42/amyloid-beta 40 ratio, features a modification of the amino acid from Y to H at position 115.
+The protein's natural variant, known as in AD3;, features a modification of the amino acid from T to I at position 116.
+The protein's natural variant, known as in AD3; unusual amyloid cotton wool plaques detected in one patient's brain; severe decrease of protease activity with APP; results in increased amyloid-beta 42/amyloid-beta 40 ratio;, features a modification of the amino acid from T to N at position 116.
+The protein's natural variant, known as in AD3; impaired ability to cleave Ephb2/CTF1; results in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio; impaired regulation of neurite outgrowth;, features a modification of the amino acid from P to L at position 117.
+The protein's natural variant, known as in AD3; results in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio; impaired regulation of neurite outgrowth;, features a modification of the amino acid from P to S at position 117.
+The protein's natural variant, known as in AD3; impaired protease activity with APP and increased amyloid-beta 42/amyloid-beta 40 ratio;, features a modification of the amino acid from E to D at position 120.
+The protein's natural variant, known as in AD3; impaired protease activity with APP and increased amyloid-beta 42/amyloid-beta 40 ratio;, features a modification of the amino acid from E to K at position 120.
+The protein's natural variant, known as in AD3; uncertain pathological significance; loss of protease activity with APP;, features a modification of the amino acid from L to R at position 134.
+The protein's natural variant, known as in AD3; impaired protease activity with APP and increased amyloid-beta 42/amyloid-beta 40 ratio;, features a modification of the amino acid from N to D at position 135.
+The protein's natural variant, known as in AD3;, features a modification of the amino acid from M to I at position 139.
+The protein's natural variant, known as in AD3;, features a modification of the amino acid from M to K at position 139.
+The protein's natural variant, known as in AD3;, features a modification of the amino acid from M to T at position 139.
+The protein's natural variant, known as in AD3; increased amyloid-beta 42/amyloid-beta 40 ratio;, features a modification of the amino acid from M to V at position 139.
+The protein's natural variant, known as in AD3; unknown pathological significance, features a modification of the amino acid from V to F at position 142.
+The protein's natural variant, known as in AD3;, features a modification of the amino acid from I to F at position 143.
+The protein's natural variant, known as in AD3; impaired protease activity with APP; results in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio;, features a modification of the amino acid from I to T at position 143.
+The protein's natural variant, known as in AD3;, features a modification of the amino acid from M to I at position 146.
+The protein's natural variant, known as in AD3; disease phenotype shows high clinical variability; founder mutation originating from Southern Italy and distributed worldwide; alters the conformation of the active site; slightly increased protease activity with APP; decreased activity for Notch1 cleavage; no loss of its ability to cleave Ephb2/CTF1;, features a modification of the amino acid from M to L at position 146.
+The protein's natural variant, known as in AD3; loss of function as calcium-leak channel; results in calcium overload in the endoplasmic reticulum;, features a modification of the amino acid from M to V at position 146.
+The protein's natural variant, known as in AD3; results in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio;, features a modification of the amino acid from T to I at position 147.
+The protein's natural variant, known as in AD3; abolishes protease activity with APP resulting in decreased amyloid-beta 42 and amyloid-beta 40 production;, features a modification of the amino acid from L to V at position 153.
+The protein's natural variant, known as in AD3; unknown pathological significance;, features a modification of the amino acid from Y to C at position 154.
+The protein's natural variant, known as in AD3; disease phenotype includes spastic paraparesis; abolishes protease activity with APP resulting in decreased amyloid-beta 42 and amyloid-beta 40 production;, features a modification of the amino acid from Y to N at position 154.
+The protein's natural variant, known as in AD3; unknown pathological significance, features a modification of the amino acid from Y to FTY at position 156.
+The protein's natural variant, known as in AD3; unknown pathological significance;, features a modification of the amino acid from Y to F at position 159.
+The protein's natural variant, known as in AD3; abolishes protease activity with APP; decreased activity for Notch cleavage;, features a modification of the amino acid from H to R at position 163.
+The protein's natural variant, known as in AD3; slightly increased protease activity with APP and slightly increased amyloid-beta 42 production;, features a modification of the amino acid from H to Y at position 163.
+The protein's natural variant, known as in AD3;, features a modification of the amino acid from W to C at position 165.
+The protein's natural variant, known as in AD3; onset in adolescence; severe decrease of protease activity with APP; results in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio; results in reduced Notch proteolysis;, features a modification of the amino acid from L to P at position 166.
+The protein's natural variant, known as in AD3;, features a modification of the amino acid from S to L at position 169.
+The protein's natural variant, known as in AD3; results in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio;, features a modification of the amino acid from S to P at position 169.
+The protein's natural variant, known as in AD3; results in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio;, features a modification of the amino acid from S to F at position 170.
+The protein's natural variant, known as in AD3; abolishes protease activity with APP;, features a modification of the amino acid from L to P at position 171.
+The protein's natural variant, known as in AD3; results in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio;, features a modification of the amino acid from L to W at position 173.
+The protein's natural variant, known as in AD3; results in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio;, features a modification of the amino acid from L to M at position 174.
+The protein's natural variant, known as in AD3; results in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio;, features a modification of the amino acid from F to L at position 177.
+The protein's natural variant, known as in AD3; unknown pathological significance;, features a modification of the amino acid from F to S at position 177.
+The protein's natural variant, known as in AD3; unknown pathological significance; abolishes protease activity with APP;, features a modification of the amino acid from S to P at position 178.
+The protein's natural variant, known as in PIDB and AD3; neuropathologic examination of brain sections from the patient shows the presence of Pick bodies and absence of beta-amyloid plaques; unknown pathological significance; results in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio in vitro;, features a modification of the amino acid from G to V at position 183.
+The protein's natural variant, known as in AD3; results in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio;, features a modification of the amino acid from E to D at position 184.
+The protein's natural variant, known as in AD3; results in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio;, features a modification of the amino acid from G to A at position 206.
+The protein's natural variant, known as in AD3; affects APP processing resulting in increased amyloid-beta 42/amyloid-beta 40 ratio; does not affect NOTCH processing; does not affect endoproteolysis; reduced interaction with PEN2; results in decreased protein levels in the endoplasmic reticulum but increased levels in early endosome; reduced ability to maintain ER calcium homeostasis;, features a modification of the amino acid from G to D at position 206.
+The protein's natural variant, known as in AD3; results in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio;, features a modification of the amino acid from G to S at position 206.
+The protein's natural variant, known as in AD3; unknown pathological significance;, features a modification of the amino acid from G to E at position 209.
+The protein's natural variant, known as in AD3; results in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio;, features a modification of the amino acid from G to R at position 209.
+The protein's natural variant, known as in AD3; abolishes protease activity with APP;, features a modification of the amino acid from G to V at position 209.
+The protein's natural variant, known as in AD3; increases protease activity with APP resulting in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio;, features a modification of the amino acid from I to L at position 213.
+The protein's natural variant, known as in AD3; decreased protease activity with APP resulting in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio;, features a modification of the amino acid from I to T at position 213.
+The protein's natural variant, known as probable disease-associated variant found in a patient with dementia;, features a modification of the amino acid from H to Y at position 214.
+The protein's natural variant, known as in AD3; with unusual amyloid cotton wool plaques; decreased protease activity with APP resulting in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio;, features a modification of the amino acid from G to R at position 217.
+The protein's natural variant, known as in AD3;, features a modification of the amino acid from L to P at position 219.
+The protein's natural variant, known as in AD3; unknown pathological significance; slightly increased protease activity with APP and slightly increased amyloid-beta 42/amyloid-beta 40 ratio;, features a modification of the amino acid from Q to R at position 222.
+The protein's natural variant, known as in AD3; decreased protease activity with APP resulting in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio;, features a modification of the amino acid from I to F at position 229.
+The protein's natural variant, known as in AD3; decreased protease activity with APP resulting in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio;, features a modification of the amino acid from A to T at position 231.
+The protein's natural variant, known as in AD3; results in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio;, features a modification of the amino acid from A to V at position 231.
+The protein's natural variant, known as in AD3; slightly decreased protease activity with APP resulting in altered amyloid-beta production and mildly increased amyloid-beta 42/amyloid-beta 40 ratio;, features a modification of the amino acid from M to L at position 233.
+The protein's natural variant, known as in AD3; decreased protease activity with APP resulting in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio;, features a modification of the amino acid from M to T at position 233.
+The protein's natural variant, known as in AD3; abolishes protease activity with APP;, features a modification of the amino acid from L to P at position 235.
+The protein's natural variant, known as in AD3; abolishes protease activity with APP, features a modification of the amino acid from L to R at position 235.
+The protein's natural variant, known as in AD3; reduced APP cleavage resulting in decreased amyloid-beta 42 and amyloid-beta 40 production; no relevant change in amyloid-beta 42/amyloid-beta 40 ratio;, features a modification of the amino acid from L to V at position 235.
+The protein's natural variant, known as in AD3; disease phenotype includes spastic paraparesis; unknown pathological significance; severe decrease of protease activity with APP; results in decreased amyloid-beta 42 and amyloid-beta 40 production;, features a modification of the amino acid from F to I at position 237.
+The protein's natural variant, known as in AD3; unknown pathological significance;, features a modification of the amino acid from F to L at position 237.
+The protein's natural variant, known as in AD3; nearly abolishes protease activity with APP; increased amyloid-beta 42/amyloid-beta 40 ratio; no loss of its ability to cleave Ephb2/CTF1;, features a modification of the amino acid from A to E at position 246.
+The protein's natural variant, known as in AD3; nearly abolishes protease activity with APP; increased amyloid-beta 42/amyloid-beta 40 ratio;, features a modification of the amino acid from L to S at position 250.
+The protein's natural variant, known as in AD3; nearly abolishes protease activity with APP; increased amyloid-beta 42/amyloid-beta 40 ratio; impaired ability to cleave Ephb2/CTF1;, features a modification of the amino acid from A to V at position 260.
+The protein's natural variant, known as in AD3; nearly abolishes protease activity with APP; increased amyloid-beta 42/amyloid-beta 40 ratio;, features a modification of the amino acid from V to F at position 261.
+The protein's natural variant, known as in AD3; decreased protease activity with APP resulting in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio;, features a modification of the amino acid from L to F at position 262.
+The protein's natural variant, known as in AD3, features a modification of the amino acid from L to V at position 262.
+The protein's natural variant, known as in AD3; results in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio;, features a modification of the amino acid from C to F at position 263.
+The protein's natural variant, known as in AD3; decreased protease activity with APP; increased amyloid-beta 42/amyloid-beta 40 ratio;, features a modification of the amino acid from C to R at position 263.
+The protein's natural variant, known as in AD3; decreased protease activity with APP; increased amyloid-beta 42/amyloid-beta 40 ratio; impaired ability to cleave Ephb2/CTF1;, features a modification of the amino acid from P to L at position 264.
+The protein's natural variant, known as in AD3; nearly abolishes protease activity with APP; increased amyloid-beta 42/amyloid-beta 40 ratio;, features a modification of the amino acid from G to S at position 266.
+The protein's natural variant, known as in AD3; decreased protease activity with APP; increased amyloid-beta 42/amyloid-beta 40 ratio;, features a modification of the amino acid from P to S at position 267.
+The protein's natural variant, known as in AD3; decreased protease activity with APP; increased amyloid-beta 42/amyloid-beta 40 ratio;, features a modification of the amino acid from R to G at position 269.
+The protein's natural variant, known as in AD3;, features a modification of the amino acid from R to H at position 269.
+The protein's natural variant, known as in AD3; abolishes protease activity with APP;, features a modification of the amino acid from L to V at position 271.
+The protein's natural variant, known as in AD3; unknown pathological significance; abolishes protease activity with APP;, features a modification of the amino acid from T to R at position 274.
+The protein's natural variant, known as in AD3; unknown pathological significance; reduced protease activity with APP resulting in reduced amyloid-beta 40 levels but no relevant changes in amyloid-beta 42/amyloid-beta 40 ratio;, features a modification of the amino acid from A to V at position 275.
+The protein's natural variant, known as in AD3; atypical phenotype presenting as language impairment, impaired frontal executive function and relative preservation of memory; severe decrease of APP and Notch proteolysis;, features a modification of the amino acid from R to I at position 278.
+The protein's natural variant, known as in AD3;, features a modification of the amino acid from R to T at position 278.
+The protein's natural variant, known as in AD3; strong deposition of amyloid-beta 42 is observed in brain regions of AD3 patients; decreased protease activity with APP resulting in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio; decreased activity for Notch1 cleavage;, features a modification of the amino acid from E to A at position 280.
+The protein's natural variant, known as in AD3; some AD3 patients manifest spastic paraparesis and unusual amyloid plaques with prominent amyloid angiopathy on brain biopsy; decreased protease activity with APP; increased amyloid-beta 42/amyloid-beta 40 ratio; impaired ability to cleave Ephb2/CTF1;, features a modification of the amino acid from E to G at position 280.
+The protein's natural variant, known as in AD3; abolishes protease activity with APP;, features a modification of the amino acid from L to R at position 282.
+The protein's natural variant, known as in AD3; results in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio;, features a modification of the amino acid from L to V at position 282.
+The protein's natural variant, known as in AD3; slightly decreased protease activity with APP and slightly decreased amyloid-beta 42/amyloid-beta 40 ratio;, features a modification of the amino acid from A to V at position 285.
+The protein's natural variant, known as in AD3; results in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio;, features a modification of the amino acid from L to V at position 286.
+The protein's natural variant, known as in AD3, features a modification of the amino acid from S to C at position 289.
+The protein's natural variant, known as probable disease-associated variant found in patients with late-onset Alzheimer disease; results in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio;, features a modification of the amino acid from K to R at position 311.
+The protein's natural variant, known as found in a renal cell carcinoma sample; somatic mutation, features a modification of the amino acid from Y to C at position 315.
+The protein's natural variant, known as in CMD1U; results in slightly decreased protease activity with APP and slightly decreased amyloid-beta 42/amyloid-beta 40 ratio;, features a modification of the amino acid from D to G at position 333.
+The protein's natural variant, known as in AD3; unknown pathological significance, features a modification of the amino acid from R to RR at position 352.
+The protein's natural variant, known as in AD3; unknown pathological significance; results in decreased protease activity with APP and decreased amyloid-beta 42/amyloid-beta 40 ratio;, features a modification of the amino acid from T to I at position 354.
+The protein's natural variant, known as in AD3; unknown pathological significance; results in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio;, features a modification of the amino acid from R to Q at position 358.
+The protein's natural variant, known as in AD3; unknown pathological significance;, features a modification of the amino acid from S to Y at position 365.
+The protein's natural variant, known as in AD3; unknown pathological significance, features a modification of the amino acid from R to M at position 377.
+The protein's natural variant, known as in AD3; decreased protease activity with APP; results in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio, features a modification of the amino acid from G to E at position 378.
+The protein's natural variant, known as in AD3; abolishes protease activity with APP;, features a modification of the amino acid from G to V at position 378.
+The protein's natural variant, known as in AD3;, features a modification of the amino acid from L to F at position 381.
+The protein's natural variant, known as in AD3; results in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio;, features a modification of the amino acid from L to V at position 381.
+The protein's natural variant, known as in AD3; results in reduced APP and Notch proteolysis; results in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio;, features a modification of the amino acid from G to A at position 384.
+The protein's natural variant, known as in AD3; abolishes protease activity with APP;, features a modification of the amino acid from S to I at position 390.
+The protein's natural variant, known as in AD3; results in reduced APP and Notch proteolysis; results in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio;, features a modification of the amino acid from L to V at position 392.
+The protein's natural variant, known as in AD3; unknown pathological significance; abolishes protease activity with APP;, features a modification of the amino acid from G to V at position 394.
+The protein's natural variant, known as in AD3; unknown pathological significance; decreased protease activity with APP; results in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio, features a modification of the amino acid from A to T at position 396.
+The protein's natural variant, known as in AD3; unknown pathological significance; decreased protease activity with APP;, features a modification of the amino acid from N to S at position 405.
+The protein's natural variant, known as in AD3;, features a modification of the amino acid from I to T at position 408.
+The protein's natural variant, known as in AD3; unknown pathological significance; decreased protease activity with APP;, features a modification of the amino acid from A to T at position 409.
+The protein's natural variant, known as in AD3; results in reduced APP and Notch proteolysis;, features a modification of the amino acid from C to Y at position 410.
+The protein's natural variant, known as in AD3; unknown pathological significance, features a modification of the amino acid from G to A at position 417.
+The protein's natural variant, known as in AD3; unknown pathological significance; nearly abolishes protease activity with APP;, features a modification of the amino acid from L to F at position 418.
+The protein's natural variant, known as in AD3; unknown pathological significance; slightly decreased protease activity with APP;, features a modification of the amino acid from A to P at position 426.
+The protein's natural variant, known as in AD3; decreased protease activity with APP; results in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio;, features a modification of the amino acid from A to E at position 431.
+The protein's natural variant, known as in AD3; with unusual amyloid cotton wool plaques; almost abolishes gamma-secretase activity; no endoproteolytic cleavage; no APP nor NOTCH1 processing; no detectable amyloid-beta;, features a modification of the amino acid from L to F at position 435.
+The protein's natural variant, known as in AD3; severe decrease of protease activity with APP;, features a modification of the amino acid from P to Q at position 436.
+The protein's natural variant, known as in AD3; partially abolishes gamma-secretase activity; results in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio;, features a modification of the amino acid from P to S at position 436.
+The protein's natural variant, known as in AD3; unknown pathological significance; no significant change of protease activity with APP;, features a modification of the amino acid from I to V at position 439.
+The protein's natural variant, known as in minor allele, features a modification of the amino acid from Y to H at position 485.
+The protein's natural variant, known as in RP13; no effect on interaction with SNRNP200 and EFTUD2;, features a modification of the amino acid from P to T at position 2301.
+The protein's natural variant, known as in RP13;, features a modification of the amino acid from F to L at position 2304.
+The protein's natural variant, known as in RP13; no effect on interaction with SNRNP200 and EFTUD2;, features a modification of the amino acid from H to P at position 2309.
+The protein's natural variant, known as in RP13; no effect on interaction with SNRNP200 and EFTUD2;, features a modification of the amino acid from H to R at position 2309.
+The protein's natural variant, known as in RP13; reduces interaction with SNRNP200 and EFTUD2, features a modification of the amino acid from R to G at position 2310.
+The protein's natural variant, known as in RP13; reduces interaction with SNRNP200 and EFTUD2;, features a modification of the amino acid from R to K at position 2310.
+The protein's natural variant, known as in RP13; reduces interaction with EFTUD2, but not with SNRNP200, features a modification of the amino acid from F to L at position 2314.
+The protein's natural variant, known as in RP13, features a modification of the amino acid from Y to N at position 2334.
+The protein's natural variant, known as in IMD85; decreases interaction with TOLLIP and UBC, features a modification of the amino acid from G to D at position 307.
+The protein's natural variant, known as in allele alpha;, features a modification of the amino acid from N to S at position 3.
+The protein's natural variant, known as in allele alpha;, features a modification of the amino acid from G to V at position 23.
+The protein's natural variant, known as in allele alpha;, features a modification of the amino acid from R to Q at position 28.
+The protein's natural variant, known as in allele alpha;, features a modification of the amino acid from V to A at position 29.
+The protein's natural variant, known as in allele alpha;, features a modification of the amino acid from H to R at position 51.
+The protein's natural variant, known as in allele alpha;, features a modification of the amino acid from G to D at position 52.
+The protein's natural variant, known as in allele alpha;, features a modification of the amino acid from P to R at position 53.
+The protein's natural variant, known as in allele alpha;, features a modification of the amino acid from V to L at position 76.
+The protein's natural variant, known as in allele alpha;, features a modification of the amino acid from T to I at position 115.
+The protein's natural variant, known as in allele alpha; requires 2 nucleotide substitutions, features a modification of the amino acid from A to I at position 116.
+The protein's natural variant, known as in allele alpha;, features a modification of the amino acid from I to T at position 118.
+The protein's natural variant, known as in allele alpha;, features a modification of the amino acid from V to I at position 133.
+The protein's natural variant, known as in allele alpha;, features a modification of the amino acid from H to R at position 136.
+The protein's natural variant, known as in allele alpha, features a modification of the amino acid from T to M at position 141.
+The protein's natural variant, known as in allele alpha;, features a modification of the amino acid from R to P at position 168.
+The protein's natural variant, known as in allele alpha;, features a modification of the amino acid from V to I at position 205.
+The protein's natural variant, known as in allele alpha;, features a modification of the amino acid from G to D at position 245.
+The protein's natural variant, known as in MMDS1; patient's skeletal muscles and fibroblasts show deficiency of mitochondrial respiratory chain complexes;, features a modification of the amino acid from R to P at position 21.
+The protein's natural variant, known as in MMDS1; patient's skin fibroblasts show deficiency of lipoic acid synthase and reduced lipoic acid content;, features a modification of the amino acid from R to W at position 182.
+The protein's natural variant, known as in MMDS1; alters protein structure; increases likelihood of existing as monomer; decreases ability to receive a Fe/S clusters from donor proteins; decreases delivery rates of [2Fe-2S] cluster to target proteins, features a modification of the amino acid from G to R at position 189.
+The protein's natural variant, known as in MMDS1; unknown pathological significance, features a modification of the amino acid from G to R at position 190.
+The protein's natural variant, known as in MMDS1; patient's skeletal muscles and fibroblasts show deficiency of mitochondrial respiratory chain complexes; increases homodimerization; unable to receive a Fe/S clusters from donor proteins; changes delivery rates of [2Fe-2S] cluster to target proteins;, features a modification of the amino acid from G to C at position 208.
+The protein's natural variant, known as in strain: G140, features a modification of the amino acid from G to T at position 6.
+The protein's natural variant, known as in strain: Canton-S, G02, G130 and G140, features a modification of the amino acid from M to L at position 78.
+The protein's natural variant, known as in strain: G130 and G140, features a modification of the amino acid from D to G at position 94.
+The protein's natural variant, known as in CDG2K; alters subcellular location;, features a modification of the amino acid from R to C at position 126.
+The protein's natural variant, known as in CDG2K; alters subcellular location;, features a modification of the amino acid from R to H at position 126.
+The protein's natural variant, known as in CDG2K; accumulates in Golgi compartment;, features a modification of the amino acid from G to R at position 304.
+The protein's natural variant, known as in FVH2;, features a modification of the amino acid from I to S at position 32.
+The protein's natural variant, known as in FVH2, features a modification of the amino acid from M to R at position 34.
+The protein's natural variant, known as in FVH2;, features a modification of the amino acid from E to K at position 233.
+The protein's natural variant, known as in FVH2;, features a modification of the amino acid from V to D at position 236.
+The protein's natural variant, known as in FVH2;, features a modification of the amino acid from G to R at position 412.
+The natural variant of this protein is characterized by an amino acid alteration from L to V at position 532.
+The protein's natural variant, known as in ANPH2; no effect on protein abundance; loss of protein serine/threonine kinase activity; loss of autophosphorylation at T-208; loss of function in regulation of hippo signaling, features a modification of the amino acid from YDYISERQ to E at position 145.
+The protein's natural variant, known as in an ovarian Endometrioid carcinoma sample; somatic mutation;, features a modification of the amino acid from K to R at position 503.
+The protein's natural variant, known as in a breast pleomorphic lobular carcinoma sample; somatic mutation, features a modification of the amino acid from G to E at position 541.
+The protein's natural variant, known as in MOPC 47A, features a modification of the amino acid from S to A at position 2.
+The protein's natural variant, known as in MOPC 47A and M511, features a modification of the amino acid from S to C at position 18.
+The protein's natural variant, known as in MOPC 47A and M511, features a modification of the amino acid from N to S at position 67.
+The protein's natural variant, known as in MOPC 47A, features a modification of the amino acid from A to T at position 73.
+The protein's natural variant, known as in M511; requires 2 nucleotide substitutions, features a modification of the amino acid from P to G at position 112.
+The protein's natural variant, known as in MOPC 47A and M511; requires 2 nucleotide substitutions, features a modification of the amino acid from S to Q at position 135.
+The protein's natural variant, known as in MOPC 47A and M511, features a modification of the amino acid from N to D at position 141.
+The protein's natural variant, known as in MOPC 47A, features a modification of the amino acid from Q to E at position 168.
+The protein's natural variant, known as in MOPC 47A, features a modification of the amino acid from VT to SQ at position 213.
+The protein's natural variant, known as in M511, features a modification of the amino acid from E to G at position 235.
+The protein's natural variant, known as in M511; requires 2 nucleotide substitutions, features a modification of the amino acid from T to D at position 295.
+The protein's natural variant, known as in M511; requires 2 nucleotide substitutions, features a modification of the amino acid from Q to G at position 301.
+The protein's natural variant, known as in M511; requires 2 nucleotide substitutions, features a modification of the amino acid from N to Q at position 329.
+The protein's natural variant, known as in M511, features a modification of the amino acid from S to N at position 331.
+The protein's natural variant, known as in strain: Isolate AoAz2, features a modification of the amino acid from A to T at position 24.
+The natural variant of this protein is characterized by an amino acid alteration from I to L at position 16.
+The natural variant of this protein is characterized by an amino acid alteration from K to Q at position 44.
+The natural variant of this protein is characterized by an amino acid alteration from A to G at position 59.
+The natural variant of this protein is characterized by an amino acid alteration from G to A at position 78.
+The natural variant of this protein is characterized by an amino acid alteration from R to H at position 173.
+The protein's natural variant, known as in strain: 62A, features a modification of the amino acid from V to A at position 27.
+The protein's natural variant, known as in strain: 186, features a modification of the amino acid from S to R at position 714.
+The protein's natural variant, known as in strain: 130, features a modification of the amino acid from S to P at position 740.
+The protein's natural variant, known as in strain: 138, 140 and 196, features a modification of the amino acid from S to N at position 783.
+The protein's natural variant, known as in strain: 128, 130, 138, 140, 141, 186, 187 and 196, features a modification of the amino acid from T to A at position 835.
+The protein's natural variant, known as in strain: 128, 130, 138, 140, 141, 186, 187 and 196, features a modification of the amino acid from S to T at position 854.
+The protein's natural variant, known as in strain: 128, 130, 141, 186 and 187, features a modification of the amino acid from D to E at position 866.
+The protein's natural variant, known as in SCKL2;, features a modification of the amino acid from R to W at position 100.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from R to H at position 62.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from D to G at position 88.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from R to L at position 107.
+The protein's natural variant, known as found in a patient with Joubert syndrome; unknown pathological significance;, features a modification of the amino acid from E to G at position 265.
+The protein's natural variant, known as in strain: Canton-S, features a modification of the amino acid from T to S at position 167.
+The protein's natural variant, known as in strain: Canton-S, features a modification of the amino acid from S to T at position 172.
+The protein's natural variant, known as in strain: Berkeley, features a modification of the amino acid from Y to N at position 346.
+The protein's natural variant, known as in strain: NOD; reduces DNA-binding affinity, features a modification of the amino acid from L to M at position 327.
+The protein's natural variant, known as in DCBXA; reduces L-glutamate and L-cysteine transport activities; reduces cell membrane expression;, features a modification of the amino acid from R to W at position 445.
+The protein's natural variant, known as in MCIDDS; unknown pathological significance; mildly decreased function in potassium transmembrane transport;, features a modification of the amino acid from R to Q at position 89.
+The protein's natural variant, known as probable disease-associated variant found in patients with Schwannomatosis; loss of function;, features a modification of the amino acid from D to H at position 208.
+The protein's natural variant, known as in COQ10D6;, features a modification of the amino acid from G to R at position 255.
+The protein's natural variant, known as in COQ10D6; unknown pathological significance;, features a modification of the amino acid from P to L at position 261.
+The protein's natural variant, known as in COQ10D6;, features a modification of the amino acid from A to D at position 353.
+The natural variant of this protein is characterized by an amino acid alteration from Y to N at position 76.
+The protein's natural variant, known as in strain: GK, features a modification of the amino acid from R to C at position 1142.
+The protein's natural variant, known as in BARTS1;, features a modification of the amino acid from V to F at position 272.
+The protein's natural variant, known as in BARTS1;, features a modification of the amino acid from D to N at position 648.
+The protein's natural variant, known as in strain: NCTC 11638, features a modification of the amino acid from A to T at position 16.
+The protein's natural variant, known as in strain: NCTC 11638, features a modification of the amino acid from V to G at position 152.
+The protein's natural variant, known as in IMD47;, features a modification of the amino acid from L to P at position 144.
+The protein's natural variant, known as in IMD47; probable loss of proton-transporting V-type ATPase complex assembly in yeast; unable to restore V-ATPase-dependent growth in Voa1 mutant yeast;, features a modification of the amino acid from Y to C at position 313.
+The protein's natural variant, known as in IMD47; probable loss of proton-transporting V-type ATPase complex assembly in yeast; unable to restore V-ATPase-dependent growth in Voa1 mutant yeast;, features a modification of the amino acid from E to K at position 346.
+The protein's natural variant, known as in IMD47; restores V-ATPase-dependent growth in Voa1 mutant yeast;, features a modification of the amino acid from M to I at position 428.
+The protein's natural variant, known as in strain: BALB/cAn, features a modification of the amino acid from K to N at position 6.
+The protein's natural variant, known as in strain: BALB/cAn, features a modification of the amino acid from Y to D at position 58.
+The protein's natural variant, known as in strain: BALB/cAn, features a modification of the amino acid from V to G at position 100.
+The protein's natural variant, known as in strain: BALB/cAn, features a modification of the amino acid from G to R at position 131.
+The protein's natural variant, known as in strain: BALB/cAn, features a modification of the amino acid from R to M at position 245.
+The protein's natural variant, known as in strain: BALB/cAn, features a modification of the amino acid from P to S at position 297.
+The protein's natural variant, known as in strain: BALB/cAn, features a modification of the amino acid from D to E at position 324.
+The protein's natural variant, known as in strain: BALB/cAn, features a modification of the amino acid from F to L at position 339.
+The protein's natural variant, known as in strain: BALB/cAn, features a modification of the amino acid from K to T at position 436.
+The protein's natural variant, known as in strain: BALB/cAn, features a modification of the amino acid from KTQ to NRK at position 440.
+The protein's natural variant, known as in strain: BALB/cAn, features a modification of the amino acid from S to I at position 443.
+The protein's natural variant, known as in strain: BALB/cAn, features a modification of the amino acid from E to V at position 456.
+The protein's natural variant, known as in strain: BALB/cAn, features a modification of the amino acid from G to R at position 459.
+The protein's natural variant, known as in strain: BALB/cAn, features a modification of the amino acid from R to S at position 483.
+The protein's natural variant, known as in strain: BALB/cAn, features a modification of the amino acid from V to I at position 496.
+The protein's natural variant, known as in strain: BALB/cAn, features a modification of the amino acid from N to D at position 523.
+The protein's natural variant, known as in DEE105; unknown pathological significance, features a modification of the amino acid from G to D at position 187.
+The protein's natural variant, known as in DEE105; unknown pathological significance; patient fibroblasts show normal expression and localization;, features a modification of the amino acid from R to W at position 433.
+The protein's natural variant, known as in DEE105; unknown pathological significance, features a modification of the amino acid from L to P at position 533.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from R to C at position 201.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from R to H at position 201.
+The protein's natural variant, known as in GNASHYP;, features a modification of the amino acid from P to T at position 374.
+The protein's natural variant, known as in GNASHYP, features a modification of the amino acid from P to PQPIPTPGRPLTP at position 375.
+The protein's natural variant, known as in GNASHYP, features a modification of the amino acid from L to V at position 397.
+The protein's natural variant, known as in strain: cv. Castalia and cv. Walter; in allele LeMAN4i; inactive enzyme, features a modification of the amino acid from RLSKLS to AL at position 399.
+The protein's natural variant, known as in isoform CBS, features a modification of the amino acid from A to T at position 877.
+The protein's natural variant, known as in isoform CBS, features a modification of the amino acid from S to N at position 1104.
+The natural variant of this protein is characterized by an amino acid alteration from P to S at position 71.
+The protein's natural variant, known as in allele CX37*2;, features a modification of the amino acid from P to S at position 319.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from T to M at position 996.
+The protein's natural variant, known as in FRDA;, features a modification of the amino acid from L to S at position 106.
+The protein's natural variant, known as in FRDA;, features a modification of the amino acid from D to Y at position 122.
+The protein's natural variant, known as in FRDA;, features a modification of the amino acid from G to V at position 130.
+The protein's natural variant, known as in FRDA; reduces interaction with LYRM4; the interaction is rescued by nickel; a murine cellular FRDA model, deleted for endogenous frataxin and expressing human mutant frataxin cDNA shows defects in mitochondrial structure, mitochondrial iron deposits, decreased enzymatic activity of some mitochondrial and cytoplasmic iron-sulfur cluster-containing enzymes, increased RNA-binding activity of ACO1 and increased sensitivity to oxidative stress; decreases the level of covalent incorporation of sulfur into both NFS1 and ISCU;, features a modification of the amino acid from I to F at position 154.
+The protein's natural variant, known as in FRDA; reduces interaction with LYRM4; the interaction is rescued by nickel; drastically decreases affinity for the SDAU complex by > 75-fold; decreases the level of covalent incorporation of sulfur into both NFS1 and ISCU;, features a modification of the amino acid from W to R at position 155.
+The protein's natural variant, known as in FRDA; mild form; decreases affinity for the SDAU complex by 40-fold; decreases the level of covalent incorporation of sulfur into both NFS1 and ISCU;, features a modification of the amino acid from R to C at position 165.
+The protein's natural variant, known as in FRDA;, features a modification of the amino acid from L to F at position 182.
+The protein's natural variant, known as in FRDA;, features a modification of the amino acid from L to R at position 198.
+The natural variant of this protein is characterized by an amino acid alteration from G to A at position 72.
+The natural variant of this protein is characterized by an amino acid alteration from M to MM at position 124.
+The natural variant of this protein is characterized by an amino acid alteration from Q to R at position 185.
+The protein's natural variant, known as in OI15; reduced capacity to activate canonical Wnt signaling, features a modification of the amino acid from E to D at position 123.
+The protein's natural variant, known as in OI15, features a modification of the amino acid from C to F at position 143.
+The protein's natural variant, known as in OI15; reduced capacity to activate canonical Wnt signaling, features a modification of the amino acid from C to G at position 153.
+The protein's natural variant, known as in OI15; completely fails to activate the Wnt-regulated beta-catenin signaling cascade, features a modification of the amino acid from G to C at position 177.
+The protein's natural variant, known as in OSTEOP; reduced capacity to activate canonical Wnt signaling;, features a modification of the amino acid from C to G at position 218.
+The protein's natural variant, known as in OSTEOP; associated with susceptibility to early-onset osteoporosis; completely fails to activate the Wnt-regulated beta-catenin signaling cascade;, features a modification of the amino acid from R to W at position 235.
+The protein's natural variant, known as in OI15, features a modification of the amino acid from F to C at position 298.
+The protein's natural variant, known as in OI15;, features a modification of the amino acid from V to F at position 355.
+The protein's natural variant, known as in MCPH20; unknown pathological significance, features a modification of the amino acid from G to R at position 459.
+The protein's natural variant, known as in MCPH20; unknown pathological significance;, features a modification of the amino acid from S to F at position 841.
+The protein's natural variant, known as in MCPH20; Decreased expression at the mRNA level and loss of localization at the midbody during cytokinesis and consequently loss of CIT/CRIK recruitment to the midbody, when analyzed in primary fibroblasts from a patient who is a compound heterozygous with variant V-1221;, features a modification of the amino acid from H to D at position 849.
+The protein's natural variant, known as in MCPH20; Decreased expression at the mRNA level and loss of localization at the midbody during cytokinesis and consequently loss of CIT/CRIK recruitment to the midbody, when analyzed in primary fibroblasts from a patient who is a compound heterozygous with variant D-849, features a modification of the amino acid from G to V at position 1221.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from R to T at position 395.
+The protein's natural variant, known as in strain: k3 and k5, features a modification of the amino acid from S to N at position 322.
+The protein's natural variant, known as in strain: k5, features a modification of the amino acid from M to I at position 402.
+The protein's natural variant, known as in strain: Berkeley, k1, k8, Oregon-R, pe7 and pe10, features a modification of the amino acid from N to T at position 493.
+The protein's natural variant, known as in strain: k2, features a modification of the amino acid from S to T at position 527.
+The protein's natural variant, known as in strain: Berkeley, k1, k2, k3, k5, k8, k9 and k11, features a modification of the amino acid from G to A at position 639.
+The protein's natural variant, known as in strain: k5, features a modification of the amino acid from M to I at position 747.
+The protein's natural variant, known as in strain: Berkeley, k9, wi10 and wi19, features a modification of the amino acid from T to I at position 823.
+The protein's natural variant, known as in strain: k1, features a modification of the amino acid from T to S at position 830.
+The protein's natural variant, known as in strain: Berkeley, k3, k8, k9, wi10 and wi19, features a modification of the amino acid from C to S at position 837.
+The protein's natural variant, known as in strain: Berkeley, k1, k2, k3, k5, k8, k9, k11, pe1, pe4, pe45, pe5, wi4, wi7, wi10, wi13, wi18 and wi19, features a modification of the amino acid from M to T at position 842.
+The protein's natural variant, known as in strain: k8, features a modification of the amino acid from S to P at position 845.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from V to L at position 484.
+The natural variant of this protein is characterized by an amino acid alteration from R to T at position 22.
+The natural variant of this protein is characterized by an amino acid alteration from E to D at position 29.
+The natural variant of this protein is characterized by an amino acid alteration from EY to NI at position 38.
+The protein's natural variant, known as in strain: F4233 / Serotype 1/2b, F5782 /Serotype 4b, F6789 / Serotype 1/2b and 12067, features a modification of the amino acid from S to L at position 35.
+The protein's natural variant, known as in strain: F4233 / Serotype 1/2b, F5782 /Serotype 4b, F6789 / Serotype 1/2b and 12067, features a modification of the amino acid from V to I at position 438.
+The protein's natural variant, known as in strain: F4233 / Serotype 1/2b, F5782 /Serotype 4b, F6789 / Serotype 1/2b and 12067, features a modification of the amino acid from K to S at position 523.
+The protein's natural variant, known as in EKVP7; patient cells show a change in the subcellular location pattern; does not associate with cell membrane; diffuse location into the cytoplasm;, features a modification of the amino acid from G to R at position 156.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from K to N at position 209.
+The protein's natural variant, known as in RCM6; loss-of-function variant unable to rescue cardiac defects in zebrafish morphants; results in greatly reduced microtubule activated motor activity; does not localize to the spindle midzone;, features a modification of the amino acid from R to W at position 182.
+The protein's natural variant, known as in Lmbr1-N; associated with preaxial polydactyly, features a modification of the amino acid from R to Q at position 266.
+The protein's natural variant, known as in strain: Isolate TM-2, features a modification of the amino acid from V to I at position 117.
+The protein's natural variant, known as in strain: Isolate TM-2, features a modification of the amino acid from FA to LT at position 122.
+The protein's natural variant, known as in strain: Isolate TM-2 and Isolate TM-3, features a modification of the amino acid from I to T at position 257.
+The protein's natural variant, known as in strain: Isolate TM-2 and Isolate TM-3, features a modification of the amino acid from N to S at position 263.
+The natural variant of this protein is characterized by an amino acid alteration from K to R at position 146.
+The protein's natural variant, known as in LMP-2b, features a modification of the amino acid from R to H at position 60.
+The protein's natural variant, known as in LMP-2b, features a modification of the amino acid from R to C at position 126.
+The protein's natural variant, known as in LMP-2b and LMP-2q, features a modification of the amino acid from N to D at position 177.
+The protein's natural variant, known as in a non-small cell lung cancer cell line;, features a modification of the amino acid from S to F at position 353.
+The protein's natural variant, known as in strain: Isolate TS99, features a modification of the amino acid from I to L at position 7.
+The protein's natural variant, known as in strain: Isolate TS54, features a modification of the amino acid from KN to RD at position 15.
+The protein's natural variant, known as in strain: Isolate TS54, features a modification of the amino acid from T to S at position 24.
+The protein's natural variant, known as in strain: Isolate TS99, features a modification of the amino acid from A to P at position 29.
+The protein's natural variant, known as in strain: Isolate TS54, features a modification of the amino acid from G to D at position 67.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from I to T at position 289.
+The protein's natural variant, known as in strain: MB01a, MB13a, MB15b and MB46b, features a modification of the amino acid from A to V at position 14.
+The protein's natural variant, known as in strain: MB25a, features a modification of the amino acid from M to I at position 46.
+The protein's natural variant, known as in strain: MB25a, features a modification of the amino acid from I to N at position 47.
+The protein's natural variant, known as in strain: Berkeley, features a modification of the amino acid from N to Y at position 113.
+The protein's natural variant, known as in strain: MB29b, features a modification of the amino acid from L to F at position 139.
+The protein's natural variant, known as in strain: MB47a, features a modification of the amino acid from V to M at position 183.
+The protein's natural variant, known as in strain: MB33a and MB36a, features a modification of the amino acid from R to H at position 250.
+The protein's natural variant, known as in strain: MB36a, features a modification of the amino acid from S to T at position 349.
+The protein's natural variant, known as in strain: MB34a, MB36a, MB45b, MB46b, MB47a and MB58b, features a modification of the amino acid from S to T at position 351.
+The protein's natural variant, known as in strain: MB37a, features a modification of the amino acid from R to C at position 434.
+The protein's natural variant, known as in strain: SMQ-301, features a modification of the amino acid from I to V at position 42.
+The protein's natural variant, known as in strain: SMQ-301, features a modification of the amino acid from K to N at position 70.
+The protein's natural variant, known as in strain: SMQ-301, features a modification of the amino acid from I to T at position 107.
+The protein's natural variant, known as in strain: SMQ-301, features a modification of the amino acid from V to A at position 243.
+The protein's natural variant, known as in strain: SMQ-301, features a modification of the amino acid from A to D at position 480.
+The protein's natural variant, known as in strain: cv. Samsun, features a modification of the amino acid from C to Y at position 199.
+The protein's natural variant, known as in PCH17; unknown pathological significance;, features a modification of the amino acid from H to L at position 619.
+The protein's natural variant, known as in strain: cv. C24 and cv. Cvi-0, features a modification of the amino acid from Y to S at position 58.
+The protein's natural variant, known as in strain: cv. Cvi-0, features a modification of the amino acid from L to S at position 70.
+The protein's natural variant, known as in strain: cv. C24 and cv. Cvi-0, features a modification of the amino acid from L to P at position 77.
+The protein's natural variant, known as in strain: cv. Cvi-0, features a modification of the amino acid from H to Q at position 91.
+The protein's natural variant, known as in strain: cv. C24 and cv. Cvi-0, features a modification of the amino acid from Q to R at position 104.
+The protein's natural variant, known as in strain: cv. C24, features a modification of the amino acid from I to V at position 179.
+The protein's natural variant, known as in strain: cv. C24 and cv. Cvi-0, features a modification of the amino acid from T to A at position 184.
+The protein's natural variant, known as in strain: cv. Cvi-0, features a modification of the amino acid from P to A at position 191.
+The protein's natural variant, known as in strain: cv. C24, features a modification of the amino acid from R to K at position 308.
+The protein's natural variant, known as in strain: cv. Cvi-0, features a modification of the amino acid from N to S at position 311.
+The protein's natural variant, known as in strain: cv. Cvi-0, features a modification of the amino acid from G to R at position 330.
+The protein's natural variant, known as in strain: cv. C24 and cv. Cvi-0, features a modification of the amino acid from T to N at position 366.
+The protein's natural variant, known as in allele C and allele D, features a modification of the amino acid from S to P at position 28.
+The protein's natural variant, known as in allele D, features a modification of the amino acid from S to N at position 83.
+The natural variant of this protein is characterized by an amino acid alteration from I to T at position 209.
+The protein's natural variant, known as in allele UGT2B7*1;, features a modification of the amino acid from Y to H at position 268.
+The protein's natural variant, known as in variant with duplicated exon 2, features a modification of the amino acid from T to THFQTMLKSKLNVLTLKKEPLPAVIFHEPEAIELCTTTPLMKTRTHSGCK at position 43.
+The protein's natural variant, known as in NEDHRIT; undetectable protein expression;, features a modification of the amino acid from N to S at position 1076.
+The protein's natural variant, known as probable disease-associated variant found in a patient with Joubert syndrome; digenic inheritance; the patient also carries a truncating mutation in CC2D2A;, features a modification of the amino acid from M to T at position 36.
+The protein's natural variant, known as found in a patient with Meckel syndrome; unknown pathological significance, features a modification of the amino acid from Q to E at position 89.
+The protein's natural variant, known as probable disease-associated variant found in a patient with Joubert syndrome; digenic inheritance; the patient also carries a truncating mutation in KIF7;, features a modification of the amino acid from R to H at position 179.
+The protein's natural variant, known as found in a patient with autism; unknown pathological significance;, features a modification of the amino acid from P to A at position 206.
+The protein's natural variant, known as found in a patient with autism; unknown pathological significance;, features a modification of the amino acid from C to G at position 240.
+The protein's natural variant, known as probable disease-associated variant found in a patient with Joubert syndrome; digenic inheritance; the patient also carries mutation A-1447 in CC2D2A;, features a modification of the amino acid from R to C at position 360.
+The protein's natural variant, known as associated with increased risk for AD; possibly influences secretion and intracellular maturation;, features a modification of the amino acid from A to V at position 58.
+The protein's natural variant, known as in CLN10;, features a modification of the amino acid from F to I at position 229.
+The protein's natural variant, known as in CLN10;, features a modification of the amino acid from W to C at position 383.
+The protein's natural variant, known as de novo variant found in a patient with childhood apraxia of speech; unknown pathological significance, features a modification of the amino acid from N to T at position 168.
+The protein's natural variant, known as in strain: Isolate LOKO4.37, features a modification of the amino acid from P to R at position 60.
+The natural variant of this protein is characterized by an amino acid alteration from L to P at position 172.
+The protein's natural variant, known as in an ovarian mucinous carcinoma sample; somatic mutation, features a modification of the amino acid from S to F at position 81.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation, features a modification of the amino acid from L to V at position 97.
+The protein's natural variant, known as in an ovarian mucinous carcinoma sample; somatic mutation;, features a modification of the amino acid from M to V at position 104.
+The natural variant of this protein is characterized by an amino acid alteration from D to N at position 158.
+The protein's natural variant, known as in PNPD;, features a modification of the amino acid from E to K at position 89.
+The protein's natural variant, known as in PNPD;, features a modification of the amino acid from D to G at position 128.
+The protein's natural variant, known as in PNPD;, features a modification of the amino acid from A to P at position 174.
+The protein's natural variant, known as in PNPD;, features a modification of the amino acid from Y to C at position 192.
+The protein's natural variant, known as in PNPD;, features a modification of the amino acid from R to P at position 234.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from E to V at position 675.
+The protein's natural variant, known as in a pancreatic ductal adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from A to T at position 880.
+The protein's natural variant, known as in an acute myeloid leukemia sample; somatic mutation;, features a modification of the amino acid from A to V at position 338.
+The protein's natural variant, known as in allele B, features a modification of the amino acid from G to S at position 15.
+The protein's natural variant, known as in allele B, features a modification of the amino acid from K to H at position 18.
+The protein's natural variant, known as in allele D-Zambia, features a modification of the amino acid from D to G at position 20.
+The protein's natural variant, known as in allele D-Zambia, features a modification of the amino acid from S to T at position 43.
+The protein's natural variant, known as in allele B, features a modification of the amino acid from K to N at position 119.
+The protein's natural variant, known as in allele C-Rhodesia, features a modification of the amino acid from K to Q at position 131.
+The protein's natural variant, known as found in a renal cell carcinoma sample; somatic mutation, features a modification of the amino acid from K to Q at position 5.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from K to N at position 67.
+The protein's natural variant, known as in XID; prevents interaction with ARID3A, features a modification of the amino acid from R to C at position 28.
+The natural variant of this protein is characterized by an amino acid alteration from H to R at position 485.
+The natural variant of this protein is characterized by an amino acid alteration from V to L at position 490.
+The protein's natural variant, known as in CAID; patient fibroblasts exhibit significantly faster cell proliferation than controls; during mitosis the mutant protein is localized in an ordered fashion around the centromeres but display a rather homogeneous cytoplasmic localization pattern;, features a modification of the amino acid from K to E at position 23.
+The protein's natural variant, known as in strain: cv. CMV3, features a modification of the amino acid from G to D at position 12.
+The protein's natural variant, known as in strain: cv. CML258, cv. CML5, cv. NC354 and cv. Q6199, features a modification of the amino acid from G to GG at position 13.
+The protein's natural variant, known as in strain: cv. H99, cv. NC260, cv. PA91, cv. U267Y, cv. W64A and cv. WF9, features a modification of the amino acid from G to V at position 28.
+The protein's natural variant, known as in D8-d1; induces a dwarf phenotype, features a modification of the amino acid from DVAQK to G at position 59.
+The protein's natural variant, known as in strain: cv. MO24W, features a modification of the amino acid from Q to H at position 255.
+The protein's natural variant, known as in strain: cv. B103, features a modification of the amino acid from S to R at position 304.
+The protein's natural variant, known as in strain: cv. EP1, features a modification of the amino acid from T to I at position 390.
+The protein's natural variant, known as in strain: cv. CMV3, features a modification of the amino acid from Y to C at position 413.
+The protein's natural variant, known as in strain: cv. GT112, features a modification of the amino acid from I to T at position 475.
+The protein's natural variant, known as in strain: cv. H99, features a modification of the amino acid from E to K at position 480.
+The protein's natural variant, known as in strain: cv. NC260, features a modification of the amino acid from N to S at position 484.
+The protein's natural variant, known as in strain: cv. KUI43, features a modification of the amino acid from N to D at position 486.
+The protein's natural variant, known as in strain: cv. NC320, features a modification of the amino acid from Y to H at position 500.
+The protein's natural variant, known as in strain: cv. NC250, features a modification of the amino acid from F to S at position 505.
+The protein's natural variant, known as in strain: cv. A619, cv. CM105, cv. CM7, cv. CM174, cv. CMV3, cv. F2834T, cv. F7, cv. N192, cv. Ohio 43 and cv. P39, features a modification of the amino acid from T to A at position 519.
+The protein's natural variant, known as in strain: cv. F2, features a modification of the amino acid from M to K at position 533.
+The protein's natural variant, known as in strain: cv. M37W and cv. Tzi10, features a modification of the amino acid from G to S at position 578.
+The protein's natural variant, known as in cells resistant to the antineoplastic agents VP-16 and VM-26, features a modification of the amino acid from R to Q at position 493.
+The protein's natural variant, known as in TEMTYS;, features a modification of the amino acid from L to Q at position 51.
+The protein's natural variant, known as in strain: 51, features a modification of the amino acid from PG to QA at position 16.
+The protein's natural variant, known as probable disease-associated variant found in patients with pathologic myopia; may decrease mitochondrial complex I activity; decreases the production of ATP; decreases reactive oxygen species production, features a modification of the amino acid from D to E at position 266.
+The protein's natural variant, known as no significant functional differences;, features a modification of the amino acid from N to D at position 32.
+The protein's natural variant, known as no changes in receptor binding or functional signaling;, features a modification of the amino acid from G to R at position 34.
+The natural variant of this protein is characterized by an amino acid alteration from Y to H at position 250.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from V to I at position 33.
+The protein's natural variant, known as in DEE57; decreased protein abundance; loss of chloride-activated potassium channel activity; loss of potassium selectivity;, features a modification of the amino acid from F to L at position 240.
+The protein's natural variant, known as in RP2, features a modification of the amino acid from C to Y at position 67.
+The protein's natural variant, known as in RP2, features a modification of the amino acid from C to Y at position 86.
+The protein's natural variant, known as in RP2; uncertain pathological significance, features a modification of the amino acid from P to L at position 95.
+The protein's natural variant, known as in RP2, features a modification of the amino acid from C to G at position 108.
+The protein's natural variant, known as in RP2, features a modification of the amino acid from C to Y at position 108.
+The protein's natural variant, known as in RP2;, features a modification of the amino acid from R to C at position 118.
+The protein's natural variant, known as in RP2; reduces affinity for ARL3 800-fold; loss of stimulation of tubulin GTPase activity; no effect on subcellular location;, features a modification of the amino acid from R to H at position 118.
+The protein's natural variant, known as in RP2;, features a modification of the amino acid from R to L at position 118.
+The protein's natural variant, known as in RP2; reduces affinity for ARL3 150-fold and inhibits the GTP-hydrolysis rate of ARL3, features a modification of the amino acid from E to G at position 138.
+The protein's natural variant, known as in RP2, features a modification of the amino acid from L to P at position 188.
+The protein's natural variant, known as in RP2, features a modification of the amino acid from L to R at position 253.
+The protein's natural variant, known as reduces affinity for ARL3 3-fold;, features a modification of the amino acid from R to W at position 282.
+The protein's natural variant, known as in beta-B, features a modification of the amino acid from G to S at position 1.
+The protein's natural variant, known as in beta-B, features a modification of the amino acid from T to S at position 4.
+The protein's natural variant, known as in beta-B, features a modification of the amino acid from N to S at position 139.
+The protein's natural variant, known as in beta-B, features a modification of the amino acid from K to R at position 144.
+The protein's natural variant, known as in DFNX7; requires 2 nucleotide substitutions, features a modification of the amino acid from A to N at position 573.
+The protein's natural variant, known as in EHMTO; loss of methanethiol oxidation in patient cells;, features a modification of the amino acid from G to W at position 225.
+The protein's natural variant, known as in EHMTO; loss of methanethiol oxidation in patient cells;, features a modification of the amino acid from H to Y at position 329.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from Q to E at position 227.
+The protein's natural variant, known as in FANCE; uncertain pathological significance, features a modification of the amino acid from P to Q at position 184.
+The protein's natural variant, known as in DEE27; unknown pathological significance;, features a modification of the amino acid from V to M at position 15.
+The protein's natural variant, known as found in a patient with schizophrenia; unknown pathological significance, features a modification of the amino acid from I to N at position 50.
+The protein's natural variant, known as found in a patient with schizophrenia; unknown pathological significance, features a modification of the amino acid from L to M at position 362.
+The natural variant of this protein is characterized by an amino acid alteration from S to N at position 407.
+The protein's natural variant, known as in MRD6; decreased protein abundance; decreased localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by decreased glutamate potency;, features a modification of the amino acid from E to G at position 413.
+The protein's natural variant, known as in MRD6; decreased protein abundance; decreased localization to the cell membrane;, features a modification of the amino acid from C to R at position 436.
+The protein's natural variant, known as in MRD6; decreased protein abundance; decreased localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by increased glutamate and glycine potency and increased open probability;, features a modification of the amino acid from C to Y at position 456.
+The protein's natural variant, known as in MRD6; decreased protein abundance; decreased localization to the cell membrane; decreased glutamate-gated calcium ion channel activity characterized by decreased glutamate potency and increased glycine potency;, features a modification of the amino acid from C to F at position 461.
+The protein's natural variant, known as in DEE27; decreased protein abundance; decreased localization to the cell membrane; increased glutamate-gated calcium ion channel activity via an allosteric effect which is characterized by increased glutamate and glycine potency and increased open probability; the mutant channel is less sensitive to magnesium inhibition and has increased calcium permeability compared to wild-type;, features a modification of the amino acid from R to H at position 540.
+The protein's natural variant, known as in MRD6; no effect on localization to the cell membrane; loss of glutamate-gated calcium ion channel activity;, features a modification of the amino acid from P to L at position 553.
+The protein's natural variant, known as in DEE27; severe phenotype with early onset seizures; gain of function mutation; results in neuronal hyperexcitability; the mutant channel is not inhibited by magnesium and has increased calcium permeability compared to wild-type;, features a modification of the amino acid from N to I at position 615.
+The protein's natural variant, known as in DEE27; severe phenotype with early onset seizures; gain of function mutation; results in neuronal hyperexcitability; the mutant channel is not inhibited by magnesium and has increased calcium permeability compared to wild-type;, features a modification of the amino acid from V to G at position 618.
+The protein's natural variant, known as in MRD6; decreased protein abundance; no effect on localization to the cell membrane; no significant effect on calcium ion transmembrane import into cytosol; analysis of agonist dose-response curves for glutamate and glycine are not consistent;, features a modification of the amino acid from R to C at position 682.
+The protein's natural variant, known as in MRD6; decreased protein abundance; decreased localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by increased glutamate and glycine potency;, features a modification of the amino acid from R to H at position 696.
+The protein's natural variant, known as in MRD6;, features a modification of the amino acid from G to E at position 820.
+The protein's natural variant, known as probable disease-associated variant found in a patient with autism spectrum disorder;, features a modification of the amino acid from L to V at position 825.
+The protein's natural variant, known as found in a patient with schizophrenia; unknown pathological significance, features a modification of the amino acid from Q to R at position 1014.
+The natural variant of this protein is characterized by an amino acid alteration from M to R at position 1342.
+The protein's natural variant, known as found in a patient with autism spectrum disorder; unknown pathological significance;, features a modification of the amino acid from S to L at position 1415.
+The protein's natural variant, known as found in a patient with Landau-Kleffner syndrome; unknown pathological significance;, features a modification of the amino acid from P to A at position 1439.
+The protein's natural variant, known as found in a patient with schizophrenia; unknown pathological significance;, features a modification of the amino acid from S to F at position 1452.
+The protein's natural variant, known as in OOMD5; decreased WEE2 phosphorylation at serine residues; decreased CDK1/CDC2 phosphorylation at 'Y-15';, features a modification of the amino acid from D to H at position 234.
+The protein's natural variant, known as in a gastric adenocarcinoma sample; somatic mutation, features a modification of the amino acid from N to K at position 332.
+The protein's natural variant, known as in an ovarian mucinous carcinoma sample; somatic mutation;, features a modification of the amino acid from R to H at position 398.
+The protein's natural variant, known as in HCP;, features a modification of the amino acid from V to A at position 135.
+The protein's natural variant, known as in HCP; <5% of activity;, features a modification of the amino acid from G to S at position 189.
+The protein's natural variant, known as in HCP, features a modification of the amino acid from G to W at position 197.
+The protein's natural variant, known as in HCP;, features a modification of the amino acid from E to K at position 201.
+The protein's natural variant, known as in HCP;, features a modification of the amino acid from S to F at position 208.
+The protein's natural variant, known as in HCP, features a modification of the amino acid from L to R at position 214.
+The protein's natural variant, known as in HCP, features a modification of the amino acid from P to R at position 249.
+The protein's natural variant, known as in HCP, features a modification of the amino acid from P to S at position 249.
+The protein's natural variant, known as in HCP; a patient carrying also the L-12 mutation in ALAD;, features a modification of the amino acid from G to R at position 279.
+The protein's natural variant, known as in HCP, features a modification of the amino acid from G to R at position 280.
+The protein's natural variant, known as in HCP;, features a modification of the amino acid from H to D at position 295.
+The protein's natural variant, known as in HARPO;, features a modification of the amino acid from H to R at position 327.
+The protein's natural variant, known as in HCP;, features a modification of the amino acid from R to C at position 328.
+The protein's natural variant, known as in HCP;, features a modification of the amino acid from R to W at position 331.
+The protein's natural variant, known as in HARPO;, features a modification of the amino acid from K to E at position 404.
+The protein's natural variant, known as in HCP, features a modification of the amino acid from W to R at position 427.
+The protein's natural variant, known as in HCP;, features a modification of the amino acid from R to C at position 447.
+The protein's natural variant, known as in POADS;, features a modification of the amino acid from G to E at position 19.
+The protein's natural variant, known as in POADS;, features a modification of the amino acid from R to C at position 135.
+The protein's natural variant, known as in POADS;, features a modification of the amino acid from G to R at position 152.
+The protein's natural variant, known as in POADS;, features a modification of the amino acid from R to C at position 199.
+The protein's natural variant, known as in POADS;, features a modification of the amino acid from G to A at position 202.
+The protein's natural variant, known as in POADS;, features a modification of the amino acid from G to D at position 202.
+The protein's natural variant, known as in POADS;, features a modification of the amino acid from R to W at position 244.
+The protein's natural variant, known as in POADS, features a modification of the amino acid from T to I at position 284.
+The protein's natural variant, known as in POADS;, features a modification of the amino acid from R to W at position 346.
+The protein's natural variant, known as in POADS;, features a modification of the amino acid from D to G at position 392.
+The protein's natural variant, known as found in a patient with atrioventricular canal-cleft mitral valve; unknown pathological significance;, features a modification of the amino acid from R to H at position 68.
+The protein's natural variant, known as in TOF;, features a modification of the amino acid from G to D at position 162.
+The protein's natural variant, known as in a patient with Rastelli type atrioventricular canal, features a modification of the amino acid from G to S at position 262.
+The protein's natural variant, known as in CTHM; double-outlet right ventricle;, features a modification of the amino acid from C to Y at position 267.
+The protein's natural variant, known as in TOF;, features a modification of the amino acid from S to P at position 309.
+The protein's natural variant, known as in TOF, features a modification of the amino acid from P to T at position 312.
+The protein's natural variant, known as in CHTD6;, features a modification of the amino acid from A to T at position 318.
+The protein's natural variant, known as in CHTD6;, features a modification of the amino acid from M to T at position 364.
+The natural variant of this protein is characterized by an amino acid alteration from L to V at position 9.
+The natural variant of this protein is characterized by an amino acid alteration from E to K at position 29.
+The natural variant of this protein is characterized by an amino acid alteration from G to E at position 43.
+The natural variant of this protein is characterized by an amino acid alteration from T to R at position 71.
+The natural variant of this protein is characterized by an amino acid alteration from E to K at position 78.
+The natural variant of this protein is characterized by an amino acid alteration from E to L at position 78.
+The natural variant of this protein is characterized by an amino acid alteration from S to G at position 89.
+The natural variant of this protein is characterized by an amino acid alteration from G to E at position 102.
+The natural variant of this protein is characterized by an amino acid alteration from Q to P at position 105.
+The natural variant of this protein is characterized by an amino acid alteration from F to V at position 111.
+The protein's natural variant, known as in LS; decrease in succinate dehydrogenase activity, features a modification of the amino acid from C to G at position 189.
+The protein's natural variant, known as in NDAXOA;, features a modification of the amino acid from R to C at position 451.
+The protein's natural variant, known as in MC2DN1; unknown pathological significance;, features a modification of the amino acid from S to L at position 509.
+The protein's natural variant, known as in LS;, features a modification of the amino acid from A to V at position 524.
+The protein's natural variant, known as in LS;, features a modification of the amino acid from R to W at position 554.
+The protein's natural variant, known as in MC2DN1 and CMD1GG;, features a modification of the amino acid from G to E at position 555.
+The protein's natural variant, known as in PGL5; loss of activity;, features a modification of the amino acid from R to W at position 589.
+The protein's natural variant, known as in HH19;, features a modification of the amino acid from F to I at position 77.
+The protein's natural variant, known as in HH19; rare variant associated with susceptibility to disease; the patient carries a second mutation in the HH-associated gene FGFR1;, features a modification of the amino acid from S to F at position 182.
+The protein's natural variant, known as in HH19;, features a modification of the amino acid from N to S at position 189.
+The protein's natural variant, known as in HH19; rare variant associated with susceptibility to disease; the patient carries a second variant in the HH-associated gene SPRY4;, features a modification of the amino acid from T to M at position 346.
+The protein's natural variant, known as in CSGD; reduced glutamine synthetase activity;, features a modification of the amino acid from R to C at position 324.
+The protein's natural variant, known as in CSGD; suggests reduced glutamine synthetase activity;, features a modification of the amino acid from R to C at position 341.
+The natural variant of this protein is characterized by an amino acid alteration from K to M at position 313.
+The protein's natural variant, known as in allele A, features a modification of the amino acid from E to G at position 34.
+The protein's natural variant, known as in allele A, features a modification of the amino acid from L to LV at position 140.
+The protein's natural variant, known as in allele A;, features a modification of the amino acid from V to I at position 189.
+The protein's natural variant, known as in allele B;, features a modification of the amino acid from N to S at position 409.
+The protein's natural variant, known as in URCTU; changed N-glycosylation; increased protein degradation; affects urinary excretion of uridine and cytidine;, features a modification of the amino acid from R to C at position 510.
+The protein's natural variant, known as in alleles B and C;, features a modification of the amino acid from D to N at position 521.
+The protein's natural variant, known as in URCTU; no effect on localization to the cell membrane; loss of pyrimidine- and adenosine-specific:sodium symporter activity; affects urinary excretion of uridine and cytidine;, features a modification of the amino acid from S to P at position 546.
+The protein's natural variant, known as in URCTU; changed N-glycosylation; increased protein degradation; affects urinary excretion of uridine and cytidine, features a modification of the amino acid from R to Q at position 561.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from Q to E at position 151.
+The protein's natural variant, known as in EDSMC2; shows a loss of epimerase activity towards partially desulfated dermatan sulfate; patient-derived fibroblasts show also a significant reduction in activity;, features a modification of the amino acid from S to L at position 268.
+The protein's natural variant, known as in strain: NIHSwiss, features a modification of the amino acid from D to G at position 131.
+The protein's natural variant, known as in SCAX1; the mutant protein is expressed at the plasma membrane, but shows impaired extrusion of intracellular calcium, features a modification of the amino acid from R to H at position 482.
+The protein's natural variant, known as in SCAX1; the mutant protein is expressed at the plasma membrane but shows impaired extrusion of intracellular calcium with prolonged retention of cytoplasmic calcium compared to wild-type under physiologic conditions;, features a modification of the amino acid from G to D at position 1107.
+The protein's natural variant, known as in strain: 8107, features a modification of the amino acid from ANDPSK to GA at position 85.
+The protein's natural variant, known as in strain: OE1-1, features a modification of the amino acid from L to P at position 173.
+The protein's natural variant, known as in strain: 8107 and OE1-1, features a modification of the amino acid from G to A at position 177.
+The protein's natural variant, known as in strain: OE1-1, features a modification of the amino acid from N to I at position 229.
+The protein's natural variant, known as in strain: 8107, features a modification of the amino acid from G to A at position 269.
+The protein's natural variant, known as in strain: OE1-1, features a modification of the amino acid from G to D at position 305.
+The protein's natural variant, known as in strain: OE1-1, features a modification of the amino acid from A to E at position 329.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from A to V at position 1201.
+The protein's natural variant, known as in strain: Raleigh Inbred 6, Raleigh Inbred 9, Raleigh Inbred 11, Raleigh Inbred 27 and Raleigh Inbred 33, features a modification of the amino acid from A to T at position 58.
+The protein's natural variant, known as in strain: Raleigh Inbred 6, Raleigh Inbred 9, Raleigh Inbred 11, Raleigh Inbred 27 and Raleigh Inbred 33, features a modification of the amino acid from A to P at position 61.
+The protein's natural variant, known as in strain: Raleigh Inbred 11, features a modification of the amino acid from A to V at position 77.
+The protein's natural variant, known as in strain: Raleigh Inbred 6, Raleigh Inbred 9, Raleigh Inbred 11 and Raleigh Inbred 33, features a modification of the amino acid from N to S at position 84.
+The natural variant of this protein is characterized by an amino acid alteration from E to K at position 293.
+The protein's natural variant, known as found in a patient with mild intellectual disability and eye movement disorder; unknown pathological significance;, features a modification of the amino acid from W to G at position 65.
+The protein's natural variant, known as found in a patient with mild intellectual disability and eye movement disorder; unknown pathological significance;, features a modification of the amino acid from G to E at position 345.
+The natural variant of this protein is characterized by an amino acid alteration from S to G at position 31.
+The natural variant of this protein is characterized by an amino acid alteration from H to Y at position 119.
+The natural variant of this protein is characterized by an amino acid alteration from K to N at position 126.
+The protein's natural variant, known as confers acriflavine-resistance, features a modification of the amino acid from N to K at position 303.
+The protein's natural variant, known as in EBS, features a modification of the amino acid from E to K at position 478.
+The protein's natural variant, known as in CPHD2; familial; no detectable DNA binding observed with the mutant protein in electromobility shift assays; whereas in vitro translated PROP1 and the mutant proteins were similar in their expression and electrophoretic properties;, features a modification of the amino acid from R to C at position 73.
+The protein's natural variant, known as in CPHD2; familial;, features a modification of the amino acid from R to H at position 73.
+The protein's natural variant, known as in CPHD2; impairs binding of the mutated protein to DNA target sequences;, features a modification of the amino acid from F to S at position 88.
+The protein's natural variant, known as in CPHD2; displays a significant decrease in DNA binding on a paired-box response element (PRDQ9) and trans-activation of a luciferase reporter gene;, features a modification of the amino acid from R to Q at position 99.
+The protein's natural variant, known as in CPHD2; familial;, features a modification of the amino acid from F to I at position 117.
+The protein's natural variant, known as in CPHD2; familial;, features a modification of the amino acid from R to C at position 120.
+The protein's natural variant, known as in CPHD2;, features a modification of the amino acid from R to W at position 125.
+The protein's natural variant, known as in strain: PI 161375, allele nsv, features a modification of the amino acid from H to L at position 228.
+The protein's natural variant, known as in D2HGA1; unknown pathological significance; significant loss of catalytic activity;, features a modification of the amino acid from S to W at position 109.
+The protein's natural variant, known as in D2HGA1; unknown pathological significance; complete loss of catalytic activity;, features a modification of the amino acid from N to K at position 127.
+The protein's natural variant, known as in D2HGA1; unknown pathological significance; complete loss of catalytic activity, features a modification of the amino acid from G to V at position 131.
+The protein's natural variant, known as in D2HGA1; severe phenotype; unknown pathological significance; almost complete loss of catalytic activity;, features a modification of the amino acid from I to S at position 147.
+The protein's natural variant, known as in D2HGA1; unknown pathological significance; significant loss of catalytic activity, features a modification of the amino acid from M to T at position 153.
+The protein's natural variant, known as in D2HGA1; unknown pathological significance; significant loss of catalytic activity;, features a modification of the amino acid from M to V at position 153.
+The protein's natural variant, known as in D2HGA1; unknown pathological significance; moderate reduction in catalytic activity;, features a modification of the amino acid from C to Y at position 172.
+The protein's natural variant, known as in D2HGA1; unknown pathological significance; almost complete loss of catalytic activity;, features a modification of the amino acid from P to L at position 189.
+The protein's natural variant, known as in D2HGA1; unknown pathological significance; almost complete loss of catalytic activity;, features a modification of the amino acid from A to V at position 205.
+The protein's natural variant, known as in D2HGA1; unknown pathological significance; significant loss of catalytic activity, features a modification of the amino acid from A to V at position 231.
+The protein's natural variant, known as in D2HGA1; unknown pathological significance; no effect on catalytic activity;, features a modification of the amino acid from G to S at position 233.
+The protein's natural variant, known as in D2HGA1; unknown pathological significance; moderate reduction in catalytic activity;, features a modification of the amino acid from D to Y at position 375.
+The protein's natural variant, known as in D2HGA1; unknown pathological significance; moderate reduction in catalytic activity;, features a modification of the amino acid from V to M at position 399.
+The protein's natural variant, known as in D2HGA1; unknown pathological significance; moderate reduction in catalytic activity;, features a modification of the amino acid from R to H at position 419.
+The protein's natural variant, known as in D2HGA1; unknown pathological significance; no effect on catalytic activity;, features a modification of the amino acid from A to T at position 426.
+The protein's natural variant, known as slight reduction in catalytic activity, features a modification of the amino acid from G to V at position 436.
+The protein's natural variant, known as in D2HGA1; mild phenotype; unknown pathological significance; moderate reduction in catalytic activity;, features a modification of the amino acid from N to D at position 439.
+The protein's natural variant, known as in D2HGA1; severe phenotype; unknown pathological significance; significant reduction in catalytic activity;, features a modification of the amino acid from V to A at position 444.
+The protein's natural variant, known as in D2HGA1; unknown pathological significance; moderate reduction in catalytic activity;, features a modification of the amino acid from A to V at position 446.
+The protein's natural variant, known as in D2HGA1; unknown pathological significance; almost complete loss of catalytic activity;, features a modification of the amino acid from G to R at position 477.
+The natural variant of this protein is characterized by an amino acid alteration from C to CS at position 337.
+The natural variant of this protein is characterized by an amino acid alteration from AHMPC to VHMPY at position 373.
+The protein's natural variant, known as streptomycin resistant. Also confers streptomycin independence on streptomycin-dependent S12 mutant P91D, features a modification of the amino acid from Q to L at position 54.
+The protein's natural variant, known as confers streptomycin independence on streptomycin-dependent S12 mutant P90R. ARAM mutant, features a modification of the amino acid from Q to P at position 54.
+The protein's natural variant, known as confers streptomycin independence on streptomycin-dependent S12 mutant P91D. ARAM mutant, features a modification of the amino acid from I to N at position 200.
+The protein's natural variant, known as in JB221; fast-growing suppressor of streptomycin resistant mutant S12 K42N. ARAM mutant, features a modification of the amino acid from K to N at position 206.
+The protein's natural variant, known as confers streptomycin independence on streptomycin-dependent S12 mutant P90R. ARAM mutant, features a modification of the amino acid from K to T at position 206.
+The protein's natural variant, known as in MOCODB; in a patient with mild form of the disease; impairs interaction with MOCS2B;, features a modification of the amino acid from V to F at position 7.
+The protein's natural variant, known as found in a patient with a neurodevelopmental disorder; unknown pathological significance;, features a modification of the amino acid from W to C at position 8.
+The protein's natural variant, known as in Munster-3C;, features a modification of the amino acid from P to H at position 27.
+The protein's natural variant, known as in Munster-3B;, features a modification of the amino acid from P to R at position 28.
+The protein's natural variant, known as in Baltimore;, features a modification of the amino acid from R to L at position 34.
+The protein's natural variant, known as in AMYL8; also found in a family with amyloid polyneuropathy-nephropathy Iowa;, features a modification of the amino acid from G to R at position 50.
+The protein's natural variant, known as in AMYL8;, features a modification of the amino acid from L to R at position 84.
+The protein's natural variant, known as confirmed at protein level;, features a modification of the amino acid from T to I at position 92.
+The protein's natural variant, known as in Hita, features a modification of the amino acid from A to D at position 119.
+The protein's natural variant, known as in Munster-3A;, features a modification of the amino acid from D to N at position 127.
+The protein's natural variant, known as in Tsushima, features a modification of the amino acid from W to R at position 132.
+The protein's natural variant, known as in Fukuoka, features a modification of the amino acid from E to K at position 134.
+The protein's natural variant, known as in Norway;, features a modification of the amino acid from E to K at position 160.
+The protein's natural variant, known as in Giessen;, features a modification of the amino acid from P to R at position 167.
+The protein's natural variant, known as in Zaragoza, features a modification of the amino acid from L to R at position 168.
+The protein's natural variant, known as in AMYL8; unknown pathological significance, features a modification of the amino acid from R to P at position 173.
+The protein's natural variant, known as in Boston; no evidence of association with premature coronary heart disease; associated with decreased levels of HDL cholesterol; associated with decreased serum cellular cholesterol efflux; associated with decreased lecithin-cholesterol acyltransferase (LCAT) activity, features a modification of the amino acid from R to S at position 173.
+The protein's natural variant, known as in Oita; 60% of normal apoA-I and normal HDL cholesterol levels; rapidly cleared from plasma;, features a modification of the amino acid from V to E at position 180.
+The protein's natural variant, known as in Milano; no evidence of association with premature vascular disease; associated with decreased HDL levels and moderate increase in triglycerides; allows the formation of disulfide-linked homodimers via the introduced cysteine; assembles properly in HDL; alters protein structure; has no tendency to form fibrils and aggregates;, features a modification of the amino acid from R to C at position 197.
+The protein's natural variant, known as in AMYL8; plasma level of HDL and apoA-I protein were significantly lower in the patient, features a modification of the amino acid from L to S at position 198.
+The protein's natural variant, known as in AMYL8; unknown pathological significance, features a modification of the amino acid from A to P at position 199.
+The protein's natural variant, known as in Munster-4;, features a modification of the amino acid from E to K at position 222.
+The protein's natural variant, known as in a lung carcinoma sample; somatic mutation; shows greater kinase activity, provides a cell growth advantage and increases its interaction with the PML tumor suppressor protein and PML degradation;, features a modification of the amino acid from I to T at position 133.
+The protein's natural variant, known as in IMD31C; gain of function mutation associated with increased STAT1 phosphorylation due to impaired nuclear dephosphorylation;, features a modification of the amino acid from D to G at position 165.
+The protein's natural variant, known as in IMD31C;, features a modification of the amino acid from D to H at position 165.
+The protein's natural variant, known as in IMD31C;, features a modification of the amino acid from Y to N at position 170.
+The protein's natural variant, known as in IMD31C;, features a modification of the amino acid from C to R at position 174.
+The protein's natural variant, known as in IMD31C; gain of function; increases transactivation activity in response to IFNG;, features a modification of the amino acid from N to K at position 179.
+The protein's natural variant, known as in IMD31B; not deleterious in terms of most STAT1 functions; causes abnormal splicing out of exon 8 from most mRNAs thereby decreasing protein levels by approximately 70%;, features a modification of the amino acid from K to N at position 201.
+The protein's natural variant, known as in IMD31C, features a modification of the amino acid from M to I at position 202.
+The protein's natural variant, known as in IMD31C;, features a modification of the amino acid from M to V at position 202.
+The protein's natural variant, known as in IMD31C;, features a modification of the amino acid from A to V at position 267.
+The protein's natural variant, known as in IMD31C;, features a modification of the amino acid from Q to P at position 271.
+The protein's natural variant, known as in IMD31C; gain of function; increases STAT1 phosphorylation due to impaired nuclear dephosphorylation; increases transactivation activity in response to IFNG;, features a modification of the amino acid from R to Q at position 274.
+The protein's natural variant, known as in IMD31C; gain of function; increases phosphorylation in response to IFNG, IFNA and IL27 due to a loss of dephosphorylation;, features a modification of the amino acid from R to W at position 274.
+The protein's natural variant, known as in IMD31C; gain of function; increases phosphorylation in response to IFNG and IFNA due to a loss of dephosphorylation;, features a modification of the amino acid from K to E at position 278.
+The protein's natural variant, known as in IMD31C; gain of function; increases transactivation activity in response to IFNG;, features a modification of the amino acid from Q to R at position 285.
+The protein's natural variant, known as in IMD31C;, features a modification of the amino acid from K to I at position 286.
+The protein's natural variant, known as in IMD31C;, features a modification of the amino acid from T to A at position 288.
+The protein's natural variant, known as in IMD31C; gain of function; increases basal STAT1 phosphorylation levels which are 10-20 fold higher than controls after IFNG stimulation, features a modification of the amino acid from K to N at position 298.
+The protein's natural variant, known as in IMD31A; affects the DNA-binding activity of the protein;, features a modification of the amino acid from E to Q at position 320.
+The protein's natural variant, known as in IMD31C; gain of function; increases phosphorylation in response to IFNG and IFNA due to a loss of dephosphorylation;, features a modification of the amino acid from G to D at position 384.
+The protein's natural variant, known as in IMD31C; gain of function; increases phosphorylation in response to IFNG, IFNA and IL27 due to a loss of dephosphorylation;, features a modification of the amino acid from T to M at position 385.
+The protein's natural variant, known as in IMD31A; affects the DNA-binding activity of the protein;, features a modification of the amino acid from Q to H at position 463.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from P to A at position 491.
+The protein's natural variant, known as in IMD31B; found in an infant who died of a viral-like illness associated with complete STAT1 deficiency;, features a modification of the amino acid from L to P at position 600.
+The protein's natural variant, known as in IMD31A; affects both phosphorylation and DNA-binding activity; results in impaired STAT1-mediated cellular response to IFN-gamma and interleukin-27;, features a modification of the amino acid from K to E at position 637.
+The protein's natural variant, known as in IMD31A; impairs tyrosine phosphorylation; results in impaired STAT1-mediated cellular response to IFN-gamma and interleukin-27;, features a modification of the amino acid from K to R at position 673.
+The protein's natural variant, known as in IMD31B; disrupts transactivation activity in response to IFNG, features a modification of the amino acid from Y to C at position 701.
+The protein's natural variant, known as in IMD31A; loss of GAF and ISGF3 activation; impairs the nuclear accumulation of GAF but not of ISGF3 in heterozygous cells stimulated by IFNs; affects phosphorylation of the protein;, features a modification of the amino acid from L to S at position 706.
+The natural variant of this protein is characterized by an amino acid alteration from L to P at position 153.
+The protein's natural variant, known as in MOPC 104E, features a modification of the amino acid from S to N at position 77.
+The protein's natural variant, known as in MOPC 104E, features a modification of the amino acid from H to Q at position 100.
+The protein's natural variant, known as in TEPC183 and MOPC 104E, features a modification of the amino acid from T to N at position 225.
+The protein's natural variant, known as in TEPC183, features a modification of the amino acid from N to S at position 257.
+The protein's natural variant, known as in MOPC 104E, features a modification of the amino acid from N to T at position 257.
+The protein's natural variant, known as in TEPC183 and MOPC 104E; requires 2 nucleotide substitutions, features a modification of the amino acid from L to K at position 367.
+The natural variant of this protein is characterized by an amino acid alteration from A to G at position 126.
+The protein's natural variant, known as in strain: IS58, features a modification of the amino acid from S to H at position 2.
+The protein's natural variant, known as in strain: IS58, features a modification of the amino acid from K to T at position 5.
+The protein's natural variant, known as in CMT2FF; results in misfolding due to the creation of a non-native disulfide bond with C-152, features a modification of the amino acid from Y to C at position 138.
+The protein's natural variant, known as in MGORS2;, features a modification of the amino acid from Y to C at position 174.
+The protein's natural variant, known as in MDHLO; unknown pathological significance; shows no change in farnesyltranstransferase activity, features a modification of the amino acid from P to S at position 15.
+The protein's natural variant, known as in MDHLO; shows slightly decreased farnesyltranstransferase activity, features a modification of the amino acid from F to C at position 257.
+The protein's natural variant, known as in MDHLO; shows slightly decreased farnesyltranstransferase activity, features a modification of the amino acid from Y to C at position 259.
+The protein's natural variant, known as in MDHLO; shows slightly decreased farnesyltranstransferase activity, features a modification of the amino acid from R to G at position 261.
+The protein's natural variant, known as in MDHLO; shows slightly decreased farnesyltranstransferase activity, features a modification of the amino acid from R to H at position 261.
+The protein's natural variant, known as may be associated with an increase in number of vertebrae in European domestic breds, features a modification of the amino acid from P to L at position 192.
+The protein's natural variant, known as in strain: Italicus /IFO 0253, features a modification of the amino acid from Y to YKREADAEAWHWLQLKPGQPMY at position 165.
+The protein's natural variant, known as in PITA2;, features a modification of the amino acid from E to D at position 308.
+The natural variant of this protein is characterized by an amino acid alteration from P to S at position 345.
+The protein's natural variant, known as in strain: NTHI 289 and UC1, features a modification of the amino acid from Q to E at position 102.
+The protein's natural variant, known as in strain: UC1, features a modification of the amino acid from D to N at position 146.
+The protein's natural variant, known as in strain: NTHI 289 and UC10, features a modification of the amino acid from K to R at position 157.
+The protein's natural variant, known as in strain: NTHI 289, UC1 and UC2, features a modification of the amino acid from I to V at position 170.
+The protein's natural variant, known as in DFNX2;, features a modification of the amino acid from A to V at position 312.
+The protein's natural variant, known as in DFNX2;, features a modification of the amino acid from L to W at position 317.
+The protein's natural variant, known as in DFNX2; somatic mosaicism in 50% of the peripheral blood lymphocytes;, features a modification of the amino acid from R to G at position 323.
+The protein's natural variant, known as in DFNX2;, features a modification of the amino acid from R to S at position 330.
+The protein's natural variant, known as in DFNX2;, features a modification of the amino acid from K to E at position 334.
+The natural variant of this protein is characterized by an amino acid alteration from E to K at position 360.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from T to A at position 483.
+The protein's natural variant, known as in NECFM;, features a modification of the amino acid from R to W at position 298.
+The protein's natural variant, known as in strain: ZBMEL384, features a modification of the amino acid from V to G at position 14.
+The protein's natural variant, known as in strain: MEL14 and ZBMEL384, features a modification of the amino acid from I to M at position 30.
+The protein's natural variant, known as in strain: ZBMEL82, ZBMEL95, ZBMEL131, ZBMEL145, ZBMEL157, ZBMEL229, ZBMEL377 and ZBMEL398, features a modification of the amino acid from A to S at position 118.
+The protein's natural variant, known as in strain: ZBMEL82, ZBMEL95, ZBMEL131, ZBMEL145, ZBMEL157, ZBMEL229, ZBMEL377 and ZBMEL398, features a modification of the amino acid from M to L at position 125.
+The protein's natural variant, known as in strain: MEL14, ZBMEL82, ZBMEL95, ZBMEL131, ZBMEL145, ZBMEL157, ZBMEL229, ZBMEL377 and ZBMEL398, features a modification of the amino acid from Y to F at position 138.
+The protein's natural variant, known as in strain: MEL20, features a modification of the amino acid from N to K at position 152.
+The protein's natural variant, known as in strain: MEL11 and MEL13, features a modification of the amino acid from D to N at position 163.
+The protein's natural variant, known as in strain: MEL14, ZBMEL82, ZBMEL131, ZBMEL145, ZBMEL157, ZBMEL229, ZBMEL377, ZBMEL384 and ZBMEL398, features a modification of the amino acid from S to N at position 226.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from H to Y at position 830.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to W at position 835.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to C at position 856.
+The protein's natural variant, known as in NEDSCAC; unknown pathological significance;, features a modification of the amino acid from V to G at position 63.
+The protein's natural variant, known as in NEDSCAC; unknown pathological significance;, features a modification of the amino acid from S to F at position 232.
+The protein's natural variant, known as in NEDSCAC; unknown pathological significance;, features a modification of the amino acid from V to A at position 242.
+The protein's natural variant, known as in NEDSCAC; unknown pathological significance, features a modification of the amino acid from P to L at position 259.
+The protein's natural variant, known as in NEDSCAC; unknown pathological significance;, features a modification of the amino acid from P to L at position 280.
+The protein's natural variant, known as in NEDSCAC; unknown pathological significance;, features a modification of the amino acid from G to S at position 291.
+The protein's natural variant, known as in NEDSCAC; unknown pathological significance;, features a modification of the amino acid from P to L at position 293.
+The protein's natural variant, known as in patients with gastrointestinal diffuse large cell lymphoma;, features a modification of the amino acid from R to W at position 263.
+The protein's natural variant, known as in patients with gastrointestinal diffuse large cell lymphoma; somatic mutation;, features a modification of the amino acid from T to M at position 286.
+The protein's natural variant, known as in patients with gastrointestinal diffuse large cell lymphoma;, features a modification of the amino acid from I to T at position 374.
+The protein's natural variant, known as in patients with gastrointestinal diffuse large cell lymphoma; somatic mutation; loss of inhibitory activity on CARD11- and TNF-induced NF-kappa-B activation, features a modification of the amino acid from E to K at position 476.
+The protein's natural variant, known as in 30% hemoglobin I and in hemoglobin II, features a modification of the amino acid from E to D at position 31.
+The protein's natural variant, known as in hemoglobin II, features a modification of the amino acid from R to Q at position 86.
+The protein's natural variant, known as in some hemoglobin I and in hemoglobin II, features a modification of the amino acid from A to V at position 151.
+The protein's natural variant, known as in JBTS5 and SLSN6;, features a modification of the amino acid from W to C at position 7.
+The protein's natural variant, known as in JBTS5;, features a modification of the amino acid from E to K at position 534.
+The protein's natural variant, known as in MKS4; unknown pathological significance, features a modification of the amino acid from Q to L at position 819.
+The protein's natural variant, known as in LCA10; unknown pathological significance, features a modification of the amino acid from A to P at position 1566.
+The protein's natural variant, known as in MKS4; unknown pathological significance, features a modification of the amino acid from T to M at position 1602.
+The protein's natural variant, known as in LCA10; unknown pathological significance, features a modification of the amino acid from L to P at position 1694.
+The protein's natural variant, known as in JBTS5; benign variant;, features a modification of the amino acid from I to T at position 2134.
+The protein's natural variant, known as in LCA10; unknown pathological significance;, features a modification of the amino acid from S to G at position 2263.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation, features a modification of the amino acid from T to S at position 79.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation, features a modification of the amino acid from C to R at position 228.
+The protein's natural variant, known as in KERSEB, BLC, keratinocytic non-epidermolytic nevus and TD1; severe and lethal; also found as somatic mutation in one patient with multiple myeloma; constitutive dimerization and kinase activation;, features a modification of the amino acid from R to C at position 248.
+The protein's natural variant, known as in KERSEB, BLC, cervical cancer and TD1;, features a modification of the amino acid from S to C at position 249.
+The protein's natural variant, known as in MNKS; also some individuals with autosomal dominant congenital sensorineural deafness without craniosynostosis;, features a modification of the amino acid from P to R at position 250.
+The protein's natural variant, known as in colorectal cancer;, features a modification of the amino acid from E to K at position 322.
+The natural variant of this protein is characterized by an amino acid alteration from T to M at position 338.
+The protein's natural variant, known as in KERSEB, BLC, keratinocytic non-epidermolytic nevus and TD1;, features a modification of the amino acid from G to C at position 370.
+The protein's natural variant, known as in KERSEB and TD1;, features a modification of the amino acid from S to C at position 371.
+The protein's natural variant, known as in KERSEB and TD1; disulfide-linked dimer with constitutive kinase activation;, features a modification of the amino acid from Y to C at position 373.
+The protein's natural variant, known as in ACH;, features a modification of the amino acid from G to C at position 375.
+The protein's natural variant, known as in keratinocytic non-epidermolytic nevus and ACH; very common mutation; constitutively activated kinase with impaired internalization and degradation, resulting in prolonged FGFR3 signaling;, features a modification of the amino acid from G to R at position 380.
+The protein's natural variant, known as in CAN;, features a modification of the amino acid from A to E at position 391.
+The protein's natural variant, known as in LADD2; unknown pathological significance;, features a modification of the amino acid from D to N at position 513.
+The protein's natural variant, known as in hypochondroplasia;, features a modification of the amino acid from I to V at position 538.
+The protein's natural variant, known as in hypochondroplasia;, features a modification of the amino acid from N to K at position 540.
+The protein's natural variant, known as in hypochondroplasia; mild;, features a modification of the amino acid from N to S at position 540.
+The protein's natural variant, known as in hypochondroplasia;, features a modification of the amino acid from N to T at position 540.
+The protein's natural variant, known as in CATSHLS;, features a modification of the amino acid from R to H at position 621.
+The natural variant of this protein is characterized by an amino acid alteration from D to N at position 646.
+The protein's natural variant, known as in KERSEB, TD2, TGCT and BLC; bladder transitional cell carcinoma; somatic mutation; constitutively activated kinase with impaired internalization and degradation, resulting in prolonged FGFR3 signaling;, features a modification of the amino acid from K to E at position 650.
+The protein's natural variant, known as in KERSEB, ACH, TD1 and SADDAN; constitutively activated kinase with impaired internalization and degradation, resulting in prolonged FGFR3 signaling;, features a modification of the amino acid from K to M at position 650.
+The protein's natural variant, known as in hypochondroplasia and BLC; in hypochondroplasia the form is milder than that seen in individuals with the K-540 or M-650 mutations; constitutively activated kinase;, features a modification of the amino acid from K to Q at position 650.
+The protein's natural variant, known as in MCPH21; found in two patients from a consanguineous family; unknown pathological significance, features a modification of the amino acid from F to S at position 8.
+The protein's natural variant, known as in RP;, features a modification of the amino acid from R to Q at position 41.
+The protein's natural variant, known as in CORD2; exhibits reduced DNA binding, transcriptional synergy and interaction with NRL;, features a modification of the amino acid from R to W at position 41.
+The protein's natural variant, known as in LCA7; unknown pathological significance;, features a modification of the amino acid from E to K at position 42.
+The protein's natural variant, known as in CORD2;, features a modification of the amino acid from E to A at position 80.
+The protein's natural variant, known as in LCA7; reduces NRL transactivation and reduces steady state levels of CRX and NRL; altered localization to the cytoplasm, features a modification of the amino acid from K to N at position 88.
+The protein's natural variant, known as in LCA7; reduced DNA-binding ability, transcriptional synergy and interaction with NRL;, features a modification of the amino acid from R to W at position 90.
+The protein's natural variant, known as in RP; unknown pathological significance;, features a modification of the amino acid from R to Q at position 115.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from S to F at position 141.
+The protein's natural variant, known as in CORD2;, features a modification of the amino acid from V to M at position 242.
+The protein's natural variant, known as in allele 2, allele 4, allele 7, allele 8, allele 12 and allele 15, features a modification of the amino acid from M to V at position 6.
+The protein's natural variant, known as in allele 15, features a modification of the amino acid from K to D at position 9.
+The protein's natural variant, known as in allele 1, allele 2, allele 4, allele 7, allele 8, allele 9, allele 10, allele 11, allele 12 and allele 16, features a modification of the amino acid from K to N at position 9.
+The protein's natural variant, known as in allele 1, allele 2, allele 4, allele 7, allele 8, allele 9, allele 10, allele 11, allele 12 and allele 16, features a modification of the amino acid from T to V at position 13.
+The protein's natural variant, known as in allele 4, allele 8, allele 12 and allele 15, features a modification of the amino acid from R to H at position 26.
+The protein's natural variant, known as in allele 10 and allele 15, features a modification of the amino acid from K to E at position 50.
+The protein's natural variant, known as in allele 15, features a modification of the amino acid from A to T at position 53.
+The protein's natural variant, known as in allele 15, features a modification of the amino acid from I to L at position 75.
+The protein's natural variant, known as in allele 15, features a modification of the amino acid from V to G at position 110.
+The protein's natural variant, known as in allele 7, features a modification of the amino acid from V to I at position 110.
+The protein's natural variant, known as in allele 15, features a modification of the amino acid from QI to KK at position 123.
+The protein's natural variant, known as in allele 15, features a modification of the amino acid from K to D at position 127.
+The protein's natural variant, known as in allele 7, allele 8, allele 9, allele 10, allele 11 and allele 14, features a modification of the amino acid from T to S at position 129.
+The protein's natural variant, known as in allele 16, features a modification of the amino acid from R to C at position 139.
+The protein's natural variant, known as in allele 13, features a modification of the amino acid from L to I at position 144.
+The protein's natural variant, known as in allele 5, allele 10, allele 13 and allele 15, features a modification of the amino acid from R to K at position 164.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from E to V at position 49.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from E to K at position 285.
+The protein's natural variant, known as in a family with cystinuria;, features a modification of the amino acid from E to D at position 112.
+The protein's natural variant, known as in DOORS;, features a modification of the amino acid from Q to E at position 20.
+The protein's natural variant, known as in DOORS;, features a modification of the amino acid from R to C at position 40.
+The protein's natural variant, known as in DFNB86;, features a modification of the amino acid from D to Y at position 70.
+The protein's natural variant, known as in DOORS; unknown pathological significance;, features a modification of the amino acid from G to S at position 110.
+The protein's natural variant, known as in DEE16;, features a modification of the amino acid from A to D at position 113.
+The protein's natural variant, known as in FIME; significantly impairs the interaction with ARF6; partially induces neurite overgrowth when overexpressed in primary cortical neurons;, features a modification of the amino acid from D to H at position 147.
+The protein's natural variant, known as in DEE16;, features a modification of the amino acid from L to P at position 159.
+The protein's natural variant, known as in DFNA65;, features a modification of the amino acid from S to L at position 178.
+The protein's natural variant, known as in EPRPDC; unknown pathological significance;, features a modification of the amino acid from T to M at position 182.
+The protein's natural variant, known as in DEE16; loss of function mutation; impairs the interaction with ARF6; overexpression of the mutant protein in primary cortical neurons abolishes the ability to increase neurite length and arborization;, features a modification of the amino acid from F to S at position 229.
+The protein's natural variant, known as in DOORS;, features a modification of the amino acid from R to C at position 242.
+The protein's natural variant, known as in FIME; fails to induce neurite overgrowth when overexpressed in primary cortical neurons;, features a modification of the amino acid from F to L at position 251.
+The protein's natural variant, known as in DFNB86;, features a modification of the amino acid from R to P at position 293.
+The protein's natural variant, known as in DOORS;, features a modification of the amino acid from L to F at position 333.
+The protein's natural variant, known as in EPRPDC;, features a modification of the amino acid from R to H at position 360.
+The protein's natural variant, known as in EPRPDC;, features a modification of the amino acid from A to V at position 500.
+The protein's natural variant, known as in EPRPDC; results in synaptic vesicle trafficking defects when expressed in a heterologous system; does not affect localization to presynapse when expressed in a heterologous system;, features a modification of the amino acid from G to R at position 501.
+The protein's natural variant, known as in EPRPDC; unknown pathological significance;, features a modification of the amino acid from G to R at position 511.
+The protein's natural variant, known as in FIME; does not affect the interaction with ARF6; fails to induce neurite overgrowth when overexpressed in primary cortical neurons;, features a modification of the amino acid from A to V at position 515.
+The protein's natural variant, known as in variant 2, features a modification of the amino acid from V to A at position 40.
+The protein's natural variant, known as in variant 2, features a modification of the amino acid from S to T at position 44.
+The protein's natural variant, known as in variant 2, features a modification of the amino acid from P to L at position 103.
+The protein's natural variant, known as in variant 2, features a modification of the amino acid from K to KKSK at position 140.
+The protein's natural variant, known as in variant 2, features a modification of the amino acid from R to K at position 153.
+The protein's natural variant, known as in gamma induced thymic lymphomas, features a modification of the amino acid from K to T at position 676.
+The protein's natural variant, known as in gamma induced thymic lymphomas, features a modification of the amino acid from R to C at position 783.
+The protein's natural variant, known as in gamma induced thymic lymphomas, features a modification of the amino acid from C to S at position 849.
+The protein's natural variant, known as in allele GLX-2, features a modification of the amino acid from K to T at position 308.
+The protein's natural variant, known as in CPHD7; impairs binding to U12 and U6atac small nuclear RNAs; leads to a partial defect in the folding of RRM 2 domain and reduced stability of the full-length protein;, features a modification of the amino acid from P to T at position 474.
+The protein's natural variant, known as in strain: CWL029 and TW-183, features a modification of the amino acid from V to A at position 423.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from D to H at position 352.
+The protein's natural variant, known as in strain: B3, features a modification of the amino acid from G to E at position 15.
+The protein's natural variant, known as in strain: BBK-1, features a modification of the amino acid from A to T at position 22.
+The protein's natural variant, known as in strain: BBK-1, features a modification of the amino acid from G to A at position 65.
+The protein's natural variant, known as in strain: A13, BBK-1 and B3, features a modification of the amino acid from G to S at position 69.
+The protein's natural variant, known as in strain: A13 and B3, features a modification of the amino acid from D to E at position 195.
+The protein's natural variant, known as in strain: BBK-1, features a modification of the amino acid from E to A at position 216.
+The protein's natural variant, known as likely benign variant; it rescues craniofacial patterning defects in zebrafish morphant embryos;, features a modification of the amino acid from A to V at position 137.
+The protein's natural variant, known as likely benign variant; it rescues craniofacial patterning defects in zebrafish morphant embryos;, features a modification of the amino acid from E to K at position 143.
+The protein's natural variant, known as in MRXSA; unknown pathological significance; does not affect FAM50A protein levels in patient cells; does not affect localization to the nucleus;, features a modification of the amino acid from W to G at position 206.
+The protein's natural variant, known as in MRXSA; hypomorphic variant; does not fully rescue craniofacial patterning defects in zebrafish morphant embryos; does not affect FAM50A protein levels in patient cells; does not affect localization to the nucleus;, features a modification of the amino acid from E to G at position 254.
+The protein's natural variant, known as in MRXSA; hypomorphic variant; does not fully rescue craniofacial patterning defects in zebrafish morphant embryos; does not affect localization to the nucleus;, features a modification of the amino acid from D to G at position 255.
+The protein's natural variant, known as in MRXSA; hypomorphic variant; does not fully rescue craniofacial patterning defects in zebrafish morphant embryos;, features a modification of the amino acid from D to N at position 255.
+The protein's natural variant, known as in MRXSA; hypomorphic variant; does not fully rescue craniofacial patterning defects in zebrafish morphant embryos;, features a modification of the amino acid from R to W at position 273.
+The protein's natural variant, known as significant independent determinant of CIMT; may protect from early atherosclerosis in subject at risk for diabetes; associated with BMI;, features a modification of the amino acid from P to A at position 12.
+The protein's natural variant, known as in obesity;, features a modification of the amino acid from P to Q at position 113.
+The protein's natural variant, known as in colon cancer; sporadic; somatic mutation; loss of ligand-binding;, features a modification of the amino acid from Q to P at position 314.
+The protein's natural variant, known as in colon cancer; sporadic; somatic mutation; partial loss of ligand-binding;, features a modification of the amino acid from R to H at position 316.
+The protein's natural variant, known as in diabetes;, features a modification of the amino acid from V to M at position 318.
+The protein's natural variant, known as in FPLD3;, features a modification of the amino acid from F to L at position 388.
+The protein's natural variant, known as in FPLD3;, features a modification of the amino acid from R to C at position 425.
+The protein's natural variant, known as in diabetes;, features a modification of the amino acid from P to L at position 495.
+The protein's natural variant, known as in CFEOM5; causes loss of stability; causes incorrect folding;, features a modification of the amino acid from G to R at position 382.
+The natural variant of this protein is characterized by an amino acid alteration from P to S at position 64.
+The protein's natural variant, known as in SDS2; unknown pathological significance;, features a modification of the amino acid from M to K at position 882.
+The protein's natural variant, known as in SDS2; unknown pathological significance;, features a modification of the amino acid from R to Q at position 1095.
+The protein's natural variant, known as in strain: MDR25, features a modification of the amino acid from A to V at position 53.
+The protein's natural variant, known as in strain: MDR25, features a modification of the amino acid from A to V at position 164.
+The protein's natural variant, known as in strain: MDR25, features a modification of the amino acid from N to S at position 201.
+The protein's natural variant, known as in JMML; somatic mutation;, features a modification of the amino acid from N to S at position 417.
+The protein's natural variant, known as in strain: N7 AMYEN+, features a modification of the amino acid from AKAPHVFLE to EMRCNTFFQ at position 477.
+The protein's natural variant, known as in some patients with early onset breast cancer, features a modification of the amino acid from D to G at position 30.
+The protein's natural variant, known as in some patients with early onset breast cancer; requires 2 nucleotide substitutions, features a modification of the amino acid from P to W at position 195.
+The protein's natural variant, known as in some patients with early onset breast cancer; requires 2 nucleotide substitutions, features a modification of the amino acid from I to D at position 196.
+The protein's natural variant, known as in some patients with early onset breast cancer, features a modification of the amino acid from H to Y at position 197.
+The protein's natural variant, known as in some patients with early onset breast cancer; requires 2 nucleotide substitutions, features a modification of the amino acid from V to H at position 199.
+The protein's natural variant, known as in some patients with early onset breast cancer;, features a modification of the amino acid from T to A at position 319.
+The protein's natural variant, known as in 30% of the molecules, features a modification of the amino acid from S to G at position 37.
+The protein's natural variant, known as in TSC2; unknown pathological significance;, features a modification of the amino acid from H to R at position 137.
+The protein's natural variant, known as in TSC2;, features a modification of the amino acid from C to Y at position 227.
+The protein's natural variant, known as in TSC2;, features a modification of the amino acid from K to N at position 258.
+The protein's natural variant, known as in TSC2;, features a modification of the amino acid from R to P at position 261.
+The protein's natural variant, known as in TSC2;, features a modification of the amino acid from L to P at position 292.
+The protein's natural variant, known as in TSC2;, features a modification of the amino acid from G to E at position 294.
+The protein's natural variant, known as in TSC2, features a modification of the amino acid from W to WGMALW at position 304.
+The protein's natural variant, known as could be associated with TSC2;, features a modification of the amino acid from L to F at position 320.
+The protein's natural variant, known as in TSC2;, features a modification of the amino acid from N to K at position 331.
+The protein's natural variant, known as in TSC2;, features a modification of the amino acid from L to P at position 361.
+The protein's natural variant, known as in TSC2;, features a modification of the amino acid from Y to D at position 407.
+The protein's natural variant, known as in TSC2;, features a modification of the amino acid from M to I at position 449.
+The protein's natural variant, known as in TSC2;, features a modification of the amino acid from N to I at position 486.
+The protein's natural variant, known as in TSC2;, features a modification of the amino acid from N to S at position 525.
+The protein's natural variant, known as in TSC2; impairs repression of EIF4EBP1 phosphorylation;, features a modification of the amino acid from K to M at position 599.
+The protein's natural variant, known as in TSC2 and LAM; impairs phosphorylation at S-1387, S-1418 and S-1420; enhances ubiquitination by MYCBP2;, features a modification of the amino acid from R to Q at position 611.
+The protein's natural variant, known as in TSC2; impairs phosphorylation at S-1387, S-1418 and S-1420;, features a modification of the amino acid from R to W at position 611.
+The protein's natural variant, known as in TSC2;, features a modification of the amino acid from A to D at position 614.
+The protein's natural variant, known as in TSC2; unknown pathological significance;, features a modification of the amino acid from D to N at position 647.
+The protein's natural variant, known as in TSC2;, features a modification of the amino acid from C to Y at position 696.
+The protein's natural variant, known as in TSC2;, features a modification of the amino acid from L to R at position 717.
+The protein's natural variant, known as in TSC2; unknown pathological significance;, features a modification of the amino acid from V to E at position 769.
+The protein's natural variant, known as in TSC2;, features a modification of the amino acid from P to L at position 816.
+The protein's natural variant, known as in TSC2;, features a modification of the amino acid from L to M at position 826.
+The protein's natural variant, known as in TSC2;, features a modification of the amino acid from M to V at position 895.
+The protein's natural variant, known as in TSC2;, features a modification of the amino acid from R to Q at position 905.
+The protein's natural variant, known as in TSC2;, features a modification of the amino acid from R to W at position 905.
+The protein's natural variant, known as in TSC2; unknown pathological significance;, features a modification of the amino acid from V to M at position 963.
+The protein's natural variant, known as in TSC2;, features a modification of the amino acid from L to P at position 1027.
+The protein's natural variant, known as in TSC2;, features a modification of the amino acid from D to E at position 1084.
+The protein's natural variant, known as in TSC2;, features a modification of the amino acid from V to M at position 1144.
+The protein's natural variant, known as in TSC2;, features a modification of the amino acid from R to W at position 1200.
+The protein's natural variant, known as in TSC2, features a modification of the amino acid from P to L at position 1227.
+The protein's natural variant, known as in TSC2, features a modification of the amino acid from R to W at position 1240.
+The protein's natural variant, known as in TSC2, features a modification of the amino acid from D to V at position 1295.
+The protein's natural variant, known as in TSC2;, features a modification of the amino acid from P to S at position 1315.
+The protein's natural variant, known as in TSC2;, features a modification of the amino acid from P to R at position 1497.
+The protein's natural variant, known as in TSC2;, features a modification of the amino acid from S to N at position 1498.
+The protein's natural variant, known as in FCORD2; somatic mutation; decreased function in negative regulation of TOR signaling; does not affect interaction with TSC1;, features a modification of the amino acid from V to I at position 1547.
+The protein's natural variant, known as in TSC2;, features a modification of the amino acid from Y to C at position 1549.
+The protein's natural variant, known as in TSC2; unknown pathological significance;, features a modification of the amino acid from L to M at position 1594.
+The protein's natural variant, known as in TSC2;, features a modification of the amino acid from H to Y at position 1620.
+The protein's natural variant, known as in TSC2;, features a modification of the amino acid from N to I at position 1643.
+The protein's natural variant, known as in TSC2; Abolishes GAP activity;, features a modification of the amino acid from N to K at position 1643.
+The protein's natural variant, known as in TSC2;, features a modification of the amino acid from Y to C at position 1650.
+The protein's natural variant, known as in TSC2; greatly reduces the ability to enhance the RHEBGTPase activity;, features a modification of the amino acid from N to S at position 1651.
+The protein's natural variant, known as in TSC2;, features a modification of the amino acid from S to F at position 1653.
+The protein's natural variant, known as in TSC2;, features a modification of the amino acid from P to L at position 1675.
+The protein's natural variant, known as in TSC2; Abolishes GAP activity;, features a modification of the amino acid from N to K at position 1681.
+The protein's natural variant, known as in TSC2;, features a modification of the amino acid from D to Y at position 1690.
+The protein's natural variant, known as in TSC2;, features a modification of the amino acid from S to T at position 1704.
+The protein's natural variant, known as in TSC2;, features a modification of the amino acid from P to L at position 1709.
+The protein's natural variant, known as in TSC2, features a modification of the amino acid from A to E at position 1712.
+The protein's natural variant, known as in TSC2; Abolishes GAP activity;, features a modification of the amino acid from R to P at position 1743.
+The protein's natural variant, known as in TSC2;, features a modification of the amino acid from R to Q at position 1743.
+The protein's natural variant, known as in TSC2;, features a modification of the amino acid from L to P at position 1744.
+The protein's natural variant, known as in TSC2;, features a modification of the amino acid from L to F at position 1750.
+The protein's natural variant, known as in TSC2;, features a modification of the amino acid from H to P at position 1773.
+The protein's natural variant, known as in TSC2;, features a modification of the amino acid from E to Q at position 1783.
+The protein's natural variant, known as found in patients with severe ciliopathies and left-right asymmetry defects; inhibits AURKA activity;, features a modification of the amino acid from R to K at position 80.
+The protein's natural variant, known as found in patients with Moyamoya disease; unknown pathological significance, features a modification of the amino acid from TEEKG to PS at position 80.
+The protein's natural variant, known as found in patients with Moyamoya disease; unknown pathological significance;, features a modification of the amino acid from E to K at position 242.
+The protein's natural variant, known as in NEDFACH; unknown pathological significance; no effect on protein abundance, features a modification of the amino acid from R to H at position 130.
+The protein's natural variant, known as in NEDFACH; unknown pathological significance; no effect on protein abundance, features a modification of the amino acid from L to S at position 580.
+The protein's natural variant, known as in NEDMVIC; unknown pathological significance, features a modification of the amino acid from P to L at position 152.
+The protein's natural variant, known as in NEDMVIC; unknown pathological significance, features a modification of the amino acid from N to K at position 184.
+The protein's natural variant, known as in NEDMVIC; unknown pathological significance, features a modification of the amino acid from P to L at position 223.
+The protein's natural variant, known as in NEDMVIC, features a modification of the amino acid from I to T at position 249.
+The protein's natural variant, known as in strain: 129/Sv; requires 2 nucleotide substitutions, features a modification of the amino acid from Y to I at position 658.
+The protein's natural variant, known as in CHDTHP; impairs protein stability;, features a modification of the amino acid from D to N at position 54.
+The protein's natural variant, known as in a patient with Meckel syndrome compound heterozygous for mutations in CC2D2A;, features a modification of the amino acid from R to K at position 55.
+The protein's natural variant, known as in a patient with Bardet-Biedl syndrome compound heterozygous for mutations in BBS12, features a modification of the amino acid from L to F at position 205.
+The natural variant of this protein is characterized by an amino acid alteration from S to F at position 708.
+The natural variant of this protein is characterized by an amino acid alteration from Y to L at position 306.
+The natural variant of this protein is characterized by an amino acid alteration from V to M at position 314.
+The natural variant of this protein is characterized by an amino acid alteration from L to I at position 405.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from D to H at position 21.
+The protein's natural variant, known as in N(1),N(12)-bis(ethyl)spermine-resistant cell line C55.7Res, features a modification of the amino acid from L to F at position 156.
+The natural variant of this protein is characterized by an amino acid alteration from V to F at position 59.
+The protein's natural variant, known as in MACTHC2; unknown pathological significance; results in impaired TUBA8 incorporation into the microtubule network, features a modification of the amino acid from C to Y at position 20.
+The protein's natural variant, known as in MACTHC2; unknown pathological significance; results in impaired TUBA8 incorporation into the microtubule network, features a modification of the amino acid from I to L at position 68.
+The protein's natural variant, known as in MACTHC2; unknown pathological significance, features a modification of the amino acid from R to C at position 214.
+The protein's natural variant, known as in MACTHC2; unknown pathological significance; results in impaired TUBA8 incorporation into the microtubule network, features a modification of the amino acid from R to C at position 243.
+The protein's natural variant, known as in MACTHC2; unknown pathological significance, features a modification of the amino acid from E to K at position 290.
+The protein's natural variant, known as in MACTHC2; unknown pathological significance; results in impaired TUBA8 incorporation into the microtubule network, features a modification of the amino acid from R to W at position 320.
+The protein's natural variant, known as in a renal clear cell carcinoma sample; somatic mutation, features a modification of the amino acid from F to Y at position 58.
+The protein's natural variant, known as in JPS, features a modification of the amino acid from Y to D at position 62.
+The protein's natural variant, known as in JPS, features a modification of the amino acid from C to Y at position 82.
+The protein's natural variant, known as in JPS;, features a modification of the amino acid from C to R at position 124.
+The protein's natural variant, known as in JPS;, features a modification of the amino acid from C to R at position 130.
+The protein's natural variant, known as in JPS;, features a modification of the amino acid from A to D at position 338.
+The protein's natural variant, known as in JPS;, features a modification of the amino acid from C to Y at position 376.
+The protein's natural variant, known as in JPS;, features a modification of the amino acid from R to C at position 443.
+The protein's natural variant, known as found in a patient with tubular adenoma and rectal neuroendocrine tumor; unknown pathological significance;, features a modification of the amino acid from M to T at position 460.
+The protein's natural variant, known as in JPS;, features a modification of the amino acid from M to T at position 470.
+The protein's natural variant, known as in a gastric adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from R to Q at position 486.
+The protein's natural variant, known as confirmed at protein level;, features a modification of the amino acid from T to M at position 72.
+The protein's natural variant, known as in strain: cv. Oy-0, features a modification of the amino acid from G to D at position 175.
+The protein's natural variant, known as in strain: cv. An-1, cv. Ct-1, cv. Cvi-1 and cv. Wassilewskija, features a modification of the amino acid from N to K at position 188.
+The protein's natural variant, known as in strain: cv. An-1, cv. Ct-1, cv. Cvi-1 and cv. Wassilewskija, features a modification of the amino acid from H to D at position 244.
+The protein's natural variant, known as in strain: cv. An-1, cv. Ct-1, cv. Cvi-1 and cv. Wassilewskija, features a modification of the amino acid from T to S at position 256.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to H at position 515.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation, features a modification of the amino acid from E to Q at position 278.
+The protein's natural variant, known as in a glioblastoma multiforme sample; somatic mutation, features a modification of the amino acid from G to E at position 1065.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from L to V at position 409.
+The protein's natural variant, known as in PNRIID; unknown pathological significance, features a modification of the amino acid from M to T at position 762.
+The protein's natural variant, known as in PNRIID; unknown pathological significance, features a modification of the amino acid from A to D at position 867.
+The protein's natural variant, known as in PNRIID; unknown pathological significance, features a modification of the amino acid from L to S at position 870.
+The protein's natural variant, known as in PNRIID; unknown pathological significance;, features a modification of the amino acid from R to H at position 878.
+The protein's natural variant, known as in PNRIID; unknown pathological significance;, features a modification of the amino acid from E to K at position 915.
+The protein's natural variant, known as in PNRIID; unknown pathological significance, features a modification of the amino acid from S to P at position 951.
+The protein's natural variant, known as in PNRIID; unknown pathological significance;, features a modification of the amino acid from V to M at position 1272.
+The protein's natural variant, known as in PNRIID; unknown pathological significance;, features a modification of the amino acid from E to K at position 1577.
+The protein's natural variant, known as found in a family with atypical autism and severe epilepsy; unknown pathological significance, features a modification of the amino acid from P to L at position 29.
+The natural variant of this protein is characterized by an amino acid alteration from T to K at position 375.
+The protein's natural variant, known as not associated with susceptibility to breast cancer;, features a modification of the amino acid from R to W at position 15.
+The protein's natural variant, known as not associated with susceptibility to breast cancer;, features a modification of the amino acid from M to T at position 353.
+The protein's natural variant, known as not associated with susceptibility to breast cancer;, features a modification of the amino acid from P to L at position 435.
+The protein's natural variant, known as not associated with susceptibility to breast cancer;, features a modification of the amino acid from C to R at position 511.
+The protein's natural variant, known as in strain: FCR-3 and ITG, features a modification of the amino acid from E to V at position 1031.
+The protein's natural variant, known as in UTEX 646 / Bohlin, features a modification of the amino acid from L to F at position 65.
+The protein's natural variant, known as in UTEX 646 / Bohlin, features a modification of the amino acid from R to Q at position 132.
+The protein's natural variant, known as in UTEX 646 / Bohlin, features a modification of the amino acid from G to D at position 155.
+The protein's natural variant, known as in UTEX 646 / Bohlin, features a modification of the amino acid from I to T at position 282.
+The protein's natural variant, known as in strain: R-2617; in allele 249 D, features a modification of the amino acid from Q to QA at position 33.
+The protein's natural variant, known as in strain: R-2805; in allele 255 A, features a modification of the amino acid from QQ to AQAQA at position 35.
+The protein's natural variant, known as in strain: R-2617, R-2624, R-2777 and R-2805; in allele 246 D, 249 E, 249 C and 246 E, features a modification of the amino acid from Q to A at position 34.
+The protein's natural variant, known as in strain: R-2621; in allele 249 B, features a modification of the amino acid from Q to QQ at position 41.
+The protein's natural variant, known as in strain: R-2617; in allele 246 D, features a modification of the amino acid from A to T at position 52.
+The protein's natural variant, known as in strain: cv. Est-1, features a modification of the amino acid from T to N at position 10.
+The protein's natural variant, known as in strain: cv. Est-1, features a modification of the amino acid from C to G at position 27.
+The protein's natural variant, known as in strain: cv. Est-1, features a modification of the amino acid from S to N at position 60.
+The protein's natural variant, known as in strain: cv. Est-1, features a modification of the amino acid from L to V at position 109.
+The protein's natural variant, known as in ACRDYS2;, features a modification of the amino acid from S to A at position 190.
+The protein's natural variant, known as in ACRDYS2;, features a modification of the amino acid from P to T at position 225.
+The protein's natural variant, known as in ACRDYS2;, features a modification of the amino acid from F to S at position 226.
+The protein's natural variant, known as in ACRDYS2, features a modification of the amino acid from A to S at position 227.
+The protein's natural variant, known as in ACRDYS2;, features a modification of the amino acid from Q to E at position 228.
+The protein's natural variant, known as in ACRDYS2, features a modification of the amino acid from S to T at position 301.
+The protein's natural variant, known as in ACRDYS2;, features a modification of the amino acid from A to V at position 304.
+The protein's natural variant, known as in ACRDYS2, features a modification of the amino acid from V to A at position 329.
+The protein's natural variant, known as in ACRDYS2;, features a modification of the amino acid from T to P at position 587.
+The protein's natural variant, known as in ACRDYS2, features a modification of the amino acid from E to A at position 590.
+The protein's natural variant, known as in ACRDYS2;, features a modification of the amino acid from G to D at position 673.
+The protein's natural variant, known as in ACRDYS2;, features a modification of the amino acid from I to T at position 678.
+The protein's natural variant, known as in p individuals; complete loss of activity;, features a modification of the amino acid from M to K at position 183.
+The protein's natural variant, known as in p individuals; partial loss of activity;, features a modification of the amino acid from G to D at position 187.
+The protein's natural variant, known as in individuals with NOR polyagglutination syndrome; causes the synthesis of both Gal(alpha1-4)Gal and Gal(alpha1-4)GalNAc moieties;, features a modification of the amino acid from Q to E at position 211.
+The protein's natural variant, known as in p individuals; complete loss of activity;, features a modification of the amino acid from P to L at position 251.
+The protein's natural variant, known as in HPABH4A; severe decrease in activity; diminishes phosphorylation by PKG;, features a modification of the amino acid from R to C at position 16.
+The protein's natural variant, known as in HPABH4A; severe form;, features a modification of the amino acid from R to G at position 25.
+The protein's natural variant, known as in HPABH4A; abolishes activity; no effect on phosphorylation by PKG;, features a modification of the amino acid from R to Q at position 25.
+The protein's natural variant, known as in HPABH4A;, features a modification of the amino acid from L to F at position 26.
+The protein's natural variant, known as in HPABH4A;, features a modification of the amino acid from E to G at position 35.
+The protein's natural variant, known as in HPABH4A;, features a modification of the amino acid from N to K at position 36.
+The protein's natural variant, known as in HPABH4A; transient phenotype due to partial PTS deficiency; total loss of activity;, features a modification of the amino acid from N to D at position 47.
+The protein's natural variant, known as in HPABH4A; severe form;, features a modification of the amino acid from N to S at position 52.
+The protein's natural variant, known as in HPABH4A; mild form;, features a modification of the amino acid from V to M at position 56.
+The protein's natural variant, known as in HPABH4A;, features a modification of the amino acid from T to M at position 67.
+The protein's natural variant, known as in HPABH4A;, features a modification of the amino acid from V to D at position 70.
+The protein's natural variant, known as in HPABH4A;, features a modification of the amino acid from P to L at position 87.
+The protein's natural variant, known as in HPABH4A; severe form;, features a modification of the amino acid from P to S at position 87.
+The protein's natural variant, known as in HPABH4A; severe form;, features a modification of the amino acid from D to N at position 96.
+The protein's natural variant, known as in HPABH4A;, features a modification of the amino acid from V to M at position 97.
+The protein's natural variant, known as in HPABH4A;, features a modification of the amino acid from Y to C at position 99.
+The protein's natural variant, known as in HPABH4A, features a modification of the amino acid from F to V at position 100.
+The protein's natural variant, known as in HPABH4A;, features a modification of the amino acid from T to M at position 106.
+The protein's natural variant, known as in HPABH4A;, features a modification of the amino acid from I to V at position 114.
+The protein's natural variant, known as in HPABH4A; transient phenotype due to partial PTS deficiency; mild decrease of activity;, features a modification of the amino acid from D to G at position 116.
+The protein's natural variant, known as in HPABH4A;, features a modification of the amino acid from V to L at position 124.
+The protein's natural variant, known as in HPABH4A;, features a modification of the amino acid from K to E at position 129.
+The protein's natural variant, known as in HPABH4A;, features a modification of the amino acid from D to G at position 136.
+The protein's natural variant, known as in HPABH4A, features a modification of the amino acid from D to V at position 136.
+The protein's natural variant, known as in D, features a modification of the amino acid from C to P at position 110.
+The protein's natural variant, known as in D, features a modification of the amino acid from G to D at position 162.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from Q to R at position 16.
+The natural variant of this protein is characterized by an amino acid alteration from K to M at position 4.
+The natural variant of this protein is characterized by an amino acid alteration from A to D at position 53.
+The natural variant of this protein is characterized by an amino acid alteration from T to A at position 199.
+The protein's natural variant, known as in IIAE9; decreased nuclear transport in patient cells; decreased protein levels in patient cells;, features a modification of the amino acid from R to C at position 38.
+The protein's natural variant, known as in IIAE9; unknown pathological significance;, features a modification of the amino acid from D to G at position 154.
+The protein's natural variant, known as in IIAE9;, features a modification of the amino acid from P to S at position 387.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from G to A at position 424.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from P to L at position 1378.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from A to V at position 1392.
+The protein's natural variant, known as in RDEOA;, features a modification of the amino acid from V to M at position 307.
+The protein's natural variant, known as in RDEOA;, features a modification of the amino acid from W to C at position 310.
+The protein's natural variant, known as in RDEOA;, features a modification of the amino acid from H to Y at position 325.
+The protein's natural variant, known as in RDEOA; unknown pathological significance;, features a modification of the amino acid from H to R at position 384.
+The protein's natural variant, known as in RDEOA;, features a modification of the amino acid from L to F at position 388.
+The protein's natural variant, known as in RDEOA; unknown pathological significance;, features a modification of the amino acid from S to L at position 401.
+The natural variant of this protein is characterized by an amino acid alteration from T to I at position 500.
+The protein's natural variant, known as no effect on enzyme activity;, features a modification of the amino acid from N to H at position 13.
+The protein's natural variant, known as nearly abolishes enzyme activity;, features a modification of the amino acid from N to K at position 17.
+The protein's natural variant, known as reduced enzyme activity;, features a modification of the amino acid from E to Q at position 61.
+The protein's natural variant, known as no effect on enzyme activity;, features a modification of the amino acid from K to E at position 81.
+The protein's natural variant, known as nearly abolishes enzyme activity;, features a modification of the amino acid from V to M at position 171.
+The protein's natural variant, known as nearly abolishes enzyme activity;, features a modification of the amino acid from D to G at position 210.
+The protein's natural variant, known as no effect on enzyme activity;, features a modification of the amino acid from K to R at position 219.
+The protein's natural variant, known as reduced enzyme activity;, features a modification of the amino acid from P to L at position 243.
+The protein's natural variant, known as reduced enzyme activity;, features a modification of the amino acid from I to M at position 269.
+The protein's natural variant, known as reduced enzyme activity;, features a modification of the amino acid from C to S at position 273.
+The protein's natural variant, known as reduced enzyme activity;, features a modification of the amino acid from G to A at position 278.
+The protein's natural variant, known as no effect on enzyme activity;, features a modification of the amino acid from E to D at position 288.
+The protein's natural variant, known as nearly abolishes enzyme activity;, features a modification of the amino acid from R to Q at position 291.
+The protein's natural variant, known as found in patients with neuropsychiatric disorders; unknown pathological significance; nearly abolishes enzyme activity;, features a modification of the amino acid from L to F at position 298.
+The protein's natural variant, known as found in a patient with bipolar disorder; unknown pathological significance; reduced enzyme activity, features a modification of the amino acid from V to M at position 305.
+The protein's natural variant, known as in BLS2; loss of expression;, features a modification of the amino acid from L to P at position 195.
+The natural variant of this protein is characterized by an amino acid alteration from V to L at position 25.
+The natural variant of this protein is characterized by an amino acid alteration from K to D at position 157.
+The protein's natural variant, known as in the I-A' sequence, features a modification of the amino acid from D to N at position 40.
+The protein's natural variant, known as in the I-B sequence, features a modification of the amino acid from R to H at position 60.
+The protein's natural variant, known as in NEDSTO; unknown pathological significance, features a modification of the amino acid from A to T at position 397.
+The protein's natural variant, known as in NEDSTO; unknown pathological significance, features a modification of the amino acid from D to N at position 532.
+The protein's natural variant, known as in NEDSTO; unknown pathological significance, features a modification of the amino acid from S to R at position 1119.
+The protein's natural variant, known as in NEDSTO, features a modification of the amino acid from R to W at position 1192.
+The protein's natural variant, known as in strain: USDA 2478, features a modification of the amino acid from V to E at position 97.
+The protein's natural variant, known as in strain: USDA 2478, features a modification of the amino acid from N to K at position 110.
+The protein's natural variant, known as in strain: USDA 2478, features a modification of the amino acid from A to AQ at position 123.
+The protein's natural variant, known as in SHNKND; loss of transporter activity;, features a modification of the amino acid from T to P at position 65.
+The protein's natural variant, known as found in a patient with type II collagenopathy; markedly decreases transporter activity;, features a modification of the amino acid from P to L at position 133.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from E to Q at position 146.
+The protein's natural variant, known as in truncate (tc); affects homeodomain stability, features a modification of the amino acid from F to C at position 168.
+The protein's natural variant, known as in SPG20; significant decrease in protein expression; significantly reduced COX respiratory chain complex IV activity in muscle mitochondria;, features a modification of the amino acid from M to V at position 330.
+The protein's natural variant, known as in SPG20; unknown pathological significance, features a modification of the amino acid from A to P at position 442.
+The protein's natural variant, known as in IMD21;, features a modification of the amino acid from P to L at position 254.
+The protein's natural variant, known as in IMD21 and MDS;, features a modification of the amino acid from T to M at position 354.
+The protein's natural variant, known as in LMPM, features a modification of the amino acid from R to P at position 361.
+The protein's natural variant, known as in LMPM;, features a modification of the amino acid from C to R at position 373.
+The protein's natural variant, known as in IMD21;, features a modification of the amino acid from R to W at position 398.
+The protein's natural variant, known as in haplotypes MA, features a modification of the amino acid from I to V at position 26.
+The protein's natural variant, known as in Bochum-1;, features a modification of the amino acid from L to P at position 78.
+The natural variant of this protein is characterized by an amino acid alteration from A to G at position 167.
+The protein's natural variant, known as in Bonn-1;, features a modification of the amino acid from P to A at position 252.
+The protein's natural variant, known as associated with occlusive-cerebrovascular disease; Isehara-1;, features a modification of the amino acid from M to V at position 401.
+The protein's natural variant, known as in OPA10;, features a modification of the amino acid from R to H at position 103.
+The protein's natural variant, known as in strain: 767 and 794, features a modification of the amino acid from P to L at position 63.
+The protein's natural variant, known as in strain: 432, features a modification of the amino acid from T to I at position 64.
+The protein's natural variant, known as in strain: 1124, features a modification of the amino acid from A to T at position 66.
+The protein's natural variant, known as in strain: 773, 796 and 1231, features a modification of the amino acid from VT to TI at position 108.
+The protein's natural variant, known as in strain: 162, 375, 723, 788, 800, 1008, 1124, 1158, 1180, 1181, 1207, 1233, 1247, a6062, e6158, e6229, e7066, f6237 and 1209, features a modification of the amino acid from V to I at position 107.
+The protein's natural variant, known as in strain: a7205, BR355 and e6181, features a modification of the amino acid from V to T at position 107.
+The protein's natural variant, known as in strain: c6132, features a modification of the amino acid from A to V at position 128.
+The protein's natural variant, known as in strain: a7205, features a modification of the amino acid from A to S at position 135.
+The protein's natural variant, known as in strain: f6252, features a modification of the amino acid from G to D at position 163.
+The protein's natural variant, known as in strain: 176, 667, a7205, b7017, c1271, c6134, c7424 and c8032, features a modification of the amino acid from K to E at position 193.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from D to N at position 565.
+The protein's natural variant, known as in strain: Isolate JP132, features a modification of the amino acid from S to A at position 39.
+The protein's natural variant, known as no effect on transcriptional activity shown in IFNB1 promoter-driven luciferase assay;, features a modification of the amino acid from A to T at position 95.
+The protein's natural variant, known as no effect on transcriptional activity shown in IFNB1 promoter-driven luciferase assay;, features a modification of the amino acid from A to V at position 147.
+The protein's natural variant, known as no effect on transcriptional activity shown in IFNB1 promoter-driven luciferase assay;, features a modification of the amino acid from R to K at position 177.
+The protein's natural variant, known as no effect on transcriptional activity shown in IFNB1 promoter-driven luciferase assay;, features a modification of the amino acid from T to N at position 187.
+The protein's natural variant, known as in AIFBL2; loss of transcriptional activity shown in IFNB1 promoter-driven luciferase assay; decreased IFNB1 promoter binding; impaired binding to GPR35, GPR162 and PLCB2 promoters, features a modification of the amino acid from W to R at position 231.
+The protein's natural variant, known as in AIFBL2; elevated IL17A expression in patient colon biopsies; patient CD8+ T cells have reduced PRF1 expression when activated with IL-2 compared to CD8+ T cells from a healthy donor; severely decreased transcriptional activity shown in IFNB1 promoter-driven luciferase assay, features a modification of the amino acid from W to S at position 251.
+The protein's natural variant, known as no effect on transcriptional activity shown in IFNB1 promoter-driven luciferase assay;, features a modification of the amino acid from S to T at position 345.
+The protein's natural variant, known as no effect on transcriptional activity shown in IFNB1 promoter-driven luciferase assay;, features a modification of the amino acid from P to L at position 368.
+The protein's natural variant, known as no effect on transcriptional activity shown in IFNB1 promoter-driven luciferase assay;, features a modification of the amino acid from V to I at position 382.
+The protein's natural variant, known as no effect on transcriptional activity shown in IFNB1 promoter-driven luciferase assay;, features a modification of the amino acid from V to M at position 408.
+The protein's natural variant, known as no effect on transcriptional activity shown in IFNB1 promoter-driven luciferase assay;, features a modification of the amino acid from V to M at position 411.
+The protein's natural variant, known as no effect on transcriptional activity shown in IFNB1 promoter-driven luciferase assay;, features a modification of the amino acid from A to V at position 500.
+The protein's natural variant, known as no effect on transcriptional activity shown in IFNB1 promoter-driven luciferase assay;, features a modification of the amino acid from P to L at position 512.
+The protein's natural variant, known as no effect on transcriptional activity shown in IFNB1 promoter-driven luciferase assay;, features a modification of the amino acid from R to C at position 604.
+The protein's natural variant, known as in PDHAD; affects mitochondrial import of precursor protein;, features a modification of the amino acid from R to P at position 10.
+The protein's natural variant, known as in PDHAD;, features a modification of the amino acid from R to C at position 72.
+The protein's natural variant, known as in PDHAD, features a modification of the amino acid from H to D at position 113.
+The protein's natural variant, known as probable disease-associated variant found in a patient with moderate developmental delay, mild dysmorphism and mildly elevated serum lactate;, features a modification of the amino acid from A to T at position 136.
+The protein's natural variant, known as in PDHAD;, features a modification of the amino acid from G to R at position 162.
+The protein's natural variant, known as in PDHAD, features a modification of the amino acid from V to M at position 167.
+The protein's natural variant, known as in PDHAD, features a modification of the amino acid from A to T at position 199.
+The protein's natural variant, known as in PDHAD;, features a modification of the amino acid from F to L at position 205.
+The protein's natural variant, known as in PDHAD;, features a modification of the amino acid from M to V at position 210.
+The protein's natural variant, known as in PDHAD;, features a modification of the amino acid from P to L at position 217.
+The protein's natural variant, known as in PDHAD, features a modification of the amino acid from T to A at position 231.
+The protein's natural variant, known as in PDHAD;, features a modification of the amino acid from Y to N at position 243.
+The protein's natural variant, known as in PDHAD;, features a modification of the amino acid from D to A at position 258.
+The protein's natural variant, known as in PDHAD;, features a modification of the amino acid from R to G at position 263.
+The protein's natural variant, known as in PDHAD, features a modification of the amino acid from R to Q at position 263.
+The protein's natural variant, known as in PDHAD;, features a modification of the amino acid from R to H at position 288.
+The protein's natural variant, known as in PDHAD, features a modification of the amino acid from H to L at position 292.
+The protein's natural variant, known as in PDHAD; loss of activity; common mutation;, features a modification of the amino acid from R to C at position 302.
+The protein's natural variant, known as in PDHAD;, features a modification of the amino acid from R to H at position 302.
+The protein's natural variant, known as in PDHAD, features a modification of the amino acid from E to EDSYRTRE at position 305.
+The protein's natural variant, known as in PDHAD, features a modification of the amino acid from I to IPPHSYRTREEI at position 307.
+The protein's natural variant, known as in PDHAD;, features a modification of the amino acid from D to N at position 315.
+The protein's natural variant, known as in PDHAD;, features a modification of the amino acid from R to H at position 378.
+The protein's natural variant, known as in PA-2; likely benign variant;, features a modification of the amino acid from L to M at position 17.
+The protein's natural variant, known as in PA-2, features a modification of the amino acid from R to P at position 44.
+The protein's natural variant, known as in PA-2;, features a modification of the amino acid from R to S at position 67.
+The protein's natural variant, known as in PA-2, features a modification of the amino acid from S to R at position 106.
+The protein's natural variant, known as in PA-2;, features a modification of the amino acid from V to M at position 107.
+The protein's natural variant, known as in PA-2;, features a modification of the amino acid from G to D at position 112.
+The protein's natural variant, known as in PA-2, features a modification of the amino acid from G to R at position 131.
+The protein's natural variant, known as in PA-2, features a modification of the amino acid from K to KICK at position 140.
+The protein's natural variant, known as in PA-2;, features a modification of the amino acid from A to P at position 153.
+The protein's natural variant, known as in PA-2; does not affect either heteromeric or homomeric assembly;, features a modification of the amino acid from R to Q at position 165.
+The protein's natural variant, known as in PA-2; no effect on affinity for propionyl-CoA; decreased reaction kinetics for the propionyl-CoA carboxylase activity; decreased thermostability affecting holoenzyme oligomerization;, features a modification of the amino acid from R to W at position 165.
+The protein's natural variant, known as in PA-2; no effect on affinity for propionyl-CoA; decreased reaction kinetics for the propionyl-CoA carboxylase activity; decreased thermostability affecting holoenzyme oligomerization;, features a modification of the amino acid from E to K at position 168.
+The protein's natural variant, known as in PA-2;, features a modification of the amino acid from G to R at position 188.
+The protein's natural variant, known as in PA-2;, features a modification of the amino acid from G to D at position 198.
+The protein's natural variant, known as in PA-2, features a modification of the amino acid from V to D at position 205.
+The protein's natural variant, known as in PA-2;, features a modification of the amino acid from P to L at position 228.
+The protein's natural variant, known as in PA-2, features a modification of the amino acid from G to V at position 246.
+The protein's natural variant, known as in PA-2; no effect on affinity for propionyl-CoA; decreased reaction kinetics for the propionyl-CoA carboxylase activity; decreased thermostability affecting holoenzyme oligomerization;, features a modification of the amino acid from R to W at position 410.
+The protein's natural variant, known as in PA-2;, features a modification of the amino acid from T to I at position 428.
+The protein's natural variant, known as in PA-2, features a modification of the amino acid from I to L at position 430.
+The protein's natural variant, known as in PA-2;, features a modification of the amino acid from Y to C at position 435.
+The protein's natural variant, known as in PA-2;, features a modification of the amino acid from Y to C at position 439.
+The protein's natural variant, known as in PA-2, features a modification of the amino acid from M to T at position 442.
+The protein's natural variant, known as in PA-2;, features a modification of the amino acid from A to T at position 468.
+The protein's natural variant, known as found in patients with propionic acidemia; does not affect either heteromeric or homomeric assembly; decreased thermostability affecting holoenzyme oligomerization; no effect on propionyl-CoA carboxylase activity;, features a modification of the amino acid from A to V at position 497.
+The protein's natural variant, known as in PA-2; affects heteromeric and homomeric assembly;, features a modification of the amino acid from R to C at position 512.
+The protein's natural variant, known as in PA-2; affects heteromeric and homomeric assembly;, features a modification of the amino acid from L to P at position 519.
+The protein's natural variant, known as in PA-2; affects heteromeric and homomeric assembly;, features a modification of the amino acid from N to D at position 536.
+The protein's natural variant, known as in pheochromocytoma; likely benign variant;, features a modification of the amino acid from P to L at position 25.
+The protein's natural variant, known as in VHLD; type II, features a modification of the amino acid from S to P at position 38.
+The protein's natural variant, known as in VHLD; type I;, features a modification of the amino acid from E to K at position 52.
+The protein's natural variant, known as in pheochromocytoma;, features a modification of the amino acid from L to P at position 63.
+The protein's natural variant, known as in pheochromocytoma;, features a modification of the amino acid from R to P at position 64.
+The protein's natural variant, known as in pheochromocytoma;, features a modification of the amino acid from S to A at position 65.
+The protein's natural variant, known as in VHLD; type I;, features a modification of the amino acid from S to L at position 65.
+The protein's natural variant, known as in VHLD; type I;, features a modification of the amino acid from S to W at position 65.
+The protein's natural variant, known as in pheochromocytoma and VHLD; type II, features a modification of the amino acid from S to W at position 68.
+The protein's natural variant, known as in VHLD; type I;, features a modification of the amino acid from E to K at position 70.
+The protein's natural variant, known as in VHLD; type I-II;, features a modification of the amino acid from V to G at position 74.
+The protein's natural variant, known as in VHLD; type I;, features a modification of the amino acid from F to I at position 76.
+The protein's natural variant, known as in VHLD; type I, features a modification of the amino acid from F to L at position 76.
+The protein's natural variant, known as in VHLD; type I;, features a modification of the amino acid from F to S at position 76.
+The protein's natural variant, known as in VHLD; type I;, features a modification of the amino acid from N to H at position 78.
+The protein's natural variant, known as in VHLD; type I; common mutation;, features a modification of the amino acid from N to S at position 78.
+The protein's natural variant, known as in VHLD; type I;, features a modification of the amino acid from N to T at position 78.
+The protein's natural variant, known as in VHLD, features a modification of the amino acid from R to P at position 79.
+The protein's natural variant, known as in VHLD; type I;, features a modification of the amino acid from S to I at position 80.
+The protein's natural variant, known as in pheochromocytoma and VHLD; type I;, features a modification of the amino acid from S to N at position 80.
+The protein's natural variant, known as in VHLD; type I;, features a modification of the amino acid from S to R at position 80.
+The protein's natural variant, known as in VHLD; type I;, features a modification of the amino acid from P to S at position 81.
+The protein's natural variant, known as in VHLD; type I;, features a modification of the amino acid from R to P at position 82.
+The protein's natural variant, known as in VHLD; type II and type 2C;, features a modification of the amino acid from V to L at position 84.
+The protein's natural variant, known as in VHLD; type I;, features a modification of the amino acid from P to A at position 86.
+The protein's natural variant, known as in VHLD, features a modification of the amino acid from P to H at position 86.
+The protein's natural variant, known as in VHLD; type I;, features a modification of the amino acid from P to L at position 86.
+The protein's natural variant, known as in VHLD; type I;, features a modification of the amino acid from P to R at position 86.
+The protein's natural variant, known as in VHLD;, features a modification of the amino acid from P to S at position 86.
+The protein's natural variant, known as in VHLD; type I;, features a modification of the amino acid from W to R at position 88.
+The protein's natural variant, known as in VHLD; type I;, features a modification of the amino acid from W to S at position 88.
+The protein's natural variant, known as in lung cancer;, features a modification of the amino acid from L to H at position 89.
+The protein's natural variant, known as in VHLD; type I;, features a modification of the amino acid from L to P at position 89.
+The protein's natural variant, known as in cerebellar hemangioblastoma;, features a modification of the amino acid from F to L at position 91.
+The protein's natural variant, known as in pheochromocytoma and VHLD; type II;, features a modification of the amino acid from G to C at position 93.
+The protein's natural variant, known as in VHLD;, features a modification of the amino acid from G to D at position 93.
+The protein's natural variant, known as in pheochromocytoma and VHLD; type II;, features a modification of the amino acid from G to S at position 93.
+The protein's natural variant, known as in VHLD; type I;, features a modification of the amino acid from Q to P at position 96.
+The protein's natural variant, known as in pheochromocytoma and VHLD; type II;, features a modification of the amino acid from Y to H at position 98.
+The protein's natural variant, known as in VHLD; type I; requires 2 nucleotide substitutions, features a modification of the amino acid from L to G at position 101.
+The protein's natural variant, known as in VHLD; type I, features a modification of the amino acid from L to R at position 101.
+The protein's natural variant, known as in cerebellar hemangioblastoma;, features a modification of the amino acid from G to A at position 104.
+The protein's natural variant, known as in VHLD; type I;, features a modification of the amino acid from T to P at position 105.
+The protein's natural variant, known as in lung cancer;, features a modification of the amino acid from G to D at position 106.
+The protein's natural variant, known as in pheochromocytoma;, features a modification of the amino acid from R to G at position 107.
+The protein's natural variant, known as in VHLD; type I;, features a modification of the amino acid from R to P at position 107.
+The protein's natural variant, known as in VHLD; type II;, features a modification of the amino acid from S to C at position 111.
+The protein's natural variant, known as in VHLD; type I;, features a modification of the amino acid from S to N at position 111.
+The protein's natural variant, known as in VHLD; type I;, features a modification of the amino acid from S to R at position 111.
+The protein's natural variant, known as in VHLD; type IIA;, features a modification of the amino acid from Y to H at position 112.
+The protein's natural variant, known as in VHLD;, features a modification of the amino acid from Y to N at position 112.
+The protein's natural variant, known as in VHLD; type II, features a modification of the amino acid from G to C at position 114.
+The protein's natural variant, known as in VHLD; type I-II;, features a modification of the amino acid from G to R at position 114.
+The protein's natural variant, known as in VHLD; type II;, features a modification of the amino acid from G to S at position 114.
+The protein's natural variant, known as in VHLD; type II;, features a modification of the amino acid from H to Q at position 115.
+The protein's natural variant, known as in VHLD; type II;, features a modification of the amino acid from H to R at position 115.
+The protein's natural variant, known as in VHLD; type I;, features a modification of the amino acid from H to Y at position 115.
+The protein's natural variant, known as in VHLD, features a modification of the amino acid from L to V at position 116.
+The protein's natural variant, known as in VHLD; type I;, features a modification of the amino acid from W to C at position 117.
+The protein's natural variant, known as in VHLD; type I;, features a modification of the amino acid from L to P at position 118.
+The protein's natural variant, known as in VHLD;, features a modification of the amino acid from L to R at position 118.
+The protein's natural variant, known as in pheochromocytoma and VHLD; type II;, features a modification of the amino acid from F to L at position 119.
+The protein's natural variant, known as in VHLD; type II, features a modification of the amino acid from F to S at position 119.
+The protein's natural variant, known as in VHLD; type I;, features a modification of the amino acid from D to G at position 121.
+The protein's natural variant, known as in pheochromocytoma; requires 2 nucleotide substitutions, features a modification of the amino acid from A to I at position 122.
+The protein's natural variant, known as in ECYT2;, features a modification of the amino acid from D to Y at position 126.
+The protein's natural variant, known as in VHLD; type II;, features a modification of the amino acid from L to F at position 128.
+The protein's natural variant, known as in VHLD, features a modification of the amino acid from L to LE at position 129.
+The protein's natural variant, known as in ECYT2 and VHLD; type I;, features a modification of the amino acid from V to L at position 130.
+The protein's natural variant, known as in VHLD; type I;, features a modification of the amino acid from N to K at position 131.
+The protein's natural variant, known as in VHLD; type I, features a modification of the amino acid from N to T at position 131.
+The protein's natural variant, known as in hemangioblastoma;, features a modification of the amino acid from L to F at position 135.
+The protein's natural variant, known as in pheochromocytoma and VHLD; type II;, features a modification of the amino acid from F to C at position 136.
+The protein's natural variant, known as in VHLD;, features a modification of the amino acid from F to S at position 136.
+The protein's natural variant, known as in VHLD, features a modification of the amino acid from F to Y at position 136.
+The protein's natural variant, known as in VHLD; type II;, features a modification of the amino acid from D to E at position 143.
+The protein's natural variant, known as in VHLD;, features a modification of the amino acid from Q to H at position 145.
+The protein's natural variant, known as in pheochromocytoma;, features a modification of the amino acid from I to T at position 147.
+The protein's natural variant, known as in VHLD; type II;, features a modification of the amino acid from A to T at position 149.
+The protein's natural variant, known as in VHLD; type II;, features a modification of the amino acid from P to L at position 154.
+The protein's natural variant, known as in VHLD; type II, features a modification of the amino acid from V to G at position 155.
+The protein's natural variant, known as in VHLD; with RCC;, features a modification of the amino acid from V to M at position 155.
+The protein's natural variant, known as in pheochromocytoma and VHLD; type I;, features a modification of the amino acid from Y to C at position 156.
+The protein's natural variant, known as in VHLD; type I, features a modification of the amino acid from Y to D at position 156.
+The protein's natural variant, known as in pheochromocytoma, features a modification of the amino acid from Y to N at position 156.
+The protein's natural variant, known as in VHLD; type II;, features a modification of the amino acid from T to I at position 157.
+The protein's natural variant, known as in VHLD; type I, features a modification of the amino acid from T to TF at position 157.
+The protein's natural variant, known as in VHLD; type I-II; abolishes release from chaperonin complex and the interaction with Elongin BC complex;, features a modification of the amino acid from L to P at position 158.
+The protein's natural variant, known as in VHLD; type I;, features a modification of the amino acid from L to V at position 158.
+The protein's natural variant, known as in VHLD; type II;, features a modification of the amino acid from K to E at position 159.
+The protein's natural variant, known as in VHLD; type II;, features a modification of the amino acid from R to G at position 161.
+The protein's natural variant, known as in pheochromocytoma and VHLD; type I, features a modification of the amino acid from R to P at position 161.
+The protein's natural variant, known as in pheochromocytoma and VHLD; type II;, features a modification of the amino acid from R to Q at position 161.
+The protein's natural variant, known as in VHLD; type I; No effect on interaction with HIF1A nor on HIF1A degradation;, features a modification of the amino acid from C to F at position 162.
+The protein's natural variant, known as in VHLD; type I;, features a modification of the amino acid from C to R at position 162.
+The protein's natural variant, known as in VHLD; type I-II;, features a modification of the amino acid from C to W at position 162.
+The protein's natural variant, known as in VHLD; type I;, features a modification of the amino acid from C to Y at position 162.
+The protein's natural variant, known as in RCC; with paraneoplastic erythrocytosis; inhibits binding to HIF1AN;, features a modification of the amino acid from L to P at position 163.
+The protein's natural variant, known as in VHLD;, features a modification of the amino acid from Q to H at position 164.
+The protein's natural variant, known as in VHLD; type II;, features a modification of the amino acid from Q to R at position 164.
+The protein's natural variant, known as in VHLD; with RCC;, features a modification of the amino acid from V to D at position 166.
+The protein's natural variant, known as in VHLD; type IIA;, features a modification of the amino acid from V to F at position 166.
+The protein's natural variant, known as in VHLD; type I-II;, features a modification of the amino acid from R to G at position 167.
+The protein's natural variant, known as in pheochromocytoma and VHLD; type II; common mutation;, features a modification of the amino acid from R to Q at position 167.
+The protein's natural variant, known as in pheochromocytoma and VHLD; type II; common mutation;, features a modification of the amino acid from R to W at position 167.
+The protein's natural variant, known as in VHLD; type II;, features a modification of the amino acid from V to D at position 170.
+The protein's natural variant, known as in VHLD; type II, features a modification of the amino acid from V to F at position 170.
+The protein's natural variant, known as in VHLD; type I, features a modification of the amino acid from V to G at position 170.
+The protein's natural variant, known as in VHLD; type I, features a modification of the amino acid from Y to D at position 175.
+The protein's natural variant, known as in VHLD, features a modification of the amino acid from R to W at position 176.
+The protein's natural variant, known as in VHLD; type I, features a modification of the amino acid from R to RLRVKPE at position 177.
+The protein's natural variant, known as in VHLD; type I-II; common mutation;, features a modification of the amino acid from L to P at position 178.
+The protein's natural variant, known as in VHLD; type II;, features a modification of the amino acid from L to Q at position 178.
+The protein's natural variant, known as in VHLD; type I;, features a modification of the amino acid from I to V at position 180.
+The protein's natural variant, known as in VHLD; type I;, features a modification of the amino acid from L to P at position 184.
+The protein's natural variant, known as in VHLD; type I, features a modification of the amino acid from L to R at position 184.
+The protein's natural variant, known as in VHLD; type I;, features a modification of the amino acid from E to K at position 186.
+The protein's natural variant, known as in VHLD; type I-II;, features a modification of the amino acid from L to P at position 188.
+The protein's natural variant, known as in VHLD; type I;, features a modification of the amino acid from L to Q at position 188.
+The protein's natural variant, known as in ECYT2, pheochromocytoma and VHLD; type IIA;, features a modification of the amino acid from L to V at position 188.
+The protein's natural variant, known as in ECYT2;, features a modification of the amino acid from H to D at position 191.
+The protein's natural variant, known as in ECYT2;, features a modification of the amino acid from P to S at position 192.
+The protein's natural variant, known as in pheochromocytoma, features a modification of the amino acid from L to Q at position 198.
+The protein's natural variant, known as in ECYT2 and VHLD; type II, features a modification of the amino acid from L to R at position 198.
+The protein's natural variant, known as in ECYT2 and VHLD; type I;, features a modification of the amino acid from R to W at position 200.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from E to K at position 262.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from A to V at position 309.
+The protein's natural variant, known as in IDPFH; de novo mutation; loss of function in transactivation of transcription; reduces the interaction between isoform 2 and isoform 3; disrupts the nuclear paraspeckle distribution of isoform 2 and isoform 3; does not affect the interaction of isoform 2 with TBR1;, features a modification of the amino acid from T to P at position 47.
+The protein's natural variant, known as in IDPFH; de novo mutation; loss of function in transactivation of transcription; reduces the interaction between isoform 2 and isoform 3; disrupts the nuclear paraspeckle distribution of isoform 2 and isoform 3; does not affect the interaction of isoform 2 with TBR1;, features a modification of the amino acid from C to F at position 48.
+The protein's natural variant, known as in IDPFH; de novo mutation; loss of function in transactivation of transcription; reduces the interaction between isoform 2 and isoform 3; disrupts the nuclear paraspeckle distribution of isoform 2 and isoform 3; does not affect the interaction of isoform 2 with TBR1;, features a modification of the amino acid from H to Q at position 66.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from S to F at position 142.
+The protein's natural variant, known as in NTD; uncertain pathological significance;, features a modification of the amino acid from G to V at position 55.
+The protein's natural variant, known as in NTD; uncertain pathological significance;, features a modification of the amino acid from T to A at position 71.
+The protein's natural variant, known as in NTD; uncertain pathological significance, features a modification of the amino acid from A to T at position 128.
+The protein's natural variant, known as in RREI; decreases succinate dehydrogenase activity and glycerol-3-phosphate dehydrogenase activity;, features a modification of the amino acid from R to H at position 147.
+The protein's natural variant, known as in NTD; uncertain pathological significance, features a modification of the amino acid from S to N at position 260.
+The protein's natural variant, known as in MC4DN18; reduced complex IV assembly; decreased COX6A2 protein stability;, features a modification of the amino acid from S to R at position 39.
+The protein's natural variant, known as in MC4DN18; reduced complex IV assembly; decreased COX6A2 protein stability;, features a modification of the amino acid from C to R at position 43.
+The natural variant of this protein is characterized by an amino acid alteration from H to N at position 245.
+The protein's natural variant, known as in strain: Chinese, features a modification of the amino acid from V to I at position 567.
+The protein's natural variant, known as in strain: Chinese, features a modification of the amino acid from F to Y at position 720.
+The protein's natural variant, known as in CSID; missorting of the enzyme to the basolateral membrane;, features a modification of the amino acid from Q to R at position 117.
+The protein's natural variant, known as in CSID; causes loss of anchored SI from the membrane;, features a modification of the amino acid from L to P at position 341.
+The protein's natural variant, known as in CSID;, features a modification of the amino acid from V to G at position 577.
+The protein's natural variant, known as in CSID;, features a modification of the amino acid from S to P at position 594.
+The protein's natural variant, known as in CSID; SI accumulates predominantly in the ER;, features a modification of the amino acid from L to P at position 620.
+The protein's natural variant, known as in CSID, features a modification of the amino acid from T to P at position 694.
+The protein's natural variant, known as in CSID;, features a modification of the amino acid from G to D at position 1073.
+The protein's natural variant, known as in CSID; exhibits intracellular accumulation of mannose-rich SI in the Golgi;, features a modification of the amino acid from Q to P at position 1098.
+The protein's natural variant, known as in CSID;, features a modification of the amino acid from C to Y at position 1229.
+The protein's natural variant, known as in CSID;, features a modification of the amino acid from R to G at position 1367.
+The protein's natural variant, known as in CSID;, features a modification of the amino acid from F to C at position 1745.
+The natural variant of this protein is characterized by an amino acid alteration from M to L at position 41.
+The natural variant of this protein is characterized by an amino acid alteration from M to Y at position 165.
+The natural variant of this protein is characterized by an amino acid alteration from N to KY at position 183.
+The natural variant of this protein is characterized by an amino acid alteration from V to A at position 236.
+The natural variant of this protein is characterized by an amino acid alteration from Q to T at position 269.
+The protein's natural variant, known as in ORTHYP1;, features a modification of the amino acid from V to M at position 101.
+The protein's natural variant, known as in ORTHYP1;, features a modification of the amino acid from D to E at position 114.
+The protein's natural variant, known as in allele DBH-B;, features a modification of the amino acid from A to S at position 318.
+The protein's natural variant, known as in ORTHYP1;, features a modification of the amino acid from D to N at position 345.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from P to L at position 474.
+The protein's natural variant, known as in strain: ATCC 56676, features a modification of the amino acid from F to L at position 7.
+The protein's natural variant, known as in strain: ATCC 56676, features a modification of the amino acid from P to A at position 57.
+The protein's natural variant, known as in strain: ATCC 56676, features a modification of the amino acid from R to K at position 69.
+The protein's natural variant, known as in strain: ATCC 56676, features a modification of the amino acid from HV to QL at position 126.
+The protein's natural variant, known as in strain: ATCC 56676, features a modification of the amino acid from N to D at position 189.
+The protein's natural variant, known as in strain: ATCC 56676, features a modification of the amino acid from A to G at position 194.
+The protein's natural variant, known as in strain: ATCC 56676, features a modification of the amino acid from K to R at position 219.
+The protein's natural variant, known as in strain: cv. Akisengoku, features a modification of the amino acid from Q to K at position 3.
+The natural variant of this protein is characterized by an amino acid alteration from S to T at position 235.
+The protein's natural variant, known as in CSS7; abolishes interaction with acetylated or methylated histone H3;, features a modification of the amino acid from C to F at position 276.
+The protein's natural variant, known as in CSS7; abolishes interaction with acetylated or methylated histone H3;, features a modification of the amino acid from C to W at position 330.
+The protein's natural variant, known as in CSS7;, features a modification of the amino acid from D to G at position 346.
+The protein's natural variant, known as in CSS7; abolishes interaction with acetylated histone H3; strongly decreased interaction with methylated histone H3;, features a modification of the amino acid from R to H at position 350.
+The protein's natural variant, known as in CSS7, features a modification of the amino acid from W to R at position 369.
+The protein's natural variant, known as in allele B, features a modification of the amino acid from Q to R at position 162.
+The protein's natural variant, known as in allele B, features a modification of the amino acid from T to A at position 193.
+The protein's natural variant, known as in allele B, features a modification of the amino acid from N to D at position 299.
+The protein's natural variant, known as in allele B, features a modification of the amino acid from M to I at position 300.
+The protein's natural variant, known as in allele CYP6D1v3 and allele CYP6D1v5, features a modification of the amino acid from M to L at position 55.
+The protein's natural variant, known as in allele CYP6D1v1, features a modification of the amino acid from A to D at position 150.
+The protein's natural variant, known as in allele CYP6D1v1, features a modification of the amino acid from L to I at position 153.
+The protein's natural variant, known as in allele CYP6D1v1, features a modification of the amino acid from S to T at position 165.
+The protein's natural variant, known as in allele CYP6D1v5, features a modification of the amino acid from I to N at position 182.
+The protein's natural variant, known as in allele CYP6D1v5 and allele CYP6D1v1, features a modification of the amino acid from Q to E at position 218.
+The protein's natural variant, known as in allele CYP6D1v1, features a modification of the amino acid from F to I at position 220.
+The protein's natural variant, known as in allele CYP6D1v5 and allele CYP6D1v1, features a modification of the amino acid from NFI to TFM at position 227.
+The protein's natural variant, known as in allele CYP6D1v5, features a modification of the amino acid from K to T at position 262.
+The protein's natural variant, known as in allele CYP6D1v3, features a modification of the amino acid from R to P at position 266.
+The protein's natural variant, known as in allele CYP6D1v5, features a modification of the amino acid from D to N at position 447.
+The protein's natural variant, known as in allele CYP6D1v4, allele CYP6D1v5 and allele CYP6D1v1, features a modification of the amino acid from M to I at position 469.
+The protein's natural variant, known as in rpsD3; suppresses S12 mutation K55D, features a modification of the amino acid from E to K at position 46.
+The protein's natural variant, known as in rpsD1; suppresses S12 mutation K55D. A ram mutation, features a modification of the amino acid from L to LAGKL at position 78.
+The protein's natural variant, known as in granular corneal dystrophy; unclassified form; with centrifuge pattern of opacities;, features a modification of the amino acid from V to I at position 113.
+The protein's natural variant, known as in granular corneal dystrophy; unclassified form; Hanoi;, features a modification of the amino acid from D to H at position 123.
+The protein's natural variant, known as in CDL1; cysteinylated; no effect on the disulfide bond pattern;, features a modification of the amino acid from R to C at position 124.
+The protein's natural variant, known as in CDA; most common mutation in Japanese;, features a modification of the amino acid from R to H at position 124.
+The protein's natural variant, known as in CDRB;, features a modification of the amino acid from R to L at position 124.
+The protein's natural variant, known as in CDGG1; late-onset; mild ocular irritation and reduction in visual acuity;, features a modification of the amino acid from R to S at position 124.
+The protein's natural variant, known as in CDL3A;, features a modification of the amino acid from P to T at position 501.
+The protein's natural variant, known as in CDL1, features a modification of the amino acid from V to D at position 505.
+The protein's natural variant, known as in EBMD;, features a modification of the amino acid from L to R at position 509.
+The protein's natural variant, known as in CDL1, features a modification of the amino acid from L to P at position 518.
+The protein's natural variant, known as in CDL1; severe phenotype; delayed age of onset, features a modification of the amino acid from L to R at position 518.
+The protein's natural variant, known as in CDL1; late-onset; found also in sporadic cases;, features a modification of the amino acid from L to R at position 527.
+The protein's natural variant, known as in CDL1; delayed age of onset, features a modification of the amino acid from T to R at position 538.
+The protein's natural variant, known as in lattice corneal dystrophy; unclassified form;, features a modification of the amino acid from V to D at position 539.
+The protein's natural variant, known as in CDL3A;, features a modification of the amino acid from F to S at position 540.
+The protein's natural variant, known as found in lattice corneal dystrophy; unclassified form; late-onset;, features a modification of the amino acid from N to S at position 544.
+The protein's natural variant, known as in CDL1; associated with Q-551;, features a modification of the amino acid from A to D at position 546.
+The protein's natural variant, known as in CDL3A, features a modification of the amino acid from A to T at position 546.
+The protein's natural variant, known as in CDL1; associated with D-546;, features a modification of the amino acid from P to Q at position 551.
+The protein's natural variant, known as in CDTB; originally thought to cause CDRB;, features a modification of the amino acid from R to Q at position 555.
+The protein's natural variant, known as in CDGG1; common mutation in Europe and United States; rare in Japan;, features a modification of the amino acid from R to W at position 555.
+The protein's natural variant, known as in CDL1, features a modification of the amino acid from L to R at position 569.
+The protein's natural variant, known as in CDL1; late-onset, features a modification of the amino acid from H to R at position 572.
+The protein's natural variant, known as in lattice corneal dystrophy; unclassified form, features a modification of the amino acid from G to V at position 594.
+The protein's natural variant, known as in asymmetric lattice corneal dystrophy, features a modification of the amino acid from N to H at position 622.
+The protein's natural variant, known as in CDL3A, features a modification of the amino acid from N to K at position 622.
+The protein's natural variant, known as in CDL1; delayed age of onset;, features a modification of the amino acid from G to D at position 623.
+The protein's natural variant, known as in CDL1, features a modification of the amino acid from H to P at position 626.
+The protein's natural variant, known as in CDL1; delayed age of onset;, features a modification of the amino acid from H to R at position 626.
+The protein's natural variant, known as found in lattice corneal dystrophy; unclassified form, features a modification of the amino acid from V to D at position 631.
+The protein's natural variant, known as in EBMD; unknown pathological significance;, features a modification of the amino acid from R to S at position 666.
+The protein's natural variant, known as in VWS1;, features a modification of the amino acid from A to V at position 2.
+The protein's natural variant, known as in VWS1;, features a modification of the amino acid from R to C at position 6.
+The protein's natural variant, known as in VWS1, features a modification of the amino acid from A to V at position 16.
+The protein's natural variant, known as in VWS1; abrogates DNA binding, features a modification of the amino acid from V to A at position 18.
+The protein's natural variant, known as in VWS1; abrogates DNA binding;, features a modification of the amino acid from V to M at position 18.
+The protein's natural variant, known as in VWS1 and PPS; abrogates DNA binding;, features a modification of the amino acid from L to P at position 22.
+The protein's natural variant, known as in VWS1, features a modification of the amino acid from P to A at position 39.
+The protein's natural variant, known as in VWS1;, features a modification of the amino acid from R to Q at position 45.
+The protein's natural variant, known as in PPS; abrogates DNA binding, features a modification of the amino acid from W to G at position 60.
+The protein's natural variant, known as in VWS1, features a modification of the amino acid from A to G at position 61.
+The protein's natural variant, known as in VWS1, features a modification of the amino acid from T to I at position 64.
+The protein's natural variant, known as in PPS, features a modification of the amino acid from K to T at position 66.
+The protein's natural variant, known as in VWS1; does not affect DNA binding;, features a modification of the amino acid from G to R at position 70.
+The protein's natural variant, known as in VWS1; abrogates DNA binding;, features a modification of the amino acid from P to S at position 76.
+The protein's natural variant, known as in PPS, features a modification of the amino acid from Q to K at position 82.
+The protein's natural variant, known as in PPS; abrogates DNA binding;, features a modification of the amino acid from R to C at position 84.
+The protein's natural variant, known as in VWS1; abrogates DNA binding, features a modification of the amino acid from R to G at position 84.
+The protein's natural variant, known as in PPS; abrogates DNA binding;, features a modification of the amino acid from R to H at position 84.
+The protein's natural variant, known as in PPS;, features a modification of the amino acid from R to L at position 84.
+The protein's natural variant, known as in VWS1, features a modification of the amino acid from N to H at position 88.
+The protein's natural variant, known as in PPS; abrogates DNA binding, features a modification of the amino acid from K to E at position 89.
+The protein's natural variant, known as in VWS1, features a modification of the amino acid from S to G at position 90.
+The protein's natural variant, known as in VWS1; abrogates DNA binding;, features a modification of the amino acid from D to H at position 98.
+The protein's natural variant, known as in VWS1, features a modification of the amino acid from T to A at position 100.
+The protein's natural variant, known as in VWS1;, features a modification of the amino acid from R to Q at position 250.
+The protein's natural variant, known as in VWS1, features a modification of the amino acid from L to P at position 251.
+The protein's natural variant, known as in VWS1, features a modification of the amino acid from Q to R at position 273.
+The protein's natural variant, known as 3% in European-descended and 22% in Asian populations; responsible for 12% of the genetic contribution to cleft lip or palate; tripled the risk of recurrence in families that already had 1 affected child;, features a modification of the amino acid from V to I at position 274.
+The protein's natural variant, known as in VWS1, features a modification of the amino acid from FTSKLLD to L at position 296.
+The protein's natural variant, known as in VWS1, features a modification of the amino acid from L to P at position 294.
+The protein's natural variant, known as in VWS1;, features a modification of the amino acid from V to I at position 297.
+The protein's natural variant, known as in VWS1, features a modification of the amino acid from K to E at position 320.
+The protein's natural variant, known as in VWS1, features a modification of the amino acid from V to M at position 321.
+The protein's natural variant, known as in VWS1, features a modification of the amino acid from G to E at position 325.
+The protein's natural variant, known as in VWS1;, features a modification of the amino acid from R to I at position 339.
+The protein's natural variant, known as in VWS1, features a modification of the amino acid from L to P at position 345.
+The protein's natural variant, known as in VWS1, features a modification of the amino acid from C to F at position 347.
+The protein's natural variant, known as in VWS1, features a modification of the amino acid from E to V at position 349.
+The protein's natural variant, known as in VWS1 and OFC6;, features a modification of the amino acid from F to S at position 369.
+The protein's natural variant, known as in VWS1, features a modification of the amino acid from C to W at position 374.
+The protein's natural variant, known as in VWS1, features a modification of the amino acid from K to E at position 388.
+The protein's natural variant, known as in VWS1;, features a modification of the amino acid from P to S at position 396.
+The protein's natural variant, known as in VWS1;, features a modification of the amino acid from R to W at position 400.
+The protein's natural variant, known as in PPS; significant decrease of transcriptional activity;, features a modification of the amino acid from S to L at position 424.
+The protein's natural variant, known as in PPS, features a modification of the amino acid from D to N at position 430.
+The protein's natural variant, known as in PPS; unknown pathological significance;, features a modification of the amino acid from L to P at position 439.
+The protein's natural variant, known as in PHA;, features a modification of the amino acid from P to L at position 119.
+The protein's natural variant, known as in REYNS;, features a modification of the amino acid from R to C at position 372.
+The protein's natural variant, known as in GRBGD; significant reduction in affinity for NADPH; loss of cholesterol biosynthesis; does not affect protein stability;, features a modification of the amino acid from N to D at position 547.
+The protein's natural variant, known as in SKPHA; unknown pathological significance;, features a modification of the amino acid from N to S at position 547.
+The protein's natural variant, known as in PHA;, features a modification of the amino acid from P to R at position 569.
+The protein's natural variant, known as in GRBGD; significant reduction in affinity for NADPH; loss of cholesterol biosynthesis; does not affect protein stability;, features a modification of the amino acid from R to Q at position 583.
+The protein's natural variant, known as in SKPHA; unknown pathological significance;, features a modification of the amino acid from R to H at position 586.
+The natural variant of this protein is characterized by an amino acid alteration from I to N at position 49.
+The protein's natural variant, known as in JBTS3; loss of localization at cilium basal body and cell-cell junctions;, features a modification of the amino acid from R to L at position 351.
+The protein's natural variant, known as in JBTS3; alters interaction with HAP1 and NPHP1; loss of NPHP1AHI1(2):NPHP1(2) tetramers; loss of localization at cilium basal body and cell-cell junctions; loss of positive modulation of classical Wnt signaling; decreased interaction with CTNNB1;, features a modification of the amino acid from V to D at position 443.
+The protein's natural variant, known as in JBTS3;, features a modification of the amino acid from T to I at position 671.
+The protein's natural variant, known as in JBTS3;, features a modification of the amino acid from D to G at position 719.
+The protein's natural variant, known as in JBTS3; loss of localization at the primary cilium; loss of positive modulation of classical Wnt signaling; no effect on interaction with CTNNB1;, features a modification of the amino acid from R to Q at position 723.
+The protein's natural variant, known as in JBTS3; loss of localization at the primary cilium; loss of positive modulation of classical Wnt signaling; no effect on interaction with CTNNB1;, features a modification of the amino acid from H to R at position 896.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to Q at position 28.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from L to P at position 276.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from V to A at position 901.
+The protein's natural variant, known as in strain: Black Langshan, features a modification of the amino acid from S to P at position 34.
+The protein's natural variant, known as in strain: Dun, features a modification of the amino acid from A to V at position 35.
+The protein's natural variant, known as in strain: Dun, features a modification of the amino acid from G to S at position 96.
+The protein's natural variant, known as in strain: Broiler, features a modification of the amino acid from A to V at position 232.
+The protein's natural variant, known as in strain: Dun and Red jungle fowl, features a modification of the amino acid from D to N at position 399.
+The protein's natural variant, known as in strain: Broiler, features a modification of the amino acid from G to GPTAA at position 495.
+The protein's natural variant, known as in strain: Dun and Red jungle fowl, features a modification of the amino acid from G to GPTAAATAESIADPTAGATDGDAVGPTAA at position 495.
+The protein's natural variant, known as in strain: Broiler, Dun and Red jungle fowl, features a modification of the amino acid from TA to IV at position 506.
+The protein's natural variant, known as in strain: Broiler, features a modification of the amino acid from E to K at position 558.
+The protein's natural variant, known as in strain: Dun, features a modification of the amino acid from R to C at position 712.
+The protein's natural variant, known as in SRXY1, features a modification of the amino acid from S to L at position 3.
+The protein's natural variant, known as in SRXY1; partial; also in two patients with a Turner syndrome phenotype;, features a modification of the amino acid from S to N at position 18.
+The protein's natural variant, known as in SRXY1;, features a modification of the amino acid from V to A at position 60.
+The protein's natural variant, known as in SRXY1;, features a modification of the amino acid from V to L at position 60.
+The protein's natural variant, known as in SRXY1, features a modification of the amino acid from R to G at position 62.
+The protein's natural variant, known as in SRXY1; alters interaction with DNA and DNA bending;, features a modification of the amino acid from M to I at position 64.
+The protein's natural variant, known as in SRXY1, features a modification of the amino acid from M to R at position 64.
+The protein's natural variant, known as in SRXY1, features a modification of the amino acid from F to V at position 67.
+The protein's natural variant, known as in SRXY1;, features a modification of the amino acid from I to T at position 68.
+The protein's natural variant, known as in SRXY1; localizes mainly in the cytoplasm, features a modification of the amino acid from R to M at position 75.
+The protein's natural variant, known as in SRXY1, features a modification of the amino acid from R to S at position 76.
+The protein's natural variant, known as in SRXY1, features a modification of the amino acid from M to T at position 78.
+The protein's natural variant, known as in SRXY1, features a modification of the amino acid from N to Y at position 87.
+The protein's natural variant, known as in SRXY1;, features a modification of the amino acid from I to M at position 90.
+The protein's natural variant, known as in SRXY1, features a modification of the amino acid from S to G at position 91.
+The protein's natural variant, known as in SRXY1;, features a modification of the amino acid from G to E at position 95.
+The protein's natural variant, known as in SRXY1;, features a modification of the amino acid from G to R at position 95.
+The protein's natural variant, known as in SRXY1, features a modification of the amino acid from L to H at position 101.
+The protein's natural variant, known as in SRXY1;, features a modification of the amino acid from K to I at position 106.
+The protein's natural variant, known as in SRXY1, features a modification of the amino acid from P to R at position 108.
+The protein's natural variant, known as in SRXY1;, features a modification of the amino acid from F to S at position 109.
+The protein's natural variant, known as in SRXY1;, features a modification of the amino acid from A to T at position 113.
+The protein's natural variant, known as in SRXY1, features a modification of the amino acid from P to L at position 125.
+The protein's natural variant, known as in SRXY1;, features a modification of the amino acid from Y to C at position 127.
+The protein's natural variant, known as in SRXY1;, features a modification of the amino acid from Y to F at position 127.
+The protein's natural variant, known as in SRXY1, features a modification of the amino acid from P to R at position 131.
+The protein's natural variant, known as in SRXY1;, features a modification of the amino acid from R to W at position 133.
+The natural variant of this protein is characterized by an amino acid alteration from K to N at position 2.
+The natural variant of this protein is characterized by an amino acid alteration from V to L at position 5.
+The natural variant of this protein is characterized by an amino acid alteration from P to S at position 85.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to W at position 165.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from E to D at position 379.
+The protein's natural variant, known as in DKCB8; decreased interaction with TERF2, features a modification of the amino acid from L to F at position 142.
+The protein's natural variant, known as in DKCB8; decreased interaction with TERF2, features a modification of the amino acid from L to S at position 142.
+The protein's natural variant, known as in strain: N16961, features a modification of the amino acid from S to F at position 453.
+The protein's natural variant, known as in SEMDG;, features a modification of the amino acid from H to N at position 29.
+The protein's natural variant, known as in SEMDG;, features a modification of the amino acid from G to V at position 133.
+The protein's natural variant, known as in SEMDG;, features a modification of the amino acid from R to H at position 151.
+The protein's natural variant, known as in SEMDG;, features a modification of the amino acid from Y to H at position 188.
+The protein's natural variant, known as in SEMDG;, features a modification of the amino acid from P to L at position 189.
+The protein's natural variant, known as in SEMDG;, features a modification of the amino acid from R to C at position 237.
+The protein's natural variant, known as in SEMDG, features a modification of the amino acid from I to II at position 327.
+The natural variant of this protein is characterized by an amino acid alteration from Y to F at position 415.
+The natural variant of this protein is characterized by an amino acid alteration from Q to H at position 681.
+The protein's natural variant, known as in SCN4; complete loss of activity;, features a modification of the amino acid from P to L at position 44.
+The protein's natural variant, known as in SCN4; complete loss of activity; purified neutrophils from patients have higher levels of spontaneous and staurosporine-induced apoptosis than controls;, features a modification of the amino acid from P to S at position 44.
+The protein's natural variant, known as in SCN4;, features a modification of the amino acid from W to R at position 59.
+The protein's natural variant, known as in SCN4; complete loss of activity;, features a modification of the amino acid from M to I at position 116.
+The protein's natural variant, known as in SCN4; the patient also carries mutation Thr-166 in ELANE; complete loss of activity, features a modification of the amino acid from M to K at position 116.
+The protein's natural variant, known as in SCN4; complete loss of activity, features a modification of the amino acid from M to T at position 116.
+The protein's natural variant, known as in DURSS and SCN4; complete loss of activity;, features a modification of the amino acid from M to V at position 116.
+The protein's natural variant, known as in SCN4; complete loss of activity;, features a modification of the amino acid from T to R at position 118.
+The protein's natural variant, known as in SCN4; partial loss of activity, features a modification of the amino acid from S to I at position 139.
+The protein's natural variant, known as in SCN4; complete loss of activity, features a modification of the amino acid from L to P at position 154.
+The protein's natural variant, known as in SCN4; complete loss of activity;, features a modification of the amino acid from R to Q at position 161.
+The protein's natural variant, known as in SCN4; complete loss of activity;, features a modification of the amino acid from L to P at position 185.
+The protein's natural variant, known as in SCN4; partial loss of activity;, features a modification of the amino acid from R to Q at position 189.
+The protein's natural variant, known as in SCN4; complete loss of activity, features a modification of the amino acid from L to R at position 208.
+The protein's natural variant, known as in SCN4;, features a modification of the amino acid from R to C at position 253.
+The protein's natural variant, known as in SCN4; complete loss of activity; peripheral-blood patient neutrophils have an increased rate of spontaneous apoptosis; transmission electron microscopy of patient bone marrow cells shows an enlarged rough endoplasmic reticulum in myeloid progenitor cells consistent with increased ER stress;, features a modification of the amino acid from R to H at position 253.
+The protein's natural variant, known as in SCN4; complete loss of activity, features a modification of the amino acid from G to D at position 260.
+The protein's natural variant, known as in SCN4; complete loss of activity;, features a modification of the amino acid from G to R at position 260.
+The protein's natural variant, known as in SCN4;, features a modification of the amino acid from G to R at position 262.
+The protein's natural variant, known as in SCN4, features a modification of the amino acid from L to R at position 325.
+The protein's natural variant, known as in CONDBA; increased RNA polymerase I core element sequence-specific DNA binding; increased transcription from RNA polymerase I promoter;, features a modification of the amino acid from E to K at position 210.
+The natural variant of this protein is characterized by an amino acid alteration from P to PP at position 19.
+The natural variant of this protein is characterized by an amino acid alteration from P to R at position 19.
+The natural variant of this protein is characterized by an amino acid alteration from F to Y at position 337.
+The protein's natural variant, known as 16% of the population; infertile and fertile individuals;, features a modification of the amino acid from A to V at position 10.
+The protein's natural variant, known as in fertile and infertile individuals, features a modification of the amino acid from I to T at position 34.
+The protein's natural variant, known as in fertile and infertile individuals;, features a modification of the amino acid from S to R at position 125.
+The protein's natural variant, known as in ACFD;, features a modification of the amino acid from P to L at position 46.
+The protein's natural variant, known as in BDA1; decreases the stability of the indian hedgehog protein N-product;, features a modification of the amino acid from E to K at position 95.
+The protein's natural variant, known as in BDA1; decreases the stability of the indian hedgehog protein N-product;, features a modification of the amino acid from D to E at position 100.
+The protein's natural variant, known as in BDA1; decreases the stability of the indian hedgehog protein N-product;, features a modification of the amino acid from D to N at position 100.
+The protein's natural variant, known as in BDA1; no effect on the stability of the indian hedgehog protein N-product;, features a modification of the amino acid from E to K at position 131.
+The protein's natural variant, known as in ACFD;, features a modification of the amino acid from V to A at position 190.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation, features a modification of the amino acid from P to T at position 20.
+The protein's natural variant, known as in a lung small cell carcinoma sample; somatic mutation, features a modification of the amino acid from S to Y at position 392.
+The protein's natural variant, known as in strain: Tw-5/OT and APa-2, features a modification of the amino acid from M to V at position 249.
+The protein's natural variant, known as in strain: BOUR, features a modification of the amino acid from I to V at position 321.
+The natural variant of this protein is characterized by an amino acid alteration from T to TKLLSPAYSWDLAFSPPPQIQYVKVAHDSQRKL at position 276.
+The protein's natural variant, known as in 40% of the molecules, features a modification of the amino acid from I to V at position 15.
+The protein's natural variant, known as in 50% of the molecules, features a modification of the amino acid from S to G at position 17.
+The protein's natural variant, known as in CFDD;, features a modification of the amino acid from V to G at position 213.
+The protein's natural variant, known as in CFDD;, features a modification of the amino acid from C to R at position 214.
+The protein's natural variant, known as in toxin 11A, features a modification of the amino acid from F to Y at position 10.
+The protein's natural variant, known as in strain: CWL029 and TW-183, features a modification of the amino acid from I to V at position 1134.
+The protein's natural variant, known as in isoform B, features a modification of the amino acid from G to R at position 22.
+The natural variant of this protein is characterized by an amino acid alteration from G to E at position 47.
+The natural variant of this protein is characterized by an amino acid alteration from M to V at position 52.
+The natural variant of this protein is characterized by an amino acid alteration from R to I at position 71.
+The protein's natural variant, known as in PLCA2, features a modification of the amino acid from S to F at position 489.
+The natural variant of this protein is characterized by an amino acid alteration from L to P at position 109.
+The natural variant of this protein is characterized by an amino acid alteration from H to P at position 292.
+The natural variant of this protein is characterized by an amino acid alteration from H to Q at position 292.
+The protein's natural variant, known as in a glioblastoma multiforme sample; somatic mutation, features a modification of the amino acid from V to A at position 793.
+The natural variant of this protein is characterized by an amino acid alteration from D to E at position 1030.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation, features a modification of the amino acid from K to E at position 1044.
+The protein's natural variant, known as in DEE14;, features a modification of the amino acid from G to S at position 269.
+The protein's natural variant, known as in ENFL5;, features a modification of the amino acid from R to Q at position 379.
+The protein's natural variant, known as in DEE14; gain-of-function mutation;, features a modification of the amino acid from R to Q at position 409.
+The protein's natural variant, known as in DEE14;, features a modification of the amino acid from R to H at position 455.
+The protein's natural variant, known as in DEE14;, features a modification of the amino acid from M to V at position 497.
+The protein's natural variant, known as in DEE14; unknown pathological significance;, features a modification of the amino acid from T to I at position 562.
+The protein's natural variant, known as in DEE14;, features a modification of the amino acid from I to M at position 741.
+The protein's natural variant, known as in ENFL5;, features a modification of the amino acid from Y to H at position 777.
+The protein's natural variant, known as in ENFL5;, features a modification of the amino acid from M to I at position 877.
+The protein's natural variant, known as in DEE14; unknown pathological significance, features a modification of the amino acid from M to K at position 877.
+The protein's natural variant, known as in ENFL5;, features a modification of the amino acid from R to C at position 909.
+The protein's natural variant, known as in DEE14; gain-of-function mutation;, features a modification of the amino acid from A to T at position 915.
+The protein's natural variant, known as in DEE14;, features a modification of the amino acid from K to E at position 928.
+The protein's natural variant, known as in DEE14; variant homologue in rat has increased channel activity upon positive potentials;, features a modification of the amino acid from A to T at position 947.
+The protein's natural variant, known as in DEE14; unknown pathological significance;, features a modification of the amino acid from R to Q at position 1088.
+The protein's natural variant, known as in NS7;, features a modification of the amino acid from T to M at position 241.
+The protein's natural variant, known as in CFC1 and LPRD3;, features a modification of the amino acid from T to P at position 241.
+The protein's natural variant, known as in NS7;, features a modification of the amino acid from T to R at position 241.
+The protein's natural variant, known as in CFC1;, features a modification of the amino acid from T to P at position 244.
+The protein's natural variant, known as in CFC1;, features a modification of the amino acid from L to F at position 245.
+The protein's natural variant, known as in CFC1;, features a modification of the amino acid from A to P at position 246.
+The protein's natural variant, known as in CFC1;, features a modification of the amino acid from Q to R at position 257.
+The protein's natural variant, known as in CFC1;, features a modification of the amino acid from Q to K at position 262.
+The protein's natural variant, known as in CFC1, features a modification of the amino acid from E to K at position 275.
+The protein's natural variant, known as in CRC;, features a modification of the amino acid from R to I at position 462.
+The protein's natural variant, known as in CRC;, features a modification of the amino acid from I to S at position 463.
+The protein's natural variant, known as in CRC;, features a modification of the amino acid from G to E at position 464.
+The protein's natural variant, known as in a colorectal cancer cell line; elevated kinase activity; efficiently induces cell transformation;, features a modification of the amino acid from G to V at position 464.
+The protein's natural variant, known as in melanoma;, features a modification of the amino acid from G to A at position 466.
+The protein's natural variant, known as in melanoma;, features a modification of the amino acid from G to E at position 466.
+The protein's natural variant, known as in LNCR;, features a modification of the amino acid from G to V at position 466.
+The protein's natural variant, known as in CFC1;, features a modification of the amino acid from S to A at position 467.
+The protein's natural variant, known as in CFC1;, features a modification of the amino acid from F to S at position 468.
+The protein's natural variant, known as in NHL; also in a lung adenocarcinoma sample; somatic mutation; elevated kinase activity; efficiently induces cell transformation;, features a modification of the amino acid from G to A at position 469.
+The protein's natural variant, known as in CFC1 and colon cancer;, features a modification of the amino acid from G to E at position 469.
+The protein's natural variant, known as in NHL;, features a modification of the amino acid from G to R at position 469.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from G to V at position 469.
+The protein's natural variant, known as in CFC1;, features a modification of the amino acid from L to F at position 485.
+The protein's natural variant, known as in CFC1;, features a modification of the amino acid from K to E at position 499.
+The protein's natural variant, known as in CFC1;, features a modification of the amino acid from K to N at position 499.
+The protein's natural variant, known as in CFC1;, features a modification of the amino acid from E to G at position 501.
+The protein's natural variant, known as in CFC1;, features a modification of the amino acid from E to K at position 501.
+The protein's natural variant, known as in CFC1;, features a modification of the amino acid from L to P at position 525.
+The protein's natural variant, known as in NS7;, features a modification of the amino acid from W to C at position 531.
+The protein's natural variant, known as in CFC1, features a modification of the amino acid from N to D at position 580.
+The protein's natural variant, known as in CFC1;, features a modification of the amino acid from N to D at position 581.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from N to S at position 581.
+The protein's natural variant, known as in ovarian cancer;, features a modification of the amino acid from E to K at position 586.
+The protein's natural variant, known as in NHL;, features a modification of the amino acid from D to G at position 594.
+The protein's natural variant, known as in CFC1; also found in colon cancer;, features a modification of the amino acid from F to L at position 595.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from G to R at position 596.
+The protein's natural variant, known as in CFC1;, features a modification of the amino acid from G to V at position 596.
+The protein's natural variant, known as in LNCR; also found in an ovarian serous carcinoma sample; somatic mutation;, features a modification of the amino acid from L to R at position 597.
+The protein's natural variant, known as in NS7; also in a lung adenocarcinoma sample; somatic mutation; elevated kinase activity; efficiently induces cell transformation;, features a modification of the amino acid from L to V at position 597.
+The protein's natural variant, known as in CFC1;, features a modification of the amino acid from T to R at position 599.
+The protein's natural variant, known as in a melanoma cell line; requires 2 nucleotide substitutions;, features a modification of the amino acid from V to D at position 600.
+The protein's natural variant, known as in CRC; also found in sarcoma, metastatic melanoma, ovarian serous carcinoma, pilocytic astrocytoma; somatic mutation; most common mutation; constitutive and elevated kinase activity; efficiently induces cell transformation; suppression of mutation in melanoma causes growth arrest and promotes apoptosis; loss of regulation by PMRT5;, features a modification of the amino acid from V to E at position 600.
+The protein's natural variant, known as in CRC;, features a modification of the amino acid from K to E at position 601.
+The protein's natural variant, known as in CFC1;, features a modification of the amino acid from K to Q at position 601.
+The protein's natural variant, known as in CFC1;, features a modification of the amino acid from D to E at position 638.
+The protein's natural variant, known as in CFC1;, features a modification of the amino acid from Q to R at position 709.
+The protein's natural variant, known as in BARTS5; loss of interaction with GNAS;, features a modification of the amino acid from R to C at position 446.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from K to Q at position 458.
+The protein's natural variant, known as in Wpk, features a modification of the amino acid from P to L at position 389.
+The protein's natural variant, known as in ADWH; results in disruption of keratin intermediate filament formation in cultured cells;, features a modification of the amino acid from N to K at position 148.
+The protein's natural variant, known as in ECTD7; autosomal recessive;, features a modification of the amino acid from F to S at position 274.
+The protein's natural variant, known as in HYPT3;, features a modification of the amino acid from D to N at position 482.
+The protein's natural variant, known as in Gl-8; requires 2 nucleotide substitutions, features a modification of the amino acid from P to C at position 53.
+The protein's natural variant, known as probable disease-associated variant found in patients with undefined congenital myopathy;, features a modification of the amino acid from D to V at position 2.
+The protein's natural variant, known as in NEM4, features a modification of the amino acid from A to G at position 3.
+The protein's natural variant, known as in NEM4;, features a modification of the amino acid from D to V at position 14.
+The protein's natural variant, known as in NEM4; also found in a patient with congenital myopathy with fiber-type disproportion and patients with undefined congenital myopathy;, features a modification of the amino acid from E to K at position 41.
+The protein's natural variant, known as in CAPM2, features a modification of the amino acid from G to GG at position 52.
+The protein's natural variant, known as in DA1A;, features a modification of the amino acid from R to G at position 91.
+The protein's natural variant, known as probable disease-associated variant found in patients with undefined congenital myopathy;, features a modification of the amino acid from Q to H at position 93.
+The protein's natural variant, known as in DA1A;, features a modification of the amino acid from Q to R at position 93.
+The protein's natural variant, known as in DA2B4; unknown pathological significance;, features a modification of the amino acid from Q to R at position 103.
+The protein's natural variant, known as in NEM4, features a modification of the amino acid from E to A at position 117.
+The protein's natural variant, known as in DA1A; also found in a patient with congenital myopathy with fiber-type disproportion;, features a modification of the amino acid from E to K at position 117.
+The protein's natural variant, known as probable disease-associated variant found in a patient with congenital myopathy with fiber-type disproportion and patients with undefined congenital myopathy;, features a modification of the amino acid from K to E at position 128.
+The protein's natural variant, known as probable disease-associated variant found in a patient with congenital myopathy with fiber-type disproportion and patients with undefined congenital myopathy;, features a modification of the amino acid from R to P at position 133.
+The protein's natural variant, known as in DA2B4, NEM4 and DA1A; also found in a patient with congenital myopathy with fiber-type disproportion;, features a modification of the amino acid from R to W at position 133.
+The protein's natural variant, known as in NEM4; also found in a patient with congenital myopathy with fiber-type disproportion, features a modification of the amino acid from L to P at position 143.
+The protein's natural variant, known as in NEM4;, features a modification of the amino acid from Q to P at position 147.
+The protein's natural variant, known as in NEM4; also found in a patient with congenital myopathy with fiber-type disproportion, features a modification of the amino acid from L to P at position 148.
+The protein's natural variant, known as probable disease-associated variant found in patients with undefined congenital myopathy;, features a modification of the amino acid from A to T at position 155.
+The protein's natural variant, known as in CAPM2;, features a modification of the amino acid from N to K at position 202.
+The protein's natural variant, known as in DA1A; also found in patients with undefined congenital myopathy;, features a modification of the amino acid from Y to C at position 261.
+The protein's natural variant, known as in STSL2; unknown pathological significance, features a modification of the amino acid from M to R at position 99.
+The protein's natural variant, known as in STSL2; decreased maturation of glycan chains;, features a modification of the amino acid from E to Q at position 146.
+The protein's natural variant, known as in STSL2; loss of normal maturation of glycan chains;, features a modification of the amino acid from R to H at position 389.
+The protein's natural variant, known as in STSL2; loss of normal maturation of glycan chains;, features a modification of the amino acid from R to H at position 419.
+The protein's natural variant, known as in STSL2; strongly decreased maturation of glycan chains;, features a modification of the amino acid from R to P at position 419.
+The protein's natural variant, known as in STSL2; loss of normal maturation of glycan chains;, features a modification of the amino acid from N to K at position 437.
+The protein's natural variant, known as in STSL2, features a modification of the amino acid from R to S at position 550.
+The protein's natural variant, known as in NICCD;, features a modification of the amino acid from E to K at position 601.
+The protein's natural variant, known as in strain: Eagan, features a modification of the amino acid from A to G at position 60.
+The protein's natural variant, known as in strain: NC350 and NC358, features a modification of the amino acid from K to N at position 27.
+The protein's natural variant, known as in strain: Canton-S, features a modification of the amino acid from S to T at position 144.
+The protein's natural variant, known as in strain: Canton-S, features a modification of the amino acid from W to C at position 149.
+The protein's natural variant, known as in strain: Australia 2, Kenya 38, Kenya 43, Peru and USA 3, features a modification of the amino acid from S to T at position 154.
+The protein's natural variant, known as in strain: Australia 5, features a modification of the amino acid from M to I at position 198.
+The protein's natural variant, known as in strain: Japan, features a modification of the amino acid from N to Y at position 236.
+The protein's natural variant, known as in strain: Australia 5 and USA 1, features a modification of the amino acid from Y to F at position 273.
+The protein's natural variant, known as in hscy, features a modification of the amino acid from C to F at position 161.
+The protein's natural variant, known as in strain: SK1 and YJM421, features a modification of the amino acid from N to S at position 41.
+The protein's natural variant, known as in strain: SK1 and YJM421, features a modification of the amino acid from I to T at position 112.
+The protein's natural variant, known as in strain: SK1, YJM320, YJM339 and YJM421, features a modification of the amino acid from F to V at position 384.
+The protein's natural variant, known as in strain: YJM320, features a modification of the amino acid from E to V at position 392.
+The protein's natural variant, known as in strain: SK1, YJM320, YJM339 and YJM421, features a modification of the amino acid from T to S at position 400.
+The protein's natural variant, known as in strain: YJM320 and YJM421, features a modification of the amino acid from A to S at position 401.
+The protein's natural variant, known as in strain: SK1, YJM320, YJM339 and YJM421, features a modification of the amino acid from T to TCEGT at position 416.
+The protein's natural variant, known as in strain: EAY1068, features a modification of the amino acid from D to Y at position 458.
+The protein's natural variant, known as in strain: YJM339, features a modification of the amino acid from D to N at position 475.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from Y to F at position 513.
+The protein's natural variant, known as in strain: YJM320, features a modification of the amino acid from A to V at position 564.
+The protein's natural variant, known as in strain: YJM320, features a modification of the amino acid from K to R at position 768.
+The protein's natural variant, known as in strain: SK1 and YJM320; forms a non-functional heterodimer with MHL1 from strain S288c, resulting in an accumulation of mutations in spore progeny of crosses between these strains, features a modification of the amino acid from R to K at position 818.
+The protein's natural variant, known as in NPHP18; does not affect interaction with CEP164 and IFT20, features a modification of the amino acid from L to P at position 87.
+The protein's natural variant, known as in NPHP18; does not interact with CEP164 and IFT20;, features a modification of the amino acid from R to P at position 511.
+The protein's natural variant, known as in ALS21; unknown pathological significance, features a modification of the amino acid from A to T at position 72.
+The protein's natural variant, known as in ALS21; results in increased interaction with TARDBP;, features a modification of the amino acid from S to C at position 85.
+The protein's natural variant, known as in ALS21;, features a modification of the amino acid from F to C at position 115.
+The protein's natural variant, known as in ALS21; unknown pathological significance, features a modification of the amino acid from R to W at position 147.
+The protein's natural variant, known as in ALS21; unknown pathological significance;, features a modification of the amino acid from P to S at position 154.
+The protein's natural variant, known as in ALS21;, features a modification of the amino acid from T to A at position 622.
+The protein's natural variant, known as in strain: 10901, features a modification of the amino acid from I to T at position 29.
+The protein's natural variant, known as in strain: Chevalieri / ATCC 10604, features a modification of the amino acid from P to S at position 141.
+The protein's natural variant, known as no effect on sulfotransferase activity, features a modification of the amino acid from R to C at position 144.
+The protein's natural variant, known as decreases levels of sulfotransferase activity; accelerates proteasome-dependent degradation, features a modification of the amino acid from K to N at position 234.
+The protein's natural variant, known as in strain: cv. Baekmibaekdadagi, features a modification of the amino acid from YIY to FFF at position 1354.
+The protein's natural variant, known as in strain: cv. Baekmibaekdadagi, features a modification of the amino acid from YI to FF at position 1372.
+The protein's natural variant, known as in strain: cv. Baekmibaekdadagi, features a modification of the amino acid from E to K at position 1384.
+The protein's natural variant, known as in strain: cv. Baekmibaekdadagi, features a modification of the amino acid from YKY to FKS at position 1389.
+The protein's natural variant, known as in strain: cv. Baekmibaekdadagi, features a modification of the amino acid from R to K at position 1421.
+The protein's natural variant, known as in strain: cv. Baekmibaekdadagi, features a modification of the amino acid from R to K at position 1435.
+The protein's natural variant, known as in strain: cv. Baekmibaekdadagi, features a modification of the amino acid from R to Q at position 1448.
+The protein's natural variant, known as in strain: cv. Baekmibaekdadagi, features a modification of the amino acid from R to K at position 1451.
+The protein's natural variant, known as in allelic sequence, features a modification of the amino acid from E to K at position 7.
+The protein's natural variant, known as in allelic sequence, features a modification of the amino acid from A to S at position 10.
+The protein's natural variant, known as in allelic sequence, features a modification of the amino acid from G to D at position 70.
+The natural variant of this protein is characterized by an amino acid alteration from V to A at position 60.
+The protein's natural variant, known as in a glioma cell line;, features a modification of the amino acid from G to E at position 162.
+The natural variant of this protein is characterized by an amino acid alteration from Q to L at position 337.
+The natural variant of this protein is characterized by an amino acid alteration from R to G at position 364.
+The protein's natural variant, known as in a glioma sample; glioblastoma multiforme; somatic mutation;, features a modification of the amino acid from Q to H at position 420.
+The protein's natural variant, known as in a glioma cell line;, features a modification of the amino acid from N to S at position 546.
+The protein's natural variant, known as in a glioma sample; pilocytic astrocytoma, features a modification of the amino acid from G to V at position 607.
+The protein's natural variant, known as found in a consanguineous family with intellectual disability; unknown pathological significance;, features a modification of the amino acid from T to R at position 969.
+The natural variant of this protein is characterized by an amino acid alteration from R to W at position 1434.
+The protein's natural variant, known as requires 2 nucleotide substitutions, features a modification of the amino acid from H to S at position 1732.
+The natural variant of this protein is characterized by an amino acid alteration from T to P at position 1961.
+The protein's natural variant, known as found in non-small cell lung cancer; somatic mutation; reduced localization to chromatin; reduced histone deacetylase activity; does not affect the protein-lysine demyristoylase activity;, features a modification of the amino acid from D to N at position 25.
+The protein's natural variant, known as found in kidney cancer; somatic mutation; reduced histone deacetylase activity; does not affect the protein-lysine demyristoylase activity, features a modification of the amino acid from E to V at position 36.
+The protein's natural variant, known as does not affect histone deacetylase activity;, features a modification of the amino acid from S to N at position 46.
+The protein's natural variant, known as found in a family presenting with four cases of perinatal lethality caused by severe neurodevelopmental and cardiac anomalies; abolished histone deacetylase activity; abolished protein demyristoylase activity; decreased ability to recognize and bind double-strand breaks (DSBs) sites; does not affect nuclear localization;, features a modification of the amino acid from D to H at position 63.
+The protein's natural variant, known as found in non-small cell lung cancer; somatic mutation; does not affect ability to recognize and bind double-strand breaks (DSBs) sites; strongly reduced histone deacetylase activity; strongly reduced the protein-lysine demyristoylase activity, features a modification of the amino acid from D to Y at position 63.
+The protein's natural variant, known as found in non-small cell lung cancer; somatic mutation; reduced histone deacetylase activity; does not affect the protein-lysine demyristoylase activity, features a modification of the amino acid from A to S at position 89.
+The protein's natural variant, known as found in non-small cell lung cancer; somatic mutation; reduced localization to chromatin; strongly reduced histone deacetylase activity; strongly reduced the protein-lysine demyristoylase activity;, features a modification of the amino acid from D to N at position 116.
+The protein's natural variant, known as found in cervical cancer; somatic mutation; reduced histone deacetylase activity; slightly reduced the protein-lysine demyristoylase activity;, features a modification of the amino acid from T to P at position 263.
+The protein's natural variant, known as found in melanoma; somatic mutation; reduced histone deacetylase activity; does not affect the protein-lysine demyristoylase activity, features a modification of the amino acid from P to L at position 274.
+The protein's natural variant, known as in CMH8;, features a modification of the amino acid from E to G at position 56.
+The protein's natural variant, known as in CMH8; autosomal recessive;, features a modification of the amino acid from E to K at position 143.
+The protein's natural variant, known as in CMH8; with mid-left ventricular chamber thickening;, features a modification of the amino acid from M to V at position 149.
+The protein's natural variant, known as in CMH8; with mid-left ventricular chamber thickening;, features a modification of the amino acid from R to H at position 154.
+The protein's natural variant, known as in CMH8;, features a modification of the amino acid from E to G at position 177.
+The natural variant of this protein is characterized by an amino acid alteration from E to A at position 117.
+The protein's natural variant, known as in allele SED1-2, features a modification of the amino acid from T to TSTEAPTTDTTSEAPTTAIPTNG at position 94.
+The protein's natural variant, known as in allele SED1-5, features a modification of the amino acid from T to TSTEAPTTDTTTEAPTTAIPTNG at position 94.
+The protein's natural variant, known as in allele SED1-3 and SED1-6, features a modification of the amino acid from T to TSTEAPTTDTTTEAPTTALPTNGTSTEAPTDTTTEAPTTALPTNG at position 94.
+The protein's natural variant, known as in allele SED1-4, SED1-5 and SED1-6, features a modification of the amino acid from P to PTTTSTTEYTVVTEYTTYCPEPTTFTTNGKTYTVTEPTTLTITDCPCTIEK at position 212.
+The protein's natural variant, known as in allele SED1-7, features a modification of the amino acid from P to PTTTSTTEYTVVTEYTTYCPEPTTFTTNGKTYTVTEPTTLTITDCPCTIEKPTTTSTTEYTVVTEYTTYCPEPTTFTTNGKTYTVTEPTTLTITDCPCTIEK at position 212.
+The natural variant of this protein is characterized by an amino acid alteration from P to H at position 27.
+The protein's natural variant, known as associated with increased levels of soluble IL6RB in blood serum;, features a modification of the amino acid from G to R at position 148.
+The protein's natural variant, known as found in patient with lung cancer; unknown pathological significance;, features a modification of the amino acid from A to G at position 200.
+The protein's natural variant, known as in HIES4B; results in defective cytokine-mediated signaling pathway with loss of response to IL-6, IL-11, IL-27, OSM but not LIF, features a modification of the amino acid from N to Y at position 404.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from T to I at position 415.
+The protein's natural variant, known as in HIES4B; results in defective cytokine-mediated signaling pathway, features a modification of the amino acid from P to L at position 498.
+The protein's natural variant, known as in HIES4B; results in impaired cytokine-mediated signaling pathway with loss of response to IL-6, IL-11, IL-27 and reduced response to OSM, CNTF and LIF, features a modification of the amino acid from A to P at position 517.
+The protein's natural variant, known as in AI1H;, features a modification of the amino acid from A to T at position 143.
+The protein's natural variant, known as in AI1H;, features a modification of the amino acid from P to T at position 196.
+The protein's natural variant, known as in AI1H;, features a modification of the amino acid from H to Q at position 275.
+The protein's natural variant, known as in strain: Isolate 1, features a modification of the amino acid from V to I at position 118.
+The protein's natural variant, known as in strain: Isolate 1, features a modification of the amino acid from A to V at position 238.
+The protein's natural variant, known as no effect on affinity for testosterone; no effect on affinity for NADPH; no effect on Vmax;, features a modification of the amino acid from C to R at position 5.
+The protein's natural variant, known as increased affinity for testosterone; increased affinity for NADPH; decreased Vmax, features a modification of the amino acid from P to L at position 30.
+The protein's natural variant, known as found in individual with micropenis; unknown pathological significance;, features a modification of the amino acid from G to R at position 34.
+The protein's natural variant, known as increased affinity for testosterone; increased affinity for NADPH; decreased Vmax;, features a modification of the amino acid from P to R at position 48.
+The protein's natural variant, known as increased affinity for testosterone; no effect on affinity for NADPH; increased Vmax;, features a modification of the amino acid from A to T at position 49.
+The protein's natural variant, known as no effect on affinity for testosterone; increased affinity for NADPH; decreased Vmax;, features a modification of the amino acid from A to T at position 51.
+The protein's natural variant, known as in PPSH;, features a modification of the amino acid from L to Q at position 55.
+The protein's natural variant, known as in PPSH;, features a modification of the amino acid from G to D at position 85.
+The protein's natural variant, known as no effect on affinity for testosterone; no effect on affinity for NADPH; increased Vmax;, features a modification of the amino acid from L to V at position 89.
+The protein's natural variant, known as in PPSH;, features a modification of the amino acid from G to D at position 115.
+The protein's natural variant, known as in PPSH;, features a modification of the amino acid from G to R at position 123.
+The protein's natural variant, known as in PPSH;, features a modification of the amino acid from Q to R at position 126.
+The protein's natural variant, known as in PPSH;, features a modification of the amino acid from R to W at position 145.
+The protein's natural variant, known as in PPSH, features a modification of the amino acid from G to R at position 158.
+The protein's natural variant, known as in PPSH;, features a modification of the amino acid from P to L at position 181.
+The protein's natural variant, known as in PPSH;, features a modification of the amino acid from G to S at position 183.
+The protein's natural variant, known as no effect on affinity for testosterone; increased affinity for NADPH; decreased Vmax;, features a modification of the amino acid from T to M at position 187.
+The protein's natural variant, known as no effect on affinity for testosterone; increased affinity for NADPH; increased Vmax;, features a modification of the amino acid from F to L at position 194.
+The protein's natural variant, known as in PPSH;, features a modification of the amino acid from G to S at position 196.
+The protein's natural variant, known as in PPSH;, features a modification of the amino acid from E to D at position 197.
+The protein's natural variant, known as in PPSH;, features a modification of the amino acid from E to K at position 200.
+The protein's natural variant, known as in PPSH;, features a modification of the amino acid from A to D at position 207.
+The protein's natural variant, known as in PPSH;, features a modification of the amino acid from P to R at position 212.
+The protein's natural variant, known as in PPSH; also found in individuals with micropenis; increased affinity for testosterone; increased affinity for NADPH; decreased Vmax;, features a modification of the amino acid from R to Q at position 227.
+The protein's natural variant, known as in PPSH;, features a modification of the amino acid from A to T at position 228.
+The protein's natural variant, known as in PPSH;, features a modification of the amino acid from H to R at position 231.
+The protein's natural variant, known as increased affinity for testosterone; increased affinity for NADPH; decreased Vmax;, features a modification of the amino acid from F to L at position 234.
+The protein's natural variant, known as in PPSH;, features a modification of the amino acid from Y to F at position 235.
+The protein's natural variant, known as in PPSH;, features a modification of the amino acid from S to Y at position 245.
+The protein's natural variant, known as in PPSH;, features a modification of the amino acid from R to Q at position 246.
+The protein's natural variant, known as in PPSH;, features a modification of the amino acid from R to W at position 246.
+The natural variant of this protein is characterized by an amino acid alteration from A to T at position 63.
+The protein's natural variant, known as in strain: PB303, features a modification of the amino acid from S to N at position 132.
+The protein's natural variant, known as in strain: CB4857, features a modification of the amino acid from N to I at position 143.
+The protein's natural variant, known as in strain: AB2, CB4852, CB4853, CB4855, CB4858 and PB306, features a modification of the amino acid from S to N at position 186.
+The protein's natural variant, known as in strain: AB1 and KR314, features a modification of the amino acid from V to M at position 216.
+The protein's natural variant, known as in WARBM3; abnormal endoplasmic reticulum structure; in fibroblasts ER spread away from the perinuclear region into the cell periphery and there is a loss of fragmentation of ER tubules;, features a modification of the amino acid from L to Q at position 24.
+The protein's natural variant, known as in WARBM3; unknown pathological significance, features a modification of the amino acid from T to M at position 95.
+The protein's natural variant, known as in SPGF58; affects subcellular location, instead of being homogenously distributed along the sperm flagellum, concentrates in the proximal part of the flagellum; also affects splicing, features a modification of the amino acid from G to S at position 86.
+The protein's natural variant, known as in JBTS40; partial loss of function; contrary to wild-type, only partially rescues the phenotype of IFT74 knockdown zebrafish; does not affect interaction with IFT81 and IFT27; does not affect protein level;, features a modification of the amino acid from Q to E at position 179.
+The protein's natural variant, known as may be involved in congenital central hypoventilation syndrome;, features a modification of the amino acid from L to R at position 371.
+The protein's natural variant, known as in strain: K8, features a modification of the amino acid from NI to YM at position 30.
+The protein's natural variant, known as in strain: K8, features a modification of the amino acid from R to K at position 38.
+The protein's natural variant, known as found in patients with chronic lymphocytic leukemia; associated with BTK mutation S-481; unknown pathological significance; results in resistance to ibrutinib therapy;, features a modification of the amino acid from R to W at position 665.
+The protein's natural variant, known as in APLAID; results in increased epidermal growth factor-stimulated production of intracellular IP3 and increased intracellular calcium release; is a hypermorphic mutation;, features a modification of the amino acid from S to Y at position 707.
+The protein's natural variant, known as found in patients with chronic lymphocytic leukemia; associated with BTK mutation S-481; unknown pathological significance; results in resistance to ibrutinib therapy;, features a modification of the amino acid from L to F at position 845.
+The protein's natural variant, known as in KTCN1;, features a modification of the amino acid from L to P at position 17.
+The protein's natural variant, known as in KTCN1; unknown pathological significance;, features a modification of the amino acid from L to M at position 159.
+The protein's natural variant, known as in KTCN1; unknown pathological significance;, features a modification of the amino acid from G to D at position 160.
+The protein's natural variant, known as in KTCN1; sporadic;, features a modification of the amino acid from R to W at position 166.
+The protein's natural variant, known as in KTCN1;, features a modification of the amino acid from Q to H at position 175.
+The protein's natural variant, known as in KTCN1; unknown pathological significance;, features a modification of the amino acid from G to R at position 239.
+The protein's natural variant, known as in KTCN1; unknown pathological significance;, features a modification of the amino acid from H to R at position 244.
+The protein's natural variant, known as in KTCN1; unknown pathological significance; also in a patient with retinal dysfunction;, features a modification of the amino acid from P to R at position 247.
+The protein's natural variant, known as in CAASDS;, features a modification of the amino acid from A to S at position 256.
+The protein's natural variant, known as in CHEDDA, features a modification of the amino acid from H to N at position 1054.
+The protein's natural variant, known as in CHEDDA, features a modification of the amino acid from H to Y at position 1058.
+The protein's natural variant, known as in CHEDDA; unknown pathological significance, features a modification of the amino acid from SH to DL at position 1060.
+The protein's natural variant, known as in CHEDDA; unknown pathological significance, features a modification of the amino acid from SH to NL at position 1060.
+The protein's natural variant, known as in CHEDDA; the mutation resulted in a perturbation of the structural and functional integrity of the HX repeat; altered zinc-binding properties of the HX repeat, features a modification of the amino acid from H to Y at position 1060.
+The protein's natural variant, known as in CHEDDA, features a modification of the amino acid from H to D at position 1062.
+The protein's natural variant, known as in CHEDDA, features a modification of the amino acid from H to R at position 1062.
+The protein's natural variant, known as in CHEDDA, features a modification of the amino acid from L to R at position 1063.
+The protein's natural variant, known as in EVR6; unknown pathological significance; does not affect localization to the nucleus;, features a modification of the amino acid from S to N at position 126.
+The protein's natural variant, known as in EVR6; severely decreased localization to the nucleus;, features a modification of the amino acid from H to Y at position 455.
+The protein's natural variant, known as in RP72; decreased localization to the nucleus;, features a modification of the amino acid from R to C at position 541.
+The natural variant of this protein is characterized by an amino acid alteration from Q to K at position 583.
+The protein's natural variant, known as in SPG33; no effect on its function in the regulation of ER morphology and stability, no effect on its localization to ER but according to PubMed:16826525 an aberrant subcellular localization to cell membrane seen, altered interaction with SPAST, increased susceptibility to ER stress, no effect on its interaction with REEP1, REEP5 and ATL1 and increased protein stability;, features a modification of the amino acid from G to V at position 191.
+The protein's natural variant, known as in FSGS2; unknown pathological significance, features a modification of the amino acid from F to FAYMF at position 88.
+The protein's natural variant, known as in FSGS2; increases calcium ion transport, features a modification of the amino acid from G to S at position 109.
+The protein's natural variant, known as in FSGS2; increases calcium ion transport;, features a modification of the amino acid from P to Q at position 112.
+The protein's natural variant, known as in FSGS2; unknown pathological significance; decreases calcium ion transport;, features a modification of the amino acid from N to S at position 125.
+The protein's natural variant, known as in FSGS2; increases cation channel activity; does not change the outward peak current; increases significantly the inward peak current amplitude; increases calcium ion transport;, features a modification of the amino acid from N to S at position 143.
+The protein's natural variant, known as in FSGS2; increases cation channel activity; does not change plasma membrane expression; increases calcium ion transport;, features a modification of the amino acid from R to Q at position 175.
+The protein's natural variant, known as in FSGS2; increases calcium ion transport;, features a modification of the amino acid from H to L at position 218.
+The protein's natural variant, known as in FSGS2;, features a modification of the amino acid from S to T at position 270.
+The protein's natural variant, known as in FSGS2; unknown pathological significance;, features a modification of the amino acid from R to H at position 360.
+The protein's natural variant, known as in FSGS2; unknown pathological significance; requires 2 nucleotide substitutions; decreases calcium ion transport, features a modification of the amino acid from L to A at position 395.
+The protein's natural variant, known as increases calcium ion transport;, features a modification of the amino acid from A to V at position 404.
+The protein's natural variant, known as in FSGS2; decreases calcium ion transport; does not change localization at cell membrane; does not affect homodimer formation, features a modification of the amino acid from G to D at position 757.
+The protein's natural variant, known as in FSGS2; unknown pathological significance; decreases calcium ion transport;, features a modification of the amino acid from L to P at position 780.
+The protein's natural variant, known as in FSGS2; increases cation channel activity; does not change plasma membrane expression; significantly reduces the ratio of cell-surface to total expression; increases calcium ion transport;, features a modification of the amino acid from R to C at position 895.
+The protein's natural variant, known as in FSGS2; decreases calcium ion transport, features a modification of the amino acid from R to L at position 895.
+The protein's natural variant, known as in FSGS2; increases calcium ion transport;, features a modification of the amino acid from E to K at position 897.
+The protein's natural variant, known as in MADB; does not affect enzyme activity;, features a modification of the amino acid from P to L at position 248.
+The protein's natural variant, known as in MADB;, features a modification of the amino acid from N to S at position 265.
+The protein's natural variant, known as in MADB;, features a modification of the amino acid from W to R at position 340.
+The protein's natural variant, known as in strain: cv. PR 261 and cv. RRIM 600, features a modification of the amino acid from N to D at position 342.
+The protein's natural variant, known as in strain: cv. PR 261 and cv. RRIM 600, features a modification of the amino acid from S to G at position 352.
+The protein's natural variant, known as in DFNB42; no effect on interaction with MARVELD2; loss of tight junction location;, features a modification of the amino acid from R to Q at position 97.
+The protein's natural variant, known as in DFNB42; uncertain pathological significance; no effect on interaction with MARVELD2; no effect on tight junction location;, features a modification of the amino acid from R to Q at position 453.
+The protein's natural variant, known as in AN1, features a modification of the amino acid from N to S at position 17.
+The protein's natural variant, known as in AN1, features a modification of the amino acid from G to W at position 18.
+The protein's natural variant, known as in AN1, features a modification of the amino acid from R to P at position 19.
+The protein's natural variant, known as in ASGD5;, features a modification of the amino acid from R to G at position 26.
+The protein's natural variant, known as in AN1, features a modification of the amino acid from I to S at position 29.
+The protein's natural variant, known as in AN1, features a modification of the amino acid from I to V at position 29.
+The protein's natural variant, known as in AN1, features a modification of the amino acid from A to P at position 33.
+The protein's natural variant, known as in FVH1; unknown pathological significance, features a modification of the amino acid from R to Q at position 38.
+The protein's natural variant, known as in AN1; mild, features a modification of the amino acid from I to S at position 42.
+The protein's natural variant, known as in AN1, features a modification of the amino acid from S to P at position 43.
+The protein's natural variant, known as in AN1, features a modification of the amino acid from R to Q at position 44.
+The protein's natural variant, known as in AN1; shows almost no binding efficiency; transcriptional activation ability is about 50% lower than that of the wild-type protein, features a modification of the amino acid from L to R at position 46.
+The protein's natural variant, known as in AN1; shows almost no binding efficiency; transcriptional activation ability is about 50% lower than that of the wild-type protein, features a modification of the amino acid from C to R at position 52.
+The protein's natural variant, known as in ASGD5; also found in patients with congenital cataract and foveal hypoplasia, features a modification of the amino acid from V to D at position 53.
+The protein's natural variant, known as in AN1; mild; shows 50% lower DNA-binding and transactivation ability than the wild-type protein, features a modification of the amino acid from V to L at position 53.
+The protein's natural variant, known as in AN1; shows only one-quarter to one-third the binding ability of the normal wild-type protein; exhibits normal transactivation, features a modification of the amino acid from I to T at position 56.
+The protein's natural variant, known as in AN1; mild, features a modification of the amino acid from T to P at position 63.
+The protein's natural variant, known as in foveal hypoplasia; associated with presenile cataract syndrome;, features a modification of the amino acid from G to V at position 64.
+The protein's natural variant, known as in morning glory disk anomaly; significant impairment of transcriptional activation ability;, features a modification of the amino acid from P to S at position 68.
+The protein's natural variant, known as in AN1; shows almost no binding efficiency; transcriptional activation ability is about 80% of that of the wild-type protein, features a modification of the amino acid from G to D at position 73.
+The protein's natural variant, known as in AN1; mild, features a modification of the amino acid from A to E at position 79.
+The protein's natural variant, known as in AN1, features a modification of the amino acid from I to K at position 87.
+The protein's natural variant, known as in AN1; loss of activity, features a modification of the amino acid from I to R at position 87.
+The protein's natural variant, known as in a family with nystagmus associated with a variant form of aniridia, features a modification of the amino acid from P to R at position 118.
+The protein's natural variant, known as in AN1;, features a modification of the amino acid from S to R at position 119.
+The protein's natural variant, known as in FVH1; isolated, features a modification of the amino acid from R to C at position 125.
+The protein's natural variant, known as in AN1; atypical form;, features a modification of the amino acid from V to D at position 126.
+The protein's natural variant, known as in FVH1; isolated;, features a modification of the amino acid from R to C at position 128.
+The protein's natural variant, known as in AN1, features a modification of the amino acid from Q to H at position 178.
+The protein's natural variant, known as in AN1; mild;, features a modification of the amino acid from R to Q at position 208.
+The protein's natural variant, known as in AN1;, features a modification of the amino acid from R to W at position 208.
+The protein's natural variant, known as in AN1; the mutant homeodomain binds DNA as well as the wild-type homeodomain; the mutant does not modify the DNA-binding properties of the paired domain; the steady-state levels of the full-length mutant protein are higher than those of the wild-type one; a responsive promoter is activated to a higher extent by the mutant protein than by the wild-type protein; the presence of the mutation reduces sensitivity to trypsin digestion;, features a modification of the amino acid from R to T at position 242.
+The protein's natural variant, known as in COAD and COLON; significant impairment of transcriptional activation ability;, features a modification of the amino acid from F to S at position 258.
+The protein's natural variant, known as in BONH; significant impairment of ability to activate transcription, features a modification of the amino acid from S to I at position 292.
+The protein's natural variant, known as shows about two-fold higher binding efficiency than the normal wild-type protein; transcriptional activation ability is about 89% of that of the wild-type protein, features a modification of the amino acid from A to T at position 321.
+The protein's natural variant, known as in AN1;, features a modification of the amino acid from S to A at position 353.
+The protein's natural variant, known as in ASGD5, features a modification of the amino acid from S to P at position 363.
+The protein's natural variant, known as in AN1; reduced DNA binding ability;, features a modification of the amino acid from P to Q at position 375.
+The protein's natural variant, known as in optic nerve aplasia, features a modification of the amino acid from Q to R at position 378.
+The protein's natural variant, known as in BONH, features a modification of the amino acid from M to V at position 381.
+The protein's natural variant, known as in BONH;, features a modification of the amino acid from T to A at position 391.
+The protein's natural variant, known as in AN1, features a modification of the amino acid from G to R at position 395.
+The protein's natural variant, known as in AN1 and ocular anterior segment anomalies; loss of DNA binding ability;, features a modification of the amino acid from Q to R at position 422.
+The protein's natural variant, known as in copy number mutant, features a modification of the amino acid from A to D at position 60.
+The natural variant of this protein is characterized by an amino acid alteration from DS to QN at position 203.
+The protein's natural variant, known as in strain: NJL/Msf, BLG2/Msf, MSM/Msf and SWN/Msf, features a modification of the amino acid from A to T at position 4.
+The protein's natural variant, known as in strain: SWN/Msf, features a modification of the amino acid from R to H at position 87.
+The protein's natural variant, known as in strain: CAST/Ei, features a modification of the amino acid from T to M at position 128.
+The protein's natural variant, known as in Sol g 4.02, features a modification of the amino acid from M to V at position 28.
+The protein's natural variant, known as in Sol g 4.02, features a modification of the amino acid from E to K at position 33.
+The protein's natural variant, known as in Sol g 4.02, features a modification of the amino acid from L to R at position 123.
+The natural variant of this protein is characterized by an amino acid alteration from V to A at position 30.
+The protein's natural variant, known as in SCA23;, features a modification of the amino acid from C to Y at position 22.
+The protein's natural variant, known as in SCA23; PDYN, dynorphin A and dynorphin B are located in Purkinje cells as observed in control cerebellum, but cerebellar tissue with the mutation has decreased levels of SLC1A6 and CALB1, both of which are markers of Purkinje cells; SLC1A6 accumulates and aggregates in patient cerebellar tissue;, features a modification of the amino acid from R to S at position 138.
+The protein's natural variant, known as in SCA23;, features a modification of the amino acid from R to C at position 206.
+The protein's natural variant, known as in SCA23;, features a modification of the amino acid from R to H at position 206.
+The protein's natural variant, known as in SCA23; the mutant PDYN protein is produced, but processing to opioid peptides is dramatically affected, with increased levels of dynorphin A compared to dynorphin B; these results suggest slow conversion of dynorphin A to short enkephalins; mutant S-211 dynorphin A is not neurotoxic to cultured striatal neurons; no effect on membrane property;, features a modification of the amino acid from L to S at position 211.
+The protein's natural variant, known as in SCA23; the mutant PDYN protein is produced, but processing to opioid peptides is dramatically affected, with increased levels of dynorphin A compared to dynorphin B; mutant dynorphin A is neurotoxic to cultured striatal neurons, suggesting a dominant-negative effect; disrupts membrane property;, features a modification of the amino acid from R to W at position 212.
+The protein's natural variant, known as in SCA23; the mutant PDYN protein is produced, but processing to opioid peptides is dramatically affected, resulting in an approximately 2-fold decreased level of dynorphin B compared to dynorphin A; mutant dynorphin A is neurotoxic to cultured striatal neurons, suggesting a dominant-negative effect; disrupts membrane property;, features a modification of the amino acid from R to C at position 215.
+The protein's natural variant, known as in SCA23, features a modification of the amino acid from G to D at position 227.
+The protein's natural variant, known as in strain: CC-503, features a modification of the amino acid from S to T at position 449.
+The protein's natural variant, known as in strain: CC-503, features a modification of the amino acid from RK to KN at position 549.
+The protein's natural variant, known as in strain: Neijang, features a modification of the amino acid from R to C at position 131.
+The protein's natural variant, known as may be associated with susceptibility to lupus nephritis; does not efficiently recognize IgG2;, features a modification of the amino acid from H to R at position 167.
+The natural variant of this protein is characterized by an amino acid alteration from A to S at position 173.
+The natural variant of this protein is characterized by an amino acid alteration from Q to E at position 536.
+The protein's natural variant, known as in HH22; partial loss of function;, features a modification of the amino acid from H to Y at position 278.
+The natural variant of this protein is characterized by an amino acid alteration from TN to AT at position 352.
+The protein's natural variant, known as in NMTC2; does not affect the interaction with ROBO1; decreased GTPase activator activity; in SLIT2 and ROBO1-mediated inhibition of CDC42;, features a modification of the amino acid from Q to H at position 149.
+The protein's natural variant, known as in NMTC2; does not affect the interaction with ROBO1; slightly increased GTPase activator activity; in SLIT2 and ROBO1-mediated inhibition of CDC42;, features a modification of the amino acid from A to T at position 275.
+The protein's natural variant, known as in NMTC2; does not affect the interaction with ROBO1; decreased GTPase activator activity; in SLIT2 and ROBO1-mediated inhibition of CDC42;, features a modification of the amino acid from R to C at position 617.
+The protein's natural variant, known as in NMTC2; does not affect the interaction with ROBO1; slightly increased GTPase activator activity; in SLIT2 and ROBO1-mediated inhibition of CDC42;, features a modification of the amino acid from H to R at position 875.
+The protein's natural variant, known as in CTLN1;, features a modification of the amino acid from G to S at position 14.
+The protein's natural variant, known as in CTLN1;, features a modification of the amino acid from S to L at position 18.
+The protein's natural variant, known as in CTLN1, features a modification of the amino acid from C to R at position 19.
+The protein's natural variant, known as in CTLN1, features a modification of the amino acid from Q to L at position 40.
+The protein's natural variant, known as in CTLN1; unknown pathological significance;, features a modification of the amino acid from V to I at position 64.
+The protein's natural variant, known as in CTLN1;, features a modification of the amino acid from V to A at position 69.
+The protein's natural variant, known as in CTLN1, features a modification of the amino acid from S to P at position 79.
+The protein's natural variant, known as in CTLN1;, features a modification of the amino acid from R to C at position 86.
+The protein's natural variant, known as in CTLN1;, features a modification of the amino acid from R to H at position 86.
+The protein's natural variant, known as in CTLN1; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity;, features a modification of the amino acid from T to P at position 91.
+The protein's natural variant, known as in CTLN1; increased thermal stability; loss of argininosuccinate synthase activity, features a modification of the amino acid from R to S at position 95.
+The protein's natural variant, known as in CTLN1; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity, features a modification of the amino acid from P to H at position 96.
+The protein's natural variant, known as in CTLN1; decreased thermal stability; decreased affinity for aspartate; decreased affinity for citrulline; loss of argininosuccinate synthase activity, features a modification of the amino acid from P to L at position 96.
+The protein's natural variant, known as in CTLN1; no effect on thermal stability; decreased argininosuccinate synthase activity, features a modification of the amino acid from P to S at position 96.
+The protein's natural variant, known as in CTLN1;, features a modification of the amino acid from R to C at position 100.
+The protein's natural variant, known as in CTLN1;, features a modification of the amino acid from R to H at position 100.
+The protein's natural variant, known as in CTLN1;, features a modification of the amino acid from R to L at position 108.
+The protein's natural variant, known as in CTLN1, features a modification of the amino acid from A to D at position 111.
+The protein's natural variant, known as in CTLN1, features a modification of the amino acid from G to C at position 117.
+The protein's natural variant, known as in CTLN1, features a modification of the amino acid from G to D at position 117.
+The protein's natural variant, known as in CTLN1; decreased thermal stability; loss of argininosuccinate synthase activity;, features a modification of the amino acid from G to S at position 117.
+The protein's natural variant, known as in CTLN1; decreased thermal stability; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity;, features a modification of the amino acid from A to T at position 118.
+The protein's natural variant, known as in CTLN1; decreased thermal stability; loss of argininosuccinate synthase activity, features a modification of the amino acid from T to I at position 119.
+The protein's natural variant, known as in CTLN1; loss of argininosuccinate synthase activity;, features a modification of the amino acid from D to N at position 124.
+The protein's natural variant, known as increased thermal stability; loss of argininosuccinate synthase activity;, features a modification of the amino acid from R to L at position 127.
+The protein's natural variant, known as in CTLN1; increased thermal stability; loss of argininosuccinate synthase activity;, features a modification of the amino acid from R to Q at position 127.
+The protein's natural variant, known as in CTLN1; severe clinical course; loss of argininosuccinate synthase activity;, features a modification of the amino acid from R to W at position 127.
+The protein's natural variant, known as in CTLN1;, features a modification of the amino acid from V to G at position 141.
+The protein's natural variant, known as in CTLN1; decreased thermal stability; loss of argininosuccinate synthase activity;, features a modification of the amino acid from R to C at position 157.
+The protein's natural variant, known as in CTLN1; loss of argininosuccinate synthase activity;, features a modification of the amino acid from R to H at position 157.
+The protein's natural variant, known as in CTLN1, features a modification of the amino acid from R to S at position 157.
+The protein's natural variant, known as in CTLN1;, features a modification of the amino acid from L to P at position 160.
+The protein's natural variant, known as in CTLN1, features a modification of the amino acid from A to P at position 164.
+The protein's natural variant, known as in CTLN1; mild; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity;, features a modification of the amino acid from W to R at position 179.
+The protein's natural variant, known as in CTLN1; increased thermal stability; loss of argininosuccinate synthase activity;, features a modification of the amino acid from S to I at position 180.
+The protein's natural variant, known as in CTLN1; decreased thermal stability; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity;, features a modification of the amino acid from S to N at position 180.
+The protein's natural variant, known as in CTLN1;, features a modification of the amino acid from N to K at position 184.
+The protein's natural variant, known as in CTLN1, features a modification of the amino acid from Y to D at position 190.
+The protein's natural variant, known as in CTLN1;, features a modification of the amino acid from E to K at position 191.
+The protein's natural variant, known as in CTLN1; loss of argininosuccinate synthase activity, features a modification of the amino acid from E to Q at position 191.
+The protein's natural variant, known as in CTLN1; decreased protein abundance, features a modification of the amino acid from A to V at position 192.
+The protein's natural variant, known as in CTLN1;, features a modification of the amino acid from A to E at position 202.
+The protein's natural variant, known as in CTLN1, features a modification of the amino acid from L to P at position 206.
+The protein's natural variant, known as in CTLN1, features a modification of the amino acid from G to R at position 230.
+The protein's natural variant, known as in CTLN1, features a modification of the amino acid from N to I at position 237.
+The protein's natural variant, known as in CTLN1, features a modification of the amino acid from A to P at position 258.
+The protein's natural variant, known as in CTLN1;, features a modification of the amino acid from A to V at position 258.
+The protein's natural variant, known as in CTLN1; mild clinical course; no effect on affinity for aspartate; no effect on affinity for citrulline; decreased argininosuccinate synthase activity;, features a modification of the amino acid from V to M at position 263.
+The protein's natural variant, known as in CTLN1; severe clinical course; loss of argininosuccinate synthase activity;, features a modification of the amino acid from R to C at position 265.
+The protein's natural variant, known as in CTLN1;, features a modification of the amino acid from R to H at position 265.
+The protein's natural variant, known as in CTLN1;, features a modification of the amino acid from V to M at position 269.
+The protein's natural variant, known as in CTLN1; loss of argininosuccinate synthase activity;, features a modification of the amino acid from E to Q at position 270.
+The protein's natural variant, known as in CTLN1; increased thermal stability; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity;, features a modification of the amino acid from R to C at position 272.
+The protein's natural variant, known as in CTLN1; increased thermal stability; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity;, features a modification of the amino acid from R to H at position 272.
+The protein's natural variant, known as in CTLN1; increased thermal stability; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity;, features a modification of the amino acid from R to L at position 272.
+The protein's natural variant, known as in CTLN1, features a modification of the amino acid from K to T at position 277.
+The protein's natural variant, known as in CTLN1;, features a modification of the amino acid from R to Q at position 279.
+The protein's natural variant, known as in CTLN1; loss of argininosuccinate synthase activity, features a modification of the amino acid from G to R at position 280.
+The protein's natural variant, known as in CTLN1;, features a modification of the amino acid from E to K at position 283.
+The protein's natural variant, known as in CTLN1; mild clinical course;, features a modification of the amino acid from T to I at position 284.
+The protein's natural variant, known as in CTLN1, features a modification of the amino acid from L to P at position 290.
+The protein's natural variant, known as in CTLN1, features a modification of the amino acid from Y to S at position 291.
+The protein's natural variant, known as in CTLN1, features a modification of the amino acid from D to G at position 296.
+The protein's natural variant, known as in CTLN1;, features a modification of the amino acid from A to D at position 299.
+The protein's natural variant, known as in CTLN1; no effect on affinity for aspartate; no effect on affinity for citrulline; decreased argininosuccinate synthase activity, features a modification of the amino acid from M to V at position 302.
+The protein's natural variant, known as in CTLN1; decreased protein abundance;, features a modification of the amino acid from R to W at position 304.
+The protein's natural variant, known as in CTLN1, features a modification of the amino acid from V to G at position 306.
+The protein's natural variant, known as in CTLN1;, features a modification of the amino acid from R to C at position 307.
+The protein's natural variant, known as in CTLN1;, features a modification of the amino acid from K to Q at position 310.
+The protein's natural variant, known as in CTLN1;, features a modification of the amino acid from K to R at position 310.
+The protein's natural variant, known as in CTLN1;, features a modification of the amino acid from V to M at position 321.
+The protein's natural variant, known as in CTLN1; loss of argininosuccinate synthase activity;, features a modification of the amino acid from G to S at position 324.
+The protein's natural variant, known as in CTLN1, features a modification of the amino acid from G to V at position 324.
+The protein's natural variant, known as in CTLN1;, features a modification of the amino acid from R to H at position 335.
+The protein's natural variant, known as in CTLN1, features a modification of the amino acid from C to R at position 337.
+The protein's natural variant, known as in CTLN1, features a modification of the amino acid from S to F at position 341.
+The protein's natural variant, known as in CTLN1, features a modification of the amino acid from V to G at position 345.
+The protein's natural variant, known as in CTLN1; severe clinical course, features a modification of the amino acid from G to R at position 347.
+The protein's natural variant, known as in CTLN1, features a modification of the amino acid from G to V at position 356.
+The protein's natural variant, known as in CTLN1; mild clinical course, features a modification of the amino acid from Y to D at position 359.
+The protein's natural variant, known as in CTLN1; mild; no effect on affinity for aspartate; no effect on affinity for citrulline; decreased argininosuccinate synthase activity;, features a modification of the amino acid from G to V at position 362.
+The protein's natural variant, known as in CTLN1, features a modification of the amino acid from R to G at position 363.
+The protein's natural variant, known as in CTLN1, features a modification of the amino acid from R to L at position 363.
+The protein's natural variant, known as in CTLN1;, features a modification of the amino acid from R to Q at position 363.
+The protein's natural variant, known as in CTLN1;, features a modification of the amino acid from R to W at position 363.
+The protein's natural variant, known as in CTLN1;, features a modification of the amino acid from T to I at position 389.
+The protein's natural variant, known as in CTLN1, features a modification of the amino acid from T to P at position 389.
+The protein's natural variant, known as in CTLN1; loss of argininosuccinate synthase activity;, features a modification of the amino acid from G to R at position 390.
+The natural variant of this protein is characterized by an amino acid alteration from EE to GK at position 23.
+The natural variant of this protein is characterized by an amino acid alteration from Q to H at position 40.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from Y to C at position 331.
+The protein's natural variant, known as in strain: cv. Cvi-1 and cv. Nd-1, features a modification of the amino acid from I to T at position 11.
+The protein's natural variant, known as in strain: cv. Nok-0, features a modification of the amino acid from S to Y at position 20.
+The protein's natural variant, known as in strain: cv. Cvi-1, cv. Fe-1a, cv. Nd-1 and cv. Wei-0, features a modification of the amino acid from K to S at position 30.
+The protein's natural variant, known as in strain: cv. Cvi-1, cv. Di-0, cv. Fe-1a, cv. Goe-0, cv. Ita-0, cv. Kas-1, cv. Landsberg erecta, cv. Le-0, cv. Nd-1, cv. Nok-0, cv. Rsch-0, cv. Sah-0, cv. Ta-0, cv. Wei-0 and cv. Wil-2, features a modification of the amino acid from F to S at position 59.
+The protein's natural variant, known as in a pancreatic ductal adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from G to R at position 227.
+The protein's natural variant, known as in a pancreatic ductal adenocarcinoma sample; somatic mutation, features a modification of the amino acid from K to M at position 274.
+The protein's natural variant, known as in strain: Isolate LAF1511, features a modification of the amino acid from A to V at position 232.
+The protein's natural variant, known as in strain: Isolate LAF1511, features a modification of the amino acid from A to V at position 236.
+The protein's natural variant, known as in D-GA; the mutant protein is not expressed and has no enzymatic activity;, features a modification of the amino acid from F to C at position 493.
+The protein's natural variant, known as in allele GC*1S;, features a modification of the amino acid from D to E at position 432.
+The protein's natural variant, known as in allele GC*2, allele GC*2A9;, features a modification of the amino acid from T to K at position 436.
+The protein's natural variant, known as in allele GC*2A9; requires 2 nucleotide substitutions, features a modification of the amino acid from H to C at position 445.
+The protein's natural variant, known as in allele GC*1F, allele GC*2 and allele GC*1S;, features a modification of the amino acid from H to R at position 445.
+The protein's natural variant, known as in strain: cv. Shikoku Hadaka 84, features a modification of the amino acid from L to F at position 9.
+The protein's natural variant, known as in strain: cv. Iyatoma Mochi, cv. Mochimugi-D, cv. Shikoku Hadaka 84, cv. Waxy Oderbrucker and cv. SB 85750, features a modification of the amino acid from R to RSAPSM at position 21.
+The protein's natural variant, known as in strain: cv. Iyatoma Mochi, cv. Mochimugi-D, cv. Shikoku Hadaka 84, cv. Waxy Oderbrucker and cv. SB 85750, features a modification of the amino acid from RP to HA at position 25.
+The protein's natural variant, known as in strain: cv. Iyatoma Mochi, cv. Mochimugi-D, cv. Shikoku Hadaka 84, cv. Waxy Oderbrucker and cv. SB 85750, features a modification of the amino acid from N to K at position 34.
+The protein's natural variant, known as in strain: cv. Iyatoma Mochi, cv. Mochimugi-D, cv. Shikoku Hadaka 84, cv. Waxy Oderbrucker and cv. SB 85750, features a modification of the amino acid from AAL to GTF at position 40.
+The protein's natural variant, known as in strain: cv. Iyatoma Mochi, cv. Mochimugi-D, cv. Shikoku Hadaka 84, cv. Waxy Oderbrucker and cv. SB 85750, features a modification of the amino acid from I to V at position 45.
+The protein's natural variant, known as in strain: cv. Iyatoma Mochi, cv. Mochimugi-D, cv. Shikoku Hadaka 84, cv. Waxy Oderbrucker and cv. SB 85750, features a modification of the amino acid from S to N at position 61.
+The protein's natural variant, known as in strain: cv. Iyatoma Mochi, cv. Morex, cv. Mochimugi-D, cv. Shikoku Hadaka 84, cv. Waxy Oderbrucker and cv. SB 85750, features a modification of the amino acid from S to R at position 70.
+The protein's natural variant, known as in strain: cv. CDCAlamo, features a modification of the amino acid from D to V at position 287.
+The protein's natural variant, known as in strain: cv. Iyatoma Mochi, features a modification of the amino acid from R to W at position 391.
+The protein's natural variant, known as in strain: cv. Iyatoma Mochi, features a modification of the amino acid from A to V at position 414.
+The protein's natural variant, known as in strain: cv. Iyatoma Mochi, cv. Waxy Oderbrucker and cv. SB 85750, features a modification of the amino acid from G to W at position 513.
+The protein's natural variant, known as in strain: cv. CDCAlamo, features a modification of the amino acid from MI to VV at position 559.
+The protein's natural variant, known as in allele NKG2-F*02, features a modification of the amino acid from T to I at position 7.
+The protein's natural variant, known as in allele NKG2-F*02, features a modification of the amino acid from R to K at position 22.
+The protein's natural variant, known as in allele NKG2-F*02, allele NKG2-F*04 and allele NKG2-F*05, features a modification of the amino acid from K to E at position 35.
+The protein's natural variant, known as in allele NKG2-F*02, allele NKG2-F*04 and allele NKG2-F*05, features a modification of the amino acid from R to K at position 70.
+The protein's natural variant, known as in allele NKG2-F*04, features a modification of the amino acid from T to I at position 90.
+The protein's natural variant, known as in allele NKG2-F*02, features a modification of the amino acid from H to R at position 119.
+The protein's natural variant, known as in allele NKG2-F*04 and allele NKG2-F*05, features a modification of the amino acid from T to I at position 126.
+The protein's natural variant, known as in allele NKG2-F*02, allele NKG2-F*04 and allele NKG2-F*05, features a modification of the amino acid from G to R at position 144.
+The protein's natural variant, known as in allele NKG2-F*02, allele NKG2-F*03, allele NKG2-F*04 and allele NKG2-F*05, features a modification of the amino acid from Q to R at position 151.
+The protein's natural variant, known as in MC1DN12;, features a modification of the amino acid from G to R at position 8.
+The protein's natural variant, known as in MC1DN12;, features a modification of the amino acid from R to S at position 37.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to C at position 53.
+The protein's natural variant, known as in CSNU;, features a modification of the amino acid from L to P at position 89.
+The protein's natural variant, known as in CSNU, features a modification of the amino acid from P to S at position 122.
+The protein's natural variant, known as in CSNU;, features a modification of the amino acid from M to R at position 123.
+The protein's natural variant, known as in CSNU;, features a modification of the amino acid from Y to C at position 124.
+The protein's natural variant, known as in CSNU;, features a modification of the amino acid from P to Q at position 128.
+The protein's natural variant, known as in CSNU, features a modification of the amino acid from S to P at position 130.
+The protein's natural variant, known as in CSNU, features a modification of the amino acid from D to G at position 137.
+The protein's natural variant, known as in CSNU;, features a modification of the amino acid from G to R at position 140.
+The protein's natural variant, known as in CSNU, features a modification of the amino acid from L to Q at position 149.
+The protein's natural variant, known as in CSNU;, features a modification of the amino acid from Y to C at position 151.
+The protein's natural variant, known as in CSNU;, features a modification of the amino acid from D to Y at position 179.
+The protein's natural variant, known as in CSNU;, features a modification of the amino acid from R to Q at position 181.
+The protein's natural variant, known as in CSNU; unknown pathological significance; impairs protein stability and dimer formation;, features a modification of the amino acid from V to A at position 183.
+The protein's natural variant, known as in CSNU;, features a modification of the amino acid from T to M at position 189.
+The protein's natural variant, known as in CSNU; impairs protein stability and dimer formation;, features a modification of the amino acid from T to M at position 216.
+The protein's natural variant, known as in CSNU, features a modification of the amino acid from N to K at position 253.
+The protein's natural variant, known as in CSNU; reduction in amino acid transport activity;, features a modification of the amino acid from E to K at position 268.
+The protein's natural variant, known as in CSNU; reduction in amino acid transport activity;, features a modification of the amino acid from T to A at position 341.
+The protein's natural variant, known as in CSNU; unknown pathological significance, features a modification of the amino acid from L to P at position 346.
+The protein's natural variant, known as in CSNU;, features a modification of the amino acid from H to P at position 348.
+The protein's natural variant, known as in CSNU;, features a modification of the amino acid from R to C at position 362.
+The protein's natural variant, known as in CSNU;, features a modification of the amino acid from R to H at position 362.
+The protein's natural variant, known as in CSNU;, features a modification of the amino acid from R to P at position 365.
+The protein's natural variant, known as in CSNU;, features a modification of the amino acid from R to W at position 365.
+The protein's natural variant, known as in CSNU;, features a modification of the amino acid from G to R at position 398.
+The protein's natural variant, known as in CSNU;, features a modification of the amino acid from N to K at position 410.
+The protein's natural variant, known as in CSNU, features a modification of the amino acid from P to R at position 441.
+The protein's natural variant, known as in CSNU; unknown pathological significance;, features a modification of the amino acid from I to T at position 445.
+The protein's natural variant, known as in CSNU;, features a modification of the amino acid from R to Q at position 452.
+The protein's natural variant, known as in CSNU;, features a modification of the amino acid from R to W at position 452.
+The protein's natural variant, known as in CSNU;, features a modification of the amino acid from S to L at position 455.
+The protein's natural variant, known as in CSNU;, features a modification of the amino acid from R to C at position 456.
+The protein's natural variant, known as in CSNU;, features a modification of the amino acid from R to H at position 456.
+The protein's natural variant, known as in CSNU;, features a modification of the amino acid from Y to H at position 461.
+The protein's natural variant, known as in CSNU;, features a modification of the amino acid from M to K at position 467.
+The protein's natural variant, known as in CSNU; impairs protein stability and dimer formation; loss of 80% of amino acid transport activity;, features a modification of the amino acid from M to T at position 467.
+The protein's natural variant, known as in CSNU, features a modification of the amino acid from G to V at position 481.
+The protein's natural variant, known as in CSNU, features a modification of the amino acid from E to K at position 482.
+The protein's natural variant, known as in CSNU, features a modification of the amino acid from S to L at position 507.
+The protein's natural variant, known as in CSNU;, features a modification of the amino acid from P to A at position 508.
+The protein's natural variant, known as in CSNU;, features a modification of the amino acid from Q to R at position 510.
+The protein's natural variant, known as in CSNU;, features a modification of the amino acid from S to W at position 547.
+The protein's natural variant, known as in CSNU;, features a modification of the amino acid from G to S at position 568.
+The protein's natural variant, known as in CSNU;, features a modification of the amino acid from Y to H at position 582.
+The protein's natural variant, known as in CSNU;, features a modification of the amino acid from R to T at position 584.
+The protein's natural variant, known as in CSNU;, features a modification of the amino acid from F to S at position 599.
+The protein's natural variant, known as in CSNU;, features a modification of the amino acid from G to E at position 600.
+The protein's natural variant, known as in CSNU;, features a modification of the amino acid from P to T at position 615.
+The protein's natural variant, known as in CSNU;, features a modification of the amino acid from F to S at position 648.
+The protein's natural variant, known as in CSNU;, features a modification of the amino acid from T to R at position 652.
+The protein's natural variant, known as in CSNU, features a modification of the amino acid from C to W at position 666.
+The protein's natural variant, known as in CSNU; unknown pathological significance;, features a modification of the amino acid from C to R at position 673.
+The protein's natural variant, known as in CSNU;, features a modification of the amino acid from L to P at position 678.
+The protein's natural variant, known as rifampicin resistant, features a modification of the amino acid from D to N at position 473.
+The protein's natural variant, known as rifampicin resistant, features a modification of the amino acid from G to D at position 479.
+The protein's natural variant, known as rifampicin resistant, features a modification of the amino acid from H to L at position 483.
+The protein's natural variant, known as rifampicin resistant, features a modification of the amino acid from H to Y at position 483.
+The protein's natural variant, known as rifampicin resistant, features a modification of the amino acid from L to F at position 528.
+The protein's natural variant, known as rifampicin resistant, features a modification of the amino acid from N to Y at position 530.
+The protein's natural variant, known as in MRT12; most of the mutant protein is improperly localized to the endoplasmic reticulum preventing the protein from interacting with its substrates in the Golgi and resulting in a loss-of-function;, features a modification of the amino acid from A to D at position 13.
+The protein's natural variant, known as in DEE15, features a modification of the amino acid from A to P at position 320.
+The protein's natural variant, known as in MRT12; the mutant protein is improperly localized to the endoplasmic reticulum preventing the protein from interacting with its substrates in the Golgi and resulting in a loss-of-function; shows a complete lack of enzyme activity; secretion of the mutant protein is dramatically reduced compared to wild-type, features a modification of the amino acid from D to Y at position 370.
+The protein's natural variant, known as in MDDGA6;, features a modification of the amino acid from S to F at position 331.
+The protein's natural variant, known as in MDDGA6, features a modification of the amino acid from C to Y at position 443.
+The protein's natural variant, known as in MDDGA6;, features a modification of the amino acid from W to R at position 495.
+The protein's natural variant, known as in MDDGB6;, features a modification of the amino acid from E to K at position 509.
+The protein's natural variant, known as in LMPHM11; unknown pathological significance;, features a modification of the amino acid from R to C at position 481.
+The protein's natural variant, known as in LMPHM11; unknown pathological significance;, features a modification of the amino acid from E to K at position 1061.
+The protein's natural variant, known as in LMPHM11; unknown pathological significance;, features a modification of the amino acid from R to H at position 1109.
+The protein's natural variant, known as in some primary melanomas and melanoma cell lines, features a modification of the amino acid from L to F at position 151.
+The natural variant of this protein is characterized by an amino acid alteration from E to V at position 93.
+The protein's natural variant, known as in cph; loss of a phosphorylation site and loss of trafficking to the apical cell membrane; causes aberrant location at the basolateral cell membrane, features a modification of the amino acid from S to L at position 256.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 8.
+The natural variant of this protein is characterized by an amino acid alteration from S to K at position 234.
+The natural variant of this protein is characterized by an amino acid alteration from G to Q at position 247.
+The protein's natural variant, known as in OPTB8;, features a modification of the amino acid from R to L at position 16.
+The protein's natural variant, known as in OPTB8;, features a modification of the amino acid from Y to S at position 32.
+The protein's natural variant, known as in OPTB8, features a modification of the amino acid from R to P at position 51.
+The protein's natural variant, known as in OPTB8; increased expression, produces extensive cytoplasmic vacuolation and impairs bone resorptive function;, features a modification of the amino acid from R to Q at position 51.
+The protein's natural variant, known as in CNMX; greatly reduced binding to PI(3,5)P2; abolishes interaction with MTMR12; does not translocate to the late endosome following EGF stimulation; shows normal EGFR degradation;, features a modification of the amino acid from V to F at position 49.
+The protein's natural variant, known as in CNMX, features a modification of the amino acid from Y to D at position 68.
+The protein's natural variant, known as in CNMX; mild; reduced response to PI5P and reduced binding to PI(3,5)P2; abolishes interaction with MTMR12;, features a modification of the amino acid from R to C at position 69.
+The protein's natural variant, known as in CNMX, features a modification of the amino acid from R to P at position 69.
+The protein's natural variant, known as in CNMX; severe, features a modification of the amino acid from R to S at position 69.
+The protein's natural variant, known as in CNMX; mild; reduced binding to PI(3,5)P2;, features a modification of the amino acid from L to F at position 70.
+The protein's natural variant, known as in CNMX; mild; reduced binding to PI(3,5)P2;, features a modification of the amino acid from L to P at position 87.
+The protein's natural variant, known as in CNMX;, features a modification of the amino acid from E to K at position 157.
+The protein's natural variant, known as in CNMX; mild;, features a modification of the amino acid from P to S at position 179.
+The protein's natural variant, known as in CNMX; very mild, features a modification of the amino acid from N to K at position 180.
+The protein's natural variant, known as in CNMX; severe; loss of activity; abolishes interaction with DES and MTMR12;, features a modification of the amino acid from R to G at position 184.
+The protein's natural variant, known as in CNMX, features a modification of the amino acid from R to L at position 184.
+The protein's natural variant, known as in CNMX;, features a modification of the amino acid from T to I at position 186.
+The protein's natural variant, known as in CNMX;, features a modification of the amino acid from N to S at position 189.
+The protein's natural variant, known as in CNMX, features a modification of the amino acid from T to I at position 197.
+The protein's natural variant, known as in CNMX; severe, features a modification of the amino acid from Y to N at position 198.
+The protein's natural variant, known as in CNMX, features a modification of the amino acid from P to S at position 199.
+The protein's natural variant, known as in CNMX; severe, features a modification of the amino acid from L to S at position 202.
+The protein's natural variant, known as in CNMX; severe; dramatic decrease in phosphatase activity; abolishes interaction with DES and MTMR12;, features a modification of the amino acid from P to L at position 205.
+The protein's natural variant, known as in CNMX; mild, features a modification of the amino acid from I to T at position 225.
+The protein's natural variant, known as in CNMX;, features a modification of the amino acid from P to T at position 226.
+The protein's natural variant, known as in CNMX;, features a modification of the amino acid from V to M at position 227.
+The protein's natural variant, known as in CNMX;, features a modification of the amino acid from L to P at position 228.
+The protein's natural variant, known as in CNMX; mild, features a modification of the amino acid from S to P at position 229.
+The protein's natural variant, known as in CNMX, features a modification of the amino acid from W to C at position 230.
+The protein's natural variant, known as in CNMX, features a modification of the amino acid from H to R at position 232.
+The protein's natural variant, known as in CNMX; mild to moderate; abolishes interaction with DES, but not with MTMR12; reduces MTMR12 protein levels in myotubes;, features a modification of the amino acid from R to C at position 241.
+The protein's natural variant, known as in CNMX; severe; loss of activity, features a modification of the amino acid from R to L at position 241.
+The protein's natural variant, known as in CNMX; severe;, features a modification of the amino acid from I to S at position 264.
+The protein's natural variant, known as in CNMX, features a modification of the amino acid from A to G at position 279.
+The protein's natural variant, known as in CNMX; mild, features a modification of the amino acid from M to R at position 317.
+The protein's natural variant, known as in CNMX; mild, features a modification of the amino acid from W to C at position 346.
+The protein's natural variant, known as in CNMX, features a modification of the amino acid from W to S at position 346.
+The protein's natural variant, known as in CNMX, features a modification of the amino acid from V to G at position 364.
+The protein's natural variant, known as in CNMX;, features a modification of the amino acid from H to D at position 374.
+The protein's natural variant, known as in CNMX; dramatic decrease in phosphatase activity, features a modification of the amino acid from S to N at position 376.
+The protein's natural variant, known as in CNMX, features a modification of the amino acid from G to E at position 378.
+The protein's natural variant, known as in CNMX; severe; dramatic decrease in phosphatase activity; does not affect EGFR degradation;, features a modification of the amino acid from G to R at position 378.
+The protein's natural variant, known as in CNMX;, features a modification of the amino acid from S to Y at position 387.
+The protein's natural variant, known as in CNMX; severe, features a modification of the amino acid from A to D at position 389.
+The protein's natural variant, known as in CNMX, features a modification of the amino acid from L to P at position 391.
+The protein's natural variant, known as in CNMX; severe; dramatic decrease in phosphatase activity;, features a modification of the amino acid from Y to C at position 397.
+The protein's natural variant, known as in CNMX; mild;, features a modification of the amino acid from G to A at position 402.
+The protein's natural variant, known as in CNMX;, features a modification of the amino acid from G to R at position 402.
+The protein's natural variant, known as in CNMX, features a modification of the amino acid from G to V at position 402.
+The protein's natural variant, known as in CNMX; mild;, features a modification of the amino acid from E to K at position 404.
+The protein's natural variant, known as in CNMX; severe, features a modification of the amino acid from L to P at position 406.
+The protein's natural variant, known as in CNMX;, features a modification of the amino acid from W to C at position 411.
+The protein's natural variant, known as in CNMX; severe, features a modification of the amino acid from S to SFIQ at position 420.
+The protein's natural variant, known as in CNMX; severe; reduced activity and response to PI5P; does not affect interaction with DES or MTMR12;, features a modification of the amino acid from R to Q at position 421.
+The protein's natural variant, known as in CNMX; severe, features a modification of the amino acid from R to RFIQ at position 421.
+The protein's natural variant, known as in CNMX;, features a modification of the amino acid from D to N at position 431.
+The protein's natural variant, known as in CNMX;, features a modification of the amino acid from D to N at position 433.
+The protein's natural variant, known as in CNMX, features a modification of the amino acid from C to Y at position 444.
+The protein's natural variant, known as in CNMX;, features a modification of the amino acid from H to P at position 469.
+The protein's natural variant, known as in CNMX; severe, features a modification of the amino acid from L to P at position 470.
+The protein's natural variant, known as in CNMX; mild, features a modification of the amino acid from N to Y at position 481.
+The protein's natural variant, known as in CNMX; mild;, features a modification of the amino acid from W to R at position 499.
+The protein's natural variant, known as in CNMX; severe, features a modification of the amino acid from K to N at position 510.
+The protein's natural variant, known as in allele 2, features a modification of the amino acid from N to S at position 25.
+The protein's natural variant, known as in allele 2, features a modification of the amino acid from P to A at position 126.
+The protein's natural variant, known as found in a patient with disseminated superficial actinic porokeratosis; unknown pathological significance;, features a modification of the amino acid from V to M at position 591.
+The protein's natural variant, known as probable disease-associated variant found in a patient with severe intellectual disease, microcephaly and feeding difficulties as well as cerebral atrophy;, features a modification of the amino acid from R to C at position 270.
+The protein's natural variant, known as found in a patient with centronuclear myopathy; also identified in a Becker muscular dystrophy patient; unknown pathological significance;, features a modification of the amino acid from A to S at position 112.
+The natural variant of this protein is characterized by an amino acid alteration from E to G at position 422.
+The protein's natural variant, known as in Niigata;, features a modification of the amino acid from V to A at position 2.
+The protein's natural variant, known as in Catania;, features a modification of the amino acid from H to L at position 3.
+The protein's natural variant, known as in Sphakia;, features a modification of the amino acid from H to R at position 3.
+The protein's natural variant, known as in haplotype T11; Kenya;, features a modification of the amino acid from T to S at position 5.
+The protein's natural variant, known as in MUMC/Corleone, features a modification of the amino acid from A to D at position 11.
+The protein's natural variant, known as in Pylos;, features a modification of the amino acid from V to G at position 12.
+The protein's natural variant, known as in NYU;, features a modification of the amino acid from N to K at position 13.
+The protein's natural variant, known as in Delta';, features a modification of the amino acid from G to R at position 17.
+The protein's natural variant, known as in Roosevelt;, features a modification of the amino acid from V to E at position 21.
+The protein's natural variant, known as in Flatbush;, features a modification of the amino acid from A to E at position 23.
+The protein's natural variant, known as in Victoria;, features a modification of the amino acid from G to D at position 25.
+The protein's natural variant, known as in Yokoshima;, features a modification of the amino acid from G to D at position 26.
+The protein's natural variant, known as in Puglia;, features a modification of the amino acid from E to D at position 27.
+The protein's natural variant, known as in Yialousa;, features a modification of the amino acid from A to S at position 28.
+The protein's natural variant, known as in Metaponto;, features a modification of the amino acid from P to H at position 37.
+The protein's natural variant, known as in Agrinio;, features a modification of the amino acid from E to G at position 44.
+The protein's natural variant, known as in Melbourne;, features a modification of the amino acid from E to K at position 44.
+The protein's natural variant, known as in Parkville;, features a modification of the amino acid from D to V at position 48.
+The protein's natural variant, known as in Adria;, features a modification of the amino acid from P to R at position 52.
+The protein's natural variant, known as in Campania;, features a modification of the amino acid from N to K at position 58.
+The protein's natural variant, known as in Indonesia;, features a modification of the amino acid from G to R at position 70.
+The protein's natural variant, known as in Ventimiglia;, features a modification of the amino acid from A to G at position 71.
+The protein's natural variant, known as in Grovetown;, features a modification of the amino acid from L to V at position 76.
+The protein's natural variant, known as in Etolia;, features a modification of the amino acid from F to S at position 86.
+The protein's natural variant, known as in Montechiaro;, features a modification of the amino acid from Q to K at position 88.
+The protein's natural variant, known as in Lucania;, features a modification of the amino acid from L to V at position 89.
+The protein's natural variant, known as in Honai;, features a modification of the amino acid from E to V at position 91.
+The protein's natural variant, known as in Sant' Antioco;, features a modification of the amino acid from C to G at position 94.
+The protein's natural variant, known as in Wrens; unstable;, features a modification of the amino acid from V to M at position 99.
+The protein's natural variant, known as in Canada; O(2) affinity up;, features a modification of the amino acid from D to N at position 100.
+The protein's natural variant, known as in Capri;, features a modification of the amino acid from R to S at position 105.
+The protein's natural variant, known as in Corfu/Troodos;, features a modification of the amino acid from R to C at position 117.
+The protein's natural variant, known as in Coburg;, features a modification of the amino acid from R to H at position 117.
+The protein's natural variant, known as in LiangCheng;, features a modification of the amino acid from N to D at position 118.
+The protein's natural variant, known as in Manzanares; unstable;, features a modification of the amino acid from E to V at position 122.
+The protein's natural variant, known as in Zagreb;, features a modification of the amino acid from Q to E at position 126.
+The protein's natural variant, known as in Ninive;, features a modification of the amino acid from V to A at position 134.
+The protein's natural variant, known as in Babinga;, features a modification of the amino acid from G to D at position 137.
+The protein's natural variant, known as in Bagheria;, features a modification of the amino acid from A to V at position 141.
+The protein's natural variant, known as in Pelendri;, features a modification of the amino acid from L to P at position 142.
+The protein's natural variant, known as in Fitzroy;, features a modification of the amino acid from A to D at position 143.
+The protein's natural variant, known as in Monreale;, features a modification of the amino acid from H to R at position 147.
+The protein's natural variant, known as in strain: 85P, features a modification of the amino acid from T to V at position 75.
+The natural variant of this protein is characterized by an amino acid alteration from C to S at position 218.
+The protein's natural variant, known as in strain: CWL029 and TW-183, features a modification of the amino acid from Y to H at position 482.
+The protein's natural variant, known as in RNA edited version;, features a modification of the amino acid from R to G at position 78.
+The protein's natural variant, known as in RNA edited version;, features a modification of the amino acid from K to R at position 95.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from T to I at position 484.
+The protein's natural variant, known as in CSTNU; reduces catalytic activity and affinity for pyridoxal phosphate;, features a modification of the amino acid from T to I at position 67.
+The protein's natural variant, known as in CSTNU; strongly reduces catalytic activity and affinity for pyridoxal phosphate;, features a modification of the amino acid from Q to E at position 240.
+The protein's natural variant, known as in strain: B/TW-05/OT, features a modification of the amino acid from I to V at position 233.
+The protein's natural variant, known as in plasmid pYVa127/90, features a modification of the amino acid from Q to R at position 58.
+The protein's natural variant, known as in plasmid pYVa127/90, features a modification of the amino acid from A to T at position 77.
+The protein's natural variant, known as in plasmid pYVa127/90, features a modification of the amino acid from N to S at position 88.
+The protein's natural variant, known as in strain: L2, features a modification of the amino acid from V to A at position 124.
+The protein's natural variant, known as in strain: L2, features a modification of the amino acid from I to V at position 131.
+The protein's natural variant, known as in strain: L2, features a modification of the amino acid from R to K at position 132.
+The protein's natural variant, known as in strain: L2, features a modification of the amino acid from I to V at position 189.
+The protein's natural variant, known as in strain: L2, features a modification of the amino acid from E to D at position 191.
+The protein's natural variant, known as in strain: L2, features a modification of the amino acid from D to E at position 217.
+The protein's natural variant, known as in strain: L2, features a modification of the amino acid from E to V at position 255.
+The protein's natural variant, known as in strain: L2, features a modification of the amino acid from V to G at position 264.
+The protein's natural variant, known as in strain: L2, features a modification of the amino acid from L to F at position 289.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from Y to N at position 75.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from A to D at position 514.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from S to R at position 240.
+The protein's natural variant, known as in strain: YJM326 and YJM339, features a modification of the amino acid from D to E at position 242.
+The protein's natural variant, known as in strain: EAY1066, EAY1068, M2-8, M7-8, M5-7, SK1, YJM269, YJM280, YJM320, YJM326, YJM339 and YJM627, features a modification of the amino acid from L to P at position 271.
+The protein's natural variant, known as in strain: M2-8, features a modification of the amino acid from P to L at position 309.
+The protein's natural variant, known as in strain: EAY1066, features a modification of the amino acid from E to D at position 321.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from E to K at position 333.
+The protein's natural variant, known as in strain: YJM339, features a modification of the amino acid from A to T at position 375.
+The protein's natural variant, known as in strain: EAY1068, M2-8, M7-8, M5-7, YJM269 and YJM627, features a modification of the amino acid from S to G at position 452.
+The protein's natural variant, known as in strain: EAY1066 and YJM280, features a modification of the amino acid from D to N at position 465.
+The protein's natural variant, known as in strain: YJM339, features a modification of the amino acid from P to S at position 470.
+The protein's natural variant, known as in strain: EAY1068, M2-8, M7-8, M5-7 and YJM627, features a modification of the amino acid from L to F at position 607.
+The protein's natural variant, known as in strain: SK1, YJM320 and YJM339, features a modification of the amino acid from D to N at position 678.
+The protein's natural variant, known as in strain: SK1, YJM320 and YJM339, features a modification of the amino acid from P to L at position 703.
+The protein's natural variant, known as in strain: EAY1066, EAY1068, M2-8, M7-8, M5-7, SK1, YJM145, YJM269, YJM320, YJM339 and YJM627; forms a non-functional heterodimer with PMS1 from strain S288c, resulting in an accumulation of mutations in spore progeny of crosses between these strains, features a modification of the amino acid from D to G at position 761.
+The protein's natural variant, known as in BAMLAZ; without choanal atresia; no effect on protein abundance; no effect on localization to the nucleus; decreased sequence-specific DNA binding; decreased transcriptional activity;, features a modification of the amino acid from S to N at position 57.
+The protein's natural variant, known as in BAMLAZ; loss of sequence-specific DNA binding; loss of transcriptional activity;, features a modification of the amino acid from A to V at position 65.
+The protein's natural variant, known as in BAMLAZ; no effect on protein abundance; no effect on sequence-specific DNA binding; enhances transcriptional activity toward TG and TPO genes, features a modification of the amino acid from R to S at position 73.
+The protein's natural variant, known as in congenital hypothyroidism; with absence of thyroid agenesis; loss of sequence-specific DNA binding; loss of transcriptional activity;, features a modification of the amino acid from R to C at position 102.
+The protein's natural variant, known as in congenital hypothyroidism; slightly decreased sequence-specific DNA binding to the TPO promoter; 0.5 fold decreased transcriptional activity;, features a modification of the amino acid from N to D at position 132.
+The protein's natural variant, known as in congenital hypothyroidism; loss of sequence-specific DNA binding; loss of transcriptional activity, features a modification of the amino acid from F to S at position 137.
+The natural variant of this protein is characterized by an amino acid alteration from A to AAA at position 179.
+The protein's natural variant, known as in NMTC4; increased cell growth; increased cell migration; associated with increased expression of the WNT5A gene;, features a modification of the amino acid from A to G at position 248.
+The protein's natural variant, known as in HH7; is able to bind GnRH but with a reduced affinity in vitro;, features a modification of the amino acid from N to K at position 10.
+The protein's natural variant, known as in HH7;, features a modification of the amino acid from N to S at position 18.
+The protein's natural variant, known as in HH7;, features a modification of the amino acid from I to S at position 37.
+The protein's natural variant, known as in HH7; the patient also carries a mutation in FGFR1;, features a modification of the amino acid from L to V at position 83.
+The protein's natural variant, known as in HH7, features a modification of the amino acid from E to D at position 90.
+The protein's natural variant, known as in HH7; virtual abolition of GnRH agonist binding and agonist-stimulated phosphoinositide turnover; impairs GnRHR-effector coupling;, features a modification of the amino acid from E to K at position 90.
+The protein's natural variant, known as in HH7; some patients also carry mutations in FGFR1; decreases but does not eliminate GnRH binding;, features a modification of the amino acid from Q to R at position 106.
+The protein's natural variant, known as in HH7; complete loss of function;, features a modification of the amino acid from A to D at position 129.
+The protein's natural variant, known as in HH7; completely eliminates detectable GnRH-binding activity and prevents GnRH-induced stimulation of inositol phosphate accumulation in vitro;, features a modification of the amino acid from R to H at position 139.
+The protein's natural variant, known as in HH7;, features a modification of the amino acid from P to S at position 146.
+The protein's natural variant, known as in HH7; complete loss of the receptor-mediated signaling response;, features a modification of the amino acid from S to R at position 168.
+The protein's natural variant, known as in HH7; complete loss of ligand binding and receptor activation; specific receptor binding of radioisotope-labeled GnRH ligand is undetectable in transfected cells;, features a modification of the amino acid from A to T at position 171.
+The protein's natural variant, known as in HH7; altered hormone binding;, features a modification of the amino acid from S to R at position 217.
+The protein's natural variant, known as in HH7; unknown pathological significance; some patients also carry mutations in FGFR1; minimal effects upon receptor affinity but expression decreased; altered activation of phospholipase C;, features a modification of the amino acid from R to Q at position 262.
+The protein's natural variant, known as in HH7; unknown pathological significance;, features a modification of the amino acid from L to R at position 266.
+The protein's natural variant, known as in HH7; minimal effects upon receptor affinity but receptor expression decreased;, features a modification of the amino acid from Y to C at position 284.
+The protein's natural variant, known as found in autosomal recessive retinitis pigmentosa; unknown pathological significance; results in increased ciliary length;, features a modification of the amino acid from A to V at position 609.
+The protein's natural variant, known as in SCFI; loss of function in regulation of mitochondrial membrane potential, features a modification of the amino acid from S to P at position 61.
+The protein's natural variant, known as in SCFI;, features a modification of the amino acid from M to V at position 94.
+The protein's natural variant, known as in SCFI;, features a modification of the amino acid from M to I at position 106.
+The protein's natural variant, known as in SCFI;, features a modification of the amino acid from R to L at position 127.
+The protein's natural variant, known as in SCFI; decreased inorganic diphosphatase activity;, features a modification of the amino acid from P to L at position 167.
+The protein's natural variant, known as in SCFI and SCFAI; loss of function in regulation of mitochondrial membrane potential; decreased inorganic diphosphatase activity;, features a modification of the amino acid from E to K at position 172.
+The protein's natural variant, known as in SCFAI; decreased inorganic diphosphatase activity;, features a modification of the amino acid from P to L at position 228.
+The protein's natural variant, known as in SCFI;, features a modification of the amino acid from Q to P at position 294.
+The protein's natural variant, known as in beta-2, features a modification of the amino acid from Q to P at position 16.
+The protein's natural variant, known as in beta-2, features a modification of the amino acid from S to A at position 66.
+The protein's natural variant, known as in beta-2, features a modification of the amino acid from A to G at position 168.
+The natural variant of this protein is characterized by an amino acid alteration from W to R at position 92.
+The protein's natural variant, known as in strain: PLe, features a modification of the amino acid from A to S at position 111.
+The protein's natural variant, known as in strain: PLj7, features a modification of the amino acid from I to T at position 200.
+The protein's natural variant, known as in strain: PLj7, features a modification of the amino acid from I to V at position 240.
+The protein's natural variant, known as in strain: PLe, features a modification of the amino acid from L to F at position 254.
+The protein's natural variant, known as in strain: TW-183, features a modification of the amino acid from R to W at position 48.
+The natural variant of this protein is characterized by an amino acid alteration from P to Q at position 22.
+The natural variant of this protein is characterized by an amino acid alteration from YS to NA at position 25.
+The natural variant of this protein is characterized by an amino acid alteration from I to T at position 26.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 26.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 32.
+The natural variant of this protein is characterized by an amino acid alteration from VQ to AG at position 95.
+The protein's natural variant, known as in NPHS21; inhibited actin bundling capacity; slightly decreased interaction with PLCE1; disrupted EGF-induced diacylglycerol generation by PLCE1;, features a modification of the amino acid from R to Q at position 135.
+The protein's natural variant, known as in NPHS21; inhibited actin bundling capacity; decreases interaction with PLCE1; disrupted EGF-induced diacylglycerol generation by PLCE1;, features a modification of the amino acid from L to M at position 425.
+The protein's natural variant, known as in NPHS21; unknown pathological significance;, features a modification of the amino acid from R to H at position 446.
+The protein's natural variant, known as in OOMD10; unknown pathological significance; decreases protein level; does not affect interaction with MEI4 and IHO1; decreases MEI4 stability;, features a modification of the amino acid from C to G at position 133.
+The natural variant of this protein is characterized by an amino acid alteration from S to G at position 439.
+The protein's natural variant, known as in strain: GS-5, features a modification of the amino acid from V to I at position 21.
+The protein's natural variant, known as in strain: MT4239, features a modification of the amino acid from P to L at position 81.
+The protein's natural variant, known as in strain: GS-5, features a modification of the amino acid from D to V at position 106.
+The protein's natural variant, known as in strain: GS-5 and MT4467, features a modification of the amino acid from S to A at position 116.
+The protein's natural variant, known as in strain: GS-5, features a modification of the amino acid from A to T at position 126.
+The protein's natural variant, known as in strain: GS-5, MT4239 and MT4467, features a modification of the amino acid from SR to PK at position 151.
+The protein's natural variant, known as in strain: GS-5 and MT4467, features a modification of the amino acid from A to V at position 256.
+The protein's natural variant, known as in strain: MT4251, features a modification of the amino acid from R to N at position 425.
+The protein's natural variant, known as in strain: MT4245 and MT4251, features a modification of the amino acid from Y to D at position 519.
+The protein's natural variant, known as in strain: MT4245 and MT4251, features a modification of the amino acid from R to K at position 538.
+The protein's natural variant, known as in strain: MT4245 and MT4251, features a modification of the amino acid from Y to F at position 545.
+The protein's natural variant, known as in strain: MT4245, MT4251, MT4467 and MT8148, features a modification of the amino acid from N to D at position 597.
+The protein's natural variant, known as in strain: MT4245, MT4251, MT4467 and MT8148, features a modification of the amino acid from R to K at position 600.
+The protein's natural variant, known as in strain: GS-5, features a modification of the amino acid from A to T at position 601.
+The protein's natural variant, known as in strain: GS-5, features a modification of the amino acid from M to T at position 614.
+The protein's natural variant, known as in strain: MT8148, features a modification of the amino acid from T to I at position 727.
+The protein's natural variant, known as in strain: MT8148, features a modification of the amino acid from A to V at position 734.
+The protein's natural variant, known as in strain: MT4239, features a modification of the amino acid from L to F at position 964.
+The protein's natural variant, known as in strain: MT4239, features a modification of the amino acid from N to Y at position 1113.
+The protein's natural variant, known as in strain: MT4239, features a modification of the amino acid from A to T at position 1118.
+The protein's natural variant, known as in strain: GS-5, MT4239, MT4467 and MT8148, features a modification of the amino acid from I to V at position 1204.
+The protein's natural variant, known as in strain: MT8148, features a modification of the amino acid from V to I at position 1208.
+The protein's natural variant, known as in strain: GS-5, MT4467 and sMT8148, features a modification of the amino acid from DGH to NGY at position 1294.
+The protein's natural variant, known as in strain: MT8148, features a modification of the amino acid from I to V at position 1326.
+The protein's natural variant, known as in strain: GS-5, MT4239, MT4467 and MT8148, features a modification of the amino acid from T to A at position 1331.
+The protein's natural variant, known as in strain: MT8148, features a modification of the amino acid from R to K at position 1377.
+The protein's natural variant, known as in strain: MT8148, features a modification of the amino acid from V to I at position 1398.
+The protein's natural variant, known as in strain: MT4239, features a modification of the amino acid from D to N at position 1424.
+The protein's natural variant, known as in strain: MT4239 and MT8148, features a modification of the amino acid from V to I at position 1439.
+The protein's natural variant, known as in strain: MT8148, features a modification of the amino acid from S to P at position 1444.
+The protein's natural variant, known as in XHED; unknown pathological significance, features a modification of the amino acid from L to Q at position 51.
+The protein's natural variant, known as in XHED, features a modification of the amino acid from H to Y at position 54.
+The protein's natural variant, known as in XHED, features a modification of the amino acid from L to R at position 55.
+The protein's natural variant, known as in XHED, features a modification of the amino acid from C to R at position 60.
+The protein's natural variant, known as in XHED;, features a modification of the amino acid from Y to H at position 61.
+The protein's natural variant, known as in XHED;, features a modification of the amino acid from E to K at position 63.
+The protein's natural variant, known as in STHAGX1;, features a modification of the amino acid from R to G at position 65.
+The protein's natural variant, known as in XHED;, features a modification of the amino acid from R to L at position 69.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from P to L at position 118.
+The protein's natural variant, known as in XHED; unknown pathological significance, features a modification of the amino acid from S to C at position 125.
+The protein's natural variant, known as in XHED; unknown pathological significance, features a modification of the amino acid from Q to P at position 132.
+The protein's natural variant, known as in XHED; abolishes proteolytic processing;, features a modification of the amino acid from R to C at position 153.
+The protein's natural variant, known as in XHED; unknown pathological significance;, features a modification of the amino acid from R to H at position 153.
+The protein's natural variant, known as in XHED; abolishes proteolytic processing;, features a modification of the amino acid from R to C at position 155.
+The protein's natural variant, known as in XHED; abolishes proteolytic processing;, features a modification of the amino acid from R to C at position 156.
+The protein's natural variant, known as in XHED, features a modification of the amino acid from R to G at position 156.
+The protein's natural variant, known as in XHED; abolishes proteolytic processing;, features a modification of the amino acid from R to H at position 156.
+The protein's natural variant, known as in XHED, features a modification of the amino acid from R to S at position 156.
+The protein's natural variant, known as in XHED; abolishes proteolytic processing;, features a modification of the amino acid from K to N at position 158.
+The protein's natural variant, known as in XHED, features a modification of the amino acid from G to E at position 189.
+The protein's natural variant, known as in XHED, features a modification of the amino acid from G to A at position 198.
+The protein's natural variant, known as in XHED, features a modification of the amino acid from G to R at position 207.
+The protein's natural variant, known as in XHED, features a modification of the amino acid from G to V at position 207.
+The protein's natural variant, known as in XHED;, features a modification of the amino acid from P to L at position 209.
+The protein's natural variant, known as in XHED, features a modification of the amino acid from T to R at position 211.
+The protein's natural variant, known as in XHED, features a modification of the amino acid from G to D at position 218.
+The protein's natural variant, known as in XHED; unknown pathological significance, features a modification of the amino acid from G to D at position 221.
+The protein's natural variant, known as in XHED;, features a modification of the amino acid from G to A at position 224.
+The protein's natural variant, known as in XHED; loss of interaction with EDAR for isoform 1; decreased interaction with EDA2R for isoform 3; changed downstream signaling;, features a modification of the amino acid from H to L at position 252.
+The protein's natural variant, known as in XHED, features a modification of the amino acid from H to Y at position 252.
+The protein's natural variant, known as in XHED, features a modification of the amino acid from G to C at position 255.
+The protein's natural variant, known as in XHED; mild;, features a modification of the amino acid from G to D at position 255.
+The protein's natural variant, known as in STHAGX1; decreased interaction with EDAR for isoform 1; decreased interaction with EDA2R for isoform 3; changed downstream signaling;, features a modification of the amino acid from A to E at position 259.
+The protein's natural variant, known as in STHAGX1, features a modification of the amino acid from I to S at position 260.
+The protein's natural variant, known as in XHED, features a modification of the amino acid from L to R at position 266.
+The protein's natural variant, known as in XHED, features a modification of the amino acid from G to V at position 269.
+The protein's natural variant, known as in XHED, features a modification of the amino acid from W to G at position 274.
+The protein's natural variant, known as in XHED, features a modification of the amino acid from W to R at position 274.
+The protein's natural variant, known as in STHAGX1; decreased interaction with EDAR for isoform 1; decreased interaction with EDA2R for isoform 3; changed downstream signaling;, features a modification of the amino acid from R to C at position 289.
+The protein's natural variant, known as in STHAGX1, features a modification of the amino acid from R to L at position 289.
+The protein's natural variant, known as in XHED; when associated in cis with C-290; loss of function in EDAR-mediated signaling when associated in cis with C-290; not secreted when associated in cis with C-290;, features a modification of the amino acid from R to P at position 289.
+The protein's natural variant, known as in XHED; when associated in cis with P-289; loss of function in EDAR-mediated signaling when associated in cis with P-289; not secreted when associated in cis with P-289, features a modification of the amino acid from S to C at position 290.
+The protein's natural variant, known as in XHED;, features a modification of the amino acid from G to R at position 291.
+The protein's natural variant, known as in XHED, features a modification of the amino acid from G to W at position 291.
+The protein's natural variant, known as in XHED, features a modification of the amino acid from L to P at position 293.
+The protein's natural variant, known as in XHED, features a modification of the amino acid from L to V at position 296.
+The protein's natural variant, known as in XHED, features a modification of the amino acid from D to H at position 298.
+The protein's natural variant, known as in XHED, features a modification of the amino acid from D to Y at position 298.
+The protein's natural variant, known as in XHED, features a modification of the amino acid from G to D at position 299.
+The protein's natural variant, known as in XHED;, features a modification of the amino acid from G to S at position 299.
+The protein's natural variant, known as in XHED, features a modification of the amino acid from F to S at position 302.
+The protein's natural variant, known as in XHED; unknown pathological significance, features a modification of the amino acid from Y to H at position 304.
+The protein's natural variant, known as in XHED, features a modification of the amino acid from Q to H at position 306.
+The protein's natural variant, known as in XHED, features a modification of the amino acid from V to G at position 307.
+The protein's natural variant, known as in XHED; unknown pathological significance, features a modification of the amino acid from D to E at position 316.
+The protein's natural variant, known as in XHED, features a modification of the amino acid from S to R at position 319.
+The protein's natural variant, known as in XHED, features a modification of the amino acid from Y to C at position 320.
+The protein's natural variant, known as in XHED, features a modification of the amino acid from V to G at position 323.
+The protein's natural variant, known as in XHED; unknown pathological significance, features a modification of the amino acid from C to F at position 332.
+The protein's natural variant, known as in XHED;, features a modification of the amino acid from C to Y at position 332.
+The protein's natural variant, known as in STHAGX1; decreased interaction with EDAR for isoform 1; decreased interaction with EDA2R for isoform 3; changed downstream signaling;, features a modification of the amino acid from R to H at position 334.
+The protein's natural variant, known as in STHAGX1 and XHED;, features a modification of the amino acid from T to M at position 338.
+The protein's natural variant, known as in XHED; loss of interaction with EDAR for isoform 1; decreased interaction with EDA2R for isoform 3; changed downstream signaling, features a modification of the amino acid from Y to C at position 343.
+The protein's natural variant, known as in XHED, features a modification of the amino acid from C to Y at position 346.
+The protein's natural variant, known as in XHED;, features a modification of the amino acid from A to T at position 349.
+The protein's natural variant, known as in XHED; unknown pathological significance, features a modification of the amino acid from G to D at position 350.
+The protein's natural variant, known as in XHED, features a modification of the amino acid from L to P at position 354.
+The protein's natural variant, known as in XHED, features a modification of the amino acid from A to D at position 356.
+The protein's natural variant, known as in XHED;, features a modification of the amino acid from A to V at position 356.
+The protein's natural variant, known as in XHED;, features a modification of the amino acid from R to P at position 357.
+The protein's natural variant, known as in XHED;, features a modification of the amino acid from Q to E at position 358.
+The protein's natural variant, known as in XHED; unknown pathological significance, features a modification of the amino acid from Q to H at position 358.
+The protein's natural variant, known as in XHED, features a modification of the amino acid from I to N at position 360.
+The protein's natural variant, known as in XHED, features a modification of the amino acid from N to D at position 372.
+The protein's natural variant, known as in XHED, features a modification of the amino acid from M to I at position 373.
+The protein's natural variant, known as in XHED; decreased interaction with EDAR for isoform 1; decreased interaction with EDA2R for isoform 3; changed downstream signaling, features a modification of the amino acid from S to R at position 374.
+The protein's natural variant, known as in XHED;, features a modification of the amino acid from T to M at position 378.
+The protein's natural variant, known as in XHED, features a modification of the amino acid from T to P at position 378.
+The protein's natural variant, known as in XHED; loss of function in EDAR-mediated signaling; not secreted, features a modification of the amino acid from F to S at position 379.
+The protein's natural variant, known as in STHAGX1, features a modification of the amino acid from F to V at position 379.
+The protein's natural variant, known as in XHED, features a modification of the amino acid from G to R at position 381.
+The protein's natural variant, known as in XHED; unknown pathological significance, features a modification of the amino acid from G to V at position 381.
+The protein's natural variant, known as in MGCA7B; increased ATP hydrolysis activity; severely decreased ATP-dependent protein disaggregase activity;, features a modification of the amino acid from T to M at position 268.
+The protein's natural variant, known as in MGCA7B;, features a modification of the amino acid from Y to C at position 272.
+The natural variant of this protein is characterized by an amino acid alteration from R to W at position 327.
+The protein's natural variant, known as in SCN9, features a modification of the amino acid from T to K at position 388.
+The protein's natural variant, known as in MGCA7A; decreased ATP hydrolysis activity; decreased ATP-dependent protein disaggregase activity, features a modification of the amino acid from K to T at position 404.
+The protein's natural variant, known as in MGCA7B; decreased ATP hydrolysis activity; decreased ATP-dependent protein disaggregase activity; not changed mitochondrial respiration;, features a modification of the amino acid from R to G at position 408.
+The protein's natural variant, known as in MGCA7B;, features a modification of the amino acid from M to I at position 411.
+The protein's natural variant, known as in MGCA7A; decreased ATP hydrolysis activity; decreased ATP-dependent protein disaggregase activity, features a modification of the amino acid from P to L at position 427.
+The protein's natural variant, known as in MGCA7B, features a modification of the amino acid from EG to DP at position 436.
+The protein's natural variant, known as in MGCA7B;, features a modification of the amino acid from C to R at position 486.
+The protein's natural variant, known as in SCN9; decreased granulocyte differentiation; decreased ATP hydrolysis activity; decreased ATP-dependent protein disaggregase activity; does not render cells more sensitive to ER stress-induced apoptosis, features a modification of the amino acid from N to K at position 496.
+The protein's natural variant, known as in MGCA7B;, features a modification of the amino acid from E to K at position 501.
+The protein's natural variant, known as in SCN9; decreased granulocyte differentiation; decreased ATP hydrolysis activity; decreased ATP-dependent protein disaggregase activity; decreased mitochondrial respiration, features a modification of the amino acid from E to K at position 557.
+The protein's natural variant, known as in MGCA7A; decreased ATP hydrolysis activity; decreased ATP-dependent protein disaggregase activity, features a modification of the amino acid from G to R at position 560.
+The protein's natural variant, known as in SCN9; decreased granulocyte differentiation; loss of ATP hydrolysis activity; loss of ATP-dependent protein disaggregase activity; decreased mitochondrial respiration, features a modification of the amino acid from R to G at position 561.
+The protein's natural variant, known as in SCN9; decreased mitochondrial respiration, features a modification of the amino acid from R to Q at position 561.
+The protein's natural variant, known as in MGCA7A, features a modification of the amino acid from R to W at position 561.
+The protein's natural variant, known as in MGCA7B;, features a modification of the amino acid from Y to C at position 567.
+The protein's natural variant, known as in MGCA7B; loss of ATP hydrolysis activity; loss of ATP-dependent protein disaggregase activity;, features a modification of the amino acid from A to V at position 591.
+The protein's natural variant, known as normal ATP hydrolysis activity; normal ATP-dependent protein disaggregase activity, features a modification of the amino acid from R to H at position 603.
+The protein's natural variant, known as in MGCA7B;, features a modification of the amino acid from Y to C at position 617.
+The protein's natural variant, known as in SCN9; decreased granulocyte differentiation; loss of ATP hydrolysis activity; loss of ATP-dependent protein disaggregase activity; does not render cells more sensitive to ER stress-induced apoptosis, features a modification of the amino acid from R to C at position 620.
+The protein's natural variant, known as in MGCA7B; unknown pathological significance, features a modification of the amino acid from R to C at position 628.
+The protein's natural variant, known as in MGCA7B; unknown pathological significance; requires 2 nucleotide substitutions, features a modification of the amino acid from A to K at position 635.
+The protein's natural variant, known as in MGCA7B;, features a modification of the amino acid from G to V at position 646.
+The protein's natural variant, known as in MGCA7B;, features a modification of the amino acid from I to N at position 682.
+The protein's natural variant, known as in strain: PAK, features a modification of the amino acid from T to A at position 18.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to Q at position 326.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from V to M at position 574.
+The natural variant of this protein is characterized by an amino acid alteration from I to T at position 923.
+The protein's natural variant, known as in DFNA83; unknown pathological significance; reduced neurite length in otic sensory neuron-like cells from patient-derived indifferentiated pluripotent stem cells, features a modification of the amino acid from S to G at position 1400.
+The natural variant of this protein is characterized by an amino acid alteration from F to L at position 1838.
+The natural variant of this protein is characterized by an amino acid alteration from I to T at position 39.
+The protein's natural variant, known as in EPIDACH; expression in patient fibroblasts is reduced to 25% of control values in normoxic conditions; the mutant protein shows an impaired response to hypoxia;, features a modification of the amino acid from E to K at position 138.
+The protein's natural variant, known as in DFNA25;, features a modification of the amino acid from A to V at position 211.
+The protein's natural variant, known as in SEDCJD; decreased chondroitin sulfate biosynthetic process;, features a modification of the amino acid from R to W at position 222.
+The protein's natural variant, known as in SEDCJD; decreased chondroitin sulfate biosynthetic process;, features a modification of the amino acid from L to P at position 259.
+The protein's natural variant, known as in SEDCJD; loss of chondroitin 6-sulfotransferase activity;, features a modification of the amino acid from R to Q at position 304.
+The protein's natural variant, known as in SEDCJD;, features a modification of the amino acid from L to P at position 307.
+The protein's natural variant, known as in SEDCJD;, features a modification of the amino acid from E to K at position 372.
+The protein's natural variant, known as in clone 1800-2, features a modification of the amino acid from L to S at position 9.
+The protein's natural variant, known as in clone 1800-2, features a modification of the amino acid from T to A at position 35.
+The protein's natural variant, known as in clone 1800-2, features a modification of the amino acid from A to V at position 39.
+The protein's natural variant, known as in clone 1800-4, features a modification of the amino acid from S to N at position 51.
+The protein's natural variant, known as in clone 1800-2, features a modification of the amino acid from A to R at position 56.
+The protein's natural variant, known as in clone 1800-4, features a modification of the amino acid from N to G at position 76.
+The protein's natural variant, known as in clone 1800-4, features a modification of the amino acid from Q to G at position 109.
+The protein's natural variant, known as in clone 1800-2, features a modification of the amino acid from K to N at position 117.
+The natural variant of this protein is characterized by an amino acid alteration from S to G at position 146.
+The protein's natural variant, known as in strain: RA, features a modification of the amino acid from EC to SG at position 158.
+The protein's natural variant, known as in clones 1800-2 and 1800-4, features a modification of the amino acid from S to G at position 186.
+The protein's natural variant, known as in strain: RA, features a modification of the amino acid from A to G at position 204.
+The protein's natural variant, known as in clones 1800-2 and 1800-4, features a modification of the amino acid from WL to CV at position 251.
+The protein's natural variant, known as in strain: RA, features a modification of the amino acid from VD to H at position 262.
+The protein's natural variant, known as in clone 1800-4, features a modification of the amino acid from V to F at position 286.
+The protein's natural variant, known as in strain: RA, features a modification of the amino acid from V to L at position 286.
+The protein's natural variant, known as in clone 1800-2, features a modification of the amino acid from T to A at position 308.
+The natural variant of this protein is characterized by an amino acid alteration from E to D at position 313.
+The protein's natural variant, known as in clone 1800-2, features a modification of the amino acid from L to F at position 409.
+The protein's natural variant, known as in clone 1800-2, features a modification of the amino acid from K to Q at position 427.
+The protein's natural variant, known as in clone 1800-2, features a modification of the amino acid from R to W at position 430.
+The protein's natural variant, known as in clone 1800-2, features a modification of the amino acid from H to Y at position 457.
+The protein's natural variant, known as in clone 1800-2, features a modification of the amino acid from H to Q at position 461.
+The protein's natural variant, known as in strain: SF300, features a modification of the amino acid from A to C at position 106.
+The protein's natural variant, known as in strain: SF300, features a modification of the amino acid from E to D at position 153.
+The protein's natural variant, known as in strain: SF300, features a modification of the amino acid from RT to GA at position 162.
+The protein's natural variant, known as in strain: SF300, features a modification of the amino acid from S to G at position 185.
+The protein's natural variant, known as in strain: SF300, features a modification of the amino acid from I to T at position 258.
+The protein's natural variant, known as in strain: Guyane 11, features a modification of the amino acid from S to R at position 253.
+The protein's natural variant, known as in VWM;, features a modification of the amino acid from V to E at position 85.
+The protein's natural variant, known as found in a patient with Rett syndrome-like phenotype; unknown pathological significance;, features a modification of the amino acid from A to V at position 127.
+The protein's natural variant, known as in VWM; with ovarian failure;, features a modification of the amino acid from S to F at position 171.
+The protein's natural variant, known as in VWM;, features a modification of the amino acid from P to S at position 196.
+The protein's natural variant, known as in VWM;, features a modification of the amino acid from G to V at position 200.
+The protein's natural variant, known as in VWM; with and without ovarian failure;, features a modification of the amino acid from E to G at position 213.
+The protein's natural variant, known as in VWM, features a modification of the amino acid from C to Y at position 268.
+The protein's natural variant, known as in VWM;, features a modification of the amino acid from K to R at position 273.
+The protein's natural variant, known as in VWM;, features a modification of the amino acid from V to D at position 316.
+The protein's natural variant, known as in VWM;, features a modification of the amino acid from G to V at position 329.
+The protein's natural variant, known as in CFEOM2;, features a modification of the amino acid from A to V at position 72.
+The protein's natural variant, known as may be involved in congenital central hypoventilation syndrome;, features a modification of the amino acid from P to Q at position 256.
+The protein's natural variant, known as in strain: O44:K74, features a modification of the amino acid from A to T at position 54.
+The protein's natural variant, known as in strain: O44:K74, features a modification of the amino acid from L to V at position 90.
+The protein's natural variant, known as in strain: O44:K74, features a modification of the amino acid from R to H at position 126.
+The protein's natural variant, known as in strain: O44:K74, features a modification of the amino acid from N to S at position 143.
+The protein's natural variant, known as in strain: O44:K74, features a modification of the amino acid from R to Q at position 153.
+The protein's natural variant, known as in strain: O44:K74, features a modification of the amino acid from V to A at position 168.
+The protein's natural variant, known as in strain: ECOR 67, features a modification of the amino acid from W to S at position 58.
+The protein's natural variant, known as in strain: ECOR 13, ECOR 20, ECOR 26 and ECOR 70, features a modification of the amino acid from G to C at position 60.
+The protein's natural variant, known as in strain: ECOR 50, features a modification of the amino acid from G to R at position 64.
+The protein's natural variant, known as in strain: ECOR 51, ECOR 52, ECOR 57, ECOR 59, ECOR 62 and ECOR 64, features a modification of the amino acid from Q to K at position 135.
+The protein's natural variant, known as in strain: ECOR 67, features a modification of the amino acid from Q to R at position 153.
+The protein's natural variant, known as in strain: ECOR 35, features a modification of the amino acid from R to C at position 155.
+The protein's natural variant, known as found in a renal cell carcinoma sample; somatic mutation, features a modification of the amino acid from F to I at position 172.
+The protein's natural variant, known as in strain: NCIMB 9866, features a modification of the amino acid from D to A at position 74.
+The protein's natural variant, known as in CMS4B; impaired association with alpha CHRNA1 subunit of AChR;, features a modification of the amino acid from G to R at position 13.
+The protein's natural variant, known as in CMS4B; strongly reduces agonist affinity and gating efficiency;, features a modification of the amino acid from W to R at position 75.
+The protein's natural variant, known as in CMS4A; rare example of recessive inheritance;, features a modification of the amino acid from L to P at position 98.
+The protein's natural variant, known as in CMS4B; marked decrease in rate of AChR channel opening; reduction in frequency of open channel state and resistance to desensitization by ACh;, features a modification of the amino acid from P to L at position 141.
+The protein's natural variant, known as in CMS4B; fails to assemble with alpha CHRNA1 subunit of AChR;, features a modification of the amino acid from S to L at position 163.
+The protein's natural variant, known as in CMS4C; significantly reduced AChR expression;, features a modification of the amino acid from R to L at position 167.
+The protein's natural variant, known as in CMS4A; mild form with variable penetrance;, features a modification of the amino acid from L to F at position 241.
+The protein's natural variant, known as in CMS4C; prolongs burst open duration 2-fold by slowing the rate of channel closing;, features a modification of the amino acid from P to L at position 265.
+The protein's natural variant, known as in CMS4A; markedly prolonged channel openings in presence of agonist; as well as opening in the absence of agonist;, features a modification of the amino acid from T to P at position 284.
+The protein's natural variant, known as in CMS4A; slow-channel mutation; increases gating equilibrium constant by 25-fold, owing to increased opening rate and decreased closing rate; no effect on the choline dissociation rate constant;, features a modification of the amino acid from V to A at position 285.
+The protein's natural variant, known as in CMS4A; slows rate of AChR channel closure and increases apparent affinity for ACh; causes pathologic channel openings even in the absence of ACh resulting in a leaky channel;, features a modification of the amino acid from L to F at position 289.
+The protein's natural variant, known as in CMS4C; shortens burst duration 2-fold by slowing the rate of channel opening and speeding the rate of ACh dissociation; has a mild fast-channel kinetic effect on the AChR by shortening the long burst and increasing the decay of the endplate current;, features a modification of the amino acid from R to W at position 331.
+The protein's natural variant, known as in CMS4B; causes an increase in distributions of rates for channel opening and closing increasing the range of activation kinetics;, features a modification of the amino acid from A to P at position 431.
+The protein's natural variant, known as in IBMPFD1; cultured cells expressing the mutant protein show a marked general increase in the level of ubiquitin-conjugated proteins and impaired protein degradation through the endoplasmic reticulum-associated degradation (ERAD) pathway; shows strongly reduced affinity for ADP and increased affinity for ATP; abolishes enhancement of K-315 methylation by ASPSCR1; decreased interaction with CAV1 and UBXN6;, features a modification of the amino acid from R to G at position 95.
+The protein's natural variant, known as in CMT2Y; increased ATPase activity;, features a modification of the amino acid from G to E at position 97.
+The protein's natural variant, known as in IBMPFD1; unknown pathological significance, features a modification of the amino acid from I to F at position 126.
+The protein's natural variant, known as in IBMPFD1; also in one patient without evidence of Paget disease of the bone;, features a modification of the amino acid from R to C at position 155.
+The protein's natural variant, known as in FTDALS6 and IBMPFD1; properly assembles into a hexameric structure; cultured cells expressing the mutant protein show a marked general increase in the level of ubiquitin-conjugated proteins and impaired protein degradation through the endoplasmic reticulum-associated degradation (ERAD) pathway; shows strongly reduced affinity for ADP and increased affinity for ATP; shows normal ATPase activity according to PubMed:16321991 while according to PubMed:25878907 and PubMed:25125609 shows increased ATPase activity; no defect in ubiquitin-dependent protein degradation by the proteasome; impaired autophagic function; defective maturation of ubiquitin-containing autophagosomes; decreased interaction with CAV1 and UBXN6; decreased endosome to lysosome transport via multivesicular body sorting pathway of CAV1; decreases the arsenite-induced stress granules (SGs) clearance process;, features a modification of the amino acid from R to H at position 155.
+The protein's natural variant, known as in IBMPFD1;, features a modification of the amino acid from R to L at position 155.
+The protein's natural variant, known as in IBMPFD1;, features a modification of the amino acid from R to P at position 155.
+The protein's natural variant, known as in IBMPFD1; impaired autophagic function;, features a modification of the amino acid from R to S at position 155.
+The protein's natural variant, known as in FTDALS6;, features a modification of the amino acid from R to G at position 159.
+The protein's natural variant, known as in IBMPFD1; without frontotemporal dementia; abolishes enhancement of K-315 methylation by ASPSCR1;, features a modification of the amino acid from R to H at position 159.
+The protein's natural variant, known as in CMT2Y; normal ATPase activity; impaired autophagic function;, features a modification of the amino acid from E to K at position 185.
+The protein's natural variant, known as in FTDALS6 and IBMPFD1; abolishes enhancement of K-315 methylation by ASPSCR1;, features a modification of the amino acid from R to Q at position 191.
+The protein's natural variant, known as in IBMPFD1; increased ATPase activity; impaired autophagic function;, features a modification of the amino acid from L to W at position 198.
+The protein's natural variant, known as in IBMPFD1; increased ATPase activity; no defect in ubiquitin-dependent protein degradation by the proteasome; impaired autophagic function; defect in maturation of ubiquitin-containing autophagosomes; decreased interaction with CAV1 and UBXN6;, features a modification of the amino acid from A to E at position 232.
+The protein's natural variant, known as in IBMPFD1; unknown pathological significance;, features a modification of the amino acid from N to H at position 387.
+The protein's natural variant, known as in FTDALS6;, features a modification of the amino acid from D to N at position 592.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from H to R at position 474.
+The protein's natural variant, known as in TTD3;, features a modification of the amino acid from L to P at position 21.
+The protein's natural variant, known as found in patients with Stickler syndrome; unknown pathological significance;, features a modification of the amino acid from C to Y at position 676.
+The protein's natural variant, known as in strain: Beverley, features a modification of the amino acid from Y to H at position 6.
+The protein's natural variant, known as in strain: Beverley, features a modification of the amino acid from K to R at position 91.
+The protein's natural variant, known as in strain: Beverley, features a modification of the amino acid from Q to R at position 101.
+The natural variant of this protein is characterized by an amino acid alteration from L to P at position 1.
+The protein's natural variant, known as in allele CYP3A5*8;, features a modification of the amino acid from R to C at position 28.
+The protein's natural variant, known as in allele CYP3A5*4;, features a modification of the amino acid from Q to R at position 200.
+The protein's natural variant, known as in allele CYP3A5*9;, features a modification of the amino acid from A to T at position 337.
+The protein's natural variant, known as in allele CYP3A5*2;, features a modification of the amino acid from T to N at position 398.
+The protein's natural variant, known as in a breast pleomorphic lobular carcinoma sample; somatic mutation, features a modification of the amino acid from L to F at position 560.
+The protein's natural variant, known as in an ovarian serous carcinoma sample; somatic mutation;, features a modification of the amino acid from A to S at position 877.
+The protein's natural variant, known as in NBLST3; somatic mutation;, features a modification of the amino acid from D to N at position 1091.
+The protein's natural variant, known as in NBLST3;, features a modification of the amino acid from G to A at position 1128.
+The protein's natural variant, known as in NBLST3;, features a modification of the amino acid from T to M at position 1151.
+The protein's natural variant, known as in NBLST3; somatic mutation;, features a modification of the amino acid from M to R at position 1166.
+The protein's natural variant, known as in NBLST3; somatic mutation;, features a modification of the amino acid from I to N at position 1171.
+The protein's natural variant, known as in NBLST3;, features a modification of the amino acid from F to C at position 1174.
+The protein's natural variant, known as in NBLST3; somatic mutation;, features a modification of the amino acid from F to I at position 1174.
+The protein's natural variant, known as in NBLST3; somatic mutation; constitutively activated; retained in the endoplasmic reticulum and Golgi compartments;, features a modification of the amino acid from F to L at position 1174.
+The protein's natural variant, known as in NBLST3; somatic mutation; constitutively activated; retained in the endoplasmic reticulum and Golgi compartments;, features a modification of the amino acid from F to V at position 1174.
+The protein's natural variant, known as in NBLST3;, features a modification of the amino acid from R to P at position 1192.
+The protein's natural variant, known as in NBLST3; somatic mutation, features a modification of the amino acid from A to T at position 1234.
+The protein's natural variant, known as in NBLST3; somatic mutation;, features a modification of the amino acid from F to C at position 1245.
+The protein's natural variant, known as in NBLST3; somatic mutation;, features a modification of the amino acid from F to V at position 1245.
+The protein's natural variant, known as in NBLST3; somatic mutation;, features a modification of the amino acid from I to T at position 1250.
+The protein's natural variant, known as observed in neuroblastoma;, features a modification of the amino acid from R to L at position 1275.
+The protein's natural variant, known as in NBLST3; constitutively activated; retained in the endoplasmic reticulum and Golgi compartments;, features a modification of the amino acid from R to Q at position 1275.
+The protein's natural variant, known as in NBLST3; somatic mutation;, features a modification of the amino acid from Y to S at position 1278.
+The protein's natural variant, known as in gastric-carcinoma cell line, features a modification of the amino acid from G to R at position 11.
+The protein's natural variant, known as in gastric-carcinoma cell line, features a modification of the amino acid from A to E at position 149.
+The natural variant of this protein is characterized by an amino acid alteration from E to Q at position 156.
+The protein's natural variant, known as in gastric-carcinoma cell line, features a modification of the amino acid from D to G at position 190.
+The protein's natural variant, known as in strain: HNI, features a modification of the amino acid from M to V at position 13.
+The protein's natural variant, known as in strain: HNI, features a modification of the amino acid from A to P at position 155.
+The protein's natural variant, known as in strain: HNI, features a modification of the amino acid from S to T at position 353.
+The protein's natural variant, known as the protein is normally bound to microtubules;, features a modification of the amino acid from N to S at position 343.
+The protein's natural variant, known as in XLID101; the mutant is abnormally localized in aggregates or enclosed in cytoplasmic vesicles rather than being bound to microtubules;, features a modification of the amino acid from R to Q at position 347.
+The protein's natural variant, known as in LIS3;, features a modification of the amino acid from I to L at position 188.
+The protein's natural variant, known as in LIS3;, features a modification of the amino acid from P to T at position 263.
+The protein's natural variant, known as in LIS3;, features a modification of the amino acid from R to C at position 264.
+The protein's natural variant, known as in LIS3, features a modification of the amino acid from L to F at position 286.
+The protein's natural variant, known as in LIS3;, features a modification of the amino acid from R to C at position 402.
+The protein's natural variant, known as in LIS3;, features a modification of the amino acid from R to H at position 402.
+The protein's natural variant, known as in LIS3;, features a modification of the amino acid from R to L at position 402.
+The protein's natural variant, known as in LIS3;, features a modification of the amino acid from S to L at position 419.
+The protein's natural variant, known as associated with F-303 in San Diego; partial thyroxine-binding globulin deficiency;, features a modification of the amino acid from S to T at position 43.
+The protein's natural variant, known as gary; severe thyroxine-binding globulin deficiency;, features a modification of the amino acid from I to N at position 116.
+The protein's natural variant, known as montreal/TBG-M; partial thyroxine-binding globulin deficiency;, features a modification of the amino acid from A to P at position 133.
+The protein's natural variant, known as tBG-S/Slow;, features a modification of the amino acid from D to N at position 191.
+The protein's natural variant, known as tBG-A/Aborigine;, features a modification of the amino acid from A to T at position 211.
+The protein's natural variant, known as cD5; complete thyroxine-binding globulin deficiency;, features a modification of the amino acid from L to P at position 247.
+The protein's natural variant, known as associated with T-43 in San Diego;, features a modification of the amino acid from L to F at position 303.
+The protein's natural variant, known as quebec; partial thyroxine-binding globulin deficiency;, features a modification of the amino acid from H to Y at position 351.
+The protein's natural variant, known as kumamoto; partial thyroxine-binding globulin deficiency;, features a modification of the amino acid from P to L at position 383.
+The protein's natural variant, known as in pseudo-NALD;, features a modification of the amino acid from G to C at position 178.
+The protein's natural variant, known as in pseudo-NALD;, features a modification of the amino acid from S to L at position 184.
+The protein's natural variant, known as in pseudo-NALD, features a modification of the amino acid from G to V at position 231.
+The protein's natural variant, known as in MITCH; gain-of-function; increased dimerization; increased protein levels and peroxisomal acyl-coenzyme A oxidase function; increased levels of reactive oxygen species; no effect on VLCFA levels; no effect on peroxisome location; causes Schwann cell death and myelination defects;, features a modification of the amino acid from N to S at position 237.
+The protein's natural variant, known as in pseudo-NALD;, features a modification of the amino acid from M to V at position 278.
+The protein's natural variant, known as in pseudo-NALD;, features a modification of the amino acid from Q to R at position 309.
+The protein's natural variant, known as in pseudo-NALD;, features a modification of the amino acid from S to P at position 310.
+The protein's natural variant, known as in Pseudo-NALD; unknown pathological significance, features a modification of the amino acid from F to S at position 420.
+The protein's natural variant, known as in NEDBGF, features a modification of the amino acid from V to M at position 128.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from R to C at position 332.
+The protein's natural variant, known as in strain: Korean, features a modification of the amino acid from R to Q at position 132.
+The protein's natural variant, known as in strain: BNS3, features a modification of the amino acid from P to L at position 77.
+The protein's natural variant, known as found in patients with teratozoospermia; unknown pathological significance; sperm heads are malformed and contain vacuoles; chromatin packaging and structure is abnormal with an increase in fragmented DNA; decreases sperm filamentous structure formation; loss of SEPTIN14 and ACTN4 localization to cell filament structures; no effect on interaction with ACTN4;, features a modification of the amino acid from A to T at position 123.
+The protein's natural variant, known as found in patients with teratozoospermia; unknown pathological significance; sperm heads are malformed and contain vacuoles; chromatin packaging and structure is abnormal with an increase in fragmented DNA; decreases sperm filamentous structure formation; loss of SEPTIN14 and ACTN4 localization to cell filament structures; no effect on interaction with ACTN4;, features a modification of the amino acid from I to T at position 333.
+The protein's natural variant, known as in strain: TRPA2/COLVB, features a modification of the amino acid from C to S at position 13.
+The protein's natural variant, known as in NPHS5;, features a modification of the amino acid from H to R at position 147.
+The protein's natural variant, known as in PIERS; without ocular abnormalities;, features a modification of the amino acid from R to Q at position 246.
+The protein's natural variant, known as in PIERS;, features a modification of the amino acid from R to W at position 246.
+The protein's natural variant, known as in PIERS and NPHS5; with mild ocular abnormalities;, features a modification of the amino acid from C to R at position 321.
+The protein's natural variant, known as in NPHS5; unknown pathological significance;, features a modification of the amino acid from R to H at position 644.
+The protein's natural variant, known as in NPHS5; unknown pathological significance;, features a modification of the amino acid from L to V at position 1258.
+The protein's natural variant, known as in PIERS and NPHS5; with mild ocular abnormalities; associated with F-1393;, features a modification of the amino acid from N to K at position 1380.
+The protein's natural variant, known as in PIERS and NPHS5; with mild ocular abnormalities; associated with K-1380;, features a modification of the amino acid from L to F at position 1393.
+The protein's natural variant, known as in ASD7; somatic mutation, features a modification of the amino acid from L to P at position 7.
+The protein's natural variant, known as in ASD7;, features a modification of the amino acid from K to I at position 15.
+The protein's natural variant, known as in ASD7; somatic mutation, features a modification of the amino acid from N to S at position 19.
+The protein's natural variant, known as in TOF and ASD7;, features a modification of the amino acid from E to Q at position 21.
+The protein's natural variant, known as in ASD7 and TOF;, features a modification of the amino acid from Q to P at position 22.
+The protein's natural variant, known as in ASD7, TOF, CHNG5, HLHS2 and CTHM; unknown pathological significance; exhibits significant functional impairment with reduction of transactivation properties and dominant-negative effect; the mutant protein activity on the DIO2, TG and TPO promoters is significantly impaired;, features a modification of the amino acid from R to C at position 25.
+The protein's natural variant, known as in ASD7; somatic mutation;, features a modification of the amino acid from S to P at position 45.
+The protein's natural variant, known as in ASD7; somatic mutation;, features a modification of the amino acid from F to L at position 51.
+The protein's natural variant, known as in VSD3; significantly reduced activation of NPPA gene compared to wild-type;, features a modification of the amino acid from P to A at position 59.
+The protein's natural variant, known as in ASD7;, features a modification of the amino acid from A to V at position 63.
+The protein's natural variant, known as in ASD7; somatic mutation, features a modification of the amino acid from L to P at position 69.
+The protein's natural variant, known as in ASD7; somatic mutation, features a modification of the amino acid from P to L at position 77.
+The protein's natural variant, known as in ASD7; somatic mutation, features a modification of the amino acid from C to R at position 114.
+The protein's natural variant, known as in ASD7; somatic mutation, features a modification of the amino acid from C to S at position 114.
+The protein's natural variant, known as in ASD7; somatic mutation, features a modification of the amino acid from K to R at position 118.
+The protein's natural variant, known as in CHNG5; exhibits a significant functional impairment with reduction of transactivation properties and dominant-negative effect which was associated with reduced DNA binding;, features a modification of the amino acid from A to S at position 119.
+The protein's natural variant, known as in ASD7; somatic mutation, features a modification of the amino acid from K to R at position 124.
+The protein's natural variant, known as in ASD7; somatic mutation, features a modification of the amino acid from E to V at position 126.
+The protein's natural variant, known as in ASD7;, features a modification of the amino acid from A to E at position 127.
+The protein's natural variant, known as in ASD7; somatic mutation;, features a modification of the amino acid from P to S at position 133.
+The protein's natural variant, known as in ASD7; somatic mutation, features a modification of the amino acid from A to T at position 135.
+The protein's natural variant, known as in ASD7, features a modification of the amino acid from R to C at position 142.
+The protein's natural variant, known as in ASD7; somatic mutation, features a modification of the amino acid from L to P at position 144.
+The protein's natural variant, known as in CHNG5; exhibits a significant functional impairment with reduction of transactivation properties and dominant-negative effect which was associated with reduced DNA binding;, features a modification of the amino acid from R to P at position 161.
+The protein's natural variant, known as in ASD7;, features a modification of the amino acid from T to M at position 178.
+The protein's natural variant, known as in ASD7; somatic mutation;, features a modification of the amino acid from K to E at position 183.
+The protein's natural variant, known as in ASD7, features a modification of the amino acid from Q to H at position 187.
+The protein's natural variant, known as in ASD7, features a modification of the amino acid from N to K at position 188.
+The protein's natural variant, known as in ASD7, features a modification of the amino acid from R to G at position 189.
+The protein's natural variant, known as in ASD7;, features a modification of the amino acid from R to C at position 190.
+The protein's natural variant, known as in ASD7, features a modification of the amino acid from Y to C at position 191.
+The protein's natural variant, known as in ASD7; somatic mutation, features a modification of the amino acid from K to R at position 192.
+The protein's natural variant, known as in ASD7; somatic mutation, features a modification of the amino acid from K to T at position 192.
+The protein's natural variant, known as in ASD7; somatic mutation, features a modification of the amino acid from K to R at position 194.
+The protein's natural variant, known as in ASD7; somatic mutation, features a modification of the amino acid from V to E at position 205.
+The protein's natural variant, known as in TOF and ASD7;, features a modification of the amino acid from R to C at position 216.
+The protein's natural variant, known as in ASD7 and TOF; somatic mutation;, features a modification of the amino acid from A to V at position 219.
+The protein's natural variant, known as in ASD7; somatic mutation;, features a modification of the amino acid from D to N at position 226.
+The protein's natural variant, known as found in patients with isolated congenital asplenia; unknown pathological significance; does not affect DNA binding; impairs transactivation activity;, features a modification of the amino acid from P to H at position 236.
+The protein's natural variant, known as in ASD7; somatic mutation, features a modification of the amino acid from Y to H at position 248.
+The protein's natural variant, known as in ASD7;, features a modification of the amino acid from P to T at position 275.
+The protein's natural variant, known as in ASD7; somatic mutation;, features a modification of the amino acid from S to F at position 279.
+The protein's natural variant, known as in ASD7; somatic mutation, features a modification of the amino acid from S to P at position 279.
+The protein's natural variant, known as in ASD7; somatic mutation, features a modification of the amino acid from A to V at position 281.
+The protein's natural variant, known as in VSD3;, features a modification of the amino acid from P to Q at position 283.
+The protein's natural variant, known as in ASD7; somatic mutation, features a modification of the amino acid from A to V at position 286.
+The protein's natural variant, known as in ASD7; somatic mutation, features a modification of the amino acid from N to H at position 294.
+The protein's natural variant, known as in ASD7; somatic mutation;, features a modification of the amino acid from D to G at position 299.
+The protein's natural variant, known as in ASD7; somatic mutation, features a modification of the amino acid from S to G at position 305.
+The protein's natural variant, known as in ASD7; somatic mutation, features a modification of the amino acid from G to S at position 320.
+The protein's natural variant, known as in ASD7; somatic mutation, features a modification of the amino acid from R to Q at position 322.
+The protein's natural variant, known as in ASD7 and TOF, features a modification of the amino acid from A to T at position 323.
+The protein's natural variant, known as retains the ability to associate with HDL particles;, features a modification of the amino acid from R to H at position 92.
+The protein's natural variant, known as associated with asthma and atopy; retains the ability to associate with HDL particles;, features a modification of the amino acid from I to T at position 198.
+The protein's natural variant, known as in PAFAD; loss of function; risk factor for coronary arthery disease and stroke;, features a modification of the amino acid from V to F at position 279.
+The protein's natural variant, known as in PAFAD; loss of function;, features a modification of the amino acid from Q to R at position 281.
+The protein's natural variant, known as retains the ability to associate with HDL particles;, features a modification of the amino acid from V to A at position 379.
+The protein's natural variant, known as in METAG;, features a modification of the amino acid from H to L at position 44.
+The protein's natural variant, known as in DFNA56;, features a modification of the amino acid from V to M at position 1773.
+The protein's natural variant, known as in DFNA56;, features a modification of the amino acid from T to S at position 1796.
+The protein's natural variant, known as probable disease-associated variant found in a patient with moderate intellectual disability, authism and intractable epilepsy, features a modification of the amino acid from R to P at position 138.
+The protein's natural variant, known as in allele NOD(DTW), features a modification of the amino acid from S to N at position 94.
+The natural variant of this protein is characterized by an amino acid alteration from L to F at position 3.
+The protein's natural variant, known as in IDDSELD, features a modification of the amino acid from V to G at position 129.
+The protein's natural variant, known as in IDDSELD, features a modification of the amino acid from R to W at position 1885.
+The protein's natural variant, known as in IDDSELD, features a modification of the amino acid from R to C at position 1902.
+The protein's natural variant, known as in IDDSELD, features a modification of the amino acid from F to L at position 1945.
+The protein's natural variant, known as in MC1DN29; decreased function in complex I assembly;, features a modification of the amino acid from G to V at position 212.
+The protein's natural variant, known as in RENS1; impairs interaction with WBP11, CGAS, SF3B1 and ATN1;, features a modification of the amino acid from Y to C at position 65.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from R to W at position 224.
+The protein's natural variant, known as probable disease-associated variant found in a patient with autism;, features a modification of the amino acid from P to L at position 244.
+The protein's natural variant, known as in HYDM4; unknown pathological significance, features a modification of the amino acid from S to P at position 401.
+The protein's natural variant, known as does not change ATP-induced inward current; does not change affinity for ATP;, features a modification of the amino acid from A to S at position 6.
+The protein's natural variant, known as does not change protein expression; does not affect membrane subcellular location; increases ATP-induced inward current;, features a modification of the amino acid from G to S at position 135.
+The protein's natural variant, known as does not change ATP-induced inward current; does not change affinity for ATP;, features a modification of the amino acid from S to G at position 242.
+The protein's natural variant, known as may influence susceptibility to multiple sclerosis in the presence of variants M-205 and S-361 in P2RX7; does not affect membrane subcellular location; reduces ATP-induced inward current; decreases affinity for ATP;, features a modification of the amino acid from Y to C at position 315.
+The protein's natural variant, known as in strain: AR39, J138 and TW-183, features a modification of the amino acid from T to A at position 177.
+The protein's natural variant, known as in strain: K12 / BW25113, may not bind DNA, features a modification of the amino acid from G to V at position 61.
+The protein's natural variant, known as in allele A3Z3; haplotype 5; confers resistance to FIV vif-mediated degradation, features a modification of the amino acid from A to I at position 65.
+The protein's natural variant, known as in allele A3Z3; haplotype 2; 3; 4 and 7, features a modification of the amino acid from A to S at position 65.
+The protein's natural variant, known as in allele A3Z3; haplotype 3 and 7, features a modification of the amino acid from R to Q at position 68.
+The protein's natural variant, known as in allele A3Z3; haplotype 3, features a modification of the amino acid from A to T at position 94.
+The protein's natural variant, known as in allele A3Z3; haplotype 4 and 6, features a modification of the amino acid from V to I at position 96.
+The protein's natural variant, known as in MAC-41S, features a modification of the amino acid from A to S at position 110.
+The protein's natural variant, known as in RBS;, features a modification of the amino acid from W to G at position 539.
+The protein's natural variant, known as in strain: cv. Pin Gaew 53, features a modification of the amino acid from HLQQAC to QPC at position 423.
+The protein's natural variant, known as in COXPD28; loss of S-adenosyl-L-methionine/S-adenosyl-L-homocysteine antiporter activity;, features a modification of the amino acid from A to V at position 102.
+The protein's natural variant, known as in COXPD28; unknown pathological significance; decreased S-adenosyl-L-methionine/S-adenosyl-L-homocysteine antiporter activity, features a modification of the amino acid from E to G at position 135.
+The protein's natural variant, known as in COXPD28; unknown pathological significance; decreased protein abundance; decreased S-adenosyl-L-methionine/S-adenosyl-L-homocysteine antiporter activity, features a modification of the amino acid from R to Q at position 142.
+The protein's natural variant, known as in COXPD28; decreased S-adenosyl-L-methionine/S-adenosyl-L-homocysteine antiporter activity;, features a modification of the amino acid from V to G at position 148.
+The protein's natural variant, known as in COXPD28; loss of S-adenosyl-L-methionine/S-adenosyl-L-homocysteine antiporter activity;, features a modification of the amino acid from P to L at position 199.
+The protein's natural variant, known as in MC1DN35; decreased protein abundance; decreased CHCHD4-mediated oxidation; loss of mitochondrial localization; retained in the cytosol; loss of function in mitochondrial respiratory chain complex I assembly, features a modification of the amino acid from C to S at position 107.
+The protein's natural variant, known as in AICSR; reduced activity;, features a modification of the amino acid from L to W at position 141.
+The protein's natural variant, known as in AICSR; no loss of activity;, features a modification of the amino acid from A to V at position 189.
+The protein's natural variant, known as in AICSR; markedly reduced activity;, features a modification of the amino acid from L to P at position 222.
+The protein's natural variant, known as in AICSR; complete loss of activity, features a modification of the amino acid from D to DGD at position 271.
+The protein's natural variant, known as in AICSR; loss of activity;, features a modification of the amino acid from R to W at position 353.
+The protein's natural variant, known as in AICSR; markedly reduced activity;, features a modification of the amino acid from A to V at position 359.
+The protein's natural variant, known as in AICSR; complete loss of activity;, features a modification of the amino acid from V to E at position 415.
+The protein's natural variant, known as in IMD76; no effect on protein levels; formation of large cell membrane-dissociated agglomerations; failed to facilitate the formation of clathrin-coated vesicles; impaired TCR internalization, features a modification of the amino acid from A to P at position 34.
+The protein's natural variant, known as in IMD76; no effect on protein levels; loss of clathrin-coated vesicles location and association with cell membrane; failed to facilitate the formation of clathrin-coated vesicles; impaired TCR internalization, features a modification of the amino acid from R to P at position 679.
+The natural variant of this protein is characterized by an amino acid alteration from D to E at position 24.
+The protein's natural variant, known as found in a patient with isolated coloboma; increases interaction with actin, features a modification of the amino acid from N to S at position 608.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from K to R at position 114.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to Q at position 129.
+The natural variant of this protein is characterized by an amino acid alteration from S to G at position 230.
+The protein's natural variant, known as in LIBF; loss of autocatalytic processing; decreased protein abundance; decreased phosphatidylserine decarboxylase activity; changed mitochondrion organization;, features a modification of the amino acid from R to Q at position 277.
+The protein's natural variant, known as in LIBF; loss of autocatalytic processing; probably decreased phosphatidylserine decarboxylase activity; changed mitochondrion organization; patient-derived fibroblasts show fragmented mitochondrial morphology around the nucleus; decreased cell viability with increased CASP3 and CASP7 activation, features a modification of the amino acid from C to Y at position 300.
+The protein's natural variant, known as in SPENCDI, features a modification of the amino acid from K to M at position 52.
+The protein's natural variant, known as in SPENCDI;, features a modification of the amino acid from T to I at position 89.
+The protein's natural variant, known as in SPENCDI;, features a modification of the amino acid from G to R at position 109.
+The protein's natural variant, known as in SPENCDI;, features a modification of the amino acid from L to P at position 201.
+The protein's natural variant, known as in SPENCDI;, features a modification of the amino acid from G to R at position 215.
+The protein's natural variant, known as in SPENCDI, features a modification of the amino acid from D to N at position 241.
+The protein's natural variant, known as in SPENCDI;, features a modification of the amino acid from N to H at position 262.
+The protein's natural variant, known as in SPENCDI;, features a modification of the amino acid from M to K at position 264.
+The protein's natural variant, known as in Okinawa habu, features a modification of the amino acid from M to V at position 34.
+The protein's natural variant, known as in Okinawa habu, features a modification of the amino acid from R to C at position 313.
+The protein's natural variant, known as in one individual with tumoral calcinosis;, features a modification of the amino acid from D to N at position 117.
+The protein's natural variant, known as rare variant; found in a patient with hypertrophic cardiomyopathy; unknown pathological significance;, features a modification of the amino acid from S to L at position 5.
+The natural variant of this protein is characterized by an amino acid alteration from S to R at position 61.
+The protein's natural variant, known as rare variant; found in a patient with hypertrophic cardiomyopathy; unknown pathological significance;, features a modification of the amino acid from F to S at position 73.
+The protein's natural variant, known as rare variant; found in a patient with hypertrophic cardiomyopathy; unknown pathological significance;, features a modification of the amino acid from R to C at position 86.
+The protein's natural variant, known as rare variant; found in a patient with hypertrophic cardiomyopathy; unknown pathological significance;, features a modification of the amino acid from R to H at position 86.
+The protein's natural variant, known as rare variant; found in a patient with hypertrophic cardiomyopathy; unknown pathological significance, features a modification of the amino acid from I to F at position 101.
+The protein's natural variant, known as rare variant; found in a patient with hypertrophic cardiomyopathy; unknown pathological significance;, features a modification of the amino acid from T to M at position 232.
+The natural variant of this protein is characterized by an amino acid alteration from D to N at position 254.
+The natural variant of this protein is characterized by an amino acid alteration from M to I at position 305.
+The protein's natural variant, known as rare variant; found in a patient with hypertrophic cardiomyopathy; unknown pathological significance;, features a modification of the amino acid from A to D at position 318.
+The natural variant of this protein is characterized by an amino acid alteration from A to D at position 321.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from M to MLGRREEWQRQGSPVSRRLSARRGPQAPGTRLPRRHPARAFPAATM at position 1.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from I to T at position 280.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from M to V at position 635.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from I to V at position 1025.
+The protein's natural variant, known as decreased function in taurocholate transport;, features a modification of the amino acid from R to C at position 21.
+The protein's natural variant, known as decreased function in taurocholate transport;, features a modification of the amino acid from M to T at position 39.
+The protein's natural variant, known as decreased function in taurocholate transport;, features a modification of the amino acid from S to L at position 41.
+The protein's natural variant, known as decreased function in taurocholate transport;, features a modification of the amino acid from A to T at position 64.
+The protein's natural variant, known as severely decreased function in taurocholate transport;, features a modification of the amino acid from P to T at position 73.
+The protein's natural variant, known as in FHCA2; decreased function in taurocholate transport;, features a modification of the amino acid from I to T at position 88.
+The protein's natural variant, known as loss of function in taurocholate transport;, features a modification of the amino acid from L to P at position 138.
+The protein's natural variant, known as decreased function in taurocholate transport;, features a modification of the amino acid from I to M at position 159.
+The protein's natural variant, known as decreased function in taurocholate transport;, features a modification of the amino acid from R to Q at position 180.
+The protein's natural variant, known as decreased function in taurocholate transport;, features a modification of the amino acid from G to E at position 190.
+The protein's natural variant, known as in FHCA2;, features a modification of the amino acid from S to R at position 199.
+The protein's natural variant, known as decreased transport of taurocholate and cholate; decreased transport of estron sulfate; decreased expression at the cell membrane due to intracellular retention;, features a modification of the amino acid from I to T at position 223.
+The protein's natural variant, known as slightly decreased function in taurocholate transport;, features a modification of the amino acid from I to T at position 232.
+The protein's natural variant, known as severely decreased function in taurocholate transport;, features a modification of the amino acid from F to L at position 234.
+The protein's natural variant, known as loss of function in taurocholate transport;, features a modification of the amino acid from S to F at position 241.
+The protein's natural variant, known as severely decreased function in taurocholate transport;, features a modification of the amino acid from R to W at position 249.
+The protein's natural variant, known as severely decreased function in taurocholate transport;, features a modification of the amino acid from R to C at position 252.
+The protein's natural variant, known as in FHCA2; loss of function in taurocholate transport; loss of localization to the cell membrane due to intracellular retention;, features a modification of the amino acid from R to H at position 252.
+The protein's natural variant, known as severely decreased function in taurocholate transport;, features a modification of the amino acid from R to S at position 252.
+The protein's natural variant, known as decreased function in taurocholate transport;, features a modification of the amino acid from T to S at position 258.
+The protein's natural variant, known as in FHCA2; associated with resistance to hepatitis B virus infection and chronic hepatitis; unable to transport taurocholate and cholate; does not affect uptake of estrone sulfate; does not affect localization to the cell membrane;, features a modification of the amino acid from S to F at position 267.
+The protein's natural variant, known as decreased transport of taurocholate and cholate; decreased transport of estron sulfate; does not affect localization to the cell membrane;, features a modification of the amino acid from I to T at position 279.
+The protein's natural variant, known as decreased function in taurocholate transport;, features a modification of the amino acid from Q to E at position 293.
+The protein's natural variant, known as decreased transport of taurocholate and cholate; decreased transport of estron sulfate; does not affect localization to the cell membrane;, features a modification of the amino acid from K to E at position 314.
+The protein's natural variant, known as in strain: CLIB 219, features a modification of the amino acid from S to P at position 24.
+The protein's natural variant, known as in strain: CLIB 630 haplotype Ha2, features a modification of the amino acid from P to S at position 62.
+The protein's natural variant, known as in strain: CLIB 556 haplotype Ha1, features a modification of the amino acid from T to A at position 82.
+The protein's natural variant, known as in strain: CLIB 95, CLIB 219, CLIB 382, CLIB 388, CLIB 410, CLIB 413, CLIB 556, CLIB 630, K1, R12, R13 haplotype Ha2, Sigma 1278B haplotype Ha1, YIIc12 and YIIc17, features a modification of the amino acid from D to A at position 91.
+The protein's natural variant, known as in strain: CLIB 556 haplotype Ha1, features a modification of the amino acid from D to A at position 125.
+The protein's natural variant, known as in strain: CLIB 388, CLIB 410, CLIB 413, CLIB 630 haplotype Ha1, K1, YIIc12 haplotype Ha2 and YIIc17 haplotype Ha1, features a modification of the amino acid from D to E at position 196.
+The protein's natural variant, known as in HIES5; decreased STAT1 and STAT3 phosphorylation;, features a modification of the amino acid from I to N at position 279.
+The protein's natural variant, known as in HIES5; unknown pathological significance; no effect on STAT1 and STAT3 phosphorylation, features a modification of the amino acid from H to P at position 280.
+The protein's natural variant, known as significantly associated with circulating levels of IL6 and soluble IL6R; increases cleavage by ADAM17;, features a modification of the amino acid from D to A at position 358.
+The protein's natural variant, known as in PPH4; loss of function; channel activity can be rescued with the use of the phospholipase A2 inhibitor ONO-RS-082;, features a modification of the amino acid from T to K at position 8.
+The protein's natural variant, known as in PPH4; loss of function;, features a modification of the amino acid from G to R at position 97.
+The protein's natural variant, known as in PPH4; loss of function; channel activity can be rescued with the use of the phospholipase A2 inhibitor ONO-RS-082;, features a modification of the amino acid from E to K at position 182.
+The protein's natural variant, known as in PPH4; loss of function;, features a modification of the amino acid from Y to C at position 192.
+The protein's natural variant, known as in PPH4; loss of function; channel activity cannot be rescued with the use of the phospholipase A2 inhibitor ONO-RS-082;, features a modification of the amino acid from G to D at position 203.
+The protein's natural variant, known as in PPH4; loss of function;, features a modification of the amino acid from V to L at position 221.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from S to N at position 291.
+The protein's natural variant, known as found in a patient with clinical features of Galloway-Mowat syndrome; unknown pathological significance;, features a modification of the amino acid from G to R at position 1046.
+The protein's natural variant, known as in strain: UK and VS116, features a modification of the amino acid from S to P at position 4.
+The protein's natural variant, known as in strain: UK and VS116, features a modification of the amino acid from V to I at position 9.
+The protein's natural variant, known as in strain: POTIB1, POTIB2 and POTIB3, features a modification of the amino acid from IVD to VVN at position 16.
+The protein's natural variant, known as in strain: A44S and NY13-87, features a modification of the amino acid from S to A at position 19.
+The protein's natural variant, known as in strain: 25015, CA2, CA55, CA128, DN127, POTIB1, POTIB2, POTIB3, UK and VS116, features a modification of the amino acid from K to R at position 23.
+The protein's natural variant, known as in strain: CA55, CA128 and DN127, features a modification of the amino acid from Y to C at position 33.
+The protein's natural variant, known as in strain: 25015, features a modification of the amino acid from V to L at position 65.
+The protein's natural variant, known as in strain: DN127, features a modification of the amino acid from K to R at position 69.
+The protein's natural variant, known as in strain: NY13-87, features a modification of the amino acid from E to V at position 81.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from A to V at position 64.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from V to I at position 81.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from A to V at position 220.
+The protein's natural variant, known as in AIEFL; prevents cleavage by CASP8; increased kinase activity; increased inflammatory response, features a modification of the amino acid from D to H at position 324.
+The protein's natural variant, known as in AIEFL; prevents cleavage by CASP8; changed inflammatory response;, features a modification of the amino acid from D to N at position 324.
+The protein's natural variant, known as in AIEFL; prevents cleavage by CASP8; increased kinase activity; increased inflammatory response, features a modification of the amino acid from D to V at position 324.
+The protein's natural variant, known as in AIEFL; prevents cleavage by CASP8; changed inflammatory response, features a modification of the amino acid from D to Y at position 324.
+The natural variant of this protein is characterized by an amino acid alteration from C to S at position 8.
+The natural variant of this protein is characterized by an amino acid alteration from A to G at position 55.
+The natural variant of this protein is characterized by an amino acid alteration from A to G at position 91.
+The natural variant of this protein is characterized by an amino acid alteration from T to P at position 412.
+The natural variant of this protein is characterized by an amino acid alteration from G to A at position 459.
+The protein's natural variant, known as found in a patient with isolated coloboma; unknown pathological significance;, features a modification of the amino acid from P to S at position 134.
+The protein's natural variant, known as in MSSGM2; no effect on localization; increased protein abundance; loss of interaction with protein phosphatase catalytic subunit PP1; decreased dephosphorylation of EIF2S1;, features a modification of the amino acid from R to C at position 658.
+The protein's natural variant, known as in RP68;, features a modification of the amino acid from A to V at position 132.
+The protein's natural variant, known as in RP68; uncertain pathological significance;, features a modification of the amino acid from N to S at position 209.
+The protein's natural variant, known as in RP68; uncertain pathological significance, features a modification of the amino acid from M to I at position 323.
+The protein's natural variant, known as in RP68; affects subcellular location;, features a modification of the amino acid from G to R at position 330.
+The protein's natural variant, known as in RP68; uncertain pathological significance;, features a modification of the amino acid from S to L at position 391.
+The protein's natural variant, known as in RP68;, features a modification of the amino acid from C to F at position 464.
+The protein's natural variant, known as in RP68; uncertain pathological significance;, features a modification of the amino acid from R to C at position 695.
+The protein's natural variant, known as in RP68;, features a modification of the amino acid from F to V at position 708.
+The protein's natural variant, known as in mutant 12-2B; increase in substrate affinity, features a modification of the amino acid from R to C at position 95.
+The protein's natural variant, known as in strain: AL202, AT4 and PV259, features a modification of the amino acid from H to Y at position 46.
+The protein's natural variant, known as in strain: AL202, AT4, FD70 and PV259, features a modification of the amino acid from V to I at position 103.
+The protein's natural variant, known as in strain: TV46 and TV51, features a modification of the amino acid from V to I at position 118.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation, features a modification of the amino acid from G to E at position 627.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation, features a modification of the amino acid from A to V at position 662.
+The protein's natural variant, known as in SCN8, features a modification of the amino acid from G to R at position 113.
+The protein's natural variant, known as in SCN8; decreases expression levels; decreases GTPase activity; decreases neutrophil numbers and migration capacity, features a modification of the amino acid from T to A at position 115.
+The protein's natural variant, known as in SCN8; decreased granulocyte proliferation; increased apoptosis, features a modification of the amino acid from C to Y at position 118.
+The protein's natural variant, known as in SCN8; decreased granulocyte proliferation; delayed granulocytic differentiation; impaired signaling; induced autophagy, features a modification of the amino acid from C to Y at position 136.
+The protein's natural variant, known as in SCN8; decreased granulocyte proliferation; induced autophagy, features a modification of the amino acid from A to D at position 223.
+The protein's natural variant, known as in SCN8; decreases expression levels; decreases neutrophil numbers and migration capacity; faster dissociation of the interaction with the SRP receptor subunit SRPRA; reduced SR compaction; impaired interaction with SR; impaired detachment from ribosome; effects on enzymatic activity are unclear as both normal and reduced GTPase activity have been reported, features a modification of the amino acid from G to E at position 226.
+The protein's natural variant, known as in SCN8, features a modification of the amino acid from G to D at position 274.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from G to S at position 78.
+The protein's natural variant, known as in basal cell carcinomas;, features a modification of the amino acid from R to L at position 398.
+The protein's natural variant, known as in basal cell carcinomas;, features a modification of the amino acid from K to E at position 400.
+The protein's natural variant, known as in basal cell carcinomas;, features a modification of the amino acid from I to V at position 401.
+The protein's natural variant, known as in CMAVM1; unknown pathological significance;, features a modification of the amino acid from Y to C at position 528.
+The protein's natural variant, known as in CMAVM1, features a modification of the amino acid from V to D at position 530.
+The protein's natural variant, known as in CMAVM1;, features a modification of the amino acid from C to Y at position 540.
+The protein's natural variant, known as in CMAVM1;, features a modification of the amino acid from A to E at position 626.
+The protein's natural variant, known as in CMAVM1; unknown pathological significance;, features a modification of the amino acid from E to V at position 763.
+The protein's natural variant, known as in an ovarian mucinous carcinoma sample; somatic mutation;, features a modification of the amino acid from T to M at position 443.
+The protein's natural variant, known as found in patients with steroid-resistant nephrotic syndrome; unknown pathological significance;, features a modification of the amino acid from K to M at position 301.
+The protein's natural variant, known as in strain: SK1048; decreases translational rate, tRNA binding and subunit association at 44 degrees Celsius; does not alter 23S rRNA or L4 interactions; not erythromycin resistant, features a modification of the amino acid from R to C at position 8.
+The protein's natural variant, known as in IDDALDS; unknown pathological significance;, features a modification of the amino acid from R to H at position 755.
+The protein's natural variant, known as in IDDALDS; reduced interaction with KIF1A; impaired neuronal dense core vesicles transport; no effect on dendritic spine location;, features a modification of the amino acid from R to C at position 760.
+The protein's natural variant, known as in IDDALDS; unknown pathological significance;, features a modification of the amino acid from A to V at position 794.
+The protein's natural variant, known as in IDDALDS; unknown pathological significance;, features a modification of the amino acid from R to Q at position 961.
+The protein's natural variant, known as found in a patient with isolated coloboma; unknown pathological significance, features a modification of the amino acid from G to V at position 1280.
+The protein's natural variant, known as in IDDALDS; unknown pathological significance;, features a modification of the amino acid from H to R at position 1689.
+The protein's natural variant, known as in ATRST2;, features a modification of the amino acid from R to Q at position 150.
+The natural variant of this protein is characterized by an amino acid alteration from Y to YRR at position 151.
+The protein's natural variant, known as in MRXSRC; also in patients with complex congenital diaphragmatic hernia; unknown pathological significance; no reduction in outwardly-rectifying currents; does not affect its localization in endoplasmic reticulum membrane;, features a modification of the amino acid from D to N at position 15.
+The protein's natural variant, known as in MRXSRC; marked reduction in outwardly-rectifying currents;, features a modification of the amino acid from G to S at position 78.
+The protein's natural variant, known as in MRXSRC; marked reduction in outwardly-rectifying currents; does not affect its localization in endoplasmic reticulum membrane;, features a modification of the amino acid from V to G at position 212.
+The protein's natural variant, known as in MRXSRC; marked reduction in outwardly-rectifying currents; does not affect its localization in endoplasmic reticulum membrane;, features a modification of the amino acid from L to P at position 221.
+The protein's natural variant, known as in MRXSRC; marked reduction in outwardly-rectifying currents;, features a modification of the amino acid from L to V at position 221.
+The protein's natural variant, known as in MRXSRC; marked reduction in outwardly-rectifying currents; does not affect its localization in endoplasmic reticulum;, features a modification of the amino acid from V to M at position 275.
+The protein's natural variant, known as in MRXSRC; marked reduction in outwardly-rectifying currents; does not affect its localization in endoplasmic reticulum membrane;, features a modification of the amino acid from S to L at position 534.
+The protein's natural variant, known as in MRXSRC; marked reduction in outwardly-rectifying currents;, features a modification of the amino acid from V to M at position 536.
+The protein's natural variant, known as in MRXSRC; has normal localization to structures resembling endoplasmic reticulum membranes; almost abolishes the outwardly-rectifying currents;, features a modification of the amino acid from G to R at position 544.
+The protein's natural variant, known as in MRXSRC; marked reduction in outwardly-rectifying currents; does not affect its localization in endoplasmic reticulum membrane;, features a modification of the amino acid from A to V at position 555.
+The protein's natural variant, known as in MRXSRC; marked reduction in outwardly-rectifying currents; does not affect its localization in endoplasmic reticulum membrane;, features a modification of the amino acid from R to W at position 718.
+The protein's natural variant, known as in MRXSRC; marked reduction in outwardly-rectifying currents;, features a modification of the amino acid from G to R at position 731.
+The protein's natural variant, known as in MMERV;, features a modification of the amino acid from Q to R at position 403.
+The protein's natural variant, known as in CUGS;, features a modification of the amino acid from G to R at position 435.
+The protein's natural variant, known as in CUGS; unknown pathological significance, features a modification of the amino acid from V to A at position 679.
+The protein's natural variant, known as in CUGS; unknown pathological significance;, features a modification of the amino acid from R to H at position 695.
+The protein's natural variant, known as in plasmid pWR100 and plasmid pWR501, features a modification of the amino acid from R to H at position 600.
+The protein's natural variant, known as in plasmid pWR100 and plasmid pWR501, features a modification of the amino acid from F to S at position 740.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from A to E at position 1164.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from R to Q at position 1945.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 512.
+The protein's natural variant, known as in non-inducible mutant SN0301-1, features a modification of the amino acid from G to D at position 151.
+The protein's natural variant, known as in non-inducible mutant SN0301-3, features a modification of the amino acid from G to D at position 268.
+The protein's natural variant, known as in non-inducible mutant SN0301-5, features a modification of the amino acid from G to D at position 373.
+The protein's natural variant, known as in 50% of the molecules, features a modification of the amino acid from L to V at position 6.
+The protein's natural variant, known as in 50% of the molecules, features a modification of the amino acid from P to A at position 12.
+The natural variant of this protein is characterized by an amino acid alteration from E to D at position 33.
+The protein's natural variant, known as in 33% of the molecules, features a modification of the amino acid from G to A at position 96.
+The protein's natural variant, known as may exacerbate the severity of non-syndromic sensorineural hearing loss in patients with clinically relevant CDH23 variants; delayed calcium export, features a modification of the amino acid from G to S at position 293.
+The protein's natural variant, known as may exacerbate the severity of non-syndromic sensorineural hearing loss in patients with clinically relevant CDH23 variants; resulted in 50% decrease of the calcium ATPase activity, features a modification of the amino acid from V to M at position 631.
+The protein's natural variant, known as found in a patient with a neurodevelopmental disorder; unknown pathological significance, features a modification of the amino acid from R to W at position 168.
+The protein's natural variant, known as in FTHS;, features a modification of the amino acid from R to W at position 43.
+The protein's natural variant, known as requires 2 nucleotide substitutions, after 37 telithromycin passages; confers resistance to various antibiotics in combination with R114T, a 23S rRNA mutation and protein L4 H70L, features a modification of the amino acid from N to R at position 112.
+The protein's natural variant, known as after 20 and 32 telithromycin passages; confers resistance to various antibiotics in combination with a 23S rRNA mutation with and without protein L4 H70L, features a modification of the amino acid from R to T at position 114.
+The natural variant of this protein is characterized by an amino acid alteration from V to A at position 440.
+The natural variant of this protein is characterized by an amino acid alteration from A to P at position 593.
+The natural variant of this protein is characterized by an amino acid alteration from I to M at position 1204.
+The natural variant of this protein is characterized by an amino acid alteration from C to S at position 1371.
+The natural variant of this protein is characterized by an amino acid alteration from T to A at position 1390.
+The natural variant of this protein is characterized by an amino acid alteration from A to V at position 1443.
+The protein's natural variant, known as in IMGT allele IGKV1D-16*02, features a modification of the amino acid from S to R at position 48.
+The protein's natural variant, known as in IMD42; does not affect nuclear localization; loss of transcription regulatory region sequence-specific DNA binding; loss of transcriptional activity;, features a modification of the amino acid from S to L at position 38.
+The protein's natural variant, known as in BBSOAS; decreases transcriptional activity;, features a modification of the amino acid from R to K at position 112.
+The protein's natural variant, known as in BBSOAS; decreases transcriptional activity;, features a modification of the amino acid from S to R at position 113.
+The protein's natural variant, known as in BBSOAS; decreases transcriptional activity;, features a modification of the amino acid from R to P at position 115.
+The protein's natural variant, known as in BBSOAS; decreases transcriptional activity;, features a modification of the amino acid from L to P at position 252.
+The protein's natural variant, known as in BH;, features a modification of the amino acid from W to R at position 225.
+The protein's natural variant, known as in BH; decreased microtubule-binding;, features a modification of the amino acid from T to A at position 243.
+The natural variant of this protein is characterized by an amino acid alteration from E to D at position 54.
+The natural variant of this protein is characterized by an amino acid alteration from A to G at position 108.
+The protein's natural variant, known as in a gastric adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from F to L at position 173.
+The protein's natural variant, known as in MRD57; unknown pathological significance;, features a modification of the amino acid from G to D at position 297.
+The protein's natural variant, known as in MRD57; unknown pathological significance;, features a modification of the amino acid from R to Q at position 339.
+The protein's natural variant, known as in MRD57; unknown pathological significance;, features a modification of the amino acid from R to W at position 339.
+The protein's natural variant, known as in MRD57; unknown pathological significance;, features a modification of the amino acid from E to K at position 447.
+The protein's natural variant, known as in MRD57; reduced kinase activity;, features a modification of the amino acid from H to R at position 493.
+The protein's natural variant, known as in MRD57; severely reduced kinase activity;, features a modification of the amino acid from H to R at position 518.
+The protein's natural variant, known as in MRD57; unknown pathological significance; exhibits abnormal perinuclear localization instead of diffuse nuclear localization; mildly impairs kinase activity; reduced phosphorylation of ASF1A;, features a modification of the amino acid from D to G at position 551.
+The protein's natural variant, known as in MRD57;, features a modification of the amino acid from R to W at position 568.
+The protein's natural variant, known as in MRD57; exhibits abnormal perinuclear localization instead of diffuse nuclear localization; impairs kinase activity; reduced phosphorylation of ASF1A;, features a modification of the amino acid from S to L at position 617.
+The protein's natural variant, known as in MRD57; reduced phosphorylation of ASF1A;, features a modification of the amino acid from D to N at position 629.
+The protein's natural variant, known as in MRD57;, features a modification of the amino acid from P to R at position 680.
+The protein's natural variant, known as in DFNB68;, features a modification of the amino acid from R to P at position 108.
+The protein's natural variant, known as in DFNB68;, features a modification of the amino acid from Y to C at position 140.
+The protein's natural variant, known as in strain: KBN616, features a modification of the amino acid from K to N at position 260.
+The protein's natural variant, known as in THC6; increased protein tyrosine kinase activity; increased autophosphorylation at Y-419; causes defective megakaryopoiesis associated with increased overall tyrosine phosphorylation in megakaryocytes;, features a modification of the amino acid from E to K at position 527.
+The protein's natural variant, known as in NSLH2;, features a modification of the amino acid from P to R at position 49.
+The protein's natural variant, known as in NSLH2;, features a modification of the amino acid from A to P at position 56.
+The protein's natural variant, known as in NSLH2;, features a modification of the amino acid from E to A at position 183.
+The protein's natural variant, known as in NSLH2;, features a modification of the amino acid from E to V at position 183.
+The protein's natural variant, known as in NSLH2;, features a modification of the amino acid from D to Y at position 252.
+The protein's natural variant, known as in NSLH2; unknown pathological significance;, features a modification of the amino acid from E to K at position 274.
+The protein's natural variant, known as in HKLLS3; affects proteolytic maturation and impairs secretion;, features a modification of the amino acid from L to P at position 168.
+The protein's natural variant, known as in HKLLS3; affects proteolytic maturation and impairs secretion;, features a modification of the amino acid from I to T at position 291.
+The natural variant of this protein is characterized by an amino acid alteration from V to L at position 114.
+The protein's natural variant, known as in ACEC816; constitutively activated, features a modification of the amino acid from R to C at position 118.
+The protein's natural variant, known as in strain: cv. Samsun, features a modification of the amino acid from Y to F at position 54.
+The protein's natural variant, known as in strain: TE3285 and ATCC 31156, features a modification of the amino acid from A to T at position 210.
+The protein's natural variant, known as in strain: TE3285 and ATCC 31156, features a modification of the amino acid from T to A at position 301.
+The protein's natural variant, known as in strain: AB1, AB2, CB4852, CB4853, CB4855, CB4857, CB4858, KR314 and PB306, features a modification of the amino acid from V to I at position 39.
+The protein's natural variant, known as in strain: CB4854, features a modification of the amino acid from A to S at position 81.
+The protein's natural variant, known as in strain: AB1, AB2, CB4852, CB4853, CB4855, CB4857, CB4858, KR314 and PB306, features a modification of the amino acid from L to F at position 90.
+The protein's natural variant, known as in MC1DN36; highly decreased mitochondrial membrane respiratory chain NADH dehydrogenase complex I activity; decreased complex I assembly and protein levels;, features a modification of the amino acid from H to Y at position 58.
+The natural variant of this protein is characterized by an amino acid alteration from F to L at position 63.
+The protein's natural variant, known as in UP-FTD; no significant difference in the total mRNA between cases and controls; although the mutant protein is expressed it is not secreted and appears to be trapped within an intracellular compartment;, features a modification of the amino acid from A to D at position 9.
+The protein's natural variant, known as in HH3; phenotype consistent with normosmic idiopathic hypogonadotropic hypogonadism; decreased signaling activity;, features a modification of the amino acid from R to C at position 85.
+The protein's natural variant, known as in HH3; decreased signaling activity;, features a modification of the amino acid from R to H at position 85.
+The protein's natural variant, known as in HH3;, features a modification of the amino acid from Y to H at position 113.
+The protein's natural variant, known as in HH3; phenotype consistent with Kallmann syndrome;, features a modification of the amino acid from V to M at position 115.
+The protein's natural variant, known as in HH3; phenotype consistent with Kallmann syndrome;, features a modification of the amino acid from V to I at position 158.
+The protein's natural variant, known as in HH3; phenotype consistent with Kallmann syndrome; decreased signaling activity;, features a modification of the amino acid from R to Q at position 164.
+The protein's natural variant, known as in HH3; phenotype consistent with Kallmann syndrome; decreased signaling activity;, features a modification of the amino acid from L to R at position 173.
+The protein's natural variant, known as in HH3; decreased signaling activity;, features a modification of the amino acid from W to S at position 178.
+The protein's natural variant, known as in HH3;, features a modification of the amino acid from S to L at position 188.
+The protein's natural variant, known as in HH3; triallelic inheritance; the patient also carries mutations in GNRH1 and FGFR1;, features a modification of the amino acid from S to G at position 202.
+The protein's natural variant, known as in HH3; phenotype consistent with Kallmann syndrome; decreased signaling activity; abolished ligand binding;, features a modification of the amino acid from Q to R at position 210.
+The protein's natural variant, known as in HH3;, features a modification of the amino acid from R to Q at position 248.
+The protein's natural variant, known as in HH3; benign variant; signaling activity is impaired;, features a modification of the amino acid from R to C at position 268.
+The protein's natural variant, known as in HH3; phenotype consistent with Kallmann syndrome; signaling activity is impaired; impaired cell surface-targeting;, features a modification of the amino acid from P to S at position 290.
+The protein's natural variant, known as in HH3; phenotype consistent with Kallmann syndrome; signaling activity is impaired;, features a modification of the amino acid from M to I at position 323.
+The protein's natural variant, known as in HH3; likely benign variant;, features a modification of the amino acid from V to M at position 331.
+The protein's natural variant, known as in HH3; phenotype consistent with Kallmann syndrome;, features a modification of the amino acid from V to M at position 334.
+The protein's natural variant, known as in HH3;, features a modification of the amino acid from R to W at position 357.
+The protein's natural variant, known as in strain: ATCC 13813, features a modification of the amino acid from V to I at position 60.
+The protein's natural variant, known as in strain: ATCC 13813, features a modification of the amino acid from E to D at position 98.
+The protein's natural variant, known as in strain: ATCC 13813, features a modification of the amino acid from N to D at position 104.
+The protein's natural variant, known as found in an activated B cell-like diffuse large B-cell lymphoma (ABC-DLBCL) cell line; protein instability caused by increased susceptibility to proteasomal degradation, features a modification of the amino acid from P to R at position 84.
+The protein's natural variant, known as found in an activated B cell-like diffuse large B-cell lymphoma (ABC-DLBCL) cell line; protein instability caused by increased susceptibility to proteasomal degradation, features a modification of the amino acid from I to R at position 107.
+The protein's natural variant, known as in NEDMOSBA, features a modification of the amino acid from G to S at position 72.
+The protein's natural variant, known as in NEDMOSBA; unknown pathological significance, features a modification of the amino acid from V to M at position 148.
+The protein's natural variant, known as in NEDMOSBA; unknown pathological significance, features a modification of the amino acid from G to R at position 176.
+The protein's natural variant, known as in strain: CC-503, features a modification of the amino acid from L to R at position 30.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from A to V at position 115.
+The protein's natural variant, known as in strain: TN106, features a modification of the amino acid from A to V at position 17.
+The protein's natural variant, known as in strain: TN106, features a modification of the amino acid from E to K at position 31.
+The protein's natural variant, known as in strain: TN106, features a modification of the amino acid from D to N at position 66.
+The protein's natural variant, known as in strain: TN106, features a modification of the amino acid from G to E at position 116.
+The protein's natural variant, known as in strain: TN106, features a modification of the amino acid from G to E at position 120.
+The protein's natural variant, known as in strain: TN106, features a modification of the amino acid from K to Q at position 134.
+The protein's natural variant, known as in strain: TN106, features a modification of the amino acid from E to D at position 140.
+The protein's natural variant, known as in strain: TN106, features a modification of the amino acid from E to K at position 146.
+The protein's natural variant, known as in strain: TN106, features a modification of the amino acid from K to R at position 226.
+The protein's natural variant, known as in a lung large cell carcinoma sample; somatic mutation, features a modification of the amino acid from Q to E at position 433.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation, features a modification of the amino acid from G to E at position 1364.
+The protein's natural variant, known as in SEMDHL; severe decrease of protein expression;, features a modification of the amino acid from Q to H at position 235.
+The protein's natural variant, known as in SEMDHL;, features a modification of the amino acid from D to G at position 237.
+The protein's natural variant, known as in SEMDHL;, features a modification of the amino acid from D to V at position 237.
+The protein's natural variant, known as in COXPD6; reduced protein amount in muscle compared to controls; no effect on reduction with NADH; strongly decreased NADH oxidase activity; no effect on dimerization; no effect on DNA-binding;, features a modification of the amino acid from V to L at position 243.
+The protein's natural variant, known as in DFNX5;, features a modification of the amino acid from T to A at position 260.
+The protein's natural variant, known as probable disease-associated variant found in patient with mitochondrial encephalomyopathy with moderate clinical severity and slow progressive course despite early onset as well as and cerebellar involvement; decreased protein level; strongly decreased redox potential; strongly decreased NADH oxidase activity; no effect on DNA-binding;, features a modification of the amino acid from G to S at position 262.
+The protein's natural variant, known as in COXPD6; with prenatal ventriculomegaly and severe postnatal encephalomyopathy; no effect on redox potential; slowered reduction with NADH; strongly decreased NADH oxidase activity; strongly decreased NADH oxidase activity; no effect on DNA-binding; decreased interaction with CHCHDE;, features a modification of the amino acid from G to E at position 308.
+The protein's natural variant, known as in COXPD6; with early-onset severe motor neuron involvement; decreased protein levels; decreased oxidoreductase activity on cytochrome C; slowered reduction with NADH; strongly decreased NADH oxidase activity; strongly decreased NADH oxidase activity; no effect on DNA-binding;, features a modification of the amino acid from G to E at position 338.
+The protein's natural variant, known as in DFNX5; unknown pathological significance;, features a modification of the amino acid from L to F at position 344.
+The protein's natural variant, known as in DFNX5; unknown pathological significance;, features a modification of the amino acid from G to R at position 360.
+The protein's natural variant, known as in DFNX5;, features a modification of the amino acid from R to Q at position 422.
+The protein's natural variant, known as in DFNX5;, features a modification of the amino acid from R to W at position 422.
+The protein's natural variant, known as in DFNX5; unknown pathological significance;, features a modification of the amino acid from R to C at position 430.
+The protein's natural variant, known as in DFNX5;, features a modification of the amino acid from R to Q at position 451.
+The protein's natural variant, known as in DFNX5; unknown pathological significance, features a modification of the amino acid from A to V at position 472.
+The protein's natural variant, known as in DFNX5; unknown pathological significance;, features a modification of the amino acid from P to L at position 475.
+The protein's natural variant, known as in CMTX4; increases affinity for NADH and electron transfer activity; increases affinity for DNA, resulting in increased apoptosis; no effect on interaction with CHCHD4;, features a modification of the amino acid from E to V at position 493.
+The protein's natural variant, known as in DFNX5; unknown pathological significance;, features a modification of the amino acid from V to M at position 498.
+The protein's natural variant, known as in DFNX5; unknown pathological significance, features a modification of the amino acid from I to M at position 591.
+The protein's natural variant, known as may be associated with risk of familial obesity;, features a modification of the amino acid from R to W at position 125.
+The natural variant of this protein is characterized by an amino acid alteration from T to M at position 13.
+The protein's natural variant, known as in SPG85, features a modification of the amino acid from C to R at position 102.
+The protein's natural variant, known as in SPG85, features a modification of the amino acid from C to W at position 107.
+The protein's natural variant, known as in SNAX1;, features a modification of the amino acid from R to C at position 199.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from G to R at position 784.
+The protein's natural variant, known as in SPGF17; loss of function in egg activation;, features a modification of the amino acid from I to F at position 489.
+The protein's natural variant, known as in COXPD10;, features a modification of the amino acid from A to T at position 453.
+The protein's natural variant, known as in ApoE5; associated with hyperlipoproteinemia and atherosclerosis; increased binding to LDL receptor;, features a modification of the amino acid from E to K at position 21.
+The protein's natural variant, known as in HLPP3; ApoE4 Philadelphia, ApoE5 French-Canadian and ApoE5-type; only ApoE4 Philadelphia is associated with HLPP3;, features a modification of the amino acid from E to K at position 31.
+The protein's natural variant, known as in LPG; ApoE2 Kyoto;, features a modification of the amino acid from R to C at position 43.
+The protein's natural variant, known as found in a patient with hypercholesterolemia; unknown pathological significance; ApoE4 Freiburg;, features a modification of the amino acid from L to P at position 46.
+The protein's natural variant, known as in ApoE3 Freiburg;, features a modification of the amino acid from T to A at position 60.
+The protein's natural variant, known as confirmed at protein level;, features a modification of the amino acid from Q to H at position 64.
+The protein's natural variant, known as in ApoE5 Frankfurt;, features a modification of the amino acid from Q to K at position 99.
+The protein's natural variant, known as in ApoE5-type; no hyperlipidemia;, features a modification of the amino acid from P to R at position 102.
+The protein's natural variant, known as in ApoE3*;, features a modification of the amino acid from A to T at position 117.
+The protein's natural variant, known as in ApoE3 Basel;, features a modification of the amino acid from A to V at position 124.
+The protein's natural variant, known as in HLPP3 and AD2; ApoE4, ApoE3 Leiden, ApoE3**, ApoE5-Frankfurt and ApoE5-type; ApoE3 Leiden and ApoE3** are associated with HLPP3; ApoE4 is associated with AD2; changed protein structure; no effect on binding to LDL receptor; decreased association with HDL and enrichment in VLDL and IDL; may prevent the interaction with MAP2 and MAPT; changed interaction with APP/A4 amyloid-beta peptide; increased ability to induce APP transcription; increased C-terminal proteolytic processing in neurons; decreased function in neurite outgrowth; ApoE4 is associated with higher susceptibility to SARS-CoV-2 infection in neurons and astrocytes;, features a modification of the amino acid from C to R at position 130.
+The protein's natural variant, known as found in a patient with hypercholesterolemia; unknown pathological significance; ApoE1 Weisgraber;, features a modification of the amino acid from G to D at position 145.
+The protein's natural variant, known as in HLPP3; ApoE3 Leiden; no effect on glycosylation, features a modification of the amino acid from G to GEVQAMLG at position 145.
+The protein's natural variant, known as in ApoE2-type; no hyperlipidemia;, features a modification of the amino acid from R to Q at position 152.
+The protein's natural variant, known as in HLPP3; ApoE2-type;, features a modification of the amino acid from R to C at position 154.
+The protein's natural variant, known as in HLPP3; ApoE2 Christchurch; decreased binding to LDL receptor;, features a modification of the amino acid from R to S at position 154.
+The protein's natural variant, known as in HLPP3; ApoE3**;, features a modification of the amino acid from R to C at position 160.
+The protein's natural variant, known as in HLPP3; also found in a patient with hypercholesterolemia; ApoE4 Philadelphia and ApoE2-type;, features a modification of the amino acid from R to C at position 163.
+The protein's natural variant, known as in HLPP3; unknown pathological significance; ApoEKochi;, features a modification of the amino acid from R to H at position 163.
+The protein's natural variant, known as in LPG; ApoE2 Sendai; decreased binding to LDL receptor; induces intraglomerular deposition of ApoE-containing lipoproteins;, features a modification of the amino acid from R to P at position 163.
+The protein's natural variant, known as in HLPP3; ApoE1 Harrisburg; decreased binding to LDL receptor; probable dominant negative effect; decreased in vitro binding to heparin;, features a modification of the amino acid from K to E at position 164.
+The protein's natural variant, known as in HLPP3; ApoE2**;, features a modification of the amino acid from K to Q at position 164.
+The protein's natural variant, known as in ApoE3*; decreased binding to LDL receptor;, features a modification of the amino acid from A to P at position 170.
+The protein's natural variant, known as in HLPP3; ApoE2, ApoE2 Fukuoka, ApoE1 Weisgraber and ApoE3**; ApoE3** is associated with HLPP3; changed protein structure; decreased binding to LDLR and other lipoprotein receptors; decreased in vitro binding to heparin; no effect on distribution among plasma lipoproteins;, features a modification of the amino acid from R to C at position 176.
+The protein's natural variant, known as in ApoE2 Fukuoka;, features a modification of the amino acid from R to Q at position 242.
+The protein's natural variant, known as in ApoE2 Dunedin;, features a modification of the amino acid from R to C at position 246.
+The protein's natural variant, known as in ApoE2 WG;, features a modification of the amino acid from V to E at position 254.
+The protein's natural variant, known as in HLPP3; ApoE7 Suita, features a modification of the amino acid from EE to KK at position 263.
+The protein's natural variant, known as in ApoE3 HB;, features a modification of the amino acid from R to G at position 269.
+The protein's natural variant, known as in ApoE1 HE; requires 2 nucleotide substitutions, features a modification of the amino acid from L to E at position 270.
+The protein's natural variant, known as in ApoE4 PD;, features a modification of the amino acid from R to H at position 292.
+The protein's natural variant, known as in ApoE4 HG;, features a modification of the amino acid from S to R at position 314.
+The protein's natural variant, known as in RDYS;, features a modification of the amino acid from R to W at position 103.
+The protein's natural variant, known as in RDYS;, features a modification of the amino acid from D to G at position 165.
+The protein's natural variant, known as in allele GPT*2;, features a modification of the amino acid from H to N at position 14.
+The protein's natural variant, known as found in patient with Joubert syndrome; unknown pathological significance;, features a modification of the amino acid from E to Q at position 430.
+The protein's natural variant, known as found in patient with Joubert syndrome; unknown pathological significance;, features a modification of the amino acid from V to L at position 452.
+The protein's natural variant, known as in allele B, features a modification of the amino acid from SQ to IE at position 243.
+The protein's natural variant, known as in EPM12; due to a nucleotide substitution that can result in aberrant splicing; patient cells contain both normally spliced transcripts and transcripts that retained intron 1; marked reduction of protein expression in patient cells;, features a modification of the amino acid from Q to R at position 64.
+The protein's natural variant, known as in strain: Isolate SIK0557, features a modification of the amino acid from A to T at position 122.
+The natural variant of this protein is characterized by an amino acid alteration from A to D at position 96.
+The protein's natural variant, known as in DEE19;, features a modification of the amino acid from R to Q at position 112.
+The protein's natural variant, known as in DEE19, features a modification of the amino acid from L to M at position 146.
+The protein's natural variant, known as in EIG13; the mutant protein is partially retained in the endoplasmic reticulum and has decreased expression at the plasma membrane; causes decreased current amplitude in response to GABA compared to wild-type and alters receptor gating kinetics including faster desensitization;, features a modification of the amino acid from D to N at position 219.
+The protein's natural variant, known as in DEE19;, features a modification of the amino acid from G to S at position 251.
+The protein's natural variant, known as in DEE19;, features a modification of the amino acid from K to T at position 306.
+The protein's natural variant, known as in EJM5;, features a modification of the amino acid from A to D at position 322.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from Q to K at position 1204.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from A to S at position 891.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from T to A at position 1228.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from V to M at position 478.
+The protein's natural variant, known as in CMD1; dimerization and the resulting capacity to activate promoters via dimeric binding sites is lost; other features of the protein function remain unaltered;, features a modification of the amino acid from A to E at position 76.
+The protein's natural variant, known as in CMD1, features a modification of the amino acid from P to L at position 108.
+The protein's natural variant, known as in CMD1; loss of DNA binding;, features a modification of the amino acid from F to L at position 112.
+The protein's natural variant, known as in CMD1, features a modification of the amino acid from F to S at position 112.
+The protein's natural variant, known as in CMD1, features a modification of the amino acid from M to T at position 113.
+The protein's natural variant, known as in CMD1; residual DNA binding and transactivation of regulated genes, features a modification of the amino acid from M to V at position 113.
+The protein's natural variant, known as in CMD1; almost no loss of DNA binding, features a modification of the amino acid from A to V at position 119.
+The protein's natural variant, known as in CMD1, features a modification of the amino acid from W to R at position 143.
+The protein's natural variant, known as in CMD1, features a modification of the amino acid from R to P at position 152.
+The protein's natural variant, known as in CMD1; 5% of wild-type DNA binding activity; transcriptional activation is only reduced to 26% of wild-type activity;, features a modification of the amino acid from F to L at position 154.
+The protein's natural variant, known as in CMD1; 17% of wild-type DNA binding activity; shows a 2-fold reduction in nuclear import efficiency; transcriptional activation is only reduced to 62% of wild-type activity;, features a modification of the amino acid from A to T at position 158.
+The protein's natural variant, known as in CMD1; residual DNA binding and transactivation of regulated genes, features a modification of the amino acid from H to Q at position 165.
+The protein's natural variant, known as in CMD1; loss of DNA binding;, features a modification of the amino acid from H to Y at position 165.
+The protein's natural variant, known as in CMD1; decreased 75% transactivational activity, features a modification of the amino acid from H to P at position 169.
+The protein's natural variant, known as in CMD1; mild form overlapping with small patella syndrome; decreased 50% transactivational activity;, features a modification of the amino acid from H to Q at position 169.
+The protein's natural variant, known as in CMD1;, features a modification of the amino acid from P to L at position 170.
+The protein's natural variant, known as in CMD1, features a modification of the amino acid from P to R at position 170.
+The protein's natural variant, known as in CMD1;, features a modification of the amino acid from K to E at position 173.
+The protein's natural variant, known as in mutant TS-38, features a modification of the amino acid from E to K at position 802.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from D to N at position 166.
+The protein's natural variant, known as in MRD36, features a modification of the amino acid from V to L at position 132.
+The protein's natural variant, known as in MRD36; reduces PPP2CA binding; reduces PPP2R5A binding; reduces PPP2R5C binding; does not affect PPP2R5D binding; reduces PPP2R2A binding; reduces PPP2R2B binding; does not affect PPP2R3A binding; decreases phosphatase activity of PPP2CA;, features a modification of the amino acid from P to L at position 179.
+The protein's natural variant, known as in MRD36; reduces PPP2CA binding; reduces PPP2R5A binding; reduces PPP2R5C binding; does not affect PPP2R5D binding; reduces PPP2R2A binding; reduces PPP2R2B binding; reduces PPP2R3A binding; decreases phosphatase activity of PPP2CA;, features a modification of the amino acid from R to W at position 182.
+The protein's natural variant, known as in MRD36; reduces PPP2CA binding; reduces PPP2R5A binding; reduces PPP2R5C binding; does not affect PPP2R5D binding; reduces PPP2R2A binding; reduces PPP2R2B binding; reduces PPP2R3A binding; does not affect phosphatase activity of PPP2CA;, features a modification of the amino acid from R to H at position 258.
+The protein's natural variant, known as in HKPX2; heteropentameric channel complexes with GLRA1 require much higher glycine levels for channel activation; no effect on expression at the cell membrane;, features a modification of the amino acid from M to R at position 199.
+The protein's natural variant, known as in HKPX2; heteropentameric channel complexes with GLRA1 require much higher glycine levels for channel activation;, features a modification of the amino acid from G to D at position 251.
+The protein's natural variant, known as in HKPX2; heteropentameric channel complexes with GLRA1 have reduced expression at the cell membrane and display spontaneous channel opening in the absence of extracellular glycine, features a modification of the amino acid from L to R at position 307.
+The protein's natural variant, known as in HKPX2; heteropentameric channel complexes with GLRA1 have reduced expression at the cell membrane and reduced channel activity, features a modification of the amino acid from W to C at position 332.
+The protein's natural variant, known as found in patients with hemolytic anemia; unknown pathological significance; Montefiore;, features a modification of the amino acid from E to K at position 40.
+The protein's natural variant, known as in Di(a)/Memphis-II antigen;, features a modification of the amino acid from K to E at position 56.
+The protein's natural variant, known as in SPH4; Cape Town;, features a modification of the amino acid from E to K at position 90.
+The protein's natural variant, known as in SPH4; Fukoka;, features a modification of the amino acid from G to R at position 130.
+The protein's natural variant, known as in SPH4; Mondego, features a modification of the amino acid from P to S at position 147.
+The protein's natural variant, known as in SPH4; Boston, features a modification of the amino acid from A to D at position 285.
+The protein's natural variant, known as in SPH4; Tuscaloosa;, features a modification of the amino acid from P to R at position 327.
+The protein's natural variant, known as in NFLD+ antigen;, features a modification of the amino acid from E to D at position 429.
+The protein's natural variant, known as in ELO antigen;, features a modification of the amino acid from R to W at position 432.
+The protein's natural variant, known as in DRTA4; decreased expression; decreased stability; no effect on dimerization;, features a modification of the amino acid from T to N at position 444.
+The protein's natural variant, known as in SPH4; Benesov, features a modification of the amino acid from G to E at position 455.
+The protein's natural variant, known as in SPH4; Yamagata, features a modification of the amino acid from G to R at position 455.
+The protein's natural variant, known as in FR(a+) antigen;, features a modification of the amino acid from E to K at position 480.
+The protein's natural variant, known as in SPH4; Coimbra; also in AR-dRTA;, features a modification of the amino acid from V to M at position 488.
+The protein's natural variant, known as in SPH4; Bicetre I;, features a modification of the amino acid from R to C at position 490.
+The protein's natural variant, known as in SPH4; Pinhal;, features a modification of the amino acid from R to H at position 490.
+The protein's natural variant, known as in SPH4; Dresden;, features a modification of the amino acid from R to C at position 518.
+The protein's natural variant, known as in RB(A) antigen;, features a modification of the amino acid from P to L at position 548.
+The protein's natural variant, known as in TR(A) antigen, features a modification of the amino acid from K to N at position 551.
+The protein's natural variant, known as in WARR antigen, features a modification of the amino acid from T to I at position 552.
+The protein's natural variant, known as in VG(a) antigen, features a modification of the amino acid from Y to H at position 555.
+The protein's natural variant, known as in WD(a) antigen;, features a modification of the amino acid from V to M at position 557.
+The protein's natural variant, known as in NFLD+ antigen, features a modification of the amino acid from P to A at position 561.
+The protein's natural variant, known as in BOW antigen, features a modification of the amino acid from P to S at position 561.
+The protein's natural variant, known as in WU antigen;, features a modification of the amino acid from G to A at position 565.
+The protein's natural variant, known as in KREP antigen, features a modification of the amino acid from P to A at position 566.
+The protein's natural variant, known as in PN(a) antigen;, features a modification of the amino acid from P to S at position 566.
+The protein's natural variant, known as in BP(a) antigen, features a modification of the amino acid from N to K at position 569.
+The protein's natural variant, known as in DRTA1; reduced red cell sulfate transport and altered glycosylation of the red cell band 3 N-glycan chain;, features a modification of the amino acid from R to C at position 589.
+The protein's natural variant, known as in DRTA1;, features a modification of the amino acid from R to H at position 589.
+The protein's natural variant, known as in DRTA1;, features a modification of the amino acid from R to S at position 589.
+The protein's natural variant, known as in DRTA4;, features a modification of the amino acid from R to H at position 602.
+The protein's natural variant, known as in DRTA1; detected subapically and at the apical membrane as well as at the basolateral membrane in contrast to the normal basolateral appearance of wild-type protein;, features a modification of the amino acid from G to R at position 609.
+The protein's natural variant, known as in DRTA1; markedly increased red cell sulfate transport but almost normal red cell iodide transport;, features a modification of the amino acid from S to F at position 613.
+The protein's natural variant, known as in SW(a+) antigen;, features a modification of the amino acid from R to Q at position 646.
+The protein's natural variant, known as in SW(a+) antigen;, features a modification of the amino acid from R to W at position 646.
+The protein's natural variant, known as in HG(a) antigen;, features a modification of the amino acid from R to C at position 656.
+The protein's natural variant, known as in MO(a) antigen;, features a modification of the amino acid from R to H at position 656.
+The protein's natural variant, known as in WR(a) antigen;, features a modification of the amino acid from E to K at position 658.
+The protein's natural variant, known as in SPH4; Tambau, features a modification of the amino acid from M to K at position 663.
+The protein's natural variant, known as in CHC; Blackburn; induces abnormal cations sodium and potassium fluxes; decreases anion chloride transport;, features a modification of the amino acid from L to P at position 687.
+The protein's natural variant, known as in DRTA4 and dRTA-NRC; impairs expression at the cell membrane;, features a modification of the amino acid from G to D at position 701.
+The protein's natural variant, known as in SPH4; Horam; induces abnormal cations sodium and potassium fluxes; decreases anion chloride transport, features a modification of the amino acid from D to Y at position 705.
+The protein's natural variant, known as in SPH4; Most, features a modification of the amino acid from L to P at position 707.
+The protein's natural variant, known as in SPH4; Okinawa, features a modification of the amino acid from G to R at position 714.
+The protein's natural variant, known as in CHC; Hemel; induces abnormal cations sodium and potassium fluxes; decreases anion chloride transport;, features a modification of the amino acid from S to P at position 731.
+The protein's natural variant, known as in CHC; Hurstpierpont; induces abnormal cations sodium and potassium fluxes; decreases anion chloride transport;, features a modification of the amino acid from H to R at position 734.
+The protein's natural variant, known as in SPH4; Prague II; induces abnormal cations sodium and potassium fluxes; decreases anion chloride transport;, features a modification of the amino acid from R to Q at position 760.
+The protein's natural variant, known as in SPH4; Hradec Kralove;, features a modification of the amino acid from R to W at position 760.
+The protein's natural variant, known as in SPH4; Chur;, features a modification of the amino acid from G to D at position 771.
+The protein's natural variant, known as in dRTA-NRC;, features a modification of the amino acid from S to P at position 773.
+The protein's natural variant, known as in SPH4; Napoli II, features a modification of the amino acid from I to N at position 783.
+The protein's natural variant, known as in SPH4; Jablonec;, features a modification of the amino acid from R to C at position 808.
+The protein's natural variant, known as in SPH4; Nara;, features a modification of the amino acid from R to H at position 808.
+The protein's natural variant, known as in SPH4; Birmingham, features a modification of the amino acid from H to P at position 834.
+The protein's natural variant, known as in SPH4; Tokyo;, features a modification of the amino acid from T to A at position 837.
+The protein's natural variant, known as in SPH4; Philadelphia, features a modification of the amino acid from T to M at position 837.
+The protein's natural variant, known as in SPH4; Nagoya, features a modification of the amino acid from T to R at position 837.
+The protein's natural variant, known as in Di(a)/Memphis-II antigen;, features a modification of the amino acid from P to L at position 854.
+The protein's natural variant, known as in DRTA1; impairs expression at the cell membrane;, features a modification of the amino acid from A to D at position 858.
+The protein's natural variant, known as in acanthocytosis; slightly increases transporter activity; impairs expression at the cell membrane;, features a modification of the amino acid from P to L at position 868.
+The protein's natural variant, known as in SPH4; Prague III;, features a modification of the amino acid from R to W at position 870.
+The protein's natural variant, known as in strain: Zim2, features a modification of the amino acid from N to S at position 82.
+The protein's natural variant, known as in strain: Zim3, features a modification of the amino acid from F to L at position 110.
+The protein's natural variant, known as in strain: Zim8, features a modification of the amino acid from T to I at position 699.
+The protein's natural variant, known as in strain: Zim1, features a modification of the amino acid from E to G at position 845.
+The protein's natural variant, known as in strain: Zim8, features a modification of the amino acid from S to N at position 862.
+The protein's natural variant, known as in strain: F, features a modification of the amino acid from T to I at position 227.
+The protein's natural variant, known as in cancer;, features a modification of the amino acid from S to C at position 104.
+The protein's natural variant, known as in ATLD1;, features a modification of the amino acid from N to S at position 117.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from F to C at position 237.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from H to Y at position 302.
+The protein's natural variant, known as in ovarian cancer;, features a modification of the amino acid from R to W at position 305.
+The protein's natural variant, known as in cancer;, features a modification of the amino acid from R to H at position 503.
+The protein's natural variant, known as in cancer;, features a modification of the amino acid from R to Q at position 572.
+The protein's natural variant, known as in CONDSIAS; unknown pathological significance; reduced protein abundance; increased levels of ADP-ribose; May result in protein misfolding or aggregation, features a modification of the amino acid from C to F at position 26.
+The protein's natural variant, known as in CONDSIAS; unknown pathological significance;, features a modification of the amino acid from D to N at position 34.
+The protein's natural variant, known as in CONDSIAS; severely reduced protein levels in patient fibroblasts; decreased stability and reduced Tm; reduced alpha-helix content and altered secondary structure detected by circular dichroism spectroscopy;, features a modification of the amino acid from T to P at position 79.
+The protein's natural variant, known as in CONDSIAS; unknown pathological significance;, features a modification of the amino acid from S to L at position 177.
+The protein's natural variant, known as in CONDSIAS; no detectable protein levels in patient fibroblasts, features a modification of the amino acid from KI to N at position 249.
+The protein's natural variant, known as in CONDSIAS; unknown pathological significance; results in accumulation of poly(ADP-ribose) in the nucleus of patient cells after exposure to H(2)O(2); reduced protein abundance in fibroblasts; localization to the cytoplasm in fibroblasts; no effect on hydrolase activity in vitro; may result in reduced protein stability;, features a modification of the amino acid from V to G at position 335.
+The protein's natural variant, known as in some alleles, features a modification of the amino acid from KSTWS to MSTLG at position 34.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from E to K at position 607.
+The protein's natural variant, known as in FRBRL, features a modification of the amino acid from Q to H at position 22.
+The protein's natural variant, known as in FRBRL, features a modification of the amino acid from H to D at position 23.
+The protein's natural variant, known as in FRBRL;, features a modification of the amino acid from Y to C at position 36.
+The protein's natural variant, known as in SMAPME; unknown pathological significance; decreased ceramide catabolic process;, features a modification of the amino acid from T to A at position 42.
+The protein's natural variant, known as in SMAPME; results in reduced activity;, features a modification of the amino acid from T to M at position 42.
+The protein's natural variant, known as in FRBRL; decreased ceramide catabolic process, features a modification of the amino acid from V to E at position 97.
+The protein's natural variant, known as in FRBRL, features a modification of the amino acid from V to G at position 97.
+The protein's natural variant, known as in FRBRL; loss of ceramidase activity;, features a modification of the amino acid from E to V at position 138.
+The protein's natural variant, known as in SMAPME; decreased protein abundance; alters the splicing of ASAH1 transcripts;, features a modification of the amino acid from K to N at position 152.
+The protein's natural variant, known as in FRBRL, features a modification of the amino acid from G to W at position 168.
+The protein's natural variant, known as in FRBRL; unknown pathological significance;, features a modification of the amino acid from W to R at position 169.
+The protein's natural variant, known as in FRBRL;, features a modification of the amino acid from L to V at position 182.
+The protein's natural variant, known as in FRBRL;, features a modification of the amino acid from T to K at position 222.
+The protein's natural variant, known as in FRBRL; decreased ceramide catabolic process;, features a modification of the amino acid from G to R at position 235.
+The protein's natural variant, known as in FRBRL; unknown pathological significance; loss of ceramidase activity, features a modification of the amino acid from R to G at position 254.
+The protein's natural variant, known as in FRBRL;, features a modification of the amino acid from N to D at position 320.
+The protein's natural variant, known as in FRBRL; unknown pathological significance;, features a modification of the amino acid from R to C at position 333.
+The protein's natural variant, known as in FRBRL; loss of ceramidase activity, features a modification of the amino acid from P to R at position 362.
+The protein's natural variant, known as in FCORD2; somatic mutation; decreased interaction with TSC2; decreased function in negative regulation of TOR signaling;, features a modification of the amino acid from R to W at position 22.
+The protein's natural variant, known as in TSC1; unknown pathological significance;, features a modification of the amino acid from E to D at position 51.
+The protein's natural variant, known as in TSC1; unknown pathological significance; reduced expression; altered subcellular localization; reduced inhibition of TORC1 signaling;, features a modification of the amino acid from L to R at position 61.
+The protein's natural variant, known as in a bladder tumor; somatic mutation; reduced stability; does not affect interaction with TSC2;, features a modification of the amino acid from H to R at position 68.
+The protein's natural variant, known as in TSC1;, features a modification of the amino acid from L to P at position 72.
+The protein's natural variant, known as in TSC1; reduced expression; altered subcellular localization; reduced interaction with TSC2; reduced inhibition of TORC1 signaling;, features a modification of the amino acid from L to P at position 117.
+The protein's natural variant, known as in TSC1; unknown pathological significance; no effect on expression; no effect on subcellular localization; no effect on inhibition of TORC1 signaling;, features a modification of the amino acid from V to I at position 126.
+The protein's natural variant, known as in TSC1; unknown pathological significance; reduced expression; altered subcellular localization; reduced inhibition of TORC1 signaling;, features a modification of the amino acid from G to D at position 132.
+The protein's natural variant, known as in TSC1; unknown pathological significance; no effect on expression; no effect on subcellular localization; no effect on inhibition of TORC1 signaling;, features a modification of the amino acid from V to I at position 133.
+The protein's natural variant, known as in a bladder tumor; somatic mutation; reduced stability; does not affect interaction with TSC2;, features a modification of the amino acid from F to C at position 158.
+The protein's natural variant, known as found in a patient suspected of having tuberous sclerosis; unknown pathological significance; reduced expression; altered subcellular localization; reduced inhibition of TORC1 signaling;, features a modification of the amino acid from F to S at position 158.
+The protein's natural variant, known as in TSC1; reduced expression; reduced inhibition of TORC1 signaling;, features a modification of the amino acid from L to P at position 180.
+The natural variant of this protein is characterized by an amino acid alteration from R to S at position 190.
+The protein's natural variant, known as in TSC1; reduced expression; reduced inhibition of TORC1 signaling;, features a modification of the amino acid from L to H at position 191.
+The protein's natural variant, known as in TSC1; reduced expression; altered subcellular localization; reduced interaction with TSC2; reduced inhibition of TORC1 signaling, features a modification of the amino acid from NF to I at position 199.
+The protein's natural variant, known as in FCORD2; somatic mutation; decreased interaction with TSC2; decreased function in negative regulation of TOR signaling;, features a modification of the amino acid from R to C at position 204.
+The protein's natural variant, known as found in a patient suspected of having tuberous sclerosis; reduced expression; altered subcellular localization; reduced inhibition of TORC1 signaling;, features a modification of the amino acid from R to P at position 204.
+The protein's natural variant, known as in a bladder tumor; somatic mutation; reduced stability; does not affect interaction with TSC2, features a modification of the amino acid from H to D at position 206.
+The protein's natural variant, known as in a bladder tumor; diffuse punctate cytoplasmic distribution in aminoacid-starved conditions; does not affect interaction with TSC2;, features a modification of the amino acid from F to L at position 216.
+The protein's natural variant, known as in TSC1; reduced expression; reduced inhibition of TORC1 signaling;, features a modification of the amino acid from M to R at position 224.
+The protein's natural variant, known as in TSC1; unknown pathological significance; no effect on expression; no effect on inhibition of TORC1 signaling;, features a modification of the amino acid from R to K at position 246.
+The protein's natural variant, known as in TSC1; unknown pathological significance; no effect on expression; no effect on inhibition of TORC1 signaling;, features a modification of the amino acid from G to R at position 305.
+The protein's natural variant, known as in TSC1; unknown pathological significance; no effect on expression; no effect on inhibition of TORC1 signaling;, features a modification of the amino acid from G to W at position 305.
+The protein's natural variant, known as in TSC1; unknown pathological significance; no effect on expression; no effect on subcellular localization; no effect on inhibition of TORC1 signaling;, features a modification of the amino acid from R to Q at position 336.
+The protein's natural variant, known as in TSC1; unknown pathological significance; no effect on expression; no effect on subcellular localization; no effect on inhibition of TORC1 signaling;, features a modification of the amino acid from P to S at position 362.
+The protein's natural variant, known as in TSC1; unknown pathological significance; no effect on expression; no effect on subcellular localization; no effect on inhibition of TORC1 signaling;, features a modification of the amino acid from L to I at position 411.
+The protein's natural variant, known as in TSC1; unknown pathological significance; does not affect interaction with TSC2;, features a modification of the amino acid from T to I at position 417.
+The protein's natural variant, known as no effect on expression; no effect on subcellular localization; no effect on inhibition of TORC1 signaling;, features a modification of the amino acid from P to S at position 448.
+The protein's natural variant, known as in TSC1;, features a modification of the amino acid from R to Q at position 500.
+The protein's natural variant, known as no effect on expression; no effect on inhibition of TORC1 signaling;, features a modification of the amino acid from R to Q at position 509.
+The protein's natural variant, known as in TSC1; unknown pathological significance; no effect on expression; no effect on subcellular localization; no effect on inhibition of TORC1 signaling;, features a modification of the amino acid from A to P at position 523.
+The protein's natural variant, known as no effect on expression; no effect on subcellular localization; no effect on inhibition of TORC1 signaling;, features a modification of the amino acid from A to V at position 567.
+The protein's natural variant, known as in TSC1, features a modification of the amino acid from CKIP to S at position 589.
+The protein's natural variant, known as in TSC1;, features a modification of the amino acid from Q to E at position 654.
+The protein's natural variant, known as in TSC1; unknown pathological significance; no effect on expression; no effect on subcellular localization; no effect on inhibition of TORC1 signaling;, features a modification of the amino acid from D to H at position 693.
+The protein's natural variant, known as in TSC1; unknown pathological significance; no effect on expression; no effect on subcellular localization; no effect on inhibition of TORC1 signaling;, features a modification of the amino acid from L to R at position 698.
+The protein's natural variant, known as in TSC1; unknown pathological significance; no effect on expression; no effect on subcellular localization; no effect on inhibition of TORC1 signaling;, features a modification of the amino acid from Q to H at position 701.
+The protein's natural variant, known as in TSC1;, features a modification of the amino acid from A to E at position 726.
+The protein's natural variant, known as might be associated with susceptibility to focal cortical dysplasia of the Taylor balloon cell type;, features a modification of the amino acid from H to Y at position 732.
+The protein's natural variant, known as in TSC1; unknown pathological significance; no effect on expression; no effect on subcellular localization; no effect on inhibition of TORC1 signaling;, features a modification of the amino acid from N to S at position 762.
+The protein's natural variant, known as in TSC1; unknown pathological significance; no effect on expression; no effect on subcellular localization; no effect on inhibition of TORC1 signaling;, features a modification of the amino acid from R to G at position 811.
+The protein's natural variant, known as in TSC1; unknown pathological significance; no effect on expression; no effect on subcellular localization; no effect on inhibition of TORC1 signaling;, features a modification of the amino acid from A to T at position 883.
+The protein's natural variant, known as in TSC1;, features a modification of the amino acid from T to S at position 899.
+The protein's natural variant, known as in TSC1; unknown pathological significance; no effect on expression; no effect on subcellular localization; no effect on inhibition of TORC1 signaling;, features a modification of the amino acid from L to V at position 978.
+The protein's natural variant, known as no effect on expression; no effect on inhibition of TORC1 signaling;, features a modification of the amino acid from G to S at position 1035.
+The protein's natural variant, known as no effect on expression; no effect on inhibition of TORC1 signaling;, features a modification of the amino acid from R to H at position 1097.
+The protein's natural variant, known as in TSC1; unknown pathological significance; no effect on expression; no effect on subcellular localization; no effect on inhibition of TORC1 signaling;, features a modification of the amino acid from D to Y at position 1146.
+The protein's natural variant, known as reduced activity towards daunorubicin;, features a modification of the amino acid from N to S at position 52.
+The protein's natural variant, known as reduced activity towards daunorubicin;, features a modification of the amino acid from E to D at position 55.
+The protein's natural variant, known as in strain: cv. Bus-1, cv. Ci-0, cv. Cvi-0, cv. Edi-0, cv. Kas-1 and cv. Ost-0, features a modification of the amino acid from H to L at position 17.
+The protein's natural variant, known as in strain: cv. Pog-0, features a modification of the amino acid from D to N at position 63.
+The protein's natural variant, known as in strain: cv. Bl-1, features a modification of the amino acid from N to S at position 240.
+The protein's natural variant, known as in strain: cv. Edi-0, features a modification of the amino acid from F to L at position 259.
+The protein's natural variant, known as in strain: DAT2, features a modification of the amino acid from K to T at position 3.
+The protein's natural variant, known as in strain: DAT2, features a modification of the amino acid from EA to TD at position 8.
+The protein's natural variant, known as in strain: 10581, features a modification of the amino acid from A to V at position 8.
+The protein's natural variant, known as in strain: DAT2, features a modification of the amino acid from E to Q at position 11.
+The protein's natural variant, known as in strain: DAT2, features a modification of the amino acid from I to V at position 19.
+The protein's natural variant, known as in strain: DAT2 and 10581, features a modification of the amino acid from N to K at position 124.
+The protein's natural variant, known as in strain: 10581, features a modification of the amino acid from D to N at position 205.
+The protein's natural variant, known as in strain: 181, 217, 191 and 204, features a modification of the amino acid from E to D at position 1.
+The protein's natural variant, known as in strain: 50, features a modification of the amino acid from I to V at position 18.
+The protein's natural variant, known as in strain: 50, features a modification of the amino acid from E to D at position 29.
+The protein's natural variant, known as in strain: 181, 217 and 191, features a modification of the amino acid from G to S at position 46.
+The protein's natural variant, known as in strain: 50, features a modification of the amino acid from H to R at position 47.
+The protein's natural variant, known as in strain: 181 and 217, features a modification of the amino acid from P to A at position 63.
+The protein's natural variant, known as in strain: 181, 217 and 204, features a modification of the amino acid from Q to P at position 65.
+The protein's natural variant, known as in strain: 191, features a modification of the amino acid from E to Q at position 70.
+The protein's natural variant, known as in MRT50; does not enhance DCP2 decapping activity;, features a modification of the amino acid from F to S at position 54.
+The protein's natural variant, known as in a rhabdomyosarcoma sample, features a modification of the amino acid from R to C at position 86.
+The protein's natural variant, known as in lung cancer; somatic mutation;, features a modification of the amino acid from S to F at position 233.
+The protein's natural variant, known as in BIRGD; abolishes mannose-binding ability;, features a modification of the amino acid from W to R at position 264.
+The protein's natural variant, known as no effect on mannose-binding ability;, features a modification of the amino acid from V to A at position 278.
+The protein's natural variant, known as significant reduction in mannose-binding ability;, features a modification of the amino acid from N to D at position 288.
+The protein's natural variant, known as significant reduction in mannose-binding ability; significant decrease in thermal stability; increased sensitivity of sugar binding to pH change;, features a modification of the amino acid from A to P at position 300.
+The protein's natural variant, known as in RTSC2; may affect splicing and/or have a negative impact on transcription efficiency; results in decreased interaction with COMMD1;, features a modification of the amino acid from T to A at position 17.
+The protein's natural variant, known as in RTSC2;, features a modification of the amino acid from Y to C at position 557.
+The protein's natural variant, known as in FRTS3; the mutant is mistargeted to mitochondria; results in impaired mitochondrial oxidative phosphorylation and defects in the transport of fluids across the epithelium of renal proximal tubular cells;, features a modification of the amino acid from E to K at position 3.
+The protein's natural variant, known as in EPM10; does not affect interaction with EPM2A and NHLRC1;, features a modification of the amino acid from F to L at position 261.
+The protein's natural variant, known as in THMD2;, features a modification of the amino acid from G to V at position 23.
+The protein's natural variant, known as in THMD2;, features a modification of the amino acid from T to A at position 422.
+The natural variant of this protein is characterized by an amino acid alteration from S to A at position 47.
+The protein's natural variant, known as impairs antimicrobial activity against S.aureus;, features a modification of the amino acid from R to H at position 71.
+The protein's natural variant, known as in AI1G; impaired folding of the protein; abolishes ability to activate FAM20C protein kinase activity, features a modification of the amino acid from L to R at position 173.
+The protein's natural variant, known as in AI1G, features a modification of the amino acid from DYSQDEKALLGACDCTQI to V at position 214.
+The protein's natural variant, known as in AI1G; impaired folding of the protein; abolishes ability to activate FAM20C protein kinase activity;, features a modification of the amino acid from G to D at position 331.
+The protein's natural variant, known as in AI1G; impaired folding of the protein; abolishes ability to activate FAM20C protein kinase activity;, features a modification of the amino acid from D to N at position 403.
+The natural variant of this protein is characterized by an amino acid alteration from P to L at position 45.
+The protein's natural variant, known as in strain: MI112, features a modification of the amino acid from A to V at position 165.
+The protein's natural variant, known as in KOS;, features a modification of the amino acid from Q to P at position 727.
+The protein's natural variant, known as in CLN4B; results in near absence of palmitoylated monomeric forms of the protein and formation of high molecular mass aggregates with diffuse intracellular localization;, features a modification of the amino acid from L to R at position 115.
+The protein's natural variant, known as in allele GSTZ1*C;, features a modification of the amino acid from K to E at position 32.
+The protein's natural variant, known as in allele GSTZ1*B and allele GSTZ1*C;, features a modification of the amino acid from R to G at position 42.
+The protein's natural variant, known as in MAAID; decreased maleylacetoacetate isomerase activity, features a modification of the amino acid from V to M at position 99.
+The protein's natural variant, known as in MAAID; decreased maleylacetoacetate isomerase activity, features a modification of the amino acid from A to V at position 150.
+The protein's natural variant, known as in strain: SJL/J, features a modification of the amino acid from S to G at position 50.
+The protein's natural variant, known as in strain: SJL/J, features a modification of the amino acid from R to Q at position 92.
+The protein's natural variant, known as in strain: ZIM(S)24, features a modification of the amino acid from M to V at position 150.
+The protein's natural variant, known as in EDSCL1; not or less efficiently secreted into the extracellular matrix, features a modification of the amino acid from L to P at position 25.
+The protein's natural variant, known as in EDSCL1; not or less efficiently secreted into the extracellular matrix, features a modification of the amino acid from L to R at position 25.
+The protein's natural variant, known as in FMDMF; unknown pathological significance;, features a modification of the amino acid from Q to E at position 123.
+The protein's natural variant, known as associated with increased risk of cervical artery dissection, features a modification of the amino acid from D to N at position 229.
+The protein's natural variant, known as in FMDMF;, features a modification of the amino acid from G to S at position 514.
+The protein's natural variant, known as in EDSCL1;, features a modification of the amino acid from G to S at position 530.
+The protein's natural variant, known as in FMDMF; unknown pathological significance, features a modification of the amino acid from R to W at position 611.
+The protein's natural variant, known as found in a renal cell carcinoma case; somatic mutation;, features a modification of the amino acid from P to L at position 908.
+The protein's natural variant, known as in FMDMF; unknown pathological significance, features a modification of the amino acid from P to L at position 1164.
+The protein's natural variant, known as in FMDMF; unknown pathological significance, features a modification of the amino acid from P to S at position 1400.
+The protein's natural variant, known as in EDSCL1, features a modification of the amino acid from G to C at position 1486.
+The protein's natural variant, known as in EDSCL1, features a modification of the amino acid from G to D at position 1489.
+The protein's natural variant, known as in EDSCL1;, features a modification of the amino acid from C to S at position 1639.
+The natural variant of this protein is characterized by an amino acid alteration from C to L at position 57.
+The protein's natural variant, known as in IMGT allele IGHV1-2*01, features a modification of the amino acid from W to R at position 69.
+The protein's natural variant, known as in IMGT allele IGHV1-2*01, features a modification of the amino acid from W to R at position 86.
+The protein's natural variant, known as in IMGT allele IGHV1-2*01, requires 2 nucleotide substitutions, features a modification of the amino acid from M to S at position 89.
+The protein's natural variant, known as in IMGT allele IGHV1-2*01, features a modification of the amino acid from A to V at position 111.
+The protein's natural variant, known as in IOLOD; decreased protein abundance;, features a modification of the amino acid from Y to C at position 97.
+The protein's natural variant, known as in IOLOD; decreased protein abundance;, features a modification of the amino acid from A to P at position 106.
+The protein's natural variant, known as in ADSD2; no effect on basal 3',5'-cyclic-nucleotide phosphodiesterase activity; the mutation severely disrupts the stimulatory effect on the enzyme activity mediated by cAMP binding;, features a modification of the amino acid from F to L at position 290.
+The natural variant of this protein is characterized by an amino acid alteration from L to P at position 303.
+The protein's natural variant, known as in ADSD2; no effect on basal 3',5'-cyclic-nucleotide phosphodiesterase activity; the mutation severely disrupts the stimulatory effect on the enzyme activity mediated by cAMP binding;, features a modification of the amino acid from F to L at position 324.
+The protein's natural variant, known as in a patient with amyotrophic lateral sclerosis;, features a modification of the amino acid from H to Y at position 507.
+The natural variant of this protein is characterized by an amino acid alteration from R to K at position 151.
+The natural variant of this protein is characterized by an amino acid alteration from S to T at position 710.
+The protein's natural variant, known as in strain: BS202, features a modification of the amino acid from N to K at position 8.
+The protein's natural variant, known as in strain: G7, features a modification of the amino acid from I to L at position 11.
+The protein's natural variant, known as in strain: G7, features a modification of the amino acid from P to S at position 13.
+The protein's natural variant, known as in strain: G7, features a modification of the amino acid from A to P at position 16.
+The protein's natural variant, known as in strain: G7, features a modification of the amino acid from L to M at position 36.
+The protein's natural variant, known as in strain: G7, features a modification of the amino acid from I to T at position 48.
+The protein's natural variant, known as in strain: G7, features a modification of the amino acid from EN to GS at position 59.
+The protein's natural variant, known as in strain: G7, features a modification of the amino acid from QS to LP at position 62.
+The protein's natural variant, known as in strain: G7, features a modification of the amino acid from T to V at position 65.
+The protein's natural variant, known as in strain: G7, features a modification of the amino acid from KQ to EH at position 68.
+The protein's natural variant, known as in strain: G7, features a modification of the amino acid from G to H at position 79.
+The protein's natural variant, known as in strain: G7, features a modification of the amino acid from V to I at position 85.
+The protein's natural variant, known as in strain: G7, features a modification of the amino acid from A to T at position 88.
+The protein's natural variant, known as in strain: G7, features a modification of the amino acid from S to A at position 121.
+The protein's natural variant, known as in strain: G7, features a modification of the amino acid from K to N at position 195.
+The protein's natural variant, known as in strain: G7, features a modification of the amino acid from S to L at position 222.
+The protein's natural variant, known as in strain: G7, features a modification of the amino acid from T to M at position 264.
+The protein's natural variant, known as in strain: G7, features a modification of the amino acid from G to S at position 270.
+The protein's natural variant, known as in strain: G7, features a modification of the amino acid from I to V at position 276.
+The protein's natural variant, known as in strain: G7, features a modification of the amino acid from L to I at position 285.
+The protein's natural variant, known as in ATFB16; affects steady-state channel inactivation;, features a modification of the amino acid from R to K at position 6.
+The protein's natural variant, known as in BRGDA7 and ATFB16; unknown pathological significance; results in a decrease in peak sodium current density;, features a modification of the amino acid from L to P at position 10.
+The protein's natural variant, known as found in a case of idiopathic ventricular fibrillation; unknown pathological significance;, features a modification of the amino acid from V to G at position 54.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from Q to L at position 89.
+The protein's natural variant, known as in ATFB16; results in decreased sodium current density;, features a modification of the amino acid from A to V at position 130.
+The protein's natural variant, known as in ATFB16; results in a decrease in peak sodium current density;, features a modification of the amino acid from M to T at position 161.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from A to T at position 195.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from K to T at position 597.
+The protein's natural variant, known as in ZLS2;, features a modification of the amino acid from R to P at position 485.
+The protein's natural variant, known as in strain: Isolate CMF 960522.46, features a modification of the amino acid from I to V at position 39.
+The protein's natural variant, known as in strain: Isolate CMF 960522.46, features a modification of the amino acid from M to T at position 257.
+The protein's natural variant, known as in strain: Isolate CMF 960522.46 and Isolate FMNHEAR1223, features a modification of the amino acid from S to T at position 316.
+The protein's natural variant, known as in strain: Isolate FMNHEAR1223, features a modification of the amino acid from V to M at position 348.
+The protein's natural variant, known as in strain: Isolate CMF 960522.46, features a modification of the amino acid from I to T at position 356.
+The protein's natural variant, known as in NEDMHAL; unknown pathological significance; results in impaired proteasome assembly, features a modification of the amino acid from Y to H at position 103.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from S to F at position 13.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from R to L at position 31.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from S to F at position 42.
+The protein's natural variant, known as in CF; unknown pathological significance;, features a modification of the amino acid from D to G at position 44.
+The protein's natural variant, known as in CBAVD;, features a modification of the amino acid from S to Y at position 50.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from W to G at position 57.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from P to L at position 67.
+The protein's natural variant, known as in CF and CBAVD;, features a modification of the amino acid from R to W at position 74.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from G to E at position 85.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from F to L at position 87.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from G to R at position 91.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from E to K at position 92.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from Q to R at position 98.
+The protein's natural variant, known as in CF, features a modification of the amino acid from I to S at position 105.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from Y to C at position 109.
+The protein's natural variant, known as in CF and CBAVD;, features a modification of the amino acid from D to H at position 110.
+The protein's natural variant, known as in CBAVD;, features a modification of the amino acid from P to L at position 111.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from R to C at position 117.
+The protein's natural variant, known as in CF and CBAVD; strong decrease in single channel conductance; promotes rapid return to the closed state of the channel; decrease in bicarbonate transport;, features a modification of the amino acid from R to H at position 117.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from R to L at position 117.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from R to P at position 117.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from A to T at position 120.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from H to R at position 139.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from A to D at position 141.
+The protein's natural variant, known as in CF; unknown pathological significance; loss of bicarbonate transport; decreased inhibition of epithelial sodium channel (ENaC), when tested in a heterologous system; no effect on protein maturation, subcellular location at the plasma membrane, nor on chloride channel activity;, features a modification of the amino acid from I to T at position 148.
+The protein's natural variant, known as in CBAVD;, features a modification of the amino acid from G to R at position 149.
+The protein's natural variant, known as in CBAVD; unknown pathological significance;, features a modification of the amino acid from R to H at position 170.
+The protein's natural variant, known as in CF; loss of bicarbonate transport; no effect on protein maturation, subcellular location at the plasma membrane, nor on chloride channel activity;, features a modification of the amino acid from G to R at position 178.
+The protein's natural variant, known as in CBAVD and CF; decrease in bicarbonate transport; no effect on chloride channel activity;, features a modification of the amino acid from E to K at position 193.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from H to Q at position 199.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from H to Y at position 199.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from P to S at position 205.
+The protein's natural variant, known as in CF and CBAVD;, features a modification of the amino acid from L to W at position 206.
+The protein's natural variant, known as in CF; unknown pathological significance;, features a modification of the amino acid from C to R at position 225.
+The protein's natural variant, known as in CBAVD;, features a modification of the amino acid from V to D at position 232.
+The protein's natural variant, known as in CBAVD;, features a modification of the amino acid from M to K at position 244.
+The protein's natural variant, known as in CBAVD;, features a modification of the amino acid from R to G at position 258.
+The protein's natural variant, known as in CF; decreased presence at the cell membrane due to increased internalization from the apical cell membrane; no effect on single channel gating and conductance;, features a modification of the amino acid from N to Y at position 287.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from R to Q at position 297.
+The protein's natural variant, known as in CF; unknown pathological significance;, features a modification of the amino acid from Y to C at position 301.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from S to N at position 307.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from F to L at position 311.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from G to E at position 314.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from G to R at position 314.
+The protein's natural variant, known as in CF and CBAVD; mild; does not prevent maturation of glycans;, features a modification of the amino acid from R to W at position 334.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from I to K at position 336.
+The protein's natural variant, known as in CF; mild; isolated hypotonic dehydration;, features a modification of the amino acid from T to I at position 338.
+The protein's natural variant, known as in CF; dominant mutation but mild phenotype;, features a modification of the amino acid from L to P at position 346.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from R to H at position 347.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from R to L at position 347.
+The protein's natural variant, known as in CF; MILD;, features a modification of the amino acid from R to P at position 347.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from R to Q at position 352.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from QT to KK at position 360.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from Q to K at position 359.
+The protein's natural variant, known as in CF, features a modification of the amino acid from K to KNK at position 370.
+The protein's natural variant, known as in CBAVD; unknown pathological significance;, features a modification of the amino acid from D to Y at position 443.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from A to E at position 455.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from V to F at position 456.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from G to V at position 458.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from G to C at position 480.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from S to F at position 492.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from E to Q at position 504.
+The protein's natural variant, known as in CBAVD;, features a modification of the amino acid from D to G at position 513.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from V to F at position 520.
+The protein's natural variant, known as in CBAVD;, features a modification of the amino acid from G to V at position 544.
+The protein's natural variant, known as in CF; impaired maturation of glycan chains;, features a modification of the amino acid from S to I at position 549.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from S to N at position 549.
+The protein's natural variant, known as in CF; impaired maturation of glycan chains;, features a modification of the amino acid from S to R at position 549.
+The protein's natural variant, known as in CF; decrease in the frequency of channel opening in vitro; decrease in channel activity and ATPase activity; complete loss of bicarbonate transport; no effect on trafficking to the cell membrane, protein stability, nor on the maturation of glycans;, features a modification of the amino acid from G to D at position 551.
+The protein's natural variant, known as in CF; decrease in bicarbonate transport; no effect on chloride channel activity;, features a modification of the amino acid from G to S at position 551.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from R to Q at position 553.
+The protein's natural variant, known as in CBAVD; unknown pathological significance;, features a modification of the amino acid from I to V at position 556.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from L to S at position 558.
+The protein's natural variant, known as in CF; impaired maturation of glycan chains;, features a modification of the amino acid from A to T at position 559.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from R to K at position 560.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from R to S at position 560.
+The protein's natural variant, known as in CF; impairs maturation and trafficking to the cell membrane; decrease in channel activity;, features a modification of the amino acid from R to T at position 560.
+The protein's natural variant, known as in CF; impairs maturation and trafficking to the cell membrane; decrease in channel activity;, features a modification of the amino acid from A to E at position 561.
+The protein's natural variant, known as in CBAVD and CF; unknown pathological significance; found in cis of the IVS8 TG11-T5 allele, which affects exon 9 splicing; no effect on protein maturation, trafficking to the cell membrane, nor on channel activity;, features a modification of the amino acid from V to I at position 562.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from V to L at position 562.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from Y to N at position 563.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from Y to C at position 569.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from Y to D at position 569.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from Y to H at position 569.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from L to S at position 571.
+The protein's natural variant, known as in CF; impaired maturation of glycan chains;, features a modification of the amino acid from D to N at position 572.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from P to H at position 574.
+The protein's natural variant, known as in CBAVD; unknown pathological significance;, features a modification of the amino acid from G to A at position 576.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from D to G at position 579.
+The protein's natural variant, known as in CF; impaired maturation of glycan chains;, features a modification of the amino acid from I to F at position 601.
+The protein's natural variant, known as in CF; impaired maturation of glycan chains;, features a modification of the amino acid from L to S at position 610.
+The protein's natural variant, known as in CF; impaired maturation of glycan chains;, features a modification of the amino acid from A to T at position 613.
+The protein's natural variant, known as in CF; impaired maturation of glycan chains;, features a modification of the amino acid from D to G at position 614.
+The protein's natural variant, known as in CF; impaired maturation of glycan chains;, features a modification of the amino acid from I to T at position 618.
+The protein's natural variant, known as in CF; impaired maturation of glycan chains;, features a modification of the amino acid from L to S at position 619.
+The protein's natural variant, known as in CF; impaired maturation of glycan chains;, features a modification of the amino acid from H to P at position 620.
+The protein's natural variant, known as in CF; strong decrease in bicarbonate transport; increase in chloride channel activity in vitro; no effect on glycan maturation;, features a modification of the amino acid from H to Q at position 620.
+The protein's natural variant, known as in CBAVD; decreased channel activity; has no effect on glycan maturation;, features a modification of the amino acid from G to D at position 622.
+The protein's natural variant, known as in CF; impaired maturation of glycan chains;, features a modification of the amino acid from G to R at position 628.
+The protein's natural variant, known as in CF; impaired maturation of glycan chains;, features a modification of the amino acid from L to P at position 633.
+The protein's natural variant, known as in CF; decrease in bicarbonate transport; no effect chloride channel activity;, features a modification of the amino acid from D to V at position 648.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from D to N at position 651.
+The protein's natural variant, known as in CF; no effect on glycan maturation and channel activity;, features a modification of the amino acid from T to S at position 665.
+The protein's natural variant, known as in CBAVD; unknown pathological significance;, features a modification of the amino acid from R to C at position 668.
+The protein's natural variant, known as in CF; unknown pathological significance;, features a modification of the amino acid from F to L at position 693.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from V to M at position 754.
+The protein's natural variant, known as in CBAVD;, features a modification of the amino acid from R to M at position 766.
+The protein's natural variant, known as in CBAVD; no effect on glycan maturation but decreased channel activity;, features a modification of the amino acid from R to G at position 792.
+The protein's natural variant, known as in CBAVD; small decrease in bicarbonate transport; increase in chloride channel activity in vitro; no effect on glycan maturation;, features a modification of the amino acid from A to G at position 800.
+The protein's natural variant, known as in CBAVD;, features a modification of the amino acid from I to M at position 807.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from E to K at position 822.
+The protein's natural variant, known as in thoracic sarcoidosis; no effect on glycan maturation and channel activity;, features a modification of the amino acid from E to K at position 826.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from C to Y at position 866.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from Y to C at position 913.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from Y to C at position 917.
+The protein's natural variant, known as in CBAVD; unknown pathological significance;, features a modification of the amino acid from V to G at position 938.
+The protein's natural variant, known as in CF; decrease in bicarbonate transport; no effect on chloride channel activity;, features a modification of the amino acid from H to Y at position 949.
+The protein's natural variant, known as in CF and CBAVD; unknown pathological significance;, features a modification of the amino acid from M to I at position 952.
+The protein's natural variant, known as in CBAVD; unknown pathological significance;, features a modification of the amino acid from A to V at position 959.
+The protein's natural variant, known as in CBAVD; unknown pathological significance;, features a modification of the amino acid from S to F at position 977.
+The protein's natural variant, known as in CF and CBAVD; unknown pathological significance;, features a modification of the amino acid from L to F at position 997.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from I to R at position 1005.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from A to E at position 1006.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from P to L at position 1013.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from M to I at position 1028.
+The protein's natural variant, known as in CBAVD; unknown pathological significance;, features a modification of the amino acid from Y to C at position 1032.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from F to V at position 1052.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from G to R at position 1061.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from L to P at position 1065.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from L to R at position 1065.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from R to C at position 1066.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from R to H at position 1066.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from R to L at position 1066.
+The protein's natural variant, known as in CF; loss of bicarbonate transport; no effect on protein maturation, subcellular location at the plasma membrane, nor on chloride channel activity;, features a modification of the amino acid from A to T at position 1067.
+The protein's natural variant, known as in CBAVD; unknown pathological significance;, features a modification of the amino acid from G to R at position 1069.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from R to P at position 1070.
+The protein's natural variant, known as in CF; decrease in bicarbonate transport; no effect on chloride channel activity;, features a modification of the amino acid from R to Q at position 1070.
+The protein's natural variant, known as in CBAVD;, features a modification of the amino acid from R to W at position 1070.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from Q to P at position 1071.
+The protein's natural variant, known as in CF, features a modification of the amino acid from P to L at position 1072.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from L to P at position 1077.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from H to R at position 1085.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from W to R at position 1098.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from M to K at position 1101.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from M to R at position 1101.
+The protein's natural variant, known as in CF; decreases channel activity; no visible effect on protein maturation;, features a modification of the amino acid from M to V at position 1137.
+The protein's natural variant, known as in CF and CBAVD; decreases channel activity; no visible effect on protein maturation;, features a modification of the amino acid from D to H at position 1152.
+The protein's natural variant, known as in CBAVD; unknown pathological significance;, features a modification of the amino acid from V to E at position 1153.
+The protein's natural variant, known as in CF; unknown pathological significance, features a modification of the amino acid from K to E at position 1200.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from I to V at position 1234.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from S to R at position 1235.
+The protein's natural variant, known as in CF; loss of bicarbonate transport; no effect on protein maturation, subcellular location at the plasma membrane, nor on chloride channel activity;, features a modification of the amino acid from G to E at position 1244.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from G to E at position 1249.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from S to N at position 1251.
+The protein's natural variant, known as in CF; loss of bicarbonate transport; no effect on protein maturation, subcellular location at the plasma membrane, nor on chloride channel activity;, features a modification of the amino acid from S to P at position 1255.
+The protein's natural variant, known as in CF and CBAVD;, features a modification of the amino acid from D to N at position 1270.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from W to R at position 1282.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from R to M at position 1283.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from F to S at position 1286.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from Q to H at position 1291.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from Q to R at position 1291.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from N to H at position 1303.
+The protein's natural variant, known as in CF; impaired maturation of glycan chains; has low in vitro channel activity at low temperature;, features a modification of the amino acid from N to K at position 1303.
+The protein's natural variant, known as in CF; loss of bicarbonate transport; no effect on protein maturation, subcellular location at the plasma membrane, nor on chloride channel activity;, features a modification of the amino acid from G to D at position 1349.
+The protein's natural variant, known as in CBAVD; unknown pathological significance;, features a modification of the amino acid from Q to H at position 1352.
+The protein's natural variant, known as in CBAVD;, features a modification of the amino acid from A to V at position 1364.
+The protein's natural variant, known as in CF;, features a modification of the amino acid from V to E at position 1397.
+The protein's natural variant, known as in strain: S 4074 / Serotype 1 and Isolate CVI 13261 / Serotype 9, features a modification of the amino acid from A to R at position 14.
+The protein's natural variant, known as in strain: S 4074 / Serotype 1 and Isolate CVI 13261 / Serotype 9, features a modification of the amino acid from G to D at position 94.
+The protein's natural variant, known as in strain: S 4074 / Serotype 1 and Isolate CVI 13261 / Serotype 9, features a modification of the amino acid from E to Q at position 113.
+The protein's natural variant, known as in strain: S 4074 / Serotype 1 and Isolate CVI 13261 / Serotype 9, features a modification of the amino acid from S to I at position 228.
+The protein's natural variant, known as in strain: S 4074 / Serotype 1 and Isolate CVI 13261 / Serotype 9, features a modification of the amino acid from Y to GT at position 335.
+The protein's natural variant, known as in IBGC6; phosphate efflux is impaired; present at the plasma membrane;, features a modification of the amino acid from S to N at position 136.
+The protein's natural variant, known as in IBGC6; phosphate efflux is impaired; present at the plasma membrane;, features a modification of the amino acid from L to P at position 140.
+The protein's natural variant, known as in IBGC6; dominant negative; phosphate efflux is impaired; loss of localization to the plasma membrane;, features a modification of the amino acid from L to P at position 145.
+The protein's natural variant, known as in IBGC6; phosphate efflux is impaired; present at the plasma membrane;, features a modification of the amino acid from L to S at position 218.
+The protein's natural variant, known as in IBGC6; phosphate efflux is decreased; present at the plasma membrane, features a modification of the amino acid from R to C at position 459.
+The protein's natural variant, known as in IBGC6; phosphate efflux is impaired; present at the plasma membrane, features a modification of the amino acid from N to D at position 619.
+The protein's natural variant, known as in IBGC6; phosphate efflux is decreased; present at the plasma membrane, features a modification of the amino acid from I to S at position 629.
+The protein's natural variant, known as decreased activation of transcription from PGF and C3 promoters;, features a modification of the amino acid from A to G at position 356.
+The protein's natural variant, known as increased activation of transcription from the C3 promoter but no effect on the PGF promoter;, features a modification of the amino acid from I to M at position 364.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 437.
+The natural variant of this protein is characterized by an amino acid alteration from A to S at position 442.
+The protein's natural variant, known as in strain: NOD, features a modification of the amino acid from K to R at position 7.
+The protein's natural variant, known as in strain: NOD, features a modification of the amino acid from K to R at position 71.
+The protein's natural variant, known as in strain: DSM 149, features a modification of the amino acid from V to I at position 31.
+The protein's natural variant, known as in BBS2, features a modification of the amino acid from R to P at position 23.
+The protein's natural variant, known as in RP74;, features a modification of the amino acid from A to D at position 33.
+The protein's natural variant, known as in BBS2; in linkage disequilibrium with V-123 in a Bedouin kindred;, features a modification of the amino acid from V to G at position 75.
+The protein's natural variant, known as in BBS2;, features a modification of the amino acid from G to C at position 81.
+The protein's natural variant, known as in BBS2 and RP74;, features a modification of the amino acid from D to A at position 104.
+The protein's natural variant, known as in BBS2, features a modification of the amino acid from L to R at position 125.
+The protein's natural variant, known as in RP74;, features a modification of the amino acid from P to R at position 134.
+The protein's natural variant, known as in BBS2, features a modification of the amino acid from A to P at position 136.
+The protein's natural variant, known as in BBS2;, features a modification of the amino acid from G to V at position 139.
+The protein's natural variant, known as in BBS2;, features a modification of the amino acid from D to E at position 174.
+The protein's natural variant, known as in BBS2, features a modification of the amino acid from C to W at position 307.
+The protein's natural variant, known as in BBS2;, features a modification of the amino acid from R to Q at position 315.
+The protein's natural variant, known as in BBS2;, features a modification of the amino acid from R to W at position 315.
+The protein's natural variant, known as in BBS2;, features a modification of the amino acid from Y to C at position 317.
+The protein's natural variant, known as in BBS2; has a modifier effect on BBS;, features a modification of the amino acid from L to W at position 349.
+The protein's natural variant, known as in BBS2;, features a modification of the amino acid from T to I at position 558.
+The protein's natural variant, known as in a patient with Bardet-Biedl syndrome compound heterozygote for mutations in BBS10; uncertain pathological role;, features a modification of the amino acid from E to K at position 629.
+The protein's natural variant, known as in BBS2 and RP74;, features a modification of the amino acid from R to P at position 632.
+The protein's natural variant, known as in BBS2;, features a modification of the amino acid from R to H at position 643.
+The protein's natural variant, known as in strain: CCUC 7757 and LCDC 845, features a modification of the amino acid from S to P at position 26.
+The protein's natural variant, known as in strain: CCUC 7757, features a modification of the amino acid from S to R at position 36.
+The protein's natural variant, known as in strain: CCUC 7757 and LCDC 845, features a modification of the amino acid from T to V at position 60.
+The protein's natural variant, known as in strain: CCUC 7757 and LCDC 845, features a modification of the amino acid from G to S at position 96.
+The protein's natural variant, known as in strain: CCUC 7757 and LCDC 845, features a modification of the amino acid from T to I at position 103.
+The protein's natural variant, known as in strain: CCUC 7757 and LCDC 845, features a modification of the amino acid from EG to QS at position 137.
+The protein's natural variant, known as in strain: CCUG 7852, features a modification of the amino acid from P to A at position 140.
+The protein's natural variant, known as in strain: LCDC 845, features a modification of the amino acid from NAVAE to HAAAK at position 153.
+The protein's natural variant, known as in strain: CCUC 7757, features a modification of the amino acid from NAV to HAA at position 151.
+The protein's natural variant, known as in strain: LCDC 77-143, features a modification of the amino acid from A to R at position 150.
+The protein's natural variant, known as in strain: CCUC 7757 and LCDC 845, features a modification of the amino acid from ANP to ENA at position 165.
+The protein's natural variant, known as in strain: CCUC 7757 and LCDC 845, features a modification of the amino acid from GVG to NVD at position 173.
+The protein's natural variant, known as in strain: CCUC 7757, CCUG 7852, LCDC 80-111 and LCDC 845, features a modification of the amino acid from I to V at position 189.
+The protein's natural variant, known as in strain: CCUC 7757 and LCDC 845, features a modification of the amino acid from D to N at position 199.
+The protein's natural variant, known as in strain: CCUC 7757 and LCDC 845, features a modification of the amino acid from S to P at position 204.
+The protein's natural variant, known as in strain: CCUG 7852 and LCDC 80-111, features a modification of the amino acid from Q to K at position 214.
+The protein's natural variant, known as in strain: CCUC 7757 and LCDC 845, features a modification of the amino acid from I to V at position 231.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 341.
+The protein's natural variant, known as found in a patient with congenital cataract and developmental delay; unknown pathological significance;, features a modification of the amino acid from E to G at position 41.
+The natural variant of this protein is characterized by an amino acid alteration from K to Q at position 31.
+The natural variant of this protein is characterized by an amino acid alteration from K to R at position 31.
+The natural variant of this protein is characterized by an amino acid alteration from K to T at position 5.
+The natural variant of this protein is characterized by an amino acid alteration from I to T at position 31.
+The natural variant of this protein is characterized by an amino acid alteration from D to A at position 16.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from G to S at position 202.
+The protein's natural variant, known as in LEMSPAD; unknown pathological significance; mildly reduced phosphorylation of eukaryotic translation initiation factor 2-alpha;, features a modification of the amino acid from I to V at position 448.
+The protein's natural variant, known as in ARVD10;, features a modification of the amino acid from R to Q at position 46.
+The protein's natural variant, known as in ARVD10;, features a modification of the amino acid from R to H at position 49.
+The protein's natural variant, known as associated with CMD1BB and ARVD10 although it may not be sufficient by itself to result in cardiomyopathy;, features a modification of the amino acid from V to M at position 56.
+The protein's natural variant, known as in ARVD10;, features a modification of the amino acid from T to A at position 335.
+The protein's natural variant, known as in ARVD10;, features a modification of the amino acid from C to Y at position 507.
+The protein's natural variant, known as in ARVD10;, features a modification of the amino acid from G to C at position 812.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from D to N at position 177.
+The protein's natural variant, known as in RP18;, features a modification of the amino acid from P to S at position 493.
+The protein's natural variant, known as in RP18; reduces phosphorylation; impairs binding to PRPF4; impairs self-association; affects interaction with the U4/U5/U6 tri-snRNP complex; does not affect global pre-mRNA splicing;, features a modification of the amino acid from T to M at position 494.
+The protein's natural variant, known as in Kilifi; at homozygosity it is associated with increased susceptibility to cerebral malaria;, features a modification of the amino acid from K to M at position 56.
+The protein's natural variant, known as in OOMD13; unknown pathological significance, features a modification of the amino acid from S to A at position 308.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from Q to R at position 457.
+The protein's natural variant, known as in XLID106; decreased protein abundance; reduced protein stability;, features a modification of the amino acid from L to F at position 254.
+The protein's natural variant, known as in XLID106; decreased protein abundance; decreased enzyme activity; reduced protein stability;, features a modification of the amino acid from R to P at position 284.
+The protein's natural variant, known as in XLID106; unknown pathological significance;, features a modification of the amino acid from A to T at position 319.
+The protein's natural variant, known as found in a renal cell carcinoma sample; somatic mutation, features a modification of the amino acid from L to P at position 538.
+The natural variant of this protein is characterized by an amino acid alteration from P to L at position 42.
+The natural variant of this protein is characterized by an amino acid alteration from Q to R at position 63.
+The protein's natural variant, known as in LS; unknown pathological significance; decrease in enzyme activity and impaired assembly of complex I;, features a modification of the amino acid from L to P at position 71.
+The natural variant of this protein is characterized by an amino acid alteration from S to P at position 148.
+The protein's natural variant, known as in LHON; secondary mutation; does not seem to directly cause the disease;, features a modification of the amino acid from N to D at position 150.
+The natural variant of this protein is characterized by an amino acid alteration from I to T at position 159.
+The natural variant of this protein is characterized by an amino acid alteration from T to A at position 185.
+The protein's natural variant, known as in LHON; rare primary mutation;, features a modification of the amino acid from G to S at position 259.
+The protein's natural variant, known as in AD-MT, features a modification of the amino acid from A to S at position 331.
+The protein's natural variant, known as in LCA14; loss of function;, features a modification of the amino acid from S to R at position 175.
+The protein's natural variant, known as in ARCI4A; skin phenotype consistent with non-bullous congenital ichthyosiform erythroderma;, features a modification of the amino acid from T to P at position 345.
+The protein's natural variant, known as in ARCI4B;, features a modification of the amino acid from S to N at position 387.
+The protein's natural variant, known as in a pancreatic ductal adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from A to V at position 476.
+The protein's natural variant, known as in ARCI4A; skin phenotype consistent with non-bullous congenital ichthyosiform erythroderma, features a modification of the amino acid from G to D at position 1136.
+The protein's natural variant, known as in ARCI4B;, features a modification of the amino acid from G to R at position 1179.
+The protein's natural variant, known as in ARCI4A; skin phenotype consistent with non-bullous congenital ichthyosiform erythroderma, features a modification of the amino acid from W to S at position 1235.
+The protein's natural variant, known as in ARCI4A;, features a modification of the amino acid from N to S at position 1380.
+The protein's natural variant, known as in ARCI4A;, features a modification of the amino acid from G to E at position 1381.
+The protein's natural variant, known as in ARCI4A; skin phenotype consistent with non-bullous congenital ichthyosiform erythroderma;, features a modification of the amino acid from I to T at position 1494.
+The protein's natural variant, known as in ARCI4A;, features a modification of the amino acid from R to H at position 1514.
+The protein's natural variant, known as in ARCI4A;, features a modification of the amino acid from E to K at position 1539.
+The protein's natural variant, known as in ARCI4A; skin phenotype consistent with non-bullous congenital ichthyosiform erythroderma;, features a modification of the amino acid from G to V at position 1559.
+The protein's natural variant, known as in ARCI4A;, features a modification of the amino acid from G to S at position 1651.
+The protein's natural variant, known as in ARCI4A; skin phenotype consistent with non-bullous congenital ichthyosiform erythroderma;, features a modification of the amino acid from P to L at position 1798.
+The protein's natural variant, known as in ARCI4A; skin phenotype consistent with non-bullous congenital ichthyosiform erythroderma;, features a modification of the amino acid from T to K at position 1980.
+The protein's natural variant, known as in P2, features a modification of the amino acid from I to M at position 384.
+The protein's natural variant, known as in strain: Berkeley and bIf, features a modification of the amino acid from V to L at position 286.
+The protein's natural variant, known as in strain: Berkeley, bIf and Apxo, features a modification of the amino acid from I to T at position 311.
+The protein's natural variant, known as in strain: Berkeley, bIf and Apxo, features a modification of the amino acid from T to A at position 333.
+The protein's natural variant, known as in strain: Berkeley, bIf and Apxo, features a modification of the amino acid from Q to E at position 338.
+The protein's natural variant, known as in strain: Berkeley and bIf, features a modification of the amino acid from K to N at position 340.
+The protein's natural variant, known as in strain: Berkeley, bIf and Apxo, features a modification of the amino acid from I to V at position 489.
+The protein's natural variant, known as in strain: G-77/a, G-77/b and G-79, features a modification of the amino acid from R to K at position 25.
+The protein's natural variant, known as in strain: G-77/a, G-77/b and G-79, features a modification of the amino acid from A to E at position 35.
+The protein's natural variant, known as in allele b, features a modification of the amino acid from A to T at position 39.
+The protein's natural variant, known as in allele b, features a modification of the amino acid from S to G at position 42.
+The protein's natural variant, known as in strain: G-77/a, G-77/b and G-79, features a modification of the amino acid from E to D at position 45.
+The protein's natural variant, known as in strain: G-77/a, G-77/b and G-79, features a modification of the amino acid from M to L at position 75.
+The protein's natural variant, known as in strain: G-77/a, G-77/b and G-79, features a modification of the amino acid from L to M at position 78.
+The protein's natural variant, known as in allele b, features a modification of the amino acid from M to I at position 95.
+The protein's natural variant, known as in strain: G-77/a, G-77/b and G-79, features a modification of the amino acid from A to T at position 105.
+The protein's natural variant, known as in strain: G-77/a, G-77/b and G-79, features a modification of the amino acid from Q to E at position 106.
+The protein's natural variant, known as in allele b, features a modification of the amino acid from A to T at position 117.
+The protein's natural variant, known as in allele b, features a modification of the amino acid from V to A at position 136.
+The protein's natural variant, known as in allele b, features a modification of the amino acid from V to I at position 139.
+The protein's natural variant, known as in allele b, features a modification of the amino acid from E to K at position 151.
+The protein's natural variant, known as in allele b, features a modification of the amino acid from G to A at position 152.
+The protein's natural variant, known as confirmed at protein level;, features a modification of the amino acid from C to Y at position 89.
+The protein's natural variant, known as in CILD23; no effect on subcellular location, markedly reduced ciliary beat frequency and amplitude or complete immotility in most, but not all, respiratory cilia;, features a modification of the amino acid from L to W at position 927.
+The protein's natural variant, known as in VBU; affects the regulation of mast cells degranulation; results in increased vibration-induced mast cells degranulation; no effect on localization to plasma membrane;, features a modification of the amino acid from C to Y at position 492.
+The protein's natural variant, known as in CPVT2; reduces calcium-dependent dimerization;, features a modification of the amino acid from R to Q at position 33.
+The protein's natural variant, known as no effect on calcium-binding and calcium-dependent dimerization;, features a modification of the amino acid from T to A at position 66.
+The protein's natural variant, known as increases dimerization in the absence of calcium;, features a modification of the amino acid from V to M at position 76.
+The protein's natural variant, known as in CPVT2; alters protein folding; reduces calcium-binding; reduces calcium-dependent oligomerization; decreases sarcoplasmic reticulum Ca(2+) storing capacity; reduces the amplitude of I(Ca)-induced Ca(2+) transients; reduces spontaneous Ca(2+) sparks in permeabilized myocytes;, features a modification of the amino acid from L to H at position 167.
+The protein's natural variant, known as in CPVT2;, features a modification of the amino acid from K to R at position 180.
+The protein's natural variant, known as in CPVT2; reduces calcium-binding; impairs calcium-dependent oligomerization; causes 50% decrease in calcium-dependent binding to TRDN; causes 50% decrease in calcium-dependent binding to ASPH;, features a modification of the amino acid from D to H at position 307.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from E to Q at position 132.
+The protein's natural variant, known as in strain: biovar 1, features a modification of the amino acid from I to T at position 55.
+The protein's natural variant, known as in IMD30;, features a modification of the amino acid from R to W at position 213.
+The protein's natural variant, known as in DA1B; may affect splicing;, features a modification of the amino acid from E to K at position 161.
+The protein's natural variant, known as in DA1B;, features a modification of the amino acid from W to R at position 211.
+The protein's natural variant, known as in MYOTREM; changes in electrostatic interactions resulting in increased myosin binding; no effect on actin binding;, features a modification of the amino acid from Y to H at position 222.
+The protein's natural variant, known as in MYOTREM; changes in electrostatic interactions resulting in increased myosin binding; no effect on actin binding;, features a modification of the amino acid from E to K at position 223.
+The protein's natural variant, known as in MYOTREM; no effects on myosin or actin binding; reduced helicity of certain domains;, features a modification of the amino acid from L to P at position 234.
+The protein's natural variant, known as in MYOTREM; decreased binding to myosin; no effect on actin binding;, features a modification of the amino acid from L to R at position 238.
+The protein's natural variant, known as in DA1B;, features a modification of the amino acid from Y to H at position 849.
+The protein's natural variant, known as in strain: B1, TD04/1a and TD04/1b, features a modification of the amino acid from T to S at position 96.
+The protein's natural variant, known as in strain: TD04/1a and TD04/1b, features a modification of the amino acid from V to I at position 175.
+The protein's natural variant, known as in strain: TD04/1b, features a modification of the amino acid from Q to QAATTTASVSTKSSAAAVSQIGDGQIQATTKTTAAAVSQIGDGQIQ at position 176.
+The protein's natural variant, known as in strain: B1, TD04/1a and TD04/1b, features a modification of the amino acid from V to I at position 199.
+The protein's natural variant, known as in strain: B1, TD04/1a and TD04/1b, features a modification of the amino acid from T to S at position 297.
+The natural variant of this protein is characterized by an amino acid alteration from L to R at position 7.
+The natural variant of this protein is characterized by an amino acid alteration from F to L at position 10.
+The natural variant of this protein is characterized by an amino acid alteration from L to W at position 13.
+The natural variant of this protein is characterized by an amino acid alteration from Y to N at position 87.
+The natural variant of this protein is characterized by an amino acid alteration from Y to S at position 215.
+The natural variant of this protein is characterized by an amino acid alteration from F to S at position 298.
+The protein's natural variant, known as in CFTD;, features a modification of the amino acid from A to V at position 4.
+The protein's natural variant, known as in NEM1; decrease in the sensitivity of contraction to activating calcium;, features a modification of the amino acid from M to R at position 9.
+The protein's natural variant, known as in NEM1 and CAPM1, features a modification of the amino acid from S to F at position 88.
+The protein's natural variant, known as probable disease-associated variant found in patients with undefined congenital myopathy;, features a modification of the amino acid from R to C at position 91.
+The protein's natural variant, known as in CFTD;, features a modification of the amino acid from R to P at position 91.
+The protein's natural variant, known as in CFTD;, features a modification of the amino acid from L to M at position 100.
+The protein's natural variant, known as in CFTD;, features a modification of the amino acid from L to V at position 100.
+The protein's natural variant, known as in CAPM1, features a modification of the amino acid from L to I at position 149.
+The protein's natural variant, known as in CAPM1, features a modification of the amino acid from E to A at position 151.
+The protein's natural variant, known as in CFTD, CAPM1 and NEM1; also found in patients with undefined congenital myopathy;, features a modification of the amino acid from R to C at position 168.
+The protein's natural variant, known as in CFTD;, features a modification of the amino acid from R to G at position 168.
+The protein's natural variant, known as in NEM1, CAPM1 and CFTD; also found in patients with undefined congenital myopathy;, features a modification of the amino acid from R to H at position 168.
+The protein's natural variant, known as in CFTD;, features a modification of the amino acid from K to E at position 169.
+The protein's natural variant, known as in CFTD;, features a modification of the amino acid from E to A at position 174.
+The protein's natural variant, known as in CFTD;, features a modification of the amino acid from E to K at position 241.
+The protein's natural variant, known as in CFTD;, features a modification of the amino acid from R to G at position 245.
+The protein's natural variant, known as in CAPM1;, features a modification of the amino acid from R to I at position 245.
+The protein's natural variant, known as probable disease-associated variant found in patients with undefined congenital myopathy;, features a modification of the amino acid from T to K at position 253.
+The protein's natural variant, known as in allele ALDH2*3;, features a modification of the amino acid from E to K at position 496.
+The protein's natural variant, known as in AMEDS; allele ALDH2*2; drastic reduction of enzyme activity;, features a modification of the amino acid from E to K at position 504.
+The protein's natural variant, known as in strain: 910-L8, 910-16, 976-L5, 976-L14, 1054-S11 and PCOLVCA7V, features a modification of the amino acid from A to I at position 47.
+The protein's natural variant, known as in strain: VP102-10A, features a modification of the amino acid from LRNM to HVKTKADVWKPSRVGYTDIFSQEYKGIVVAIKFVICSDAEGTLYPREYNSRLHDIKRLGRTGLSFTDKKEAYLLEFKNQDVVDHVHKLILPFNTSWQSN at position 745.
+The protein's natural variant, known as in ATITHS; decreased transcriptional activity shown in a luciferase assay;, features a modification of the amino acid from Q to R at position 306.
+The protein's natural variant, known as in strain: PAK, features a modification of the amino acid from V to L at position 26.
+The protein's natural variant, known as in strain: PAK, features a modification of the amino acid from A to T at position 30.
+The protein's natural variant, known as in strain: PAK, features a modification of the amino acid from S to N at position 46.
+The protein's natural variant, known as in strain: PAK, features a modification of the amino acid from K to R at position 74.
+The protein's natural variant, known as in strain: PAK, features a modification of the amino acid from P to A at position 109.
+The protein's natural variant, known as in strain: PAK, features a modification of the amino acid from S to N at position 146.
+The protein's natural variant, known as in strain: PAK, features a modification of the amino acid from IGSADKST to VGVKETSG at position 171.
+The protein's natural variant, known as in strain: PAK, features a modification of the amino acid from AS to TG at position 176.
+The protein's natural variant, known as in strain: PAK, features a modification of the amino acid from E to D at position 467.
+The protein's natural variant, known as in strain: PAK, features a modification of the amino acid from R to K at position 470.
+The protein's natural variant, known as in strain: PAK, features a modification of the amino acid from DK to EL at position 482.
+The protein's natural variant, known as does not affect lipoxygenase activity;, features a modification of the amino acid from D to H at position 134.
+The protein's natural variant, known as does not affect lipoxygenase activity;, features a modification of the amino acid from E to K at position 259.
+The protein's natural variant, known as does not affect lipoxygenase activity;, features a modification of the amino acid from Q to R at position 261.
+The natural variant of this protein is characterized by an amino acid alteration from A to T at position 298.
+The protein's natural variant, known as does not affect lipoxygenase activity;, features a modification of the amino acid from N to S at position 322.
+The protein's natural variant, known as in DFNA68;, features a modification of the amino acid from R to P at position 196.
+The protein's natural variant, known as in allele SAA1.2, SAA1.3, SAA1.4 and SAA1.5, features a modification of the amino acid from V to A at position 70.
+The protein's natural variant, known as in allele SAA1.2, SAA1.4 and SAA1.5, features a modification of the amino acid from A to V at position 75.
+The protein's natural variant, known as in allele SAA1.4;, features a modification of the amino acid from D to N at position 78.
+The protein's natural variant, known as in allele SAA1.2;, features a modification of the amino acid from G to D at position 90.
+The protein's natural variant, known as found in patients with very early onset inflammatory bowel disease; increases NOS2 activity;, features a modification of the amino acid from S to L at position 608.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from A to S at position 679.
+The protein's natural variant, known as in strain: M26, features a modification of the amino acid from V to A at position 8.
+The protein's natural variant, known as in strain: B226 and B316, features a modification of the amino acid from A to P at position 11.
+The protein's natural variant, known as in strain: MJ3, features a modification of the amino acid from L to V at position 14.
+The protein's natural variant, known as in strain: B316, features a modification of the amino acid from Q to E at position 20.
+The protein's natural variant, known as in strain: M40, features a modification of the amino acid from I to IFT at position 45.
+The protein's natural variant, known as in strain: MJ1, features a modification of the amino acid from I to V at position 45.
+The protein's natural variant, known as in strain: MJ1, features a modification of the amino acid from N to D at position 56.
+The protein's natural variant, known as in strain: Z24, features a modification of the amino acid from A to G at position 61.
+The protein's natural variant, known as in strain: ATCC 19435, features a modification of the amino acid from E to D at position 703.
+The protein's natural variant, known as in MRD42; unknown pathological significance; no effect on protein abundance; no effect on complex formation with gamma subunit; no effect on trimer formation with alpha and gamma subunits; no effect on receptor-driven G protein activation;, features a modification of the amino acid from L to F at position 30.
+The protein's natural variant, known as in MRD42; decreases receptor-driven G protein activation; no effect on protein abundance; no effect on complex formation with gamma subunit; decreases trimer formation with alpha and gamma subunit, features a modification of the amino acid from R to G at position 52.
+The protein's natural variant, known as in MRD42; decreases receptor-driven G protein activation; decreases protein abundance; decreases complex formation with gamma subunit; decreases trimer formation with alpha and gamma subunit, features a modification of the amino acid from G to V at position 64.
+The protein's natural variant, known as in MRD42;, features a modification of the amino acid from D to E at position 76.
+The protein's natural variant, known as in MRD42;, features a modification of the amino acid from D to G at position 76.
+The protein's natural variant, known as in MRD42;, features a modification of the amino acid from G to S at position 77.
+The protein's natural variant, known as in MRD42;, features a modification of the amino acid from K to R at position 78.
+The protein's natural variant, known as in MRD42; also found in patients with acute lymphoblastic T-cell leukemia; reduces interaction with GNAI2, GNAI3, GNA13 and GNA11; induces activation of PI3K-AKT-mTOR and MAPK pathways;, features a modification of the amino acid from I to N at position 80.
+The protein's natural variant, known as in MRD42; also found in patient with hematologic malignancies; reduces interaction with GNAI2, GNAI3, GNA13 and GNA11; induces activation of PI3K-AKT-mTOR and MAPK pathways;, features a modification of the amino acid from I to T at position 80.
+The protein's natural variant, known as in MRD42; unknown pathological significance; no effect on protein abundance; no effect on complex formation with gamma subunit; no effect on trimer formation with apha and gamma subunits; no effect on receptor-driven G protein activation, features a modification of the amino acid from H to R at position 91.
+The protein's natural variant, known as in MRD42; decreases receptor-driven G protein activation; increases trimer formation with alpha and gamma subunits; no effect on protein abundance; no effect on complex formation with gamma subunit, features a modification of the amino acid from A to T at position 92.
+The protein's natural variant, known as in MRD42; decreases receptor-driven G protein activation; decreases trimer formation with alpha and gamma subunit; no effect on protein abundance;no effect on complex formation with gamma subunit, features a modification of the amino acid from P to S at position 94.
+The protein's natural variant, known as in MRD42;, features a modification of the amino acid from L to P at position 95.
+The protein's natural variant, known as in MRD42; decreases receptor-driven G protein activation; decreases trimer formation with alpha and gamma subunit; no effect on protein abundance; no effect on complex formation with gamma subunit, features a modification of the amino acid from R to L at position 96.
+The protein's natural variant, known as in MRD42;, features a modification of the amino acid from M to V at position 101.
+The protein's natural variant, known as in MRD42; decreases receptor-driven G protein activation; decreases complex formation with gamma subunit; decreases trimer formation with alpha and gamma subunit; no effect on protein abundance, features a modification of the amino acid from A to T at position 106.
+The protein's natural variant, known as in MRD42; decreases receptor-driven G protein activation; no effect on protein abundance; no effect on complex formation with gamma subunit; no effect on trimer formation with alpha and gamma subunits;, features a modification of the amino acid from D to G at position 118.
+The protein's natural variant, known as in MRD42;, features a modification of the amino acid from A to T at position 326.
+The protein's natural variant, known as in MRD42; unknown pathological significance; no effect on protein abundance; no effect on complex formation with gamma subunit; no effect on trimer formation with alpha and gamma subunits; no effect on receptor-driven G protein activation, features a modification of the amino acid from K to Q at position 337.
+The natural variant of this protein is characterized by an amino acid alteration from S to I at position 6.
+The natural variant of this protein is characterized by an amino acid alteration from T to P at position 26.
+The natural variant of this protein is characterized by an amino acid alteration from H to R at position 31.
+The natural variant of this protein is characterized by an amino acid alteration from F to L at position 70.
+The natural variant of this protein is characterized by an amino acid alteration from L to S at position 149.
+The protein's natural variant, known as in ORTHYP2;, features a modification of the amino acid from G to R at position 88.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from R to T at position 887.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from T to A at position 339.
+The protein's natural variant, known as in a glioblastoma cell line, features a modification of the amino acid from V to A at position 455.
+The protein's natural variant, known as in a sarcoma cell line, features a modification of the amino acid from R to G at position 518.
+The protein's natural variant, known as in a neuroblastoma cell line, features a modification of the amino acid from T to I at position 568.
+The protein's natural variant, known as in a glioblastoma cell line, features a modification of the amino acid from A to V at position 651.
+The protein's natural variant, known as in a glioblastoma cell line, features a modification of the amino acid from E to V at position 767.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from D to Y at position 816.
+The protein's natural variant, known as in a glioblastoma cell line, features a modification of the amino acid from N to D at position 939.
+The protein's natural variant, known as in a sarcoma cell line, features a modification of the amino acid from V to M at position 947.
+The protein's natural variant, known as in a glioblastoma cell line, features a modification of the amino acid from S to P at position 1022.
+The protein's natural variant, known as in AOS4;, features a modification of the amino acid from W to S at position 207.
+The protein's natural variant, known as in AOS4;, features a modification of the amino acid from R to Q at position 377.
+The protein's natural variant, known as associated with less backfat thickness, slower growth rate and lower feed intake, features a modification of the amino acid from D to N at position 298.
+The protein's natural variant, known as in AHUS2;, features a modification of the amino acid from C to Y at position 35.
+The protein's natural variant, known as in AHUS2; reduced cell surface expression;, features a modification of the amino acid from P to S at position 165.
+The protein's natural variant, known as in AHUS2, features a modification of the amino acid from W to C at position 216.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from C to Y at position 228.
+The protein's natural variant, known as in AHUS2;, features a modification of the amino acid from P to R at position 231.
+The protein's natural variant, known as in AHUS2; no change in cell surface expression but reduced activity;, features a modification of the amino acid from S to P at position 240.
+The natural variant of this protein is characterized by an amino acid alteration from V to G at position 355.
+The protein's natural variant, known as in CORLK; decreased activity; decreased sensitivity to allosteric inhibition by AMP; decreased thermal stability, features a modification of the amino acid from V to M at position 115.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to C at position 133.
+The natural variant of this protein is characterized by an amino acid alteration from D to N at position 379.
+The protein's natural variant, known as in XLID63;, features a modification of the amino acid from R to S at position 570.
+The protein's natural variant, known as in a bladder transitional cell carcinoma sample; somatic mutation, features a modification of the amino acid from S to P at position 400.
+The natural variant of this protein is characterized by an amino acid alteration from E to K at position 1161.
+The protein's natural variant, known as in EHK;, features a modification of the amino acid from M to R at position 150.
+The protein's natural variant, known as in EHK; also found in a patient with hyperkeratotic epidermal nevi due to genetic mosaicism;, features a modification of the amino acid from M to T at position 150.
+The protein's natural variant, known as in EHK;, features a modification of the amino acid from N to H at position 154.
+The protein's natural variant, known as in EHK;, features a modification of the amino acid from R to C at position 156.
+The protein's natural variant, known as in EHK;, features a modification of the amino acid from R to H at position 156.
+The protein's natural variant, known as in EHK;, features a modification of the amino acid from R to P at position 156.
+The protein's natural variant, known as in EHK;, features a modification of the amino acid from R to S at position 156.
+The protein's natural variant, known as in EHK; severe phenotype;, features a modification of the amino acid from Y to D at position 160.
+The protein's natural variant, known as in EHK; severe phenotype, features a modification of the amino acid from Y to N at position 160.
+The protein's natural variant, known as in EHK; severe phenotype;, features a modification of the amino acid from Y to S at position 160.
+The protein's natural variant, known as in EHK;, features a modification of the amino acid from L to S at position 161.
+The protein's natural variant, known as in AEI1; requires 2 nucleotide substitutions;, features a modification of the amino acid from R to E at position 422.
+The protein's natural variant, known as in IHL; unknown pathological significance, features a modification of the amino acid from L to P at position 435.
+The protein's natural variant, known as in EHK; mild phenotype;, features a modification of the amino acid from K to E at position 439.
+The protein's natural variant, known as in EHK;, features a modification of the amino acid from L to Q at position 442.
+The protein's natural variant, known as in AEI1;, features a modification of the amino acid from I to T at position 446.
+The protein's natural variant, known as in EHK;, features a modification of the amino acid from Y to C at position 449.
+The protein's natural variant, known as in allele B, features a modification of the amino acid from R to G at position 162.
+The protein's natural variant, known as in allele B, features a modification of the amino acid from V to M at position 304.
+The protein's natural variant, known as in IBD28;, features a modification of the amino acid from W to R at position 69.
+The protein's natural variant, known as in IBD28;, features a modification of the amino acid from T to I at position 84.
+The protein's natural variant, known as in IBD28;, features a modification of the amino acid from Y to C at position 91.
+The protein's natural variant, known as in IBD28;, features a modification of the amino acid from R to W at position 101.
+The protein's natural variant, known as in IBD28;, features a modification of the amino acid from R to H at position 117.
+The protein's natural variant, known as in IBD28;, features a modification of the amino acid from G to R at position 141.
+The protein's natural variant, known as in IBD28;, features a modification of the amino acid from R to C at position 262.
+The protein's natural variant, known as in clone 284.4, features a modification of the amino acid from R to G at position 55.
+The protein's natural variant, known as in clone 334.8, features a modification of the amino acid from K to M at position 149.
+The protein's natural variant, known as in clone 334.8, features a modification of the amino acid from D to N at position 181.
+The protein's natural variant, known as in clone 334.8, features a modification of the amino acid from P to A at position 186.
+The protein's natural variant, known as in CGL1; reduced 1-acyl-sn-glycerol-3-phosphate acyltransferase activity;, features a modification of the amino acid from G to R at position 136.
+The protein's natural variant, known as in CGL1; reduced 1-acyl-sn-glycerol-3-phosphate acyltransferase activity;, features a modification of the amino acid from L to P at position 228.
+The protein's natural variant, known as in CGL1; 90% of wild-type 1-acyl-sn-glycerol-3-phosphate acyltransferase activity;, features a modification of the amino acid from A to V at position 239.
+The protein's natural variant, known as in the spontaneous pleiotropic mutant BL915-1, features a modification of the amino acid from P to L at position 90.
+The protein's natural variant, known as in the spontaneous pleiotropic mutant BL915-2, features a modification of the amino acid from T to I at position 182.
+The protein's natural variant, known as myocardial infarction susceptibility;, features a modification of the amino acid from K to N at position 167.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from R to L at position 275.
+The protein's natural variant, known as found in a renal cell carcinoma case; somatic mutation, features a modification of the amino acid from C to R at position 766.
+The natural variant of this protein is characterized by an amino acid alteration from M to I at position 27.
+The protein's natural variant, known as in BIBARS; inactive;, features a modification of the amino acid from G to R at position 236.
+The protein's natural variant, known as in BIBARS, features a modification of the amino acid from A to D at position 237.
+The protein's natural variant, known as in TCMGLY;, features a modification of the amino acid from Y to H at position 174.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from L to V at position 6.
+The protein's natural variant, known as in albino mice, features a modification of the amino acid from C to S at position 103.
+The protein's natural variant, known as in strain: Himalayan, features a modification of the amino acid from H to R at position 420.
+The protein's natural variant, known as in chinchilla mice, features a modification of the amino acid from A to T at position 482.
+The protein's natural variant, known as in OS;, features a modification of the amino acid from C to W at position 41.
+The protein's natural variant, known as in CHIDG; reduced recombination activity;, features a modification of the amino acid from T to N at position 77.
+The protein's natural variant, known as in T(-)B(-)NK(+) SCID;, features a modification of the amino acid from R to Q at position 229.
+The protein's natural variant, known as in OS;, features a modification of the amino acid from M to R at position 285.
+The protein's natural variant, known as in CHIDG; reduced recombination activity;, features a modification of the amino acid from G to A at position 451.
+The protein's natural variant, known as in T(-)B(-)NK(+) SCID;, features a modification of the amino acid from C to Y at position 478.
+The protein's natural variant, known as in ADMIO2; decreases interaction with phosphorylated CD247; decreases ZAP70 phosphorylation; no effect on subcellular localization of CD69 at the cell surface;, features a modification of the amino acid from R to W at position 192.
+The protein's natural variant, known as in IMD48;, features a modification of the amino acid from L to R at position 337.
+The protein's natural variant, known as in ADMIO2; no effect on interaction with phosphorylated CD247; increases TCR-induced Y-319 and Y-493 phosphorylation of ZAP70 and phosphorylation of LAT and LCP2; increases subcellular localization of CD69 at the cell surface; weakly decreases autoinhibition conformation;, features a modification of the amino acid from R to P at position 360.
+The protein's natural variant, known as in a head and neck squamous cell carcinoma sample; somatic mutation, features a modification of the amino acid from G to E at position 448.
+The protein's natural variant, known as in IMD48;, features a modification of the amino acid from R to C at position 465.
+The protein's natural variant, known as in IMD48;, features a modification of the amino acid from R to H at position 465.
+The protein's natural variant, known as in IMD48, features a modification of the amino acid from A to V at position 507.
+The protein's natural variant, known as in IMD48;, features a modification of the amino acid from S to R at position 518.
+The protein's natural variant, known as in IMD48, features a modification of the amino acid from K to KLEQ at position 541.
+The protein's natural variant, known as in IMD48, features a modification of the amino acid from C to R at position 564.
+The protein's natural variant, known as in CMH4;, features a modification of the amino acid from G to R at position 5.
+The protein's natural variant, known as in CMH4;, features a modification of the amino acid from T to A at position 59.
+The protein's natural variant, known as in CMH4;, features a modification of the amino acid from P to S at position 161.
+The protein's natural variant, known as in CMH4;, features a modification of the amino acid from V to L at position 219.
+The protein's natural variant, known as in CMH4;, features a modification of the amino acid from D to N at position 228.
+The protein's natural variant, known as in CMH4;, features a modification of the amino acid from Y to S at position 237.
+The protein's natural variant, known as in CMH4;, features a modification of the amino acid from V to I at position 256.
+The protein's natural variant, known as in CMH4;, features a modification of the amino acid from H to P at position 257.
+The protein's natural variant, known as in CMH4;, features a modification of the amino acid from E to K at position 258.
+The protein's natural variant, known as in CMH4;, features a modification of the amino acid from G to R at position 263.
+The protein's natural variant, known as in CMH4; unknown pathological significance;, features a modification of the amino acid from R to C at position 272.
+The protein's natural variant, known as in CMH4; unknown pathological significance;, features a modification of the amino acid from R to H at position 273.
+The protein's natural variant, known as in CMH4; benign variant;, features a modification of the amino acid from G to E at position 278.
+The protein's natural variant, known as in CMH4; unknown pathological significance;, features a modification of the amino acid from G to A at position 279.
+The protein's natural variant, known as in CMH4;, features a modification of the amino acid from R to W at position 282.
+The protein's natural variant, known as in CMH4; also found in a patient with RCM; decreases protein abundance; increases polyubiquitination level; accelerates the degradation process; no effect on phosphorylation; decreases endopeptidase activity; increases apoptotic process;, features a modification of the amino acid from E to K at position 334.
+The protein's natural variant, known as in CMH4, features a modification of the amino acid from I to V at position 336.
+The protein's natural variant, known as in CMH4;, features a modification of the amino acid from V to D at position 342.
+The protein's natural variant, known as in CMH4;, features a modification of the amino acid from L to P at position 352.
+The protein's natural variant, known as in CMH4, features a modification of the amino acid from A to S at position 417.
+The protein's natural variant, known as in CMH4;, features a modification of the amino acid from E to Q at position 451.
+The protein's natural variant, known as in CMH4;, features a modification of the amino acid from R to H at position 458.
+The protein's natural variant, known as in CMH4, CMD1MM and LVNC10;, features a modification of the amino acid from G to R at position 490.
+The protein's natural variant, known as in CMH4;, features a modification of the amino acid from G to V at position 490.
+The protein's natural variant, known as in CMH4;, features a modification of the amino acid from R to G at position 495.
+The protein's natural variant, known as in CMH4;, features a modification of the amino acid from R to Q at position 495.
+The protein's natural variant, known as in CMH4;, features a modification of the amino acid from R to Q at position 502.
+The protein's natural variant, known as in CMH4;, features a modification of the amino acid from R to W at position 502.
+The protein's natural variant, known as in CMH4;, features a modification of the amino acid from G to R at position 507.
+The protein's natural variant, known as in CMH4;, features a modification of the amino acid from G to W at position 523.
+The protein's natural variant, known as in CMH4;, features a modification of the amino acid from E to Q at position 542.
+The protein's natural variant, known as in CMH4;, features a modification of the amino acid from A to V at position 562.
+The protein's natural variant, known as in CMH4;, features a modification of the amino acid from C to R at position 566.
+The protein's natural variant, known as in CMH4;, features a modification of the amino acid from D to V at position 604.
+The protein's natural variant, known as in CMH4; unknown pathological significance;, features a modification of the amino acid from D to N at position 605.
+The protein's natural variant, known as in CMH4;, features a modification of the amino acid from P to L at position 608.
+The protein's natural variant, known as in CMH4;, features a modification of the amino acid from A to V at position 627.
+The protein's natural variant, known as in CMH4; unknown pathological significance; as well folded and stable as the wild-type;, features a modification of the amino acid from R to H at position 654.
+The protein's natural variant, known as in CMH4;, features a modification of the amino acid from R to H at position 668.
+The protein's natural variant, known as in CMH4;, features a modification of the amino acid from R to P at position 668.
+The protein's natural variant, known as in CMH4, features a modification of the amino acid from L to H at position 669.
+The protein's natural variant, known as in CMH4; unknown pathological significance;, features a modification of the amino acid from R to C at position 733.
+The protein's natural variant, known as in CMH4; destabilizes the structure of Ig-like C2-type domain 5;, features a modification of the amino acid from N to K at position 755.
+The protein's natural variant, known as in CMH4;, features a modification of the amino acid from E to D at position 759.
+The protein's natural variant, known as in CMH4;, features a modification of the amino acid from D to N at position 770.
+The protein's natural variant, known as in CMH4;, features a modification of the amino acid from V to M at position 771.
+The protein's natural variant, known as in CMH4;, features a modification of the amino acid from W to R at position 792.
+The protein's natural variant, known as in CMH4;, features a modification of the amino acid from R to H at position 810.
+The protein's natural variant, known as in CMH4;, features a modification of the amino acid from K to R at position 811.
+The protein's natural variant, known as in CMH4;, features a modification of the amino acid from R to Q at position 820.
+The protein's natural variant, known as in CMH4 and CMD1MM;, features a modification of the amino acid from A to T at position 833.
+The protein's natural variant, known as in CMH4; benign variant;, features a modification of the amino acid from A to V at position 833.
+The protein's natural variant, known as in CMH4, features a modification of the amino acid from R to T at position 834.
+The protein's natural variant, known as in CMH4; unknown pathological significance;, features a modification of the amino acid from R to W at position 834.
+The protein's natural variant, known as in CMH4;, features a modification of the amino acid from P to H at position 873.
+The protein's natural variant, known as in LVNC10;, features a modification of the amino acid from P to L at position 873.
+The protein's natural variant, known as may act as a phenotype modifier in cardiomyopathy patients;, features a modification of the amino acid from V to M at position 896.
+The protein's natural variant, known as in CMH4;, features a modification of the amino acid from N to T at position 948.
+The protein's natural variant, known as in CMH4;, features a modification of the amino acid from T to S at position 957.
+The protein's natural variant, known as in CMH4;, features a modification of the amino acid from T to I at position 958.
+The protein's natural variant, known as in CMH4; no effect on protein abundance; no effect on endopeptidase activity;, features a modification of the amino acid from Q to E at position 998.
+The protein's natural variant, known as in CMH4;, features a modification of the amino acid from Q to R at position 998.
+The protein's natural variant, known as in CMH4;, features a modification of the amino acid from R to Q at position 1002.
+The protein's natural variant, known as in CMH4, features a modification of the amino acid from P to Q at position 1003.
+The protein's natural variant, known as in CMH4;, features a modification of the amino acid from T to S at position 1028.
+The protein's natural variant, known as in CMH4; no effect on protein abundance; no effect on endopeptidase activity;, features a modification of the amino acid from T to M at position 1046.
+The protein's natural variant, known as in CMH4;, features a modification of the amino acid from F to I at position 1113.
+The protein's natural variant, known as in CMH4;, features a modification of the amino acid from V to I at position 1115.
+The protein's natural variant, known as in CMH4; unknown pathological significance;, features a modification of the amino acid from I to T at position 1131.
+The protein's natural variant, known as in CMH4;, features a modification of the amino acid from A to T at position 1194.
+The protein's natural variant, known as in CMH4; unknown pathological significance;, features a modification of the amino acid from G to R at position 1248.
+The protein's natural variant, known as in CMH4;, features a modification of the amino acid from A to T at position 1255.
+The protein's natural variant, known as in CMD1MM;, features a modification of the amino acid from C to F at position 1264.
+The protein's natural variant, known as in JEB1A; somatic second-site mutation;, features a modification of the amino acid from G to A at position 199.
+The protein's natural variant, known as in JEB1A; somatic second-site mutation;, features a modification of the amino acid from K to Q at position 207.
+The protein's natural variant, known as in JEB1A;, features a modification of the amino acid from E to K at position 210.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to C at position 450.
+The protein's natural variant, known as in JEB1B;, features a modification of the amino acid from P to L at position 679.
+The protein's natural variant, known as in strain: ILS, features a modification of the amino acid from G to R at position 10.
+The protein's natural variant, known as increased sensitivity to strychnine, features a modification of the amino acid from E to G at position 194.
+The protein's natural variant, known as in CLN13;, features a modification of the amino acid from Y to C at position 231.
+The protein's natural variant, known as in CLN13;, features a modification of the amino acid from Q to R at position 321.
+The protein's natural variant, known as in CLN13;, features a modification of the amino acid from G to A at position 458.
+The protein's natural variant, known as in CLN13;, features a modification of the amino acid from S to L at position 480.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from A to D at position 429.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from Q to E at position 1008.
+The protein's natural variant, known as no loss of alanine--glyoxylate aminotransferase activity;, features a modification of the amino acid from T to N at position 9.
+The protein's natural variant, known as reduction of specific alanine--glyoxylate aminotransferase activity in vitro; causes mitochondrial mistargeting when associated with R-170;, features a modification of the amino acid from P to L at position 11.
+The protein's natural variant, known as in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in loss of alanine--glyoxylate aminotransferase activity;, features a modification of the amino acid from R to C at position 36.
+The protein's natural variant, known as in HP1; loss of alanine--glyoxylate aminotransferase activity;, features a modification of the amino acid from G to E at position 41.
+The protein's natural variant, known as in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in loss of protein stability; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; partial mitochondrial mistargeting; intraperoxisomal protein aggregation seen;, features a modification of the amino acid from G to R at position 41.
+The protein's natural variant, known as in HP1; reduced alanine--glyoxylate aminotransferase activity; no loss of dimerization; no effect on protein stability;, features a modification of the amino acid from G to V at position 41.
+The protein's natural variant, known as in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in protein misfolding; decreased alanine--glyoxylate aminotransferase activity; reduced expression levels; reduced pyridoxal phosphate binding; reduced dimerization; reduced thermostability; increased propensity to aggregation; increased susceptibility to proteolytic degradation within the N-terminal region; mitochondrial mistargeting; exposure to pyridoxine can rescue the functionality by partially preventing aggregation and degradation and by redirecting all the protein to the peroxisome;, features a modification of the amino acid from G to R at position 47.
+The protein's natural variant, known as in HP1; abolishes alanine--glyoxylate aminotransferase activity by interfering with pyridoxal phosphate binding;, features a modification of the amino acid from G to E at position 82.
+The protein's natural variant, known as in HP1;, features a modification of the amino acid from G to R at position 82.
+The protein's natural variant, known as in HP1, features a modification of the amino acid from E to EE at position 95.
+The protein's natural variant, known as in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability;, features a modification of the amino acid from W to R at position 108.
+The protein's natural variant, known as in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; causes protein aggregation;, features a modification of the amino acid from A to D at position 112.
+The protein's natural variant, known as in HP1;, features a modification of the amino acid from G to R at position 116.
+The protein's natural variant, known as in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in loss of alanine--glyoxylate aminotransferase activity;, features a modification of the amino acid from L to P at position 150.
+The protein's natural variant, known as in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in protein destabilization; decreased alanine--glyoxylate aminotransferase activity; no loss of dimerization; mitochondrial mistargeting;, features a modification of the amino acid from F to I at position 152.
+The protein's natural variant, known as in HP1;, features a modification of the amino acid from L to V at position 153.
+The protein's natural variant, known as in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability;, features a modification of the amino acid from G to R at position 156.
+The protein's natural variant, known as in HP1; loss of alanine--glyoxylate aminotransferase activity;, features a modification of the amino acid from S to L at position 158.
+The protein's natural variant, known as in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in loss of alanine--glyoxylate aminotransferase activity; reduced expression levels; decreased protein stability; protein aggregation seen in the cytosol with a decreased aggregation propensity in the presence of pyridoxal phosphate; reduced peroxisomal localization;, features a modification of the amino acid from G to C at position 161.
+The protein's natural variant, known as in HP1; loss of alanine--glyoxylate aminotransferase activity; reduced expression levels; decreased protein stability; protein aggregation seen in the cytosol with a decreased aggregation propensity in the presence of pyridoxal phosphate; loss of dimerization;, features a modification of the amino acid from G to R at position 161.
+The protein's natural variant, known as in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in loss of alanine--glyoxylate aminotransferase activity; reduced expression levels; decreased protein stability; protein aggregation seen in the cytosol with a decreased aggregation propensity in the presence of pyridoxal phosphate; reduced peroxisomal localization;, features a modification of the amino acid from G to S at position 161.
+The protein's natural variant, known as in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in loss of alanine--glyoxylate aminotransferase activity;, features a modification of the amino acid from L to P at position 166.
+The protein's natural variant, known as in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in mitochondrial mistargeting; slight decrease in alanine--glyoxylate aminotransferase activity; loss of dimerization; partial loss of protein stability but protein stability increases in the presence of pyridoxal phosphate; causes protein aggregation;, features a modification of the amino acid from G to R at position 170.
+The protein's natural variant, known as in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; causes protein aggregation;, features a modification of the amino acid from C to Y at position 173.
+The protein's natural variant, known as in HP1; loss of alanine--glyoxylate aminotransferase activity; no loss of dimerization; no effect on protein stability;, features a modification of the amino acid from D to N at position 183.
+The protein's natural variant, known as in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization but improved dimerization in the presence of pyridoxal phosphate; decreased protein stability;, features a modification of the amino acid from S to F at position 187.
+The protein's natural variant, known as in HP1;, features a modification of the amino acid from G to R at position 190.
+The protein's natural variant, known as in HP1;, features a modification of the amino acid from M to R at position 195.
+The protein's natural variant, known as in HP1;, features a modification of the amino acid from D to E at position 201.
+The protein's natural variant, known as in HP1; unknown pathological significance;, features a modification of the amino acid from I to N at position 202.
+The protein's natural variant, known as in HP1; loss of alanine--glyoxylate aminotransferase activity; decreased protein stability;, features a modification of the amino acid from S to P at position 205.
+The protein's natural variant, known as in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; no effect on protein stability;, features a modification of the amino acid from S to L at position 218.
+The protein's natural variant, known as in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in loss of alanine--glyoxylate aminotransferase activity;, features a modification of the amino acid from R to C at position 233.
+The protein's natural variant, known as in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in loss of alanine--glyoxylate aminotransferase activity;, features a modification of the amino acid from R to H at position 233.
+The protein's natural variant, known as in HP1;, features a modification of the amino acid from R to L at position 233.
+The protein's natural variant, known as in HP1;, features a modification of the amino acid from D to H at position 243.
+The protein's natural variant, known as in HP1; prevalent mutation in the Canary islands; when associated with L-11 and M-340 on the minor AGXT allele; results in protein misfolding; decreased alanine--glyoxylate aminotransferase activity; no loss of dimerization; partial mitochondrial mistargeting;, features a modification of the amino acid from I to T at position 244.
+The protein's natural variant, known as in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in loss of alanine--glyoxylate aminotransferase activity;, features a modification of the amino acid from C to R at position 253.
+The protein's natural variant, known as in HP1;, features a modification of the amino acid from I to M at position 279.
+The protein's natural variant, known as in HP1;, features a modification of the amino acid from S to T at position 287.
+The protein's natural variant, known as in HP1;, features a modification of the amino acid from R to C at position 289.
+The protein's natural variant, known as in HP1;, features a modification of the amino acid from L to P at position 298.
+The protein's natural variant, known as in HP1;, features a modification of the amino acid from V to D at position 336.
+The protein's natural variant, known as associated with hyperoxaluria;, features a modification of the amino acid from I to M at position 340.
+The protein's natural variant, known as in HP1;, features a modification of the amino acid from G to D at position 350.
+The protein's natural variant, known as in BPES; sporadic; nuclear and cytoplasmic aggregation; impaired transactivation activity, features a modification of the amino acid from S to L at position 58.
+The protein's natural variant, known as in BPES;, features a modification of the amino acid from I to T at position 63.
+The protein's natural variant, known as in BPES;, features a modification of the amino acid from M to V at position 65.
+The protein's natural variant, known as in BPES; nuclear and cytoplasmic aggregation; impaired transactivation activity, features a modification of the amino acid from A to V at position 66.
+The protein's natural variant, known as in BPES; sporadic; nuclear aggregation; normal transactivation activity;, features a modification of the amino acid from E to K at position 69.
+The protein's natural variant, known as in BPES; nuclear and cytoplasmic aggregation; impaired transactivation activity, features a modification of the amino acid from I to T at position 80.
+The protein's natural variant, known as in BPES; nuclear and cytoplasmic aggregation; impaired transactivation activity, features a modification of the amino acid from I to N at position 84.
+The protein's natural variant, known as in BPES; type I;, features a modification of the amino acid from I to S at position 84.
+The protein's natural variant, known as in BPES; nuclear and cytoplasmic aggregation; impaired transactivation activity, features a modification of the amino acid from F to S at position 90.
+The protein's natural variant, known as in BPES; nuclear and cytoplasmic aggregation; impaired transactivation activity, features a modification of the amino acid from W to G at position 98.
+The protein's natural variant, known as in BPES;, features a modification of the amino acid from W to R at position 98.
+The protein's natural variant, known as in BPES; nuclear aggregation; impaired transactivation activity;, features a modification of the amino acid from S to R at position 101.
+The protein's natural variant, known as in BPES; nuclear and cytoplasmic aggregation; impaired transactivation activity, features a modification of the amino acid from I to T at position 102.
+The protein's natural variant, known as in BPES; nuclear and cytoplasmic aggregation; normal transactivation activity, features a modification of the amino acid from R to C at position 103.
+The protein's natural variant, known as in BPES; diffuse nuclear localization as wild type; normal transactivation activity;, features a modification of the amino acid from H to R at position 104.
+The protein's natural variant, known as in BPES; type II, features a modification of the amino acid from N to S at position 105.
+The protein's natural variant, known as in BPES; sporadic; nuclear and cytoplasmic aggregation; impaired transactivation activity;, features a modification of the amino acid from L to F at position 106.
+The protein's natural variant, known as in BPES; nuclear and cytoplasmic aggregation; impaired transactivation activity, features a modification of the amino acid from L to P at position 106.
+The protein's natural variant, known as in BPES; nuclear aggregation and cytoplasmic mislocalization; impaired transactivation activity, features a modification of the amino acid from L to P at position 108.
+The protein's natural variant, known as in BPES; type II; diffuse nuclear localization as wild type; impaired transactivation activity, features a modification of the amino acid from N to K at position 109.
+The protein's natural variant, known as in granulosa-cell tumors of the ovary; not commonly found in other tumor types;, features a modification of the amino acid from C to W at position 134.
+The protein's natural variant, known as in POF3; does not affect nuclear localization; reduces transcriptional activation of OSR2;, features a modification of the amino acid from G to D at position 187.
+The protein's natural variant, known as in BPES; type II;, features a modification of the amino acid from K to R at position 193.
+The protein's natural variant, known as in BPES;, features a modification of the amino acid from Y to C at position 215.
+The protein's natural variant, known as in BPES; diffuse nuclear localization; normal transcriptional activation, features a modification of the amino acid from S to C at position 217.
+The protein's natural variant, known as in BPES; diffuse nuclear localization; increased transactivation activity;, features a modification of the amino acid from S to F at position 217.
+The protein's natural variant, known as in BPES; significant higher cytoplasmic retention compared to the wild-type protein, features a modification of the amino acid from A to AAAAAA at position 234.
+The protein's natural variant, known as in BPES; type II, features a modification of the amino acid from A to AAAAAAAAAAA at position 234.
+The protein's natural variant, known as in BPES, features a modification of the amino acid from A to AAAAAAAAAAAA at position 234.
+The protein's natural variant, known as in POF3;, features a modification of the amino acid from Y to N at position 258.
+The natural variant of this protein is characterized by an amino acid alteration from P to S at position 285.
+The protein's natural variant, known as in ASD8; demonstrates only about 75% of the repressive activity of wild-type, features a modification of the amino acid from S to GGSSTPGGS at position 179.
+The protein's natural variant, known as in IAD;, features a modification of the amino acid from S to F at position 128.
+The protein's natural variant, known as in Ty1-15, features a modification of the amino acid from N to I at position 12.
+The protein's natural variant, known as in Ty1-15, features a modification of the amino acid from PASVPP to TAQSHS at position 79.
+The protein's natural variant, known as in Ty1-15, features a modification of the amino acid from S to R at position 142.
+The protein's natural variant, known as in FANCW; abolishes interaction with the RPA complex and subsequent recruitment of the protein at DNA damage sites; decreased function in double-strand break repair via homologous recombination;, features a modification of the amino acid from I to K at position 639.
+The protein's natural variant, known as in allelic sequence, features a modification of the amino acid from A to T at position 77.
+The protein's natural variant, known as in strain: NRRL 13383 and NRRL 28439, features a modification of the amino acid from Q to K at position 54.
+The protein's natural variant, known as in strain: NRRL 28336, features a modification of the amino acid from A to S at position 124.
+The protein's natural variant, known as in strain: NRRL 29169, features a modification of the amino acid from E to K at position 133.
+The protein's natural variant, known as in strain: IBT1958, features a modification of the amino acid from N to D at position 137.
+The protein's natural variant, known as in strain: NRRL 28336, features a modification of the amino acid from H to N at position 206.
+The protein's natural variant, known as in strain: NRRL 28336, features a modification of the amino acid from S to T at position 212.
+The protein's natural variant, known as in strain: NRRL 28336, features a modification of the amino acid from S to A at position 278.
+The protein's natural variant, known as in strain: IBT1958, features a modification of the amino acid from Q to K at position 317.
+The protein's natural variant, known as in strain: NRRL 28336, features a modification of the amino acid from V to M at position 360.
+The protein's natural variant, known as in strain: NRRL 13383 and NRRL 28439, features a modification of the amino acid from Q to H at position 364.
+The protein's natural variant, known as in MCD, features a modification of the amino acid from L to P at position 15.
+The protein's natural variant, known as in MCD;, features a modification of the amino acid from L to R at position 22.
+The protein's natural variant, known as in MCD;, features a modification of the amino acid from P to S at position 31.
+The protein's natural variant, known as in MCD, features a modification of the amino acid from H to Y at position 42.
+The protein's natural variant, known as in MCD; abolishes the ability to sulfate keratan;, features a modification of the amino acid from R to C at position 50.
+The protein's natural variant, known as in MCD;, features a modification of the amino acid from S to L at position 51.
+The protein's natural variant, known as in MCD, features a modification of the amino acid from G to D at position 52.
+The protein's natural variant, known as in MCD, features a modification of the amino acid from S to L at position 53.
+The protein's natural variant, known as in MCD, features a modification of the amino acid from L to P at position 59.
+The protein's natural variant, known as in MCD;, features a modification of the amino acid from N to T at position 61.
+The protein's natural variant, known as in MCD;, features a modification of the amino acid from V to L at position 66.
+The protein's natural variant, known as in MCD;, features a modification of the amino acid from Y to H at position 68.
+The protein's natural variant, known as in MCD, features a modification of the amino acid from M to L at position 70.
+The protein's natural variant, known as in MCD;, features a modification of the amino acid from P to S at position 72.
+The protein's natural variant, known as in MCD, features a modification of the amino acid from V to M at position 76.
+The protein's natural variant, known as in MCD, features a modification of the amino acid from R to H at position 93.
+The protein's natural variant, known as in MCD;, features a modification of the amino acid from R to P at position 97.
+The protein's natural variant, known as in MCD, features a modification of the amino acid from S to W at position 98.
+The protein's natural variant, known as in MCD;, features a modification of the amino acid from C to G at position 102.
+The protein's natural variant, known as in MCD, features a modification of the amino acid from C to Y at position 102.
+The protein's natural variant, known as in MCD;, features a modification of the amino acid from M to V at position 104.
+The protein's natural variant, known as in MCD;, features a modification of the amino acid from F to S at position 107.
+The protein's natural variant, known as in MCD;, features a modification of the amino acid from Y to C at position 110.
+The protein's natural variant, known as in MCD; unknown pathological significance, features a modification of the amino acid from S to F at position 118.
+The protein's natural variant, known as in MCD;, features a modification of the amino acid from F to L at position 121.
+The protein's natural variant, known as in MCD;, features a modification of the amino acid from Q to P at position 122.
+The protein's natural variant, known as in MCD, features a modification of the amino acid from R to C at position 127.
+The protein's natural variant, known as in MCD;, features a modification of the amino acid from A to V at position 128.
+The protein's natural variant, known as in MCD, features a modification of the amino acid from S to P at position 131.
+The protein's natural variant, known as in MCD;, features a modification of the amino acid from L to P at position 152.
+The protein's natural variant, known as in MCD;, features a modification of the amino acid from R to G at position 162.
+The protein's natural variant, known as in MCD;, features a modification of the amino acid from R to P at position 166.
+The protein's natural variant, known as in MCD; abolishes the ability to sulfate keratan;, features a modification of the amino acid from K to R at position 174.
+The protein's natural variant, known as in MCD, features a modification of the amino acid from R to G at position 177.
+The protein's natural variant, known as in MCD, features a modification of the amino acid from R to H at position 177.
+The protein's natural variant, known as in MCD;, features a modification of the amino acid from P to R at position 186.
+The protein's natural variant, known as in MCD, features a modification of the amino acid from V to E at position 198.
+The protein's natural variant, known as in MCD;, features a modification of the amino acid from L to R at position 200.
+The protein's natural variant, known as in MCD, features a modification of the amino acid from R to S at position 202.
+The protein's natural variant, known as in MCD; abolishes the ability to sulfate keratan;, features a modification of the amino acid from D to E at position 203.
+The protein's natural variant, known as in MCD;, features a modification of the amino acid from P to Q at position 204.
+The protein's natural variant, known as in MCD, features a modification of the amino acid from R to L at position 205.
+The protein's natural variant, known as in MCD;, features a modification of the amino acid from R to Q at position 205.
+The protein's natural variant, known as in MCD;, features a modification of the amino acid from R to W at position 205.
+The protein's natural variant, known as in MCD;, features a modification of the amino acid from A to T at position 206.
+The protein's natural variant, known as in MCD, features a modification of the amino acid from A to V at position 206.
+The protein's natural variant, known as in MCD;, features a modification of the amino acid from S to F at position 210.
+The protein's natural variant, known as in MCD;, features a modification of the amino acid from R to Q at position 211.
+The protein's natural variant, known as in MCD; abolishes the ability to sulfate keratan;, features a modification of the amino acid from R to W at position 211.
+The protein's natural variant, known as in MCD; abolishes ability to sulfate keratan;, features a modification of the amino acid from A to T at position 217.
+The protein's natural variant, known as in MCD, features a modification of the amino acid from D to E at position 221.
+The protein's natural variant, known as in MCD, features a modification of the amino acid from D to Y at position 221.
+The protein's natural variant, known as in MCD;, features a modification of the amino acid from H to P at position 249.
+The protein's natural variant, known as in MCD;, features a modification of the amino acid from Y to C at position 268.
+The protein's natural variant, known as in MCD; abolishes the ability to sulfate keratan;, features a modification of the amino acid from E to K at position 274.
+The protein's natural variant, known as in MCD;, features a modification of the amino acid from L to P at position 276.
+The protein's natural variant, known as in MCD; unknown pathological significance, features a modification of the amino acid from H to Y at position 308.
+The protein's natural variant, known as in MCD, features a modification of the amino acid from Y to D at position 358.
+The protein's natural variant, known as in MCD;, features a modification of the amino acid from Y to H at position 358.
+The natural variant of this protein is characterized by an amino acid alteration from F to V at position 394.
+The natural variant of this protein is characterized by an amino acid alteration from G to M at position 405.
+The protein's natural variant, known as in CDCBM3; results in abnormal cellular localization with predominant decoration of microtubules rather than diffuse punctiform cytoplasmic and nuclear distribution as observed for wild-type protein;, features a modification of the amino acid from S to N at position 317.
+The protein's natural variant, known as in CDCBM3; results in abnormal cellular localization with predominant decoration of microtubules rather than diffuse punctiform cytoplasmic and nuclear distribution as observed for wild-type protein;, features a modification of the amino acid from H to D at position 321.
+The protein's natural variant, known as found in patients with alcohol-responsive myoclonus-dystonia; unknown pathological significance; the mutation does not affect functional properties;, features a modification of the amino acid from V to I at position 154.
+The protein's natural variant, known as may be associated with a higher risk for schizophrenia;, features a modification of the amino acid from S to C at position 311.
+The protein's natural variant, known as in toppler (to) mice; impairs ceramide synthase activity, features a modification of the amino acid from A to D at position 266.
+The protein's natural variant, known as found in patients with atrial fibrillation; unknown pathological significance; loss of its inhibitory effects on KCNQ1;, features a modification of the amino acid from L to F at position 65.
+The protein's natural variant, known as found in patients with ventricular fibrillation; unknown pathological significance; loss of its inhibitory effects on KCNQ1;, features a modification of the amino acid from Y to H at position 81.
+The protein's natural variant, known as in strain: V1-09 and YJM339, features a modification of the amino acid from R to Q at position 11.
+The protein's natural variant, known as in strain: YJM269, YJM270, YJM326 and YJM1129, features a modification of the amino acid from S to P at position 31.
+The protein's natural variant, known as in HSAN3; mild phenotype; phosphorylation is reduced; does not affect interaction with ELP2; reduced interaction with ELP3; does not affect dimerization;, features a modification of the amino acid from R to P at position 696.
+The protein's natural variant, known as in HSAN3; reduced interaction with ELP2; does not affect interaction with ELP3; does not affect dimerization, features a modification of the amino acid from P to L at position 914.
+The protein's natural variant, known as reduced interaction with ELP2; does not affect interaction with ELP3; does not affect dimerization;, features a modification of the amino acid from C to S at position 1072.
+The protein's natural variant, known as reduced interaction with ELP2; does not affect interaction with ELP3; does not affect dimerization;, features a modification of the amino acid from P to L at position 1158.
+The natural variant of this protein is characterized by an amino acid alteration from S to N at position 185.
+The natural variant of this protein is characterized by an amino acid alteration from N to H at position 232.
+The protein's natural variant, known as in GKD;, features a modification of the amino acid from N to D at position 294.
+The natural variant of this protein is characterized by an amino acid alteration from A to T at position 382.
+The protein's natural variant, known as in GKD;, features a modification of the amino acid from D to V at position 446.
+The protein's natural variant, known as in GKD;, features a modification of the amino acid from W to R at position 509.
+The protein's natural variant, known as does not affect COL4A2 and COL4A1 secretion;, features a modification of the amino acid from V to F at position 192.
+The protein's natural variant, known as does not affect COL4A2 and COL4A1 secretion;, features a modification of the amino acid from K to R at position 701.
+The protein's natural variant, known as does not affect COL4A2 and COL4A1 secretion;, features a modification of the amino acid from P to S at position 718.
+The protein's natural variant, known as in BSVD2;, features a modification of the amino acid from G to E at position 1037.
+The protein's natural variant, known as does not affect COL4A2 and COL4A1 secretion;, features a modification of the amino acid from R to Q at position 1109.
+The protein's natural variant, known as associated with ICH susceptibility; results in a significantly decreased extracellular-to-intracellular ratio of COL4A2 and COL4A1 proteins, indicating interference with the proper secretion of both these proteins;, features a modification of the amino acid from E to G at position 1123.
+The protein's natural variant, known as associated with ICH susceptibility; results in a significantly decreased extracellular-to-intracellular ratio of COL4A2 and COL4A1 proteins, indicating interference with the proper secretion of both these proteins;, features a modification of the amino acid from Q to K at position 1150.
+The protein's natural variant, known as in BSVD2; incomplete penetrance;, features a modification of the amino acid from G to D at position 1152.
+The protein's natural variant, known as probable disease-associated variant found in a family with porencephaly and small-vessel disease in the form of scattered white matter lesions; impairs COL4A2 and COL4A1 secretion; the mutant protein is retained in the endoplasmic reticulum, features a modification of the amino acid from G to R at position 1389.
+The protein's natural variant, known as associated with ICH susceptibility; results in a significantly decreased extracellular-to-intracellular ratio of COL4A2 and COL4A1 proteins, indicating interference with the proper secretion of both these proteins;, features a modification of the amino acid from A to T at position 1690.
+The protein's natural variant, known as in plasmid pCHL1, features a modification of the amino acid from Y to H at position 55.
+The protein's natural variant, known as in plasmid pCHL1, features a modification of the amino acid from A to V at position 188.
+The protein's natural variant, known as in plasmid pCHL1 and plasmid pCTT1, features a modification of the amino acid from T to A at position 189.
+The protein's natural variant, known as in plasmid pCHL1 and plasmid pCTT1, features a modification of the amino acid from A to G at position 200.
+The protein's natural variant, known as in plasmid pCTT1, features a modification of the amino acid from I to V at position 267.
+The protein's natural variant, known as in HADDS; significant loss of transcriptional activator activity; localizes both in the cytoplasm and the nucleus; decreased chromatin binding;, features a modification of the amino acid from N to D at position 66.
+The protein's natural variant, known as in HADDS; significant loss of transcriptional activator activity; localizes both in the cytoplasm and the nucleus; decreased chromatin-binding;, features a modification of the amino acid from Y to C at position 141.
+The protein's natural variant, known as in HADDS; significant loss of transcriptional activator activity; localizes both in the cytoplasm and the nucleus; decreased chromatin-binding, features a modification of the amino acid from I to IHEI at position 159.
+The protein's natural variant, known as in HADDS; partial loss of transcriptional activator activity;, features a modification of the amino acid from R to L at position 163.
+The protein's natural variant, known as in HADDS; loss of transcriptional activator activity;, features a modification of the amino acid from R to P at position 163.
+The protein's natural variant, known as in HADDS; loss of transcriptional activator activity;, features a modification of the amino acid from R to Q at position 163.
+The protein's natural variant, known as in HADDS; significant loss of transcriptional activator activity; localizes both in the cytoplasm and the nucleus; decreased chromatin-binding;, features a modification of the amino acid from G to D at position 171.
+The protein's natural variant, known as in HADDS; according to PubMed:28017373 shows significant loss of transcriptional activator activity while according to PubMed:28017370 shows partial loss of transcriptional activator activity; localizes both in the cytoplasm and the nucleus; decreased chromatin-binding;, features a modification of the amino acid from P to L at position 177.
+The protein's natural variant, known as in HADDS; significant loss of transcriptional activator activity;, features a modification of the amino acid from K to N at position 193.
+The protein's natural variant, known as in HADDS; significant loss of transcriptional activator activity; localizes both in the cytoplasm and the nucleus; decreased chromatin-binding;, features a modification of the amino acid from R to W at position 209.
+The protein's natural variant, known as in strain: ECOR 52, features a modification of the amino acid from V to I at position 26.
+The protein's natural variant, known as in strain: ECOR 31, features a modification of the amino acid from A to V at position 46.
+The protein's natural variant, known as in strain: ECOR 16, features a modification of the amino acid from D to N at position 65.
+The protein's natural variant, known as in strain: ECOR 60, features a modification of the amino acid from I to V at position 119.
+The protein's natural variant, known as in strain: ECOR 16, ECOR 28, ECOR 31, ECOR 37, ECOR 50 and ECOR 71, features a modification of the amino acid from V to I at position 172.
+The protein's natural variant, known as in strain: ECOR 31, ECOR 46, ECOR 50, ECOR 52 and ECOR 60, features a modification of the amino acid from I to V at position 233.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from V to M at position 94.
+The protein's natural variant, known as in SCA19, features a modification of the amino acid from V to E at position 338.
+The protein's natural variant, known as in SCA19;, features a modification of the amino acid from G to V at position 345.
+The protein's natural variant, known as in SCA19; loss of channel activity;, features a modification of the amino acid from T to P at position 352.
+The protein's natural variant, known as in SCA19; unknown pathological significance; causes reduced channel activity;, features a modification of the amino acid from M to I at position 373.
+The protein's natural variant, known as in SCA19, features a modification of the amino acid from T to M at position 377.
+The protein's natural variant, known as in SCA19, features a modification of the amino acid from G to S at position 384.
+The protein's natural variant, known as in SCA19; unknown pathological significance; results in impaired cell surface expression;, features a modification of the amino acid from S to N at position 390.
+The protein's natural variant, known as in BRGDA9; unknown pathological significance; gain of function mutation;, features a modification of the amino acid from V to I at position 392.
+The protein's natural variant, known as in BRGDA9; unknown pathological significance; gain of function mutation;, features a modification of the amino acid from L to F at position 450.
+The protein's natural variant, known as in BRGDA9; unknown pathological significance; does not affect the electrophysiological properties of the channel, features a modification of the amino acid from S to R at position 530.
+The protein's natural variant, known as in BRGDA9; unknown pathological significance; gain of function mutation;, features a modification of the amino acid from G to R at position 600.
+The protein's natural variant, known as in AOVD3; loss of endothelial barrier function in a dextran permeability assay;, features a modification of the amino acid from R to C at position 64.
+The protein's natural variant, known as in AOVD3; unknown pathological significance;, features a modification of the amino acid from A to T at position 95.
+The protein's natural variant, known as in AOVD3; unknown pathological significance;, features a modification of the amino acid from T to M at position 232.
+The protein's natural variant, known as in AOVD3; unknown pathological significance;, features a modification of the amino acid from V to A at position 247.
+The protein's natural variant, known as in AOVD3; unknown pathological significance;, features a modification of the amino acid from Y to S at position 280.
+The protein's natural variant, known as in AOVD3; unknown pathological significance;, features a modification of the amino acid from H to Q at position 411.
+The protein's natural variant, known as in AOVD3; unknown pathological significance;, features a modification of the amino acid from D to V at position 510.
+The protein's natural variant, known as in AOVD3; unknown pathological significance;, features a modification of the amino acid from D to H at position 622.
+The protein's natural variant, known as in AOVD3; unknown pathological significance; requires 2 nucleotide substitutions;, features a modification of the amino acid from A to L at position 749.
+The protein's natural variant, known as in NEM3; some patients have core lesions on muscle biopsy;, features a modification of the amino acid from D to Y at position 3.
+The protein's natural variant, known as in MPCETM;, features a modification of the amino acid from G to R at position 17.
+The protein's natural variant, known as in NEM3, features a modification of the amino acid from G to S at position 17.
+The protein's natural variant, known as in NEM3, features a modification of the amino acid from D to N at position 27.
+The protein's natural variant, known as in NEM3;, features a modification of the amino acid from V to L at position 37.
+The protein's natural variant, known as in NEM3, features a modification of the amino acid from P to L at position 40.
+The protein's natural variant, known as in NEM3; severe, features a modification of the amino acid from H to Y at position 42.
+The protein's natural variant, known as in NEM3;, features a modification of the amino acid from Q to R at position 43.
+The protein's natural variant, known as in NEM3, features a modification of the amino acid from G to V at position 44.
+The protein's natural variant, known as in NEM3;, features a modification of the amino acid from V to F at position 45.
+The protein's natural variant, known as in NEM3;, features a modification of the amino acid from I to N at position 66.
+The protein's natural variant, known as in NEM3, features a modification of the amino acid from T to I at position 68.
+The protein's natural variant, known as in NEM3;, features a modification of the amino acid from P to R at position 72.
+The protein's natural variant, known as in NEM3, features a modification of the amino acid from E to K at position 74.
+The protein's natural variant, known as in NEM3, features a modification of the amino acid from H to L at position 75.
+The protein's natural variant, known as in NEM3, features a modification of the amino acid from H to R at position 75.
+The protein's natural variant, known as in NEM3, features a modification of the amino acid from I to L at position 77.
+The protein's natural variant, known as in NEM3, features a modification of the amino acid from T to A at position 79.
+The protein's natural variant, known as in NEM3, features a modification of the amino acid from E to K at position 85.
+The protein's natural variant, known as in NEM3; autosomal recessive;, features a modification of the amino acid from L to P at position 96.
+The protein's natural variant, known as in NEM3, features a modification of the amino acid from A to T at position 116.
+The protein's natural variant, known as in NEM3;, features a modification of the amino acid from A to V at position 116.
+The protein's natural variant, known as in NEM3; autosomal dominant;, features a modification of the amino acid from N to S at position 117.
+The protein's natural variant, known as in NEM3, features a modification of the amino acid from N to T at position 117.
+The protein's natural variant, known as in NEM3, features a modification of the amino acid from R to H at position 118.
+The protein's natural variant, known as in NEM3; autosomal dominant;, features a modification of the amino acid from M to V at position 134.
+The protein's natural variant, known as in NEM3, features a modification of the amino acid from V to A at position 136.
+The protein's natural variant, known as in NEM3; autosomal recessive;, features a modification of the amino acid from I to M at position 138.
+The protein's natural variant, known as in NEM3, features a modification of the amino acid from A to P at position 140.
+The protein's natural variant, known as in NEM3;, features a modification of the amino acid from L to P at position 142.
+The protein's natural variant, known as in NEM3, features a modification of the amino acid from G to D at position 148.
+The protein's natural variant, known as in NEM3, features a modification of the amino acid from T to N at position 150.
+The protein's natural variant, known as in NEM3, features a modification of the amino acid from D to N at position 156.
+The protein's natural variant, known as in MPCETM;, features a modification of the amino acid from V to L at position 165.
+The protein's natural variant, known as in NEM3; results in sequestration of sarcomeric and Z line proteins into intranuclear aggregates; there is some evidence of muscle regeneration suggesting a compensatory effect;, features a modification of the amino acid from V to M at position 165.
+The protein's natural variant, known as in NEM3, features a modification of the amino acid from A to G at position 172.
+The protein's natural variant, known as in NEM3, features a modification of the amino acid from D to G at position 181.
+The protein's natural variant, known as in NEM3, features a modification of the amino acid from D to H at position 181.
+The protein's natural variant, known as in NEM3, features a modification of the amino acid from D to N at position 181.
+The protein's natural variant, known as in NEM3; mild, features a modification of the amino acid from G to D at position 184.
+The protein's natural variant, known as in NEM3; severe;, features a modification of the amino acid from R to C at position 185.
+The protein's natural variant, known as in NEM3; requires 2 nucleotide substitutions, features a modification of the amino acid from R to D at position 185.
+The protein's natural variant, known as in NEM3; autosomal dominant; severe, features a modification of the amino acid from R to G at position 185.
+The protein's natural variant, known as in NEM3;, features a modification of the amino acid from R to S at position 185.
+The protein's natural variant, known as in SHPM; no effect on cytoskeleton structure;, features a modification of the amino acid from E to D at position 197.
+The protein's natural variant, known as in NEM3, features a modification of the amino acid from R to L at position 198.
+The protein's natural variant, known as in NEM3, features a modification of the amino acid from G to S at position 199.
+The protein's natural variant, known as in CFTD;, features a modification of the amino acid from L to P at position 223.
+The protein's natural variant, known as in NEM3, features a modification of the amino acid from E to G at position 226.
+The protein's natural variant, known as in NEM3;, features a modification of the amino acid from E to Q at position 226.
+The protein's natural variant, known as in NEM3; requires 2 nucleotide substitutions, features a modification of the amino acid from N to V at position 227.
+The protein's natural variant, known as in NEM3, features a modification of the amino acid from M to I at position 229.
+The protein's natural variant, known as in NEM3, features a modification of the amino acid from M to T at position 229.
+The protein's natural variant, known as in NEM3;, features a modification of the amino acid from M to V at position 229.
+The protein's natural variant, known as in NEM3;, features a modification of the amino acid from E to K at position 243.
+The protein's natural variant, known as in NEM3;, features a modification of the amino acid from Q to K at position 248.
+The protein's natural variant, known as in NEM3, features a modification of the amino acid from Q to R at position 248.
+The protein's natural variant, known as in NEM3, features a modification of the amino acid from G to D at position 253.
+The protein's natural variant, known as in NEM3; severe;, features a modification of the amino acid from R to H at position 258.
+The protein's natural variant, known as in NEM3, features a modification of the amino acid from R to L at position 258.
+The protein's natural variant, known as in NEM3; autosomal recessive;, features a modification of the amino acid from E to V at position 261.
+The protein's natural variant, known as in NEM3; severe, features a modification of the amino acid from Q to L at position 265.
+The protein's natural variant, known as in NEM3; autosomal dominant;, features a modification of the amino acid from G to C at position 270.
+The protein's natural variant, known as in NEM3, features a modification of the amino acid from G to D at position 270.
+The protein's natural variant, known as in NEM3;, features a modification of the amino acid from G to R at position 270.
+The protein's natural variant, known as in NEM3; autosomal dominant;, features a modification of the amino acid from M to R at position 271.
+The protein's natural variant, known as in NEM3;, features a modification of the amino acid from A to E at position 274.
+The protein's natural variant, known as in NEM3, features a modification of the amino acid from Y to H at position 281.
+The protein's natural variant, known as in NEM3; severe, features a modification of the amino acid from N to K at position 282.
+The protein's natural variant, known as in NEM3, features a modification of the amino acid from M to K at position 285.
+The protein's natural variant, known as in NEM3; severe; formation of rod-like structure, features a modification of the amino acid from D to G at position 288.
+The protein's natural variant, known as in CFTD; results in decreased motility due to abnormal interactions between actin and tropomyosin with tropomyosin stabilized in the 'off' position; the mutant protein incorporates into actin filaments and does not result in increased actin aggregation or disruption of the sarcomere;, features a modification of the amino acid from D to V at position 294.
+The protein's natural variant, known as in NEM3; no effect on actin structure; higher sensitivity to calcium;, features a modification of the amino acid from K to N at position 328.
+The protein's natural variant, known as in CFTD;, features a modification of the amino acid from P to S at position 334.
+The protein's natural variant, known as in NEM3;, features a modification of the amino acid from E to A at position 336.
+The protein's natural variant, known as in NEM3, features a modification of the amino acid from K to E at position 338.
+The protein's natural variant, known as in NEM3, features a modification of the amino acid from K to I at position 338.
+The protein's natural variant, known as in NEM3, features a modification of the amino acid from S to L at position 350.
+The protein's natural variant, known as in NEM3; found in a patient with a rare combination of NEM3 and dilated cardiomyopathy;, features a modification of the amino acid from W to C at position 358.
+The protein's natural variant, known as in NEM3; autosomal dominant; severe;, features a modification of the amino acid from I to L at position 359.
+The protein's natural variant, known as in NEM3; severe, features a modification of the amino acid from V to F at position 372.
+The protein's natural variant, known as in NEM3, features a modification of the amino acid from R to S at position 374.
+The protein's natural variant, known as in NEM3;, features a modification of the amino acid from K to E at position 375.
+The protein's natural variant, known as in NEM3, features a modification of the amino acid from K to Q at position 375.
+The protein's natural variant, known as in strain: Y-2, features a modification of the amino acid from N to D at position 22.
+The protein's natural variant, known as in strain: Y-0 and Y-1, features a modification of the amino acid from L to M at position 53.
+The protein's natural variant, known as in strain: Y-0 and Y-1, features a modification of the amino acid from P to PSKE at position 56.
+The protein's natural variant, known as in MCC1D;, features a modification of the amino acid from G to E at position 46.
+The protein's natural variant, known as in MCC1D;, features a modification of the amino acid from N to K at position 56.
+The protein's natural variant, known as in MCC1D, features a modification of the amino acid from M to L at position 65.
+The protein's natural variant, known as in MCC1D, features a modification of the amino acid from Y to C at position 79.
+The protein's natural variant, known as in MCC1D;, features a modification of the amino acid from S to F at position 120.
+The protein's natural variant, known as in MCC1D, features a modification of the amino acid from Q to H at position 123.
+The protein's natural variant, known as in MCC1D, features a modification of the amino acid from I to M at position 125.
+The protein's natural variant, known as in MCC1D; clinically asymptomatic form;, features a modification of the amino acid from G to S at position 130.
+The protein's natural variant, known as in MCC1D;, features a modification of the amino acid from E to K at position 134.
+The protein's natural variant, known as in MCC1D, features a modification of the amino acid from M to R at position 160.
+The protein's natural variant, known as in MCC1D;, features a modification of the amino acid from G to V at position 180.
+The protein's natural variant, known as in MCC1D;, features a modification of the amino acid from S to P at position 187.
+The protein's natural variant, known as in MCC1D;, features a modification of the amino acid from G to V at position 209.
+The protein's natural variant, known as in MCC1D;, features a modification of the amino acid from R to W at position 232.
+The protein's natural variant, known as in MCC1D, features a modification of the amino acid from A to D at position 268.
+The protein's natural variant, known as in MCC1D;, features a modification of the amino acid from C to R at position 276.
+The protein's natural variant, known as in MCC1D;, features a modification of the amino acid from R to Q at position 281.
+The protein's natural variant, known as in MCC1D; shows no residual activity;, features a modification of the amino acid from E to G at position 288.
+The protein's natural variant, known as in MCC1D; mild form;, features a modification of the amino acid from A to V at position 289.
+The protein's natural variant, known as in MCC1D; associated with a reduction of wild-type residual activity;, features a modification of the amino acid from A to V at position 291.
+The protein's natural variant, known as in MCC1D;, features a modification of the amino acid from M to R at position 325.
+The protein's natural variant, known as in MCC1D; unknown pathological significance;, features a modification of the amino acid from E to K at position 366.
+The protein's natural variant, known as in MCC1D;, features a modification of the amino acid from Q to P at position 372.
+The protein's natural variant, known as in MCC1D, features a modification of the amino acid from G to D at position 379.
+The protein's natural variant, known as in MCC1D;, features a modification of the amino acid from G to S at position 379.
+The protein's natural variant, known as in MCC1D;, features a modification of the amino acid from H to P at position 380.
+The protein's natural variant, known as in MCC1D; unknown pathological significance;, features a modification of the amino acid from E to K at position 383.
+The protein's natural variant, known as in MCC1D; severe form;, features a modification of the amino acid from R to S at position 385.
+The protein's natural variant, known as in MCC1D; shows some wild-type residual activity;, features a modification of the amino acid from I to M at position 434.
+The protein's natural variant, known as in MCC1D; severe form;, features a modification of the amino acid from L to P at position 437.
+The protein's natural variant, known as in MCC1D;, features a modification of the amino acid from V to M at position 439.
+The protein's natural variant, known as in MCC1D;, features a modification of the amino acid from R to H at position 444.
+The protein's natural variant, known as in MCC1D;, features a modification of the amino acid from I to M at position 460.
+The protein's natural variant, known as in MCC1D; severe form;, features a modification of the amino acid from D to H at position 532.
+The protein's natural variant, known as in MCC1D; asymptomatic form;, features a modification of the amino acid from S to F at position 535.
+The protein's natural variant, known as in PFIC5; loss of isoform 4 transcription regulatory region sequence-specific DNA binding activity; loss of isoform 4 function in regulation of transcription DNA-templated, features a modification of the amino acid from Y to YK at position 149.
+The protein's natural variant, known as in some patients with hereditary hemochromatosis;, features a modification of the amino acid from R to H at position 226.
+The natural variant of this protein is characterized by an amino acid alteration from A to S at position 55.
+The natural variant of this protein is characterized by an amino acid alteration from V to M at position 58.
+The protein's natural variant, known as in MCDR4; leads to thinning in both the outer nuclear layer and whole retina and to impaired retinal function, when tested in a heterologous system, features a modification of the amino acid from A to D at position 180.
+The protein's natural variant, known as risk factor for prostate cancer; reduced enzymatic activity;, features a modification of the amino acid from R to Q at position 462.
+The protein's natural variant, known as no change in enzymatic activity;, features a modification of the amino acid from D to E at position 541.
+The protein's natural variant, known as in BSVD3; loss of galactosyltransferase activity;, features a modification of the amino acid from L to R at position 151.
+The protein's natural variant, known as in BSVD3;, features a modification of the amino acid from A to P at position 154.
+The protein's natural variant, known as in BSVD3;, features a modification of the amino acid from G to R at position 377.
+The protein's natural variant, known as in allele 6M1-6*02 and allele 6M1-6*03;, features a modification of the amino acid from H to Y at position 74.
+The protein's natural variant, known as in allele 6M1-6*03;, features a modification of the amino acid from A to T at position 111.
+The protein's natural variant, known as in allele 6M1-6*02 and allele 6M1-6*03;, features a modification of the amino acid from A to V at position 146.
+The protein's natural variant, known as in allele 6M1-6*02 and allele 6M1-6*03;, features a modification of the amino acid from A to T at position 218.
+The protein's natural variant, known as in POBINDS; unknown pathological significance; associated in cis with 5-E--R-215 del, features a modification of the amino acid from R to C at position 86.
+The protein's natural variant, known as in POBINDS, features a modification of the amino acid from R to P at position 111.
+The protein's natural variant, known as in POBINDS, features a modification of the amino acid from C to F at position 137.
+The protein's natural variant, known as in POBINDS, features a modification of the amino acid from C to G at position 137.
+The protein's natural variant, known as in POBINDS, features a modification of the amino acid from L to R at position 187.
+The protein's natural variant, known as probably interferes with the activity;, features a modification of the amino acid from C to Y at position 972.
+The protein's natural variant, known as reduces Vmax with p-nitrophenol as substrate; binds to adenosine 3',5'-bisphosphate with a dissociation constant (Kd) value increases 4-fold compared with wild-type; binds to PAPS with a dissociation constant (Kd) value similar to wild-type;, features a modification of the amino acid from L to V at position 145.
+The protein's natural variant, known as results in 10-fold decrease of enzymatic activity;, features a modification of the amino acid from L to F at position 263.
+The protein's natural variant, known as in MC4DN14; unknown pathological significance, features a modification of the amino acid from Y to C at position 72.
+The protein's natural variant, known as in CILD18; decreased protein abundance;, features a modification of the amino acid from L to P at position 795.
+The protein's natural variant, known as in strain: cv. Shaoniejing; induces an ideal plant phenotype with a reduced tiller number, increased lodging resistance and enhanced grain yield, features a modification of the amino acid from L to I at position 292.
+The protein's natural variant, known as in SQT7; loss-of-function variant unable to rescue systolic contraction abnormalities in zebrafish morphants; decreased chloride-bicarbonate exchange in transfected cells; decreased localization to cell membrane, features a modification of the amino acid from R to H at position 343.
+The protein's natural variant, known as in SQT7; unknown pathological significance; unable to rescue heart rate abnormalities in zebrafish morphants, features a modification of the amino acid from R to C at position 573.
+The protein's natural variant, known as in SQT7; unknown pathological significance; unable to rescue heart rate abnormalities in zebrafish morphants, features a modification of the amino acid from R to W at position 594.
+The protein's natural variant, known as in SQT7; unknown pathological significance; unable to rescue heart rate abnormalities in zebrafish morphants, features a modification of the amino acid from E to D at position 825.
+The protein's natural variant, known as in SQT7; unknown pathological significance; unable to rescue heart rate abnormalities in zebrafish morphants, features a modification of the amino acid from R to H at position 925.
+The protein's natural variant, known as in strain: Wisconsin, features a modification of the amino acid from F to V at position 123.
+The protein's natural variant, known as in strain: Riv04, Riv14, Riv16, Riv17, Riv18, Riv35, Riv59 and Wisconsin, features a modification of the amino acid from T to S at position 316.
+The protein's natural variant, known as in MRXSCJ; no effect on subcellular location and enzymatic activity, features a modification of the amino acid from D to G at position 87.
+The protein's natural variant, known as in MRXSCJ; impairs enzymatic activity and binding to H3-K9Me3;, features a modification of the amino acid from A to P at position 388.
+The protein's natural variant, known as in MRXSCJ; decreases enzymatic activity, features a modification of the amino acid from D to Y at position 402.
+The protein's natural variant, known as in MRXSCJ;, features a modification of the amino acid from S to R at position 451.
+The protein's natural variant, known as in MRXSCJ; patient fibroblasts show decreased enzymatic activity;, features a modification of the amino acid from P to L at position 480.
+The protein's natural variant, known as de novo mutation found in a patient with intellectual disability, features a modification of the amino acid from C to Y at position 640.
+The protein's natural variant, known as in MRXSCJ; impairs enzymatic activity, features a modification of the amino acid from F to L at position 642.
+The protein's natural variant, known as in MRXSCJ;, features a modification of the amino acid from E to K at position 698.
+The protein's natural variant, known as in MRXSCJ; impairs enzymatic activity;, features a modification of the amino acid from L to F at position 731.
+The protein's natural variant, known as in MRXSCJ, features a modification of the amino acid from R to W at position 750.
+The protein's natural variant, known as in MRXSCJ; impairs enzymatic activity, features a modification of the amino acid from Y to C at position 751.
+The protein's natural variant, known as in allele ALDH9A1*2, features a modification of the amino acid from C to S at position 116.
+The protein's natural variant, known as in allele, features a modification of the amino acid from H to Q at position 2.
+The protein's natural variant, known as in CIMAH;, features a modification of the amino acid from S to F at position 49.
+The protein's natural variant, known as in CIMAH;, features a modification of the amino acid from L to P at position 51.
+The protein's natural variant, known as in CIMAH;, features a modification of the amino acid from R to C at position 173.
+The protein's natural variant, known as in CIMAH;, features a modification of the amino acid from T to I at position 269.
+The protein's natural variant, known as in NTDFS; associated with disease susceptibility;, features a modification of the amino acid from R to H at position 293.
+The protein's natural variant, known as in NTDFS; associated with disease susceptibility; increases risk for congenital heart defects; decreased enzyme stability; no effect on methylenetetrahydrofolate dehydrogenase (NADP+) activity; no effect on formyltetrahydrofolate synthetase activity;, features a modification of the amino acid from R to Q at position 653.
+The protein's natural variant, known as in MRT48;, features a modification of the amino acid from G to R at position 162.
+The protein's natural variant, known as in MRT48;, features a modification of the amino acid from P to R at position 633.
+The protein's natural variant, known as in 3Y1tsD123 cell line; reversibly arrested in G1 phase of cell cycle at the restrictive temperature of 39.8 degrees Celsius; due to extensive degradation by the proteasome, features a modification of the amino acid from A to V at position 109.
+The protein's natural variant, known as in DDISBA; affects function in neuronal axonal growth; reduced F-actin binding; disturbs cytoskeleton organization and dynamics, features a modification of the amino acid from T to I at position 59.
+The protein's natural variant, known as in DDISBA; affects function in neuronal axonal growth; forms cytosolic aggregates; decreased interaction with SPTAN1; disturbs cytoskeleton organization and dynamics, features a modification of the amino acid from G to D at position 205.
+The protein's natural variant, known as in DDISBA; affects function in neuronal axonal growth; forms cytosolic aggregates; decreased interaction with SPTAN1; disturbs cytoskeleton organization and dynamics;, features a modification of the amino acid from G to S at position 205.
+The protein's natural variant, known as in DDISBA; affects function in neuronal axonal growth; forms cytosolic aggregates; disturbs cytoskeleton organization and dynamics, features a modification of the amino acid from L to H at position 247.
+The protein's natural variant, known as in DDISBA; affects function in neuronal axonal growth; forms cytosolic aggregates; disturbs cytoskeleton organization and dynamics, features a modification of the amino acid from L to R at position 250.
+The protein's natural variant, known as in DDISBA; disturbs cytoskeleton organization and dynamics, features a modification of the amino acid from D to E at position 255.
+The protein's natural variant, known as in DDISBA; affects function in neuronal axonal growth; no effect on F-actin binding; disturbs cytoskeleton organization and dynamics, features a modification of the amino acid from T to A at position 268.
+The protein's natural variant, known as in DDISBA; affects function in neuronal axonal growth; no effect on F-actin binding; disturbs cytoskeleton organization and dynamics, features a modification of the amino acid from T to N at position 268.
+The protein's natural variant, known as in DDISBA; affects function in neuronal axonal growth; no effect on F-actin binding; disturbs cytoskeleton organization and dynamics, features a modification of the amino acid from T to S at position 268.
+The protein's natural variant, known as in DDISBA; affects function in neuronal axonal growth; increased F-actin binding; disturbs cytoskeleton organization and dynamics, features a modification of the amino acid from V to M at position 271.
+The protein's natural variant, known as in DDISBA; affects function in neuronal axonal growth; increased F-actin binding; disturbs cytoskeleton organization and dynamics, features a modification of the amino acid from H to R at position 275.
+The protein's natural variant, known as in DDISBA; unknown pathological significance, features a modification of the amino acid from F to L at position 344.
+The protein's natural variant, known as in DDISBA;, features a modification of the amino acid from R to Q at position 411.
+The protein's natural variant, known as in DDISBA; disturbs cytoskeleton organization and dynamics, features a modification of the amino acid from R to W at position 411.
+The protein's natural variant, known as in DDISBA; disturbs cytoskeleton organization and dynamics, features a modification of the amino acid from E to Q at position 491.
+The protein's natural variant, known as in DDISBA; affects function in neuronal axonal growth; increased F-actin binding; disturbs cytoskeleton organization and dynamics;, features a modification of the amino acid from A to G at position 850.
+The protein's natural variant, known as in DDISBA; affects function in neuronal axonal growth; decreased interaction with SPTAN1; disturbs cytoskeleton organization and dynamics, features a modification of the amino acid from R to W at position 1003.
+The protein's natural variant, known as in DDISBA, features a modification of the amino acid from A to T at position 1086.
+The protein's natural variant, known as in DDISBA; distursb cytoskeleton organization and dynamics, features a modification of the amino acid from E to D at position 1110.
+The protein's natural variant, known as in DDISBA; unknown pathological significance;, features a modification of the amino acid from G to S at position 1398.
+The protein's natural variant, known as in DDISBA, features a modification of the amino acid from S to P at position 1674.
+The protein's natural variant, known as in DDISBA; disturbs cytoskeleton organization and dynamics, features a modification of the amino acid from E to Q at position 1886.
+The protein's natural variant, known as in strain: Oregon-R, features a modification of the amino acid from T to I at position 143.
+The protein's natural variant, known as in APRTD;, features a modification of the amino acid from L to P at position 33.
+The protein's natural variant, known as in APRTD; Icelandic type;, features a modification of the amino acid from D to V at position 65.
+The protein's natural variant, known as in APRTD;, features a modification of the amino acid from V to M at position 84.
+The protein's natural variant, known as in APRTD; Newfoundland type;, features a modification of the amino acid from L to P at position 110.
+The protein's natural variant, known as in APRTD;, features a modification of the amino acid from G to D at position 133.
+The protein's natural variant, known as in APRTD; Japanese type; allele APRT*J; most common mutation;, features a modification of the amino acid from M to T at position 136.
+The protein's natural variant, known as in APRTD;, features a modification of the amino acid from V to F at position 150.
+The protein's natural variant, known as in APRTD, features a modification of the amino acid from C to R at position 153.
+The protein's natural variant, known as in PBD10A, features a modification of the amino acid from G to E at position 138.
+The protein's natural variant, known as in PBD10B;, features a modification of the amino acid from G to R at position 331.
+The protein's natural variant, known as in strain: Isolate C-type, features a modification of the amino acid from A to V at position 215.
+The protein's natural variant, known as in CTRCT17, features a modification of the amino acid from V to F at position 96.
+The protein's natural variant, known as probable disease-associated variant found in a family with autosomal dominant congenital cataract and microcornea; significantly decreased thermal stability of CRYBB1/CRYBA1-crystallin heteromer but not CRYBB1-crystallin homomer;, features a modification of the amino acid from S to R at position 129.
+The protein's natural variant, known as in CTRCT17; unknown pathological significance, features a modification of the amino acid from D to Y at position 170.
+The protein's natural variant, known as in CTRCT17; unknown pathological significance;, features a modification of the amino acid from R to C at position 230.
+The protein's natural variant, known as in ACHM7; reduced ATF6-mediated unfolded protein response;, features a modification of the amino acid from R to C at position 324.
+The protein's natural variant, known as in ACHM7;, features a modification of the amino acid from Y to N at position 567.
+The protein's natural variant, known as in MC4DN1; benign variant;, features a modification of the amino acid from A to G at position 56.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from N to K at position 89.
+The protein's natural variant, known as in MC4DN1;, features a modification of the amino acid from L to P at position 90.
+The protein's natural variant, known as in MC4DN1; reduced protein stability;, features a modification of the amino acid from G to E at position 124.
+The protein's natural variant, known as in MC4DN1;, features a modification of the amino acid from G to R at position 124.
+The protein's natural variant, known as in MC4DN1, features a modification of the amino acid from V to G at position 177.
+The protein's natural variant, known as in MC4DN1; unknown pathological significance; reduces protein stability; impairs complex IV assembly;, features a modification of the amino acid from N to Y at position 178.
+The protein's natural variant, known as in CMT4K; unknown pathological significance;, features a modification of the amino acid from R to W at position 192.
+The protein's natural variant, known as in MC4DN1, features a modification of the amino acid from G to E at position 205.
+The protein's natural variant, known as in MC4DN1; unknown pathological significance;, features a modification of the amino acid from W to R at position 227.
+The protein's natural variant, known as in MC4DN1;, features a modification of the amino acid from M to T at position 235.
+The protein's natural variant, known as in MC4DN1, features a modification of the amino acid from I to T at position 246.
+The protein's natural variant, known as in MC4DN1, features a modification of the amino acid from A to D at position 248.
+The protein's natural variant, known as in MC4DN1, features a modification of the amino acid from G to R at position 257.
+The protein's natural variant, known as in MC4DN1;, features a modification of the amino acid from G to V at position 257.
+The protein's natural variant, known as in MC4DN1; unknown pathological significance; reduces protein stability; impairs complex IV assembly, features a modification of the amino acid from P to S at position 258.
+The protein's natural variant, known as in MC4DN1; unknown pathological significance; reduces protein stability; impairs complex IV assembly; ;, features a modification of the amino acid from E to EHLQYE at position 270.
+The protein's natural variant, known as in MC4DN1;, features a modification of the amino acid from Y to D at position 274.
+The protein's natural variant, known as in CDG2T; loss-of-funtion variant resulting in lack of ApoC-III and IgA1 glycosylation;, features a modification of the amino acid from F to S at position 104.
+The protein's natural variant, known as in CDG2T; loss of ApoC-III glycosylation, features a modification of the amino acid from R to P at position 210.
+The protein's natural variant, known as likely benign variant; does not affect ApoC-III glycosylation, features a modification of the amino acid from K to R at position 271.
+The protein's natural variant, known as likely benign variant; does not affect ApoC-III glycosylation;, features a modification of the amino acid from M to V at position 493.
+The protein's natural variant, known as in allele EPHX1*2;, features a modification of the amino acid from R to C at position 49.
+The protein's natural variant, known as in allele EPHX1*3; benign variant; frequent in the human population; 55% of wild type enzyme activity;, features a modification of the amino acid from Y to H at position 113.
+The protein's natural variant, known as in allele EPHX1*4; benign variant; frequent in the human population; 62% of wild type enzyme activity;, features a modification of the amino acid from H to R at position 139.
+The protein's natural variant, known as in allele EPHX1*1G, features a modification of the amino acid from L to P at position 260.
+The protein's natural variant, known as either a rare variant or a sequencing error, features a modification of the amino acid from T to I at position 396.
+The protein's natural variant, known as in allele EPHX1*5;, features a modification of the amino acid from R to Q at position 454.
+The protein's natural variant, known as in IIB, features a modification of the amino acid from QGA to LF at position 26.
+The protein's natural variant, known as higher specific activity;, features a modification of the amino acid from V to L at position 35.
+The protein's natural variant, known as in FA13AD; decreased intracellular protein abundance; loss of protein-glutamine gamma-glutamyltransferase activity; decreased alpha-2-antiplasmin to fibrin cross-linking activity; no effect on fibrin alpha chain and gamma chain cross-linking activity; decreased clot fiber thickness;, features a modification of the amino acid from R to Q at position 38.
+The protein's natural variant, known as in FA13AD; mild; no effect on intracellular protein abundance; no effect on protein-glutamine gamma-glutamyltransferase activity; no effect on alpha-2-antiplasmin to fibrin cross-linking activity; loss of fibrin alpha chain cross-linking activity; decreased clot fiber thickness;, features a modification of the amino acid from P to L at position 167.
+The protein's natural variant, known as in FA13AD; decreased intracellular protein abundance; decreased protein-glutamine gamma-glutamyltransferase activity; no effect on alpha-2-antiplasmin to fibrin cross-linking activity; loss of fibrin alpha chain cross-linking activity; decreased clot fiber thickness;, features a modification of the amino acid from Y to C at position 168.
+The protein's natural variant, known as in FA13AD; mild; decreased intracellular protein abundance; loss of protein-glutamine gamma-glutamyltransferase activity; decreased alpha-2-antiplasmin to fibrin cross-linking activity; decreased rate of fibrin gamma chain cross-linking activity; decreased rate of fibrin alpha chain cross-linking activity; decreased clot fiber thickness;, features a modification of the amino acid from R to Q at position 172.
+The protein's natural variant, known as in FA13AD, features a modification of the amino acid from G to V at position 274.
+The protein's natural variant, known as in FA13AD; decreased intracellular protein abundance; loss of protein-glutamine gamma-glutamyltransferase activity; loss of alpha-2-antiplasmin to fibrin cross-linking activity; loss of fibrin gamma chain cross-linking activity; decreased rate of fibrin alpha chain cross-linking activity; decreased clot fiber thickness, features a modification of the amino acid from P to R at position 290.
+The protein's natural variant, known as in FA13AD; mild; decreased intracellular protein abundance; loss of protein-glutamine gamma-glutamyltransferase activity; decreased alpha-2-antiplasmin to fibrin cross-linking activity; loss of fibrin gamma chain cross-linking activity; decreased rate of fibrin alpha chain cross-linking activity; decreased clot fiber thickness, features a modification of the amino acid from H to Y at position 343.
+The protein's natural variant, known as in FA13AD; unknown pathological significance, features a modification of the amino acid from A to D at position 347.
+The protein's natural variant, known as in FA13AD; unknown pathological significance, features a modification of the amino acid from W to R at position 376.
+The protein's natural variant, known as in FA13AD; unknown pathological significance;, features a modification of the amino acid from S to L at position 414.
+The protein's natural variant, known as in FA13AD; mild; no effect on intracellular protein abundance; no effect on protein-glutamine gamma-glutamyltransferase activity; no effect on alpha-2-antiplasmin to fibrin cross-linking activity; no effect on fibrin alpha chain and gamma chain cross-linking activity; decreased clot fiber thickness, features a modification of the amino acid from Q to R at position 416.
+The protein's natural variant, known as in FA13AD; mild; decreased intracellular protein abundance; loss of protein-glutamine gamma-glutamyltransferase activity; decreased alpha-2-antiplasmin to fibrin cross-linking activity; loss of fibrin gamma chain cross-linking activity; decreased clot fiber thickness, features a modification of the amino acid from L to P at position 530.
+The protein's natural variant, known as in FA13AD; decreased intracellular protein abundance; no effect on protein-glutamine gamma-glutamyltransferase activity; no effect on alpha-2-antiplasmin to fibrin cross-linking activity; no effect on fibrin alpha chain and gamma chain cross-linking activity; decreased clot fiber thickness;, features a modification of the amino acid from R to Q at position 541.
+The protein's natural variant, known as in allele F13A*1A, allele F13A*2A and allele F13*(2)A;, features a modification of the amino acid from P to L at position 565.
+The protein's natural variant, known as in FA13AD; no effect on intracellular protein abundance; increased protein-glutamine gamma-glutamyltransferase activity; no effect on alpha-2-antiplasmin to fibrin cross-linking activity; no effect on fibrin alpha chain and gamma chain cross-linking activity; decreased clot fiber thickness;, features a modification of the amino acid from G to S at position 593.
+The protein's natural variant, known as in FA13AD; mild; decreased intracellular protein abundance; loss of protein-glutamine gamma-glutamyltransferase activity; loss of alpha-2-antiplasmin to fibrin cross-linking activity; decreased rate of fibrin gamma chain cross-linking activity; loss of fibrin alpha chain cross-linking activity; decreased clot fiber thickness;, features a modification of the amino acid from Q to K at position 602.
+The protein's natural variant, known as in FA13AD; decreased intracellular protein abundance; decreased protein-glutamine gamma-glutamyltransferase activity; decreased alpha-2-antiplasmin to fibrin cross-linking activity; no effect on fibrin alpha chain and gamma chain cross-linking activity; decreased clot fiber thickness;, features a modification of the amino acid from R to H at position 612.
+The protein's natural variant, known as in allele F13A*2A and allele F13A*2B;, features a modification of the amino acid from V to I at position 651.
+The protein's natural variant, known as in allele F13A*2A and allele F13A*2B;, features a modification of the amino acid from E to Q at position 652.
+The protein's natural variant, known as in FA13AD; decreased intracellular protein abundance; decreased protein-glutamine gamma-glutamyltransferase activity; decreased alpha-2-antiplasmin to fibrin cross-linking activity; decreased rate of fibrin alpha chain cross-linking activity; decreased clot fiber thickness;, features a modification of the amino acid from D to G at position 669.
+The protein's natural variant, known as in FA13AD;, features a modification of the amino acid from R to H at position 682.
+The protein's natural variant, known as in FA13AD; mild; decreased intracellular protein abundance; loss of protein-glutamine gamma-glutamyltransferase activity; decreased alpha-2-antiplasmin to fibrin cross-linking activity; decreased rate of fibrin alpha chain cross-linking activity; decreased clot fiber thickness;, features a modification of the amino acid from R to Q at position 704.
+The protein's natural variant, known as in FA13AD; mild; decreased intracellular protein abundance; loss of protein-glutamine gamma-glutamyltransferase activity; decreased alpha-2-antiplasmin to fibrin cross-linking activity; decreased rate of fibrin gamma chain cross-linking activity; decreased rate of fibrin alpha chain cross-linking activity; decreased clot fiber thickness;, features a modification of the amino acid from R to G at position 716.
+The protein's natural variant, known as requires 2 nucleotide substitutions;, features a modification of the amino acid from W to Q at position 205.
+The protein's natural variant, known as requires 2 nucleotide substitutions, features a modification of the amino acid from Y to R at position 400.
+The protein's natural variant, known as in TOKAS;, features a modification of the amino acid from Y to C at position 356.
+The protein's natural variant, known as in TOKAS, features a modification of the amino acid from R to C at position 387.
+The protein's natural variant, known as in TOKAS, features a modification of the amino acid from P to R at position 587.
+The natural variant of this protein is characterized by an amino acid alteration from H to P at position 590.
+The protein's natural variant, known as in TOKAS, features a modification of the amino acid from R to C at position 599.
+The protein's natural variant, known as in strain: Milan normotensive and FHH hypertensive; no constriction of afferent arterioles in response to increased pressure and impaired renal blood flow autoregulation resulting in kidney disease in both strains; redistributes from the cell membrane to perinuclear location and disrupts the F-actin cytoskeleton in the kidney and renal vascular smooth muscle cells of FHH; elevated membrane expression of the iberiotoxin-sensitive potassium channel alpha and elevated iberiotoxin-sensitive potassium channel current in renal vascular smooth muscle cells of FHH; proteinuria, renal interstitial fibrosis, alterations in gromelural capillary pressure, increased permeability to albumin and impaired glomerular function in FHH after induction of hypertension, features a modification of the amino acid from K to Q at position 572.
+The natural variant of this protein is characterized by an amino acid alteration from N to M at position 110.
+The natural variant of this protein is characterized by an amino acid alteration from S to H at position 147.
+The natural variant of this protein is characterized by an amino acid alteration from N to M at position 359.
+The natural variant of this protein is characterized by an amino acid alteration from K to Q at position 374.
+The protein's natural variant, known as in FHCL1; San Francisco;, features a modification of the amino acid from C to W at position 27.
+The protein's natural variant, known as in FHCL1; Japanese patient;, features a modification of the amino acid from C to S at position 46.
+The protein's natural variant, known as in FHCL1; German patient;, features a modification of the amino acid from A to S at position 50.
+The protein's natural variant, known as in FHCL1; unknown pathological significance;, features a modification of the amino acid from A to T at position 50.
+The protein's natural variant, known as in Paris-4;, features a modification of the amino acid from C to Y at position 52.
+The protein's natural variant, known as in FHCL1;, features a modification of the amino acid from S to P at position 56.
+The protein's natural variant, known as in FHCL1;, features a modification of the amino acid from R to C at position 78.
+The protein's natural variant, known as in FHCL1; French Canadian-4;, features a modification of the amino acid from W to G at position 87.
+The protein's natural variant, known as in FHCL1;, features a modification of the amino acid from C to Y at position 89.
+The protein's natural variant, known as in FHCL1; London-4;, features a modification of the amino acid from D to G at position 90.
+The protein's natural variant, known as in FHCL1;, features a modification of the amino acid from D to N at position 90.
+The protein's natural variant, known as in FHCL1; Durban-1;, features a modification of the amino acid from D to Y at position 90.
+The protein's natural variant, known as in FHCL1; Spanish patient;, features a modification of the amino acid from Q to E at position 92.
+The protein's natural variant, known as in FHCL1; Spanish patient;, features a modification of the amino acid from C to G at position 95.
+The protein's natural variant, known as in FHCL1; Lancashire; 6% of American English;, features a modification of the amino acid from E to K at position 101.
+The protein's natural variant, known as in Munster-1;, features a modification of the amino acid from C to R at position 109.
+The protein's natural variant, known as in FHCL1; does not affect receptor expression at the cell surface; results in reduced LDL binding; results in reduced LDL uptake and internalization;, features a modification of the amino acid from C to R at position 116.
+The protein's natural variant, known as in FHCL1;, features a modification of the amino acid from C to F at position 134.
+The protein's natural variant, known as in FHCL1;, features a modification of the amino acid from C to W at position 134.
+The protein's natural variant, known as found in a patient with hypercholesterolemia;, features a modification of the amino acid from D to H at position 139.
+The protein's natural variant, known as in FHCL1; Philippines/Durban-2/Japan;, features a modification of the amino acid from E to K at position 140.
+The protein's natural variant, known as in FHCL1;, features a modification of the amino acid from C to R at position 143.
+The protein's natural variant, known as in FHCL1;, features a modification of the amino acid from C to Y at position 148.
+The protein's natural variant, known as in Germany;, features a modification of the amino acid from C to G at position 155.
+The protein's natural variant, known as in FHCL1; results in defective LDL binding; does not affect receptor expression at the cell surface;, features a modification of the amino acid from C to Y at position 155.
+The protein's natural variant, known as in FHCL1; unknown pathological significance;, features a modification of the amino acid from C to Y at position 160.
+The protein's natural variant, known as in FHCL1; unknown pathological significance;, features a modification of the amino acid from D to A at position 168.
+The protein's natural variant, known as in FHCL1; Sephardic/Safed; 10% of the Sephardic Jews;, features a modification of the amino acid from D to H at position 168.
+The protein's natural variant, known as in FHCL1; does not affect receptor expression at the cell surface; results in reduced LDL binding; results in reduced LDL uptake and internalization;, features a modification of the amino acid from D to N at position 168.
+The protein's natural variant, known as in FHCL1;, features a modification of the amino acid from D to Y at position 168.
+The protein's natural variant, known as may contribute to familial hypercholesterolemia;, features a modification of the amino acid from D to H at position 172.
+The protein's natural variant, known as in FHCL1; does not affect receptor expression at the cell surface; results in reduced LDL binding; results in reduced LDL uptake and internalization;, features a modification of the amino acid from D to N at position 172.
+The protein's natural variant, known as in Greece-1;, features a modification of the amino acid from C to R at position 173.
+The protein's natural variant, known as in FHCL1;, features a modification of the amino acid from C to W at position 173.
+The protein's natural variant, known as in FHCL1; Afrikaner-3; 5-10% of Afrikaners;, features a modification of the amino acid from D to N at position 175.
+The protein's natural variant, known as in FHCL1;, features a modification of the amino acid from D to Y at position 175.
+The protein's natural variant, known as in FHCL1; Puerto Rico;, features a modification of the amino acid from S to L at position 177.
+The protein's natural variant, known as in FHCL1;, features a modification of the amino acid from C to W at position 184.
+The protein's natural variant, known as in FHCL1; Glasco;, features a modification of the amino acid from C to Y at position 184.
+The protein's natural variant, known as in Shreveport;, features a modification of the amino acid from C to F at position 197.
+The protein's natural variant, known as in FHCL1; British patient;, features a modification of the amino acid from C to R at position 197.
+The protein's natural variant, known as in El Salvador-1;, features a modification of the amino acid from C to Y at position 197.
+The protein's natural variant, known as found in a patient with hypercholesterolemia;, features a modification of the amino acid from E to K at position 201.
+The protein's natural variant, known as in FHCL1; unknown pathological significance;, features a modification of the amino acid from H to L at position 211.
+The protein's natural variant, known as in FHCL1; Padova;, features a modification of the amino acid from D to G at position 221.
+The protein's natural variant, known as in FHCL1; German patient;, features a modification of the amino acid from D to N at position 221.
+The protein's natural variant, known as in FHCL1; Cologne patient;, features a modification of the amino acid from D to Y at position 221.
+The protein's natural variant, known as in FHCL1;, features a modification of the amino acid from C to Y at position 222.
+The protein's natural variant, known as in Italy-2;, features a modification of the amino acid from D to G at position 224.
+The protein's natural variant, known as in Portugal;, features a modification of the amino acid from D to N at position 224.
+The protein's natural variant, known as in FHCL1; Cologne patient;, features a modification of the amino acid from D to V at position 224.
+The protein's natural variant, known as in Miami-1;, features a modification of the amino acid from S to P at position 226.
+The protein's natural variant, known as in FHCL1; Afrikaner-1/Maine; 65-70% of Afrikaner Americans;, features a modification of the amino acid from D to E at position 227.
+The protein's natural variant, known as in Chieti-3, features a modification of the amino acid from E to CK at position 228.
+The protein's natural variant, known as in FHCL1; French Canadian-3/Mexico; 2% of French Canadians;, features a modification of the amino acid from E to K at position 228.
+The protein's natural variant, known as in FHCL1; Tulsa-2;, features a modification of the amino acid from E to Q at position 228.
+The protein's natural variant, known as in FHCL1; Norwegian patient;, features a modification of the amino acid from C to G at position 231.
+The protein's natural variant, known as in Charlotte;, features a modification of the amino acid from E to K at position 240.
+The protein's natural variant, known as in FHCL1; unknown pathological significance;, features a modification of the amino acid from C to R at position 243.
+The protein's natural variant, known as in Bretagne-1;, features a modification of the amino acid from C to F at position 248.
+The protein's natural variant, known as in FHCL1; British patient;, features a modification of the amino acid from C to Y at position 248.
+The protein's natural variant, known as may contribute to familial hypercholesterolemia;, features a modification of the amino acid from R to W at position 253.
+The protein's natural variant, known as in FHCL1;, features a modification of the amino acid from Q to P at position 254.
+The protein's natural variant, known as found in a patient with hypercholesterolemia;, features a modification of the amino acid from C to S at position 255.
+The protein's natural variant, known as in Nevers;, features a modification of the amino acid from D to G at position 256.
+The protein's natural variant, known as does not affect receptor expression at the cell surface; does not affect LDL binding; does not affect LDL uptake and internalization;, features a modification of the amino acid from R to W at position 257.
+The protein's natural variant, known as in FHCL1; rare mutation; strongly reduced receptor activity;, features a modification of the amino acid from C to F at position 261.
+The protein's natural variant, known as in FHCL1; Cincinnati-1; unknown pathological significance;, features a modification of the amino acid from D to E at position 266.
+The protein's natural variant, known as in Miami-2;, features a modification of the amino acid from C to Y at position 270.
+The protein's natural variant, known as in FHCL1;, features a modification of the amino acid from C to R at position 276.
+The protein's natural variant, known as in FHCL1; unknown pathological significance;, features a modification of the amino acid from C to W at position 276.
+The protein's natural variant, known as in FHCL1; Syrian patient;, features a modification of the amino acid from C to Y at position 276.
+The protein's natural variant, known as in FHCL1; patients from Sweden and La Havana; unknown pathological significance;, features a modification of the amino acid from E to K at position 277.
+The protein's natural variant, known as in FHCL1; unknown pathological significance;, features a modification of the amino acid from H to Y at position 285.
+The protein's natural variant, known as in FHCL1; Greece-2; unknown pathological significance;, features a modification of the amino acid from S to R at position 286.
+The protein's natural variant, known as in FHCL1; German patient;, features a modification of the amino acid from E to K at position 288.
+The protein's natural variant, known as in FHCL1; does not affect receptor expression at the cell surface; results in reduced LDL binding; results in reduced LDL uptake and internalization;, features a modification of the amino acid from R to G at position 300.
+The protein's natural variant, known as in FHCL1; Greek patient;, features a modification of the amino acid from D to A at position 301.
+The protein's natural variant, known as in FHCL1; does not affect receptor expression at the cell surface; results in reduced LDL binding; results in reduced LDL uptake and internalization;, features a modification of the amino acid from D to G at position 301.
+The protein's natural variant, known as in FHCL1; Iraki patient;, features a modification of the amino acid from C to W at position 302.
+The protein's natural variant, known as in FHCL1; Spanish patient;, features a modification of the amino acid from C to Y at position 302.
+The protein's natural variant, known as in Baltimore-1;, features a modification of the amino acid from D to E at position 304.
+The protein's natural variant, known as in Denver-2;, features a modification of the amino acid from D to N at position 304.
+The protein's natural variant, known as in FHCL1; Amsterdam; unknown pathological significance;, features a modification of the amino acid from S to L at position 306.
+The protein's natural variant, known as in FHCL1;, features a modification of the amino acid from C to Y at position 313.
+The protein's natural variant, known as in FHCL1; unknown pathological significance;, features a modification of the amino acid from G to R at position 314.
+The protein's natural variant, known as in FHCL1; Trieste;, features a modification of the amino acid from C to F at position 318.
+The protein's natural variant, known as in FHCL1;, features a modification of the amino acid from C to R at position 318.
+The protein's natural variant, known as in Mexico-1; leads to a defect in the intracellular transport of the receptor;, features a modification of the amino acid from C to Y at position 318.
+The protein's natural variant, known as in FHCL1; unknown pathological significance;, features a modification of the amino acid from S to C at position 326.
+The protein's natural variant, known as in FHCL1;, features a modification of the amino acid from H to Y at position 327.
+The protein's natural variant, known as in FHCL1;, features a modification of the amino acid from C to F at position 329.
+The protein's natural variant, known as in FHCL1; Chinese patient;, features a modification of the amino acid from C to Y at position 329.
+The protein's natural variant, known as in Paris-6;, features a modification of the amino acid from G to S at position 335.
+The protein's natural variant, known as in FHCL1; Japanese patients;, features a modification of the amino acid from C to S at position 338.
+The protein's natural variant, known as in New York-1;, features a modification of the amino acid from D to E at position 342.
+The protein's natural variant, known as in FHCL1; unknown pathological significance;, features a modification of the amino acid from D to N at position 342.
+The protein's natural variant, known as in FHCL1; Picardie; unknown pathological significance;, features a modification of the amino acid from G to S at position 343.
+The protein's natural variant, known as in FHCL1;, features a modification of the amino acid from R to P at position 350.
+The protein's natural variant, known as in FHCL1; unknown pathological significance;, features a modification of the amino acid from C to R at position 352.
+The protein's natural variant, known as in Mexico-2;, features a modification of the amino acid from C to Y at position 352.
+The protein's natural variant, known as in Munster-2;, features a modification of the amino acid from D to G at position 354.
+The protein's natural variant, known as in Oklahoma;, features a modification of the amino acid from D to V at position 354.
+The protein's natural variant, known as in FHCL1;, features a modification of the amino acid from D to Y at position 356.
+The protein's natural variant, known as in Paris-7;, features a modification of the amino acid from E to K at position 357.
+The protein's natural variant, known as in FHCL1;, features a modification of the amino acid from C to Y at position 358.
+The protein's natural variant, known as in Mexico-3;, features a modification of the amino acid from C to R at position 364.
+The protein's natural variant, known as in FHCL1;, features a modification of the amino acid from Q to R at position 366.
+The protein's natural variant, known as in FHCL1; French Canadian patient;, features a modification of the amino acid from C to R at position 368.
+The protein's natural variant, known as in FHCL1; unknown pathological significance;, features a modification of the amino acid from C to Y at position 368.
+The protein's natural variant, known as in FHCL1;, features a modification of the amino acid from N to T at position 370.
+The protein's natural variant, known as in FHCL1; unknown pathological significance;, features a modification of the amino acid from G to D at position 373.
+The protein's natural variant, known as in Naples-1;, features a modification of the amino acid from C to R at position 379.
+The protein's natural variant, known as in FHCL1;, features a modification of the amino acid from C to Y at position 379.
+The protein's natural variant, known as in FHCL1;, features a modification of the amino acid from A to D at position 399.
+The protein's natural variant, known as in Pori;, features a modification of the amino acid from L to H at position 401.
+The protein's natural variant, known as in FHCL1;, features a modification of the amino acid from L to V at position 401.
+The protein's natural variant, known as in FHCL1; Japanese patient;, features a modification of the amino acid from F to L at position 403.
+The protein's natural variant, known as in FHCL1; unknown pathological significance;, features a modification of the amino acid from T to P at position 404.
+The protein's natural variant, known as may contribute to familial hypercholesterolemia;, features a modification of the amino acid from R to Q at position 406.
+The protein's natural variant, known as in FHCL1; unknown pathological significance;, features a modification of the amino acid from R to W at position 406.
+The protein's natural variant, known as in FHCL1; Algeria-1; unknown pathological significance;, features a modification of the amino acid from E to K at position 408.
+The protein's natural variant, known as in FHCL1; Chinese patient;, features a modification of the amino acid from L to R at position 414.
+The protein's natural variant, known as in FHCL1;, features a modification of the amino acid from D to G at position 415.
+The protein's natural variant, known as in FHCL1; German patient;, features a modification of the amino acid from R to Q at position 416.
+The protein's natural variant, known as in FHCL1; results in reduced receptor expression at the cell surface due to defective receptor recycling;, features a modification of the amino acid from R to W at position 416.
+The protein's natural variant, known as in FHCL1; Swedish patient;, features a modification of the amino acid from I to T at position 423.
+The protein's natural variant, known as in FHCL1; Afrikaner-2; 20-30% of Afrikaners and 2% of FHCL1 Dutch;, features a modification of the amino acid from V to M at position 429.
+The protein's natural variant, known as in FHCL1; Algeria-2; unknown pathological significance;, features a modification of the amino acid from A to T at position 431.
+The protein's natural variant, known as in FHCL1; German patient;, features a modification of the amino acid from L to V at position 432.
+The protein's natural variant, known as in FHCL1; Osaka-3;, features a modification of the amino acid from D to H at position 433.
+The protein's natural variant, known as in FHCL1; Algeria-3; unknown pathological significance;, features a modification of the amino acid from T to K at position 434.
+The protein's natural variant, known as in Rouen;, features a modification of the amino acid from I to M at position 441.
+The protein's natural variant, known as in Russia-1;, features a modification of the amino acid from I to N at position 441.
+The protein's natural variant, known as in FHCL1; unknown pathological significance;, features a modification of the amino acid from Y to H at position 442.
+The protein's natural variant, known as in North Platt;, features a modification of the amino acid from W to C at position 443.
+The protein's natural variant, known as in FHCL1;, features a modification of the amino acid from I to T at position 451.
+The protein's natural variant, known as in FHCL1; results in reduced receptor expression at the cell surface due to defective receptor recycling;, features a modification of the amino acid from T to N at position 454.
+The protein's natural variant, known as found in a patient with hypercholesterolemia;, features a modification of the amino acid from R to G at position 471.
+The protein's natural variant, known as in New York-2;, features a modification of the amino acid from G to R at position 478.
+The protein's natural variant, known as in FHCL1;, features a modification of the amino acid from L to P at position 479.
+The protein's natural variant, known as in FHCL1;, features a modification of the amino acid from D to H at position 482.
+The protein's natural variant, known as in FHCL1;, features a modification of the amino acid from W to R at position 483.
+The protein's natural variant, known as in Milan;, features a modification of the amino acid from H to R at position 485.
+The protein's natural variant, known as in FHCL1; unknown pathological significance;, features a modification of the amino acid from D to N at position 492.
+The protein's natural variant, known as in FHCL1; Kuwait;, features a modification of the amino acid from V to M at position 523.
+The protein's natural variant, known as in FHCL1; Cincinnati-3; unknown pathological significance;, features a modification of the amino acid from P to S at position 526.
+The protein's natural variant, known as in Saint Omer; retention in the ER;, features a modification of the amino acid from G to D at position 546.
+The protein's natural variant, known as in FHCL1; Genoa;, features a modification of the amino acid from G to D at position 549.
+The protein's natural variant, known as in FHCL1;, features a modification of the amino acid from N to H at position 564.
+The protein's natural variant, known as in FHCL1; Sicily;, features a modification of the amino acid from N to S at position 564.
+The protein's natural variant, known as in Naples-2;, features a modification of the amino acid from G to V at position 565.
+The protein's natural variant, known as in FHCL1; Japanese patient;, features a modification of the amino acid from L to V at position 568.
+The protein's natural variant, known as in FHCL1;, features a modification of the amino acid from R to C at position 574.
+The protein's natural variant, known as in FHCL1; unknown pathological significance;, features a modification of the amino acid from R to H at position 574.
+The protein's natural variant, known as in FHCL1; results in loss of receptor expression at the cell surface;, features a modification of the amino acid from W to G at position 577.
+The protein's natural variant, known as in FHCL1; unknown pathological significance;, features a modification of the amino acid from W to S at position 577.
+The protein's natural variant, known as in FHCL1; Cincinnati-4; less than 2% receptor activity;, features a modification of the amino acid from D to N at position 579.
+The protein's natural variant, known as in FHCL1;, features a modification of the amino acid from D to Y at position 579.
+The protein's natural variant, known as in FHCL1; unknown pathological significance;, features a modification of the amino acid from I to T at position 585.
+The protein's natural variant, known as in FHCL1; Sicily;, features a modification of the amino acid from G to E at position 592.
+The protein's natural variant, known as in FHCL1; unknown pathological significance;, features a modification of the amino acid from R to W at position 595.
+The protein's natural variant, known as in London-5;, features a modification of the amino acid from L to S at position 599.
+The protein's natural variant, known as in FHCL1; unknown pathological significance;, features a modification of the amino acid from D to H at position 601.
+The protein's natural variant, known as in FHCL1;, features a modification of the amino acid from P to S at position 608.
+The protein's natural variant, known as in FHCL1;, features a modification of the amino acid from R to C at position 633.
+The protein's natural variant, known as in FHCL1;, features a modification of the amino acid from V to D at position 639.
+The protein's natural variant, known as in FHCL1;, features a modification of the amino acid from P to L at position 649.
+The protein's natural variant, known as in FHCL1; French Canadian-2; 5% of French Canadians;, features a modification of the amino acid from C to Y at position 667.
+The protein's natural variant, known as in FHCL1; New York-3;, features a modification of the amino acid from C to R at position 677.
+The protein's natural variant, known as in Issoire;, features a modification of the amino acid from L to P at position 682.
+The protein's natural variant, known as in FHCL1; Gujerat/Zambia/Belgian/Dutch/Sweden/Japan;, features a modification of the amino acid from P to L at position 685.
+The protein's natural variant, known as in FHCL1; unknown pathological significance;, features a modification of the amino acid from P to L at position 699.
+The protein's natural variant, known as in FHCL1; Spanish patient;, features a modification of the amino acid from D to E at position 700.
+The protein's natural variant, known as in FHCL1; Japanese patient;, features a modification of the amino acid from E to K at position 714.
+The protein's natural variant, known as in FHCL1; Paris-9; unknown pathological significance;, features a modification of the amino acid from T to I at position 726.
+The protein's natural variant, known as in Russia-2;, features a modification of the amino acid from I to F at position 792.
+The protein's natural variant, known as in FHCL1; La Havana patient;, features a modification of the amino acid from V to M at position 797.
+The protein's natural variant, known as in FHCL1; unknown pathological significance;, features a modification of the amino acid from V to D at position 806.
+The protein's natural variant, known as in FHCL1; unknown pathological significance;, features a modification of the amino acid from R to Q at position 814.
+The protein's natural variant, known as in FHCL1; does not affect receptor expression at the cell surface; does not affect LDL binding; results in impaired LDL uptake and internalization;, features a modification of the amino acid from N to K at position 825.
+The protein's natural variant, known as in FHCL1;, features a modification of the amino acid from P to S at position 826.
+The protein's natural variant, known as in New York-5;, features a modification of the amino acid from V to I at position 827.
+The protein's natural variant, known as in FHCL1; J.D.Bari/Syria; 2-fold decreased affinity for LDLRAP1;, features a modification of the amino acid from Y to C at position 828.
+The protein's natural variant, known as in Turku;, features a modification of the amino acid from G to D at position 844.
+The protein's natural variant, known as in strain: kenya_2, features a modification of the amino acid from N to S at position 27.
+The protein's natural variant, known as in strain: kenya_2, features a modification of the amino acid from I to V at position 72.
+The protein's natural variant, known as in strain: NRRL 26156, features a modification of the amino acid from E to K at position 320.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from K to T at position 316.
+The protein's natural variant, known as in POROK7; unknown pathological significance;, features a modification of the amino acid from P to R at position 101.
+The protein's natural variant, known as in POROK7; unknown pathological significance;, features a modification of the amino acid from A to V at position 128.
+The protein's natural variant, known as in POROK7; unknown pathological significance, features a modification of the amino acid from R to L at position 161.
+The protein's natural variant, known as in POROK7; 1000-fold diminution in diphosphomevalonate decarboxylase activity;, features a modification of the amino acid from R to Q at position 161.
+The protein's natural variant, known as in POROK7; unknown pathological significance;, features a modification of the amino acid from R to Q at position 228.
+The protein's natural variant, known as in POROK7; unknown pathological significance;, features a modification of the amino acid from R to W at position 228.
+The protein's natural variant, known as in POROK7;, features a modification of the amino acid from F to S at position 249.
+The protein's natural variant, known as in POROK7;, features a modification of the amino acid from N to S at position 292.
+The protein's natural variant, known as in POROK7; unknown pathological significance;, features a modification of the amino acid from G to R at position 376.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation, features a modification of the amino acid from P to S at position 98.
+The protein's natural variant, known as in a glioblastoma multiforme sample; somatic mutation, features a modification of the amino acid from D to N at position 467.
+The protein's natural variant, known as in strain: MEL01, features a modification of the amino acid from P to A at position 16.
+The protein's natural variant, known as in strain: MEL02 and ZBMEL377, features a modification of the amino acid from C to CGPCC at position 18.
+The protein's natural variant, known as in strain: ZBMEL131, features a modification of the amino acid from C to W at position 31.
+The protein's natural variant, known as in strain: oKB105, features a modification of the amino acid from S to T at position 22.
+The protein's natural variant, known as in strain: oKB105, features a modification of the amino acid from C to G at position 97.
+The protein's natural variant, known as in strain: 168 and its derivatives, non surfactin-producing strains, features a modification of the amino acid from EGKGLSLPLDSFSVRLHQDGQVSIELPDSHSPCYIKTYEVDPGYKMAVCAAHPDFPEDITMVSYEELL to GRQRLIASA at position 224.
+The protein's natural variant, known as in AI3C; unknown pathological significance;, features a modification of the amino acid from R to P at position 422.
+The protein's natural variant, known as in Rumpshaker, features a modification of the amino acid from I to T at position 187.
+The protein's natural variant, known as in Jimpy MSD, features a modification of the amino acid from A to V at position 243.
+The protein's natural variant, known as in allele NKG2-E*02, features a modification of the amino acid from C to R at position 213.
+The protein's natural variant, known as no effect on cell membrane location;, features a modification of the amino acid from L to F at position 17.
+The protein's natural variant, known as probable disease-associated variant found in patients with Waardenburg syndrome 2; loss of cell membrane location; new cytoplasmic location, features a modification of the amino acid from L to P at position 17.
+The protein's natural variant, known as associated with increased susceptibility for Hirschsprung disease; sex-dependent gene dosage effect;, features a modification of the amino acid from G to S at position 57.
+The protein's natural variant, known as probable disease-associated variant found in patients with Waardenburg syndrome 2; decreased calcium release upon endothelin 3 exposure; loss of downstream pathway activation upon endothelin 3 exposure; no effect on cell membrane location; no effect on internalization upon endothelin 3 exposure, features a modification of the amino acid from N to Y at position 137.
+The protein's natural variant, known as probable disease-associated variant found in patients with Waardenburg syndrome 2; loss of cell membrane location; new cytoplasmic location, features a modification of the amino acid from P to R at position 156.
+The protein's natural variant, known as in WS4A;, features a modification of the amino acid from A to G at position 183.
+The protein's natural variant, known as in HSCR2;, features a modification of the amino acid from W to C at position 276.
+The protein's natural variant, known as in WS4A, features a modification of the amino acid from F to L at position 292.
+The protein's natural variant, known as in HSCR2; sporadic;, features a modification of the amino acid from R to W at position 319.
+The protein's natural variant, known as in HSCR2; decreased calcium release; no effect on cell membrane location, features a modification of the amino acid from M to I at position 374.
+The protein's natural variant, known as in HSCR2; familial; loss of cell membrane location; new cytoplasmic location, features a modification of the amino acid from P to L at position 383.
+The protein's natural variant, known as in CTRCT2; reduces protein-protein interactions in vivo;, features a modification of the amino acid from T to P at position 5.
+The protein's natural variant, known as in CTRCT2; unknown pathological significance, features a modification of the amino acid from S to F at position 78.
+The protein's natural variant, known as in CTRCT2;, features a modification of the amino acid from G to C at position 129.
+The protein's natural variant, known as in CTRCT2; congenital lamellar cataract; unknown pathological significance;, features a modification of the amino acid from R to W at position 168.
+The protein's natural variant, known as in STHAG3;, features a modification of the amino acid from G to S at position 51.
+The protein's natural variant, known as in CCM2;, features a modification of the amino acid from L to R at position 198.
+The protein's natural variant, known as in CCM2; associated with Q-229, features a modification of the amino acid from Q to H at position 215.
+The protein's natural variant, known as in CCM2; associated with H-215, features a modification of the amino acid from L to Q at position 229.
+The protein's natural variant, known as in an ovarian mucinous carcinoma sample; somatic mutation;, features a modification of the amino acid from P to L at position 432.
+The protein's natural variant, known as in nal-24, nal-102, nal-103, nal-107, nal-108, nal-111, nal-114, en-2 and en-5 mutants; resistant to nalidixic acid and to enoxacin, features a modification of the amino acid from D to N at position 426.
+The protein's natural variant, known as in nal-31, nal-109, nal-115 and nal-120 mutants; resistant to nalidixic acid, features a modification of the amino acid from K to E at position 447.
+The protein's natural variant, known as in microcin B17 resistant mutant, features a modification of the amino acid from W to R at position 751.
+The protein's natural variant, known as in acriflavine susceptible mutant acrB, decreased supercoiling activity, ATPase activity no longer stimulated by DNA, decreased DNA-binding, bind GyrA normally, features a modification of the amino acid from SR to RC at position 760.
+The protein's natural variant, known as in MC1DN37; reduced enzymatic activity of the respiratory chain complex I; reduced NDUFA8 protein levels; decrease in respiratory supercomplexes comprising complex I (CI/CIII 2/CIV and CI/CIII 2) as well as an increase in unintegrated complex III dimers;, features a modification of the amino acid from R to C at position 47.
+The protein's natural variant, known as in MC1DN37; defect in the assembly of respiratory chain complex I; reduced enzymatic activity of the respiratory chain complex I; altered fibroblast mitochondria morphology and reduced mitochondrial network branching; no significant differences in mitochondrial respiratory capacity, features a modification of the amino acid from R to L at position 98.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from N to H at position 140.
+The protein's natural variant, known as in strain: L1/440-L, features a modification of the amino acid from R to C at position 200.
+The protein's natural variant, known as in strain: L1/440/LN and B/Tw-5/OT, features a modification of the amino acid from R to K at position 235.
+The protein's natural variant, known as in strain: 69A, features a modification of the amino acid from E to K at position 24.
+The protein's natural variant, known as in strain: 69A, features a modification of the amino acid from K to R at position 39.
+The protein's natural variant, known as in strain: 69A, features a modification of the amino acid from T to A at position 69.
+The protein's natural variant, known as in strain: 69A, features a modification of the amino acid from I to V at position 80.
+The protein's natural variant, known as in strain: 69A, features a modification of the amino acid from M to A at position 83.
+The protein's natural variant, known as in strain: 69A, features a modification of the amino acid from F to C at position 148.
+The protein's natural variant, known as in strain: 69A, features a modification of the amino acid from VS to IA at position 174.
+The protein's natural variant, known as in strain: 69A, features a modification of the amino acid from E to A at position 198.
+The protein's natural variant, known as in strain: 69A, features a modification of the amino acid from V to I at position 209.
+The protein's natural variant, known as in strain: 69A, features a modification of the amino acid from V to I at position 228.
+The protein's natural variant, known as in strain: 69A, features a modification of the amino acid from N to R at position 251.
+The protein's natural variant, known as in strain: 69A, features a modification of the amino acid from K to E at position 435.
+The protein's natural variant, known as in strain: 69A, features a modification of the amino acid from V to L at position 456.
+The protein's natural variant, known as in strain: 69A, features a modification of the amino acid from V to I at position 504.
+The protein's natural variant, known as in strain: 69A, features a modification of the amino acid from V to A at position 526.
+The protein's natural variant, known as in strain: 69A, features a modification of the amino acid from H to Y at position 555.
+The natural variant of this protein is characterized by an amino acid alteration from A to V at position 18.
+The protein's natural variant, known as in RP70; does not affect nuclear speck localization; disrupts interaction with PRPF3; does not affect interaction with PPIH; does not integrated in spliceosomal snRNP complex;, features a modification of the amino acid from R to H at position 192.
+The protein's natural variant, known as in RP70;, features a modification of the amino acid from P to L at position 315.
+The protein's natural variant, known as in AIPDS; decreased function in protein linear deubiquitination, features a modification of the amino acid from M to I at position 86.
+The protein's natural variant, known as does not affect down-regulation of NF-kappa-B signaling;, features a modification of the amino acid from Q to H at position 115.
+The protein's natural variant, known as in AIPDS; decreased function in protein linear deubiquitination, features a modification of the amino acid from W to S at position 167.
+The protein's natural variant, known as in AIPDS and IMD107; slightly impaired ability to mediate deubiquitination of linear polyubiquitin chains; does not affect ability to interact with RNF31; severely decreased NF-kappa-B inhibition and increased NF-kappa-B signaling;, features a modification of the amino acid from Y to C at position 244.
+The protein's natural variant, known as in IMD107; severely decreased NF-kappa-B inhibition and increased NF-kappa-B signaling, features a modification of the amino acid from D to V at position 246.
+The protein's natural variant, known as in IMD107; loss of NF-kappa-B inhibition and increased NF-kappa-B signaling;, features a modification of the amino acid from R to Q at position 263.
+The protein's natural variant, known as in AIPDS and IMD107; decreased stability; impaired ability to mediate deubiquitination of linear polyubiquitin chains; loss of NF-kappa-B inhibition and increased NF-kappa-B signaling; does not affect ability to interact with RNF31;, features a modification of the amino acid from L to P at position 272.
+The protein's natural variant, known as in PARK1; no effect on oligomerization;, features a modification of the amino acid from A to P at position 30.
+The protein's natural variant, known as in PARK1 and DLB; significant increase in binding to negatively charged phospholipid liposomes; increases oligomerization;, features a modification of the amino acid from E to K at position 46.
+The protein's natural variant, known as in PARK1; no effect on protein structure; no effect on phosphorylation of the protein; no effect on membrane- and lipid-binding; increases oligomerization; increases fibril formation; increases secretion of the protein; impairs copper-binding;, features a modification of the amino acid from H to Q at position 50.
+The protein's natural variant, known as in PARK1; no effect on osmotic stress-induced phosphorylation; increases oligomerization;, features a modification of the amino acid from A to T at position 53.
+The protein's natural variant, known as in PGBM2;, features a modification of the amino acid from A to P at position 16.
+The protein's natural variant, known as in GSD15; loss of autoglucosylation;, features a modification of the amino acid from T to M at position 83.
+The protein's natural variant, known as in PGBM2;, features a modification of the amino acid from D to H at position 102.
+The protein's natural variant, known as in resistance to benomyl and benzimidazole, features a modification of the amino acid from E to A at position 198.
+The protein's natural variant, known as in RTT;, features a modification of the amino acid from E to Q at position 10.
+The protein's natural variant, known as in RTT;, features a modification of the amino acid from D to E at position 97.
+The protein's natural variant, known as in RTT;, features a modification of the amino acid from D to Y at position 97.
+The protein's natural variant, known as in RTT;, features a modification of the amino acid from L to R at position 100.
+The protein's natural variant, known as in RTT;, features a modification of the amino acid from L to V at position 100.
+The protein's natural variant, known as in RTT;, features a modification of the amino acid from P to H at position 101.
+The protein's natural variant, known as in RTT;, features a modification of the amino acid from P to L at position 101.
+The protein's natural variant, known as in RTT; also in a patient with Angelman syndrome and some typical RTT features;, features a modification of the amino acid from P to R at position 101.
+The protein's natural variant, known as in RTT;, features a modification of the amino acid from P to S at position 101.
+The protein's natural variant, known as in RTT, features a modification of the amino acid from P to T at position 101.
+The protein's natural variant, known as in RTT;, features a modification of the amino acid from R to Q at position 106.
+The protein's natural variant, known as in RTT;, features a modification of the amino acid from R to W at position 106.
+The protein's natural variant, known as in RTT;, features a modification of the amino acid from R to G at position 111.
+The protein's natural variant, known as in RTT;, features a modification of the amino acid from Y to D at position 120.
+The protein's natural variant, known as in RTT;, features a modification of the amino acid from L to F at position 124.
+The protein's natural variant, known as in RTT;, features a modification of the amino acid from Q to P at position 128.
+The protein's natural variant, known as in RTT; impairs interaction with ATRX and abolishes ATRX recruitment to heterochromatin;, features a modification of the amino acid from R to C at position 133.
+The protein's natural variant, known as in RTT;, features a modification of the amino acid from R to H at position 133.
+The protein's natural variant, known as in RTT;, features a modification of the amino acid from S to C at position 134.
+The protein's natural variant, known as in RTT;, features a modification of the amino acid from K to E at position 135.
+The protein's natural variant, known as in MRXS13;, features a modification of the amino acid from E to G at position 137.
+The protein's natural variant, known as in MRXS13; impairs interaction with ATRX and abolishes ATRX recruitment to heterochromatin;, features a modification of the amino acid from A to V at position 140.
+The protein's natural variant, known as in RTT;, features a modification of the amino acid from P to R at position 152.
+The protein's natural variant, known as in RTT;, features a modification of the amino acid from F to I at position 155.
+The protein's natural variant, known as in RTT;, features a modification of the amino acid from F to S at position 155.
+The protein's natural variant, known as in RTT;, features a modification of the amino acid from D to G at position 156.
+The protein's natural variant, known as in RTT;, features a modification of the amino acid from T to A at position 158.
+The protein's natural variant, known as in RTT;, features a modification of the amino acid from T to M at position 158.
+The protein's natural variant, known as in RTT;, features a modification of the amino acid from G to V at position 161.
+The protein's natural variant, known as in MRXS13;, features a modification of the amino acid from R to W at position 167.
+The protein's natural variant, known as in RTT;, features a modification of the amino acid from K to I at position 210.
+The protein's natural variant, known as in MRXS13;, features a modification of the amino acid from P to L at position 225.
+The protein's natural variant, known as in RTT;, features a modification of the amino acid from P to R at position 225.
+The protein's natural variant, known as in MRXS13;, features a modification of the amino acid from K to E at position 284.
+The protein's natural variant, known as in RTT;, features a modification of the amino acid from P to A at position 302.
+The protein's natural variant, known as in RTT;, features a modification of the amino acid from P to H at position 302.
+The protein's natural variant, known as in RTT;, features a modification of the amino acid from P to L at position 302.
+The protein's natural variant, known as in RTT;, features a modification of the amino acid from P to R at position 302.
+The protein's natural variant, known as probable disease-associated variant found in a patient with drug-resistant epilepsy with intellectual disability, parkinsonism and other neurologic symptoms;, features a modification of the amino acid from K to N at position 305.
+The protein's natural variant, known as in RTT; abolishes interaction with TBL1X;, features a modification of the amino acid from K to R at position 305.
+The protein's natural variant, known as in RTT; abolishes interaction with TBL1X and TBL1XR1;, features a modification of the amino acid from R to C at position 306.
+The protein's natural variant, known as in RTT;, features a modification of the amino acid from R to H at position 306.
+The protein's natural variant, known as in RTT;, features a modification of the amino acid from P to A at position 322.
+The protein's natural variant, known as in RTT;, features a modification of the amino acid from P to L at position 322.
+The protein's natural variant, known as in MRXS13;, features a modification of the amino acid from P to S at position 322.
+The protein's natural variant, known as in RTT;, features a modification of the amino acid from R to W at position 344.
+The protein's natural variant, known as in RTT; unknown pathological significance;, features a modification of the amino acid from P to S at position 388.
+The protein's natural variant, known as in MRXS13; unknown pathological significance;, features a modification of the amino acid from P to L at position 399.
+The protein's natural variant, known as in ENS-MECP2; uncertain pathological significance;, features a modification of the amino acid from G to S at position 428.
+The protein's natural variant, known as in MRXS13;, features a modification of the amino acid from R to Q at position 453.
+The protein's natural variant, known as in strain: CD-1, features a modification of the amino acid from S to G at position 11.
+The protein's natural variant, known as in strain: CD-1, features a modification of the amino acid from G to A at position 14.
+The protein's natural variant, known as in strain: CD-1, features a modification of the amino acid from FQ to YH at position 155.
+The protein's natural variant, known as in BETB, features a modification of the amino acid from E to D at position 39.
+The protein's natural variant, known as in BETB, features a modification of the amino acid from S to A at position 283.
+The protein's natural variant, known as in SIALIDOSIS; type 1; mild mutation as residual activity is still measurable, features a modification of the amino acid from V to M at position 54.
+The protein's natural variant, known as in SIALIDOSIS; type 2; less than 10% of activity, features a modification of the amino acid from G to V at position 68.
+The protein's natural variant, known as in SIALIDOSIS; type 2; no enzyme activity; retained in the endoplasmic reticulum / Golgi or rapidly degraded in the lysosomes;, features a modification of the amino acid from P to L at position 80.
+The protein's natural variant, known as does not affect sialidase activity;, features a modification of the amino acid from G to A at position 88.
+The protein's natural variant, known as does not affect sialidase activity;, features a modification of the amino acid from L to F at position 90.
+The protein's natural variant, known as in SIALIDOSIS; type 2;, features a modification of the amino acid from L to R at position 91.
+The protein's natural variant, known as in SIALIDOSIS; type 1; normally processed;, features a modification of the amino acid from S to G at position 182.
+The protein's natural variant, known as does not affect sialidase activity;, features a modification of the amino acid from P to A at position 210.
+The protein's natural variant, known as significant decrease in sialidase activity; absence of lysosomal localization; mislocalization to the endoplasmic reticulum;, features a modification of the amino acid from V to A at position 217.
+The protein's natural variant, known as in SIALIDOSIS; type 1; partial transport and residual transport activity;, features a modification of the amino acid from V to M at position 217.
+The protein's natural variant, known as in SIALIDOSIS; type 1; unable to reach the lysosomes;, features a modification of the amino acid from G to A at position 219.
+The protein's natural variant, known as does not affect sialidase activity;, features a modification of the amino acid from T to M at position 222.
+The protein's natural variant, known as in SIALIDOSIS; type 2; impaired enzyme folding;, features a modification of the amino acid from R to P at position 225.
+The protein's natural variant, known as in SIALIDOSIS; type 1 and juvenile type 2; catalytically inactive; retained in pre-lysosomal compartments;, features a modification of the amino acid from G to R at position 227.
+The protein's natural variant, known as in SIALIDOSIS; type 1; unable to reach the lysosomes;, features a modification of the amino acid from L to H at position 231.
+The protein's natural variant, known as significant decrease in sialidase activity; absence of lysosomal localization; mislocalization to the endoplasmic reticulum;, features a modification of the amino acid from D to N at position 234.
+The protein's natural variant, known as in SIALIDOSIS; type 2; no enzyme activity; retained in the endoplasmic reticulum / Golgi or rapidly degraded in the lysosomes;, features a modification of the amino acid from W to R at position 240.
+The protein's natural variant, known as in SIALIDOSIS; type 1; no enzyme activity and no transport to the lysosome;, features a modification of the amino acid from G to R at position 243.
+The protein's natural variant, known as does not affect sialidase activity;, features a modification of the amino acid from G to S at position 252.
+The protein's natural variant, known as in SIALIDOSIS; infantile type 2; catalytically inactive; rapid intralysosomal degradation;, features a modification of the amino acid from F to Y at position 260.
+The protein's natural variant, known as in SIALIDOSIS; type 2; reduction in enzyme activity; rapid intralysosomal degradation, features a modification of the amino acid from L to F at position 270.
+The protein's natural variant, known as in SIALIDOSIS, features a modification of the amino acid from L to P at position 270.
+The protein's natural variant, known as in SIALIDOSIS; type 1; mild mutation as residual activity is still measurable;, features a modification of the amino acid from R to S at position 294.
+The protein's natural variant, known as in SIALIDOSIS; type 2; less than 10% of activity; rapid intralysosomal degradation; impaired enzyme folding;, features a modification of the amino acid from A to V at position 298.
+The protein's natural variant, known as in SIALIDOSIS; type 1; no enzyme activity; retained in the endoplasmic reticulum / Golgi or rapidly degraded in the lysosomes;, features a modification of the amino acid from P to S at position 316.
+The protein's natural variant, known as in SIALIDOSIS; type 1; reduction in enzyme activity;, features a modification of the amino acid from G to S at position 328.
+The protein's natural variant, known as in SIALIDOSIS; type 2; unable to reach the lysosomes;, features a modification of the amino acid from P to Q at position 335.
+The protein's natural variant, known as in SIALIDOSIS; type 2; affects substrate binding or catalysis;, features a modification of the amino acid from R to G at position 341.
+The protein's natural variant, known as does not affect sialidase activity;, features a modification of the amino acid from S to R at position 351.
+The protein's natural variant, known as in SIALIDOSIS; infantile type 2; unable to reach the lysosomes;, features a modification of the amino acid from L to P at position 363.
+The protein's natural variant, known as in SIALIDOSIS; infantile type 2; catalytically inactive;, features a modification of the amino acid from Y to C at position 370.
+The protein's natural variant, known as in SIALIDOSIS; type 1; mild mutation as residual activity is still measurable, features a modification of the amino acid from Y to YHY at position 400.
+The protein's natural variant, known as in SPG73; alters protein conformation; dominant negative mutation;, features a modification of the amino acid from R to C at position 37.
+The protein's natural variant, known as in SPGF9; unknown pathological significance, features a modification of the amino acid from H to R at position 192.
+The protein's natural variant, known as in SPGF9; unknown pathological significance, features a modification of the amino acid from E to Q at position 196.
+The protein's natural variant, known as in SPGF9;, features a modification of the amino acid from R to H at position 290.
+The protein's natural variant, known as in SPGF9;, features a modification of the amino acid from R to C at position 298.
+The protein's natural variant, known as in SPGF9;, features a modification of the amino acid from R to H at position 298.
+The protein's natural variant, known as in SPGF9; unknown pathological significance, features a modification of the amino acid from Q to K at position 309.
+The protein's natural variant, known as in SPGF9; unknown pathological significance, features a modification of the amino acid from E to K at position 480.
+The protein's natural variant, known as in SPGF9; unknown pathological significance;, features a modification of the amino acid from T to R at position 493.
+The protein's natural variant, known as in strain: JU403, JU439, JU516 and JU793, features a modification of the amino acid from P to S at position 54.
+The protein's natural variant, known as in strain: PB800, features a modification of the amino acid from K to T at position 97.
+The protein's natural variant, known as in strain: EG4181, features a modification of the amino acid from V to L at position 142.
+The protein's natural variant, known as in strain: JU403, JU439, JU516 and JU793, features a modification of the amino acid from S to I at position 205.
+The protein's natural variant, known as in strain: ED3092 and ED3101, features a modification of the amino acid from I to T at position 222.
+The protein's natural variant, known as in strain: ED3092 and ED3101, features a modification of the amino acid from V to F at position 234.
+The protein's natural variant, known as in strain: HK104, features a modification of the amino acid from P to L at position 257.
+The protein's natural variant, known as in strain: JU725, features a modification of the amino acid from F to V at position 297.
+The protein's natural variant, known as in strain: JU725, features a modification of the amino acid from L to W at position 317.
+The protein's natural variant, known as in strain: PB800, features a modification of the amino acid from F to L at position 321.
+The protein's natural variant, known as in strain: BW287, EG4181, EG4207A, HK104, HK105, JU403, JU439, JU516, JU725, JU793, PB800 and PB826, features a modification of the amino acid from V to F at position 342.
+The protein's natural variant, known as in strain: ED3033, ED3034, ED3035, ED3037, ED3092, ED3101 and VT847, features a modification of the amino acid from V to I at position 342.
+The protein's natural variant, known as in strain: PB826, features a modification of the amino acid from G to V at position 353.
+The protein's natural variant, known as in DEE102; unknown pathological significance, features a modification of the amino acid from R to G at position 208.
+The protein's natural variant, known as in DEE102; unknown pathological significance;, features a modification of the amino acid from A to T at position 296.
+The protein's natural variant, known as in DEE102, features a modification of the amino acid from T to P at position 375.
+The protein's natural variant, known as in DEE102; unknown pathological significance, features a modification of the amino acid from P to Q at position 387.
+The protein's natural variant, known as in COXPD11; alters homooligomeric formation of the protein; decreases the levels of mitochondrial protein synthesis;, features a modification of the amino acid from R to Q at position 417.
+The protein's natural variant, known as in mitochondrial myopathy; sporadic;, features a modification of the amino acid from G to S at position 34.
+The protein's natural variant, known as in exercice intolerance; with cardiomyopathy and septo-optic dysplasia;, features a modification of the amino acid from S to P at position 35.
+The protein's natural variant, known as in colorectal cancer;, features a modification of the amino acid from R to H at position 80.
+The protein's natural variant, known as in exercise intolerance;, features a modification of the amino acid from S to P at position 151.
+The protein's natural variant, known as in hyperthrophic cardiomyopathy;, features a modification of the amino acid from G to E at position 166.
+The protein's natural variant, known as in LHON; secondary mutation; does not seem to directly cause the disease;, features a modification of the amino acid from D to N at position 171.
+The natural variant of this protein is characterized by an amino acid alteration from IA to VT at position 190.
+The protein's natural variant, known as in CMIH;, features a modification of the amino acid from G to D at position 251.
+The protein's natural variant, known as associated with susceptibility to obesity;, features a modification of the amino acid from G to S at position 251.
+The protein's natural variant, known as in cardiomyopathy; fatal; post-partum, features a modification of the amino acid from N to H at position 255.
+The protein's natural variant, known as in colorectal cancer;, features a modification of the amino acid from F to L at position 276.
+The protein's natural variant, known as in multisystem disorder;, features a modification of the amino acid from Y to C at position 278.
+The protein's natural variant, known as in exercise intolerance;, features a modification of the amino acid from G to D at position 290.
+The protein's natural variant, known as in mitochondrial myopathy, features a modification of the amino acid from G to E at position 339.
+The protein's natural variant, known as in LHON; secondary mutation; does not seem to directly cause the disease;, features a modification of the amino acid from V to M at position 356.
+The protein's natural variant, known as in strain: IQ489, features a modification of the amino acid from D to E at position 409.
+The protein's natural variant, known as in strain: IQ490, features a modification of the amino acid from G to GG at position 423.
+The protein's natural variant, known as in strain: ECOAU9326, features a modification of the amino acid from H to Q at position 432.
+The protein's natural variant, known as in strain: ECOAU9302, ECOAU9306, ECOAU9307 and ECOAU9309, features a modification of the amino acid from Q to G at position 490.
+The protein's natural variant, known as in strain: ECOAU9306, features a modification of the amino acid from G to A at position 684.
+The protein's natural variant, known as in Milano-12;, features a modification of the amino acid from G to R at position 191.
+The protein's natural variant, known as in Tochigi/Osaka-2/Milano-5/Villajoyosa;, features a modification of the amino acid from R to C at position 301.
+The protein's natural variant, known as in DYSFIBRIN; fibrinogen Bergamo-2/Essen/Haifa/Osaka-3/Perugia/Saga/Barcelona-3/Barcelona-4;, features a modification of the amino acid from R to H at position 301.
+The protein's natural variant, known as in CAFBN; hypofibrinogenemia; heterozygous; no effect on fibrinogen complex assembly; impaired fibrinogen complex secretion, features a modification of the amino acid from T to P at position 303.
+The protein's natural variant, known as in DYSFIBRIN; fibrinogen Baltimore-1; impaired polymerization;, features a modification of the amino acid from G to V at position 318.
+The protein's natural variant, known as in CAFBN; hypofibrinogenemia; heterozygous; no effect on fibrinogen complex assembly; no effect on fibrinogen complex secretion, features a modification of the amino acid from D to H at position 327.
+The protein's natural variant, known as in Baltimore-3; impaired polymerization;, features a modification of the amino acid from N to I at position 334.
+The protein's natural variant, known as in Kyoto-1; causes accelerated cleavage by plasmin, features a modification of the amino acid from N to K at position 334.
+The protein's natural variant, known as in Hillsborough; prolonged thrombin clotting time, features a modification of the amino acid from G to D at position 335.
+The protein's natural variant, known as in Asahi; impaired polymerization;, features a modification of the amino acid from M to T at position 336.
+The protein's natural variant, known as in CAFBN; hypofibrinogenemia; heterozygous; no effect on fibrinogen complex assembly; decreased fibrinogen complex secretion, features a modification of the amino acid from N to D at position 345.
+The protein's natural variant, known as in Nagoya-1; impaired polymerization;, features a modification of the amino acid from Q to R at position 355.
+The protein's natural variant, known as in DYSFIBRIN; fibrinogen Milano-1; impaired polymerization;, features a modification of the amino acid from D to V at position 356.
+The protein's natural variant, known as in Kyoto-3; impaired polymerization;, features a modification of the amino acid from D to Y at position 356.
+The protein's natural variant, known as in Bern-1; impaired polymerization, features a modification of the amino acid from N to K at position 363.
+The protein's natural variant, known as in Paris-1; impaired polymerization, features a modification of the amino acid from G to VMCGEALPMLKDPCYS at position 377.
+The protein's natural variant, known as in Milano-7; impaired polymerization, features a modification of the amino acid from S to C at position 384.
+The protein's natural variant, known as in Osaka-5;, features a modification of the amino acid from R to G at position 401.
+The protein's natural variant, known as in CAFBN; hypofibrinogenemia; heterozygous;, features a modification of the amino acid from R to W at position 401.
+The protein's natural variant, known as in DYSFIBRIN; fibrinogen Philadelphia;, features a modification of the amino acid from S to P at position 404.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from D to N at position 323.
+The protein's natural variant, known as in XAN1;, features a modification of the amino acid from R to C at position 149.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from L to F at position 763.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from R to G at position 791.
+The protein's natural variant, known as in NEDSOA; unknown pathological significance, features a modification of the amino acid from G to S at position 45.
+The protein's natural variant, known as in NEDSOA; severely decreased tRNA binding; decreased thermal stability, features a modification of the amino acid from P to S at position 164.
+The protein's natural variant, known as in OPA9;, features a modification of the amino acid from L to V at position 74.
+The protein's natural variant, known as in ICRD; functional expression studies in yeast show that the mutant has decreased function under growth conditions requiring the TCA cycle and the glyoxylate shunt;, features a modification of the amino acid from S to R at position 112.
+The protein's natural variant, known as in ICRD;, features a modification of the amino acid from G to D at position 259.
+The protein's natural variant, known as in OPA9;, features a modification of the amino acid from G to R at position 661.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from T to N at position 697.
+The protein's natural variant, known as in ICRD;, features a modification of the amino acid from K to N at position 736.
+The protein's natural variant, known as in SMCD;, features a modification of the amino acid from G to E at position 18.
+The protein's natural variant, known as in SMCD;, features a modification of the amino acid from G to R at position 18.
+The protein's natural variant, known as in SMCD, features a modification of the amino acid from Y to D at position 582.
+The protein's natural variant, known as in SMCD;, features a modification of the amino acid from C to R at position 591.
+The protein's natural variant, known as in SMCD and spondylometaphyseal dysplasia Japanese type;, features a modification of the amino acid from G to E at position 595.
+The protein's natural variant, known as in SMCD, features a modification of the amino acid from G to R at position 595.
+The protein's natural variant, known as in SMCD;, features a modification of the amino acid from Y to C at position 597.
+The protein's natural variant, known as in SMCD, features a modification of the amino acid from Y to H at position 597.
+The protein's natural variant, known as in SMCD;, features a modification of the amino acid from Y to D at position 598.
+The protein's natural variant, known as in SMCD;, features a modification of the amino acid from S to P at position 600.
+The protein's natural variant, known as in SMCD;, features a modification of the amino acid from L to P at position 614.
+The protein's natural variant, known as in SMCD, features a modification of the amino acid from N to K at position 617.
+The protein's natural variant, known as in SMCD, features a modification of the amino acid from G to V at position 618.
+The protein's natural variant, known as in SMCD, features a modification of the amino acid from L to R at position 644.
+The protein's natural variant, known as in SMCD, features a modification of the amino acid from D to G at position 648.
+The protein's natural variant, known as in SMCD;, features a modification of the amino acid from W to R at position 651.
+The protein's natural variant, known as in SMCD;, features a modification of the amino acid from Q to P at position 653.
+The protein's natural variant, known as in SMCD;, features a modification of the amino acid from S to P at position 671.
+The protein's natural variant, known as in CDPX1; no effect on arylsulfatase activity, protein stability and localization to the Golgi apparatus;, features a modification of the amino acid from R to S at position 12.
+The protein's natural variant, known as in CDPX1, features a modification of the amino acid from I to N at position 80.
+The protein's natural variant, known as in CDPX1; significant loss of arylsulfatase activity; no effect on protein stability and localization to the Golgi apparatus;, features a modification of the amino acid from R to P at position 111.
+The protein's natural variant, known as in CDPX1;, features a modification of the amino acid from G to R at position 117.
+The protein's natural variant, known as in CDPX1; significant loss of arylsulfatase activity; no effect on protein stability and localization to the Golgi apparatus;, features a modification of the amino acid from G to V at position 137.
+The protein's natural variant, known as in CDPX1; significant loss of arylsulfatase activity; no effect on protein stability and localization to the Golgi apparatus;, features a modification of the amino acid from G to R at position 245.
+The protein's natural variant, known as in CDPX1;, features a modification of the amino acid from T to M at position 481.
+The protein's natural variant, known as in CDPX1; significant loss of arylsulfatase activity; no effect on protein stability and localization to the Golgi apparatus;, features a modification of the amino acid from C to Y at position 492.
+The protein's natural variant, known as in CDPX1;, features a modification of the amino acid from P to S at position 578.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from L to V at position 105.
+The protein's natural variant, known as found in a patient with systemic lupus erythematosus; unknown pathological significance; inhibits TNF-mediated NF-kB activation, features a modification of the amino acid from H to Q at position 198.
+The protein's natural variant, known as found in a patient with autosomal recessive retinitis pigmentosa; unknown pathological significance;, features a modification of the amino acid from G to D at position 301.
+The protein's natural variant, known as in HSNSP;, features a modification of the amino acid from H to R at position 147.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from I to V at position 325.
+The protein's natural variant, known as in a lung squamous cell carcinoma sample; somatic mutation, features a modification of the amino acid from T to S at position 669.
+The protein's natural variant, known as in LGMDR12; unknown pathological significance;, features a modification of the amino acid from N to S at position 52.
+The protein's natural variant, known as in LGMDR12; unknown pathological significance;, features a modification of the amino acid from F to S at position 54.
+The protein's natural variant, known as in LGMDR12; unknown pathological significance;, features a modification of the amino acid from R to W at position 58.
+The protein's natural variant, known as in LGMDR12; unknown pathological significance;, features a modification of the amino acid from V to I at position 87.
+The protein's natural variant, known as in LGMDR12; unknown pathological significance, features a modification of the amino acid from D to E at position 93.
+The protein's natural variant, known as in LGMDR12; unknown pathological significance, features a modification of the amino acid from Y to C at position 143.
+The protein's natural variant, known as in LGMDR12; unknown pathological significance;, features a modification of the amino acid from E to K at position 202.
+The protein's natural variant, known as in LGMDR12; unknown pathological significance;, features a modification of the amino acid from T to A at position 206.
+The protein's natural variant, known as in LGMDR12; unknown pathological significance;, features a modification of the amino acid from G to V at position 231.
+The protein's natural variant, known as in LGMDR12; unknown pathological significance, features a modification of the amino acid from K to N at position 259.
+The protein's natural variant, known as in LGMDR12; unknown pathological significance;, features a modification of the amino acid from N to S at position 265.
+The protein's natural variant, known as in LGMDR12; unknown pathological significance;, features a modification of the amino acid from P to L at position 266.
+The protein's natural variant, known as in LGMDR12; unknown pathological significance;, features a modification of the amino acid from T to S at position 267.
+The protein's natural variant, known as in GDD;, features a modification of the amino acid from C to G at position 356.
+The protein's natural variant, known as in GDD;, features a modification of the amino acid from C to R at position 356.
+The protein's natural variant, known as in GDD, features a modification of the amino acid from C to Y at position 356.
+The protein's natural variant, known as in LGMDR12; unknown pathological significance, features a modification of the amino acid from R to L at position 404.
+The protein's natural variant, known as in LGMDR12; unknown pathological significance;, features a modification of the amino acid from S to G at position 506.
+The protein's natural variant, known as in GDD; unknown pathological significance;, features a modification of the amino acid from T to I at position 513.
+The protein's natural variant, known as in LGMDR12; unknown pathological significance;, features a modification of the amino acid from R to Q at position 547.
+The protein's natural variant, known as in LGMDR12; unknown pathological significance;, features a modification of the amino acid from S to I at position 555.
+The protein's natural variant, known as in LGMDR12; unknown pathological significance;, features a modification of the amino acid from F to S at position 578.
+The protein's natural variant, known as in LGMDR12; unknown pathological significance;, features a modification of the amino acid from M to I at position 618.
+The protein's natural variant, known as in MMD3; unknown pathological significance;, features a modification of the amino acid from W to C at position 655.
+The protein's natural variant, known as in LGMDR12; unknown pathological significance;, features a modification of the amino acid from T to S at position 714.
+The protein's natural variant, known as in MMD3 and LGMDR12; unknown pathological significance;, features a modification of the amino acid from R to C at position 758.
+The protein's natural variant, known as in LGMDR12; unknown pathological significance, features a modification of the amino acid from L to P at position 781.
+The protein's natural variant, known as in LGMDR12; unknown pathological significance;, features a modification of the amino acid from S to L at position 796.
+The protein's natural variant, known as in LGMDR12; unknown pathological significance;, features a modification of the amino acid from C to S at position 804.
+The protein's natural variant, known as in LGMDR12; unknown pathological significance;, features a modification of the amino acid from A to V at position 830.
+The protein's natural variant, known as in LGMDR12; unknown pathological significance;, features a modification of the amino acid from M to K at position 833.
+The protein's natural variant, known as in LGMDR12; unknown pathological significance, features a modification of the amino acid from M to R at position 839.
+The protein's natural variant, known as in LGMDR12; unknown pathological significance;, features a modification of the amino acid from M to L at position 900.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from A to E at position 112.
+The protein's natural variant, known as in strain: Isolate TK 44636, features a modification of the amino acid from F to V at position 303.
+The protein's natural variant, known as in CTRCT12;, features a modification of the amino acid from R to W at position 287.
+The protein's natural variant, known as in CTRCT12; unknown pathological significance;, features a modification of the amino acid from A to E at position 379.
+The protein's natural variant, known as in strain: CPA-46, features a modification of the amino acid from R to P at position 29.
+The protein's natural variant, known as in strain: CPA-46, features a modification of the amino acid from N to K at position 236.
+The protein's natural variant, known as no effect on glycosylation; no effect on transport activity; no effect on plasma membrane localization;, features a modification of the amino acid from R to H at position 19.
+The protein's natural variant, known as in dry earwax and lack of axillary odor phenotype; loss of N-glycosylation; strongly reduced plasma membrane localization; no DHEAS transport and largely reduced estrone 3-sulfate transport; decreased protein concentration in axillary sweat;, features a modification of the amino acid from G to R at position 180.
+The protein's natural variant, known as no effect on glycosylation; no effect on transport activity; no effect on plasma membrane localization;, features a modification of the amino acid from A to E at position 317.
+The protein's natural variant, known as significantly decreased transport activity of DHEAS and estrone 3-sulfate; no effect on glycosylation; reduced ATP-dependent 5-FdUMP transport; no effect on plasma membrane localization;, features a modification of the amino acid from T to M at position 546.
+The protein's natural variant, known as no effect on glycosylation;, features a modification of the amino acid from R to W at position 630.
+The protein's natural variant, known as no effect on glycosylation; no effect on transport activity; no effect on plasma membrane localization;, features a modification of the amino acid from V to I at position 648.
+The protein's natural variant, known as no effect on glycosylation;, features a modification of the amino acid from V to I at position 687.
+The protein's natural variant, known as no effect on glycosylation;, features a modification of the amino acid from K to R at position 735.
+The protein's natural variant, known as no effect on glycosylation;, features a modification of the amino acid from M to V at position 970.
+The protein's natural variant, known as no effect on glycosylation; no effect on transport activity; no effect on plasma membrane localization;, features a modification of the amino acid from H to R at position 1344.
+The protein's natural variant, known as in RDMS;, features a modification of the amino acid from C to Y at position 61.
+The protein's natural variant, known as in SMDAX; patients may exhibit clinical features overlapping with Jeune syndrome; decreased function in ciliogenesis; abolishes interaction with NEK1;, features a modification of the amino acid from R to P at position 73.
+The protein's natural variant, known as in RDMS;, features a modification of the amino acid from Y to C at position 107.
+The protein's natural variant, known as in SMDAX; increases protein degradation; changes protein localization;, features a modification of the amino acid from Y to H at position 107.
+The protein's natural variant, known as in SMDAX; increases protein degradation; changes protein localization;, features a modification of the amino acid from V to M at position 111.
+The protein's natural variant, known as in SMDAX;, features a modification of the amino acid from P to L at position 116.
+The protein's natural variant, known as in SMDAX; abolishes interaction with NEK1;, features a modification of the amino acid from L to P at position 224.
+The protein's natural variant, known as in EXT1; no loss of activity, features a modification of the amino acid from Q to K at position 27.
+The protein's natural variant, known as in EXT1; loss of activity, features a modification of the amino acid from D to H at position 164.
+The protein's natural variant, known as in isolated osteochondroma; somatic mutation, features a modification of the amino acid from MLAKASIS to I at position 222.
+The protein's natural variant, known as in EXT1; loss of activity;, features a modification of the amino acid from R to G at position 280.
+The protein's natural variant, known as in EXT1; loss of activity;, features a modification of the amino acid from R to S at position 280.
+The protein's natural variant, known as in chondrosarcoma; no loss of activity, features a modification of the amino acid from N to S at position 316.
+The protein's natural variant, known as in EXT1; loss of activity;, features a modification of the amino acid from G to D at position 339.
+The protein's natural variant, known as in EXT1; loss of activity; still able to form an oligomeric complex;, features a modification of the amino acid from R to C at position 340.
+The protein's natural variant, known as in EXT1; loss of activity;, features a modification of the amino acid from R to H at position 340.
+The protein's natural variant, known as in EXT1; loss of activity;, features a modification of the amino acid from R to L at position 340.
+The protein's natural variant, known as in EXT1; loss of activity, features a modification of the amino acid from R to S at position 340.
+The protein's natural variant, known as in EXT1; no loss of activity;, features a modification of the amino acid from A to V at position 486.
+The protein's natural variant, known as in EXT1; no loss of activity, features a modification of the amino acid from P to L at position 496.
+The protein's natural variant, known as found in a patient with Bazex syndrome; unknown pathological significance, features a modification of the amino acid from E to K at position 124.
+The protein's natural variant, known as may be associated with susceptibility to spermatogenic failure in Asian individuals; this substitution may lead to affect the DAZL transcript stability and prevent its translation;, features a modification of the amino acid from T to A at position 54.
+The protein's natural variant, known as severely impaired RNA-binding, features a modification of the amino acid from R to G at position 115.
+The protein's natural variant, known as in strain: YPH499, features a modification of the amino acid from H to R at position 171.
+The protein's natural variant, known as in strain: YPH499; lack of gamma-glutamyl transferase activity, features a modification of the amino acid from G to D at position 494.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from G to D at position 212.
+The protein's natural variant, known as in SSFSC2; decreased homodimerization; does not affect heterodimerization with SCUBE1 or SCUBE2; does not affect localization to the cell surface;, features a modification of the amino acid from C to W at position 97.
+The protein's natural variant, known as in SSFSC2; unknown pathological significance;, features a modification of the amino acid from G to D at position 204.
+The protein's natural variant, known as in SSFSC2; loss of stimulation of BMP signaling; does not affect localization to the cell surface;, features a modification of the amino acid from I to T at position 815.
+The protein's natural variant, known as in CANDF6;, features a modification of the amino acid from S to L at position 95.
+The protein's natural variant, known as in strain: SR-11, RKS2985, RKS2993, RKS2995, RKS3013, RKS3014, RKS3015, RKS3057, RKS3333 and RKS4194, features a modification of the amino acid from S to T at position 263.
+The protein's natural variant, known as in strain: RKS3013, RKS3014 and RKS3015, features a modification of the amino acid from S to A at position 306.
+The protein's natural variant, known as in strain: RKS2985, RKS2993, RKS2995, RKS3013, RKS3014, RKS3015 and RKS3057, features a modification of the amino acid from S to T at position 344.
+The protein's natural variant, known as in strain: RKS3013, RKS3014 and RKS3015, features a modification of the amino acid from S to N at position 369.
+The protein's natural variant, known as in strain: RKS2985, RKS2993, RKS2995, RKS3013, RKS3014, RKS3015 and RKS3057, features a modification of the amino acid from E to D at position 381.
+The protein's natural variant, known as in strain: RKS2995 and RKS3057, features a modification of the amino acid from E to D at position 404.
+The protein's natural variant, known as in strain: RKS3013, RKS3014 and RKS3015, features a modification of the amino acid from D to S at position 407.
+The protein's natural variant, known as in strain: RKS2995 and RKS3057, features a modification of the amino acid from V to I at position 412.
+The protein's natural variant, known as in strain: RKS2985, RKS2993, RKS2995, RKS3013, RKS3014, RKS3015 and RKS3057, features a modification of the amino acid from V to A at position 440.
+The protein's natural variant, known as in strain: RKS3013, RKS3014 and RKS3015, features a modification of the amino acid from IHQ to TYH at position 450.
+The protein's natural variant, known as in strain: RKS2985, RKS2993, RKS2995 and RKS3057, features a modification of the amino acid from I to T at position 448.
+The protein's natural variant, known as in strain: RKS3013, RKS3014 and RKS3015, features a modification of the amino acid from R to Q at position 475.
+The protein's natural variant, known as in strain: SR-11, RKS2985, RKS2993, RKS2995, RKS3057, RKS3333 and RKS4194, features a modification of the amino acid from L to V at position 489.
+The protein's natural variant, known as in strain: RKS2985 and RKS2993, features a modification of the amino acid from V to I at position 600.
+The protein's natural variant, known as in strain: RKS3013, RKS3014 and RKS3015, features a modification of the amino acid from D to E at position 617.
+The protein's natural variant, known as in strain: LT7, features a modification of the amino acid from A to S at position 126.
+The protein's natural variant, known as in B form, features a modification of the amino acid from V to L at position 522.
+The protein's natural variant, known as in B form, features a modification of the amino acid from S to F at position 530.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from R to Q at position 936.
+The natural variant of this protein is characterized by an amino acid alteration from W to R at position 103.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 208.
+The protein's natural variant, known as 70% to 80% decrease in activity, features a modification of the amino acid from R to W at position 451.
+The natural variant of this protein is characterized by an amino acid alteration from R to G at position 702.
+The natural variant of this protein is characterized by an amino acid alteration from L to F at position 779.
+The natural variant of this protein is characterized by an amino acid alteration from H to P at position 825.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from F to S at position 1036.
+The protein's natural variant, known as in MYOFTA; no protein detected by western blot in patient muscle;, features a modification of the amino acid from M to R at position 163.
+The protein's natural variant, known as in AAKAD; unknown pathological significance; requires 2 nucleotide substitutions, features a modification of the amino acid from L to G at position 234.
+The protein's natural variant, known as in AAKAD; unknown pathological significance;, features a modification of the amino acid from Q to H at position 305.
+The protein's natural variant, known as in AAKAD; unknown pathological significance;, features a modification of the amino acid from R to Q at position 455.
+The protein's natural variant, known as in AAKAD; decreased interaction with DLST;, features a modification of the amino acid from R to C at position 715.
+The protein's natural variant, known as in AAKAD; affects the overall activity of OADHC complex; affects assembly with DLST leading to impaired channeling of reaction intermediates;, features a modification of the amino acid from G to R at position 729.
+The protein's natural variant, known as in AAKAD; unknown pathological significance; thermally more labile than wild-type protein;, features a modification of the amino acid from P to L at position 773.
+The protein's natural variant, known as in AAKAD; unknown pathological significance, features a modification of the amino acid from S to P at position 777.
+The protein's natural variant, known as in early-onset obesity; Japanese population; loss of methylation and repressor activity;, features a modification of the amino acid from R to W at position 57.
+The protein's natural variant, known as in early-onset obesity; Japanese population; strong decrease of repressor activity;, features a modification of the amino acid from G to E at position 189.
+The protein's natural variant, known as in early-onset obesity; Japanese population; slight decrease of repressor activity;, features a modification of the amino acid from A to S at position 195.
+The protein's natural variant, known as in early-onset obesity; Japanese population; loss of repressor activity;, features a modification of the amino acid from R to C at position 213.
+The protein's natural variant, known as no effect on repressor activity;, features a modification of the amino acid from R to H at position 216.
+The protein's natural variant, known as in mutant rodC1; temperature-sensitive, features a modification of the amino acid from S to F at position 644.
+The protein's natural variant, known as in DFNB6;, features a modification of the amino acid from R to C at position 81.
+The protein's natural variant, known as in DFNB6;, features a modification of the amino acid from R to W at position 84.
+The protein's natural variant, known as in DFNB6;, features a modification of the amino acid from R to W at position 92.
+The protein's natural variant, known as in strain: 178.7, 357F, 517S, Bar-F-77F, Bar-F-79F, Bar-F-96S, DPF-13, DPF-30, DPF-82.1, EM-10, F-274F, F-517F, F-1461S, MA-4.4 and Zim-F-H31, features a modification of the amino acid from I to T at position 10.
+The protein's natural variant, known as in strain: 178.7, 377F, 357F, 517S, Bar-F-79F, DPF-13, DPF-30, DPF-82.1, EM-10, F-274F, F-517F, F-775F, F-1461S, MA-4.4, Ven-S-13F, Zim-F-H27, Zim-F-H31, Zim-F-S11, Zim-F-S18, Zim-F-S53, Zim-S-S2, Zim-S-S30 and Zim-S-S34, features a modification of the amino acid from T to I at position 24.
+The protein's natural variant, known as in strain: Zim-S-H13, features a modification of the amino acid from P to S at position 33.
+The protein's natural variant, known as in strain: 178.7, 357F, 517S, Bar-F-77F, Bar-F-79F, Bar-F-96S, DPF-13, DPF-30, DPF-82.1, EM-10, F-274F, F-1461S, MA-4.2, VC-805, Ven-S-1F, Ven-S-2F, Ven-S-3F, Ven-S-11F, Ven-S-21F, Zim-F-H31, Zim-F-S18 and Zim-S-S10, features a modification of the amino acid from T to I at position 58.
+The protein's natural variant, known as in strain: DPF-2 and 521S, features a modification of the amino acid from S to T at position 120.
+The protein's natural variant, known as in strain: 178.7, 357F, 517S, 709.6, Bar-F-7F, Bar-F-77F, Bar-F-79F, Bar-F-93F, Bar-F-96S, DPF-13, DPF-30, DPF-46, DPF-77, DPF-82.1, EM-10, F-96S, F-274F, F-517F, F-531F, F-611F, F-775F, F-1461S, MA-4.2, Zim-F-H27, Zim-F-H31, Zim-F-S11, Zim-F-S18 and Zim-F-S53, features a modification of the amino acid from N to D at position 258.
+The protein's natural variant, known as in strain: 174F, 178.7, 357F, 517S, 709.6, Bar-F-7F, Bar-F-77F, Bar-F-79F, Bar-F-93F, Bar-F-96S, Bar-S-24F, Bar-S-60F, Bar-S-78F, Bar-S-89F, Bar-S-99F, Bar-S-95F, DPF-13, DPF-30, DPF-46, DPF-77, DPF-82.1, EM-10, F-96S, F-274F, F-517F, F-531F, S-549S, F-611F, F-775F, F-1461S, MA-4.2, S-114S, S-2588S, VC-815, Ven-S-1F, Ven-S-2F, Ven-S-3F, Ven-S-4F, Ven-S-11F, Ven-S-21F, Zim-F-H27, Zim-F-H31, Zim-F-S11, Zim-F-S18, Zim-F-S53, Zim-S-S34 and Zim-S-44F, features a modification of the amino acid from T to A at position 268.
+The protein's natural variant, known as in strain: VC-805, features a modification of the amino acid from S to P at position 276.
+The protein's natural variant, known as in strain: Ven-S-13F, features a modification of the amino acid from A to V at position 309.
+The protein's natural variant, known as in strain: F-775F, features a modification of the amino acid from I to T at position 356.
+The protein's natural variant, known as in strain: F-775F, features a modification of the amino acid from E to D at position 363.
+The protein's natural variant, known as in strain: F-775F, features a modification of the amino acid from Y to H at position 371.
+The protein's natural variant, known as in strain: Zim-S-S34, features a modification of the amino acid from R to G at position 376.
+The protein's natural variant, known as in strain: Ven-S-13F and Zim-F-S18, features a modification of the amino acid from E to D at position 394.
+The protein's natural variant, known as in strain: US-255F, features a modification of the amino acid from G to R at position 397.
+The protein's natural variant, known as in strain: 357F, 517S, Bar-F-7F, Bar-F-77F, Bar-F-79F, Bar-F-93F, Bar-F-96S, DPF-13, DPF-30, F-96S, F-274F, F-517F, F-1461S, S-114S, S-549S, S-2588S, VC-805, Ven-S-4F, Zim-S-S2, Zim-S-S30 and Zim-S-S34, features a modification of the amino acid from L to V at position 409.
+The protein's natural variant, known as in strain: Zim-F-S53, features a modification of the amino acid from V to I at position 441.
+The protein's natural variant, known as in strain: 94F, 174F, Bar-S-24F, Bar-S-89F, Bar-S-99F, Bar-S-95F, Bar-S-60F, F-531F, F-611F, MA-4.2, Zim-F-H27, Zim-F-S18 and Zim-S-44F, features a modification of the amino acid from R to K at position 492.
+The protein's natural variant, known as in strain: Zim-F-S18, Zim-S-H32 and Zim-S-S2, features a modification of the amino acid from D to N at position 500.
+The protein's natural variant, known as in strain: 357F, 517S, Bar-F-79F, Bar-S-78F, DPF-13, DPF-30, F-96S, F-517F, F-1461S, MA-4.2, VC-805, Ven-S-1F, Ven-S-2F, Ven-S-3F, Ven-S-11F, Ven-S-21F and Zim-F-S11, features a modification of the amino acid from S to A at position 508.
+The protein's natural variant, known as in strain: Canton-S, features a modification of the amino acid from I to L at position 60.
+The protein's natural variant, known as in strain: Canton-S, features a modification of the amino acid from T to I at position 69.
+The protein's natural variant, known as in CPVT6; decreased calcium-binding affinity; not changed binding to RYR2; increased RYR2 calcium-release channel activity; decreased calcium-dependent inactivation of L-type calcium channel; not changed action potential duration, features a modification of the amino acid from A to V at position 103.
+The protein's natural variant, known as in LQT16, features a modification of the amino acid from D to G at position 130.
+The protein's natural variant, known as in LQT16; loss-of-function variant causing impaired negative regulation of high voltage-gated calcium channel activity; impaired regulation of cardiac muscle cell action potential; decreased calcium ion binding, features a modification of the amino acid from E to K at position 141.
+The protein's natural variant, known as in strain: 775met9, features a modification of the amino acid from D to G at position 104.
+The protein's natural variant, known as in RCAD; gain-of-function mutation;, features a modification of the amino acid from S to F at position 36.
+The protein's natural variant, known as in RCAD;, features a modification of the amino acid from V to G at position 61.
+The protein's natural variant, known as in RCAD; unknown pathological significance;, features a modification of the amino acid from G to C at position 76.
+The protein's natural variant, known as in RCAD;, features a modification of the amino acid from V to G at position 110.
+The protein's natural variant, known as in RCAD, features a modification of the amino acid from R to P at position 112.
+The protein's natural variant, known as in RCAD, features a modification of the amino acid from Q to E at position 136.
+The protein's natural variant, known as in RCAD, features a modification of the amino acid from S to L at position 148.
+The protein's natural variant, known as in RCAD;, features a modification of the amino acid from S to W at position 148.
+The protein's natural variant, known as in RCAD, features a modification of the amino acid from S to P at position 151.
+The protein's natural variant, known as in RCAD; has diminished transcriptional activity by loss of DNA binding activity, features a modification of the amino acid from H to N at position 153.
+The protein's natural variant, known as in RCAD; no impact on interaction with PCBD1; reduced coactivation by PCBD1, features a modification of the amino acid from K to E at position 156.
+The protein's natural variant, known as in RCAD, features a modification of the amino acid from K to Q at position 164.
+The protein's natural variant, known as in RCAD;, features a modification of the amino acid from R to H at position 165.
+The protein's natural variant, known as in RCAD, features a modification of the amino acid from R to Q at position 235.
+The protein's natural variant, known as in RCAD;, features a modification of the amino acid from A to T at position 241.
+The protein's natural variant, known as in RCAD; insignificant differences in transactivation ability between wild-type and mutated HNF1B;, features a modification of the amino acid from E to D at position 260.
+The protein's natural variant, known as in RCAD; no impact on interaction with PCBD1; reduced coactivation by PCBD1, features a modification of the amino acid from R to G at position 276.
+The protein's natural variant, known as in RCAD, features a modification of the amino acid from R to Q at position 276.
+The protein's natural variant, known as in RCAD, features a modification of the amino acid from G to D at position 285.
+The protein's natural variant, known as in RCAD, features a modification of the amino acid from R to C at position 295.
+The protein's natural variant, known as in RCAD;, features a modification of the amino acid from R to H at position 295.
+The protein's natural variant, known as in RCAD, features a modification of the amino acid from R to P at position 295.
+The protein's natural variant, known as in RCAD;, features a modification of the amino acid from G to S at position 370.
+The protein's natural variant, known as in T2D; 22% reduction in activity;, features a modification of the amino acid from S to R at position 465.
+The protein's natural variant, known as in diabetes; early onset association; unknown pathological significance;, features a modification of the amino acid from G to S at position 492.
+The protein's natural variant, known as in strain: cv. Baekmibaekdadagi, features a modification of the amino acid from D to Y at position 71.
+The protein's natural variant, known as in strain: cv. Baekmibaekdadagi, features a modification of the amino acid from STYQ to YKYR at position 120.
+The protein's natural variant, known as in CLN8; associated with M-170 on the same allele;, features a modification of the amino acid from L to M at position 16.
+The protein's natural variant, known as in CLN8NE;, features a modification of the amino acid from R to G at position 24.
+The protein's natural variant, known as in CLN8;, features a modification of the amino acid from A to P at position 30.
+The protein's natural variant, known as in CLN8;, features a modification of the amino acid from R to H at position 70.
+The protein's natural variant, known as in CLN8;, features a modification of the amino acid from Q to R at position 76.
+The protein's natural variant, known as in CLN8;, features a modification of the amino acid from I to S at position 107.
+The protein's natural variant, known as in CLN8;, features a modification of the amino acid from H to Y at position 139.
+The protein's natural variant, known as in CLN8;, features a modification of the amino acid from Y to C at position 158.
+The protein's natural variant, known as in CLN8; associated with M-16 on the same allele;, features a modification of the amino acid from T to M at position 170.
+The protein's natural variant, known as in CLN8;, features a modification of the amino acid from Q to R at position 194.
+The protein's natural variant, known as in CLN8;, features a modification of the amino acid from R to C at position 204.
+The protein's natural variant, known as in CLN8;, features a modification of the amino acid from R to L at position 204.
+The protein's natural variant, known as in CLN8; unknown pathological significance;, features a modification of the amino acid from L to R at position 207.
+The protein's natural variant, known as in CLN8;, features a modification of the amino acid from G to S at position 221.
+The protein's natural variant, known as in CLN8;, features a modification of the amino acid from G to R at position 237.
+The protein's natural variant, known as in CLN8;, features a modification of the amino acid from W to C at position 263.
+The protein's natural variant, known as in CLN8;, features a modification of the amino acid from E to V at position 269.
+The protein's natural variant, known as in SPGF41; unknown pathological significance, features a modification of the amino acid from F to I at position 60.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from G to A at position 59.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from V to A at position 84.
+The protein's natural variant, known as in PAICSD; unknown pathological significance; no effect on protein abundance; decreased phosphoribosylaminoimidazole carboxylase activity; decreased phosphoribosylaminoimidazolesuccinocarboxamide synthase activity;, features a modification of the amino acid from K to R at position 53.
+The protein's natural variant, known as requires 2 nucleotide substitutions, features a modification of the amino acid from C to L at position 69.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 36.
+The natural variant of this protein is characterized by an amino acid alteration from E to Q at position 102.
+The protein's natural variant, known as in strain: NCTC 11906, features a modification of the amino acid from A to V at position 226.
+The protein's natural variant, known as in IMD93; unknown pathological significance, features a modification of the amino acid from S to N at position 1118.
+The protein's natural variant, known as in the alpha form, features a modification of the amino acid from E to Q at position 133.
+The protein's natural variant, known as in RNA edited version, Sarafotoxin-i3, features a modification of the amino acid from I to V at position 106.
+The protein's natural variant, known as in CATMANS;, features a modification of the amino acid from E to G at position 90.
+The protein's natural variant, known as in CATMANS;, features a modification of the amino acid from F to L at position 98.
+The protein's natural variant, known as in CATMANS;, features a modification of the amino acid from A to S at position 100.
+The protein's natural variant, known as in CATMANS;, features a modification of the amino acid from Y to H at position 234.
+The protein's natural variant, known as in CATMANS;, features a modification of the amino acid from N to D at position 298.
+The protein's natural variant, known as in strain 2591, features a modification of the amino acid from D to E at position 51.
+The protein's natural variant, known as in strain 2591, features a modification of the amino acid from L to V at position 56.
+The protein's natural variant, known as in strain 2591, features a modification of the amino acid from ALLS to TLLA at position 67.
+The protein's natural variant, known as in strain 2591, features a modification of the amino acid from IAAKAIGKKIHQNNGLDTENNH to VAKKAIGNLIAQNGLNAGANQ at position 93.
+The protein's natural variant, known as in strain 2591, features a modification of the amino acid from A to V at position 103.
+The protein's natural variant, known as in strain 2591, features a modification of the amino acid from KQ to AE at position 110.
+The protein's natural variant, known as in strain 2591, features a modification of the amino acid from EG to SEE at position 119.
+The protein's natural variant, known as in strain 2591, features a modification of the amino acid from DA to ED at position 126.
+The protein's natural variant, known as in strain 2591, features a modification of the amino acid from SET to NKA at position 133.
+The protein's natural variant, known as in strain 2591, features a modification of the amino acid from N to D at position 136.
+The protein's natural variant, known as in strain 2591, features a modification of the amino acid from EKHTD to SSHAE at position 144.
+The protein's natural variant, known as in strain 2591, features a modification of the amino acid from KEGV to IANGAA at position 150.
+The protein's natural variant, known as in strain 2591, features a modification of the amino acid from DAKE to NAKA at position 157.
+The protein's natural variant, known as in strain 2591, features a modification of the amino acid from T to D at position 167.
+The protein's natural variant, known as in strain 2591, features a modification of the amino acid from EELG to QELE at position 174.
+The protein's natural variant, known as in strain 2591, features a modification of the amino acid from EV to KN at position 182.
+The protein's natural variant, known as in strain 2591, features a modification of the amino acid from KEMLA to QETLN at position 192.
+The protein's natural variant, known as in strain 2591, features a modification of the amino acid from S to N at position 206.
+The protein's natural variant, known as 2.5-fold increase in affinity for indolepropinoic acyl-adenylate and cytosine; 2-fold decrease in hypoxanthine affinity; nearly no change in affinity for adenine, guanine and uracil;, features a modification of the amino acid from G to A at position 36.
+The protein's natural variant, known as in transposon Tn3411, features a modification of the amino acid from I to V at position 88.
+The protein's natural variant, known as in transposon Tn3411, features a modification of the amino acid from L to W at position 316.
+The protein's natural variant, known as in transposon Tn3411, features a modification of the amino acid from T to A at position 414.
+The protein's natural variant, known as in transposon Tn3411, features a modification of the amino acid from A to V at position 418.
+The protein's natural variant, known as in transposon Tn3411, features a modification of the amino acid from S to R at position 422.
+The protein's natural variant, known as in transposon Tn3411, features a modification of the amino acid from V to A at position 427.
+The protein's natural variant, known as in CMD1Y;, features a modification of the amino acid from E to K at position 40.
+The protein's natural variant, known as in CMD1Y;, features a modification of the amino acid from E to K at position 54.
+The protein's natural variant, known as in CMH3;, features a modification of the amino acid from A to V at position 63.
+The protein's natural variant, known as in CMH3; no change in homodimerization; no change in homodimer thermal stability; decreased actin binding; recessive effect in the homodimer; increased calcium-dependent regulation of myosin binding to actin filaments; dominant effect in the homodimer;, features a modification of the amino acid from D to N at position 175.
+The protein's natural variant, known as in CMH3; no change in homodimerization; decreased in hom odimer thermal stability; decreased in actin binding; increased calcium-dependent regulation of myosin binding to actin filaments; dominant effect in the homodimer;, features a modification of the amino acid from E to G at position 180.
+The protein's natural variant, known as in CMH3;, features a modification of the amino acid from E to V at position 180.
+The protein's natural variant, known as in LVNC9;, features a modification of the amino acid from E to K at position 192.
+The protein's natural variant, known as in LVNC9;, features a modification of the amino acid from K to E at position 248.
+The protein's natural variant, known as in GS2; does not affect GTP binding; cannot interact with MLPH; significant reduction in interaction with UNC13D; abolishes localization to lysosomes;, features a modification of the amino acid from W to G at position 73.
+The protein's natural variant, known as in GS2; strongly affects GTP binding; cannot interact with MLPH;, features a modification of the amino acid from L to P at position 130.
+The protein's natural variant, known as in GS2; interferes with melanosome transport;, features a modification of the amino acid from A to P at position 152.
+The protein's natural variant, known as in strain: BM12987 / O24, features a modification of the amino acid from A to T at position 206.
+The protein's natural variant, known as in strain: 80s-2 and BM12987 / O24, features a modification of the amino acid from I to T at position 207.
+The protein's natural variant, known as in strain: BM12987 / O24, features a modification of the amino acid from H to E at position 329.
+The protein's natural variant, known as in strain: BM12987 / O24, features a modification of the amino acid from T to S at position 595.
+The protein's natural variant, known as in strain: 80s-2, features a modification of the amino acid from E to D at position 599.
+The protein's natural variant, known as in strain: BM12987 / O24, features a modification of the amino acid from D to V at position 616.
+The protein's natural variant, known as in strain: 80s-2, features a modification of the amino acid from I to N at position 698.
+The protein's natural variant, known as in strain: BM12987 / O24, features a modification of the amino acid from R to H at position 876.
+The protein's natural variant, known as in strain: BM12987 / O24, features a modification of the amino acid from D to E at position 967.
+The protein's natural variant, known as in strain: BM12987 /O24, features a modification of the amino acid from S to SESDSDSESDSDSDSDSDSDSDS at position 990.
+The protein's natural variant, known as in strain: 80s-2, features a modification of the amino acid from D to DSDSDSD at position 1089.
+The protein's natural variant, known as in strain: ECOR 45B1, features a modification of the amino acid from ERR to ARG at position 38.
+The protein's natural variant, known as in strain: ECOR 35D, features a modification of the amino acid from Q to K at position 124.
+The protein's natural variant, known as in strain: ECOR 34B1 and ECOR 37UG, features a modification of the amino acid from N to S at position 132.
+The protein's natural variant, known as in strain: ECOR 70B1, features a modification of the amino acid from Q to H at position 135.
+The protein's natural variant, known as in strain: ECOR 37UG, features a modification of the amino acid from P to S at position 170.
+The protein's natural variant, known as in strain: ECOR 45B1, ECOR 46D, ECOR 49D and ECOR 50D, features a modification of the amino acid from A to T at position 171.
+The protein's natural variant, known as in strain: ECOR 37UG, features a modification of the amino acid from L to F at position 176.
+The protein's natural variant, known as in strain: ECOR 59B2, features a modification of the amino acid from G to S at position 201.
+The protein's natural variant, known as in strain: ECOR 37UG, ECOR 45B1, ECOR 51B2, ECOR 52B2, ECOR 58B1 and ECOR 70B1, features a modification of the amino acid from M to I at position 210.
+The protein's natural variant, known as in strain: ECOR 35D, ECOR 46D, ECOR 49D, ECOR 50D, ECOR 57B2, ECOR 59B2, ECOR 60B2 and ECOR 62B2, features a modification of the amino acid from M to T at position 210.
+The protein's natural variant, known as in strain: ECOR 59B2 and ECOR 60B2, features a modification of the amino acid from R to C at position 225.
+The protein's natural variant, known as in strain: ECOR 57B2, ECOR 59B2, ECOR 60B2 and ECOR 62B2, features a modification of the amino acid from A to S at position 310.
+The protein's natural variant, known as in strain: ECOR 35D, features a modification of the amino acid from D to N at position 321.
+The natural variant of this protein is characterized by an amino acid alteration from H to S at position 143.
+The natural variant of this protein is characterized by an amino acid alteration from K to R at position 158.
+The natural variant of this protein is characterized by an amino acid alteration from S to R at position 177.
+The natural variant of this protein is characterized by an amino acid alteration from P to V at position 187.
+The natural variant of this protein is characterized by an amino acid alteration from V to A at position 203.
+The protein's natural variant, known as in PFIC8; unknown pathological significance, features a modification of the amino acid from V to M at position 337.
+The protein's natural variant, known as in PFIC8; unknown pathological significance, features a modification of the amino acid from R to Q at position 352.
+The protein's natural variant, known as in PTORCH3; increased cellular sensitivity to type IIFNs; fails to appropriately traffic USP18 thereby preventing USP18 to inhibit responses to IFN-I, features a modification of the amino acid from R to Q at position 148.
+The protein's natural variant, known as in PTORCH3; increased cellular sensitivity to type IIFNs; loss of interaction with USP18 thereby preventing USP18 to inhibit responses to IFN-I;, features a modification of the amino acid from R to W at position 148.
+The protein's natural variant, known as in HTX10; loss of panaxonemal expression in respiratory cilia;, features a modification of the amino acid from G to R at position 271.
+The protein's natural variant, known as in HTX5;, features a modification of the amino acid from R to Q at position 183.
+The protein's natural variant, known as in HTX5; likely benign variant; decrease in signal transduction;, features a modification of the amino acid from E to K at position 203.
+The protein's natural variant, known as in HTX5; decrease in signal transduction;, features a modification of the amino acid from G to R at position 260.
+The protein's natural variant, known as in HTX5; decrease in signal transduction;, features a modification of the amino acid from R to C at position 275.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from E to K at position 279.
+The protein's natural variant, known as in HTX5; decrease in signal transduction;, features a modification of the amino acid from V to F at position 284.
+The protein's natural variant, known as in ADLI; impairs filaggrin cleavage, features a modification of the amino acid from K to E at position 199.
+The protein's natural variant, known as in ADLI; impairs filaggrin cleavage, features a modification of the amino acid from R to P at position 311.
+The protein's natural variant, known as in ADLI; impairs filaggrin cleavage, features a modification of the amino acid from P to T at position 314.
+The protein's natural variant, known as in TDH2A, features a modification of the amino acid from A to P at position 53.
+The protein's natural variant, known as in TDH2A; loss of activity;, features a modification of the amino acid from D to N at position 240.
+The protein's natural variant, known as in TDH2A, features a modification of the amino acid from N to T at position 307.
+The protein's natural variant, known as in TDH2A;, features a modification of the amino acid from A to T at position 326.
+The protein's natural variant, known as in TDH2A;, features a modification of the amino acid from E to K at position 378.
+The protein's natural variant, known as in TDH2A; unknown pathological significance;, features a modification of the amino acid from R to H at position 412.
+The protein's natural variant, known as in TDH2A;, features a modification of the amino acid from V to M at position 433.
+The protein's natural variant, known as in TDH2A;, features a modification of the amino acid from I to F at position 447.
+The protein's natural variant, known as in TDH2A;, features a modification of the amino acid from Y to D at position 453.
+The protein's natural variant, known as in TDH2A;, features a modification of the amino acid from L to P at position 458.
+The protein's natural variant, known as in TDH2A;, features a modification of the amino acid from R to H at position 491.
+The protein's natural variant, known as in TDH2A;, features a modification of the amino acid from G to S at position 493.
+The protein's natural variant, known as in TDH2A;, features a modification of the amino acid from P to L at position 499.
+The protein's natural variant, known as in TDH2A;, features a modification of the amino acid from W to C at position 527.
+The protein's natural variant, known as in TDH2A; partial defect; expression slightly lower in efficiency and more degenerative than wild-type enzyme, features a modification of the amino acid from G to C at position 533.
+The protein's natural variant, known as in TDH2A;, features a modification of the amino acid from G to S at position 590.
+The protein's natural variant, known as in TDH2A;, features a modification of the amino acid from R to Q at position 648.
+The protein's natural variant, known as in TDH2A;, features a modification of the amino acid from Q to E at position 660.
+The protein's natural variant, known as in TDH2A; fails to localize to the plasma membrane;, features a modification of the amino acid from R to W at position 665.
+The protein's natural variant, known as in TDH2A;, features a modification of the amino acid from R to W at position 693.
+The protein's natural variant, known as in TDH2A; fails to localize to the plasma membrane;, features a modification of the amino acid from G to R at position 771.
+The protein's natural variant, known as in TDH2A, features a modification of the amino acid from D to Y at position 796.
+The protein's natural variant, known as in TDH2A;, features a modification of the amino acid from E to K at position 799.
+The protein's natural variant, known as in TDH2A;, features a modification of the amino acid from C to R at position 808.
+The protein's natural variant, known as in TDH2A;, features a modification of the amino acid from V to I at position 839.
+The protein's natural variant, known as found in patients with early-onset Alzheimer disease; unknown pathological significance; associated in cis with L-55 in some patients;, features a modification of the amino acid from G to E at position 2.
+The protein's natural variant, known as found in patients with early-onset Alzheimer disease; unknown pathological significance;, features a modification of the amino acid from R to C at position 23.
+The protein's natural variant, known as found in patients with early-onset Alzheimer disease; unknown pathological significance;, features a modification of the amino acid from V to A at position 47.
+The protein's natural variant, known as found in patients with early-onset Alzheimer disease; unknown pathological significance; causes reduced expression; also leads to reduced expression of TREM2, features a modification of the amino acid from D to DPADGRLVLGDRDGR at position 50.
+The protein's natural variant, known as found in patients with early-onset Alzheimer disease; unknown pathological significance; associated in cis with E-2 in some patients;, features a modification of the amino acid from V to L at position 55.
+The protein's natural variant, known as found in patients with early-onset Alzheimer disease; unknown pathological significance;, features a modification of the amino acid from R to W at position 80.
+The protein's natural variant, known as found in patients with early-onset Alzheimer disease; unknown pathological significance, features a modification of the amino acid from I to V at position 84.
+The protein's natural variant, known as found in patients with early-onset Alzheimer disease; unknown pathological significance;, features a modification of the amino acid from S to L at position 89.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from V to F at position 137.
+The protein's natural variant, known as in PEE4;, features a modification of the amino acid from R to P at position 18.
+The protein's natural variant, known as in PEE4;, features a modification of the amino acid from N to I at position 825.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from K to E at position 152.
+The protein's natural variant, known as no effect on DNA ligase activity;, features a modification of the amino acid from R to H at position 409.
+The protein's natural variant, known as no effect on DNA ligase activity;, features a modification of the amino acid from P to L at position 529.
+The protein's natural variant, known as in IMD96; loss of DNA ligase activity;, features a modification of the amino acid from E to K at position 566.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from S to L at position 612.
+The protein's natural variant, known as in IMD96; results in decreased repair response to DNA damage as shown by rescue assays in LIG1-deficient cells; severely reduced DNA ligase activity; 2-fold decrease of affinity for DNA; 5-fold increase of affiniy for Mg2+, features a modification of the amino acid from R to L at position 641.
+The protein's natural variant, known as no effect on DNA ligase activity;, features a modification of the amino acid from V to M at position 753.
+The protein's natural variant, known as in IMD96; results in decreased repair response to DNA damage as shown by rescue assays in LIG1-deficient cells; severely reduced DNA ligase activity; 3-fold decrease of affinity for DNA; 4-fold increase of affiniy for Mg2+;, features a modification of the amino acid from R to W at position 771.
+The protein's natural variant, known as in SPGF11; results in impaired self-association;, features a modification of the amino acid from Q to P at position 216.
+The protein's natural variant, known as in SPGF11; results in impaired self-association;, features a modification of the amino acid from A to T at position 313.
+The protein's natural variant, known as in IMD13; impairs interaction with LCK; impairs LCK activation; induces LCK mislocalization;, features a modification of the amino acid from G to V at position 22.
+The natural variant of this protein is characterized by an amino acid alteration from R to K at position 345.
+The natural variant of this protein is characterized by an amino acid alteration from L to I at position 381.
+The protein's natural variant, known as in soxR102; constitutively activated allele, features a modification of the amino acid from R to C at position 20.
+The protein's natural variant, known as in CPHD5;, features a modification of the amino acid from Q to H at position 6.
+The protein's natural variant, known as in CPHD5; the mutated protein is associated with impaired transcriptional repression but not DNA binding;, features a modification of the amino acid from I to T at position 26.
+The protein's natural variant, known as in CPHD5; unknown pathological significance; loss of DNA binding ability; unable to repress PROP1-mediated activation; no effect on nuclear location; no effect on protein abundance;, features a modification of the amino acid from R to Q at position 109.
+The protein's natural variant, known as in GHDPA; unable to repress PROP1-mediated activation;, features a modification of the amino acid from E to K at position 149.
+The protein's natural variant, known as in SOD; loss of DNA-binding;, features a modification of the amino acid from R to C at position 160.
+The protein's natural variant, known as in SOD; mild;, features a modification of the amino acid from S to L at position 170.
+The protein's natural variant, known as in GHDPA;, features a modification of the amino acid from T to A at position 181.
+The protein's natural variant, known as in IDDSFAS;, features a modification of the amino acid from C to R at position 358.
+The protein's natural variant, known as in strain: RM 7004, features a modification of the amino acid from L to F at position 5.
+The protein's natural variant, known as in strain: RM 7004, features a modification of the amino acid from S to L at position 32.
+The protein's natural variant, known as in strain: RM 7004, features a modification of the amino acid from A to S at position 271.
+The protein's natural variant, known as in strain: RM 7004, features a modification of the amino acid from A to S at position 313.
+The protein's natural variant, known as in strain: RM 7004, features a modification of the amino acid from L to W at position 415.
+The protein's natural variant, known as in strain: RM 7004, features a modification of the amino acid from E to K at position 418.
+The protein's natural variant, known as in MRT75; loss of interaction with CRADD; loss of activation of CASP2 protein, features a modification of the amino acid from R to W at position 815.
+The protein's natural variant, known as in MRT75, features a modification of the amino acid from R to W at position 862.
+The natural variant of this protein is characterized by an amino acid alteration from E to D at position 65.
+The protein's natural variant, known as in strain: ATCC 7754, features a modification of the amino acid from V to A at position 33.
+The protein's natural variant, known as in strain: ATCC 7754, features a modification of the amino acid from K to R at position 36.
+The protein's natural variant, known as in strain: ATCC 7754, features a modification of the amino acid from RIPRTI to KVPQTV at position 51.
+The protein's natural variant, known as in strain: ATCC 7754, features a modification of the amino acid from RS to KF at position 68.
+The protein's natural variant, known as in strain: ATCC 7754, features a modification of the amino acid from R to K at position 104.
+The protein's natural variant, known as in strain: ATCC 7754, features a modification of the amino acid from L to S at position 116.
+The protein's natural variant, known as in strain: ATCC 7754, features a modification of the amino acid from D to N at position 125.
+The protein's natural variant, known as in strain: ATCC 7754, features a modification of the amino acid from I to T at position 136.
+The protein's natural variant, known as in strain: ATCC 4108, features a modification of the amino acid from R to H at position 137.
+The protein's natural variant, known as in strain: ATCC 7754, features a modification of the amino acid from N to D at position 144.
+The protein's natural variant, known as in strain: ATCC 7754, features a modification of the amino acid from IYDRTC to NYGRTG at position 157.
+The protein's natural variant, known as in strain: ATCC 7754, features a modification of the amino acid from N to D at position 162.
+The protein's natural variant, known as in strain: ATCC 7754, features a modification of the amino acid from F to L at position 171.
+The protein's natural variant, known as in strain: ATCC 7754, features a modification of the amino acid from P to S at position 180.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from S to L at position 674.
+The protein's natural variant, known as in allele CD94*02 and allele CD94*05, features a modification of the amino acid from T to M at position 24.
+The protein's natural variant, known as in allele CD94*03 and allele CD94*05, features a modification of the amino acid from A to S at position 135.
+The protein's natural variant, known as in Jogjakarta;, features a modification of the amino acid from K to E at position 18.
+The protein's natural variant, known as in OPTB3; in Czechoslovakia;, features a modification of the amino acid from Q to P at position 92.
+The protein's natural variant, known as in OPTB3; partial loss of activity, features a modification of the amino acid from H to Y at position 94.
+The protein's natural variant, known as in OPTB3;, features a modification of the amino acid from H to Y at position 107.
+The protein's natural variant, known as in OPTB3; complete loss of activity, features a modification of the amino acid from G to R at position 144.
+The protein's natural variant, known as in Melbourne;, features a modification of the amino acid from P to H at position 236.
+The protein's natural variant, known as decreased expression; altered subcellular localization; altered transporter activity;, features a modification of the amino acid from D to G at position 333.
+The protein's natural variant, known as altered transporter activity;, features a modification of the amino acid from R to H at position 353.
+The protein's natural variant, known as altered transporter activity;, features a modification of the amino acid from T to I at position 486.
+The protein's natural variant, known as in DJS;, features a modification of the amino acid from R to W at position 768.
+The protein's natural variant, known as altered transporter activity;, features a modification of the amino acid from G to S at position 921.
+The protein's natural variant, known as no effect on transporter activity;, features a modification of the amino acid from I to T at position 1036.
+The protein's natural variant, known as in DJS; protein is properly localized at the plasma membrane, but transporter activity is impaired;, features a modification of the amino acid from R to H at position 1150.
+The protein's natural variant, known as in DJS; decreased expression and mislocation to the endoplasmic reticulum;, features a modification of the amino acid from I to F at position 1173.
+The protein's natural variant, known as decreased expression; altered subcellular localization; decreased transporter activity;, features a modification of the amino acid from R to H at position 1174.
+The protein's natural variant, known as decreased expression;, features a modification of the amino acid from R to L at position 1181.
+The protein's natural variant, known as decreased transporter activity;, features a modification of the amino acid from N to K at position 1244.
+The protein's natural variant, known as altered transporter activity;, features a modification of the amino acid from P to L at position 1291.
+The protein's natural variant, known as in DJS;, features a modification of the amino acid from Q to R at position 1382.
+The protein's natural variant, known as in AUTSX1 and ASPGX1, features a modification of the amino acid from R to C at position 451.
+The protein's natural variant, known as in ALS18; the mutant protein is detected in the insoluble fraction of cells;, features a modification of the amino acid from C to G at position 71.
+The protein's natural variant, known as in ALS18; the mutant protein is detected in the insoluble fraction of cells;, features a modification of the amino acid from M to T at position 114.
+The protein's natural variant, known as in ALS18; unknown pathological significance; like the wild-type the mutant protein is detected in the soluble fraction of cells;, features a modification of the amino acid from E to G at position 117.
+The protein's natural variant, known as in ALS18; the mutant protein is detected in the insoluble fraction of cells;, features a modification of the amino acid from G to V at position 118.
+The protein's natural variant, known as rare variant; may act as a phenotype modifier in EIEE13 patients carrying SCN8A mutations;, features a modification of the amino acid from R to C at position 334.
+The protein's natural variant, known as rare variant; may act as a phenotype modifier in EIEE13 patients carrying SCN8A mutations;, features a modification of the amino acid from R to W at position 428.
+The protein's natural variant, known as in BSS;, features a modification of the amino acid from L to P at position 7.
+The protein's natural variant, known as in BSS;, features a modification of the amino acid from C to R at position 24.
+The protein's natural variant, known as in BSS;, features a modification of the amino acid from D to G at position 37.
+The protein's natural variant, known as in BSS;, features a modification of the amino acid from L to P at position 56.
+The protein's natural variant, known as in BSS;, features a modification of the amino acid from N to S at position 61.
+The protein's natural variant, known as in BSS;, features a modification of the amino acid from F to S at position 71.
+The protein's natural variant, known as in BSS, features a modification of the amino acid from C to Y at position 113.
+The protein's natural variant, known as in strain: IFM 45817, IFM 50993, IFM 54196 and RMSCC 1036 / AZ1, features a modification of the amino acid from R to S at position 222.
+The protein's natural variant, known as in strain: IFM 45812, IFM 4935, IFM 51112 and RMSCC 2128 / TX1, features a modification of the amino acid from N to D at position 247.
+The protein's natural variant, known as in strain: IFM 45811, IFM 45812, IFM 45813, IFM 45817, IFM 4935, IFM 4945, IFM 50993, IFM 50994, IFM 51112, IFM 54194, IFM 54195, IFM 54196, RMSCC 1036 / AZ1, RMSCC 1045 / AZ2 and RMSCC 2128 / TX1, features a modification of the amino acid from V to I at position 249.
+The protein's natural variant, known as in strain: ML 308-225, features a modification of the amino acid from K to N at position 2.
+The protein's natural variant, known as in strain: ML 308-225, features a modification of the amino acid from SL to FF at position 42.
+The protein's natural variant, known as in strain: ML 308-225, features a modification of the amino acid from T to K at position 46.
+The protein's natural variant, known as in strain: ML 308-225, features a modification of the amino acid from W to L at position 157.
+The protein's natural variant, known as in strain: ML 308-225, features a modification of the amino acid from V to F at position 188.
+The protein's natural variant, known as in strain: ML 308-225, features a modification of the amino acid from ATN to STI at position 305.
+The protein's natural variant, known as in strain: ML 308-225, features a modification of the amino acid from A to T at position 320.
+The protein's natural variant, known as in strain: ML 308-225, features a modification of the amino acid from N to Q at position 372.
+The protein's natural variant, known as in strain: ML 308-225, features a modification of the amino acid from E to V at position 493.
+The protein's natural variant, known as in strain: ML 308-225, features a modification of the amino acid from S to N at position 497.
+The protein's natural variant, known as in strain: ML 308-225, features a modification of the amino acid from H to Y at position 585.
+The protein's natural variant, known as in strain: ML 308-225, features a modification of the amino acid from E to K at position 709.
+The protein's natural variant, known as in strain: ML 308-225, features a modification of the amino acid from M to T at position 721.
+The protein's natural variant, known as in strain: ML 308-225, features a modification of the amino acid from GHL to SHF at position 753.
+The protein's natural variant, known as in strain: ML 308-225, features a modification of the amino acid from S to P at position 803.
+The protein's natural variant, known as in strain: ML 308-225, features a modification of the amino acid from A to V at position 815.
+The protein's natural variant, known as in strain: ML 308-225, features a modification of the amino acid from LNLVHTS to MNLIYNA at position 835.
+The protein's natural variant, known as in strain: ML 308-225, features a modification of the amino acid from QGT to LGA at position 847.
+The protein's natural variant, known as in strain: ML 308-225, features a modification of the amino acid from S to T at position 855.
+The protein's natural variant, known as in strain: ML 308-225, features a modification of the amino acid from Q to L at position 888.
+The protein's natural variant, known as in strain: ML 308-225, features a modification of the amino acid from S to I at position 1025.
+The protein's natural variant, known as in lit, features a modification of the amino acid from D to G at position 60.
+The protein's natural variant, known as in strain: B306, Z18, Z22 and Z24, features a modification of the amino acid from S to R at position 48.
+The protein's natural variant, known as in strain: B101, features a modification of the amino acid from S to T at position 48.
+The protein's natural variant, known as in strain: B306, Z18 and Z22, features a modification of the amino acid from A to G at position 55.
+The protein's natural variant, known as in strain: Z22, features a modification of the amino acid from S to T at position 65.
+The protein's natural variant, known as in strain: B141, features a modification of the amino acid from G to R at position 73.
+The protein's natural variant, known as in strain: Z24, features a modification of the amino acid from E to Q at position 90.
+The protein's natural variant, known as in strain: B101, features a modification of the amino acid from T to N at position 98.
+The protein's natural variant, known as in NEDMIMS; a functional model in yeast shows reduced choline kinase activity, features a modification of the amino acid from R to W at position 141.
+The protein's natural variant, known as in NEDMIMS; a functional model in yeast shows reduced choline kinase activity, features a modification of the amino acid from P to S at position 194.
+The protein's natural variant, known as in NEDMIMS, features a modification of the amino acid from F to L at position 341.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 662.
+The natural variant of this protein is characterized by an amino acid alteration from A to T at position 958.
+The natural variant of this protein is characterized by an amino acid alteration from E to K at position 1572.
+The protein's natural variant, known as does not affect insulin-stimulated lipid kinase activity;, features a modification of the amino acid from M to I at position 326.
+The protein's natural variant, known as in a patient with severe insulin resistance; lower insulin-stimulated lipid kinase activity compared with wild-type;, features a modification of the amino acid from R to Q at position 409.
+The protein's natural variant, known as in SHORTS; there is 70 to 90% reduction in the effect of insulin on AKT1 activation, glycogen synthesis and glucose uptake, indicating severe insulin resistance for both proximal and distal PI3K-dependent signaling;, features a modification of the amino acid from E to K at position 489.
+The protein's natural variant, known as in SHORTS; impairs interaction between PIK3R1 and IRS1 and reduces AKT1-mediated insulin signaling;, features a modification of the amino acid from R to W at position 649.
+The protein's natural variant, known as in NELABA;, features a modification of the amino acid from L to P at position 30.
+The protein's natural variant, known as in NELABA;, features a modification of the amino acid from L to R at position 105.
+The protein's natural variant, known as in NELABA;, features a modification of the amino acid from L to R at position 126.
+The protein's natural variant, known as in EVR1; benign variant;, features a modification of the amino acid from P to S at position 33.
+The protein's natural variant, known as in EVR1;, features a modification of the amino acid from G to D at position 36.
+The protein's natural variant, known as in EVR1;, features a modification of the amino acid from E to Q at position 40.
+The protein's natural variant, known as in EVR1; minor reduction of its wild-type activity;, features a modification of the amino acid from H to Y at position 69.
+The protein's natural variant, known as in EVR1;, features a modification of the amino acid from M to T at position 105.
+The protein's natural variant, known as in EVR1; loss of function;, features a modification of the amino acid from M to V at position 105.
+The protein's natural variant, known as in EVR1, features a modification of the amino acid from I to T at position 114.
+The protein's natural variant, known as in EVR1; loss of function;, features a modification of the amino acid from M to V at position 157.
+The protein's natural variant, known as in EVR1; increased signaling activity;, features a modification of the amino acid from C to R at position 181.
+The protein's natural variant, known as in retinopathy of prematurity;, features a modification of the amino acid from K to N at position 203.
+The protein's natural variant, known as in EVR1; reduced signaling activity in presence of WNT3A but no change in presence of NDP/norrin;, features a modification of the amino acid from C to R at position 204.
+The protein's natural variant, known as in EVR1;, features a modification of the amino acid from C to Y at position 204.
+The protein's natural variant, known as in EVR1, features a modification of the amino acid from M to K at position 223.
+The protein's natural variant, known as in EVR1;, features a modification of the amino acid from I to V at position 256.
+The protein's natural variant, known as in EVR1;, features a modification of the amino acid from W to C at position 335.
+The protein's natural variant, known as in EVR1;, features a modification of the amino acid from M to V at position 342.
+The protein's natural variant, known as in retinopathy of prematurity, features a modification of the amino acid from A to G at position 370.
+The protein's natural variant, known as in EVR1; 48% loss of its wild-type activity; associated in a EVR4 patient with mutation Cys-444 in LPR5;, features a modification of the amino acid from R to Q at position 417.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from K to T at position 436.
+The protein's natural variant, known as in EVR1;, features a modification of the amino acid from T to P at position 445.
+The protein's natural variant, known as in EVR1;, features a modification of the amino acid from G to D at position 488.
+The protein's natural variant, known as in EVR1;, features a modification of the amino acid from S to F at position 497.
+The protein's natural variant, known as in EVR1, features a modification of the amino acid from G to R at position 525.
+The protein's natural variant, known as in minor variant, features a modification of the amino acid from I to V at position 163.
+The protein's natural variant, known as in strain: KY024 and KY038, features a modification of the amino acid from A to T at position 6.
+The protein's natural variant, known as in strain: KY024, features a modification of the amino acid from V to I at position 13.
+The protein's natural variant, known as in allele DMB*01:07;, features a modification of the amino acid from T to A at position 28.
+The protein's natural variant, known as in allele DMB*01:06;, features a modification of the amino acid from S to F at position 45.
+The protein's natural variant, known as in allele DMB*01:07;, features a modification of the amino acid from D to V at position 49.
+The protein's natural variant, known as in allele DMB*01:07;, features a modification of the amino acid from S to N at position 71.
+The protein's natural variant, known as in allele DMB*01:02 and allele DMB*01:06;, features a modification of the amino acid from A to E at position 162.
+The protein's natural variant, known as in allele DMB*01:04 and allele DMB*01:05;, features a modification of the amino acid from A to V at position 162.
+The protein's natural variant, known as in allele DMB*01:01;, features a modification of the amino acid from T to I at position 197.
+The protein's natural variant, known as in strain: PAC181; butyramide inducible phenotype, features a modification of the amino acid from T to N at position 106.
+The protein's natural variant, known as in strain: C3H/HeJ, features a modification of the amino acid from D to Y at position 61.
+The protein's natural variant, known as in strain: C3H/HeJ, features a modification of the amino acid from L to M at position 87.
+The protein's natural variant, known as in strain: C3H/HeJ, features a modification of the amino acid from M to T at position 89.
+The protein's natural variant, known as in a lung neuroendocrine carcinoma sample; somatic mutation;, features a modification of the amino acid from A to T at position 103.
+The natural variant of this protein is characterized by an amino acid alteration from TA to S at position 22.
+The natural variant of this protein is characterized by an amino acid alteration from C to Y at position 97.
+The protein's natural variant, known as found in a child with sporadic epilepsy; unknown pathological significance;, features a modification of the amino acid from L to F at position 93.
+The protein's natural variant, known as allele TPMT*5; has very low activity when expressed in a heterologous system;, features a modification of the amino acid from L to S at position 49.
+The protein's natural variant, known as allele TPMT*2; TPMT*2 allele frequency is 0.5%; seems to be restricted to the Caucasian population; 100-fold reduction in activity; protein shows enhanced degradation;, features a modification of the amino acid from A to P at position 80.
+The protein's natural variant, known as allele TPMT*3A and allele TPMT*3B; very low activity; protein shows enhanced degradation leading to strongly reduced protein levels;, features a modification of the amino acid from A to T at position 154.
+The protein's natural variant, known as allele TPMT*6; reduced activity;, features a modification of the amino acid from Y to F at position 180.
+The protein's natural variant, known as allele TPMT*8; intermediate activity;, features a modification of the amino acid from R to H at position 215.
+The protein's natural variant, known as allele TPMT*7; reduced activity;, features a modification of the amino acid from H to Q at position 227.
+The protein's natural variant, known as allele TPMT*3B and allele TPMT*3C; reduced activity; protein shows enhanced degradation;, features a modification of the amino acid from Y to C at position 240.
+The protein's natural variant, known as in STUT1; unknown pathological significance;, features a modification of the amino acid from F to V at position 96.
+The protein's natural variant, known as in STUT1; unknown pathological significance;, features a modification of the amino acid from H to N at position 205.
+The protein's natural variant, known as in STUT1; unknown pathological significance;, features a modification of the amino acid from N to S at position 311.
+The protein's natural variant, known as in STUT1; unknown pathological significance;, features a modification of the amino acid from S to F at position 326.
+The protein's natural variant, known as in STUT1; unknown pathological significance;, features a modification of the amino acid from H to R at position 384.
+The protein's natural variant, known as in STUT1; unknown pathological significance;, features a modification of the amino acid from A to V at position 475.
+The protein's natural variant, known as in STUT1; slightly decreased assembly of the AP-4 complex;, features a modification of the amino acid from V to I at position 517.
+The protein's natural variant, known as in STUT1; unknown pathological significance;, features a modification of the amino acid from M to V at position 542.
+The protein's natural variant, known as in STUT1; unknown pathological significance;, features a modification of the amino acid from S to P at position 623.
+The protein's natural variant, known as found in deaf patients; unknown pathological significance, features a modification of the amino acid from K to E at position 719.
+The protein's natural variant, known as in STUT1; slightly decreased assembly of the AP-4 complex;, features a modification of the amino acid from E to K at position 801.
+The protein's natural variant, known as in STUT1; unknown pathological significance;, features a modification of the amino acid from S to P at position 905.
+The protein's natural variant, known as in STUT1; unknown pathological significance;, features a modification of the amino acid from P to S at position 978.
+The protein's natural variant, known as in STUT1; unknown pathological significance;, features a modification of the amino acid from I to V at position 1080.
+The protein's natural variant, known as in STUT1; unknown pathological significance;, features a modification of the amino acid from L to R at position 1089.
+The protein's natural variant, known as in STUT1; unknown pathological significance;, features a modification of the amino acid from R to Q at position 1105.
+The protein's natural variant, known as in CMS6; impaired activity;, features a modification of the amino acid from L to P at position 210.
+The protein's natural variant, known as in CMS6; impaired activity;, features a modification of the amino acid from P to A at position 211.
+The protein's natural variant, known as in CMS6; impaired activity;, features a modification of the amino acid from I to T at position 305.
+The protein's natural variant, known as in CMS6;, features a modification of the amino acid from I to T at position 336.
+The natural variant of this protein is characterized by an amino acid alteration from A to G at position 392.
+The protein's natural variant, known as in CMS6; impaired activity;, features a modification of the amino acid from R to C at position 420.
+The protein's natural variant, known as in CMS6; completely lack activity;, features a modification of the amino acid from E to K at position 441.
+The protein's natural variant, known as in CMS6; impaired activity;, features a modification of the amino acid from R to G at position 482.
+The protein's natural variant, known as in CMS6; impaired activity;, features a modification of the amino acid from S to L at position 498.
+The protein's natural variant, known as in CMS6; impaired activity;, features a modification of the amino acid from V to L at position 506.
+The protein's natural variant, known as in CMS6; impaired activity;, features a modification of the amino acid from R to H at position 560.
+The protein's natural variant, known as in strain: cv. Royal Gala, features a modification of the amino acid from R to G at position 307.
+The protein's natural variant, known as in strain: cv. Royal Gala, features a modification of the amino acid from RIMSMM to SQ at position 459.
+The protein's natural variant, known as in strain: VRF, features a modification of the amino acid from P to T at position 187.
+The protein's natural variant, known as in strain: VRF, features a modification of the amino acid from L to V at position 189.
+The protein's natural variant, known as in strain: VRF, features a modification of the amino acid from V to L at position 236.
+The protein's natural variant, known as in GCENSG;, features a modification of the amino acid from S to G at position 407.
+The protein's natural variant, known as in one of the major forms, features a modification of the amino acid from R to Q at position 57.
+The natural variant of this protein is characterized by an amino acid alteration from V to L at position 203.
+The natural variant of this protein is characterized by an amino acid alteration from N to S at position 305.
+The protein's natural variant, known as in a glioblastoma multiforme sample; somatic mutation, features a modification of the amino acid from M to I at position 580.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation, features a modification of the amino acid from E to K at position 811.
+The protein's natural variant, known as in a glioblastoma multiforme sample; somatic mutation, features a modification of the amino acid from P to S at position 885.
+The protein's natural variant, known as in MYP24; affects the BMP/TGF-beta pathway by suppressing expression of SMAD1; loss of function mutation;, features a modification of the amino acid from M to T at position 304.
+The protein's natural variant, known as in MYP24; unknown pathological significance, features a modification of the amino acid from G to A at position 413.
+The protein's natural variant, known as does not affect enzymatic activity;, features a modification of the amino acid from V to A at position 36.
+The protein's natural variant, known as in NPDB; unknown pathological significance;, features a modification of the amino acid from D to V at position 51.
+The protein's natural variant, known as in NPDB; requires 2 nucleotide substitutions, features a modification of the amino acid from C to H at position 91.
+The protein's natural variant, known as in NPDB, features a modification of the amino acid from C to W at position 94.
+The protein's natural variant, known as in NPDA and NPDB; expresses protein level comparable to wild-type SMPD1 expressing cells; retains very low enzyme activity;, features a modification of the amino acid from L to P at position 105.
+The protein's natural variant, known as in NPDB; expresses protein level comparable to wild-type SMPD1 expressing cells; retains 13% residual enzyme activity, features a modification of the amino acid from V to A at position 132.
+The protein's natural variant, known as in NPDB;, features a modification of the amino acid from L to P at position 139.
+The protein's natural variant, known as in NPDB;, features a modification of the amino acid from C to R at position 159.
+The protein's natural variant, known as in NPDB;, features a modification of the amino acid from L to P at position 163.
+The protein's natural variant, known as in NPDB; also in patients with an intermediate form;, features a modification of the amino acid from G to R at position 168.
+The protein's natural variant, known as in NPDB;, features a modification of the amino acid from I to N at position 178.
+The protein's natural variant, known as in NPDA; reduces enzyme activity; intermediate form with clinical features of both Niemann-Pick disease types A and B;, features a modification of the amino acid from P to L at position 186.
+The protein's natural variant, known as in NPDB;, features a modification of the amino acid from A to P at position 198.
+The protein's natural variant, known as in NPDB;, features a modification of the amino acid from R to C at position 202.
+The protein's natural variant, known as in NPDA; results in less than 0.5% of wild-type activity, features a modification of the amino acid from W to R at position 211.
+The protein's natural variant, known as in NPDA, features a modification of the amino acid from L to R at position 216.
+The protein's natural variant, known as in NPDB, features a modification of the amino acid from L to M at position 227.
+The protein's natural variant, known as in NPDB; expresses protein level comparable to wild-type SMPD1 expressing cells; retains no enzyme activity;, features a modification of the amino acid from L to P at position 227.
+The protein's natural variant, known as in NPDA;, features a modification of the amino acid from C to R at position 228.
+The protein's natural variant, known as in NPDB and NPDA; some patients have a NPDA/NPDB intermediate phenotype;, features a modification of the amino acid from R to C at position 230.
+The protein's natural variant, known as in NPDA; intermediate form with clinical features of both Niemann-Pick disease types A and B;, features a modification of the amino acid from R to H at position 230.
+The protein's natural variant, known as in NPDB, features a modification of the amino acid from G to D at position 234.
+The protein's natural variant, known as in NPDA; intermediate form with clinical features of both Niemann-Pick disease types A and B;, features a modification of the amino acid from A to V at position 243.
+The protein's natural variant, known as in NPDB;, features a modification of the amino acid from G to R at position 244.
+The protein's natural variant, known as in NPDB; expresses protein level comparable to wild-type SMPD1 expressing cells; retains no enzyme activity, features a modification of the amino acid from W to C at position 246.
+The protein's natural variant, known as in NPDA; severe decrease in activity; the mutant is highly unstable;, features a modification of the amino acid from G to D at position 247.
+The protein's natural variant, known as in NPDA and NPDB;, features a modification of the amino acid from G to S at position 247.
+The protein's natural variant, known as in NPDA;, features a modification of the amino acid from E to K at position 248.
+The protein's natural variant, known as in NPDB; 30% residual activity;, features a modification of the amino acid from E to Q at position 248.
+The protein's natural variant, known as in NPDA and NPDB; also found in patients with an intermediate form;, features a modification of the amino acid from S to R at position 250.
+The protein's natural variant, known as in NPDA; strongly reduces enzyme activity; intermediate form with clinical features of both Niemann-Pick disease types A and B, features a modification of the amino acid from D to E at position 253.
+The protein's natural variant, known as in NPDA; results in loss of activity;, features a modification of the amino acid from D to H at position 253.
+The protein's natural variant, known as in NPDA, features a modification of the amino acid from P to S at position 255.
+The protein's natural variant, known as in NPDB, features a modification of the amino acid from T to I at position 258.
+The protein's natural variant, known as in NPDA; strongly reduces enzyme activity; intermediate form with clinical features of both Niemann-Pick disease types A and B, features a modification of the amino acid from D to A at position 280.
+The protein's natural variant, known as in NPDB; requires 2 nucleotide substitutions, features a modification of the amino acid from P to F at position 282.
+The protein's natural variant, known as in NPDB; expresses protein level comparable to wild-type SMPD1 expressing cells; retains no enzyme activity;, features a modification of the amino acid from A to T at position 283.
+The protein's natural variant, known as in NPDB; also in patients with an intermediate form; unknown pathological significance;, features a modification of the amino acid from R to H at position 291.
+The protein's natural variant, known as in NPDA; strongly reduces enzyme activity; intermediate form with clinical features of both Niemann-Pick disease types A and B;, features a modification of the amino acid from Q to K at position 294.
+The protein's natural variant, known as in NPDA; in 23% of NPDAAshkenazi Jewish patients; abolishes enzyme activity;, features a modification of the amino acid from L to P at position 304.
+The protein's natural variant, known as in NPDB; results in 20% of wild-type activity;, features a modification of the amino acid from V to M at position 314.
+The protein's natural variant, known as in NPDA, features a modification of the amino acid from Y to H at position 315.
+The protein's natural variant, known as in NPDA;, features a modification of the amino acid from G to R at position 319.
+The protein's natural variant, known as in NPDB; unknown pathological significance;, features a modification of the amino acid from N to D at position 320.
+The protein's natural variant, known as in NPDA, features a modification of the amino acid from H to Y at position 321.
+The protein's natural variant, known as in NPDA; unknown pathological significance, features a modification of the amino acid from T to P at position 324.
+The protein's natural variant, known as in NPDB; results in 1-4% of wild type activity;, features a modification of the amino acid from P to A at position 325.
+The protein's natural variant, known as in NPDB;, features a modification of the amino acid from P to R at position 332.
+The protein's natural variant, known as in NPDA; strongly reduces enzyme activity; intermediate form with clinical features of both Niemann-Pick disease types A and B, features a modification of the amino acid from L to P at position 343.
+The protein's natural variant, known as in NPDA, features a modification of the amino acid from L to R at position 343.
+The protein's natural variant, known as in NPDB; sphingomyelinase activity is decreased to 4% of wild-type activity; no effect on protein abundance; no effect on protein localization to lysosome; no effect on protein localization to extracellular space;, features a modification of the amino acid from A to D at position 359.
+The protein's natural variant, known as in NPDA; unknown pathological significance, features a modification of the amino acid from L to R at position 363.
+The protein's natural variant, known as in NPDA;, features a modification of the amino acid from Y to C at position 369.
+The protein's natural variant, known as in NPDB;, features a modification of the amino acid from P to S at position 373.
+The protein's natural variant, known as in NPDB; reduces enzyme activity; some patients have a NPDA/NPDB intermediate phenotype;, features a modification of the amino acid from R to H at position 378.
+The protein's natural variant, known as in NPDB, features a modification of the amino acid from R to L at position 378.
+The protein's natural variant, known as in NPDB, features a modification of the amino acid from S to P at position 381.
+The protein's natural variant, known as in NPDA and NPDB;, features a modification of the amino acid from M to I at position 384.
+The protein's natural variant, known as in NPDB;, features a modification of the amino acid from N to S at position 385.
+The protein's natural variant, known as in NPDA, features a modification of the amino acid from C to R at position 387.
+The protein's natural variant, known as in NPDA, features a modification of the amino acid from N to H at position 391.
+The protein's natural variant, known as in NPDA, features a modification of the amino acid from N to T at position 391.
+The protein's natural variant, known as in NPDB; low sphingomyelin degradation rates;, features a modification of the amino acid from W to G at position 393.
+The protein's natural variant, known as in NPDA; intermediate form, features a modification of the amino acid from W to R at position 393.
+The protein's natural variant, known as in NPDB;, features a modification of the amino acid from A to V at position 415.
+The protein's natural variant, known as in NPDA;, features a modification of the amino acid from H to R at position 423.
+The protein's natural variant, known as in NPDB; abolishes enzyme activity;, features a modification of the amino acid from H to Y at position 423.
+The protein's natural variant, known as in NPDA;, features a modification of the amino acid from G to S at position 426.
+The protein's natural variant, known as in NPDB; results in loss of activity; the patient also carries mutation H-228 that has sufficient activity to account for the Niemann-Pick disease type B phenotype;, features a modification of the amino acid from H to R at position 427.
+The protein's natural variant, known as in NPDB;, features a modification of the amino acid from C to R at position 433.
+The protein's natural variant, known as in NPDB, features a modification of the amino acid from L to P at position 434.
+The protein's natural variant, known as in NPDB, features a modification of the amino acid from W to C at position 437.
+The protein's natural variant, known as in NPDB;, features a modification of the amino acid from S to R at position 438.
+The protein's natural variant, known as in NPDA;, features a modification of the amino acid from Y to C at position 448.
+The protein's natural variant, known as in NPDA, features a modification of the amino acid from L to P at position 452.
+The protein's natural variant, known as in NPDB, features a modification of the amino acid from A to D at position 453.
+The protein's natural variant, known as in NPDB;, features a modification of the amino acid from A to V at position 454.
+The protein's natural variant, known as in NPDB, features a modification of the amino acid from G to D at position 458.
+The protein's natural variant, known as in NPDA;, features a modification of the amino acid from F to S at position 465.
+The protein's natural variant, known as in NPDA;, features a modification of the amino acid from Y to S at position 469.
+The protein's natural variant, known as in NPDB; unknown pathological significance;, features a modification of the amino acid from R to Q at position 476.
+The protein's natural variant, known as in NPDB; some patients have a NPDA/NPDB intermediate phenotype;, features a modification of the amino acid from R to W at position 476.
+The protein's natural variant, known as in NPDA and NPDB;, features a modification of the amino acid from P to L at position 477.
+The protein's natural variant, known as in NPDB, features a modification of the amino acid from F to L at position 482.
+The protein's natural variant, known as in NPDA;, features a modification of the amino acid from A to E at position 484.
+The protein's natural variant, known as does not affect enzymatic activity;, features a modification of the amino acid from A to V at position 487.
+The protein's natural variant, known as in NPDB, features a modification of the amino acid from T to A at position 488.
+The protein's natural variant, known as in NPDB;, features a modification of the amino acid from Y to N at position 490.
+The protein's natural variant, known as in NPDB;, features a modification of the amino acid from G to S at position 492.
+The protein's natural variant, known as in NPDA; intermediate form, features a modification of the amino acid from N to I at position 494.
+The protein's natural variant, known as in NPDB;, features a modification of the amino acid from G to S at position 496.
+The protein's natural variant, known as in NPDB;, features a modification of the amino acid from R to C at position 498.
+The protein's natural variant, known as in NPDA;, features a modification of the amino acid from R to H at position 498.
+The protein's natural variant, known as in NPDA; in 32% of NPDAAshkenazi Jewish patients; nearly abolishes enzyme activity;, features a modification of the amino acid from R to L at position 498.
+The natural variant of this protein is characterized by an amino acid alteration from S to G at position 507.
+The protein's natural variant, known as does not affect enzymatic activity;, features a modification of the amino acid from G to R at position 508.
+The protein's natural variant, known as in NPDB, features a modification of the amino acid from H to Q at position 516.
+The protein's natural variant, known as in NPDB;, features a modification of the amino acid from E to V at position 517.
+The protein's natural variant, known as in NPDA;, features a modification of the amino acid from Y to C at position 519.
+The protein's natural variant, known as in NPDB, features a modification of the amino acid from I to L at position 520.
+The protein's natural variant, known as in NPDB, features a modification of the amino acid from N to S at position 522.
+The protein's natural variant, known as in NPDB; results in 64% of wild-type activity, features a modification of the amino acid from Q to H at position 525.
+The protein's natural variant, known as in NPDB and NPDA; also in patients with an intermediate form;, features a modification of the amino acid from W to R at position 535.
+The protein's natural variant, known as in NPDA, features a modification of the amino acid from Y to H at position 539.
+The protein's natural variant, known as in NPDB, features a modification of the amino acid from N to K at position 549.
+The protein's natural variant, known as in NPDB, features a modification of the amino acid from L to P at position 551.
+The protein's natural variant, known as in NPDB; expresses protein level comparable to wild-type SMPD1 expressing cells; retains 6.8% residual enzyme activity, features a modification of the amino acid from D to Y at position 565.
+The protein's natural variant, known as in NPDA; results in decreased activity; decreased stability, features a modification of the amino acid from F to L at position 572.
+The protein's natural variant, known as in NPDB; unknown pathological significance, features a modification of the amino acid from H to D at position 577.
+The protein's natural variant, known as in NPDB;, features a modification of the amino acid from K to N at position 578.
+The protein's natural variant, known as in NPDA; impairs enzyme activity; also in patients with an intermediate form;, features a modification of the amino acid from G to S at position 579.
+The protein's natural variant, known as in NPDB;, features a modification of the amino acid from Q to R at position 598.
+The protein's natural variant, known as in NPDB; unknown pathological significance;, features a modification of the amino acid from L to F at position 599.
+The protein's natural variant, known as in NPDB and NPDA; expresses protein level comparable to wild-type SMPD1 expressing cells; retains about 10% residual enzyme activity; loss of location to lysosome;, features a modification of the amino acid from R to H at position 602.
+The protein's natural variant, known as in NPDB; expresses protein level comparable to wild-type SMPD1 expressing cells; retains very low enzyme activity; loss of location to lysosome, features a modification of the amino acid from R to P at position 602.
+The natural variant of this protein is characterized by an amino acid alteration from S to G at position 605.
+The protein's natural variant, known as in NPDB; unknown pathological significance;, features a modification of the amino acid from R to C at position 610.
+The protein's natural variant, known as in PAPA6;, features a modification of the amino acid from T to I at position 474.
+The protein's natural variant, known as in strain: 487/90, features a modification of the amino acid from V to L at position 6.
+The protein's natural variant, known as in strain: 487/90, features a modification of the amino acid from L to S at position 66.
+The protein's natural variant, known as in strain: 487/90, features a modification of the amino acid from V to I at position 134.
+The protein's natural variant, known as in strain: 487/90, features a modification of the amino acid from K to N at position 141.
+The protein's natural variant, known as in strain: 487/90, features a modification of the amino acid from T to P at position 207.
+The protein's natural variant, known as in strain: 487/90, features a modification of the amino acid from T to A at position 213.
+The protein's natural variant, known as in strain: 487/90, features a modification of the amino acid from A to S at position 242.
+The protein's natural variant, known as in strain: 487/90, features a modification of the amino acid from L to S at position 256.
+The protein's natural variant, known as in strain: 487/90, features a modification of the amino acid from I to V at position 266.
+The protein's natural variant, known as in strain: 487/90, features a modification of the amino acid from I to V at position 304.
+The protein's natural variant, known as in strain: 487/90, features a modification of the amino acid from S to A at position 342.
+The protein's natural variant, known as in strain: 487/90, features a modification of the amino acid from R to H at position 406.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from S to Y at position 183.
+The protein's natural variant, known as found in a renal cell carcinoma sample; somatic mutation, features a modification of the amino acid from H to N at position 244.
+The protein's natural variant, known as in ATLD2; a hypomorphic mutation affecting DNA repair in response to UV; results in significantly decreased interaction with FEN1, LIG1 and ERCC5;, features a modification of the amino acid from S to I at position 228.
+The protein's natural variant, known as found in a patient with a 46,XY disorder of sex development; unknown pathological significance; no change in positive regulation of DNA-binding transcription factor activity;, features a modification of the amino acid from G to V at position 84.
+The protein's natural variant, known as in ODG8; completely inactive in positive regulation of DNA-binding transcription factor activity;, features a modification of the amino acid from K to R at position 314.
+The protein's natural variant, known as found in a patient with a 46,XY disorder of sex development; unknown pathological significance; shows a higher positive regulation of DNA-binding transcription factor activity;, features a modification of the amino acid from L to R at position 426.
+The protein's natural variant, known as in DFNB8; fails to undergo proteolytic cleavage and is unable to activate ENaC;, features a modification of the amino acid from D to G at position 103.
+The protein's natural variant, known as in DFNB8; fails to undergo proteolytic cleavage and is unable to activate ENaC;, features a modification of the amino acid from R to W at position 109.
+The protein's natural variant, known as in DFNB8; fails to undergo proteolytic cleavage and is unable to activate ENaC;, features a modification of the amino acid from C to F at position 194.
+The protein's natural variant, known as in DFNB8; fails to undergo proteolytic cleavage and is unable to activate ENaC;, features a modification of the amino acid from R to L at position 216.
+The protein's natural variant, known as in DFNB8; fails to undergo proteolytic cleavage and is unable to activate ENaC;, features a modification of the amino acid from W to C at position 251.
+The protein's natural variant, known as in DFNB8; fails to undergo proteolytic cleavage and is unable to activate ENaC;, features a modification of the amino acid from P to L at position 404.
+The protein's natural variant, known as in DFNB8; fails to undergo proteolytic cleavage and is unable to activate ENaC;, features a modification of the amino acid from C to R at position 407.
+The protein's natural variant, known as in DFNB8;, features a modification of the amino acid from A to T at position 426.
+The protein's natural variant, known as in strain: DBA/2; Ly17.2 allotype, features a modification of the amino acid from S to L at position 116.
+The protein's natural variant, known as in strain: NZB; Ly17.1 allotype, features a modification of the amino acid from S to P at position 116.
+The natural variant of this protein is characterized by an amino acid alteration from L to P at position 145.
+The protein's natural variant, known as in strain: DBA/2; Ly17.2 allotype, features a modification of the amino acid from H to L at position 161.
+The protein's natural variant, known as in strain: NZB; Ly17.1 allotype, features a modification of the amino acid from H to Q at position 161.
+The natural variant of this protein is characterized by an amino acid alteration from L to Q at position 190.
+The protein's natural variant, known as in strain: NZB, features a modification of the amino acid from P to T at position 195.
+The protein's natural variant, known as in strain: NZB, features a modification of the amino acid from S to I at position 287.
+The protein's natural variant, known as in strain: HFL97e3_12 and ZIM(S)e3_24, features a modification of the amino acid from N to H at position 33.
+The protein's natural variant, known as in strain: DPF96e3_3.0, DPF96e3_4.2, DPF96e3_23.1, DPF96e3_74.2, VT97e3_41, SC96e3_12.3, HFL97e3_8, HFL97e3_12, HFL97e3_15, ZIM(S)e3_24 and ZIM(S)e3_35, features a modification of the amino acid from Y to F at position 243.
+The protein's natural variant, known as in LMHD; does not affect protein levels; increases the rate of phosphatidylserine synthesis; profoundly impairs negative feedback enzyme regulation by phosphatidylserine;, features a modification of the amino acid from L to P at position 265.
+The protein's natural variant, known as in LMHD; does not affect protein levels; increases the rate of phosphatidylserine synthesis; profoundly impairs negative feedback enzyme regulation by phosphatidylserine;, features a modification of the amino acid from P to S at position 269.
+The protein's natural variant, known as in LMHD; does not affect protein levels; increases the rate of phosphatidylserine synthesis; profoundly impairs negative feedback enzyme regulation by phosphatidylserine;, features a modification of the amino acid from Q to R at position 353.
+The protein's natural variant, known as in mutant AZP12, features a modification of the amino acid from S to A at position 1175.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 67.
+The protein's natural variant, known as in strain: ECOR 1, features a modification of the amino acid from A to V at position 14.
+The protein's natural variant, known as in strain: ECOR 61, features a modification of the amino acid from A to T at position 52.
+The protein's natural variant, known as in strain: ECOR 50, features a modification of the amino acid from M to I at position 59.
+The protein's natural variant, known as in DEE108; unknown pathological significance, features a modification of the amino acid from S to F at position 101.
+The protein's natural variant, known as in DEE108, features a modification of the amino acid from S to L at position 104.
+The protein's natural variant, known as in DEE108, features a modification of the amino acid from R to P at position 406.
+The protein's natural variant, known as in DEE108, features a modification of the amino acid from G to S at position 510.
+The protein's natural variant, known as in DEE108, features a modification of the amino acid from G to S at position 515.
+The protein's natural variant, known as in DEE108, features a modification of the amino acid from L to P at position 516.
+The protein's natural variant, known as in DEE108; unknown pathological significance, features a modification of the amino acid from V to L at position 551.
+The protein's natural variant, known as found in a patient with autism spectrum disorder without history of seizures; unknown pathological significance, features a modification of the amino acid from F to L at position 655.
+The protein's natural variant, known as in MRT67; decreased protein abundance;, features a modification of the amino acid from F to V at position 232.
+The natural variant of this protein is characterized by an amino acid alteration from C to A at position 97.
+The natural variant of this protein is characterized by an amino acid alteration from L to I at position 101.
+The protein's natural variant, known as in NNO4;, features a modification of the amino acid from A to P at position 193.
+The protein's natural variant, known as in NNO4;, features a modification of the amino acid from H to P at position 196.
+The protein's natural variant, known as in MKS1; no rescue of ciliation defects in an MKS1-knockdown cell line;, features a modification of the amino acid from D to Y at position 19.
+The protein's natural variant, known as found in a patient with Joubert syndrome also carrying a deletion in MKS1 intron 15 and a missense mutation in TCTN3 gene 'P-95'; unknown pathological significance;, features a modification of the amino acid from W to C at position 80.
+The protein's natural variant, known as in MKS1; unknown pathological significance;, features a modification of the amino acid from R to W at position 166.
+The protein's natural variant, known as in MKS1; unknown pathological significance; no defect of primary cilia formation in starved fibroblasts from a patient also carrying a deletion of S-372; no effect on the localization to the transition zone;, features a modification of the amino acid from G to E at position 317.
+The protein's natural variant, known as in MKS1; unknown pathological significance; decreased primary cilia formation in starved fibroblasts from a patient also carrying a mutation potentially affecting splicing; complete rescue of ciliation defects in an MKS1-knockdown cell line; no effect on the localization to the transition zone;, features a modification of the amino acid from S to L at position 403.
+The protein's natural variant, known as in MKS1; unknown pathological significance; no effect on primary cilia formation in starved fibroblasts from a patient also carrying a mutation creating a frameshift and a premature stop codon; partial rescue of ciliation defects in an MKS1-knockdown cell line; no effect on the localization to the transition zone;, features a modification of the amino acid from P to S at position 421.
+The protein's natural variant, known as in BBS13;, features a modification of the amino acid from C to W at position 492.
+The protein's natural variant, known as in DBA7, features a modification of the amino acid from L to H at position 20.
+The protein's natural variant, known as in clone PTA1.1, features a modification of the amino acid from R to S at position 211.
+The protein's natural variant, known as in clone PTA1.1, features a modification of the amino acid from I to M at position 226.
+The protein's natural variant, known as in clone PTA1.1, features a modification of the amino acid from I to V at position 335.
+The protein's natural variant, known as in a patient with neural tube defects;, features a modification of the amino acid from D to E at position 119.
+The natural variant of this protein is characterized by an amino acid alteration from S to C at position 321.
+The protein's natural variant, known as may be a risk factor for otitis media;, features a modification of the amino acid from P to R at position 356.
+The protein's natural variant, known as may be a risk factor for otitis media;, features a modification of the amino acid from R to W at position 1001.
+The protein's natural variant, known as in FTD; reduces the ability of tau to promote microtubule assembly and promotes fibril formation in vitro;, features a modification of the amino acid from R to H at position 5.
+The protein's natural variant, known as in PSNP1; delays assembly initiation and lowers the mass of microtubules formed; but the assembly rate is increased compared to normal tau;, features a modification of the amino acid from R to L at position 5.
+The protein's natural variant, known as risk factor for PSNP1;, features a modification of the amino acid from D to N at position 285.
+The protein's natural variant, known as risk factor for PSNP1;, features a modification of the amino acid from V to A at position 289.
+The protein's natural variant, known as in PIDB; reduces the ability to promote microtubule assembly by 70%;, features a modification of the amino acid from K to T at position 574.
+The protein's natural variant, known as in FTD; less able to promote microtubule assembly than wild-type tau;, features a modification of the amino acid from L to V at position 583.
+The protein's natural variant, known as in FTD;, features a modification of the amino acid from G to V at position 589.
+The protein's natural variant, known as in FTD; increased aggregation propensity and altered binding affinity towards microtubules and F-actin;, features a modification of the amino acid from G to R at position 590.
+The protein's natural variant, known as in FTD; with parkinsonism;, features a modification of the amino acid from N to K at position 596.
+The protein's natural variant, known as in FTD; reduced the ability of tau to promote microtubule assembly without having a significant effect on tau filament formation; effects at both the RNA and the protein level;, features a modification of the amino acid from N to H at position 613.
+The protein's natural variant, known as in FTD; most common mutation; reduction in the ability to promote microtubule assembly; accelerates aggregation of tau into filaments;, features a modification of the amino acid from P to L at position 618.
+The protein's natural variant, known as in FTD and CBD; reduction in the ability to promote microtubule assembly;, features a modification of the amino acid from P to S at position 618.
+The protein's natural variant, known as in PSNP1;, features a modification of the amino acid from G to V at position 620.
+The protein's natural variant, known as in FTD; minimal parkinsonism; very early age of onset;, features a modification of the amino acid from S to N at position 622.
+The protein's natural variant, known as in FTD;, features a modification of the amino acid from K to M at position 634.
+The protein's natural variant, known as in PIDB; markedly reduced ability of tau to promote microtubule assembly;, features a modification of the amino acid from S to F at position 637.
+The protein's natural variant, known as in FTD; ultrastructural and biochemical characteristics indistinguishable from Alzheimer disease; accelerates aggregation of tau into filaments;, features a modification of the amino acid from V to M at position 654.
+The protein's natural variant, known as in FTD;, features a modification of the amino acid from E to V at position 659.
+The protein's natural variant, known as in fatal respiratory hypoventilation; unusual apparent autosomal recessive inheritance; reduced binding to microtubules as well as increased fibrillization and aggregation;, features a modification of the amino acid from S to L at position 669.
+The protein's natural variant, known as in PIDB; 90% reduction in the rate of microtubule assembly;, features a modification of the amino acid from K to I at position 686.
+The protein's natural variant, known as in PIDB; in vitro the mutation reduces the ability of tau to promote microtubule assembly by 25 to 30%;, features a modification of the amino acid from G to R at position 706.
+The protein's natural variant, known as in FTD/Alzheimer disease; accelerates aggregation of tau into filaments; reduces tau phosphorylation in cells compared to both the wild-type and other mutant forms;, features a modification of the amino acid from R to W at position 723.
+The protein's natural variant, known as in strain: River-type, features a modification of the amino acid from R to Q at position 115.
+The protein's natural variant, known as in NEDNMS; unknown pathological significance, features a modification of the amino acid from D to G at position 55.
+The protein's natural variant, known as in NEDNMS; unknown pathological significance, features a modification of the amino acid from S to P at position 134.
+The protein's natural variant, known as in NEDNMS; unknown pathological significance, features a modification of the amino acid from G to D at position 197.
+The protein's natural variant, known as in NEDNMS; unknown pathological significance, features a modification of the amino acid from N to S at position 469.
+The protein's natural variant, known as in NEDNMS; unknown pathological significance, features a modification of the amino acid from R to C at position 853.
+The protein's natural variant, known as in NEDNMS; unknown pathological significance, features a modification of the amino acid from K to T at position 902.
+The protein's natural variant, known as in NEDNMS; unknown pathological significance, features a modification of the amino acid from G to D at position 913.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from H to P at position 1093.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from G to V at position 1116.
+The protein's natural variant, known as in OPSMD;, features a modification of the amino acid from R to W at position 401.
+The protein's natural variant, known as associated with susceptibility to T2D;, features a modification of the amino acid from L to I at position 632.
+The protein's natural variant, known as in OPSMD;, features a modification of the amino acid from P to S at position 659.
+The protein's natural variant, known as in OPSMD, features a modification of the amino acid from W to C at position 688.
+The protein's natural variant, known as in OPSMD;, features a modification of the amino acid from F to I at position 722.
+The protein's natural variant, known as associated with susceptibility to T2D;, features a modification of the amino acid from N to S at position 982.
+The protein's natural variant, known as in DEDSSH2; severely impairs diphthamide modification of elongation factor 2;, features a modification of the amino acid from R to C at position 201.
+The protein's natural variant, known as in strain: JAM 2006, features a modification of the amino acid from V to A at position 170.
+The protein's natural variant, known as in strain: JAM 2006, features a modification of the amino acid from D to E at position 231.
+The protein's natural variant, known as in strain: JAM 2006, features a modification of the amino acid from S to P at position 330.
+The protein's natural variant, known as in strain: JAM 2006, features a modification of the amino acid from E to G at position 333.
+The protein's natural variant, known as in strain: JAM 2006, features a modification of the amino acid from S to G at position 436.
+The protein's natural variant, known as in strain: 69A and ATCC 53726, features a modification of the amino acid from S to A at position 40.
+The protein's natural variant, known as in strain: ATCC 53726, features a modification of the amino acid from H to Y at position 103.
+The protein's natural variant, known as in strain: 69A, features a modification of the amino acid from E to Q at position 113.
+The protein's natural variant, known as in strain: ATCC 53726, features a modification of the amino acid from D to S at position 121.
+The protein's natural variant, known as in strain: ATCC 53726, features a modification of the amino acid from Q to E at position 125.
+The protein's natural variant, known as in strain: ATCC 53726, features a modification of the amino acid from M to T at position 203.
+The protein's natural variant, known as in strain: 69A, features a modification of the amino acid from S to T at position 232.
+The protein's natural variant, known as in strain: ATCC 53726, features a modification of the amino acid from D to N at position 319.
+The protein's natural variant, known as in subsp. Sitkensis, features a modification of the amino acid from P to L at position 99.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from L to R at position 444.
+The protein's natural variant, known as in colorectal cancer;, features a modification of the amino acid from E to D at position 36.
+The protein's natural variant, known as in pancreatic cancer; associated with N-265; failure to rescue the spindle-assembly checkpoint activity as a result of a deficient recruitment of MAD2L1 and BUBR1 to kinetochores; efficient restoration of chromosome congression; reduced binding to BUB3; rescue of the ability of kinetochores to bind SGO1 and CENPF but not MCAK, features a modification of the amino acid from Y to C at position 259.
+The protein's natural variant, known as in pancreatic cancer; associated with C-259; complete rescue of the spindle-assembly checkpoint activity; increased rate of chromosome congression errors, features a modification of the amino acid from H to N at position 265.
+The protein's natural variant, known as in colorectal cancer;, features a modification of the amino acid from S to Y at position 492.
+The protein's natural variant, known as in colorectal cancer;, features a modification of the amino acid from P to R at position 648.
+The protein's natural variant, known as in PVNH6; may decrease protein stability;, features a modification of the amino acid from I to N at position 377.
+The protein's natural variant, known as in SGD1, features a modification of the amino acid from V to A at position 218.
+The protein's natural variant, known as in IMD108; gain-of-function variant resulting in increased DNA-binding transcription factor activity and decreased association with transcriptional repressors, features a modification of the amino acid from R to H at position 219.
+The protein's natural variant, known as in strain: LP-728 and Pu-9f, features a modification of the amino acid from F to L at position 4.
+The protein's natural variant, known as in strain: B-26/a, B-33/a, O-70, Pi-3/a, Pi-59 and Pi-72-nmq-15, features a modification of the amino acid from V to A at position 5.
+The protein's natural variant, known as in strain: O-23, features a modification of the amino acid from V to E at position 5.
+The protein's natural variant, known as in strain: SC-643, features a modification of the amino acid from F to L at position 9.
+The protein's natural variant, known as in strain: Pu-39, features a modification of the amino acid from L to P at position 13.
+The protein's natural variant, known as in strain: Pu-7c, features a modification of the amino acid from V to M at position 14.
+The protein's natural variant, known as in strain: Pu-9f, features a modification of the amino acid from F to L at position 16.
+The protein's natural variant, known as in strain: Pi-47, features a modification of the amino acid from F to P at position 16.
+The protein's natural variant, known as in strain: LP-745/a, features a modification of the amino acid from S to F at position 18.
+The protein's natural variant, known as in strain: Pi-72-nmq-24, features a modification of the amino acid from S to F at position 20.
+The protein's natural variant, known as in strain: G-72, G-78, G-80, O-40 and Pi-21, features a modification of the amino acid from R to K at position 25.
+The protein's natural variant, known as in strain: Pi-72-nmq-27, features a modification of the amino acid from K to R at position 26.
+The protein's natural variant, known as in strain: BQ-348, features a modification of the amino acid from I to L at position 27.
+The protein's natural variant, known as in strain: O-40 and Pi-21, features a modification of the amino acid from A to E at position 35.
+The protein's natural variant, known as in strain: Pi-78, features a modification of the amino acid from A to I at position 39.
+The protein's natural variant, known as in allele b1, allele b2 and allele b', features a modification of the amino acid from A to T at position 39.
+The protein's natural variant, known as in strain: CL-308 and Pu-40, features a modification of the amino acid from A to V at position 39.
+The protein's natural variant, known as in allele b1, allele b2 and allele b', features a modification of the amino acid from S to G at position 42.
+The protein's natural variant, known as in strain: P2-35, features a modification of the amino acid from L to P at position 43.
+The protein's natural variant, known as in strain: O-40 and Pi-21, features a modification of the amino acid from E to D at position 45.
+The protein's natural variant, known as in strain: O-40 and Pi-21, features a modification of the amino acid from I to V at position 48.
+The protein's natural variant, known as in strain: P1-67, features a modification of the amino acid from I to T at position 51.
+The protein's natural variant, known as in strain: G-78 and Pi-72-nmq-15, features a modification of the amino acid from S to L at position 55.
+The protein's natural variant, known as in strain: G-42 and Pi-78, features a modification of the amino acid from T to I at position 61.
+The protein's natural variant, known as in strain: Pu-39, features a modification of the amino acid from H to R at position 63.
+The protein's natural variant, known as in strain: G-72, G-78, G-80 and Pu-15c, features a modification of the amino acid from D to E at position 65.
+The protein's natural variant, known as in strain: SC-670, features a modification of the amino acid from L to P at position 68.
+The protein's natural variant, known as in strain: O-98, features a modification of the amino acid from H to R at position 69.
+The protein's natural variant, known as in strain: Pu-14c, features a modification of the amino acid from N to S at position 71.
+The protein's natural variant, known as in strain: O-40, Pi-21 and Pi-78, features a modification of the amino acid from M to L at position 75.
+The protein's natural variant, known as in strain: G-72, G-78, G-80, O-40, Pi-21 and Pi-78, features a modification of the amino acid from L to M at position 78.
+The protein's natural variant, known as in strain: BQ-348, features a modification of the amino acid from L to S at position 79.
+The protein's natural variant, known as in strain: O-78, features a modification of the amino acid from D to G at position 89.
+The protein's natural variant, known as in strain: O-88, features a modification of the amino acid from Y to H at position 90.
+The protein's natural variant, known as in allele b1, allele b2 and allele b', features a modification of the amino acid from M to I at position 95.
+The protein's natural variant, known as in strain: P2-72, features a modification of the amino acid from D to N at position 98.
+The protein's natural variant, known as in strain: Pu-15c, features a modification of the amino acid from I to T at position 100.
+The protein's natural variant, known as in strain: Pi-72-nmq-24, features a modification of the amino acid from K to Q at position 101.
+The protein's natural variant, known as in strain: Pu-8v, features a modification of the amino acid from T to S at position 103.
+The protein's natural variant, known as in strain: Pi-72-nmq-15, features a modification of the amino acid from D to G at position 109.
+The protein's natural variant, known as in strain: Pi-3/a, features a modification of the amino acid from R to G at position 111.
+The protein's natural variant, known as in strain: O-40, features a modification of the amino acid from E to K at position 113.
+The protein's natural variant, known as in strain: BQ-347, features a modification of the amino acid from N to S at position 116.
+The protein's natural variant, known as in allele b1, allele b2 and allele b', features a modification of the amino acid from A to T at position 117.
+The protein's natural variant, known as in strain: P2-68, features a modification of the amino acid from A to V at position 117.
+The protein's natural variant, known as in strain: O-40, Pi-21 and Pi-78, features a modification of the amino acid from M to I at position 119.
+The protein's natural variant, known as in strain: O-40, Pi-21, G-72, G-78 and G-80, features a modification of the amino acid from Q to H at position 120.
+The protein's natural variant, known as in strain: O-40 and Pi-21, features a modification of the amino acid from K to T at position 123.
+The protein's natural variant, known as in strain: O-86, features a modification of the amino acid from D to G at position 124.
+The protein's natural variant, known as in strain: SC-645, features a modification of the amino acid from M to V at position 125.
+The protein's natural variant, known as in strain: P2-50 and P2-68, features a modification of the amino acid from K to R at position 128.
+The protein's natural variant, known as in allele b1 and allele b2, features a modification of the amino acid from V to A at position 136.
+The protein's natural variant, known as in strain: O-88, features a modification of the amino acid from V to I at position 136.
+The protein's natural variant, known as in strain: LP-728, features a modification of the amino acid from C to R at position 138.
+The protein's natural variant, known as in allele b1, allele b2 and allele b', features a modification of the amino acid from V to I at position 139.
+The protein's natural variant, known as in strain: Pi-10f, features a modification of the amino acid from A to T at position 141.
+The protein's natural variant, known as in strain: AR-17f, features a modification of the amino acid from A to S at position 144.
+The protein's natural variant, known as in strain: LP-719, features a modification of the amino acid from N to H at position 150.
+The protein's natural variant, known as in strain: B-26/a, features a modification of the amino acid from N to I at position 150.
+The protein's natural variant, known as in strain: AR-25e, features a modification of the amino acid from N to S at position 150.
+The protein's natural variant, known as in allele b1 and allele b2; causes a decreased net negative charge and observed lower mobility, features a modification of the amino acid from E to K at position 151.
+The protein's natural variant, known as in allele b1, allele b2 and allele b', features a modification of the amino acid from G to A at position 152.
+The protein's natural variant, known as in strain: ATCC 43504 / NCTC 11637 / JCM 7653 / RPH 13487; resistant to metronidazole, features a modification of the amino acid from N to K at position 14.
+The protein's natural variant, known as in strain: HP500, 69A and ATCC 43504 / NCTC 11637 / JCM 7653 / RPH 13487; resistant to metronidazole, features a modification of the amino acid from T to E at position 31.
+The protein's natural variant, known as in strain: ATCC 43504 / NCTC 11637 / JCM 7653 / RPH 13487; resistant to metronidazole, features a modification of the amino acid from I to V at position 36.
+The protein's natural variant, known as in strain: ATCC 49503, features a modification of the amino acid from H to R at position 53.
+The protein's natural variant, known as in strain: ATCC 43504 / NCTC 11637 / JCM 7653 / RPH 13487; resistant to metronidazole, features a modification of the amino acid from M to I at position 56.
+The protein's natural variant, known as in strain: HP500, 69A, ATCC 43504 / NCTC 11637 / JCM 7653 / RPH 13487; resistant to metronidazole and ATCC 49503 / 60190, features a modification of the amino acid from D to N at position 59.
+The protein's natural variant, known as in strain: ATCC 43504 / NCTC 11637 / JCM 7653 / RPH 13487; resistant to metronidazole, features a modification of the amino acid from KKQIAAHSYFNEEMIKSASALMVVCSLRPSE to NHPSRNPKH at position 93.
+The protein's natural variant, known as in strain: 69A, features a modification of the amino acid from K to N at position 64.
+The protein's natural variant, known as in strain: HP500, features a modification of the amino acid from A to V at position 68.
+The protein's natural variant, known as in strain: ATCC 49503 / 60190, features a modification of the amino acid from R to K at position 90.
+The protein's natural variant, known as in strain: 69A, features a modification of the amino acid from H to T at position 97.
+The protein's natural variant, known as in strain: ATCC 49503 / 60190, features a modification of the amino acid from G to S at position 98.
+The protein's natural variant, known as in strain: 69A, features a modification of the amino acid from P to S at position 106.
+The protein's natural variant, known as in strain: 69A, features a modification of the amino acid from R to K at position 131.
+The protein's natural variant, known as in strain: 69A, features a modification of the amino acid from V to I at position 172.
+The protein's natural variant, known as in strain: ATCC 49503 / 60190, features a modification of the amino acid from A to V at position 183.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from A to T at position 148.
+The protein's natural variant, known as in AMD3; unknown pathological significance; mouse BMPR1B construct containing this mutation shows reduced GDF5-dependent receptor activation, mouse BMPR1B construct containing this mutation shows no loss of cell membrane localization;, features a modification of the amino acid from R to C at position 31.
+The protein's natural variant, known as in a gastric adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from R to H at position 31.
+The protein's natural variant, known as in AMD3; mouse BMPR1B construct containing this mutation shows loss of GDF5-dependent receptor activation, chicken BMPR1B construct containing this mutation does not show reduced chondrocyte differentiation, mouse BMPR1B construct containing this mutation shows no loss of cell membrane localization;, features a modification of the amino acid from C to R at position 53.
+The protein's natural variant, known as in BDA2; in animal models loss of kinase activity and loss of positive regulation of chondrocyte differentiation;, features a modification of the amino acid from I to K at position 200.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation, features a modification of the amino acid from D to N at position 297.
+The protein's natural variant, known as in BDA1D; acts in a dominant-negative manner;, features a modification of the amino acid from K to N at position 325.
+The protein's natural variant, known as in brachydactyly type C and BDA2; with also additional features of symphalangism-1;, features a modification of the amino acid from R to Q at position 486.
+The protein's natural variant, known as in BDA2; in animal models no effect on kinase activity but strongly decreased positive regulation of chondrocyte differentiation;, features a modification of the amino acid from R to W at position 486.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to W at position 727.
+The protein's natural variant, known as in LPI;, features a modification of the amino acid from T to I at position 5.
+The protein's natural variant, known as in LPI; failed to induce cationic amino acid transport activity;, features a modification of the amino acid from M to K at position 50.
+The protein's natural variant, known as in LPI;, features a modification of the amino acid from S to L at position 53.
+The protein's natural variant, known as in LPI; failed to induce sodium-independent cationic amino acid and sodium-dependent neutral amino acid transport activity; does not affect heterodimerization with SLC3A2; affects expression level;, features a modification of the amino acid from G to V at position 54.
+The protein's natural variant, known as in LPI;, features a modification of the amino acid from L to P at position 124.
+The protein's natural variant, known as in LPI;, features a modification of the amino acid from A to P at position 140.
+The protein's natural variant, known as in LPI; moderately reduced cationic amino acid transport activity;, features a modification of the amino acid from F to L at position 152.
+The protein's natural variant, known as in LPI; failed to induce cationic amino acid transport activity;, features a modification of the amino acid from T to I at position 188.
+The protein's natural variant, known as in LPI;, features a modification of the amino acid from K to E at position 191.
+The protein's natural variant, known as in LPI;, features a modification of the amino acid from S to F at position 238.
+The protein's natural variant, known as in LPI;, features a modification of the amino acid from E to D at position 251.
+The protein's natural variant, known as in LPI;, features a modification of the amino acid from L to P at position 261.
+The protein's natural variant, known as in LPI;, features a modification of the amino acid from R to M at position 333.
+The protein's natural variant, known as in LPI; failed to induce sodium-independent cationic amino acid and sodium-dependent neutral amino acid transport activity;, features a modification of the amino acid from L to R at position 334.
+The protein's natural variant, known as in LPI;, features a modification of the amino acid from G to D at position 338.
+The protein's natural variant, known as in LPI;, features a modification of the amino acid from N to Y at position 365.
+The protein's natural variant, known as in LPI; failed to induce cationic amino acid transport activity;, features a modification of the amino acid from S to R at position 386.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from P to S at position 413.
+The protein's natural variant, known as in LPI;, features a modification of the amino acid from S to P at position 489.
+The protein's natural variant, known as in IFN-tau3D, features a modification of the amino acid from S to P at position 25.
+The protein's natural variant, known as in IFN-tau3B, features a modification of the amino acid from A to S at position 76.
+The protein's natural variant, known as in IFN-tau3E, features a modification of the amino acid from D to G at position 126.
+The protein's natural variant, known as in IFN-tau3C, features a modification of the amino acid from V to A at position 129.
+The protein's natural variant, known as in IFN-tau3E, features a modification of the amino acid from V to M at position 146.
+The protein's natural variant, known as in ALPS1B; significant reduction in cytotoxicity and apoptosis and inhibition of the shedding of the soluble form, features a modification of the amino acid from C to S at position 202.
+The natural variant of this protein is characterized by an amino acid alteration from C to S at position 95.
+The protein's natural variant, known as in CILD22; no loss of interaction with DNAAF11;, features a modification of the amino acid from V to G at position 16.
+The protein's natural variant, known as in CILD22; no loss of interaction with DNAAF11;, features a modification of the amino acid from S to P at position 29.
+The protein's natural variant, known as in CILD22, features a modification of the amino acid from L to P at position 39.
+The protein's natural variant, known as in CILD22;, features a modification of the amino acid from L to P at position 266.
+The protein's natural variant, known as in CILD22; no loss of interaction with DNAAF11;, features a modification of the amino acid from Y to C at position 379.
+The protein's natural variant, known as in non-small cell lung cancer cell lines;, features a modification of the amino acid from R to Q at position 407.
+The protein's natural variant, known as in MGBL; unknown pathological significance; decreased function in transcriptional activation;, features a modification of the amino acid from E to G at position 530.
+The protein's natural variant, known as found in FORS blood group carriers; reactivates Forssman antigen synthesis and expression in erythrocytes;, features a modification of the amino acid from R to Q at position 296.
+The protein's natural variant, known as in NEDCDS, features a modification of the amino acid from R to Q at position 206.
+The protein's natural variant, known as in NEDCDS, features a modification of the amino acid from R to W at position 206.
+The protein's natural variant, known as in 50% of the molecules, features a modification of the amino acid from P to G at position 39.
+The protein's natural variant, known as in strain: G2, features a modification of the amino acid from V to A at position 236.
+The protein's natural variant, known as in prebycusis phenotype; when associated with waltzer cadherin 23 mutant, features a modification of the amino acid from R to H at position 109.
+The protein's natural variant, known as in MAE;, features a modification of the amino acid from R to Q at position 44.
+The protein's natural variant, known as complete loss of GABA transporter activity, features a modification of the amino acid from G to E at position 94.
+The protein's natural variant, known as found in a patient with intractable absence epilepsy; unknown pathological significance; retains about 27% of wild-type GABA transporter activity, features a modification of the amino acid from W to R at position 235.
+The protein's natural variant, known as in MAE; unknown pathological significance; retains about 2% of wild-type GABA transporter activity, features a modification of the amino acid from F to S at position 270.
+The protein's natural variant, known as in MAE;, features a modification of the amino acid from A to V at position 288.
+The protein's natural variant, known as in MAE;, features a modification of the amino acid from G to R at position 297.
+The protein's natural variant, known as in MAE;, features a modification of the amino acid from A to P at position 334.
+The protein's natural variant, known as found in a patient with generalized epilepsy; unknown pathological significance; retains about 6% of wild-type GABA transporter activity, features a modification of the amino acid from Y to C at position 445.
+The protein's natural variant, known as found in a patient with generalized epilepsy; unknown pathological significance; complete loss of GABA transporter activity, features a modification of the amino acid from G to R at position 550.
+The protein's natural variant, known as in CAON; unknown pathological significance;, features a modification of the amino acid from A to T at position 56.
+The protein's natural variant, known as in CAON;, features a modification of the amino acid from T to M at position 185.
+The protein's natural variant, known as in CAON;, features a modification of the amino acid from S to L at position 358.
+The protein's natural variant, known as in DEE103; affects voltage-gated potassium channel activity; when expressed in Xenopus laevis oocytes, it results in a shift in voltage dependence of activation to more hyperpolarized potentials and a slower deactivation time, features a modification of the amino acid from C to W at position 125.
+The protein's natural variant, known as in DEE103; affects voltage-gated potassium channel activity; when expressed in Xenopus laevis oocytes, it results in a shift in voltage dependence of activation to more hyperpolarized potentials and a slower deactivation time, features a modification of the amino acid from E to G at position 135.
+The protein's natural variant, known as in DEE103; affects voltage-gated potassium channel activity; when expressed in Xenopus laevis oocytes, it causes a shift in voltage dependence of steady-state activation to more hyperpolarized potentials and results in a significant reduction of potassium currents, features a modification of the amino acid from D to Y at position 167.
+The protein's natural variant, known as probable disease-associated variant found in a patient with generalized epilepsy; loss of voltage-gated potassium channel activity; no current is detected when mutant channels are expressed in Xenopus laevis oocytes, features a modification of the amino acid from F to S at position 219.
+The protein's natural variant, known as in DEE103, features a modification of the amino acid from R to K at position 351.
+The protein's natural variant, known as found in a patient with myoclonic-atonic epilepsy; unknown pathological significance, features a modification of the amino acid from F to C at position 382.
+The protein's natural variant, known as in DEE103; affects voltage-gated potassium channel activity; results in a shift in voltage dependence of activation to more hyperpolarized potentials, features a modification of the amino acid from R to G at position 405.
+The protein's natural variant, known as in DEE103; affects voltage-gated potassium channel activity; when expressed in Xenopus laevis oocytes, it results in a shift in voltage dependence of activation to more hyperpolarized potentials and a slower deactivation time, features a modification of the amino acid from T to A at position 437.
+The protein's natural variant, known as in DEE103, features a modification of the amino acid from V to L at position 471.
+The protein's natural variant, known as does not affect function in negative regulation of PAX6 expression;, features a modification of the amino acid from S to Y at position 64.
+The protein's natural variant, known as in AN3; affects function and results in increased negative regulation of PAX6 expression compared to wild-type;, features a modification of the amino acid from G to R at position 155.
+The protein's natural variant, known as in strain: IFM 45817, features a modification of the amino acid from N to S at position 250.
+The protein's natural variant, known as in NEDMCR; unknown pathological significance, features a modification of the amino acid from P to L at position 105.
+The protein's natural variant, known as in NEDMCR; unknown pathological significance;, features a modification of the amino acid from W to R at position 818.
+The protein's natural variant, known as in allele ZF-3d and allele ZF-3e, features a modification of the amino acid from Q to R at position 5.
+The protein's natural variant, known as in allele ZF-3a and allele ZF-3c, features a modification of the amino acid from R to G at position 56.
+The protein's natural variant, known as in allele ZF-3c, features a modification of the amino acid from D to E at position 93.
+The protein's natural variant, known as in allele ZF-3e, features a modification of the amino acid from N to D at position 102.
+The protein's natural variant, known as in allele ZF-3c, features a modification of the amino acid from G to S at position 137.
+The protein's natural variant, known as in allele ZF-3e, features a modification of the amino acid from T to A at position 141.
+The protein's natural variant, known as in allele ZF-3d and allele ZF-3e, features a modification of the amino acid from K to R at position 145.
+The protein's natural variant, known as in DKCB7; localizes properly on telomeres; decreased interaction with TINF2;, features a modification of the amino acid from P to T at position 405.
+The protein's natural variant, known as in strain: 0L136, features a modification of the amino acid from KSCDDYFDVLK to NPVMTILMCLN at position 692.
+The protein's natural variant, known as in strain: 0L136, features a modification of the amino acid from PIV to SNN at position 785.
+The protein's natural variant, known as in strain: 0L136, features a modification of the amino acid from I to T at position 974.
+The protein's natural variant, known as in strain: 0L136, features a modification of the amino acid from A to D at position 1048.
+The protein's natural variant, known as in HADH deficiency;, features a modification of the amino acid from A to T at position 40.
+The protein's natural variant, known as in HADH deficiency;, features a modification of the amino acid from D to E at position 57.
+The protein's natural variant, known as found in a patient with Reye-like syndrome. Does not affect 3-hydroxyacyl-CoA dehydrogenase activity. Increases KM value for NADH. Does not affect dimerization, features a modification of the amino acid from D to G at position 57.
+The protein's natural variant, known as found in a patient with Reye-like syndrome; loss of 3-hydroxyacyl-CoA dehydrogenase activity. Does not affect dimerization;, features a modification of the amino acid from Y to H at position 226.
+The protein's natural variant, known as in HHF4; loss of 3-hydroxyacyl-CoA dehydrogenase activity;, features a modification of the amino acid from P to L at position 258.
+The protein's natural variant, known as in HIGM5; fully active and stable when expressed in E.coli; mistargeted to mitochondria rather than the nucleus;, features a modification of the amino acid from F to S at position 251.
+The protein's natural variant, known as in napin-1B, features a modification of the amino acid from E to Q at position 37.
+The protein's natural variant, known as in strain: Isolate San Diego zoo Ppy3, Isolate Anna and Isolate Dennis, features a modification of the amino acid from R to A at position 4.
+The protein's natural variant, known as in strain: Isolate Anna, features a modification of the amino acid from V to I at position 38.
+The protein's natural variant, known as in strain: Isolate San Diego zoo Ppy3, Isolate Anna and Isolate Dennis, features a modification of the amino acid from N to S at position 54.
+The protein's natural variant, known as in strain: Isolate San Diego zoo Ppy3, features a modification of the amino acid from T to I at position 67.
+The protein's natural variant, known as in strain: Isolate San Diego zoo Ppy3, features a modification of the amino acid from F to L at position 184.
+The protein's natural variant, known as in strain: Isolate San Diego zoo PPY3, features a modification of the amino acid from A to T at position 226.
+The protein's natural variant, known as in FXS; rare variant found in a developmentally delayed male; inhibits nucleosome binding; reduces interaction with KCNMB4; inhibits presynaptic action potential (AP) broadening; does not alter postsynaptic RNA-binding and polyribosome association;, features a modification of the amino acid from R to Q at position 138.
+The protein's natural variant, known as in FXS; reduces association with polyribosome; reduces RNA-binding;, features a modification of the amino acid from G to E at position 266.
+The protein's natural variant, known as in FXS; alters protein folding and stability; increases nucleocytoplasmic shuttling; reduces localization in Cajal bodies; reduces the association with cytoplasmic granules; reduces association with polyribosome; reduces RNA-binding; attenuates mRNA translation repression; impairs homooligomerization; reduces interaction with TDRD3; reduces interaction with viral influenza A nucleoprotein (NP); does not inhibit interaction with SMN1, FXR1 and FXR2;, features a modification of the amino acid from I to N at position 304.
+The natural variant of this protein is characterized by an amino acid alteration from A to V at position 29.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from V to L at position 158.
+The protein's natural variant, known as found in patients with familial episodic ataxia and impairment of speech development; unknown pathological significance;, features a modification of the amino acid from E to K at position 224.
+The protein's natural variant, known as in MRXSW;, features a modification of the amino acid from R to Q at position 450.
+The protein's natural variant, known as in MRXSW; homomers have minimal or no current; heteromers have altered desensitization kinetics;, features a modification of the amino acid from R to S at position 631.
+The protein's natural variant, known as in MRXSW; homomers have minimal or no current; heteromers have altered desensitization kinetics;, features a modification of the amino acid from M to T at position 706.
+The protein's natural variant, known as in MRXSW; reduced receptor expression possibly due to rapid degradation;, features a modification of the amino acid from G to R at position 833.
+The protein's natural variant, known as in MARSIS;, features a modification of the amino acid from R to K at position 1913.
+The protein's natural variant, known as in GGM;, features a modification of the amino acid from D to G at position 28.
+The protein's natural variant, known as in GGM;, features a modification of the amino acid from D to N at position 28.
+The protein's natural variant, known as in GGM; slightly decreased activity;, features a modification of the amino acid from N to S at position 51.
+The protein's natural variant, known as in GGM; loss of activity, features a modification of the amino acid from R to W at position 135.
+The protein's natural variant, known as in GGM; loss of activity, features a modification of the amino acid from S to P at position 159.
+The protein's natural variant, known as in GGM; about 90% reduction in activity, features a modification of the amino acid from A to T at position 166.
+The protein's natural variant, known as in GGM; about 95% reduction in activity, features a modification of the amino acid from W to L at position 276.
+The protein's natural variant, known as in GGM; loss of activity, features a modification of the amino acid from C to Y at position 292.
+The protein's natural variant, known as in GGM; loss of activity, features a modification of the amino acid from Q to R at position 295.
+The protein's natural variant, known as in GGM; loss of activity, features a modification of the amino acid from R to S at position 300.
+The protein's natural variant, known as in GGM; impairs trafficking to the plasma membrane, features a modification of the amino acid from A to V at position 304.
+The protein's natural variant, known as in GGM;, features a modification of the amino acid from G to R at position 318.
+The protein's natural variant, known as in GGM; loss of activity, features a modification of the amino acid from L to S at position 369.
+The protein's natural variant, known as in GGM; loss of activity, features a modification of the amino acid from R to Q at position 379.
+The protein's natural variant, known as in GGM; loss of activity, features a modification of the amino acid from A to V at position 388.
+The protein's natural variant, known as in GGM; loss of activity, features a modification of the amino acid from F to S at position 405.
+The protein's natural variant, known as in GGM; slightly decreased activity;, features a modification of the amino acid from A to T at position 411.
+The protein's natural variant, known as in GGM; loss of activity, features a modification of the amino acid from G to R at position 426.
+The protein's natural variant, known as in GGM;, features a modification of the amino acid from A to V at position 468.
+The protein's natural variant, known as in GGM; requires 2 nucleotide substitutions; about 90% reduction in activity, features a modification of the amino acid from V to N at position 470.
+The protein's natural variant, known as in GGM; impairs trafficking to the plasma membrane; decreases the sugar affinity, features a modification of the amino acid from R to H at position 499.
+The protein's natural variant, known as in GGM; slightly decreased activity, features a modification of the amino acid from H to Q at position 615.
+The protein's natural variant, known as in strain: 6471/76 / Serotype O:3, features a modification of the amino acid from D to E at position 32.
+The protein's natural variant, known as in THES1;, features a modification of the amino acid from G to R at position 251.
+The protein's natural variant, known as found in a THES1 patient, features a modification of the amino acid from A to D at position 1077.
+The protein's natural variant, known as found in a THES1 patient;, features a modification of the amino acid from P to A at position 1270.
+The protein's natural variant, known as in THES1, features a modification of the amino acid from D to N at position 1283.
+The protein's natural variant, known as found in a THES1 patient, features a modification of the amino acid from L to R at position 1485.
+The protein's natural variant, known as in THES1;, features a modification of the amino acid from L to S at position 1505.
+The protein's natural variant, known as in a colorectal carcinoma sample, features a modification of the amino acid from R to C at position 133.
+The protein's natural variant, known as in CHTD8, features a modification of the amino acid from W to C at position 274.
+The protein's natural variant, known as in LDS6; unknown pathological significance, features a modification of the amino acid from A to V at position 278.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from D to V at position 300.
+The protein's natural variant, known as in CHTD8, features a modification of the amino acid from C to S at position 312.
+The protein's natural variant, known as found in a patient with Marfan syndrome-like phenotype; unknown pathological significance, features a modification of the amino acid from N to K at position 318.
+The protein's natural variant, known as in LDS6; unknown pathological significance, features a modification of the amino acid from N to T at position 361.
+The protein's natural variant, known as in LDS6; unknown pathological significance, features a modification of the amino acid from Q to R at position 388.
+The protein's natural variant, known as in LDS6; unknown pathological significance, features a modification of the amino acid from S to Y at position 397.
+The protein's natural variant, known as in a colorectal carcinoma sample, features a modification of the amino acid from L to R at position 440.
+The protein's natural variant, known as in a colorectal carcinoma sample, features a modification of the amino acid from P to H at position 445.
+The protein's natural variant, known as in LDS6; unknown pathological significance, features a modification of the amino acid from L to S at position 449.
+The protein's natural variant, known as in a colorectal carcinoma sample, features a modification of the amino acid from D to E at position 450.
+The protein's natural variant, known as in LDS6, features a modification of the amino acid from G to R at position 457.
+The protein's natural variant, known as found in a patient suspected to suffer from Marfan syndrome; unknown pathological significance, features a modification of the amino acid from S to L at position 467.
+The protein's natural variant, known as in ML4; decreases formation and extrusion of tubulo-vesicular structures when overexpressed; disrupts tetrameric assembly; abolishes lysosomal localization;, features a modification of the amino acid from L to P at position 106.
+The protein's natural variant, known as in ML4; fails to localize to late endosomes; abolishes Fe(2+) permeability; disrupts tetrameric assembly; abolishes lysosomal localization;, features a modification of the amino acid from T to P at position 232.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from V to L at position 331.
+The protein's natural variant, known as in ML4; affects channel activity; abolishes Fe(2+) permeability;, features a modification of the amino acid from D to Y at position 362.
+The protein's natural variant, known as in ML4; impairs Fe(2+) permeability;, features a modification of the amino acid from R to C at position 403.
+The protein's natural variant, known as in ML4; does not affect channel activity; affects channel inhibition by low pH; impairs Fe(2+) permeability;, features a modification of the amino acid from V to L at position 446.
+The protein's natural variant, known as in ML4;, features a modification of the amino acid from L to P at position 447.
+The protein's natural variant, known as in ML4; still localizes to late endosomes; fails to rescue defect of lactosylceramide traffic through the late endocytic pathway in ML4 patient cells; minor effect on formation and extrusion of tubulo-vesicular structures when overexpressed;, features a modification of the amino acid from F to L at position 465.
+The natural variant of this protein is characterized by an amino acid alteration from M to T at position 102.
+The protein's natural variant, known as in strain: BALB/c and C3H/HeJ, features a modification of the amino acid from G to S at position 539.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from A to P at position 317.
+The protein's natural variant, known as in NEM8;, features a modification of the amino acid from D to H at position 34.
+The protein's natural variant, known as in NEM8, features a modification of the amino acid from L to P at position 86.
+The protein's natural variant, known as in NEM8, features a modification of the amino acid from V to E at position 194.
+The protein's natural variant, known as in NEM8;, features a modification of the amino acid from W to L at position 201.
+The protein's natural variant, known as in NEM8;, features a modification of the amino acid from R to L at position 311.
+The protein's natural variant, known as in NEM8;, features a modification of the amino acid from P to L at position 397.
+The protein's natural variant, known as in NEM8;, features a modification of the amino acid from H to R at position 455.
+The protein's natural variant, known as in NEM8;, features a modification of the amino acid from G to C at position 469.
+The protein's natural variant, known as in NEM8; unknown pathological significance;, features a modification of the amino acid from R to C at position 500.
+The protein's natural variant, known as in NEM8, features a modification of the amino acid from A to P at position 505.
+The protein's natural variant, known as in NEM8;, features a modification of the amino acid from T to P at position 506.
+The protein's natural variant, known as in NEM8;, features a modification of the amino acid from E to K at position 528.
+The protein's natural variant, known as in NEM8;, features a modification of the amino acid from A to P at position 538.
+The protein's natural variant, known as in NEM8;, features a modification of the amino acid from E to K at position 588.
+The protein's natural variant, known as in strain: Congo 159, Congo 194 and Congo 216, features a modification of the amino acid from E to V at position 5.
+The protein's natural variant, known as in strain: Africa-1 and Africa-5, features a modification of the amino acid from A to S at position 48.
+The protein's natural variant, known as in strain: Congo 216, features a modification of the amino acid from D to E at position 119.
+The protein's natural variant, known as in strain: Congo 8, Congo 13, Congo 194 and Mof.820A.s, features a modification of the amino acid from G to D at position 156.
+The protein's natural variant, known as in strain: Africa-0, features a modification of the amino acid from G to C at position 202.
+The protein's natural variant, known as in strain: Congo 194, features a modification of the amino acid from A to V at position 254.
+The protein's natural variant, known as in strain: Africa-0, Africa-3, Africa-4, Congo 194 and Mof.591A.s, features a modification of the amino acid from F to Y at position 384.
+The protein's natural variant, known as in strain: cv. Kas-1, features a modification of the amino acid from K to N at position 1213.
+The protein's natural variant, known as in strain: cv. Kas-1, features a modification of the amino acid from A to G at position 1245.
+The protein's natural variant, known as in strain: cv. Kas-1, features a modification of the amino acid from E to G at position 1299.
+The protein's natural variant, known as in strain: UM4082, features a modification of the amino acid from Y to F at position 101.
+The protein's natural variant, known as in strain: UM4102, features a modification of the amino acid from Y to S at position 101.
+The protein's natural variant, known as in helpless, features a modification of the amino acid from L to R at position 102.
+The protein's natural variant, known as in HD; disrupts sequence-specific DNA-binding; no effect on homodimerization or interaction with HDAC4 and HDAC5, features a modification of the amino acid from R to G at position 389.
+The natural variant of this protein is characterized by an amino acid alteration from G to GGGG at position 30.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from L to I at position 269.
+The protein's natural variant, known as in strain: FA19, features a modification of the amino acid from A to V at position 85.
+The protein's natural variant, known as in strain: FA19, features a modification of the amino acid from R to G at position 216.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to H at position 1128.
+The protein's natural variant, known as in CHTD5; decreased transcriptional activity;, features a modification of the amino acid from Y to D at position 16.
+The protein's natural variant, known as in CHTD5; unknown pathological significance, features a modification of the amino acid from R to G at position 132.
+The protein's natural variant, known as in CHTD5; decreased transcriptional activity, features a modification of the amino acid from Y to F at position 138.
+The protein's natural variant, known as in CHTD5; unknown pathological significance;, features a modification of the amino acid from Y to H at position 142.
+The protein's natural variant, known as in CHTD5; unknown pathological significance, features a modification of the amino acid from G to V at position 184.
+The protein's natural variant, known as in CHTD5; decreased transcriptional activity, features a modification of the amino acid from R to G at position 187.
+The protein's natural variant, known as in CHTD5; unknown pathological significance;, features a modification of the amino acid from V to A at position 190.
+The protein's natural variant, known as in CHTD5; decreased transcriptional activity;, features a modification of the amino acid from L to V at position 199.
+The protein's natural variant, known as in CHTD5; decreased transcriptional activity;, features a modification of the amino acid from W to G at position 200.
+The protein's natural variant, known as in CHTD5; unknown pathological significance; decreased transcriptional activity;, features a modification of the amino acid from D to E at position 203.
+The protein's natural variant, known as in CHTD5; decreased transcriptional activity, features a modification of the amino acid from H to R at position 207.
+The protein's natural variant, known as in CHTD5; decreased transcriptional activity;, features a modification of the amino acid from C to G at position 210.
+The protein's natural variant, known as in CHTD5; unknown pathological significance, features a modification of the amino acid from K to T at position 218.
+The protein's natural variant, known as in CHTD5; unknown pathological significance, features a modification of the amino acid from N to H at position 223.
+The protein's natural variant, known as in CHTD5; decreased transcriptional activity, features a modification of the amino acid from G to D at position 240.
+The protein's natural variant, known as in CHTD5; decreased transcriptional activity, features a modification of the amino acid from T to P at position 252.
+The protein's natural variant, known as in CHTD5; unknown pathological significance, features a modification of the amino acid from A to P at position 266.
+The protein's natural variant, known as in CHTD5; unknown pathological significance, features a modification of the amino acid from H to R at position 274.
+The protein's natural variant, known as in EVC;, features a modification of the amino acid from S to N at position 206.
+The protein's natural variant, known as in WAD;, features a modification of the amino acid from S to P at position 307.
+The protein's natural variant, known as in EVC;, features a modification of the amino acid from R to Q at position 443.
+The protein's natural variant, known as in EVC; atypical phenotype with septal cardiac defects, rhizomelic limb shortening and polydactyly without the typical lip, dental and nail abnormalities of EVC;, features a modification of the amino acid from L to P at position 623.
+The natural variant of this protein is characterized by an amino acid alteration from D to G at position 953.
+The protein's natural variant, known as in strain: O44:K74, features a modification of the amino acid from C to R at position 98.
+The protein's natural variant, known as in strain: O44:K74, features a modification of the amino acid from RA to PR at position 253.
+The protein's natural variant, known as in strain: O44:K74 and B, features a modification of the amino acid from Q to R at position 286.
+The protein's natural variant, known as in strain: O44:K74, features a modification of the amino acid from I to S at position 328.
+The protein's natural variant, known as in strain: O44:K74 and B, features a modification of the amino acid from V to A at position 345.
+The protein's natural variant, known as in strain: B, features a modification of the amino acid from R to C at position 359.
+The protein's natural variant, known as in strain: O44:K74 and B, features a modification of the amino acid from I to V at position 374.
+The protein's natural variant, known as in strain: O44:K74 and B, features a modification of the amino acid from Q to K at position 388.
+The protein's natural variant, known as in strain: O44:K74, features a modification of the amino acid from A to V at position 396.
+The protein's natural variant, known as in strain: O44:K74, features a modification of the amino acid from R to C at position 408.
+The protein's natural variant, known as in strain: O44:K74 and B, features a modification of the amino acid from D to G at position 412.
+The protein's natural variant, known as in strain: O44:K74 and B, features a modification of the amino acid from A to T at position 442.
+The protein's natural variant, known as in strain: O44:K74, features a modification of the amino acid from L to LDL at position 503.
+The protein's natural variant, known as in strain: L2, features a modification of the amino acid from L to V at position 48.
+The protein's natural variant, known as in strain: L2, features a modification of the amino acid from E to V at position 65.
+The protein's natural variant, known as in strain: L2, features a modification of the amino acid from N to D at position 70.
+The protein's natural variant, known as in CMRES;, features a modification of the amino acid from A to T at position 26.
+The protein's natural variant, known as in CMRES;, features a modification of the amino acid from V to L at position 29.
+The protein's natural variant, known as in CMRES, features a modification of the amino acid from D to G at position 36.
+The protein's natural variant, known as in CMRES;, features a modification of the amino acid from D to Y at position 36.
+The protein's natural variant, known as in CMRES;, features a modification of the amino acid from V to A at position 45.
+The protein's natural variant, known as in CMRES, features a modification of the amino acid from S to W at position 52.
+The protein's natural variant, known as in CMRES, features a modification of the amino acid from S to F at position 56.
+The protein's natural variant, known as in CMRES;, features a modification of the amino acid from R to G at position 58.
+The protein's natural variant, known as in CMRES, features a modification of the amino acid from W to C at position 59.
+The protein's natural variant, known as in CMRES, features a modification of the amino acid from W to L at position 59.
+The protein's natural variant, known as in CMRES, features a modification of the amino acid from V to G at position 66.
+The protein's natural variant, known as in CMRES;, features a modification of the amino acid from V to M at position 66.
+The protein's natural variant, known as in CMRES, features a modification of the amino acid from G to A at position 71.
+The protein's natural variant, known as in CMRES, features a modification of the amino acid from N to S at position 77.
+The protein's natural variant, known as in CMRES;, features a modification of the amino acid from N to Y at position 77.
+The protein's natural variant, known as in VKCFD2; strongly reduced enzyme activity;, features a modification of the amino acid from R to W at position 98.
+The protein's natural variant, known as in CMRES, features a modification of the amino acid from I to N at position 123.
+The protein's natural variant, known as in CMRES;, features a modification of the amino acid from L to R at position 128.
+The protein's natural variant, known as in CMRES, features a modification of the amino acid from Y to H at position 139.
+The natural variant of this protein is characterized by an amino acid alteration from C to R at position 13.
+The protein's natural variant, known as found in ethnically diverse individuals;, features a modification of the amino acid from E to A at position 16.
+The natural variant of this protein is characterized by an amino acid alteration from S to P at position 37.
+The natural variant of this protein is characterized by an amino acid alteration from Q to R at position 96.
+The natural variant of this protein is characterized by an amino acid alteration from Q to R at position 146.
+The natural variant of this protein is characterized by an amino acid alteration from S to G at position 207.
+The natural variant of this protein is characterized by an amino acid alteration from N to S at position 218.
+The natural variant of this protein is characterized by an amino acid alteration from Q to R at position 301.
+The natural variant of this protein is characterized by an amino acid alteration from V to L at position 9.
+The natural variant of this protein is characterized by an amino acid alteration from K to M at position 48.
+The protein's natural variant, known as in strain: KY02106G9, features a modification of the amino acid from D to N at position 121.
+The protein's natural variant, known as in strain: KY02106G9, MEL6G59 and KSA2, features a modification of the amino acid from Y to N at position 129.
+The protein's natural variant, known as in HLD14; decreased ability to form thioester bonds with UBA5 and UFC1; decreased protein ufmylation; does not affect the cellular response to endoplasmic reticulum stress;, features a modification of the amino acid from R to C at position 81.
+The protein's natural variant, known as in CDG1D;, features a modification of the amino acid from G to D at position 118.
+The protein's natural variant, known as in CDG1D;, features a modification of the amino acid from R to Q at position 171.
+The protein's natural variant, known as found in a family with global developmental delay and myopathic hypotonia; unknown pathological significance, features a modification of the amino acid from R to C at position 538.
+The protein's natural variant, known as in clone W516, features a modification of the amino acid from L to Q at position 175.
+The protein's natural variant, known as in clone W516, features a modification of the amino acid from N to S at position 443.
+The protein's natural variant, known as in clone W516, features a modification of the amino acid from I to V at position 450.
+The protein's natural variant, known as in a gastric adenocarcinoma sample; somatic mutation, features a modification of the amino acid from Y to C at position 233.
+The protein's natural variant, known as in an ovarian serous carcinoma sample; somatic mutation, features a modification of the amino acid from N to T at position 355.
+The protein's natural variant, known as in TKFCD; very severe decrease of triokinase and glycerone kinase activities;, features a modification of the amino acid from G to S at position 445.
+The protein's natural variant, known as in TKFCD; reduced protein levels in patient cells; very severe decrease of triokinase and glycerone kinase activities;, features a modification of the amino acid from R to I at position 543.
+The protein's natural variant, known as in KRS; no effect on stability; no effect on location; decreased ATPase activity;, features a modification of the amino acid from T to M at position 12.
+The protein's natural variant, known as in KRS; decreased protein stability; loss of autophosphorylation; increased degradation by proteasome; novel location to endoplasmic reticulum; loss of lysosomal membrane location; impaired autophagosome-lysosome fusion; impaired degradation of protein aggregates, features a modification of the amino acid from F to L at position 182.
+The protein's natural variant, known as in KRS; unknown pathological significance; associated in cis with Thr-1069 in one individual;, features a modification of the amino acid from I to F at position 441.
+The protein's natural variant, known as in KRS; decreased protein stability; increased degradation by proteasome; novel location to endoplasmic reticulum; loss of lysosomal membrane location; impaired autophagosome-lysosome fusion; impaired degradation of protein aggregates;, features a modification of the amino acid from G to R at position 504.
+The protein's natural variant, known as in SPG78; no effect on protein stability; loss of autophosphorylation; loss of lysosomal location; loss of ATPase activity;, features a modification of the amino acid from T to I at position 517.
+The protein's natural variant, known as in KRS; unknown pathological significance, features a modification of the amino acid from G to V at position 522.
+The protein's natural variant, known as in a patient with early onset Parkinson disease and KRS; decreased ATPase activity; no effect on autophosphorylation; no effect on stability; no effect on location, features a modification of the amino acid from G to R at position 533.
+The protein's natural variant, known as in KRS; decreased ATPase activity; no effect on stability; no effect on location;, features a modification of the amino acid from A to T at position 746.
+The protein's natural variant, known as in KRS; some patients manifest neuropathologic findings suggestive of neuronal ceroid lipofuscinosis;, features a modification of the amino acid from M to R at position 854.
+The protein's natural variant, known as in KRS; found in two affected brothers also carrying C-481 in FBXO7; decreased protein stability; increased degradation by proteasome; novel location to endoplasmic reticulum; loss of ATPase activity; loss of autophosphorylation;, features a modification of the amino acid from G to R at position 877.
+The protein's natural variant, known as in KRS; the mutant protein is retained in the endoplasmic reticulum;, features a modification of the amino acid from L to R at position 1059.
+The protein's natural variant, known as in KRS; unknown pathological significance; associated in cis with Phe-441 in one individual;, features a modification of the amino acid from A to T at position 1069.
+The protein's natural variant, known as probable disease-associated variant found in a family with atypical autism and severe epilepsy; disrupts potassium current inactivation;, features a modification of the amino acid from V to M at position 404.
+The protein's natural variant, known as in strain: North Carolina 29, features a modification of the amino acid from Q to L at position 112.
+The protein's natural variant, known as in strain: North Carolina 19, Zimbabwe 4 and Zimbabwe 70, features a modification of the amino acid from R to Q at position 142.
+The protein's natural variant, known as in strain: Zimbabwe 4 and Zimbabwe 70, features a modification of the amino acid from K to R at position 145.
+The protein's natural variant, known as in strain: Colombia 32, features a modification of the amino acid from T to N at position 146.
+The protein's natural variant, known as in strain: North Carolina 19, Mexico 12 and Zimbabwe 4, features a modification of the amino acid from P to S at position 156.
+The protein's natural variant, known as in strain: Zimbabwe 70 and Zimbabwe 79, features a modification of the amino acid from N to Q at position 171.
+The protein's natural variant, known as in strain: Zimbabwe 70 and Zimbabwe 79, features a modification of the amino acid from E to A at position 172.
+The protein's natural variant, known as in strain: Mexico 2, Mexico 12, Mexico 23, Mexico 31, North Carolina 19, North Carolina 29, Zimbabwe 4, Zimbabwe 19, Zimbabwe 21, Zimbabwe 50, Zimbabwe 70, Zimbabwe 79, features a modification of the amino acid from V to D at position 173.
+The protein's natural variant, known as in strain: Colombia 32, features a modification of the amino acid from V to I at position 185.
+The protein's natural variant, known as in strain: Mexico 2, Mexico 23, Mexico 31, Zimbabwe 19, Zimbabwe 21, Zimbabwe 50, features a modification of the amino acid from V to M at position 185.
+The protein's natural variant, known as in strain: Zimbabwe 4, features a modification of the amino acid from M to I at position 192.
+The protein's natural variant, known as in strain: Mexico 2, Mexico 23, Mexico 31, Zimbabwe 19, Zimbabwe 21 and Zimbabwe 50, features a modification of the amino acid from M to V at position 192.
+The protein's natural variant, known as in strain: Zimbabwe 4, features a modification of the amino acid from A to S at position 193.
+The protein's natural variant, known as in strain: Colombia 32, Mexico 12, North Carolina 19, Zimbabwe 4 and Zimbabwe 70, features a modification of the amino acid from H to Q at position 212.
+The protein's natural variant, known as in strain: Mexico 2, Mexico 23, Mexico 31, Zimbabwe 19, Zimbabwe 21 and Zimbabwe 50, features a modification of the amino acid from E to V at position 220.
+The protein's natural variant, known as in strain: Mexico 12, features a modification of the amino acid from A to V at position 228.
+The protein's natural variant, known as in strain: Mexico 2, Mexico 12, Mexico 23, Mexico 31, North Carolina 19, Zimbabwe 19, Zimbabwe 21, Zimbabwe 50, features a modification of the amino acid from P to Q at position 238.
+The protein's natural variant, known as in strain: Mexico 12, features a modification of the amino acid from R to P at position 245.
+The protein's natural variant, known as in strain: Mexico 2, Mexico 12, Mexico 23, Mexico 31, Zimbabwe 4, Zimbabwe 19, Zimbabwe 21, Zimbabwe 50, Zimbabwe 70, Zimbabwe 79, features a modification of the amino acid from M to I at position 265.
+The protein's natural variant, known as in strain: Mexico 12, features a modification of the amino acid from L to I at position 274.
+The protein's natural variant, known as in P2-2, features a modification of the amino acid from M to K at position 7.
+The protein's natural variant, known as in P3, features a modification of the amino acid from S to D at position 23.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from V to I at position 659.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from V to I at position 1702.
+The protein's natural variant, known as in MRT44; unknown pathological significance, features a modification of the amino acid from M to T at position 150.
+The protein's natural variant, known as in strain: Eagan, features a modification of the amino acid from D to Y at position 140.
+The protein's natural variant, known as in strain: Eagan, features a modification of the amino acid from T to A at position 321.
+The protein's natural variant, known as in strain: Eagan, features a modification of the amino acid from V to M at position 431.
+The protein's natural variant, known as in strain: Eagan, features a modification of the amino acid from W to G at position 440.
+The protein's natural variant, known as in strain: Eagan, features a modification of the amino acid from S to P at position 465.
+The protein's natural variant, known as in strain: Eagan, features a modification of the amino acid from T to P at position 523.
+The protein's natural variant, known as in strain: Eagan, features a modification of the amino acid from E to K at position 724.
+The protein's natural variant, known as in strain: ECOR 52 and ECOR 60, features a modification of the amino acid from A to T at position 5.
+The protein's natural variant, known as in strain: ECOR 52 and ECOR 60, features a modification of the amino acid from N to K at position 13.
+The protein's natural variant, known as in strain: ECOR 4, features a modification of the amino acid from P to S at position 223.
+The protein's natural variant, known as in strain: ECOR 4, ECOR 16, ECOR 28, ECOR 31, ECOR 37, ECOR 46, ECOR 50, ECOR 52, ECOR 60 and ECOR 71, features a modification of the amino acid from L to Q at position 405.
+The protein's natural variant, known as in strain: ECOR 46, features a modification of the amino acid from E to K at position 406.
+The protein's natural variant, known as in strain: ECOR 46, features a modification of the amino acid from S to N at position 411.
+The protein's natural variant, known as in strain: ECOR 46, features a modification of the amino acid from S to L at position 414.
+The protein's natural variant, known as in strain: ECOR 28, features a modification of the amino acid from A to V at position 415.
+The protein's natural variant, known as in strain: D273-10B, features a modification of the amino acid from IS to KT at position 458.
+The protein's natural variant, known as in NPHPL2; results in exon 6 skipping; results in loss of magnesium ion transmembrane transporter activity; does not affect localization to basolateral cell membrane, features a modification of the amino acid from G to V at position 233.
+The protein's natural variant, known as increased magnesium ion transmembrane transporter activity; no effect on plasma membrane localization;, features a modification of the amino acid from A to V at position 350.
+The protein's natural variant, known as in WSN2;, features a modification of the amino acid from M to T at position 108.
+The protein's natural variant, known as in WSN2;, features a modification of the amino acid from L to P at position 111.
+The protein's natural variant, known as in WSN2;, features a modification of the amino acid from N to S at position 112.
+The protein's natural variant, known as in WSN2; unknown pathological significance;, features a modification of the amino acid from R to C at position 114.
+The protein's natural variant, known as in WSN2; unknown pathological significance;, features a modification of the amino acid from R to H at position 114.
+The protein's natural variant, known as in WSN2;, features a modification of the amino acid from L to P at position 115.
+The protein's natural variant, known as in WSN2, features a modification of the amino acid from Y to D at position 118.
+The protein's natural variant, known as in WSN2;, features a modification of the amino acid from L to P at position 119.
+The natural variant of this protein is characterized by an amino acid alteration from K to E at position 83.
+The protein's natural variant, known as in strain: AH-101, features a modification of the amino acid from E to D at position 38.
+The protein's natural variant, known as in strain: AH-101, features a modification of the amino acid from KK to EE at position 70.
+The protein's natural variant, known as in strain: AH-101, features a modification of the amino acid from KLKK to ELQN at position 77.
+The protein's natural variant, known as in strain: AH-101, features a modification of the amino acid from K to E at position 86.
+The protein's natural variant, known as in strain: AH-101, features a modification of the amino acid from N to S at position 104.
+The protein's natural variant, known as in strain: AH-101, features a modification of the amino acid from N to Y at position 292.
+The protein's natural variant, known as in strain: AH-101, features a modification of the amino acid from PS to SN at position 347.
+The protein's natural variant, known as in Drk-a1', features a modification of the amino acid from L to F at position 18.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to C at position 315.
+The protein's natural variant, known as in strain: dp cn bw, features a modification of the amino acid from V to G at position 59.
+The protein's natural variant, known as in strain: dp cn bw, features a modification of the amino acid from K to M at position 121.
+The natural variant of this protein is characterized by an amino acid alteration from P to A at position 439.
+The protein's natural variant, known as in DFNB117; due to a nucleotide substitution that can result in aberrant splicing; patient cells contain both normally spliced transcripts and transcripts that retained intron 2;, features a modification of the amino acid from T to K at position 165.
+The protein's natural variant, known as retains capacity to promote Tn synthase activity;, features a modification of the amino acid from D to E at position 131.
+The protein's natural variant, known as in TNPS; loss capacity to promote Tn synthase activity;, features a modification of the amino acid from E to K at position 152.
+The protein's natural variant, known as in TNPS;, features a modification of the amino acid from S to P at position 193.
+The protein's natural variant, known as in strain: CDC84-060418, CDC77-124615 and CDC84-060384, features a modification of the amino acid from D to DD at position 346.
+The protein's natural variant, known as in strain: CDC84-060418, CDC77-124615 and CDC84-060384, features a modification of the amino acid from F to L at position 504.
+The protein's natural variant, known as in strain: CDC84-060418, CDC77-124615 and CDC84-060384, features a modification of the amino acid from A to V at position 510.
+The protein's natural variant, known as in strain: CDC84-060418, CDC77-124615 and CDC84-060384, features a modification of the amino acid from A to G at position 516.
+The protein's natural variant, known as in strain: FA19 and CDC84-060418, features a modification of the amino acid from H to N at position 541.
+The protein's natural variant, known as in strain: CDC84-060384, features a modification of the amino acid from P to L at position 551.
+The protein's natural variant, known as in strain: CDC77-124615, features a modification of the amino acid from P to S at position 551.
+The protein's natural variant, known as in strain: CDC84-060418, features a modification of the amino acid from P to V at position 552.
+The protein's natural variant, known as in strain: CDC84-060418, features a modification of the amino acid from KI to QV at position 556.
+The protein's natural variant, known as in strain: CDC84-060418, features a modification of the amino acid from I to V at position 566.
+The protein's natural variant, known as in strain: CDC84-060418, features a modification of the amino acid from A to NV at position 574.
+The protein's natural variant, known as in ACADSD;, features a modification of the amino acid from R to W at position 46.
+The protein's natural variant, known as in ACADSD; loss of acyl-CoA dehydrogenase activity;, features a modification of the amino acid from G to S at position 90.
+The protein's natural variant, known as in ACADSD;, features a modification of the amino acid from G to C at position 92.
+The protein's natural variant, known as in ACADSD;, features a modification of the amino acid from R to C at position 107.
+The protein's natural variant, known as 69% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria;, features a modification of the amino acid from R to W at position 171.
+The protein's natural variant, known as in ACADSD;, features a modification of the amino acid from W to R at position 177.
+The protein's natural variant, known as in ACADSD; loss of acyl-CoA dehydrogenase activity;, features a modification of the amino acid from A to V at position 192.
+The protein's natural variant, known as 86% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria;, features a modification of the amino acid from G to S at position 209.
+The protein's natural variant, known as in ACADSD; loss of acyl-CoA dehydrogenase activity;, features a modification of the amino acid from R to W at position 325.
+The protein's natural variant, known as in ACADSD; loss of acyl-CoA dehydrogenase activity;, features a modification of the amino acid from S to L at position 353.
+The protein's natural variant, known as in ACADSD; loss of acyl-CoA dehydrogenase activity;, features a modification of the amino acid from R to W at position 380.
+The protein's natural variant, known as in ACADSD;, features a modification of the amino acid from R to C at position 383.
+The protein's natural variant, known as in COD4 and ACHM5; severely decreases cGMP phosphodiesterase activity;, features a modification of the amino acid from R to W at position 29.
+The protein's natural variant, known as in ACHM5; severely decreases cGMP phosphodiesterase activity;, features a modification of the amino acid from R to W at position 104.
+The protein's natural variant, known as in ACHM5; decreases cGMP phosphodiesterase activity;, features a modification of the amino acid from Y to N at position 323.
+The protein's natural variant, known as in ACHM5; severely decreases cGMP phosphodiesterase activity, features a modification of the amino acid from P to L at position 391.
+The protein's natural variant, known as in ACHM5; decreases cGMP phosphodiesterase activity;, features a modification of the amino acid from M to V at position 455.
+The protein's natural variant, known as in ACHM5; severely decreases cGMP phosphodiesterase activity;, features a modification of the amino acid from H to L at position 602.
+The protein's natural variant, known as in ACHM5; decreases cGMP phosphodiesterase activity;, features a modification of the amino acid from E to K at position 790.
+The protein's natural variant, known as found in a renal cell carcinoma sample; somatic mutation, features a modification of the amino acid from I to S at position 826.
+The protein's natural variant, known as abrogates TEA transport activity;, features a modification of the amino acid from G to E at position 462.
+The protein's natural variant, known as decreased carnitine transport; decreased acetylcholine transport;, features a modification of the amino acid from L to F at position 503.
+The protein's natural variant, known as in DEE3; disrupts L-glutamate transporter activity;, features a modification of the amino acid from P to L at position 206.
+The protein's natural variant, known as in MOCODA;, features a modification of the amino acid from R to W at position 67.
+The protein's natural variant, known as in MOCODA;, features a modification of the amino acid from R to W at position 73.
+The protein's natural variant, known as in MOCODA;, features a modification of the amino acid from C to G at position 80.
+The protein's natural variant, known as in MOCODA, features a modification of the amino acid from C to F at position 84.
+The protein's natural variant, known as in MOCODA;, features a modification of the amino acid from R to W at position 123.
+The protein's natural variant, known as in MOCODA;, features a modification of the amino acid from G to D at position 126.
+The protein's natural variant, known as in MOCODA, features a modification of the amino acid from G to D at position 127.
+The protein's natural variant, known as in MOCODA;, features a modification of the amino acid from R to Q at position 319.
+The protein's natural variant, known as in MOCODA;, features a modification of the amino acid from G to E at position 324.
+The protein's natural variant, known as in MOCODA;, features a modification of the amino acid from G to R at position 324.
+The protein's natural variant, known as increased risk for Graves disease, insulin-dependent diabetes mellitus, thyroid-associated orbitopathy, systemic lupus erythematosus and susceptibility to HBV infection;, features a modification of the amino acid from T to A at position 17.
+The protein's natural variant, known as in IDAIL;, features a modification of the amino acid from R to W at position 70.
+The protein's natural variant, known as in OHST; strongly enhances monovalent cation leak;, features a modification of the amino acid from I to R at position 61.
+The protein's natural variant, known as in OHST; enhances monovalent cation leak; decreases ammonium fluxes; highly decreases STOM expression; decreases membrane expression; no effect on water permeability;, features a modification of the amino acid from F to S at position 65.
+The protein's natural variant, known as in RHN;, features a modification of the amino acid from S to N at position 79.
+The protein's natural variant, known as in Duclos or RHAG1 antigen (030001);, features a modification of the amino acid from Q to E at position 106.
+The protein's natural variant, known as in DSLK or RHAG3 antigen (030003);, features a modification of the amino acid from K to Q at position 164.
+The protein's natural variant, known as in Ol(a) or RHAG2 antigen (030002);, features a modification of the amino acid from S to L at position 227.
+The protein's natural variant, known as in RHN;, features a modification of the amino acid from G to E at position 279.
+The protein's natural variant, known as in RHN;, features a modification of the amino acid from G to R at position 280.
+The protein's natural variant, known as in RHN;, features a modification of the amino acid from G to V at position 380.
+The natural variant of this protein is characterized by an amino acid alteration from T to P at position 398.
+The natural variant of this protein is characterized by an amino acid alteration from L to V at position 401.
+The natural variant of this protein is characterized by an amino acid alteration from H to K at position 454.
+The protein's natural variant, known as in strain: Serotype A11 / PH240 and Serotype UG3 / PH496, features a modification of the amino acid from N to K at position 40.
+The protein's natural variant, known as in strain: Serotype UG3 / PH496, features a modification of the amino acid from G to E at position 121.
+The protein's natural variant, known as in strain: Serotype A11 / PH498, features a modification of the amino acid from L to F at position 232.
+The natural variant of this protein is characterized by an amino acid alteration from S to R at position 178.
+The protein's natural variant, known as in a lung neuroendocrine carcinoma sample; somatic mutation, features a modification of the amino acid from E to K at position 50.
+The natural variant of this protein is characterized by an amino acid alteration from I to K at position 1418.
+The protein's natural variant, known as in strain: 2CPA7 and 2CPA14, features a modification of the amino acid from L to P at position 6.
+The protein's natural variant, known as in strain: 2CPA12, 2CPA43, 2CPA46, 2CPA51, 2CPA103 and 2CPA105, features a modification of the amino acid from A to T at position 15.
+The protein's natural variant, known as in strain: 2CPA1, 2CPA12, 2CPA43, 2CPA46, 2CPA51, 2CPA103 and 2CPA105, features a modification of the amino acid from V to M at position 17.
+The protein's natural variant, known as in strain: 2CPA7 and 2CPA14, features a modification of the amino acid from E to D at position 38.
+The protein's natural variant, known as in Mel 1a(beta), features a modification of the amino acid from A to D at position 282.
+The protein's natural variant, known as in Mel 1a(beta), features a modification of the amino acid from H to R at position 358.
+The protein's natural variant, known as in Mel 1a(beta), features a modification of the amino acid from I to V at position 361.
+The protein's natural variant, known as in DEE98; decreased sodium/potassium-exchanging ATPase activity; decreased affinity for sodium ions;, features a modification of the amino acid from I to M at position 293.
+The protein's natural variant, known as in DEE98;, features a modification of the amino acid from C to F at position 341.
+The protein's natural variant, known as in DEE98; decreased affinity for sodium ions; decreased affinity for potassium ions;, features a modification of the amino acid from G to A at position 366.
+The protein's natural variant, known as in AHC1;, features a modification of the amino acid from T to N at position 378.
+The protein's natural variant, known as probable disease-associated variant found in a patient with generalized tonic-clonic seizures; decreased sodium/potassium-exchanging ATPase activity;, features a modification of the amino acid from R to Q at position 593.
+The protein's natural variant, known as in DEE98;, features a modification of the amino acid from R to W at position 593.
+The protein's natural variant, known as in FHM2;, features a modification of the amino acid from R to Q at position 689.
+The protein's natural variant, known as in FHM2; de novo mutation in a sporadic case;, features a modification of the amino acid from G to R at position 715.
+The protein's natural variant, known as in FHM2;, features a modification of the amino acid from M to T at position 731.
+The protein's natural variant, known as in FHM2; loss of function;, features a modification of the amino acid from L to P at position 764.
+The protein's natural variant, known as in FHM2; some patients exhibit a clinical overlap between migraine and epilepsy;, features a modification of the amino acid from G to S at position 874.
+The protein's natural variant, known as in FHM2; loss of function;, features a modification of the amino acid from W to R at position 887.
+The protein's natural variant, known as in DEE98; decreased sodium/potassium-exchanging ATPase activity, features a modification of the amino acid from R to Q at position 908.
+The protein's natural variant, known as in FHM2; some patients exhibit a clinical overlap between migraine and epilepsy;, features a modification of the amino acid from R to W at position 1007.
+The protein's natural variant, known as probable disease-associated variant found in a patient with azoospermia; requires 2 nucleotide substitutions, features a modification of the amino acid from R to A at position 217.
+The protein's natural variant, known as probable disease-associated variant found in a patient with azoospermia; requires 2 nucleotide substitutions, features a modification of the amino acid from L to A at position 220.
+The protein's natural variant, known as probable disease-associated variant found in a patient with azoospermia; requires 2 nucleotide substitutions, features a modification of the amino acid from L to G at position 220.
+The protein's natural variant, known as probable disease-associated variant found in a patient with azoospermia, features a modification of the amino acid from L to R at position 220.
+The protein's natural variant, known as probable disease-associated variant found in a patient with azoospermia, features a modification of the amino acid from N to H at position 224.
+The natural variant of this protein is characterized by an amino acid alteration from R to Q at position 286.
+The protein's natural variant, known as in HMGCS2D; abolished protein expression;, features a modification of the amino acid from V to M at position 54.
+The protein's natural variant, known as in HMGCS2D; decreased protein abundance; abolished enzymatic activity;, features a modification of the amino acid from R to W at position 112.
+The protein's natural variant, known as in HMGCS2D; decreased protein abundance; stong reduction of enzymatic activity;, features a modification of the amino acid from V to L at position 144.
+The protein's natural variant, known as in HMGCS2D; abolished enzymatic activity;, features a modification of the amino acid from Y to C at position 167.
+The protein's natural variant, known as in HMGCS2D;, features a modification of the amino acid from G to S at position 168.
+The protein's natural variant, known as in HMGCS2D; decreased protein abundance; abolished enzymatic activity;, features a modification of the amino acid from G to D at position 169.
+The protein's natural variant, known as in HMGCS2D; reduced peptide level; strong reduction of enzymatic activity;, features a modification of the amino acid from F to L at position 174.
+The protein's natural variant, known as in HMGCS2D; strong decreased of protein expression; abolished enzymatic activity, features a modification of the amino acid from W to R at position 185.
+The protein's natural variant, known as in HMGCS2D; abolished protein expression;, features a modification of the amino acid from R to H at position 188.
+The protein's natural variant, known as in HMGCS2D; abolished protein expression;, features a modification of the amino acid from G to R at position 212.
+The protein's natural variant, known as in HMGCS2D; decreased protein abundance; abolished enzymatic activity;, features a modification of the amino acid from G to V at position 232.
+The protein's natural variant, known as in HMGCS2D; decreased protein abundance; abolished enzymatic activity;, features a modification of the amino acid from L to S at position 266.
+The protein's natural variant, known as in HMGCS2D; abolished enzymatic activity, features a modification of the amino acid from M to T at position 307.
+The protein's natural variant, known as in HMGCS2D, features a modification of the amino acid from S to P at position 360.
+The protein's natural variant, known as in HMGCS2D; abolished protein expression;, features a modification of the amino acid from G to R at position 388.
+The protein's natural variant, known as in HMGCS2D; decreased protein abundance; abolished enzymatic activity; requires 2 nucleotide substitutions, features a modification of the amino acid from F to T at position 470.
+The protein's natural variant, known as in HMGCS2D; abolished enzymatic activity;, features a modification of the amino acid from R to H at position 500.
+The protein's natural variant, known as in HMGCS2D; decreased protein abundance; stong reduction of enzymatic activity, features a modification of the amino acid from Y to C at position 503.
+The protein's natural variant, known as in HMGCS2D; decreased protein abundance; stong reduction of enzymatic activity;, features a modification of the amino acid from R to Q at position 505.
+The protein's natural variant, known as in strain: NC732 and NC390, features a modification of the amino acid from G to E at position 90.
+The protein's natural variant, known as in strain: MW6, features a modification of the amino acid from D to Y at position 97.
+The protein's natural variant, known as in strain: MW11, MW27, NC301 and NC397, features a modification of the amino acid from M to I at position 122.
+The protein's natural variant, known as in strain: MW11, features a modification of the amino acid from S to N at position 131.
+The protein's natural variant, known as in strain: MW11, features a modification of the amino acid from N to S at position 155.
+The protein's natural variant, known as in strain: MW25, MW38, MW56, MW63, MW9, NC304, NC357 and NC361, features a modification of the amino acid from R to C at position 162.
+The protein's natural variant, known as in strain: MW6, MW9, MW11, MW25, MW27, MW38, MW56, MW63, NC301, NC304, NC357, NC361, NC390, NC397 and NC732, features a modification of the amino acid from I to M at position 211.
+The protein's natural variant, known as in strain: MW11, features a modification of the amino acid from T to S at position 240.
+The protein's natural variant, known as in strain: NC357, features a modification of the amino acid from A to S at position 292.
+The protein's natural variant, known as in strain: NC397, features a modification of the amino acid from G to D at position 346.
+The protein's natural variant, known as in strain: NC335, features a modification of the amino acid from D to N at position 349.
+The protein's natural variant, known as in strain: MW6, MW27, NC301, NC304 and NC397, features a modification of the amino acid from A to T at position 383.
+The natural variant of this protein is characterized by an amino acid alteration from L to V at position 405.
+The natural variant of this protein is characterized by an amino acid alteration from V to L at position 408.
+The natural variant of this protein is characterized by an amino acid alteration from E to D at position 421.
+The natural variant of this protein is characterized by an amino acid alteration from S to G at position 423.
+The natural variant of this protein is characterized by an amino acid alteration from K to R at position 426.
+The protein's natural variant, known as in strain: NZB/BlNJ and C57BL/6, features a modification of the amino acid from I to V at position 29.
+The protein's natural variant, known as in strain: NZB/BlNJ and C57BL/6, features a modification of the amino acid from T to S at position 36.
+The protein's natural variant, known as in strain: NZB/BlNJ and C57BL/6, features a modification of the amino acid from I to T at position 40.
+The protein's natural variant, known as in strain: NZB/BlNJ and C57BL/6, features a modification of the amino acid from F to I at position 178.
+The natural variant of this protein is characterized by an amino acid alteration from A to S at position 62.
+The natural variant of this protein is characterized by an amino acid alteration from A to T at position 62.
+The natural variant of this protein is characterized by an amino acid alteration from K to Q at position 116.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from L to V at position 168.
+The protein's natural variant, known as in DFNB94; probable loss-of-function variant; unable to rescue mitochondrial respiratory chain defects in NARS2 null fibroblasts; does not affect homodimerization; does not affect localization to mitochondrion;, features a modification of the amino acid from V to F at position 213.
+The protein's natural variant, known as in COXPD24;, features a modification of the amino acid from P to L at position 214.
+The protein's natural variant, known as in COXPD24; unknown pathological significance; no effect on homodimer formation; does not affect localization to mitochondrion, features a modification of the amino acid from N to D at position 381.
+The protein's natural variant, known as in COXPD24; does not form homodimers; does not affect localization to mitochondrion;, features a modification of the amino acid from N to S at position 381.
+The protein's natural variant, known as in COXPD24; unknown pathological significance; no effect on homodimer formation; does not affect localization to mitochondrion, features a modification of the amino acid from W to C at position 430.
+The protein's natural variant, known as in CDG1F;, features a modification of the amino acid from G to E at position 73.
+The protein's natural variant, known as in CDG1F;, features a modification of the amino acid from L to S at position 74.
+The protein's natural variant, known as in CDG1F;, features a modification of the amino acid from L to P at position 119.
+The protein's natural variant, known as in JBTS8; reduces binding to GTP;, features a modification of the amino acid from R to Q at position 79.
+The protein's natural variant, known as in JBTS8; the patient also manifests obesity as a feature; decreased localization to cilium;, features a modification of the amino acid from Y to C at position 86.
+The protein's natural variant, known as in JBTS8;, features a modification of the amino acid from R to C at position 200.
+The protein's natural variant, known as in a nephronophthisis (NPHP) patient, features a modification of the amino acid from R to L at position 390.
+The protein's natural variant, known as in strain: B5233 / ATCC 13073, features a modification of the amino acid from S to A at position 443.
+The protein's natural variant, known as in NEDSMBA; unknown pathological significance, features a modification of the amino acid from G to V at position 732.
+The protein's natural variant, known as in iron-insensitive tox constitutive mutant C7hm723, features a modification of the amino acid from R to H at position 47.
+The protein's natural variant, known as in strain: CD95/211-, features a modification of the amino acid from G to R at position 141.
+The protein's natural variant, known as in strain: C7(-), C7hm723(-), 1030(-), CD95/305-, CD95/211- and CD95/407-, features a modification of the amino acid from V to A at position 147.
+The protein's natural variant, known as in strain: 1030(-), features a modification of the amino acid from I to V at position 165.
+The protein's natural variant, known as in strain: 1030(-), features a modification of the amino acid from V to A at position 174.
+The protein's natural variant, known as in strain: 1030(-), features a modification of the amino acid from S to T at position 191.
+The protein's natural variant, known as in strain: CD95/407-, features a modification of the amino acid from D to V at position 199.
+The protein's natural variant, known as in strain: CD95/305-, features a modification of the amino acid from H to R at position 201.
+The protein's natural variant, known as in strain: 1030(-), features a modification of the amino acid from S to R at position 205.
+The protein's natural variant, known as in strain: C7(-), C7hm723(-), CD95/305-, CD95/211- and CD95/407-, features a modification of the amino acid from I to L at position 214.
+The protein's natural variant, known as in strain: 1030(-), features a modification of the amino acid from I to Y at position 214.
+The protein's natural variant, known as in strain: 1030(-), features a modification of the amino acid from A to T at position 218.
+The protein's natural variant, known as in strain: CD95/211-, features a modification of the amino acid from I to M at position 221.
+The protein's natural variant, known as in strain: CD95/407-, features a modification of the amino acid from I to T at position 221.
+The protein's natural variant, known as in HTRDC; severely decreased taurine transport activity in patient cells; does not affect cell membrane localization, features a modification of the amino acid from A to E at position 78.
+The protein's natural variant, known as in HTRDC; decreased taurine transport activity; does not affect protein abundance; does not affect cell membrane localization, features a modification of the amino acid from G to V at position 399.
+The protein's natural variant, known as in alpha-3, features a modification of the amino acid from D to G at position 71.
+The protein's natural variant, known as in alpha-2, features a modification of the amino acid from Q to H at position 78.
+The protein's natural variant, known as in strain: Indian tick typhus, features a modification of the amino acid from P to A at position 61.
+The protein's natural variant, known as in strain: Indian tick typhus, features a modification of the amino acid from G to S at position 75.
+The protein's natural variant, known as in strain: Indian tick typhus, features a modification of the amino acid from K to N at position 78.
+The protein's natural variant, known as in strain: Indian tick typhus, features a modification of the amino acid from V to A at position 251.
+The protein's natural variant, known as in strain: Indian tick typhus, features a modification of the amino acid from N to D at position 413.
+The protein's natural variant, known as in strain: Indian tick typhus, features a modification of the amino acid from I to V at position 959.
+The protein's natural variant, known as in strain: Indian tick typhus, features a modification of the amino acid from A to T at position 988.
+The protein's natural variant, known as in strain: Indian tick typhus, features a modification of the amino acid from R to L at position 1139.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from DQI to EQV at position 13.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from F to S at position 121.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from R to G at position 528.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from IE to MK at position 692.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from G to R at position 1159.
+The protein's natural variant, known as in strain: NRRLY-53, features a modification of the amino acid from K to Q at position 208.
+The protein's natural variant, known as in strain: NRRLY-53, features a modification of the amino acid from A to T at position 239.
+The protein's natural variant, known as in strain: NRRLY-53, features a modification of the amino acid from T to S at position 262.
+The protein's natural variant, known as in strain: NRRLY-53, features a modification of the amino acid from LS to IF at position 281.
+The protein's natural variant, known as in DENNED; unknown pathological significance, features a modification of the amino acid from K to T at position 160.
+The protein's natural variant, known as in DENNED; unknown pathological significance, features a modification of the amino acid from H to Q at position 409.
+The protein's natural variant, known as in FENIB; Syracuse; decreased protein stability; decreased proteinase inhibitor activity; increased tendency to form polymers;, features a modification of the amino acid from S to P at position 49.
+The protein's natural variant, known as in FENIB; Portland, features a modification of the amino acid from S to R at position 52.
+The protein's natural variant, known as in strain: GB8E, features a modification of the amino acid from L to R at position 6.
+The protein's natural variant, known as in strain: GB4E, features a modification of the amino acid from S to R at position 11.
+The protein's natural variant, known as in strain: GB8E and GB336E, features a modification of the amino acid from F to N at position 42.
+The protein's natural variant, known as in strain: JR50E and GB139E, features a modification of the amino acid from E to D at position 58.
+The protein's natural variant, known as in strain: JR50E, GB8E and GB115E, features a modification of the amino acid from V to A at position 98.
+The protein's natural variant, known as in strain: JR341E, features a modification of the amino acid from F to S at position 130.
+The protein's natural variant, known as in strain: GB4E, JR50E, GB115E, GB139E, GB336E and JR341E, features a modification of the amino acid from D to G at position 170.
+The protein's natural variant, known as in strain: GB4E, JR50E, GB115E, GB139E, GB336E and JR341E, features a modification of the amino acid from M to T at position 266.
+The protein's natural variant, known as in strain: JR50E, features a modification of the amino acid from A to G at position 291.
+The protein's natural variant, known as in strain: GB115E, features a modification of the amino acid from A to T at position 307.
+The protein's natural variant, known as in strain: GB336E, features a modification of the amino acid from V to I at position 461.
+The protein's natural variant, known as in strain: JR50E and JR341E, features a modification of the amino acid from E to V at position 537.
+The natural variant of this protein is characterized by an amino acid alteration from T to A at position 437.
+The protein's natural variant, known as in DFNB109; hypomorphic mutation affecting alternative splicing in patient-derived induced pluripotent stem cells and other cell-based assays;, features a modification of the amino acid from L to V at position 259.
+The protein's natural variant, known as in HKPX1; impairs expression at the cell membrane; requires much higher glycine levels for channel activation;, features a modification of the amino acid from R to W at position 93.
+The protein's natural variant, known as in HKPX1; abolishes expression at the cell membrane; requires much higher glycine levels for channel activation;, features a modification of the amino acid from R to C at position 100.
+The protein's natural variant, known as in HKPX1; abolishes expression at the cell membrane; requires much higher glycine levels for channel activation;, features a modification of the amino acid from R to W at position 246.
+The protein's natural variant, known as in HKPX1; strongly increases sensitivity to extracellular glycine; high leak currents in the absence of glycine due to spontaneous channel opening, features a modification of the amino acid from Q to E at position 254.
+The protein's natural variant, known as in HKPX1; impairs expression at the cell membrane; requires much higher glycine levels for channel activation, features a modification of the amino acid from P to S at position 258.
+The protein's natural variant, known as in HKPX1; requires much higher glycine levels for channel activation;, features a modification of the amino acid from I to N at position 272.
+The protein's natural variant, known as in HKPX1; requires much higher glycine levels for channel activation and displays an increased rate of desensitization;, features a modification of the amino acid from P to T at position 278.
+The protein's natural variant, known as in HKPX1;, features a modification of the amino acid from R to H at position 280.
+The protein's natural variant, known as in HKPX1;, features a modification of the amino acid from Q to H at position 294.
+The protein's natural variant, known as in HKPX1; requires much higher glycine levels for channel activation;, features a modification of the amino acid from R to L at position 299.
+The protein's natural variant, known as in HKPX1; decreases unitary channel conductance and requires much higher glycine concentrations for activation;, features a modification of the amino acid from R to Q at position 299.
+The protein's natural variant, known as in HKPX1; requires much higher glycine levels for channel activation;, features a modification of the amino acid from K to E at position 304.
+The protein's natural variant, known as in HKPX1; requires much higher glycine levels for channel activation;, features a modification of the amino acid from Y to C at position 307.
+The protein's natural variant, known as in HKPX1; high leak currents in the absence of glycine due to spontaneous channel opening, features a modification of the amino acid from V to M at position 308.
+The protein's natural variant, known as in HKPX1; impairs expression at the cell membrane; requires much higher glycine levels for channel activation, features a modification of the amino acid from L to P at position 319.
+The protein's natural variant, known as in HKPX1; abolishes expression at the cell membrane, features a modification of the amino acid from D to A at position 424.
+The protein's natural variant, known as in HKPX1;, features a modification of the amino acid from R to H at position 428.
+The protein's natural variant, known as in HKPX1; displays leak currents in the absence of glycine due to spontaneous channel opening;, features a modification of the amino acid from R to H at position 450.
+The natural variant of this protein is characterized by an amino acid alteration from A to T at position 48.
+The natural variant of this protein is characterized by an amino acid alteration from A to V at position 96.
+The protein's natural variant, known as in ECYT4; impairs interaction with EGLN1 and VHL, features a modification of the amino acid from P to L at position 534.
+The protein's natural variant, known as in ECYT4, features a modification of the amino acid from M to T at position 535.
+The protein's natural variant, known as in ECYT4; impairs interaction with EGLN1;, features a modification of the amino acid from M to V at position 535.
+The protein's natural variant, known as in ECYT4; impairs interaction with EGLN1 and VHL;, features a modification of the amino acid from G to R at position 537.
+The protein's natural variant, known as in ECYT4; gain of function; affects hydroxylation;, features a modification of the amino acid from G to W at position 537.
+The protein's natural variant, known as in ECYT4; affects the interaction with EGLN1 and VHL, features a modification of the amino acid from F to L at position 540.
+The protein's natural variant, known as in PCTT; disrupts signal sequence cleavage site;, features a modification of the amino acid from A to V at position 16.
+The protein's natural variant, known as in PCTT; increased rate of activation;, features a modification of the amino acid from D to G at position 22.
+The protein's natural variant, known as in PCTT; increased rate of activation;, features a modification of the amino acid from K to R at position 23.
+The protein's natural variant, known as in PCTT;, features a modification of the amino acid from N to I at position 29.
+The protein's natural variant, known as in PCTT;, features a modification of the amino acid from N to T at position 29.
+The protein's natural variant, known as in PCTT; associated with Ile-29; the double mutant shows increased autocatalytic activation which is solely due to the Ile-29 mutation;, features a modification of the amino acid from N to S at position 54.
+The protein's natural variant, known as in PCTT; Lys-79 trypsin activates anionic trypsinogen PRSS2 2-fold while the common pancreatitis-associated mutants His-122 or Ile-29 have no such effect;, features a modification of the amino acid from E to K at position 79.
+The protein's natural variant, known as in PCTT;, features a modification of the amino acid from L to P at position 104.
+The protein's natural variant, known as in PCTT;, features a modification of the amino acid from R to C at position 116.
+The protein's natural variant, known as in PCTT; suppresses an autocleavage site;, features a modification of the amino acid from R to C at position 122.
+The protein's natural variant, known as in PCTT; suppresses an autocleavage site which is probably part of a fail-safe mechanism by which trypsin, which is activated within the pancreas, may be inactivated; loss of this cleavage site would permit autodigestion resulting in pancreatitis;, features a modification of the amino acid from R to H at position 122.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from T to M at position 137.
+The protein's natural variant, known as in PCTT, features a modification of the amino acid from C to F at position 139.
+The protein's natural variant, known as in RTS2;, features a modification of the amino acid from LTA to P at position 642.
+The protein's natural variant, known as in BGS;, features a modification of the amino acid from R to W at position 1021.
+The protein's natural variant, known as in strain: Isolate 1, features a modification of the amino acid from H to L at position 97.
+The protein's natural variant, known as in strain: Isolate 3, features a modification of the amino acid from F to S at position 121.
+The protein's natural variant, known as in strain: Isolate 4, features a modification of the amino acid from T to A at position 310.
+The protein's natural variant, known as in OLWS, features a modification of the amino acid from I to K at position 126.
+The protein's natural variant, known as in ARCI5; results in decreased synthesis of omega-hydroxyceramides;, features a modification of the amino acid from F to L at position 59.
+The protein's natural variant, known as in ARCI5; results in decreased synthesis of omega-hydroxyceramides;, features a modification of the amino acid from R to H at position 243.
+The protein's natural variant, known as in ARCI5; results in decreased synthesis of omega-hydroxyceramides;, features a modification of the amino acid from R to W at position 372.
+The protein's natural variant, known as in ARCI5; results in impaired synthesis of omega-hydroxyceramides;, features a modification of the amino acid from H to Y at position 435.
+The protein's natural variant, known as in ARCI5; results in impaired synthesis of omega-hydroxyceramides;, features a modification of the amino acid from H to D at position 436.
+The protein's natural variant, known as in allele DOB*01:02;, features a modification of the amino acid from R to Q at position 18.
+The protein's natural variant, known as in allele DOB*01:04;, features a modification of the amino acid from L to F at position 234.
+The protein's natural variant, known as in allele DOB*01:03;, features a modification of the amino acid from V to I at position 244.
+The protein's natural variant, known as in DEE70; severely impaired interaction with actin;, features a modification of the amino acid from N to I at position 479.
+The protein's natural variant, known as in DEE70; severely impaired interaction with actin;, features a modification of the amino acid from L to P at position 500.
+The protein's natural variant, known as in DEE70; loss of interaction with PP1 complex;, features a modification of the amino acid from R to C at position 521.
+The protein's natural variant, known as in ASGD7;, features a modification of the amino acid from R to C at position 880.
+The protein's natural variant, known as in strain: CIAT899, features a modification of the amino acid from R to P at position 63.
+The protein's natural variant, known as increased L-amino-acid oxidase activity;, features a modification of the amino acid from N to D at position 92.
+The protein's natural variant, known as in an ovarian cancer; decreased L-amino-acid oxidase activity, features a modification of the amino acid from R to G at position 102.
+The protein's natural variant, known as coumestan resistant, features a modification of the amino acid from N to K at position 1640.
+The protein's natural variant, known as coumestan resistant, features a modification of the amino acid from N to S at position 1640.
+The protein's natural variant, known as coumestan resistant, features a modification of the amino acid from D to G at position 1644.
+The protein's natural variant, known as coumestan resistant, features a modification of the amino acid from A to V at position 1667.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from T to N at position 209.
+The protein's natural variant, known as in SCAR18, features a modification of the amino acid from A to D at position 654.
+The protein's natural variant, known as in SCAR18; constitutively open the extracellular-glutamate-gated ion channel, features a modification of the amino acid from A to T at position 654.
+The protein's natural variant, known as in SCAR18, features a modification of the amino acid from L to V at position 656.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to W at position 172.
+The protein's natural variant, known as in MC4DN9;, features a modification of the amino acid from A to P at position 53.
+The protein's natural variant, known as in DELMNES;, features a modification of the amino acid from A to V at position 327.
+The protein's natural variant, known as in DELMNES, features a modification of the amino acid from N to I at position 376.
+The protein's natural variant, known as in DELMNES; requires 2 nucleotide substitutions, features a modification of the amino acid from A to L at position 379.
+The protein's natural variant, known as in DELMNES;, features a modification of the amino acid from R to Q at position 410.
+The protein's natural variant, known as in DFNA78;, features a modification of the amino acid from E to K at position 979.
+The protein's natural variant, known as in DELMNES;, features a modification of the amino acid from E to K at position 980.
+The protein's natural variant, known as in DFNA78; reduced chloride transmembrane transport;, features a modification of the amino acid from D to Y at position 981.
+The protein's natural variant, known as in DFNA78; reduced chloride transmembrane transport;, features a modification of the amino acid from P to T at position 988.
+The protein's natural variant, known as in an ovarian undifferentiated carcinoma sample; somatic mutation, features a modification of the amino acid from S to T at position 707.
+The protein's natural variant, known as in a gastric adenocarcinoma sample; somatic mutation, features a modification of the amino acid from I to V at position 719.
+The protein's natural variant, known as in a gastric adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from R to Q at position 743.
+The protein's natural variant, known as in strain: MA74, features a modification of the amino acid from H to Y at position 8.
+The protein's natural variant, known as in strain: NC1b, features a modification of the amino acid from M to I at position 59.
+The protein's natural variant, known as in strain: MA43 and MA74, features a modification of the amino acid from I to M at position 67.
+The protein's natural variant, known as in strain: NC1b and NC97a, features a modification of the amino acid from M to V at position 93.
+The protein's natural variant, known as in strain: CN1, CN13, CN18, CN21, CN29, CN45, CN51, LA128, LA13, LA15, LA25, LA3, LA32, LA34, LA35, LA4, MA21, MA24, NC1b, NC100b, NC37a, NC84a, NC89a and NC97a, features a modification of the amino acid from C to S at position 100.
+The protein's natural variant, known as in strain: NC97a, features a modification of the amino acid from F to L at position 102.
+The protein's natural variant, known as in strain: CN1, CN13, CN18, CN21, CN28, CN29, CN45, CN51, LA120, LA128, LA13, LA15, LA25, LA3, LA32, LA34, LA35, LA4, LA6, LA9, MA21, MA24, NC1b, NC100b, NC16a, NC37a, NC84a, NC89a and NC97a, features a modification of the amino acid from E to A at position 196.
+The protein's natural variant, known as in strain: NC1b and NC97a, features a modification of the amino acid from D to E at position 201.
+The protein's natural variant, known as in strain: CN14, features a modification of the amino acid from S to N at position 220.
+The protein's natural variant, known as in strain: CN13, features a modification of the amino acid from T to S at position 292.
+The protein's natural variant, known as in strain: LA6, features a modification of the amino acid from S to A at position 328.
+The protein's natural variant, known as in strain: LA6, features a modification of the amino acid from N to D at position 329.
+The protein's natural variant, known as in strain: LA6, features a modification of the amino acid from C to S at position 330.
+The protein's natural variant, known as in strain: LA6, features a modification of the amino acid from T to I at position 359.
+The protein's natural variant, known as in strain: LA6, features a modification of the amino acid from A to N at position 375.
+The protein's natural variant, known as in strain: LA6, features a modification of the amino acid from S to T at position 382.
+The protein's natural variant, known as in strain: NC1b and NC97a, features a modification of the amino acid from T to A at position 385.
+The protein's natural variant, known as in strain: LA6, features a modification of the amino acid from V to I at position 386.
+The protein's natural variant, known as in strain: LA6, features a modification of the amino acid from I to V at position 387.
+The protein's natural variant, known as in strain: LA6, features a modification of the amino acid from R to K at position 395.
+The protein's natural variant, known as in strain: GB4E, GB8E, GB139E and GB336E, features a modification of the amino acid from V to I at position 15.
+The protein's natural variant, known as in strain: GB4E, GB8E, GB115E, GB139E, GB336E, JR198E and JR341E, features a modification of the amino acid from S to G at position 139.
+The protein's natural variant, known as in strain: GB4E, GB8E, GB139E, JR50E and JR198E, features a modification of the amino acid from S to T at position 226.
+The protein's natural variant, known as in strain: GB4E, GB8E, GB115E, GB139E, GB336E, JR50E and JR198E, features a modification of the amino acid from L to V at position 228.
+The protein's natural variant, known as in strain: GB336E, features a modification of the amino acid from V to L at position 260.
+The protein's natural variant, known as in strain: JR341E, features a modification of the amino acid from S to N at position 266.
+The protein's natural variant, known as in strain: GB336E, features a modification of the amino acid from G to L at position 269.
+The protein's natural variant, known as in strain: GB4E, GB8E, GB115E, GB139E, JR198E and JR341E, features a modification of the amino acid from G to V at position 269.
+The protein's natural variant, known as in strain: JR341E, features a modification of the amino acid from I to S at position 281.
+The protein's natural variant, known as in strain: GB115E, features a modification of the amino acid from S to T at position 307.
+The protein's natural variant, known as in strain: JR198E, features a modification of the amino acid from K to M at position 327.
+The protein's natural variant, known as in strain: JR198E, features a modification of the amino acid from Q to K at position 330.
+The protein's natural variant, known as in strain: GB139E, features a modification of the amino acid from S to T at position 355.
+The protein's natural variant, known as in strain: JR341E, features a modification of the amino acid from Y to F at position 442.
+The protein's natural variant, known as in strain: JR341E, features a modification of the amino acid from E to D at position 451.
+The protein's natural variant, known as in strain: JR198E, features a modification of the amino acid from Q to H at position 456.
+The protein's natural variant, known as in strain: GB336E, features a modification of the amino acid from R to S at position 487.
+The protein's natural variant, known as in strain: GB139E and JR50E, features a modification of the amino acid from C to F at position 546.
+The protein's natural variant, known as in a cutaneous metastatic melanoma sample; somatic mutation;, features a modification of the amino acid from A to V at position 305.
+The protein's natural variant, known as in GNMT deficiency; 10% wild-type glycine N-methyltransferase activity;, features a modification of the amino acid from L to P at position 50.
+The protein's natural variant, known as in GNMT deficiency; 0.5% wild-type glycine N-methyltransferase activity;, features a modification of the amino acid from N to S at position 141.
+The protein's natural variant, known as in GNMT deficiency; 75% wild-type glycine N-methyltransferase activity, decreases stability of the tetramer;, features a modification of the amino acid from H to N at position 177.
+The natural variant of this protein is characterized by an amino acid alteration from T to TGG at position 73.
+The protein's natural variant, known as in HCI susceptibility; expression of FLT1 in hemangioma endothelial cells is markedly reduced compared to controls; low FLT1 expression in hemangioma cells is caused by reduced activity of a pathway involving ITGB1, ANTXR1, KDR and NFATC2IP; the mutation disrupts interaction of these molecules in a dominant-negative manner;, features a modification of the amino acid from A to T at position 326.
+The protein's natural variant, known as in SMDCD; strong reduction in protein levels and marked increase in cellular phosphatidylinositol 4,5 bisphosphate levels in patient cells, features a modification of the amino acid from A to S at position 878.
+The protein's natural variant, known as confirmed at protein level;, features a modification of the amino acid from S to G at position 58.
+The protein's natural variant, known as confirmed at protein level;, features a modification of the amino acid from K to R at position 74.
+The protein's natural variant, known as in strain: E/UW-5/Cx, features a modification of the amino acid from Y to H at position 155.
+The protein's natural variant, known as in strain: F3031, features a modification of the amino acid from G to E at position 4.
+The protein's natural variant, known as in strain: F3031, features a modification of the amino acid from F to L at position 44.
+The protein's natural variant, known as in strain: F3031, features a modification of the amino acid from C to S at position 49.
+The natural variant of this protein is characterized by an amino acid alteration from E to Q at position 264.
+The protein's natural variant, known as in PARK; unknown pathological significance;, features a modification of the amino acid from V to L at position 722.
+The protein's natural variant, known as in PARK; unknown pathological significance; affects regulation of endosomal membrane trafficking as indicated by accumulation of transferrin in endosomal compartments;, features a modification of the amino acid from N to S at position 855.
+The protein's natural variant, known as in PARK; sporadic case; unknown pathological significance;, features a modification of the amino acid from R to Q at position 1266.
+The protein's natural variant, known as in PARK; unknown pathological significance;, features a modification of the amino acid from T to M at position 1895.
+The protein's natural variant, known as in 2nd form, features a modification of the amino acid from H to V at position 37.
+The protein's natural variant, known as in 2nd form, features a modification of the amino acid from N to S at position 48.
+The protein's natural variant, known as in 2nd form, features a modification of the amino acid from AGN to SSH at position 57.
+The protein's natural variant, known as in 2nd form, features a modification of the amino acid from S to A at position 275.
+The protein's natural variant, known as in HLD16;, features a modification of the amino acid from D to N at position 252.
+The protein's natural variant, known as in strain: 28-1 and 42-1, features a modification of the amino acid from A to T at position 148.
+The protein's natural variant, known as in strain: 28-1 and 42-1, features a modification of the amino acid from Q to E at position 184.
+The protein's natural variant, known as in MSPC; increased NLRP1-inflammasome complex assembly; altered protein folding;, features a modification of the amino acid from A to T at position 54.
+The protein's natural variant, known as in MSPC; increased NLRP1-inflammasome complex assembly; altered protein folding;, features a modification of the amino acid from A to V at position 66.
+The protein's natural variant, known as in MSPC; destabilization of the N-terminal fragment;, features a modification of the amino acid from M to T at position 77.
+The protein's natural variant, known as in VAMAS1; risk factor;, features a modification of the amino acid from L to H at position 155.
+The protein's natural variant, known as in AIADK; unknown pathological significance;, features a modification of the amino acid from R to W at position 726.
+The protein's natural variant, known as in JRRP; gain-of-function variant resulting in spontaneous inflammasome activation; increased NLRP1-inflammasome complex assembly, features a modification of the amino acid from T to N at position 755.
+The protein's natural variant, known as no effect on autocatalytic processing, nor on IL1B release;, features a modification of the amino acid from M to V at position 1119.
+The protein's natural variant, known as increased autocatalytic processing and IL1B release;, features a modification of the amino acid from M to V at position 1184.
+The protein's natural variant, known as in AIADK; decreased interaction with DPP9, leading to increased inflammasome activity;, features a modification of the amino acid from P to R at position 1214.
+The natural variant of this protein is characterized by an amino acid alteration from R to T at position 143.
+The natural variant of this protein is characterized by an amino acid alteration from EK to KE at position 38.
+The natural variant of this protein is characterized by an amino acid alteration from V to L at position 46.
+The natural variant of this protein is characterized by an amino acid alteration from M to R at position 85.
+The natural variant of this protein is characterized by an amino acid alteration from D to H at position 150.
+The natural variant of this protein is characterized by an amino acid alteration from N to T at position 152.
+The natural variant of this protein is characterized by an amino acid alteration from S to R at position 155.
+The natural variant of this protein is characterized by an amino acid alteration from R to G at position 164.
+The natural variant of this protein is characterized by an amino acid alteration from W to Q at position 172.
+The natural variant of this protein is characterized by an amino acid alteration from H to R at position 175.
+The natural variant of this protein is characterized by an amino acid alteration from Y to H at position 180.
+The natural variant of this protein is characterized by an amino acid alteration from RP to KL at position 183.
+The natural variant of this protein is characterized by an amino acid alteration from R to K at position 182.
+The natural variant of this protein is characterized by an amino acid alteration from R to S at position 182.
+The natural variant of this protein is characterized by an amino acid alteration from E to S at position 192.
+The natural variant of this protein is characterized by an amino acid alteration from S to H at position 194.
+The natural variant of this protein is characterized by an amino acid alteration from S to Y at position 194.
+The natural variant of this protein is characterized by an amino acid alteration from K to W at position 200.
+The natural variant of this protein is characterized by an amino acid alteration from K to R at position 202.
+The natural variant of this protein is characterized by an amino acid alteration from T to A at position 206.
+The natural variant of this protein is characterized by an amino acid alteration from L to S at position 213.
+The natural variant of this protein is characterized by an amino acid alteration from S to Y at position 218.
+The natural variant of this protein is characterized by an amino acid alteration from A to T at position 220.
+The protein's natural variant, known as in PCH2B;, features a modification of the amino acid from Y to C at position 309.
+The protein's natural variant, known as in allele blue fox, features a modification of the amino acid from G to C at position 5.
+The protein's natural variant, known as in allele blue fox, features a modification of the amino acid from F to C at position 280.
+The protein's natural variant, known as in BSS;, features a modification of the amino acid from Y to C at position 113.
+The protein's natural variant, known as in BSS;, features a modification of the amino acid from A to P at position 133.
+The protein's natural variant, known as in NEDFCF; unknown pathological significance;, features a modification of the amino acid from T to R at position 186.
+The protein's natural variant, known as in NEDFCF; unknown pathological significance;, features a modification of the amino acid from P to H at position 416.
+The protein's natural variant, known as in NEDFCF;, features a modification of the amino acid from W to R at position 649.
+The protein's natural variant, known as in plasmid pCHL1, features a modification of the amino acid from H to Y at position 28.
+The protein's natural variant, known as in plasmid pCHL1 and plasmid pCTT1, features a modification of the amino acid from Y to H at position 244.
+The protein's natural variant, known as in plasmid pCHL1, features a modification of the amino acid from S to I at position 296.
+The protein's natural variant, known as in plasmid pCHL1 and plasmid pCTT1, features a modification of the amino acid from P to T at position 303.
+The protein's natural variant, known as in strain: FVB/N, features a modification of the amino acid from T to M at position 8.
+The protein's natural variant, known as in mutant M17, features a modification of the amino acid from G to E at position 75.
+The protein's natural variant, known as in HYDM2; unknown pathological significance;, features a modification of the amino acid from R to K at position 5.
+The protein's natural variant, known as in HYDM2; unknown pathological significance;, features a modification of the amino acid from E to Q at position 97.
+The protein's natural variant, known as in HYDM2; unknown pathological significance;, features a modification of the amino acid from A to G at position 201.
+The protein's natural variant, known as in CTHM and VCFS;, features a modification of the amino acid from F to Y at position 148.
+The protein's natural variant, known as in VCFS;, features a modification of the amino acid from H to Q at position 194.
+The protein's natural variant, known as in DGS;, features a modification of the amino acid from G to S at position 310.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from G to E at position 337.
+The protein's natural variant, known as in NLS2;, features a modification of the amino acid from A to V at position 99.
+The protein's natural variant, known as in PSATD; reduced Vmax;, features a modification of the amino acid from D to A at position 100.
+The protein's natural variant, known as in NLS2;, features a modification of the amino acid from S to L at position 179.
+The protein's natural variant, known as in DEE79; decreased subcellular localization to the cell membrane resulting in altered protein localization to the synapse and altered gamma-aminobutyric acid signaling pathway, features a modification of the amino acid from V to F at position 294.
+The protein's natural variant, known as in DEE79; increased affinity to GABA; decreased maximal GABA-evoked current density, features a modification of the amino acid from V to L at position 294.
+The protein's natural variant, known as in DEE79; decreased subcellular localization to the cell membrane resulting in altered protein localization to the synapse and altered gamma-aminobutyric acid signaling pathway; the mutant subunit decreases the trafficking of the partnering GABRB3 subunit to the cell membrane with no effect on other subunits, features a modification of the amino acid from S to F at position 413.
+The protein's natural variant, known as found in patients with female infertility; unknown pathological significance, features a modification of the amino acid from W to C at position 175.
+The protein's natural variant, known as found in patients with female infertility; unknown pathological significance;, features a modification of the amino acid from T to M at position 221.
+The protein's natural variant, known as found in patients with female infertility; unknown pathological significance;, features a modification of the amino acid from F to S at position 258.
+The protein's natural variant, known as found in patients with female infertility; unknown pathological significance;, features a modification of the amino acid from E to V at position 616.
+The protein's natural variant, known as found in patients with female infertility; unknown pathological significance, features a modification of the amino acid from E to D at position 848.
+The protein's natural variant, known as in COXPD17;, features a modification of the amino acid from F to L at position 154.
+The protein's natural variant, known as in HPC2;, features a modification of the amino acid from R to Q at position 211.
+The protein's natural variant, known as in HPC2; risk factor for disease development; does not affect the enzymatic activity;, features a modification of the amino acid from S to L at position 217.
+The protein's natural variant, known as in COXPD17;, features a modification of the amino acid from L to F at position 423.
+The protein's natural variant, known as in HPC2;, features a modification of the amino acid from G to R at position 487.
+The protein's natural variant, known as in COXPD17;, features a modification of the amino acid from T to I at position 520.
+The protein's natural variant, known as in HPC2; risk factor for disease development; does not affect the enzymatic activity;, features a modification of the amino acid from A to T at position 541.
+The protein's natural variant, known as in HPC2; higher frequency in prostate cancer cases;, features a modification of the amino acid from E to V at position 622.
+The protein's natural variant, known as in HPC2; does not affect the enzymatic activity;, features a modification of the amino acid from R to H at position 781.
+The protein's natural variant, known as in HPC2;, features a modification of the amino acid from G to R at position 806.
+The protein's natural variant, known as in strain: SAMP8, features a modification of the amino acid from S to T at position 9.
+The protein's natural variant, known as in strain: SAMP8, features a modification of the amino acid from D to E at position 40.
+The protein's natural variant, known as in strain: SAMP8, features a modification of the amino acid from E to CM at position 67.
+The protein's natural variant, known as in strain: SAMP8, features a modification of the amino acid from V to L at position 196.
+The protein's natural variant, known as in strain: SAMP8, features a modification of the amino acid from ER to RRD at position 322.
+The protein's natural variant, known as in POF19; in mice this mutation leads to a decreased protein stability with reduced fertility due to a lower frequency of crossovers in meiocytes;, features a modification of the amino acid from S to L at position 167.
+The protein's natural variant, known as in OI; severe, features a modification of the amino acid from G to A at position 208.
+The protein's natural variant, known as associated with increased risk for asthma development; at homozygosity associated with higher levels of serum total IgE in some allergic rhinitis patients;, features a modification of the amino acid from R to Q at position 144.
+The protein's natural variant, known as in GSD0;, features a modification of the amino acid from N to S at position 39.
+The protein's natural variant, known as in GSD0;, features a modification of the amino acid from A to P at position 339.
+The protein's natural variant, known as in GSD0;, features a modification of the amino acid from H to D at position 446.
+The protein's natural variant, known as in GSD0;, features a modification of the amino acid from P to Q at position 479.
+The protein's natural variant, known as in GSD0;, features a modification of the amino acid from S to P at position 483.
+The protein's natural variant, known as in GSD0;, features a modification of the amino acid from M to R at position 491.
+The protein's natural variant, known as sulfating activity toward both DHEA and pregnenolone is completely abolished;, features a modification of the amino acid from K to E at position 44.
+The protein's natural variant, known as decreases of the sulfotransferase activity toward DHEA; decreases of the sulfotransferase activity toward pregnenolone;, features a modification of the amino acid from P to T at position 76.
+The protein's natural variant, known as decreases of the sulfotransferase activity toward DHEA; no effect on the sulfotransferase activity toward pregnenolone;, features a modification of the amino acid from E to K at position 147.
+The protein's natural variant, known as decreases of the sulfotransferase activity toward DHEA; decreases of the sulfotransferase activity toward pregnenolone;, features a modification of the amino acid from E to K at position 148.
+The protein's natural variant, known as decreases of the sulfotransferase activity toward DHEA; decreases of the sulfotransferase activity toward pregnenolone;, features a modification of the amino acid from L to P at position 246.
+The protein's natural variant, known as decreases of the sulfotransferase activity toward DHEA; decreases of the sulfotransferase activity toward pregnenolone;, features a modification of the amino acid from F to L at position 258.
+The protein's natural variant, known as decreases of the sulfotransferase activity toward DHEA; no effect on the sulfotransferase activity toward pregnenolone;, features a modification of the amino acid from Q to E at position 262.
+The protein's natural variant, known as in VEODS; no effect on protein abundance; decreased DNA replication;, features a modification of the amino acid from I to S at position 79.
+The protein's natural variant, known as in VEODS; decreased protein abundance; may alter splicing;, features a modification of the amino acid from G to R at position 110.
+The protein's natural variant, known as in VEODS; no effect on protein abundance; decreased DNA replication;, features a modification of the amino acid from P to L at position 1381.
+The protein's natural variant, known as in IMD16;, features a modification of the amino acid from R to C at position 65.
+The protein's natural variant, known as in narcolepsy; autosomal recessive; loss of function, features a modification of the amino acid from E to K at position 54.
+The protein's natural variant, known as in lactoglobulin 2=A and 3=C, features a modification of the amino acid from H to Y at position 38.
+The protein's natural variant, known as in lactoglobulin 3=C, features a modification of the amino acid from R to Q at position 166.
+The protein's natural variant, known as in MRXS32; results in stimulation of RYR channels activity with channels remaining open for longer times; the mutation may impair insertion of the protein into the membrane to form a functioning ion channel;, features a modification of the amino acid from H to Q at position 101.
+The protein's natural variant, known as in CHNG8; unknown pathological significance; decreased protein expression, features a modification of the amino acid from N to Y at position 416.
+The protein's natural variant, known as in CHNG8; unknown pathological significance; no effect on protein expression, features a modification of the amino acid from A to T at position 417.
+The protein's natural variant, known as in CHNG8; unknown pathological significance, features a modification of the amino acid from W to R at position 420.
+The protein's natural variant, known as in CHNG8; unknown pathological significance; decreased protein expression, features a modification of the amino acid from H to Y at position 504.
+The protein's natural variant, known as in CHNG8; unknown pathological significance; no effect on protein expression, features a modification of the amino acid from Y to C at position 509.
+The protein's natural variant, known as found in a renal cell carcinoma sample; somatic mutation, features a modification of the amino acid from V to I at position 99.
+The protein's natural variant, known as in strain: Isolate NARA4.20, features a modification of the amino acid from T to A at position 17.
+The protein's natural variant, known as in strain: Isolate NARA4.20, features a modification of the amino acid from I to V at position 42.
+The protein's natural variant, known as in strain: Isolate NARA4.20, features a modification of the amino acid from M to I at position 58.
+The protein's natural variant, known as in strain: Isolate NARA4.20, features a modification of the amino acid from S to N at position 94.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from N to S at position 45.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from L to F at position 95.
+The protein's natural variant, known as somatic mutation in a breast cancer sample, features a modification of the amino acid from E to Q at position 99.
+The protein's natural variant, known as somatic mutation in a lung squamous cell carcinoma, features a modification of the amino acid from R to I at position 519.
+The protein's natural variant, known as in strain: 487/90 / Serotype 6, features a modification of the amino acid from I to M at position 11.
+The protein's natural variant, known as in strain: 487/90 / Serotype 6 and YPT1 /Serotype 3, features a modification of the amino acid from T to A at position 13.
+The protein's natural variant, known as in strain: 487/90 / Serotype 6, features a modification of the amino acid from M to I at position 21.
+The natural variant of this protein is characterized by an amino acid alteration from S to A at position 258.
+The protein's natural variant, known as in strain: Isolate 94sak1, features a modification of the amino acid from V to I at position 98.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation, features a modification of the amino acid from P to S at position 433.
+The protein's natural variant, known as in strain: NBD, features a modification of the amino acid from S to G at position 10.
+The protein's natural variant, known as in strain: Qingdao, features a modification of the amino acid from S to G at position 46.
+The protein's natural variant, known as in strain: NBD, features a modification of the amino acid from I to L at position 159.
+The protein's natural variant, known as in strain: NBD, features a modification of the amino acid from S to A at position 162.
+The protein's natural variant, known as in strain: NBD, features a modification of the amino acid from C to S at position 164.
+The protein's natural variant, known as in strain: 85-961, features a modification of the amino acid from K to R at position 37.
+The protein's natural variant, known as in strain: 85-961, features a modification of the amino acid from G to S at position 70.
+The protein's natural variant, known as in strain: 85-961, features a modification of the amino acid from E to D at position 78.
+The protein's natural variant, known as in strain: IFO 15366, features a modification of the amino acid from S to T at position 62.
+The protein's natural variant, known as in strain: IFO 15366, features a modification of the amino acid from E to D at position 66.
+The protein's natural variant, known as in RIEG1;, features a modification of the amino acid from L to Q at position 100.
+The protein's natural variant, known as in RDC; results in 25% loss of transactivation activity;, features a modification of the amino acid from R to H at position 108.
+The protein's natural variant, known as in RIEG1;, features a modification of the amino acid from P to L at position 110.
+The protein's natural variant, known as in RIEG1, features a modification of the amino acid from P to R at position 110.
+The protein's natural variant, known as in RIEG1;, features a modification of the amino acid from T to P at position 114.
+The protein's natural variant, known as in ASGD4;, features a modification of the amino acid from R to H at position 115.
+The protein's natural variant, known as in RIEG1; more than 200% increase in transactivation activity;, features a modification of the amino acid from V to L at position 129.
+The protein's natural variant, known as in ASGD4;, features a modification of the amino acid from R to W at position 130.
+The protein's natural variant, known as in RIEG1;, features a modification of the amino acid from K to E at position 134.
+The protein's natural variant, known as in RIEG1, features a modification of the amino acid from R to C at position 136.
+The protein's natural variant, known as in RIEG1;, features a modification of the amino acid from R to P at position 137.
+The protein's natural variant, known as in RIEG1, features a modification of the amino acid from L to V at position 151.
+The protein's natural variant, known as in RIEG1, features a modification of the amino acid from N to T at position 154.
+The protein's natural variant, known as in strain: Q903; susceptible, features a modification of the amino acid from E to D at position 448.
+The protein's natural variant, known as in strain: Q903; susceptible, features a modification of the amino acid from G to V at position 463.
+The protein's natural variant, known as in allele CYP4B1*3 and allele CYP4B1*6;, features a modification of the amino acid from R to W at position 173.
+The protein's natural variant, known as in allele CYP4B1*4;, features a modification of the amino acid from S to G at position 322.
+The protein's natural variant, known as in allele CYP4B1*2, allele CYP4B1*7 and allele CYP4B1*5;, features a modification of the amino acid from M to I at position 331.
+The protein's natural variant, known as in allele CYP4B1*2 and allele CYP4B1*7;, features a modification of the amino acid from R to C at position 340.
+The protein's natural variant, known as in allele CYP4B1*6;, features a modification of the amino acid from V to I at position 345.
+The protein's natural variant, known as in allele CYP4B1*2;, features a modification of the amino acid from R to C at position 375.
+The protein's natural variant, known as found in some patients with periodic paralysis; unknown pathological significance; alters voltage dependence, lowers current and diminishes open probability in KCNC4/KCNE3 channel; lowers current in KCNQ1/KCNE3 channel;, features a modification of the amino acid from R to H at position 83.
+The protein's natural variant, known as in BRGDA6; also in a patient suffering from drug-induced torsades de pointes; unknown pathological significance;, features a modification of the amino acid from R to H at position 99.
+The protein's natural variant, known as in strain: S3041, features a modification of the amino acid from A to G at position 390.
+The protein's natural variant, known as in strain: S3013, S3014, S3015, S3027 and S3041, features a modification of the amino acid from D to E at position 392.
+The protein's natural variant, known as in strain: S2978, S2979, S2980, S2983, S2985, S2993, S2995, S3013, S3014, S3015, S3027, S3041, S3044, S3057 and S3333, features a modification of the amino acid from A to S at position 432.
+The natural variant of this protein is characterized by an amino acid alteration from T to G at position 7.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from E to Q at position 187.
+The protein's natural variant, known as in NEDLAS; gain of function; when incorporated into kainate receptor, produces constitutively active channels with significantly altered gating kinetics; may decrease cell surface expression;, features a modification of the amino acid from A to T at position 657.
+The protein's natural variant, known as in NEDLAS; causes profound slowing of channel deactivation and constitutive tonic current activation compared to wild-type, indicating altered channel gating kinetics; may decrease cell surface expression, features a modification of the amino acid from T to K at position 660.
+The protein's natural variant, known as in NEDLAS; causes profound slowing of channel deactivation and constitutive tonic current activation compared to wild-type, indicating altered channel gating kinetics; may decrease cell surface expression, features a modification of the amino acid from T to R at position 660.
+The protein's natural variant, known as in NEDLAS; causes markedly reduced peak current amplitudes and very fast gating kinetics; no effect on homomeric receptor localization to the plasma membrane when expressed in heterologous cells, features a modification of the amino acid from I to T at position 668.
+The protein's natural variant, known as in RP40; autosomal recessive;, features a modification of the amino acid from R to C at position 74.
+The protein's natural variant, known as in RP40;, features a modification of the amino acid from R to H at position 100.
+The protein's natural variant, known as in RP40; autosomal recessive;, features a modification of the amino acid from Y to H at position 219.
+The protein's natural variant, known as in RP40; autosomal recessive and autosomal dominant, features a modification of the amino acid from L to H at position 228.
+The protein's natural variant, known as in CSNBAD2;, features a modification of the amino acid from H to N at position 258.
+The protein's natural variant, known as in RP40; autosomal recessive;, features a modification of the amino acid from L to P at position 527.
+The protein's natural variant, known as in RP40; autosomal recessive;, features a modification of the amino acid from I to N at position 535.
+The protein's natural variant, known as in RP40; autosomal recessive;, features a modification of the amino acid from R to Q at position 552.
+The protein's natural variant, known as in RP40; autosomal dominant;, features a modification of the amino acid from H to Y at position 557.
+The protein's natural variant, known as in RP40; autosomal recessive, features a modification of the amino acid from G to D at position 576.
+The protein's natural variant, known as in RP40; autosomal recessive, features a modification of the amino acid from L to R at position 699.
+The protein's natural variant, known as in RP40;, features a modification of the amino acid from D to N at position 776.
+The protein's natural variant, known as in RP40; autosomal recessive, features a modification of the amino acid from L to R at position 854.
+The protein's natural variant, known as in SLS; severe loss of activity, features a modification of the amino acid from I to F at position 45.
+The protein's natural variant, known as in SLS; severe loss of activity;, features a modification of the amino acid from V to D at position 64.
+The protein's natural variant, known as in SLS; severe loss of activity;, features a modification of the amino acid from L to R at position 106.
+The protein's natural variant, known as in SLS; severe loss of activity;, features a modification of the amino acid from P to L at position 114.
+The protein's natural variant, known as in SLS; severe loss of activity;, features a modification of the amino acid from P to L at position 121.
+The protein's natural variant, known as in SLS; severe loss of activity;, features a modification of the amino acid from T to M at position 184.
+The protein's natural variant, known as in SLS; severe loss of activity, features a modification of the amino acid from T to R at position 184.
+The protein's natural variant, known as in SLS; severe loss of activity;, features a modification of the amino acid from G to A at position 185.
+The protein's natural variant, known as in SLS; 4% of activity;, features a modification of the amino acid from C to Y at position 214.
+The protein's natural variant, known as in SLS;, features a modification of the amino acid from C to W at position 226.
+The protein's natural variant, known as in SLS; severe loss of activity;, features a modification of the amino acid from R to C at position 228.
+The protein's natural variant, known as in SLS; severe loss of activity;, features a modification of the amino acid from C to Y at position 237.
+The protein's natural variant, known as in SLS; severe loss of activity;, features a modification of the amino acid from D to N at position 245.
+The protein's natural variant, known as in SLS; mild reduction of activity; the underlying nucleotide substitution affects transcript stability;, features a modification of the amino acid from K to N at position 266.
+The protein's natural variant, known as in SLS; severe loss of activity;, features a modification of the amino acid from Y to N at position 279.
+The protein's natural variant, known as in SLS; 8% of activity, features a modification of the amino acid from AP to GAKSTVGA at position 315.
+The protein's natural variant, known as in SLS; common mutation in Europeans; severe loss of enzymatic activity;, features a modification of the amino acid from P to S at position 315.
+The protein's natural variant, known as in SLS;, features a modification of the amino acid from M to I at position 328.
+The protein's natural variant, known as in SLS; severe loss of activity;, features a modification of the amino acid from S to L at position 365.
+The protein's natural variant, known as in SLS;, features a modification of the amino acid from N to S at position 386.
+The protein's natural variant, known as in SLS, features a modification of the amino acid from G to R at position 406.
+The protein's natural variant, known as in SLS; severe loss of activity, features a modification of the amino acid from H to Y at position 411.
+The protein's natural variant, known as in SLS;, features a modification of the amino acid from G to R at position 412.
+The protein's natural variant, known as in SLS; severe loss of activity, features a modification of the amino acid from S to N at position 415.
+The protein's natural variant, known as in SLS; severe loss of activity;, features a modification of the amino acid from F to S at position 419.
+The protein's natural variant, known as in SLS; severe loss of activity;, features a modification of the amino acid from R to H at position 423.
+The protein's natural variant, known as in SLS; severe loss of activity;, features a modification of the amino acid from K to E at position 447.
+The protein's natural variant, known as found in a patient with Rett syndrome-like phenotype; unknown pathological significance;, features a modification of the amino acid from R to H at position 201.
+The protein's natural variant, known as in PARK18;, features a modification of the amino acid from A to V at position 502.
+The protein's natural variant, known as found in patients with Parkinson disease; unknown pathological significance;, features a modification of the amino acid from G to C at position 686.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from P to L at position 696.
+The protein's natural variant, known as found in a patient with Parkinson disease; unknown pathological significance;, features a modification of the amino acid from S to R at position 1164.
+The protein's natural variant, known as found in a patient with Parkinson disease; unknown pathological significance;, features a modification of the amino acid from R to W at position 1197.
+The protein's natural variant, known as in PARK18;, features a modification of the amino acid from R to H at position 1205.
+The protein's natural variant, known as in SCA38;, features a modification of the amino acid from L to V at position 72.
+The protein's natural variant, known as in SCA38;, features a modification of the amino acid from G to V at position 230.
+The protein's natural variant, known as in MTDPS17, features a modification of the amino acid from G to R at position 189.
+The protein's natural variant, known as found in a patient with connective tissue disorder and peripheral neuropathy; unknown pathological significance; decreased secretion; accumulates in the endoplasmic reticulum;, features a modification of the amino acid from A to T at position 22.
+The protein's natural variant, known as in HMN10; unable to rescue locomotor defects in Emilin1a zebrafish morphants; reduced extracellular deposition of EMILIN-1 from patient cells, features a modification of the amino acid from R to C at position 250.
+The natural variant of this protein is characterized by an amino acid alteration from Q to P at position 47.
+The protein's natural variant, known as in strain: COP; prostatic cancer cell lines, features a modification of the amino acid from V to I at position 120.
+The protein's natural variant, known as in strain: COP; prostatic cancer cell lines, features a modification of the amino acid from Q to H at position 916.
+The protein's natural variant, known as in strain: COP; prostatic cancer cell lines, features a modification of the amino acid from S to C at position 1202.
+The protein's natural variant, known as in strain: COP; prostatic cancer cell lines, features a modification of the amino acid from H to D at position 1257.
+The protein's natural variant, known as in strain: COP; prostatic cancer cell lines, features a modification of the amino acid from D to G at position 1755.
+The protein's natural variant, known as in strain: COP; prostatic cancer cell lines, features a modification of the amino acid from E to K at position 1803.
+The protein's natural variant, known as in CDG1R;, features a modification of the amino acid from G to D at position 217.
+The natural variant of this protein is characterized by an amino acid alteration from P to L at position 153.
+The natural variant of this protein is characterized by an amino acid alteration from R to Q at position 378.
+The natural variant of this protein is characterized by an amino acid alteration from C to Y at position 392.
+The protein's natural variant, known as in strain: Isolate SIM2, features a modification of the amino acid from F to L at position 50.
+The protein's natural variant, known as in strain: Isolate SIM2, features a modification of the amino acid from K to R at position 324.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from A to T at position 507.
+The natural variant of this protein is characterized by an amino acid alteration from L to P at position 27.
+The natural variant of this protein is characterized by an amino acid alteration from Q to H at position 355.
+The protein's natural variant, known as in SORDD, features a modification of the amino acid from L to F at position 10.
+The protein's natural variant, known as in SORDD; results in protein aggregation, features a modification of the amino acid from R to P at position 110.
+The protein's natural variant, known as in SORDD; results in protein aggregation, features a modification of the amino acid from H to R at position 135.
+The protein's natural variant, known as in SORDD; unknown pathological significance; results in protein aggregation;, features a modification of the amino acid from A to D at position 153.
+The protein's natural variant, known as in SORDD; unknown pathological significance;, features a modification of the amino acid from V to I at position 322.
+The protein's natural variant, known as in strain: U-51, features a modification of the amino acid from I to F at position 61.
+The protein's natural variant, known as in strain: U-51, features a modification of the amino acid from T to P at position 67.
+The protein's natural variant, known as in strain: Isolate Guatemala, features a modification of the amino acid from R to Q at position 59.
+The protein's natural variant, known as in ALS23; unknown pathological significance; changed cytoplasmic localization with decreased association with vesicle-like structures; increased interaction with S100A6;, features a modification of the amino acid from G to R at position 38.
+The protein's natural variant, known as in ALS23; forms cytoplasmic aggregates in patient tissues; no effect on nuclear and cytoplasmic localization; loss of interaction with S100A6;, features a modification of the amino acid from D to G at position 40.
+The protein's natural variant, known as in IBMWMA, features a modification of the amino acid from D to Y at position 40.
+The protein's natural variant, known as in ALS23; unknown pathological significance;, features a modification of the amino acid from G to R at position 175.
+The protein's natural variant, known as in ALS23; unknown pathological significance; no effect on aggregation; loss of interaction with S100A6;, features a modification of the amino acid from G to E at position 189.
+The protein's natural variant, known as in ALS23; unknown pathological significance; increased aggregation in the cytoplasm sequestering the wild-type protein in these aggregates; loss of interaction with S100A6;, features a modification of the amino acid from R to Q at position 235.
+The protein's natural variant, known as in ALS23; unknown pathological significance;, features a modification of the amino acid from R to C at position 346.
+The protein's natural variant, known as in MPS3A;, features a modification of the amino acid from D to E at position 32.
+The protein's natural variant, known as in MPS3A, features a modification of the amino acid from D to G at position 32.
+The protein's natural variant, known as in MPS3A; intermediate;, features a modification of the amino acid from Y to N at position 40.
+The protein's natural variant, known as in MPS3A; does not yield active enzyme; the reduction in 62 kDa precursor and 56 kDa mature forms suggests an increased degradation of the mutant enzyme, features a modification of the amino acid from N to K at position 42.
+The protein's natural variant, known as in MPS3A; severe;, features a modification of the amino acid from A to T at position 44.
+The protein's natural variant, known as in MPS3A; intermediate/severe; common mutation in Italy;, features a modification of the amino acid from S to W at position 66.
+The protein's natural variant, known as in MPS3A; intermediate/severe; the mutant is enzymatically inactive; rapid degradation rather than decrease in synthesis is responsible for the low steady state level of the mutant protein in cells; the majority of newly synthesized protein probably occurs in the endoplasmic reticulum;, features a modification of the amino acid from R to C at position 74.
+The protein's natural variant, known as in MPS3A;, features a modification of the amino acid from R to H at position 74.
+The protein's natural variant, known as in MPS3A; severe;, features a modification of the amino acid from T to P at position 79.
+The protein's natural variant, known as in MPS3A, features a modification of the amino acid from H to Y at position 84.
+The protein's natural variant, known as in MPS3A, features a modification of the amino acid from Q to R at position 85.
+The protein's natural variant, known as in MPS3A;, features a modification of the amino acid from M to T at position 88.
+The protein's natural variant, known as in MPS3A;, features a modification of the amino acid from G to R at position 90.
+The protein's natural variant, known as in MPS3A; shows 3.3% activity of the expressed wild-type enzyme; rapid degradation rather than decrease in synthesis is responsible for the low steady state level of the mutant protein in cells, features a modification of the amino acid from S to R at position 106.
+The protein's natural variant, known as in MPS3A; intermediate;, features a modification of the amino acid from G to R at position 122.
+The protein's natural variant, known as in MPS3A; intermediate;, features a modification of the amino acid from P to L at position 128.
+The protein's natural variant, known as in MPS3A;, features a modification of the amino acid from V to M at position 131.
+The protein's natural variant, known as in MPS3A;, features a modification of the amino acid from T to M at position 139.
+The protein's natural variant, known as in MPS3A; severe;, features a modification of the amino acid from L to P at position 146.
+The protein's natural variant, known as in MPS3A; severe;, features a modification of the amino acid from R to Q at position 150.
+The protein's natural variant, known as in MPS3A;, features a modification of the amino acid from R to W at position 150.
+The protein's natural variant, known as in MPS3A; the mutant is enzymatically inactive; rapid degradation rather than decrease in synthesis is responsible for the low steady state level of the mutant protein in cells; the mutant protein shows instability in the lysosomes, features a modification of the amino acid from L to P at position 163.
+The protein's natural variant, known as in MPS3A; severe;, features a modification of the amino acid from D to N at position 179.
+The protein's natural variant, known as in MPS3A; intermediate;, features a modification of the amino acid from R to C at position 182.
+The protein's natural variant, known as in MPS3A; the mutant is enzymatically inactive; rapid degradation rather than decrease in synthesis is responsible for the low steady state level of the mutant protein in cells; the majority of newly synthesized protein probably occurs in the endoplasmic reticulum;, features a modification of the amino acid from G to R at position 191.
+The protein's natural variant, known as in MPS3A, features a modification of the amino acid from F to L at position 193.
+The protein's natural variant, known as in MPS3A; the mutant enzyme retains 8% residual activity;, features a modification of the amino acid from R to P at position 206.
+The natural variant of this protein is characterized by an amino acid alteration from V to A at position 226.
+The protein's natural variant, known as in MPS3A; severe;, features a modification of the amino acid from P to R at position 227.
+The protein's natural variant, known as in MPS3A;, features a modification of the amino acid from A to G at position 234.
+The protein's natural variant, known as in MPS3A; does not yield active enzyme; the reduction in 62 kDa precursor and 56 kDa mature forms suggests an increased degradation of the mutant enzyme;, features a modification of the amino acid from D to N at position 235.
+The protein's natural variant, known as in MPS3A;, features a modification of the amino acid from D to V at position 235.
+The protein's natural variant, known as in MPS3A; severe; common mutation in Western Europe and Australia;, features a modification of the amino acid from R to H at position 245.
+The protein's natural variant, known as in MPS3A;, features a modification of the amino acid from G to A at position 251.
+The protein's natural variant, known as in MPS3A;, features a modification of the amino acid from D to N at position 273.
+The protein's natural variant, known as in MPS3A, features a modification of the amino acid from P to S at position 288.
+The protein's natural variant, known as in MPS3A; does not yield active enzyme; the reduction in 62 kDa precursor and 56 kDa mature forms suggests an increased degradation of the mutant enzyme;, features a modification of the amino acid from P to S at position 293.
+The protein's natural variant, known as in MPS3A, features a modification of the amino acid from P to T at position 293.
+The protein's natural variant, known as in MPS3A; associated with a slowly progressive clinical phenotype; rapidly degraded but small amounts of the mutant protein are correctly transported to the lysosome; low but significant residual enzymatic activity;, features a modification of the amino acid from S to P at position 298.
+The protein's natural variant, known as in MPS3A, features a modification of the amino acid from E to V at position 300.
+The protein's natural variant, known as in MPS3A, features a modification of the amino acid from Q to P at position 307.
+The protein's natural variant, known as in MPS3A;, features a modification of the amino acid from T to A at position 321.
+The protein's natural variant, known as in MPS3A, features a modification of the amino acid from I to S at position 322.
+The protein's natural variant, known as in MPS3A, features a modification of the amino acid from A to P at position 354.
+The protein's natural variant, known as in MPS3A;, features a modification of the amino acid from E to K at position 355.
+The protein's natural variant, known as in MPS3A;, features a modification of the amino acid from S to R at position 364.
+The protein's natural variant, known as in MPS3A; intermediate;, features a modification of the amino acid from E to K at position 369.
+The protein's natural variant, known as in MPS3A;, features a modification of the amino acid from Y to H at position 374.
+The protein's natural variant, known as in MPS3A; severe; does not yield active enzyme; the reduction in 62 kDa precursor and 56 kDa mature forms suggests an increased degradation of the mutant enzyme;, features a modification of the amino acid from R to C at position 377.
+The protein's natural variant, known as in MPS3A;, features a modification of the amino acid from R to H at position 377.
+The protein's natural variant, known as in MPS3A;, features a modification of the amino acid from Q to R at position 380.
+The protein's natural variant, known as in MPS3A, features a modification of the amino acid from H to HQR at position 381.
+The protein's natural variant, known as in MPS3A, features a modification of the amino acid from L to R at position 386.
+The protein's natural variant, known as in MPS3A;, features a modification of the amino acid from N to K at position 389.
+The protein's natural variant, known as in MPS3A, features a modification of the amino acid from YRAR to W at position 435.
+The protein's natural variant, known as in MPS3A; severe;, features a modification of the amino acid from R to Q at position 433.
+The protein's natural variant, known as in MPS3A; the mutant is enzymatically inactive; rapid degradation rather than decrease in synthesis is responsible for the low steady state level of the mutant protein in cells; the majority of newly synthesized protein probably occurs in the endoplasmic reticulum;, features a modification of the amino acid from R to W at position 433.
+The protein's natural variant, known as in MPS3A;, features a modification of the amino acid from E to K at position 447.
+The protein's natural variant, known as does not affect enzyme activity; cells transfected with the mutant enzyme contain a 62 kDa precursor and a 56 kDa mature form as cells transfected with the wild-type enzyme;, features a modification of the amino acid from R to H at position 456.
+The protein's natural variant, known as in MPS3A; unknown pathological significance;, features a modification of the amino acid from D to N at position 477.
+The protein's natural variant, known as in MPS3A, features a modification of the amino acid from V to F at position 486.
+The protein's natural variant, known as in HFE3;, features a modification of the amino acid from V to I at position 22.
+The protein's natural variant, known as in HFE3;, features a modification of the amino acid from M to K at position 172.
+The protein's natural variant, known as hereditary hemochromatosis modifier;, features a modification of the amino acid from R to Q at position 455.
+The protein's natural variant, known as in HFE3;, features a modification of the amino acid from Q to P at position 690.
+The protein's natural variant, known as in minor component, features a modification of the amino acid from I to T at position 13.
+The protein's natural variant, known as in minor component, features a modification of the amino acid from S to N at position 23.
+The protein's natural variant, known as in minor component, features a modification of the amino acid from P to F at position 24.
+The protein's natural variant, known as in HH14; does not affect the interaction with EMX1; does not affect the subcellular location of the protein; decreases capacity to shuttle from cilium to nucleus; decreases GLI3 protein levels;, features a modification of the amino acid from R to W at position 395.
+The protein's natural variant, known as in HH14; abolishes the interaction with EMX1; does not affect the subcellular location of the protein; decreases capacity to shuttle from cilium to nucleus; decreases interaction with EMX1; decreases GLI3 protein levels;, features a modification of the amino acid from A to T at position 435.
+The protein's natural variant, known as in HH14; reduces the interaction with EMX1; does not affect the subcellular location of the protein; decreases capacity to shuttle from cilium to nucleus; decreases GLI3 protein levels;, features a modification of the amino acid from R to Q at position 448.
+The protein's natural variant, known as in HH14; mild phenotype; decreases capacity to shuttle from cilium to nucleus; decreases interaction with EMX1; no effect on GLI3 protein levels;, features a modification of the amino acid from P to L at position 537.
+The protein's natural variant, known as in HH14; abolishes the interaction with EMX1; decreases capacity to shuttle from cilium to nucleus; decreases interaction with EMX1; decreases GLI3 protein levels;, features a modification of the amino acid from H to Q at position 690.
+The protein's natural variant, known as in HH14; does not affect the subcellular location of the protein; decreases capacity to shuttle from cilium to nucleus; decreases GLI3 protein levels;, features a modification of the amino acid from F to L at position 1150.
+The protein's natural variant, known as in GASC; somatic mutation; produces a protein with markedly reduced transcriptional activity but unaltered DNA-binding activity;, features a modification of the amino acid from M to L at position 8.
+The protein's natural variant, known as in GASC; the mutation abolishes DNA binding and transactivating activities;, features a modification of the amino acid from W to R at position 11.
+The natural variant of this protein is characterized by an amino acid alteration from S to P at position 227.
+The natural variant of this protein is characterized by an amino acid alteration from V to A at position 359.
+The natural variant of this protein is characterized by an amino acid alteration from Q to H at position 663.
+The natural variant of this protein is characterized by an amino acid alteration from S to G at position 25.
+The natural variant of this protein is characterized by an amino acid alteration from W to L at position 35.
+The natural variant of this protein is characterized by an amino acid alteration from LLR to RLK at position 90.
+The protein's natural variant, known as in OFD19; the genetic variation producing this missense variant predominantly affects splicing and the resulting mRNA is predicted to undergo nonsense-mediated mRNA decay, features a modification of the amino acid from P to Q at position 51.
+The protein's natural variant, known as does not affect activity;, features a modification of the amino acid from Q to H at position 142.
+The natural variant of this protein is characterized by an amino acid alteration from L to F at position 148.
+The natural variant of this protein is characterized by an amino acid alteration from A to V at position 314.
+The protein's natural variant, known as in strain: 53/7, features a modification of the amino acid from F to I at position 39.
+The protein's natural variant, known as in strain: 53/7, features a modification of the amino acid from L to F at position 44.
+The protein's natural variant, known as in strain: 53/7, features a modification of the amino acid from S to A at position 342.
+The protein's natural variant, known as in strain: 53/7, features a modification of the amino acid from K to R at position 455.
+The protein's natural variant, known as in strain: 53/7, features a modification of the amino acid from S to N at position 496.
+The protein's natural variant, known as in strain: 53/7, features a modification of the amino acid from H to L at position 527.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from K to R at position 113.
+The protein's natural variant, known as in strain: Serotype 10, features a modification of the amino acid from A to T at position 167.
+The protein's natural variant, known as in strain: Serotype 10 and Serotype 12, features a modification of the amino acid from PPP to APS at position 223.
+The protein's natural variant, known as in strain: ATCCVR-358 / Fuller / CIP 107027, features a modification of the amino acid from R to S at position 39.
+The protein's natural variant, known as in strain: ATCCVR-358 / Fuller / CIP 107027, features a modification of the amino acid from T to P at position 53.
+The protein's natural variant, known as in strain: ATCCVR-358 / Fuller / CIP 107027, features a modification of the amino acid from T to P at position 195.
+The protein's natural variant, known as in strain: ATCCVR-358 / Fuller /CIP 107027, features a modification of the amino acid from NIFGGN to HLEDLP at position 356.
+The protein's natural variant, known as in strain: LG/J and SM/J, features a modification of the amino acid from R to Q at position 15.
+The protein's natural variant, known as in strain: LG/J and SM/J, features a modification of the amino acid from S to I at position 17.
+The protein's natural variant, known as in strain: LG/J and SM/J, features a modification of the amino acid from G to C at position 19.
+The protein's natural variant, known as in strain: LG/J and SM/J, features a modification of the amino acid from V to M at position 462.
+The protein's natural variant, known as in strain: LG/J and SM/J, features a modification of the amino acid from T to K at position 546.
+The protein's natural variant, known as in strain: LG/J and SM/J, features a modification of the amino acid from I to V at position 583.
+The protein's natural variant, known as in NEMMLAS and PKDYS3; hypomorphic variant, clinically relevant when present in trans with an amorphic variant; impaired mitochondrial localization;, features a modification of the amino acid from W to G at position 13.
+The protein's natural variant, known as in NEMMLAS;, features a modification of the amino acid from G to V at position 45.
+The protein's natural variant, known as in PKDYS3;, features a modification of the amino acid from G to D at position 50.
+The protein's natural variant, known as in NEMMLAS; unknown pathological significance;, features a modification of the amino acid from H to Q at position 77.
+The protein's natural variant, known as in NEMMLAS;, features a modification of the amino acid from V to L at position 178.
+The protein's natural variant, known as in PKDYS3;, features a modification of the amino acid from S to W at position 228.
+The protein's natural variant, known as in NEMMLAS;, features a modification of the amino acid from V to G at position 278.
+The protein's natural variant, known as in NEMMLAS;, features a modification of the amino acid from K to M at position 313.
+The protein's natural variant, known as in NEMMLAS;, features a modification of the amino acid from V to L at position 349.
+The protein's natural variant, known as in NEMMLAS; unknown pathological significance;, features a modification of the amino acid from E to K at position 352.
+The protein's natural variant, known as in plasmid pCP301, features a modification of the amino acid from H to Y at position 14.
+The natural variant of this protein is characterized by an amino acid alteration from F to L at position 139.
+The protein's natural variant, known as in OCLSBG; causes mislocalization of the protein in the cytoplasm; impairs cilium formation;, features a modification of the amino acid from D to V at position 353.
+The natural variant of this protein is characterized by an amino acid alteration from T to A at position 322.
+The natural variant of this protein is characterized by an amino acid alteration from M to L at position 357.
+The protein's natural variant, known as in strain: La28 and La106, features a modification of the amino acid from L to S at position 5.
+The protein's natural variant, known as in strain: La120, features a modification of the amino acid from I to L at position 10.
+The protein's natural variant, known as in strain: La14, La31, La118 and Ma24, features a modification of the amino acid from L to I at position 14.
+The protein's natural variant, known as in strain: AF1, AF4, AF6, AF8, AF9, Au1, Au3, Au7, Au9, La3, La10, La14, La15, La25, La31, La108, Ma6, Ma11, Ma18, Ma20, Ma24, Ma35, Ma37, Ma53, Ma57, Ma74, Mo13a, Mo34a, Mo47a, NC-005, NC-007, NC-010, NFS 5.3, Ny1, Ny6, Ny8, SFS 2.2, TW2, TW3, TW6, TW9 and TW10, features a modification of the amino acid from S to N at position 19.
+The protein's natural variant, known as in strain: NC-005, NC-007 and NC-010, features a modification of the amino acid from Q to K at position 24.
+The protein's natural variant, known as in strain: Au6, La25, La27, La62, La108, Ma43, Mo13a, Mo34a, NFS 5.1, NFS 5.2, NFS 5.3, NFS 6.1, NFS 7.8, Ny1, Ny2, Ny6, Ny8, SFS 1.1, SFS 1.4, SFS 2.2, SFS 3.1, SFS 3.3, SFS 3.4, TW2, TW3, TW4, TW7, TW9 and TW10, features a modification of the amino acid from Q to K at position 25.
+The protein's natural variant, known as in strain: AF2, AF7, Au4, La3, La15, La37, La58, Ma21, Mo29b, Mo36a, Mo52B, Mo79b, NC-009, Ny3, Ny5 and TW11, features a modification of the amino acid from L to Q at position 32.
+The protein's natural variant, known as in strain: Ny2 and SFS 3.4, features a modification of the amino acid from S to G at position 39.
+The protein's natural variant, known as in strain: Au3, features a modification of the amino acid from A to S at position 40.
+The protein's natural variant, known as in strain: Ma18, Ma20, Ma37 and Ma53, features a modification of the amino acid from L to V at position 42.
+The protein's natural variant, known as in strain: Au3 and Ma74, features a modification of the amino acid from N to S at position 44.
+The protein's natural variant, known as in strain: AF1, AF3, AF4, AF5, AF6, AF8, AF9, AF10, Au1, Au2, Au4, Au6, Au7, Au8, Au10, La10, La13, La14, La25, La31, La32, La37, La46, La58, La60, La62, La105, La108, La116, La118, La125, Ma3, Ma6, Ma11, Ma20, Ma23, Ma24, Ma50, Ma56, Ma57, Ma60, Mo13a, Mo29b, Mo34a, Mo40b, Mo52B, Mo80b, NC-001, NC-004, NC-005, NC-006, NC-007, NC-008, NC-010, NFS 5.1, NFS 5.2, NFS 6.1, NFS 6.2, NFS 6.3, NFS 7.8, Ny1, Ny2, Ny4, Ny6, Ny8, SFS 1.1, SFS 1.4, SFS 2.2, SFS 3.1, SFS 3.2, SFS 3.3, SFS 3.4, TW1, TW2, TW3, TW4, TW5, TW6, TW7, TW8 and TW9, features a modification of the amino acid from A to P at position 46.
+The protein's natural variant, known as in strain: AF2, AF7, Au3, Au5, Au9, La3, La15, La27, La36, La54, La120, Ma18, Ma21, Ma31, Ma37, Ma43, Ma53, Ma74, Mo36a, Mo79b, NC-002, NC-003, NC-009, NFS 5.4, NFS 6.4, Ny3, Ny5, Ny7, SFS 2.4, TW10 and TW11, features a modification of the amino acid from A to T at position 46.
+The protein's natural variant, known as in strain: La116, features a modification of the amino acid from A to T at position 54.
+The protein's natural variant, known as in strain: Au3, features a modification of the amino acid from I to L at position 56.
+The protein's natural variant, known as in strain: AF8, Ma3 and SFS 2.3, features a modification of the amino acid from D to G at position 65.
+The protein's natural variant, known as in strain: La116 and NC3, features a modification of the amino acid from D to N at position 76.
+The protein's natural variant, known as in strain: Au2, Au3, Au8, La13, La32, La37, NC-004, NC-006, NC-008, Ny4, TW1, TW5 and TW8, features a modification of the amino acid from D to N at position 79.
+The protein's natural variant, known as in strain: AF1, AF2, AF3, AF5, AF6, AF7, AF8, AF9, AF10, Au3, Au4, Au6, Au7, La3, La10, La14, La15, La27, La28, La31, La36, La37, La46, La54, La58, La60, La62, La106, La116, La118, La120, La125, Ma3, Ma6, Ma11, Ma18, Ma20, Ma21, Ma23, Ma24, Ma31, Ma35, Ma37, Ma43, Ma50, Ma53, Ma56, Ma57, Ma74, Mo40b, Mo52B, NC-001, NC-002, NC-003, NC-009, NFS 5.1, NFS 5.2, NFS 6.1, NFS 6.2, NFS 6.3, NFS 7.8, Ny2, Ny3, Ny5, Ny6, SFS 1.1, SFS 1.2, SFS 1.4, SFS 2.2, SFS 2.3, SFS 2.4, SFS 3.1, SFS 3.2, SFS 3.3, SFS 3.4, TW3, TW4, TW6, TW7, TW10 and TW11, features a modification of the amino acid from N to S at position 101.
+The protein's natural variant, known as in strain: La62, features a modification of the amino acid from P to R at position 104.
+The protein's natural variant, known as in strain: AF1, AF2, AF3, AF5, AF6, AF7, AF8, AF9, AF10, Au2, Au4, Au6, Au7, Au8, La3, La10, La13, La14, La15, La27, La28, La31, La32, La37, La46, La58, La60, La62, La105, La106, La116, La118, La120, La125, Ma3, Ma6, Ma11, Ma18, Ma20, Ma21, Ma23, Ma24, Ma31, Ma35, Ma37, Ma43, Ma50, Ma53, Ma56, Ma57, Ma74, Mo40b, Mo52B, Mo80b, NC-001, NC-002, NC-004, NC-006, NC-008, NC-009, NFS 5.1, NFS 5.2, NFS 6.1, NFS 6.2, NFS 6.3, NFS 6.4, NFS 7.8, Ny2, Ny3, Ny4, Ny5, SFS 1.1, SFS 1.4, SFS 2.2, SFS 2.4, SFS 3.1, SFS 3.2, SFS 3.3, SFS 3.4, TW1, TW3, TW4, TW5, TW6, TW7, TW8, TW10 and TW11, features a modification of the amino acid from L to I at position 109.
+The protein's natural variant, known as in strain: La36, La54 and Ma20, features a modification of the amino acid from L to S at position 167.
+The protein's natural variant, known as in strain: La3, La36, La125 and Ma20, features a modification of the amino acid from L to F at position 169.
+The protein's natural variant, known as in strain: Au1, Au3 and Au9, features a modification of the amino acid from E to Q at position 172.
+The protein's natural variant, known as in strain: Au5, La10, La14, La27, La31, La36, La54, La60, La62, La105, La118, La120, La125, Ma3, Ma6, Ma11, Ma21, Ma24, Ma31, Ma35, Ma43, Ma50, Ma53, Ma56, Ma57, Ma74, Mo36a, Mo37a, Mo47a, Mo79b, NC-002, NFS 5.1, NFS 5.2, NFS 6.3, NFS 7.8, Ny2, SFS 1.1, SFS 1.2, SFS 1.4, SFS 2.3, SFS 3.1 and SFS 3.4, features a modification of the amino acid from S to I at position 207.
+The protein's natural variant, known as in strain: Ny2 and SFS 2.3, features a modification of the amino acid from A to V at position 212.
+The protein's natural variant, known as in strain: La3, La10, La15, La27, La31, La37, La60, La120, La125, Ma6, Ma18, Ma20, Ma21, Ma35, Ma37, Ma43, Mo29b, Mo34a, Mo80b, NC-002, NC-010, NFS 5.1, NFS 5.2, NFS 5.4, NFS 6.1, NFS 6.2, NFS 6.4, NFS 7.8, Ny2, SFS 1.2, SFS 1.4, SFS 2.2, SFS 2.3, SFS 3.1, SFS 3.3 and SFS 3.4, features a modification of the amino acid from R to K at position 221.
+The protein's natural variant, known as in strain: TW9, features a modification of the amino acid from N to Y at position 226.
+The protein's natural variant, known as in strain: AF6, AF8, AF9, Au4, La31, La32, La60, La125, Ma6, Ma21, Ma57, TW1 and TW11, features a modification of the amino acid from E to D at position 253.
+The protein's natural variant, known as in strain: AF5, AF10, Au5, La3, La15, La105, Mo36a, Mo37a, Mo47a, Mo79b and TW10, features a modification of the amino acid from P to S at position 262.
+The protein's natural variant, known as in IDDBCS; unknown pathological significance, features a modification of the amino acid from G to S at position 429.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 154.
+The natural variant of this protein is characterized by an amino acid alteration from R to S at position 258.
+The natural variant of this protein is characterized by an amino acid alteration from F to V at position 262.
+The natural variant of this protein is characterized by an amino acid alteration from H to R at position 286.
+The protein's natural variant, known as in clones G27W, G27X and G27Y, features a modification of the amino acid from R to C at position 343.
+The protein's natural variant, known as in clone G27W, features a modification of the amino acid from G to D at position 381.
+The protein's natural variant, known as in strain: CWL029 and TW-183, features a modification of the amino acid from L to S at position 619.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from K to N at position 17.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from M to K at position 180.
+The protein's natural variant, known as in truncated form p80HT, features a modification of the amino acid from AGN to SAS at position 669.
+The protein's natural variant, known as in CVID10; unknown pathological significance; de novo mutation;, features a modification of the amino acid from D to G at position 865.
+The protein's natural variant, known as in CVID10; unknown pathological significance; de novo mutation;, features a modification of the amino acid from A to V at position 867.
+The natural variant of this protein is characterized by an amino acid alteration from E to A at position 61.
+The protein's natural variant, known as adds an additional glycosylation site and impairs interaction with ALCAM;, features a modification of the amino acid from S to N at position 351.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from L to H at position 662.
+The protein's natural variant, known as in CTRCT23;, features a modification of the amino acid from G to W at position 64.
+The protein's natural variant, known as in CTRCT23; the patient has cataract and bilateral microphthalmia; the mutation is predicted to disrupt the beta-sheet structure of the protein;, features a modification of the amino acid from L to P at position 69.
+The protein's natural variant, known as in CTRCT23; modeling suggests that this substitution would significantly reduce the intrinsic stability of the crystalline monomer;, features a modification of the amino acid from F to S at position 94.
+The protein's natural variant, known as in CTRCT15; reduces cell-to-cell adhesion, reduces cell-to-cell gap junction coupling, no loss of cell membrane localization, no loss of water channel activity;, features a modification of the amino acid from R to C at position 33.
+The protein's natural variant, known as in CTRCT15; likely benign variant;, features a modification of the amino acid from V to I at position 107.
+The protein's natural variant, known as in CTRCT15; non-progressive lamellar cataract; loss of activity;, features a modification of the amino acid from E to G at position 134.
+The protein's natural variant, known as in CTRCT15; progressive polymorphic and lamellar cataract; loss of activity;, features a modification of the amino acid from T to R at position 138.
+The protein's natural variant, known as in CTRCT15; loss of plasma membrane expression;, features a modification of the amino acid from D to H at position 150.
+The protein's natural variant, known as in CTRCT15; unknown pathological significance; loss of plasma membrane expression, features a modification of the amino acid from G to D at position 165.
+The protein's natural variant, known as in CTRCT15; unknown pathological significance, features a modification of the amino acid from Y to C at position 177.
+The protein's natural variant, known as in CTRCT15;, features a modification of the amino acid from R to C at position 187.
+The protein's natural variant, known as in CTRCT15;, features a modification of the amino acid from R to K at position 233.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from D to N at position 103.
+The protein's natural variant, known as in COQ10D8;, features a modification of the amino acid from V to E at position 141.
+The protein's natural variant, known as in strain: SM101; temperature-sensitive, features a modification of the amino acid from G to S at position 189.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation; no effect Wnt signlaing upon RSPO1-binding, features a modification of the amino acid from G to C at position 725.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation; no effect Wnt signlaing upon RSPO1-binding, features a modification of the amino acid from P to H at position 928.
+The natural variant of this protein is characterized by an amino acid alteration from A to V at position 24.
+The protein's natural variant, known as in RCPS;, features a modification of the amino acid from D to G at position 270.
+The natural variant of this protein is characterized by an amino acid alteration from L to P at position 38.
+The natural variant of this protein is characterized by an amino acid alteration from F to S at position 48.
+The natural variant of this protein is characterized by an amino acid alteration from RR to A at position 72.
+The natural variant of this protein is characterized by an amino acid alteration from S to N at position 118.
+The protein's natural variant, known as in ARCI14; unknown pathological significance;, features a modification of the amino acid from P to L at position 149.
+The protein's natural variant, known as in ARCI14; unknown pathological significance;, features a modification of the amino acid from R to Q at position 274.
+The protein's natural variant, known as in CMD1NN; shows a mild increase in kinase activity;, features a modification of the amino acid from A to T at position 237.
+The protein's natural variant, known as in NS5;, features a modification of the amino acid from R to S at position 256.
+The protein's natural variant, known as in NS5 and LPRD2; shows in vitro greater kinase activity and enhanced ERK activation than wild-type;, features a modification of the amino acid from S to L at position 257.
+The protein's natural variant, known as in an ovarian serous carcinoma sample; somatic mutation; increased ERK activation;, features a modification of the amino acid from S to A at position 259.
+The protein's natural variant, known as in NS5;, features a modification of the amino acid from S to F at position 259.
+The protein's natural variant, known as in hypertrophic cardiomyopathy; unknown pathological significance;, features a modification of the amino acid from T to I at position 260.
+The protein's natural variant, known as in NS5, features a modification of the amino acid from T to R at position 260.
+The protein's natural variant, known as in NS5; shows in vitro greater kinase activity and enhanced MAPK1 activation than wild-type;, features a modification of the amino acid from P to A at position 261.
+The protein's natural variant, known as in NS5; shows greater kinase activity and enhanced MAPK1 activation than wild-type;, features a modification of the amino acid from P to L at position 261.
+The protein's natural variant, known as in NS5; shows in vitro greater kinase activity and enhanced MAPK1 activation than wild-type;, features a modification of the amino acid from P to S at position 261.
+The protein's natural variant, known as in NS5; shows in vitro greater kinase activity and enhanced MAPK1 activation than wild-type;, features a modification of the amino acid from V to A at position 263.
+The protein's natural variant, known as in CMD1NN; shows a mild increase in kinase activity;, features a modification of the amino acid from T to A at position 310.
+The protein's natural variant, known as in CMD1NN; shows a mild increase in kinase activity;, features a modification of the amino acid from P to A at position 332.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation, features a modification of the amino acid from Q to H at position 335.
+The protein's natural variant, known as in NS5;, features a modification of the amino acid from D to G at position 486.
+The protein's natural variant, known as in NS5; has reduced or absent kinase activity;, features a modification of the amino acid from D to N at position 486.
+The protein's natural variant, known as in NS5; has reduced or absent kinase activity;, features a modification of the amino acid from T to I at position 491.
+The protein's natural variant, known as in NS5;, features a modification of the amino acid from T to R at position 491.
+The protein's natural variant, known as in CMD1NN; shows impaired kinase activity and reduced MAPK3 activation with this mutation;, features a modification of the amino acid from L to P at position 603.
+The protein's natural variant, known as in NS5;, features a modification of the amino acid from S to T at position 612.
+The protein's natural variant, known as in NS5 and LPRD2; shows in vitro greater kinase activity and enhanced MAPK1 activation than wild-type;, features a modification of the amino acid from L to V at position 613.
+The protein's natural variant, known as in CMD1NN; shows a mild increase in kinase activity;, features a modification of the amino acid from H to R at position 626.
+The protein's natural variant, known as in CMD1NN; shows a mild increase in kinase activity;, features a modification of the amino acid from T to M at position 641.
+The protein's natural variant, known as in GSD1B;, features a modification of the amino acid from G to D at position 20.
+The protein's natural variant, known as in GSD1B;, features a modification of the amino acid from Y to H at position 24.
+The protein's natural variant, known as in GSD1B;, features a modification of the amino acid from N to K at position 27.
+The protein's natural variant, known as in GSD1B;, features a modification of the amino acid from R to C at position 28.
+The protein's natural variant, known as in GSD1B; inactive glucose-6-phosphate transport;, features a modification of the amino acid from R to H at position 28.
+The protein's natural variant, known as in GSD1B;, features a modification of the amino acid from G to E at position 50.
+The protein's natural variant, known as in GSD1B;, features a modification of the amino acid from G to R at position 50.
+The protein's natural variant, known as in GSD1B;, features a modification of the amino acid from S to R at position 54.
+The protein's natural variant, known as in GSD1B;, features a modification of the amino acid from S to R at position 55.
+The protein's natural variant, known as in GSD1B;, features a modification of the amino acid from G to R at position 68.
+The protein's natural variant, known as in GSD1B;, features a modification of the amino acid from L to P at position 85.
+The protein's natural variant, known as in GSD1B;, features a modification of the amino acid from G to D at position 88.
+The protein's natural variant, known as in GSD1B;, features a modification of the amino acid from W to R at position 118.
+The protein's natural variant, known as in GSD1C;, features a modification of the amino acid from Q to P at position 133.
+The protein's natural variant, known as in GSD1B;, features a modification of the amino acid from A to V at position 148.
+The protein's natural variant, known as in GSD1B; inactive glucose-6-phosphate transport;, features a modification of the amino acid from G to E at position 149.
+The protein's natural variant, known as in GSD1B;, features a modification of the amino acid from G to R at position 150.
+The protein's natural variant, known as in GSD1B;, features a modification of the amino acid from P to L at position 153.
+The protein's natural variant, known as in GSD1B;, features a modification of the amino acid from C to R at position 176.
+The protein's natural variant, known as in GSD1B; inactive glucose-6-phosphate transport;, features a modification of the amino acid from C to R at position 183.
+The protein's natural variant, known as in GSD1B;, features a modification of the amino acid from P to L at position 191.
+The protein's natural variant, known as in GSD1B;, features a modification of the amino acid from L to P at position 229.
+The protein's natural variant, known as in GSD1B;, features a modification of the amino acid from W to R at position 246.
+The protein's natural variant, known as in GSD1B;, features a modification of the amino acid from I to N at position 278.
+The protein's natural variant, known as in GSD1B;, features a modification of the amino acid from R to C at position 300.
+The protein's natural variant, known as in GSD1B;, features a modification of the amino acid from R to H at position 300.
+The protein's natural variant, known as in GSD1B;, features a modification of the amino acid from H to P at position 301.
+The protein's natural variant, known as in GSD1B;, features a modification of the amino acid from G to C at position 339.
+The protein's natural variant, known as in GSD1B;, features a modification of the amino acid from G to D at position 339.
+The protein's natural variant, known as in GSD1B;, features a modification of the amino acid from A to T at position 367.
+The protein's natural variant, known as in GSD1B;, features a modification of the amino acid from A to D at position 373.
+The protein's natural variant, known as in GSD1C;, features a modification of the amino acid from G to S at position 376.
+The protein's natural variant, known as in BCNS; unknown pathological significance; does not inhibit cell growth when overexpressed in vitro;, features a modification of the amino acid from R to Q at position 719.
+The protein's natural variant, known as in DYT2; no effect on protein localization; no effect on protein abundance; no effect on protein stability; no effect on protein 3D structure; decreased oligomerization; changed calcium-binding; effect on cooperativity for calcium-binding; no effect on affinity for calcium; no effect on interaction with voltage-dependent calcium channels;, features a modification of the amino acid from T to N at position 71.
+The protein's natural variant, known as in DYT2;, features a modification of the amino acid from N to K at position 75.
+The protein's natural variant, known as in DYT2; no effect on protein localization; no effect on protein abundance; no effect on protein stability; no effect on protein 3D structure; decreased oligomerization; no effect on calcium-binding; no effect on affinity for calcium; increased interaction with voltage-dependent calcium channels;, features a modification of the amino acid from A to T at position 190.
+The protein's natural variant, known as in strain: cv. Rutgers and NP24 II, features a modification of the amino acid from I to F at position 24.
+The protein's natural variant, known as in NP24 II, features a modification of the amino acid from S to F at position 38.
+The protein's natural variant, known as in strain: EM20031, MRE-600; AA sequence, features a modification of the amino acid from EL to DV at position 301.
+The protein's natural variant, known as in strain: MRE-600; AA sequence, features a modification of the amino acid from R to C at position 587.
+The protein's natural variant, known as in strain: PS102, features a modification of the amino acid from F to L at position 594.
+The protein's natural variant, known as in strain: MRE-600; AA sequence, features a modification of the amino acid from E to Q at position 637.
+The protein's natural variant, known as in strain: EM20031; AA sequence, features a modification of the amino acid from G to V at position 724.
+The protein's natural variant, known as in strain: EM20031, MRE-600; AA sequence, features a modification of the amino acid from A to P at position 738.
+The protein's natural variant, known as in strain: EM20031; AA sequence, features a modification of the amino acid from ADSV to RTVW at position 743.
+The protein's natural variant, known as in strain: MRE-600; AA sequence, features a modification of the amino acid from F to L at position 787.
+The protein's natural variant, known as in strain: MRE-600; AA sequence, features a modification of the amino acid from K to N at position 830.
+The protein's natural variant, known as in JBTS30; unknown pathological significance;, features a modification of the amino acid from G to R at position 69.
+The natural variant of this protein is characterized by an amino acid alteration from D to N at position 330.
+The protein's natural variant, known as in JBTS30; unknown pathological significance;, features a modification of the amino acid from R to C at position 343.
+The protein's natural variant, known as in JBTS30; unknown pathological significance;, features a modification of the amino acid from R to C at position 446.
+The protein's natural variant, known as in JBTS30; unknown pathological significance;, features a modification of the amino acid from G to R at position 492.
+The protein's natural variant, known as in JBTS30; unknown pathological significance;, features a modification of the amino acid from P to L at position 520.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from P to A at position 31.
+The protein's natural variant, known as in strain: cv. C24, cv. Lz-0, cv. Wei-0, cv. Yo-0, features a modification of the amino acid from E to Q at position 115.
+The protein's natural variant, known as in strain: cv. Ak-1, cv. Bay-0, cv. Di-0, cv. Landsberg erecta, cv. Tsu-0, cv. Wei-0, features a modification of the amino acid from A to V at position 293.
+The protein's natural variant, known as in MIRAGE; decreased cell proliferation; changed endosome organization, features a modification of the amino acid from R to Q at position 459.
+The protein's natural variant, known as in M7MLS2, features a modification of the amino acid from K to E at position 676.
+The protein's natural variant, known as in MIRAGE; decreased cell proliferation; changed endosome organization, features a modification of the amino acid from D to N at position 769.
+The protein's natural variant, known as in MIRAGE; decreased cell proliferation; changed endosome organization, features a modification of the amino acid from N to Y at position 834.
+The protein's natural variant, known as in MIRAGE; decreased cell proliferation; changed endosome organization;, features a modification of the amino acid from E to K at position 974.
+The protein's natural variant, known as in MIRAGE; decreased cell proliferation; changed endosome organization, features a modification of the amino acid from A to V at position 1195.
+The protein's natural variant, known as in MIRAGE; decreased cell proliferation; changed endosome organization, features a modification of the amino acid from P to L at position 1280.
+The protein's natural variant, known as in MIRAGE; decreased cell proliferation; changed endosome organization, features a modification of the amino acid from Q to K at position 1286.
+The protein's natural variant, known as in MIRAGE; decreased cell proliferation; changed endosome organization, features a modification of the amino acid from R to W at position 1293.
+The protein's natural variant, known as in NFTC; loss of cytoplasmic expression;, features a modification of the amino acid from K to E at position 1495.
+The protein's natural variant, known as in clone BOVPTT-25, features a modification of the amino acid from I to F at position 72.
+The protein's natural variant, known as in EPPK;, features a modification of the amino acid from M to K at position 157.
+The protein's natural variant, known as in EPPK;, features a modification of the amino acid from M to R at position 157.
+The protein's natural variant, known as in EPPK;, features a modification of the amino acid from M to T at position 157.
+The protein's natural variant, known as in EPPK;, features a modification of the amino acid from M to V at position 157.
+The protein's natural variant, known as in EPPK; with knuckle pads;, features a modification of the amino acid from L to F at position 160.
+The protein's natural variant, known as in EPPK;, features a modification of the amino acid from L to V at position 160.
+The protein's natural variant, known as in EPPK;, features a modification of the amino acid from N to H at position 161.
+The protein's natural variant, known as in EPPK;, features a modification of the amino acid from N to I at position 161.
+The protein's natural variant, known as in EPPK;, features a modification of the amino acid from N to K at position 161.
+The protein's natural variant, known as in EPPK;, features a modification of the amino acid from N to S at position 161.
+The protein's natural variant, known as in EPPK;, features a modification of the amino acid from N to Y at position 161.
+The protein's natural variant, known as in EPPK;, features a modification of the amino acid from R to P at position 163.
+The protein's natural variant, known as in EPPK;, features a modification of the amino acid from R to Q at position 163.
+The protein's natural variant, known as in EPPK;, features a modification of the amino acid from R to W at position 163.
+The protein's natural variant, known as in EPPK, features a modification of the amino acid from Y to WL at position 167.
+The protein's natural variant, known as in EPPK;, features a modification of the amino acid from L to S at position 168.
+The protein's natural variant, known as in EPPK;, features a modification of the amino acid from V to M at position 171.
+The protein's natural variant, known as in EPPK;, features a modification of the amino acid from Q to P at position 172.
+The protein's natural variant, known as in EPPK;, features a modification of the amino acid from C to R at position 406.
+The protein's natural variant, known as in EPPK;, features a modification of the amino acid from Y to H at position 454.
+The protein's natural variant, known as in EPPK;, features a modification of the amino acid from L to F at position 458.
+The protein's natural variant, known as in EPPK, features a modification of the amino acid from L to P at position 458.
+The protein's natural variant, known as in mutant JII8; confers telithromycin resistance; when associated with a large deletion in the upstream region of ErmB, features a modification of the amino acid from K to Q at position 94.
+The protein's natural variant, known as in strain: 3ERY and 5ROX; confers antibiotic resistance, features a modification of the amino acid from G to D at position 95.
+The protein's natural variant, known as in strain: 4ERY; confers antibiotic resistance, features a modification of the amino acid from P to Q at position 99.
+The protein's natural variant, known as in a serotype 3 clinical isolate, confers resistance to macrolide and fluoroquinolone antibiotics, features a modification of the amino acid from T to TRTAHIT at position 108.
+The protein's natural variant, known as in allele A3H-Var; haplotype 2; allele presenting a higher expression and which is more effective in retrotransposons and HIV-1 restriction; increases protein stability;, features a modification of the amino acid from G to R at position 105.
+The protein's natural variant, known as in allele A3H-Var; haplotype 2; allele presenting a higher expression and more effective in retrotransposons and HIV-1 restriction;, features a modification of the amino acid from K to E at position 121.
+The protein's natural variant, known as in allele A3H-Var; haplotype 2; allele presenting a higher expression and more effective in retrotransposons and HIV-1 restriction;, features a modification of the amino acid from E to D at position 178.
+The protein's natural variant, known as in LGMDR26; causes aberrant modulation of the mechano-gated potassium channel KCNK2, when tested in a heterologous system;, features a modification of the amino acid from L to H at position 155.
+The protein's natural variant, known as in LGMDR26; causes aberrant modulation of the mechano-gated potassium channel KCNK2, when tested in a heterologous system;, features a modification of the amino acid from L to F at position 217.
+The protein's natural variant, known as in LGMDR26; decreased protein expression in muscle; causes a slightly abnormal modulation of the mechano-gated potassium channel KCNK2, when tested in a heterologous system;, features a modification of the amino acid from R to Q at position 261.
+The protein's natural variant, known as in a gastric adenocarcinoma sample; somatic mutation, features a modification of the amino acid from G to C at position 29.
+The protein's natural variant, known as in a gastric adenocarcinoma sample; somatic mutation, features a modification of the amino acid from T to M at position 46.
+The protein's natural variant, known as in a gastric adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from R to Q at position 93.
+The protein's natural variant, known as in a gastric adenocarcinoma sample; somatic mutation, features a modification of the amino acid from S to F at position 291.
+The protein's natural variant, known as in MRXSN;, features a modification of the amino acid from R to Q at position 11.
+The protein's natural variant, known as in MRXSN;, features a modification of the amino acid from G to R at position 23.
+The natural variant of this protein is characterized by an amino acid alteration from R to T at position 936.
+The protein's natural variant, known as does not form high molecular weight multimers;, features a modification of the amino acid from G to R at position 84.
+The protein's natural variant, known as does not form high molecular weight multimers;, features a modification of the amino acid from G to S at position 90.
+The protein's natural variant, known as in ADPND; does not assemble into trimers resulting in impaired secretion from the cell;, features a modification of the amino acid from R to C at position 112.
+The protein's natural variant, known as associated with low plasma adiponectin concentration and risk for diabetes mellitus type 2; does not assemble into trimers resulting in impaired secretion from the cell;, features a modification of the amino acid from I to T at position 164.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from K to T at position 111.
+The protein's natural variant, known as found in a patient with intellectual disability, frontal epilepsy and mild facial dysmorphism, features a modification of the amino acid from R to Q at position 1012.
+The protein's natural variant, known as in strain: Nissle 1917, features a modification of the amino acid from R to K at position 140.
+The protein's natural variant, known as in strain: Nissle 1917, features a modification of the amino acid from D to N at position 352.
+The protein's natural variant, known as in strain: Nissle 1917, features a modification of the amino acid from S to T at position 579.
+The protein's natural variant, known as in strain: Nissle 1917, features a modification of the amino acid from Y to H at position 612.
+The protein's natural variant, known as in strain: Nissle 1917, features a modification of the amino acid from V to A at position 669.
+The protein's natural variant, known as in strain: Nissle 1917, features a modification of the amino acid from D to N at position 729.
+The protein's natural variant, known as in strain: Nissle 1917, features a modification of the amino acid from N to D at position 894.
+The protein's natural variant, known as in strain: Nissle 1917, features a modification of the amino acid from I to M at position 1041.
+The protein's natural variant, known as in allele MCM2-1, features a modification of the amino acid from E to K at position 392.
+The protein's natural variant, known as in strain: GS-5, MT4239, MT4245, MT4251, MT4467 and MT8148, features a modification of the amino acid from Y to H at position 10.
+The protein's natural variant, known as in strain: GS-5, MT4239, MT4245, MT4251, MT4467 and MT8148, features a modification of the amino acid from I to V at position 19.
+The protein's natural variant, known as in strain: MT4467, features a modification of the amino acid from K to E at position 58.
+The protein's natural variant, known as in strain: MT4239 and MT4245, features a modification of the amino acid from A to S at position 68.
+The protein's natural variant, known as in strain: MT4251 and MT8148, features a modification of the amino acid from A to T at position 81.
+The protein's natural variant, known as in strain: MT4239 and MT4245, features a modification of the amino acid from T to I at position 113.
+The protein's natural variant, known as in strain: MT4239, MT4245 and MT8148, features a modification of the amino acid from A to V at position 122.
+The protein's natural variant, known as in strain: GS-5 and MT4467, features a modification of the amino acid from A to S at position 132.
+The protein's natural variant, known as in strain: MT4245, features a modification of the amino acid from A to V at position 135.
+The protein's natural variant, known as in strain: GS-5, MT4239, MT4245, MT4251, MT4467 and MT8148, features a modification of the amino acid from A to T at position 137.
+The protein's natural variant, known as in strain: MT4239, features a modification of the amino acid from V to L at position 202.
+The protein's natural variant, known as in strain: MT8148, features a modification of the amino acid from D to N at position 255.
+The protein's natural variant, known as in strain: MT4239, MT4245 and MT4251, features a modification of the amino acid from E to D at position 275.
+The protein's natural variant, known as in strain: MT4239, MT4245 and MT4251, features a modification of the amino acid from D to N at position 288.
+The protein's natural variant, known as in strain: MT4245, features a modification of the amino acid from Q to H at position 301.
+The protein's natural variant, known as in strain: MT4239 and MT4251, features a modification of the amino acid from D to N at position 313.
+The protein's natural variant, known as in strain: MT4239, features a modification of the amino acid from E to K at position 317.
+The protein's natural variant, known as in strain: MT4239, features a modification of the amino acid from V to F at position 328.
+The protein's natural variant, known as in strain: MT4239, MT4251 and MT4467, features a modification of the amino acid from F to L at position 350.
+The protein's natural variant, known as in strain: MT4251, features a modification of the amino acid from KKKYTQ to EKEYTL at position 633.
+The protein's natural variant, known as in strain: MT4239, features a modification of the amino acid from A to S at position 688.
+The protein's natural variant, known as in strain: MT4251, features a modification of the amino acid from TDQGSEA to ADKGNDS at position 732.
+The protein's natural variant, known as in strain: MT4239 and MT4245, features a modification of the amino acid from TDQGS to ADKGN at position 730.
+The protein's natural variant, known as in strain: GS-5, MT4239, MT4245, MT4251, MT4467 and MT8148, features a modification of the amino acid from T to A at position 762.
+The protein's natural variant, known as in strain: MT4251, features a modification of the amino acid from D to Y at position 964.
+The protein's natural variant, known as in strain: MT4245 and MT4251, features a modification of the amino acid from E to K at position 1019.
+The protein's natural variant, known as in strain: MT4251, features a modification of the amino acid from LG to IR at position 1060.
+The protein's natural variant, known as in strain: MT4245, features a modification of the amino acid from G to R at position 1060.
+The protein's natural variant, known as in strain: MT4239, features a modification of the amino acid from G to R at position 1080.
+The protein's natural variant, known as in strain: GS-5, features a modification of the amino acid from H to Q at position 1142.
+The protein's natural variant, known as in strain: MT4239, features a modification of the amino acid from S to N at position 1198.
+The protein's natural variant, known as in strain: MT4251 and MT4467, features a modification of the amino acid from Y to C at position 1220.
+The protein's natural variant, known as in strain: MT4467, features a modification of the amino acid from F to L at position 1280.
+The protein's natural variant, known as in strain: MT4245, features a modification of the amino acid from Q to P at position 1282.
+The protein's natural variant, known as in strain: MT4245, features a modification of the amino acid from K to T at position 1290.
+The protein's natural variant, known as in strain: MT4245, features a modification of the amino acid from N to D at position 1311.
+The protein's natural variant, known as in strain: GS-5 and MT4467, features a modification of the amino acid from G to D at position 1403.
+The protein's natural variant, known as in strain: GS-5, features a modification of the amino acid from G to R at position 1425.
+The protein's natural variant, known as in strain: MT4467, features a modification of the amino acid from R to K at position 1449.
+The natural variant of this protein is characterized by an amino acid alteration from PA to RS at position 7.
+The natural variant of this protein is characterized by an amino acid alteration from A to P at position 20.
+The natural variant of this protein is characterized by an amino acid alteration from W to R at position 68.
+The natural variant of this protein is characterized by an amino acid alteration from N to H at position 81.
+The natural variant of this protein is characterized by an amino acid alteration from L to S at position 96.
+The protein's natural variant, known as requires 2 nucleotide substitutions;, features a modification of the amino acid from N to E at position 100.
+The protein's natural variant, known as requires 2 nucleotide substitutions;, features a modification of the amino acid from V to T at position 132.
+The natural variant of this protein is characterized by an amino acid alteration from F to L at position 134.
+The protein's natural variant, known as requires 2 nucleotide substitutions, features a modification of the amino acid from Q to D at position 163.
+The natural variant of this protein is characterized by an amino acid alteration from T to S at position 181.
+The natural variant of this protein is characterized by an amino acid alteration from E to Q at position 190.
+The natural variant of this protein is characterized by an amino acid alteration from VG to AR at position 202.
+The natural variant of this protein is characterized by an amino acid alteration from K to N at position 214.
+The natural variant of this protein is characterized by an amino acid alteration from E to G at position 220.
+The natural variant of this protein is characterized by an amino acid alteration from Q to R at position 236.
+The natural variant of this protein is characterized by an amino acid alteration from PL to SF at position 240.
+The natural variant of this protein is characterized by an amino acid alteration from Q to L at position 261.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 271.
+The natural variant of this protein is characterized by an amino acid alteration from R to T at position 276.
+The natural variant of this protein is characterized by an amino acid alteration from P to S at position 339.
+The natural variant of this protein is characterized by an amino acid alteration from S to P at position 367.
+The natural variant of this protein is characterized by an amino acid alteration from A to E at position 389.
+The natural variant of this protein is characterized by an amino acid alteration from Q to R at position 443.
+The protein's natural variant, known as requires 2 nucleotide substitutions, features a modification of the amino acid from A to L at position 486.
+The protein's natural variant, known as in DFNB63; unknown pathological significance;, features a modification of the amino acid from L to P at position 16.
+The protein's natural variant, known as in DFNB63; unknown pathological significance;, features a modification of the amino acid from R to W at position 52.
+The protein's natural variant, known as in DFNB63;, features a modification of the amino acid from R to Q at position 81.
+The protein's natural variant, known as in DFNB63;, features a modification of the amino acid from W to R at position 105.
+The protein's natural variant, known as in DFNB63;, features a modification of the amino acid from E to K at position 110.
+The protein's natural variant, known as in DFNB63; unknown pathological significance;, features a modification of the amino acid from R to H at position 158.
+The protein's natural variant, known as in strain: Isolate NSMT-32992, features a modification of the amino acid from V to I at position 13.
+The protein's natural variant, known as in strain: E1a, features a modification of the amino acid from I to V at position 85.
+The protein's natural variant, known as in strain: E1a, features a modification of the amino acid from D to N at position 101.
+The protein's natural variant, known as in strain: E1a, features a modification of the amino acid from T to K at position 108.
+The protein's natural variant, known as in strain: E1a, features a modification of the amino acid from LA to FG at position 122.
+The protein's natural variant, known as in strain: E1a, features a modification of the amino acid from T to S at position 151.
+The protein's natural variant, known as in strain: E1a, features a modification of the amino acid from G to A at position 304.
+The protein's natural variant, known as in strain: E1a, features a modification of the amino acid from N to D at position 560.
+The protein's natural variant, known as in strain: E1a, features a modification of the amino acid from L to F at position 633.
+The protein's natural variant, known as in strain: E1a, features a modification of the amino acid from R to H at position 658.
+The protein's natural variant, known as in strain: E1a, features a modification of the amino acid from K to E at position 689.
+The protein's natural variant, known as in strain: E1a, features a modification of the amino acid from A to T at position 755.
+The protein's natural variant, known as in strain: E1a, features a modification of the amino acid from S to G at position 782.
+The protein's natural variant, known as in HEMARS; no protein detected in patient cells that also carry R-577, suggesting the mutant is unstable;, features a modification of the amino acid from P to L at position 567.
+The protein's natural variant, known as in HEMARS; no protein detected in patient cells that also carry L-567, suggesting the mutant is unstable;, features a modification of the amino acid from G to R at position 577.
+The protein's natural variant, known as in strain: C57BL/6J, 129/Sv, BALB/c, FVB/N and more; reduces protein expression, features a modification of the amino acid from R to G at position 78.
+The protein's natural variant, known as in strain: C57BL/6J, 129/Sv, BALB/c, FVB/N and more; reduces protein expression, features a modification of the amino acid from R to C at position 242.
+The protein's natural variant, known as generates a N-glycosylation site;, features a modification of the amino acid from D to N at position 356.
+The protein's natural variant, known as in one allele, features a modification of the amino acid from E to K at position 6.
+The protein's natural variant, known as in one allele, features a modification of the amino acid from S to A at position 9.
+The protein's natural variant, known as in one allele, features a modification of the amino acid from G to D at position 69.
+The protein's natural variant, known as in strain: DBY947, features a modification of the amino acid from P to S at position 67.
+The protein's natural variant, known as in strain: DBY947, features a modification of the amino acid from P to S at position 438.
+The natural variant of this protein is characterized by an amino acid alteration from K to Q at position 29.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from K to E at position 320.
+The protein's natural variant, known as in Nv1-7, features a modification of the amino acid from A to T at position 2.
+The protein's natural variant, known as in Nv1-7 and Nv1-12, features a modification of the amino acid from F to L at position 35.
+The protein's natural variant, known as in allele 1A(0);, features a modification of the amino acid from T to N at position 9.
+The protein's natural variant, known as in allele 1A;, features a modification of the amino acid from A to P at position 91.
+The protein's natural variant, known as in ILD2; unknown pathological significance; impaired secretion, features a modification of the amino acid from N to I at position 171.
+The protein's natural variant, known as in ILD2; impaired secretion, features a modification of the amino acid from V to M at position 178.
+The protein's natural variant, known as in ILD2; unknown pathological significance; impaired secretion, features a modification of the amino acid from Y to C at position 181.
+The protein's natural variant, known as in ILD2; the mutant protein is retained in the endoplasmic reticulum and is not secreted;, features a modification of the amino acid from F to S at position 198.
+The protein's natural variant, known as in allele 1A(1), allele 1A(3) and allele 1A(4);, features a modification of the amino acid from Q to K at position 223.
+The protein's natural variant, known as in ILD2; the mutant protein is retained in the endoplasmic reticulum and is not secreted;, features a modification of the amino acid from G to V at position 231.
+The protein's natural variant, known as in ILD2; impaired secretion, features a modification of the amino acid from W to C at position 233.
+The protein's natural variant, known as in ILD2; impaired secretion, features a modification of the amino acid from W to L at position 233.
+The protein's natural variant, known as in ILD2; impaired secretion, features a modification of the amino acid from W to R at position 233.
+The protein's natural variant, known as in ILD2; impaired secretion, features a modification of the amino acid from C to S at position 238.
+The protein's natural variant, known as in ILD2; unknown pathological significance; impaired secretion, features a modification of the amino acid from R to Q at position 242.
+The protein's natural variant, known as in MCSKS; complete loss of ssRNA-binding activity with the variant protein; shows a higher stability than wild-type in tetracycline-inducible cells;, features a modification of the amino acid from E to K at position 49.
+The protein's natural variant, known as in MCSKS; complete loss of ssRNA-binding activity with the variant protein; shows a higher stability than wild-type in tetracycline-inducible cells;, features a modification of the amino acid from R to C at position 51.
+The protein's natural variant, known as in MCSKS; Decreased stability; does not affect subcellular localization;, features a modification of the amino acid from R to G at position 51.
+The protein's natural variant, known as in MCSKS; complete loss of ssRNA-binding activity with the variant protein; shows a higher stability than wild-type in tetracycline-inducible cells;, features a modification of the amino acid from R to H at position 51.
+The protein's natural variant, known as in MCSKS; complete loss of ssRNA-binding activity with the variant protein;, features a modification of the amino acid from R to Q at position 247.
+The natural variant of this protein is characterized by an amino acid alteration from C to T at position 65.
+The protein's natural variant, known as in VDEGS;, features a modification of the amino acid from C to Y at position 258.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from R to C at position 499.
+The protein's natural variant, known as found in a patient with microcephaly, developmental delay, behavioral abnormalities, dysmorphic facial features, hypotonia and other various phenotypic abnormalities; unknown pathological significance, features a modification of the amino acid from H to P at position 271.
+The protein's natural variant, known as in GDFD; has no residual normal activity, impaired ability to demethylate N(6)-methyladenosine RNAs (m6A) RNAs;, features a modification of the amino acid from R to Q at position 316.
+The protein's natural variant, known as in GDFD; reduced enzyme activity;, features a modification of the amino acid from S to F at position 319.
+The protein's natural variant, known as in GDFD;, features a modification of the amino acid from R to Q at position 322.
+The protein's natural variant, known as in strain: Indian tick typhus, features a modification of the amino acid from N to NN at position 60.
+The protein's natural variant, known as in strain: Indian tick typhus, features a modification of the amino acid from R to H at position 76.
+The protein's natural variant, known as in strain: Indian tick typhus, features a modification of the amino acid from VT to II at position 954.
+The protein's natural variant, known as in strain: Indian tick typhus, M1 and Moroccan, features a modification of the amino acid from D to A at position 1245.
+The protein's natural variant, known as in strain: Moroccan, features a modification of the amino acid from N to H at position 1308.
+The protein's natural variant, known as in strain: Indian tick typhus, features a modification of the amino acid from M to I at position 1877.
+The protein's natural variant, known as in RP36; loss of palmitoylation; reduced protein stability; fails to localize to the photoreceptor outer segment;, features a modification of the amino acid from C to Y at position 2.
+The protein's natural variant, known as in RP36; no effect on protein level, features a modification of the amino acid from P to T at position 25.
+The protein's natural variant, known as in RP36; unknown pathological significance; no effect on protein stability;, features a modification of the amino acid from V to M at position 30.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 73.
+The protein's natural variant, known as in 1st isoinhibitor, features a modification of the amino acid from H to D at position 2.
+The protein's natural variant, known as in 3rd isoinhibitor, features a modification of the amino acid from D to K at position 3.
+The protein's natural variant, known as in allele NKG2-A*03, features a modification of the amino acid from I to L at position 79.
+The protein's natural variant, known as in allele NKG2-A*03, features a modification of the amino acid from H to R at position 231.
+The protein's natural variant, known as in plasmid pLMO229, features a modification of the amino acid from L to V at position 75.
+The protein's natural variant, known as in CMAVM2; unknown pathological significance;, features a modification of the amino acid from E to K at position 59.
+The protein's natural variant, known as in CMAVM2; unknown pathological significance;, features a modification of the amino acid from R to P at position 74.
+The protein's natural variant, known as in CMAVM2; unknown pathological significance;, features a modification of the amino acid from C to R at position 107.
+The protein's natural variant, known as in CMAVM2; unknown pathological significance, features a modification of the amino acid from VK to L at position 162.
+The protein's natural variant, known as in CMAVM2; unknown pathological significance;, features a modification of the amino acid from L to P at position 187.
+The protein's natural variant, known as in CMAVM2; unknown pathological significance;, features a modification of the amino acid from C to R at position 268.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation;, features a modification of the amino acid from P to L at position 346.
+The protein's natural variant, known as in CMAVM2; unknown pathological significance;, features a modification of the amino acid from V to G at position 469.
+The protein's natural variant, known as does not affect tyrosine phosphorylation; does not affect interaction with RASA1;, features a modification of the amino acid from A to G at position 509.
+The protein's natural variant, known as in CMAVM2; unknown pathological significance;, features a modification of the amino acid from G to R at position 516.
+The protein's natural variant, known as in CMAVM2; highly decreased tyrosine phosphorylation; highly decreased interaction with RASA1;, features a modification of the amino acid from K to N at position 650.
+The protein's natural variant, known as in CMAVM2; unknown pathological significance;, features a modification of the amino acid from R to W at position 656.
+The protein's natural variant, known as in CMAVM2; the mutant protein is not detected by Western blot; loss of localization to cell membrane;, features a modification of the amino acid from E to K at position 664.
+The protein's natural variant, known as in CMAVM2; unknown pathological significance;, features a modification of the amino acid from A to T at position 725.
+The protein's natural variant, known as in LMPHM7; loss of kinase activity;, features a modification of the amino acid from R to Q at position 739.
+The protein's natural variant, known as in CMAVM2;, features a modification of the amino acid from N to D at position 745.
+The protein's natural variant, known as in LMPHM7; loss of kinase activity;, features a modification of the amino acid from I to S at position 782.
+The protein's natural variant, known as in CMAVM2; unknown pathological significance;, features a modification of the amino acid from P to R at position 789.
+The protein's natural variant, known as in CMAVM2; unknown pathological significance;, features a modification of the amino acid from P to S at position 789.
+The protein's natural variant, known as in CMAVM2;, features a modification of the amino acid from D to G at position 802.
+The protein's natural variant, known as in CMAVM2; unknown pathological significance;, features a modification of the amino acid from G to R at position 807.
+The protein's natural variant, known as in CMAVM2; unknown pathological significance;, features a modification of the amino acid from P to L at position 820.
+The protein's natural variant, known as in CMAVM2; unknown pathological significance;, features a modification of the amino acid from P to T at position 820.
+The protein's natural variant, known as in CMAVM2; the mutant protein is not detected by Western blot; loss of localization to cell membrane;, features a modification of the amino acid from R to W at position 838.
+The protein's natural variant, known as in CMAVM2; the mutant protein is not detected by Western blot; loss of localization to cell membrane;, features a modification of the amino acid from C to R at position 845.
+The protein's natural variant, known as in CMAVM2;, features a modification of the amino acid from C to Y at position 856.
+The protein's natural variant, known as in CMAVM2; the mutant protein is not detected by Western blot; loss of localization to cell membrane;, features a modification of the amino acid from R to W at position 864.
+The protein's natural variant, known as in CMAVM2; loss of tyrosine phosphorylation; loss of interaction with RASA1;, features a modification of the amino acid from F to L at position 867.
+The protein's natural variant, known as in CMAVM2; unknown pathological significance;, features a modification of the amino acid from V to E at position 870.
+The protein's natural variant, known as in CMAVM2; unknown pathological significance;, features a modification of the amino acid from L to P at position 874.
+The protein's natural variant, known as in a gastric adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from R to W at position 889.
+The protein's natural variant, known as in NPHP14; found at homozygosity in two siblings with nephronophthisis, cerebellar vermis hypoplasia and situs inversus;, features a modification of the amino acid from P to L at position 913.
+The protein's natural variant, known as in JBTS19;, features a modification of the amino acid from H to Y at position 1277.
+The protein's natural variant, known as in JBTS23; unknown pathological significance;, features a modification of the amino acid from R to K at position 403.
+The protein's natural variant, known as in JBTS23, features a modification of the amino acid from D to V at position 566.
+The protein's natural variant, known as in CTRCT31;, features a modification of the amino acid from D to V at position 129.
+The protein's natural variant, known as in CTRCT31;, features a modification of the amino acid from E to K at position 161.
+The protein's natural variant, known as in strain: BALB/c, AKR/J and SJL/J, features a modification of the amino acid from C to R at position 59.
+The protein's natural variant, known as in strain: BALB/c, AKR/J and SJL/J; reduced IL4-neutralizing capacity of soluble form, features a modification of the amino acid from T to I at position 74.
+The protein's natural variant, known as in strain: BALB/c, AKR/J and SJL/J, features a modification of the amino acid from M to T at position 193.
+The protein's natural variant, known as in strain: BALB/c, AKR/J and SJL/J, features a modification of the amino acid from L to P at position 334.
+The protein's natural variant, known as in strain: BALB/c, AKR/J and SJL/J, features a modification of the amino acid from N to S at position 374.
+The protein's natural variant, known as in strain: BALB/c, AKR/J and SJL/J, features a modification of the amino acid from I to M at position 382.
+The protein's natural variant, known as in strain: BALB/c, AKR/J and SJL/J, features a modification of the amino acid from G to D at position 472.
+The protein's natural variant, known as in strain: BALB/c, AKR/J and SJL/J, features a modification of the amino acid from D to G at position 626.
+The natural variant of this protein is characterized by an amino acid alteration from C to Y at position 124.
+The protein's natural variant, known as found in a renal cell carcinoma sample; somatic mutation, features a modification of the amino acid from A to V at position 97.
+The protein's natural variant, known as in MCPH10; hypomorphic mutation; may cause altered transcript but some full-length protein is still formed;, features a modification of the amino acid from R to H at position 1111.
+The protein's natural variant, known as found in patients with non-obstructive azoospermia; unknown pathological significance, features a modification of the amino acid from T to I at position 25.
+The protein's natural variant, known as in a glioblastoma multiforme sample; somatic mutation;, features a modification of the amino acid from G to R at position 342.
+The protein's natural variant, known as in strain: cv. Bor-1, cv. Pu2-23, cv. Pu2-7, cv. Wa-1, cv. Wassilewskija, features a modification of the amino acid from A to T at position 34.
+The protein's natural variant, known as in strain: cv. Bay-0, cv. Bil-5, cv. Bil-7, cv. Bor-1, cv. Bor-4, cv. Br-0, cv. Bur-0, cv. Ed-1, cv. Edi-0, cv. Fab-2, cv. Fab-4, cv. Ga-0, cv. Ge-0, cv. Goettingen-7, cv. HR-10, cv. Lov-1, cv. Lov-5, cv. Lz-0, cv. Mr-0, cv. Mrk-0, cv. Mz-0, cv. Nd-1, cv. Nok-3, cv. Omo2-1, cv. Omo2-3, cv. Oy-0, cv. Pu2-23, cv. Pu2-7, cv. Ra-0, cv. Spr1-2, cv. Sq-8, cv. Ts-1, cv. Uod-1, cv. Var2-1, cv. Var2-6, cv. Wa-1, cv. Wassilewskija, cv. Wt-5, cv. Zdr-1, cv. Zdr-6, features a modification of the amino acid from T to I at position 45.
+The protein's natural variant, known as in strain: cv. Bay-0, cv. Bil-5, cv. Bil-7, cv. Bor-1, cv. Br-0, cv. Bur-0, cv. Ed-1, cv. Edi-0, cv. Fab-2, cv. Fab-4, cv. Ga-0, cv. Ge-0, cv. Goettingen-7, cv. HR-10, cv. Lov-1, cv. Lov-5, cv. Lz-0, cv. Mr-0, cv. Mrk-0, cv. Mz-0, cv. Nd-1, cv. Nok-3, cv. Omo2-1, cv. Omo2-3, cv. Oy-0, cv. Pu2-23, cv. Pu2-7, cv. Ra-0, cv. Spr1-2, cv. Sq-8, cv. Ts-1, cv. Uod-1, cv. Var2-1, cv. Var2-6, cv. Wa-1, cv. Wassilewskija, cv. Wt-5, cv. Zdr-1, cv. Zdr-6, features a modification of the amino acid from D to N at position 63.
+The protein's natural variant, known as in strain: cv. Bay-0, cv. Bil-5, cv. Bil-7, cv. Bor-1, cv. Br-0, cv. Bur-0, cv. Ed-1, cv. Edi-0, cv. Fab-2, cv. Fab-4, cv. Ga-0, cv. Ge-0, cv. Goettingen-7, cv. HR-10, cv. Lov-1, cv. Lov-5, cv. Lz-0, cv. Mr-0, cv. Mrk-0, cv. Mz-0, cv. Nd-1, cv. Nok-3, cv. Omo2-1, cv. Omo2-3, cv. Oy-0, cv. Pu2-23, cv. Pu2-7, cv. Ra-0, cv. Spr1-2, cv. Sq-8, cv. Ts-1, cv. Uod-1, cv. Var2-1, cv. Var2-6, cv. Wa-1, cv. Wassilewskija, cv. Wt-5, cv. Zdr-1, cv. Zdr-6, features a modification of the amino acid from A to T at position 74.
+The protein's natural variant, known as in strain: cv. Ag-0, cv. An-1, cv. Bay-0, cv. Bil-5, cv. Bil-7, cv. Bor-1, cv. Br-0, cv. Bur-0, cv. C24, cv. CIBC-17, cv. Ct-1, cv. Ed-1, cv. Edi-0, cv. Fab-2, cv. Fab-4, cv. Fei-0, cv. Ga-0, cv. Ge-0, cv. Goettingen-22, cv. Goettingen-7, cv. Gy-0, cv. HR-10, cv. Ll-0, cv. Lov-1, cv. Lov-5, cv. Lz-0, cv. Mr-0, cv. Mrk-0, cv. Mt-0, cv. Mz-0, cv. NFA-10, cv. NFA-8, cv. Nd-1, cv. Nok-3, cv. Omo2-1, cv. Omo2-3, cv. Oy-0, cv. Pu2-23, cv. Pu2-7, cv. REN-11, cv. Ra-0, cv. Se-0, cv. Spr1-2, cv. Sq-1, cv. Sq-8, cv. Ts-1, cv. Ts-5, cv. Ull2-3, cv. Uod-1, cv. Uod-7, cv. Var2-1, cv. Var2-6, cv. Wa-1, cv. Wassilewskija, cv. Wei-0, cv. Wt-5, cv. Zdr-1, features a modification of the amino acid from S to N at position 102.
+The protein's natural variant, known as in strain: cv. Est-1, cv. Wassilewskija-2, features a modification of the amino acid from G to R at position 150.
+The protein's natural variant, known as in strain: cv. CIBC-5, cv. Ed-2, cv. HR-5, cv. Spr1-6, cv. Ull2-5, features a modification of the amino acid from A to G at position 173.
+The protein's natural variant, known as in strain: cv. Ler-1, cv. Lp2-2, cv. Lp2-6, cv. Tamm-2, cv. Tamm-27, features a modification of the amino acid from V to I at position 240.
+The protein's natural variant, known as in strain: cv. HR-10, features a modification of the amino acid from ITKS to VTKR at position 259.
+The protein's natural variant, known as in strain: cv. Edi-0, cv. Ga-0, cv. Mrk-0, cv. Mz-0, cv. Nd-1, cv. Omo2-3, cv. Oy-0, cv. Sq-8, cv. Ts-1, cv. Zdr-1, features a modification of the amino acid from IT to VS at position 257.
+The protein's natural variant, known as in strain: cv. Ag-0, cv. An-1, cv. Bay-0, cv. Bil-5, cv. Bil-7, cv. Bor-1, cv. Br-0, cv. Bur-0, cv. C24, cv. CIBC-17, cv. Ct-1, cv. Cvi-0, cv. Ed-1, cv. Fab-2, cv. Fab-4, cv. Fei-0, cv. Ge-0, cv. Goettingen-22, cv. Goettingen-7, cv. Gy-0, cv. Ll-0, cv. Lov-1, cv. Lov-5, cv. Lz-0, cv. Mr-0, cv. Mt-0, cv. NFA-10, cv. NFA-8, cv. Nok-3, cv. Omo2-1, cv. Pu2-23, cv. Pu2-7, cv. REN-11, cv. Ra-0, cv. Se-0, cv. Spr1-2, cv. Sq-1, cv. Ts-5, cv. Ull2-3, cv. Uod-1, cv. Uod-7, cv. Var2-1, cv. Var2-6, cv. Wa-1, cv. Wassilewskija, cv. Wei-0, cv. Wt-5, features a modification of the amino acid from I to V at position 256.
+The protein's natural variant, known as in strain: cv. Ag-0, cv. An-1, cv. Bay-0, cv. Bil-5, cv. Bil-7, cv. Bor-1, cv. Br-0, cv. Bur-0, cv. C24, cv. CIBC-17, cv. Ct-1, cv. Ed-1, cv. Edi-0, cv. Fab-2, cv. Fab-4, cv. Fei-0, cv. Ga-0, cv. Ge-0, cv. Goettingen-22, cv. Goettingen-7, cv. Gy-0, cv. HR-10, cv. Ll-0, cv. Lov-1, cv. Lov-5, cv. Lz-0, cv. Mr-0, cv. Mrk-0, cv. Mt-0, cv. Mz-0, cv. NFA-10, cv. NFA-8, cv. Nd-1, cv. Nok-3, cv. Omo2-1, cv. Omo2-3, cv. Oy-0, cv. Pu2-23, cv. Pu2-7, cv. REN-11, cv. Ra-0, cv. Se-0, cv. Spr1-2, cv. Sq-1, cv. Sq-8, cv. Ts-1, cv. Ts-5, cv. Ull2-3, cv. Uod-1, cv. Uod-7, cv. Var2-1, cv. Var2-6, cv. Wa-1, cv. Wassilewskija, cv. Wei-0, cv. Wt-5, cv. Zdr-1, features a modification of the amino acid from S to T at position 270.
+The protein's natural variant, known as in strain: cv. Goettingen-7, features a modification of the amino acid from V to I at position 304.
+The protein's natural variant, known as in strain: cv. CIBC-5, cv. Ed-2, cv. HR-5, cv. Spr1-6, cv. Ull2-5, features a modification of the amino acid from S to T at position 346.
+The protein's natural variant, known as in strain: cv. Lz-0, features a modification of the amino acid from L to C at position 361.
+The protein's natural variant, known as in strain: cv. Ag-0, cv. An-1, cv. Bay-0, cv. Bil-5, cv. Bil-7, cv. Bor-1, cv. Br-0, cv. Bur-0, cv. C24, cv. CIBC-17, cv. Ct-1, cv. Ed-1, cv. Edi-0, cv. Fab-4, cv. Fei-0, cv. Ga-0, cv. Ge-0, cv. Goettingen-22, cv. Goettingen-7, cv. Gy-0, cv. HR-10, cv. Ll-0, cv. Lov-1, cv. Lov-5, cv. Lz-0, cv. Mr-0, cv. Mrk-0, cv. Mz-0, cv. NFA-10, cv. NFA-8, cv. Nd-1, cv. Nok-3, cv. Omo2-1, cv. Omo2-3, cv. Oy-0, cv. Pu2-23, cv. Pu2-7, cv. REN-11, cv. Ra-0, cv. Se-0, cv. Sq-1, cv. Sq-8, cv. Ts-1, cv. Ts-5, cv. Ull2-3, cv. Uod-1, cv. Uod-7, cv. Wa-1, cv. Wassilewskija, cv. Wei-0, cv. Wt-5, cv. Zdr-1, features a modification of the amino acid from T to M at position 366.
+The protein's natural variant, known as in strain: cv. C24, cv. Mt-0, features a modification of the amino acid from T to R at position 366.
+The protein's natural variant, known as in strain: cv. Ag-0, cv. An-1, cv. Bay-0, cv. Bil-5, cv. Bil-7, cv. Bor-1, cv. Br-0, cv. Bur-0, cv. C24, cv. CIBC-17, cv. Ct-1, cv. Ed-1, cv. Edi-0, cv. Fab-4, cv. Fei-0, cv. Ga-0, cv. Ge-0, cv. Goettingen-22, cv. Goettingen-7, cv. Gy-0, cv. HR-10, cv. Ll-0, cv. Lov-1, cv. Lov-5, cv. Lz-0, cv. Mr-0, cv. Mrk-0, cv. Mt-0, cv. Mz-0, cv. NFA-10, cv. NFA-8, cv. Nd-1, cv. Nok-3, cv. Omo2-1, cv. Omo2-3, cv. Oy-0, cv. Pu2-23, cv. Pu2-7, cv. REN-11, cv. Ra-0, cv. Se-0, cv. Sq-1, cv. Sq-8, cv. Ts-1, cv. Ts-5, cv. Ull2-3, cv. Uod-1, cv. Uod-7, cv. Wa-1, cv. Wassilewskija, cv. Wei-0, cv. Wt-5, cv. Zdr-1, features a modification of the amino acid from V to L at position 375.
+The protein's natural variant, known as in strain: cv. Ag-0, cv. An-1, cv. Bay-0, cv. Bil-5, cv. Bil-7, cv. Bor-1, cv. Br-0, cv. Bur-0, cv. C24, cv. CIBC-17, cv. Ct-1, cv. Ed-1, cv. Edi-0, cv. Fab-4, cv. Fei-0, cv. Ga-0, cv. Ge-0, cv. Goettingen-22, cv. Goettingen-7, cv. Gy-0, cv. HR-10, cv. Ll-0, cv. Lov-1, cv. Lov-5, cv. Lz-0, cv. Mr-0, cv. Mrk-0, cv. Mt-0, cv. Mz-0, cv. NFA-10, cv. NFA-8, cv. Nd-1, cv. Nok-3, cv. Omo2-1, cv. Omo2-3, cv. Oy-0, cv. Pu2-23, cv. Pu2-7, cv. REN-11, cv. Ra-0, cv. Se-0, cv. Sq-1, cv. Sq-8, cv. Ts-1, cv. Ts-5, cv. Ull2-3, cv. Uod-1, cv. Uod-7, cv. Wa-1, cv. Wassilewskija, cv. Wei-0, cv. Wt-5, cv. Zdr-1, features a modification of the amino acid from R to K at position 384.
+The protein's natural variant, known as in strain: cv. Fab-2, features a modification of the amino acid from C to S at position 386.
+The protein's natural variant, known as in strain: cv. Ag-0, cv. An-1, cv. Bay-0, cv. Bil-5, cv. Bil-7, cv. Bor-1, cv. Br-0, cv. Bur-0, cv. C24, cv. CIBC-17, cv. Ct-1, cv. Ed-1, cv. Edi-0, cv. Fab-4, cv. Fei-0, cv. Ga-0, cv. Ge-0, cv. Goettingen-22, cv. Goettingen-7, cv. Gy-0, cv. HR-10, cv. Ll-0, cv. Lov-1, cv. Lov-5, cv. Lz-0, cv. Mr-0, cv. Mrk-0, cv. Mt-0, cv. Mz-0, cv. NFA-10, cv. NFA-8, cv. Nd-1, cv. Nok-3, cv. Omo2-1, cv. Omo2-3, cv. Oy-0, cv. Pu2-23, cv. Pu2-7, cv. REN-11, cv. Ra-0, cv. Se-0, cv. Sq-1, cv. Sq-8, cv. Ts-1, cv. Ts-5, cv. Ull2-3, cv. Uod-1, cv. Uod-7, cv. Wa-1, cv. Wassilewskija, cv. Wei-0, cv. Wt-5, cv. Zdr-1, features a modification of the amino acid from T to I at position 405.
+The protein's natural variant, known as in strain: Lindegren 25a, features a modification of the amino acid from D to N at position 45.
+The protein's natural variant, known as in strain: Lindegren 25a, features a modification of the amino acid from I to V at position 115.
+The protein's natural variant, known as in strain: Lindegren 25a, features a modification of the amino acid from E to D at position 597.
+The natural variant of this protein is characterized by an amino acid alteration from A to T at position 339.
+The protein's natural variant, known as in a glioblastoma multiforme sample; somatic mutation, features a modification of the amino acid from P to L at position 45.
+The protein's natural variant, known as in strain: F38011, features a modification of the amino acid from I to V at position 132.
+The protein's natural variant, known as in strain: F38011 and M129, features a modification of the amino acid from T to A at position 254.
+The protein's natural variant, known as in strain: M129, features a modification of the amino acid from F to L at position 258.
+The protein's natural variant, known as in strain: M129, features a modification of the amino acid from M to I at position 291.
+The protein's natural variant, known as in strain: M129, features a modification of the amino acid from S to N at position 469.
+The protein's natural variant, known as in strain: F38011 and M129, features a modification of the amino acid from Q to K at position 500.
+The protein's natural variant, known as in strain: M129, features a modification of the amino acid from L to F at position 605.
+The protein's natural variant, known as found in a patient with severe dilated cardiomyopathy; unknown pathological significance;, features a modification of the amino acid from A to V at position 262.
+The protein's natural variant, known as in TTD6; reduction in the levels of both TFIIE-alpha and TFIIE-beta subunits of the TFIIE complex in patient cells; reduced phosphorylation of TFIIE-alpha observed in patient cells;, features a modification of the amino acid from A to P at position 150.
+The protein's natural variant, known as in TTD6; reduction in the levels of both TFIIE-alpha and TFIIE-beta subunits of the TFIIE complex in patient cells; reduced phosphorylation of TFIIE-alpha observed in patient cells;, features a modification of the amino acid from D to Y at position 187.
+The protein's natural variant, known as in CMT4B1;, features a modification of the amino acid from R to W at position 283.
+The protein's natural variant, known as in HSCR3; unknown pathological significance;, features a modification of the amino acid from P to S at position 21.
+The protein's natural variant, known as may be a risk factor for Hirschsprung disease;, features a modification of the amino acid from R to W at position 93.
+The protein's natural variant, known as risk factor for Hirschsprung disease;, features a modification of the amino acid from D to N at position 150.
+The protein's natural variant, known as in HSCR3; sporadic form;, features a modification of the amino acid from T to S at position 154.
+The protein's natural variant, known as in HSCR3;, features a modification of the amino acid from I to M at position 211.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from T to M at position 210.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from V to I at position 512.
+The natural variant of this protein is characterized by an amino acid alteration from Y to H at position 110.
+The protein's natural variant, known as in RHZDAN, features a modification of the amino acid from E to K at position 76.
+The natural variant of this protein is characterized by an amino acid alteration from T to P at position 599.
+The natural variant of this protein is characterized by an amino acid alteration from I to M at position 601.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 627.
+The protein's natural variant, known as in COXPD23; unknown pathological significance;, features a modification of the amino acid from R to L at position 3.
+The protein's natural variant, known as in COXPD23, features a modification of the amino acid from E to K at position 142.
+The protein's natural variant, known as in COXPD23;, features a modification of the amino acid from E to V at position 159.
+The protein's natural variant, known as in COXPD23, features a modification of the amino acid from A to P at position 162.
+The protein's natural variant, known as in COXPD23;, features a modification of the amino acid from A to G at position 222.
+The protein's natural variant, known as in COXPD23, features a modification of the amino acid from P to H at position 257.
+The protein's natural variant, known as in COXPD23;, features a modification of the amino acid from D to H at position 337.
+The protein's natural variant, known as in COXPD23;, features a modification of the amino acid from E to K at position 459.
+The protein's natural variant, known as in NEDEMA; unknown pathological significance, features a modification of the amino acid from F to L at position 114.
+The protein's natural variant, known as in NEDEMA; unknown pathological significance, features a modification of the amino acid from S to R at position 349.
+The protein's natural variant, known as in NEDEMA, features a modification of the amino acid from S to G at position 351.
+The protein's natural variant, known as in NEDEMA, features a modification of the amino acid from S to R at position 351.
+The protein's natural variant, known as in NEDEMA, features a modification of the amino acid from C to R at position 352.
+The protein's natural variant, known as in NEDEMA; unknown pathological significance, features a modification of the amino acid from S to P at position 354.
+The protein's natural variant, known as in NEDEMA; unknown pathological significance, features a modification of the amino acid from Y to C at position 546.
+The protein's natural variant, known as in PPKNEFD; collapsed of the keratin filament network in a dose-dependent manner;, features a modification of the amino acid from E to K at position 472.
+The protein's natural variant, known as in strain: Oregon-R, wi4, wi15, wi6, wi24, wi30, wi32 and wi33, features a modification of the amino acid from Q to L at position 219.
+The protein's natural variant, known as in GADEVS; unknown pathological significance, features a modification of the amino acid from H to Y at position 320.
+The protein's natural variant, known as in GADEVS; unknown pathological significance;, features a modification of the amino acid from K to Q at position 339.
+The protein's natural variant, known as in GADEVS; reduced DNA-binding; reduced transcription regulator activity;, features a modification of the amino acid from L to P at position 366.
+The protein's natural variant, known as in GADEVS; unknown pathological significance;, features a modification of the amino acid from L to V at position 366.
+The protein's natural variant, known as found in patients with late onset insulinomas; alters DNA-binding motif; increases transactivation activity; produces a constitutive activation of cAMP and Ca2+ signaling pathways involved in insulin secretion;, features a modification of the amino acid from T to R at position 372.
+The protein's natural variant, known as in GADEVS; reduced DNA-binding; reduced transcription regulator activity;, features a modification of the amino acid from D to Y at position 380.
+The protein's natural variant, known as in strain: ZIM56, features a modification of the amino acid from T to A at position 7.
+The protein's natural variant, known as in strain: M47, features a modification of the amino acid from A to D at position 14.
+The protein's natural variant, known as in strain: M47, features a modification of the amino acid from T to L at position 21.
+The protein's natural variant, known as in strain: ZIM26 and ZIM42, features a modification of the amino acid from E to K at position 22.
+The protein's natural variant, known as in strain: ZIM56, features a modification of the amino acid from I to V at position 27.
+The protein's natural variant, known as in strain: M09 and WS9, features a modification of the amino acid from N to K at position 70.
+The protein's natural variant, known as in strain: SFS 3.1, features a modification of the amino acid from Y to C at position 72.
+The protein's natural variant, known as in strain: ZIM30, features a modification of the amino acid from V to D at position 83.
+The protein's natural variant, known as in strain: ZIM2, features a modification of the amino acid from Y to C at position 108.
+The protein's natural variant, known as in CORD15, features a modification of the amino acid from P to A at position 574.
+The protein's natural variant, known as found in a patient with Joubert syndrome; unknown pathological significance, features a modification of the amino acid from T to S at position 716.
+The protein's natural variant, known as in TBHS2; results in loss of cell adhesion as shown by a cell-substrate adhesion assay, features a modification of the amino acid from W to S at position 55.
+The protein's natural variant, known as in TBHS2; results in loss of cell adhesion as shown by a cell-substrate adhesion assay, features a modification of the amino acid from E to K at position 140.
+The protein's natural variant, known as in TBHS2, features a modification of the amino acid from D to E at position 260.
+The protein's natural variant, known as in TBHS2; results in decreased cell adhesion as shown by a cell-substrate adhesion assay, features a modification of the amino acid from D to N at position 260.
+The protein's natural variant, known as in TBHS2; results in decreased cell adhesion as shown by a cell-substrate adhesion assay, features a modification of the amino acid from N to I at position 262.
+The protein's natural variant, known as in TBHS2;, features a modification of the amino acid from P to L at position 266.
+The protein's natural variant, known as in TBHS2; results in increased cell migration as shown by an in vitro wound closure assay using patient cells, features a modification of the amino acid from E to Q at position 279.
+The protein's natural variant, known as in TBHS2; results in loss of cell adhesion as shown by a cell-substrate adhesion assay, features a modification of the amino acid from G to W at position 327.
+The protein's natural variant, known as in TBHS2, features a modification of the amino acid from V to E at position 374.
+The protein's natural variant, known as in strain: E/UW-5/Cx, features a modification of the amino acid from M to T at position 3.
+The protein's natural variant, known as in strain: E/UW-5/Cx, features a modification of the amino acid from A to V at position 14.
+The protein's natural variant, known as in strain: E/UW-5/Cx, features a modification of the amino acid from K to E at position 104.
+The protein's natural variant, known as in strain: E/UW-5/Cx, features a modification of the amino acid from I to V at position 263.
+The protein's natural variant, known as in strain: E/UW-5/Cx, features a modification of the amino acid from C to R at position 286.
+The protein's natural variant, known as in strain: E/UW-5/Cx, features a modification of the amino acid from P to L at position 354.
+The protein's natural variant, known as in allele NAT2*9; slow/unstable isoform, features a modification of the amino acid from N to I at position 99.
+The protein's natural variant, known as in isoform C1, features a modification of the amino acid from G to E at position 26.
+The protein's natural variant, known as in isoform C1, features a modification of the amino acid from P to S at position 34.
+The protein's natural variant, known as in PHARC; unknown pathological significance;, features a modification of the amino acid from R to P at position 186.
+The protein's natural variant, known as in PHARC; unknown pathological significance; abolished monoacyglycerol lipase activity, features a modification of the amino acid from T to I at position 202.
+The protein's natural variant, known as in PHARC; abolished monoacyglycerol lipase activity;, features a modification of the amino acid from T to R at position 253.
+The protein's natural variant, known as in PHARC; unknown pathological significance;, features a modification of the amino acid from H to Q at position 372.
+The protein's natural variant, known as in CURRAS, features a modification of the amino acid from R to W at position 243.
+The protein's natural variant, known as in CURRAS, features a modification of the amino acid from R to G at position 245.
+The protein's natural variant, known as in CURRAS, features a modification of the amino acid from R to H at position 245.
+The protein's natural variant, known as in CURRAS;, features a modification of the amino acid from T to S at position 246.
+The protein's natural variant, known as in CURRAS, features a modification of the amino acid from W to G at position 288.
+The protein's natural variant, known as in CURRAS, features a modification of the amino acid from W to L at position 288.
+The protein's natural variant, known as in CURRAS, features a modification of the amino acid from F to S at position 289.
+The protein's natural variant, known as in CURRAS, features a modification of the amino acid from Q to P at position 290.
+The protein's natural variant, known as in CURRAS, features a modification of the amino acid from R to W at position 292.
+The protein's natural variant, known as in CURRAS, features a modification of the amino acid from R to Q at position 293.
+The protein's natural variant, known as in CURRAS, features a modification of the amino acid from R to W at position 293.
+The protein's natural variant, known as in allele MPR2, features a modification of the amino acid from G to E at position 85.
+The protein's natural variant, known as in strain: cv. E41, features a modification of the amino acid from S to C at position 261.
+The protein's natural variant, known as in MC1DN15; results in altered complex I assembly;, features a modification of the amino acid from A to P at position 3.
+The protein's natural variant, known as in MC1DN15;, features a modification of the amino acid from L to P at position 65.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to W at position 350.
+The protein's natural variant, known as in SCAR26; may result in aberrant splicing;, features a modification of the amino acid from K to N at position 431.
+The natural variant of this protein is characterized by an amino acid alteration from A to G at position 18.
+The natural variant of this protein is characterized by an amino acid alteration from T to N at position 114.
+The natural variant of this protein is characterized by an amino acid alteration from L to I at position 124.
+The protein's natural variant, known as in POROK9;, features a modification of the amino acid from R to Q at position 179.
+The protein's natural variant, known as in a breast cancer sample, features a modification of the amino acid from L to P at position 827.
+The protein's natural variant, known as in a breast cancer sample;, features a modification of the amino acid from E to G at position 1013.
+The natural variant of this protein is characterized by an amino acid alteration from N to I at position 1511.
+The protein's natural variant, known as in a pancreatic cancer sample, features a modification of the amino acid from S to Y at position 1650.
+The protein's natural variant, known as in MKHK2;, features a modification of the amino acid from Q to P at position 1824.
+The protein's natural variant, known as found in a patient with spinocerebellar ataxia; unknown pathological significance;, features a modification of the amino acid from Q to R at position 2007.
+The protein's natural variant, known as in a colorectal cancer sample;, features a modification of the amino acid from P to Q at position 2221.
+The natural variant of this protein is characterized by an amino acid alteration from N to K at position 59.
+The natural variant of this protein is characterized by an amino acid alteration from S to P at position 41.
+The natural variant of this protein is characterized by an amino acid alteration from A to T at position 42.
+The natural variant of this protein is characterized by an amino acid alteration from N to K at position 49.
+The natural variant of this protein is characterized by an amino acid alteration from F to I at position 163.
+The protein's natural variant, known as in Adamts13S, features a modification of the amino acid from WKVLSLGPCSASCGLG to ALVWEAAPTFAVTRWR at position 1037.
+The protein's natural variant, known as in DEE75; unknown pathological significance;, features a modification of the amino acid from I to T at position 80.
+The protein's natural variant, known as in DEE75; unknown pathological significance;, features a modification of the amino acid from V to I at position 95.
+The protein's natural variant, known as in DEE75; unknown pathological significance;, features a modification of the amino acid from R to G at position 202.
+The protein's natural variant, known as in DEE75; unknown pathological significance;, features a modification of the amino acid from E to K at position 203.
+The protein's natural variant, known as in DEE75; unknown pathological significance;, features a modification of the amino acid from S to L at position 279.
+The protein's natural variant, known as in DEE75; unknown pathological significance;, features a modification of the amino acid from P to R at position 364.
+The protein's natural variant, known as in PBD8B, features a modification of the amino acid from P to T at position 289.
+The protein's natural variant, known as in PBD8B;, features a modification of the amino acid from Y to C at position 331.
+The protein's natural variant, known as in MSSD; completely abolishes the transcription activation with the dimerization partners TCF3, TCF4 and TCF12;, features a modification of the amino acid from N to D at position 71.
+The protein's natural variant, known as in MSSD; completely abolishes the transcription activation with the dimerization partners TCF3, TCF4 and TCF12;, features a modification of the amino acid from R to P at position 73.
+The protein's natural variant, known as in CCSPD; unknown pathological significance; requires 2 nucleotide substitutions;, features a modification of the amino acid from E to L at position 74.
+The protein's natural variant, known as in MSSD; completely abolishes the transcription activation with the dimerization partners TCF3, TCF4 and TCF12;, features a modification of the amino acid from R to L at position 75.
+The protein's natural variant, known as in GDSBA; unknown pathological significance, features a modification of the amino acid from V to G at position 1357.
+The protein's natural variant, known as recurrent gain-of-function variant found in metastatic melanoma; promotes NRAS signaling; somatic mutation;, features a modification of the amino acid from D to N at position 89.
+The protein's natural variant, known as in HADDTS;, features a modification of the amino acid from R to W at position 342.
+The protein's natural variant, known as in COXPD36; results in impaired assembly of the small mitoribosomal subunit and impaired mitochondrial translation in patient cells;, features a modification of the amino acid from R to C at position 110.
+The protein's natural variant, known as in COXPD36; results in impaired assembly of the small mitoribosomal subunit and impaired mitochondrial translation in patient cells;, features a modification of the amino acid from D to N at position 114.
+The protein's natural variant, known as in COXPD36; results in impaired assembly of the small mitoribosomal subunit and impaired mitochondrial translation in patient cells;, features a modification of the amino acid from R to H at position 138.
+The protein's natural variant, known as in T2D;, features a modification of the amino acid from V to I at position 383.
+The protein's natural variant, known as decreased phosphatase activity; no effect on epoxyde hydrolase activity;, features a modification of the amino acid from K to R at position 55.
+The protein's natural variant, known as decreased phosphatase activity; no effect on epoxyde hydrolase activity;, features a modification of the amino acid from R to C at position 103.
+The protein's natural variant, known as decreased phosphatase activity; no effect on epoxyde hydrolase activity;, features a modification of the amino acid from C to Y at position 154.
+The protein's natural variant, known as no effect on phosphatase activity; decreased epoxyde hydrolase activity;, features a modification of the amino acid from R to Q at position 287.
+The natural variant of this protein is characterized by an amino acid alteration from R to RR at position 403.
+The protein's natural variant, known as no effect on phosphatase activity and epoxyde hydrolase activity;, features a modification of the amino acid from E to G at position 470.
+The protein's natural variant, known as in VSD1;, features a modification of the amino acid from A to V at position 6.
+The protein's natural variant, known as in TOF; slightly diminished DNA-binding affinity; decreased transcriptional activity; no effect on subcellular location; no effect on interaction with TBX5;, features a modification of the amino acid from A to P at position 9.
+The protein's natural variant, known as probable disease-associated variant found in patients with dilated cardiomyopathy; results in significantly reduced transactivation activity;, features a modification of the amino acid from V to L at position 39.
+The protein's natural variant, known as in VSD1; significantly reduced activation of the NPPA promoter with the mutant protein compared to wild-type;, features a modification of the amino acid from R to W at position 43.
+The protein's natural variant, known as in TOF; slightly diminished DNA-binding affinity; decreased transcriptional activity; no effect on subcellular location; no effect on interaction with TBX5, features a modification of the amino acid from L to V at position 51.
+The protein's natural variant, known as in ASD2;, features a modification of the amino acid from S to F at position 52.
+The protein's natural variant, known as in ASD2; unknown pathological significance;, features a modification of the amino acid from G to A at position 93.
+The protein's natural variant, known as in TOF, features a modification of the amino acid from A to AA at position 118.
+The protein's natural variant, known as in AVSD4; also in a patient with VSD1 and a patient with TOF;, features a modification of the amino acid from P to S at position 163.
+The protein's natural variant, known as in TACHD; impairs the ability to bind and transactivate the promoter of AMH gene; abolishes interaction with ZFPM2;, features a modification of the amino acid from G to R at position 221.
+The protein's natural variant, known as probable disease-associated variant found in patients with dilated cardiomyopathy; results in significantly reduced transactivation activity, features a modification of the amino acid from P to Q at position 226.
+The protein's natural variant, known as probable disease-associated variant found in patients with dilated cardiomyopathy; results in significantly reduced transactivation activity, features a modification of the amino acid from C to S at position 271.
+The protein's natural variant, known as probable disease-associated variant found in patients with dilated cardiomyopathy; results in significantly reduced transactivation activity, features a modification of the amino acid from T to S at position 279.
+The protein's natural variant, known as in ASD2;, features a modification of the amino acid from T to M at position 280.
+The protein's natural variant, known as in TOF; drastically diminished DNA-binding affinity; decreased transcriptional activity; no effect on subcellular location; completely disrupted interaction with TBX5, features a modification of the amino acid from N to S at position 285.
+The protein's natural variant, known as in ASD2;, features a modification of the amino acid from G to C at position 296.
+The protein's natural variant, known as in VSD1;, features a modification of the amino acid from G to R at position 296.
+The protein's natural variant, known as in ASD2; decreased function resulting in reduced myocardial genes expression; fails to down-regulate endothelial and endocardial genes;, features a modification of the amino acid from G to S at position 296.
+The protein's natural variant, known as in ASD2;, features a modification of the amino acid from M to V at position 310.
+The protein's natural variant, known as in ASD2; unknown pathological significance;, features a modification of the amino acid from Q to E at position 316.
+The protein's natural variant, known as in AVSD4;, features a modification of the amino acid from A to V at position 346.
+The protein's natural variant, known as in VSD1;, features a modification of the amino acid from E to K at position 359.
+The protein's natural variant, known as in ASD2;, features a modification of the amino acid from L to M at position 403.
+The protein's natural variant, known as in VSD1 and TOF; unknown pathological significance;, features a modification of the amino acid from P to Q at position 407.
+The protein's natural variant, known as in VSD1, features a modification of the amino acid from S to T at position 429.
+The protein's natural variant, known as in VSD1;, features a modification of the amino acid from A to V at position 442.
+The protein's natural variant, known as in strain: L2, features a modification of the amino acid from S to A at position 56.
+The protein's natural variant, known as in strain: L2, features a modification of the amino acid from K to E at position 117.
+The protein's natural variant, known as in haplotype T3B, features a modification of the amino acid from P to R at position 147.
+The protein's natural variant, known as in haplotype T3B, features a modification of the amino acid from E to D at position 365.
+The protein's natural variant, known as in haplotype T3B, features a modification of the amino acid from P to H at position 381.
+The protein's natural variant, known as in ECTD11A, features a modification of the amino acid from D to Y at position 114.
+The protein's natural variant, known as in ECTD11A; severely impairs NF-kappa-B activation and acted in a dominant-negative manner;, features a modification of the amino acid from L to R at position 122.
+The protein's natural variant, known as in ECTD11B; may reduce binding to EDAR; impairs NF-kappa-B activation by about 50%;, features a modification of the amino acid from E to K at position 152.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from F to L at position 658.
+The protein's natural variant, known as in THC5; abrogates DNA binding; alters subcellular location; decreases transcriptional repression in a dominant-negative fashion;, features a modification of the amino acid from P to L at position 214.
+The protein's natural variant, known as in one individual with AML; somatic mutation; unable to repress transcription, features a modification of the amino acid from Y to YG at position 344.
+The protein's natural variant, known as in THC5; abrogates DNA binding; alters subcellular location; decreases transcriptional repression in a dominant-negative fashion;, features a modification of the amino acid from R to Q at position 369.
+The protein's natural variant, known as in THC5; abrogates DNA binding; alters subcellular location; decreases transcriptional repression in a dominant-negative fashion;, features a modification of the amino acid from R to C at position 399.
+The protein's natural variant, known as in a second allele, features a modification of the amino acid from G to S at position 15.
+The protein's natural variant, known as in strain: Milan hypersensitive, features a modification of the amino acid from Y to F at position 316.
+The natural variant of this protein is characterized by an amino acid alteration from F to L at position 74.
+The protein's natural variant, known as in strain: Serotype O:9, features a modification of the amino acid from D to N at position 29.
+The protein's natural variant, known as in strain: Serotype O:9, features a modification of the amino acid from L to Q at position 49.
+The protein's natural variant, known as in strain: Serotype O:9, features a modification of the amino acid from A to C at position 65.
+The protein's natural variant, known as in strain: Serotype O:9, features a modification of the amino acid from R to K at position 228.
+The protein's natural variant, known as in strain: Serotype O:9, features a modification of the amino acid from NA to KP at position 236.
+The protein's natural variant, known as in strain: Serotype O:9, features a modification of the amino acid from AGVAYA to PVWLI at position 440.
+The protein's natural variant, known as risk factor for T2D when associated with G-127, S-340 and T-443; reduced pyruvate transmembrane transporter activity, loss of interaction with BSG and decreased localization to plasma membrane when associated with G-127, S-340 and T-443;, features a modification of the amino acid from V to I at position 113.
+The protein's natural variant, known as risk factor for T2D when associated with I-113, S-340 and T-443; reduced pyruvate transmembrane transporter activity, loss of interaction with BSG and decreased localization to plasma membrane when associated with I-113, S-340 and T-443;, features a modification of the amino acid from D to G at position 127.
+The protein's natural variant, known as risk factor for T2D when associated with I-113, G-127 and T-443; reduced pyruvate transmembrane transporter activity, loss of interaction with BSG and decreased localization to plasma membrane when associated with I-113, G-127 and T-443;, features a modification of the amino acid from G to S at position 340.
+The protein's natural variant, known as risk factor for T2D when associated with I-113, G-127 and S-340; reduced pyruvate transmembrane transporter activity, loss of interaction with BSG and decreased localization to plasma membrane when associated with I-113, G-127 and S-340;, features a modification of the amino acid from P to T at position 443.
+The protein's natural variant, known as in pcd; pcd(5J) mutant, features a modification of the amino acid from D to DD at position 832.
+The protein's natural variant, known as in OKT4-negative populations;, features a modification of the amino acid from R to W at position 265.
+The protein's natural variant, known as in SCA44; enhances G-protein coupled glutamate receptor signaling pathway;, features a modification of the amino acid from Y to C at position 262.
+The protein's natural variant, known as in SCAR13, features a modification of the amino acid from L to F at position 454.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to W at position 696.
+The protein's natural variant, known as in SCA44; enhances G-protein coupled glutamate receptor signaling pathway;, features a modification of the amino acid from Y to C at position 792.
+The protein's natural variant, known as in strain: R6 / R800, features a modification of the amino acid from F to L at position 7.
+The protein's natural variant, known as in strain: NCTC 11906, SP-VA92, SP-496 and SP-VA96, features a modification of the amino acid from G to D at position 27.
+The protein's natural variant, known as in strain: R6 / R800 and R6x, features a modification of the amino acid from T to A at position 30.
+The protein's natural variant, known as in strain: NCTC 11906, SP-VA92, SP-496 and SP-VA96, features a modification of the amino acid from E to D at position 166.
+The protein's natural variant, known as in strain: R6 / R800 and R6x, features a modification of the amino acid from V to I at position 246.
+The protein's natural variant, known as in strain: NCTC 11906, SP-VA92, SP-496 and SP-VA96, features a modification of the amino acid from L to I at position 368.
+The protein's natural variant, known as in strain: R6 / R800, R6x, NCTC 11906, SP-VA92, SP-496 and SP-VA96, features a modification of the amino acid from Q to T at position 432.
+The protein's natural variant, known as in strain: NCTC 11906, SP-VA92, SP-496 and SP-VA96, features a modification of the amino acid from T to A at position 559.
+The protein's natural variant, known as in strain: SP-496, features a modification of the amino acid from T to A at position 612.
+The protein's natural variant, known as has a protective effect against diastolic hypertension;, features a modification of the amino acid from E to K at position 65.
+The protein's natural variant, known as in OFD14;, features a modification of the amino acid from C to G at position 1029.
+The protein's natural variant, known as in strain: IFO 3455 and PA103, features a modification of the amino acid from M to I at position 144.
+The protein's natural variant, known as in strain: PA103, features a modification of the amino acid from R to W at position 180.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from P to S at position 301.
+The protein's natural variant, known as in CDG2Q;, features a modification of the amino acid from W to G at position 634.
+The protein's natural variant, known as in PLCA1;, features a modification of the amino acid from G to A at position 618.
+The protein's natural variant, known as in PLCA1;, features a modification of the amino acid from D to V at position 647.
+The protein's natural variant, known as in PLCA1;, features a modification of the amino acid from I to T at position 691.
+The protein's natural variant, known as in PLCA1;, features a modification of the amino acid from P to L at position 694.
+The protein's natural variant, known as in PLCA1;, features a modification of the amino acid from K to T at position 697.
+The protein's natural variant, known as in strain: CC-503, features a modification of the amino acid from L to V at position 580.
+The protein's natural variant, known as in strain: CC-503 and cw15, features a modification of the amino acid from K to R at position 1588.
+The protein's natural variant, known as in strain: CC-503, features a modification of the amino acid from P to A at position 1610.
+The protein's natural variant, known as in strain: CC-503, features a modification of the amino acid from P to A at position 1618.
+The protein's natural variant, known as in severe obesity with type 2 diabetes;, features a modification of the amino acid from R to W at position 70.
+The protein's natural variant, known as in obesity;, features a modification of the amino acid from V to I at position 102.
+The protein's natural variant, known as found in Nmf249 mice, a Charcot-Marie-Tooth 2D model; involved in neuromuscular dysfunction; contrary to the wild-type protein, strongly interacts with NRP1 and competes with VEGFA for NRP1-binding; no effect on subcellular location, features a modification of the amino acid from P to YK at position 278.
+The protein's natural variant, known as in strain: Isolate 2, features a modification of the amino acid from M to V at position 110.
+The protein's natural variant, known as in HLD4; transfection with the mutant protein impairs cell growth that worsens with increasing temperature;, features a modification of the amino acid from D to G at position 29.
+The protein's natural variant, known as in SPG13;, features a modification of the amino acid from V to I at position 98.
+The protein's natural variant, known as in HLD9;, features a modification of the amino acid from D to G at position 2.
+The protein's natural variant, known as in HLD9;, features a modification of the amino acid from R to Q at position 512.
+The protein's natural variant, known as in 25% of the molecules, features a modification of the amino acid from K to Q at position 103.
+The protein's natural variant, known as in strain: J21, features a modification of the amino acid from S to F at position 8.
+The protein's natural variant, known as in strain: J15, J17, J24, J25, C5, C7, C24, E4, E9, E12, 184 and ATCC 24064, features a modification of the amino acid from V to I at position 11.
+The protein's natural variant, known as in strain: J26 and J19, features a modification of the amino acid from A to G at position 57.
+The protein's natural variant, known as in strain: J25, features a modification of the amino acid from D to N at position 69.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from LLLLLY to ILLFIS at position 11.
+The protein's natural variant, known as in allele ALS9-1, features a modification of the amino acid from DSLTWTRSVEYVYKG to NSLTWANAANYGYQT at position 42.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from V to A at position 39.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from T to N at position 49.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from A to P at position 63.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from M to L at position 71.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from S to T at position 80.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from DKA to ARV at position 124.
+The protein's natural variant, known as in allele ALS9-1, features a modification of the amino acid from IT to FS at position 133.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from T to A at position 146.
+The protein's natural variant, known as in allele ALS9-1, features a modification of the amino acid from M to T at position 161.
+The protein's natural variant, known as in allele ALS9-1, features a modification of the amino acid from KISTTVDFDASPVSPSGYITSSRII to EISTSVDFQASPISSSGYIASARVV at position 190.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from A to L at position 196.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from S to V at position 202.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from T to A at position 218.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from Q to N at position 220.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from I to V at position 229.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from T to S at position 250.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from SSSGIIVEYE to TSTSITVEFQ at position 265.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from SENVEQ to AENIDK at position 286.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from K to E at position 298.
+The protein's natural variant, known as in allele ALS9-1, features a modification of the amino acid from W to T at position 312.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from N to D at position 322.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from I to V at position 325.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from K to R at position 331.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from A to D at position 335.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from T to S at position 348.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from V to I at position 357.
+The protein's natural variant, known as in allele ALS9-1, features a modification of the amino acid from IGIS to VGVT at position 374.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from F to L at position 380.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from A to G at position 382.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from T to A at position 400.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from T to N at position 404.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from V to I at position 410.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from S to T at position 417.
+The protein's natural variant, known as in allele ALS9-1, features a modification of the amino acid from I to V at position 423.
+The protein's natural variant, known as in allele ALS9-1, features a modification of the amino acid from QIPSPDPTTTITEFWSESFASTTTVTNPPDGTNSVIIKEPYN to ELPSPA at position 470.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from V to I at position 453.
+The protein's natural variant, known as in allele ALS9-1, features a modification of the amino acid from I to V at position 489.
+The protein's natural variant, known as in allele ALS9-1, features a modification of the amino acid from V to I at position 501.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from V to I at position 525.
+The protein's natural variant, known as in allele ALS9-1, features a modification of the amino acid from I to V at position 561.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from Y to H at position 577.
+The protein's natural variant, known as in allele ALS9-1, features a modification of the amino acid from V to F at position 607.
+The protein's natural variant, known as in allele ALS9-1, features a modification of the amino acid from I to V at position 609.
+The protein's natural variant, known as in allele ALS9-1, features a modification of the amino acid from I to V at position 633.
+The protein's natural variant, known as in allele ALS9-1, features a modification of the amino acid from V to I at position 645.
+The protein's natural variant, known as in allele ALS9-1, features a modification of the amino acid from I to V at position 669.
+The protein's natural variant, known as in allele ALS9-1, features a modification of the amino acid from V to I at position 679.
+The protein's natural variant, known as in allele ALS9-1, features a modification of the amino acid from K to M at position 682.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from Y to F at position 685.
+The protein's natural variant, known as in allele ALS9-1, features a modification of the amino acid from T to R at position 712.
+The protein's natural variant, known as in allele ALS9-1, features a modification of the amino acid from K to M at position 718.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from V to I at position 753.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from P to L at position 781.
+The protein's natural variant, known as in allele ALS9-1, features a modification of the amino acid from V to I at position 789.
+The protein's natural variant, known as in allele ALS9-1, features a modification of the amino acid from I to V at position 813.
+The protein's natural variant, known as in allele ALS9-1, features a modification of the amino acid from T to R at position 820.
+The protein's natural variant, known as in allele ALS9-1, features a modification of the amino acid from K to M at position 826.
+The protein's natural variant, known as in allele ALS9-1, features a modification of the amino acid from I to V at position 849.
+The protein's natural variant, known as in allele ALS9-1, features a modification of the amino acid from T to S at position 882.
+The protein's natural variant, known as in allele ALS9-1, features a modification of the amino acid from I to V at position 885.
+The protein's natural variant, known as in allele ALS9-1, features a modification of the amino acid from I to V at position 921.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from T to N at position 944.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from S to Y at position 948.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from V to I at position 993.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from V to I at position 1029.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from Y to H at position 1045.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from V to I at position 1065.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from I to V at position 1077.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from Y to H at position 1081.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from KTFYSSEAQSSLEIDSSNTFMTSISVS to TIFHSSEPHYSSDFDSSDSFVTLISVT at position 1134.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from A to T at position 1149.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from ISSYSLSTSF to LSSYTWSSGL at position 1164.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from L to F at position 1170.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from SSPS to NLPT at position 1183.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from MYSSVTSAVTSIDNDREVPTSTTTYLHSKLYSESISTVI to VYSSTASAVASTDGDSVVPSSTNLVTQSISSSETYCIDISGCSSVRQSSSVMVTPSNSGRIIISDSAYLTTTYSHSESDLESIVTVV at position 1227.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from L to S at position 1238.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from N to D at position 1242.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from STVSEESLHY to TTVSDDNSYS at position 1257.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from M to V at position 1301.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from S to N at position 1308.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from M to L at position 1429.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from T to TTAESIATKTIVSETPVTKVLSSKSLAANASPSEPTSKKE at position 1488.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from D to G at position 1799.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from K to N at position 1859.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from V to I at position 1861.
+The protein's natural variant, known as in allele ALS9-2, features a modification of the amino acid from L to H at position 1875.
+The protein's natural variant, known as in HLD5; induces misfolding and degradation, leading to destabilization of the PI4K complex;, features a modification of the amino acid from L to P at position 53.
+The protein's natural variant, known as in HLD5; induces misfolding and degradation, leading to destabilization of the PI4K complex, features a modification of the amino acid from C to R at position 57.
+The protein's natural variant, known as in strain: ECOR 49 and ECOR 50, features a modification of the amino acid from V to I at position 151.
+The protein's natural variant, known as in strain: ECOR 16, features a modification of the amino acid from G to S at position 186.
+The protein's natural variant, known as in strain: ECOR 16, features a modification of the amino acid from E to H at position 252.
+The protein's natural variant, known as in strain: ECOR 49, features a modification of the amino acid from E to K at position 252.
+The protein's natural variant, known as in strain: ECOR 38, ECOR 39, ECOR 40, ECOR 50, ECOR 65 and ECOR 68, features a modification of the amino acid from E to Q at position 252.
+The protein's natural variant, known as in strain: ECOR 38, ECOR 39, ECOR 40, ECOR 49, ECOR 50 and ECOR 65, features a modification of the amino acid from A to T at position 294.
+The protein's natural variant, known as in strain: cv. Ag-0, features a modification of the amino acid from E to Q at position 47.
+The protein's natural variant, known as in strain: cv. Per-1, features a modification of the amino acid from K to R at position 95.
+The protein's natural variant, known as in strain: cv. Mal, features a modification of the amino acid from V to F at position 143.
+The protein's natural variant, known as in strain: cv. Bas-2, features a modification of the amino acid from N to S at position 182.
+The protein's natural variant, known as in strain: cv. Ct-1, features a modification of the amino acid from G to S at position 186.
+The protein's natural variant, known as in strain: cv. Tsar, features a modification of the amino acid from A to T at position 192.
+The protein's natural variant, known as in strain: cv. Edi-0, cv. Lip-0, cv. Sie and cv. Bur-0, features a modification of the amino acid from A to T at position 193.
+The protein's natural variant, known as in strain: cv. Mas, features a modification of the amino acid from V to G at position 198.
+The protein's natural variant, known as in strain: cv. Dul, features a modification of the amino acid from V to I at position 198.
+The protein's natural variant, known as in CMT1H;, features a modification of the amino acid from T to I at position 48.
+The protein's natural variant, known as in ARMD3; no effect on secretion; no effect on homodimerization;, features a modification of the amino acid from V to L at position 60.
+The protein's natural variant, known as in ARMD3; no effect on secretion; no effect on homodimerization;, features a modification of the amino acid from R to Q at position 71.
+The protein's natural variant, known as in ARMD3; no effect on secretion; slightly increases homodimerization in absence of Ca(2+);, features a modification of the amino acid from P to S at position 87.
+The protein's natural variant, known as in CMT1H;, features a modification of the amino acid from G to S at position 90.
+The protein's natural variant, known as in ARMD3; almost abolishes secretion; no effect on homodimerization, features a modification of the amino acid from Q to P at position 124.
+The protein's natural variant, known as no effect on secretion; slightly increases homodimerization in absence of Ca(2+);, features a modification of the amino acid from V to M at position 126.
+The protein's natural variant, known as in ARMD3; decreases secretion; slightly increases homodimerization in absence of Ca(2+); no effect on protein folding;, features a modification of the amino acid from I to T at position 169.
+The protein's natural variant, known as slightly increases homodimerization in absence of Ca(2+); no effect on protein folding; no effect on secretion;, features a modification of the amino acid from G to R at position 202.
+The protein's natural variant, known as in ARCL1A; formation of extracellular globular aggregates; decreases cell growth; reduces interaction with ELN; abolishes secretion; increases homodimerization;, features a modification of the amino acid from C to R at position 217.
+The protein's natural variant, known as in ARCL1A; decreases expression; produces protein misfolding; abolishes secretion; reduces interaction with ELN; increases homodimerization; impairs elastic fiber development;, features a modification of the amino acid from S to P at position 227.
+The protein's natural variant, known as in ARMD3, ARCL1A and CMT1H; produces protein misolding; decreases secretion; no effect on homodimerization;, features a modification of the amino acid from G to S at position 267.
+The protein's natural variant, known as found in a patient with autosomal recessive cutis laxa also carrying a mutation in ELN; unknown pathological significance;, features a modification of the amino acid from L to M at position 301.
+The protein's natural variant, known as in ARMD3; no effect on secretion; slightly increases homodimerization in absence of Ca(2+);, features a modification of the amino acid from R to W at position 351.
+The protein's natural variant, known as in ARMD3; no effect on secretion;, features a modification of the amino acid from A to T at position 363.
+The protein's natural variant, known as in CMT1H;, features a modification of the amino acid from R to C at position 373.
+The protein's natural variant, known as in ARMD3; decreases secretion; slightly increases homodimerization in absence of Ca(2+);, features a modification of the amino acid from G to E at position 412.
+The natural variant of this protein is characterized by an amino acid alteration from F to Y at position 100.
+The natural variant of this protein is characterized by an amino acid alteration from T to S at position 108.
+The natural variant of this protein is characterized by an amino acid alteration from L to M at position 141.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 219.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from V to L at position 221.
+The protein's natural variant, known as in SIMHA; unknown pathological significance;, features a modification of the amino acid from G to V at position 802.
+The protein's natural variant, known as in SIMHA, features a modification of the amino acid from V to VV at position 939.
+The protein's natural variant, known as in SIMHA; unknown pathological significance;, features a modification of the amino acid from R to G at position 962.
+The protein's natural variant, known as in SIMHA; unknown pathological significance;, features a modification of the amino acid from K to N at position 1214.
+The protein's natural variant, known as in SIMHA, features a modification of the amino acid from S to W at position 1685.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from S to F at position 147.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from T to R at position 262.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from Q to K at position 764.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from S to L at position 775.
+The protein's natural variant, known as probable allelic variation, features a modification of the amino acid from I to V at position 221.
+The protein's natural variant, known as in HH17; phenotype consistent with Kallmann syndrome;, features a modification of the amino acid from T to M at position 77.
+The protein's natural variant, known as in HH17; without anosmia;, features a modification of the amino acid from D to N at position 82.
+The protein's natural variant, known as in HH17; phenotype consistent with Kallmann syndrome;, features a modification of the amino acid from K to R at position 154.
+The protein's natural variant, known as in HH17; phenotype consistent with Kallmann syndrome;, features a modification of the amino acid from C to Y at position 186.
+The protein's natural variant, known as in HH17; rare variant associated with susceptibility to disease; some patients have a second mutation in another HH-associated gene including DUSP6 and FGFR1;, features a modification of the amino acid from S to Y at position 218.
+The protein's natural variant, known as in HH17; without anosmia;, features a modification of the amino acid from V to M at position 258.
+The protein's natural variant, known as in HH17; without anosmia;, features a modification of the amino acid from V to I at position 281.
+The protein's natural variant, known as in SPGF10; results in significantly reduced GTP hydrolysis; disrupts interaction with SEPTIN7, SEPTIN6 and SEPTIN2; decreases interaction with SPAG4;, features a modification of the amino acid from T to M at position 89.
+The protein's natural variant, known as in SPGF10; results in significantly reduced GTP hydrolysis due to impaired GTP binding; disrupts interaction with SEPTIN7, SEPTIN6 and SEPTIN2; absence of SEPTIN12, SEPTIN7, SEPTIN6, SEPTIN2 and SEPTIN4 from the sperm annulus; disrupts interaction with LMNB1;, features a modification of the amino acid from D to N at position 197.
+The protein's natural variant, known as in CMH29; loss-of-function variant unable to rescue heart defects and cardiac failure in zebrafish morphants, features a modification of the amino acid from R to H at position 306.
+The protein's natural variant, known as in COXPD3; decreased protein abundance; decreased mitochondrial translation products; patient fibroblast phenotype can be rescued by coexpression with wild-type TSFM;, features a modification of the amino acid from C to S at position 240.
+The protein's natural variant, known as in COXPD3;, features a modification of the amino acid from R to W at position 312.
+The protein's natural variant, known as in strain: Netherlands line N30, features a modification of the amino acid from V to G at position 75.
+The protein's natural variant, known as in strain: Netherlands line N07 and Netherlands line N14, features a modification of the amino acid from I to M at position 400.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from Q to R at position 579.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from T to I at position 53.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from V to I at position 279.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from A to T at position 667.
+The protein's natural variant, known as in plasmid pWR100 and plasmid pWR501, features a modification of the amino acid from V to A at position 725.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from S to G at position 923.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from A to T at position 961.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from G to V at position 1000.
+The protein's natural variant, known as in plasmid pINV_F6_M1382, features a modification of the amino acid from Q to H at position 1016.
+The natural variant of this protein is characterized by an amino acid alteration from H to L at position 11.
+The protein's natural variant, known as in CMTX6; gain of function; results in a 5-fold increase in kinase activity, decreased sensitivity to pyruvate inhibition, reduced affinity for nucleotides and increased affinity for pyruvate dehydrogenase complex component E2 (PDC-E2), leading to PDC hyperphosphorylation and increased inactivation;, features a modification of the amino acid from R to H at position 158.
+The protein's natural variant, known as in a head & neck squamous cell carcinoma sample; somatic mutation, features a modification of the amino acid from E to A at position 219.
+The natural variant of this protein is characterized by an amino acid alteration from Y to S at position 334.
+The protein's natural variant, known as in strain: Xc33-1, features a modification of the amino acid from APK to H at position 9.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from K to E at position 178.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from K to G at position 178.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from K to R at position 178.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from I to M at position 360.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from I to V at position 464.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from T to A at position 489.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from Q to R at position 491.
+The protein's natural variant, known as in strain: cv. Cvi-1, features a modification of the amino acid from P to T at position 49.
+The protein's natural variant, known as in DBA6;, features a modification of the amino acid from G to S at position 140.
+The protein's natural variant, known as in DBA6, features a modification of the amino acid from A to V at position 285.
+The protein's natural variant, known as in albofibrase-2, features a modification of the amino acid from V to A at position 60.
+The protein's natural variant, known as in IMMD; associated in cis with R-58 in a IMMD family; unknown pathological significance; does not affect mitochondrial structure and organization;, features a modification of the amino acid from R to S at position 15.
+The protein's natural variant, known as in FTDALS2;, features a modification of the amino acid from P to S at position 34.
+The protein's natural variant, known as in IMMD; associated in cis with S-15 in a IMMD family; causes mitochondrial fragmentation;, features a modification of the amino acid from G to R at position 58.
+The protein's natural variant, known as in FTDALS2; results in disorganization of mitochondrial cristae;, features a modification of the amino acid from S to L at position 59.
+The protein's natural variant, known as in SMAJ;, features a modification of the amino acid from G to V at position 66.
+The protein's natural variant, known as in strain: UTEX 646 / Bohlin, features a modification of the amino acid from S to G at position 35.
+The protein's natural variant, known as in strain: UTEX 646 / Bohlin, features a modification of the amino acid from QD to HE at position 153.
+The protein's natural variant, known as in strain: UTEX 646 / Bohlin, features a modification of the amino acid from D to G at position 183.
+The protein's natural variant, known as in strain: UTEX 646 / Bohlin, features a modification of the amino acid from D to G at position 211.
+The protein's natural variant, known as in strain: UTEX 646 / Bohlin, features a modification of the amino acid from T to A at position 374.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from K to N at position 369.
+The protein's natural variant, known as in MCPH2;, features a modification of the amino acid from V to M at position 65.
+The protein's natural variant, known as in MCPH2;, features a modification of the amino acid from W to S at position 224.
+The protein's natural variant, known as in MCPH2; the mutant protein does not localize to the spindle pole during mitosis;, features a modification of the amino acid from R to H at position 438.
+The protein's natural variant, known as in MCPH2;, features a modification of the amino acid from D to N at position 511.
+The protein's natural variant, known as in MCPH2;, features a modification of the amino acid from E to K at position 526.
+The protein's natural variant, known as in OOMD3; loss of interaction with ZP2;, features a modification of the amino acid from A to T at position 134.
+The protein's natural variant, known as in strain: 10, features a modification of the amino acid from I to A at position 8.
+The protein's natural variant, known as in strain: 019, features a modification of the amino acid from P to S at position 31.
+The protein's natural variant, known as in strain: 019, features a modification of the amino acid from IS to VH at position 60.
+The protein's natural variant, known as in strain: 019, features a modification of the amino acid from TGSDRK to SGTDRN at position 80.
+The protein's natural variant, known as in strain: 019, features a modification of the amino acid from VLVLHSMFNTN to GARFALRVSTG at position 95.
+The protein's natural variant, known as in strain: 76-250, features a modification of the amino acid from VLVLHS to GARFAL at position 90.
+The protein's natural variant, known as in strain: 019, features a modification of the amino acid from GTYTT to KTFTE at position 108.
+The protein's natural variant, known as in strain: 019, features a modification of the amino acid from TS to AA at position 115.
+The protein's natural variant, known as in strain: 019, features a modification of the amino acid from RH to GV at position 120.
+The protein's natural variant, known as in strain: 019, features a modification of the amino acid from QYGDFSDDRDVADGSVSTGTDLQ to KYGNETSSGTVME at position 145.
+The protein's natural variant, known as in strain: 019, features a modification of the amino acid from T to Q at position 150.
+The protein's natural variant, known as in strain: 019, features a modification of the amino acid from FK to LR at position 155.
+The protein's natural variant, known as in strain: 019, features a modification of the amino acid from I to V at position 173.
+The protein's natural variant, known as in strain: 76-250, features a modification of the amino acid from A to S at position 190.
+The protein's natural variant, known as in strain: 019 and 76-250, features a modification of the amino acid from EDVDNDYT to DNDGGYTGTTNYH at position 217.
+The protein's natural variant, known as in strain: 019 and 76-250, features a modification of the amino acid from H to D at position 224.
+The protein's natural variant, known as in strain: 019 and 76-250, features a modification of the amino acid from T to A at position 253.
+The protein's natural variant, known as in strain: 019 and 76-250, features a modification of the amino acid from R to Q at position 264.
+The protein's natural variant, known as in strain: 019 and 76-250, features a modification of the amino acid from N to D at position 280.
+The protein's natural variant, known as in strain: 76-250, features a modification of the amino acid from R to H at position 362.
+The natural variant of this protein is characterized by an amino acid alteration from L to V at position 10.
+The natural variant of this protein is characterized by an amino acid alteration from A to R at position 50.
+The natural variant of this protein is characterized by an amino acid alteration from L to V at position 98.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from A to G at position 37.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from E to K at position 110.
+The protein's natural variant, known as in CHBL1 and AGS1; autosomal dominant form; loss of 3'-to-5' DNA exonuclease activity; abolished ability to degrade micronuclear DNA and restrict activation of innate immune response;, features a modification of the amino acid from D to N at position 18.
+The protein's natural variant, known as in AGS1 and SLE; primary fibroblasts from an AGS1 patient carrying H-169 show defective G1/S transition and chronic G2/MDNA damage checkpoint activation; strongly reduces activity;, features a modification of the amino acid from R to H at position 114.
+The protein's natural variant, known as in AGS1; increases ubiquitination levels; no effect on exonuclease activity;, features a modification of the amino acid from V to A at position 122.
+The protein's natural variant, known as in SLE;, features a modification of the amino acid from A to V at position 158.
+The protein's natural variant, known as in AGS1; increases ubiquitination levels; no effect on exonuclease activity;, features a modification of the amino acid from E to K at position 198.
+The protein's natural variant, known as in AGS1; heterozygous compound with H-169; loss of activity, features a modification of the amino acid from D to DD at position 200.
+The protein's natural variant, known as in AGS1 and SLE, features a modification of the amino acid from D to H at position 200.
+The protein's natural variant, known as in AGS1; autosomal dominant form; no effect on dsDNA exonuclease activity; abolishes ssDNA exonuclease activity;, features a modification of the amino acid from D to N at position 200.
+The protein's natural variant, known as in AGS1; reduces activity by 75%;, features a modification of the amino acid from V to D at position 201.
+The protein's natural variant, known as in SLE; associated in cis with P-302;, features a modification of the amino acid from G to S at position 227.
+The protein's natural variant, known as in SLE;, features a modification of the amino acid from R to S at position 240.
+The protein's natural variant, known as in SLE; associated in cis with S-282;, features a modification of the amino acid from A to P at position 247.
+The protein's natural variant, known as in SLE; increases ubiquitination levels; no effect on exonuclease activity;, features a modification of the amino acid from P to L at position 290.
+The protein's natural variant, known as in AGS1; decreases ubiquitination levels; decreases colocalization with UBQLN1; no effect on exonuclease activity;, features a modification of the amino acid from T to P at position 303.
+The protein's natural variant, known as in SLE; decreases ubiquitination levels; decreases colocalization with UBQLN1; no effect on exonuclease activity;, features a modification of the amino acid from Y to C at position 305.
+The protein's natural variant, known as in SLE;, features a modification of the amino acid from G to A at position 306.
+The protein's natural variant, known as in ALS15; uncertain pathological significance;, features a modification of the amino acid from S to N at position 155.
+The protein's natural variant, known as in ALS15; uncertain pathological significance;, features a modification of the amino acid from P to T at position 189.
+The protein's natural variant, known as probable disease-associated variant found in a patient with frontotemporal dementia;, features a modification of the amino acid from A to V at position 282.
+The protein's natural variant, known as in ALS15;, features a modification of the amino acid from A to T at position 283.
+The protein's natural variant, known as in ALS15;, features a modification of the amino acid from Q to R at position 425.
+The protein's natural variant, known as in ALS15;, features a modification of the amino acid from T to I at position 487.
+The protein's natural variant, known as in ALS15; leads to defective ubiquitin-mediated proteasomal degradation; reduces binding to HNRNPA1 and FAF2; increases translocation of HNRNPA1 to the cytoplasm; adversely affects ERAD;, features a modification of the amino acid from P to H at position 497.
+The protein's natural variant, known as in ALS15; reduces binding to HNRNPA1; increases translocation of HNRNPA1 to the cytoplasm;, features a modification of the amino acid from P to S at position 497.
+The protein's natural variant, known as in ALS15; leads to defective ubiquitin-mediated proteasomal degradation; reduces binding to HNRNPA1; increases translocation of HNRNPA1 to the cytoplasm;, features a modification of the amino acid from P to T at position 506.
+The protein's natural variant, known as in ALS15; reduces binding to HNRNPA1; increases translocation of HNRNPA1 to the cytoplasm;, features a modification of the amino acid from P to S at position 509.
+The protein's natural variant, known as in ALS15; reduces binding to HNRNPA1; increases translocation of HNRNPA1 to the cytoplasm;, features a modification of the amino acid from P to S at position 525.
+The natural variant of this protein is characterized by an amino acid alteration from R to C at position 241.
+The protein's natural variant, known as in vim2, features a modification of the amino acid from S to SS at position 43.
+The protein's natural variant, known as in strain: ZIM30C, features a modification of the amino acid from PCCM to RVACK at position 47.
+The protein's natural variant, known as in MPS2; mild form; increase in enzyme activity observed in transfected cells, features a modification of the amino acid from L to P at position 41.
+The protein's natural variant, known as in MPS2, features a modification of the amino acid from D to N at position 45.
+The protein's natural variant, known as in MPS2; mild form;, features a modification of the amino acid from R to P at position 48.
+The protein's natural variant, known as in MPS2; severe form, features a modification of the amino acid from Y to D at position 54.
+The protein's natural variant, known as in MPS2; mild/intermediate form;, features a modification of the amino acid from N to D at position 63.
+The protein's natural variant, known as in MPS2; severe, features a modification of the amino acid from A to E at position 68.
+The protein's natural variant, known as in MPS2; mild form;, features a modification of the amino acid from S to N at position 71.
+The protein's natural variant, known as in MPS2; severe form, features a modification of the amino acid from S to R at position 71.
+The protein's natural variant, known as in MPS2; severe form, features a modification of the amino acid from L to F at position 73.
+The protein's natural variant, known as in MPS2; mild form, features a modification of the amino acid from A to E at position 79.
+The protein's natural variant, known as in MPS2, features a modification of the amino acid from A to E at position 82.
+The protein's natural variant, known as in MPS2; no significant enzyme activity, features a modification of the amino acid from A to V at position 82.
+The protein's natural variant, known as in MPS2; severe form, features a modification of the amino acid from A to S at position 85.
+The protein's natural variant, known as in MPS2; mild to severe forms;, features a modification of the amino acid from A to T at position 85.
+The protein's natural variant, known as in MPS2; intermediate to severe forms;, features a modification of the amino acid from P to L at position 86.
+The protein's natural variant, known as in MPS2, features a modification of the amino acid from P to Q at position 86.
+The protein's natural variant, known as in MPS2; severe form, features a modification of the amino acid from P to R at position 86.
+The protein's natural variant, known as in MPS2; mild form, features a modification of the amino acid from S to N at position 87.
+The protein's natural variant, known as in MPS2; severe form;, features a modification of the amino acid from R to C at position 88.
+The protein's natural variant, known as in MPS2; severe form, features a modification of the amino acid from R to G at position 88.
+The protein's natural variant, known as in MPS2; intermediate/severe form; higher affinity for the artificial substrate; poor transport to lysosomes;, features a modification of the amino acid from R to H at position 88.
+The protein's natural variant, known as in MPS2; severe form, features a modification of the amino acid from R to L at position 88.
+The protein's natural variant, known as in MPS2; severe form; total absence of residual activity; poor transport to lysosomes, features a modification of the amino acid from R to P at position 88.
+The protein's natural variant, known as in MPS2, features a modification of the amino acid from V to F at position 89.
+The protein's natural variant, known as in MPS2; severe form;, features a modification of the amino acid from L to P at position 92.
+The protein's natural variant, known as in MPS2; mild form, features a modification of the amino acid from G to D at position 94.
+The protein's natural variant, known as in MPS2; intermediate form, features a modification of the amino acid from R to G at position 95.
+The protein's natural variant, known as in MPS2; mild form, features a modification of the amino acid from R to T at position 95.
+The protein's natural variant, known as in MPS2; mild form, features a modification of the amino acid from L to R at position 102.
+The protein's natural variant, known as in MPS2; mild form, features a modification of the amino acid from Y to C at position 108.
+The protein's natural variant, known as in MPS2; mild form, features a modification of the amino acid from Y to S at position 108.
+The protein's natural variant, known as in MPS2, features a modification of the amino acid from N to Y at position 115.
+The protein's natural variant, known as in MPS2; severe form, features a modification of the amino acid from S to Y at position 117.
+The protein's natural variant, known as in MPS2; mild to severe forms; greatly reduced activity; poor transport to lysosomes, features a modification of the amino acid from T to I at position 118.
+The protein's natural variant, known as in MPS2; mild form;, features a modification of the amino acid from P to H at position 120.
+The protein's natural variant, known as in MPS2; severe form;, features a modification of the amino acid from P to R at position 120.
+The protein's natural variant, known as in MPS2; severe form, features a modification of the amino acid from Q to H at position 121.
+The protein's natural variant, known as in MPS2; severe form, features a modification of the amino acid from Q to R at position 121.
+The protein's natural variant, known as in MPS2; mild form, features a modification of the amino acid from E to V at position 125.
+The protein's natural variant, known as in MPS2; severe form, features a modification of the amino acid from S to W at position 132.
+The protein's natural variant, known as in MPS2; severe form, features a modification of the amino acid from G to R at position 134.
+The protein's natural variant, known as in MPS2; intermediate form, features a modification of the amino acid from K to N at position 135.
+The protein's natural variant, known as in MPS2; intermediate form;, features a modification of the amino acid from K to R at position 135.
+The protein's natural variant, known as in MPS2; mild/intermediate form, features a modification of the amino acid from H to D at position 138.
+The protein's natural variant, known as in MPS2; no significant enzyme activity, features a modification of the amino acid from G to V at position 140.
+The protein's natural variant, known as in MPS2, features a modification of the amino acid from S to F at position 143.
+The protein's natural variant, known as in MPS2; intermediate form, features a modification of the amino acid from D to H at position 148.
+The protein's natural variant, known as in MPS2; severe form, features a modification of the amino acid from H to P at position 159.
+The protein's natural variant, known as in MPS2;, features a modification of the amino acid from P to R at position 160.
+The protein's natural variant, known as in MPS2; mild form, features a modification of the amino acid from N to I at position 181.
+The protein's natural variant, known as in MPS2; intermediate form, features a modification of the amino acid from L to P at position 182.
+The protein's natural variant, known as in MPS2; mild/intermediate form, features a modification of the amino acid from C to F at position 184.
+The protein's natural variant, known as in MPS2, features a modification of the amino acid from C to W at position 184.
+The protein's natural variant, known as in MPS2; mild/intermediate form;, features a modification of the amino acid from L to S at position 196.
+The protein's natural variant, known as in MPS2; mild form, features a modification of the amino acid from D to G at position 198.
+The protein's natural variant, known as in MPS2; intermediate form;, features a modification of the amino acid from A to P at position 205.
+The protein's natural variant, known as in MPS2; intermediate form, features a modification of the amino acid from L to P at position 221.
+The protein's natural variant, known as in MPS2; severe form, features a modification of the amino acid from G to E at position 224.
+The protein's natural variant, known as in MPS2; intermediate form, features a modification of the amino acid from Y to D at position 225.
+The protein's natural variant, known as in MPS2; intermediate form, features a modification of the amino acid from K to M at position 227.
+The protein's natural variant, known as in MPS2; severe form, features a modification of the amino acid from K to Q at position 227.
+The protein's natural variant, known as in MPS2, features a modification of the amino acid from P to L at position 228.
+The protein's natural variant, known as in MPS2; severe form, features a modification of the amino acid from P to T at position 228.
+The protein's natural variant, known as in MPS2; intermediate/severe form;, features a modification of the amino acid from H to R at position 229.
+The protein's natural variant, known as in MPS2; severe form, features a modification of the amino acid from H to Y at position 229.
+The protein's natural variant, known as in MPS2; mild form, features a modification of the amino acid from P to L at position 231.
+The protein's natural variant, known as in MPS2;, features a modification of the amino acid from D to N at position 252.
+The protein's natural variant, known as in MPS2; severe form, features a modification of the amino acid from L to P at position 259.
+The protein's natural variant, known as in MPS2, features a modification of the amino acid from Y to N at position 264.
+The protein's natural variant, known as in MPS2; intermediate form; deleterious mutation; residual activity of 7.5% of the wild-type, features a modification of the amino acid from N to I at position 265.
+The protein's natural variant, known as in MPS2; mild form, features a modification of the amino acid from P to H at position 266.
+The protein's natural variant, known as in MPS2, features a modification of the amino acid from P to R at position 266.
+The protein's natural variant, known as in MPS2;, features a modification of the amino acid from D to V at position 269.
+The protein's natural variant, known as in MPS2; mild form, features a modification of the amino acid from Q to H at position 293.
+The protein's natural variant, known as in MPS2; mild form, features a modification of the amino acid from S to I at position 299.
+The protein's natural variant, known as in MPS2; mild form, features a modification of the amino acid from D to E at position 308.
+The protein's natural variant, known as in MPS2; intermediate form, features a modification of the amino acid from D to N at position 308.
+The protein's natural variant, known as in MPS2; severe form;, features a modification of the amino acid from T to A at position 309.
+The protein's natural variant, known as in MPS2; unknown pathological significance;, features a modification of the amino acid from R to C at position 313.
+The protein's natural variant, known as in MPS2; severe form, features a modification of the amino acid from L to P at position 314.
+The protein's natural variant, known as in MPS2; severe form;, features a modification of the amino acid from S to L at position 333.
+The protein's natural variant, known as in MPS2; severe form;, features a modification of the amino acid from D to G at position 334.
+The protein's natural variant, known as in MPS2; mild form, features a modification of the amino acid from D to N at position 334.
+The protein's natural variant, known as in MPS2; intermediate form, features a modification of the amino acid from H to R at position 335.
+The protein's natural variant, known as in MPS2; severe from, features a modification of the amino acid from G to E at position 336.
+The protein's natural variant, known as in MPS2; severe form, features a modification of the amino acid from G to R at position 336.
+The protein's natural variant, known as in MPS2; intermediate form, features a modification of the amino acid from W to R at position 337.
+The protein's natural variant, known as in MPS2; severe form, features a modification of the amino acid from L to R at position 339.
+The protein's natural variant, known as in MPS2; mild form, features a modification of the amino acid from G to D at position 340.
+The protein's natural variant, known as in MPS2; severe form, features a modification of the amino acid from E to K at position 341.
+The protein's natural variant, known as in MPS2; mild form, features a modification of the amino acid from H to Y at position 342.
+The protein's natural variant, known as in MPS2; mild form, features a modification of the amino acid from W to C at position 345.
+The protein's natural variant, known as in MPS2; mild/severe form, features a modification of the amino acid from A to D at position 346.
+The protein's natural variant, known as in MPS2; mild/severe form, features a modification of the amino acid from A to V at position 346.
+The protein's natural variant, known as in MPS2, features a modification of the amino acid from K to I at position 347.
+The protein's natural variant, known as in MPS2; severe form, features a modification of the amino acid from K to Q at position 347.
+The protein's natural variant, known as in MPS2; severe form; deleterious mutation confirmed, features a modification of the amino acid from K to T at position 347.
+The protein's natural variant, known as in MPS2, features a modification of the amino acid from Y to H at position 348.
+The protein's natural variant, known as in MPS2; severe form, features a modification of the amino acid from S to I at position 349.
+The protein's natural variant, known as in MPS2; severe form, features a modification of the amino acid from P to R at position 358.
+The protein's natural variant, known as in MPS2; intermediate form, features a modification of the amino acid from L to R at position 403.
+The protein's natural variant, known as in MPS2, features a modification of the amino acid from L to P at position 410.
+The protein's natural variant, known as in MPS2; mild form;, features a modification of the amino acid from C to G at position 422.
+The protein's natural variant, known as in MPS2; severe form;, features a modification of the amino acid from C to R at position 422.
+The protein's natural variant, known as in MPS2; severe form, features a modification of the amino acid from C to Y at position 432.
+The protein's natural variant, known as in MPS2, features a modification of the amino acid from E to K at position 434.
+The protein's natural variant, known as in MPS2; severe form, features a modification of the amino acid from Q to P at position 465.
+The protein's natural variant, known as in MPS2; severe form;, features a modification of the amino acid from P to L at position 467.
+The protein's natural variant, known as in MPS2; mild to severe forms, features a modification of the amino acid from R to G at position 468.
+The protein's natural variant, known as in MPS2; mild to severe forms;, features a modification of the amino acid from R to L at position 468.
+The protein's natural variant, known as in MPS2; severe/intermediate form; greatly reduced activity; poor transport to lysosomes;, features a modification of the amino acid from R to Q at position 468.
+The protein's natural variant, known as in MPS2; mild to severe forms;, features a modification of the amino acid from R to W at position 468.
+The protein's natural variant, known as in MPS2; mild form, features a modification of the amino acid from P to H at position 469.
+The protein's natural variant, known as in MPS2; mild form;, features a modification of the amino acid from D to G at position 478.
+The protein's natural variant, known as in MPS2; severe form, features a modification of the amino acid from D to Y at position 478.
+The protein's natural variant, known as in MPS2; mild form, features a modification of the amino acid from P to L at position 480.
+The protein's natural variant, known as in MPS2; mild form, features a modification of the amino acid from P to Q at position 480.
+The protein's natural variant, known as in MPS2; severe form, features a modification of the amino acid from P to R at position 480.
+The protein's natural variant, known as in MPS2, features a modification of the amino acid from I to K at position 485.
+The protein's natural variant, known as in MPS2; severe form, features a modification of the amino acid from I to R at position 485.
+The protein's natural variant, known as in MPS2; intermediate form; mutation A-489 confirmed as causative of MPS2, features a modification of the amino acid from MG to IA at position 489.
+The protein's natural variant, known as in MPS2; intermediate form, features a modification of the amino acid from Y to S at position 490.
+The protein's natural variant, known as in MPS2; mild form, features a modification of the amino acid from S to F at position 491.
+The protein's natural variant, known as in MPS2; severe form, features a modification of the amino acid from W to C at position 502.
+The protein's natural variant, known as in MPS2;, features a modification of the amino acid from W to S at position 502.
+The protein's natural variant, known as in MPS2; severe form, features a modification of the amino acid from E to K at position 521.
+The protein's natural variant, known as in MPS2; severe form, features a modification of the amino acid from E to V at position 521.
+The protein's natural variant, known as in MPS2; mild form;, features a modification of the amino acid from Y to C at position 523.
+The protein's natural variant, known as in strain: G7, features a modification of the amino acid from N to K at position 4.
+The protein's natural variant, known as in strain: ATCC 17484, features a modification of the amino acid from S to F at position 12.
+The protein's natural variant, known as in strain: G7, features a modification of the amino acid from S to T at position 15.
+The protein's natural variant, known as in strain: G7, features a modification of the amino acid from K to R at position 32.
+The protein's natural variant, known as in strain: G7, features a modification of the amino acid from A to S at position 50.
+The protein's natural variant, known as in strain: G7, features a modification of the amino acid from N to S at position 70.
+The protein's natural variant, known as in strain: G7, features a modification of the amino acid from SV to NA at position 91.
+The protein's natural variant, known as in strain: G7, features a modification of the amino acid from D to E at position 122.
+The protein's natural variant, known as in strain: G7, features a modification of the amino acid from M to I at position 173.
+The protein's natural variant, known as in strain: G7, features a modification of the amino acid from S to A at position 225.
+The protein's natural variant, known as in strain: BS202, features a modification of the amino acid from S to C at position 225.
+The protein's natural variant, known as in strain: G7, features a modification of the amino acid from A to V at position 232.
+The protein's natural variant, known as in strain: G7, features a modification of the amino acid from A to S at position 275.
+The protein's natural variant, known as in strain: G7, features a modification of the amino acid from E to K at position 391.
+The protein's natural variant, known as in strain: ATCC 17484, features a modification of the amino acid from Q to R at position 421.
+The protein's natural variant, known as in strain: G7, features a modification of the amino acid from H to D at position 434.
+The natural variant of this protein is characterized by an amino acid alteration from A to D at position 42.
+The natural variant of this protein is characterized by an amino acid alteration from A to G at position 146.
+The natural variant of this protein is characterized by an amino acid alteration from I to G at position 235.
+The natural variant of this protein is characterized by an amino acid alteration from D to A at position 447.
+The protein's natural variant, known as associated with an increased waist-to-hip ratio;, features a modification of the amino acid from A to T at position 64.
+The protein's natural variant, known as associated with susceptibility to type II diabetes mellitus;, features a modification of the amino acid from M to L at position 229.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from T to M at position 155.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation; increased autophosphorylation at Y-284; increased function in phosphorylation of peptide substrates; no effect on subcellular localization to perinuclear region, features a modification of the amino acid from R to L at position 34.
+The protein's natural variant, known as in an ovarian mucinous carcinoma sample; somatic mutation; increased autophosphorylation at Y-284; increased function in phosphorylation of peptide substrates and WASP; no effect on subcellular localization to perinuclear region;, features a modification of the amino acid from R to Q at position 99.
+The protein's natural variant, known as in an ovarian endometrioid cancer sample; somatic mutation; undergoes autoactivation and causes phosphorylation on Y-284 leading to activation of AKT1; increased autophosphorylation at Y-284; increased function in phosphorylation of peptide substrates and WASP; no effect on catalytic activity itself as the purified kinase domain has activity in vitro comparable to wild-type protein; no effect on subcellular localization to perinuclear region;, features a modification of the amino acid from E to K at position 346.
+The protein's natural variant, known as in a gastric adenocarcinoma sample; somatic mutation; increased autophosphorylation at Y-284; increased function in phosphorylation of peptide substrates and WASP; no effect on subcellular localization to perinuclear region, features a modification of the amino acid from M to I at position 409.
+The protein's natural variant, known as found in patients with childhood-onset epilepsy; unknown pathological significance; loss of interaction with NEDD4 and NEDD4L; increased protein abundance;, features a modification of the amino acid from V to M at position 638.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from A to V at position 418.
+The protein's natural variant, known as in strain: ATCC 49503, features a modification of the amino acid from V to I at position 280.
+The protein's natural variant, known as in strain: ATCC 49503, features a modification of the amino acid from T to N at position 332.
+The protein's natural variant, known as in strain: ATCC 49503, features a modification of the amino acid from I to V at position 392.
+The protein's natural variant, known as in strain: ATCC 49503 and NCTC 11638, features a modification of the amino acid from R to Q at position 432.
+The protein's natural variant, known as in strain: NCTC 11638, features a modification of the amino acid from D to N at position 434.
+The protein's natural variant, known as in strain: ATCC 49503, features a modification of the amino acid from S to H at position 440.
+The protein's natural variant, known as in a colorectal cancer sample, features a modification of the amino acid from R to L at position 267.
+The protein's natural variant, known as in a colorectal cancer sample;, features a modification of the amino acid from P to L at position 486.
+The protein's natural variant, known as in a colorectal cancer sample;, features a modification of the amino acid from S to L at position 490.
+The protein's natural variant, known as in colorectal cancer samples; somatic mutation; decreased binding to CCAR2; significant decrease in its ability to induce the relocalization of CCAR2 to the cytoplasm; loss of its ability to repress the beta-catenin pathway; loss of its ability to induce the SIRT1-mediated deacetylation of beta-catenin;, features a modification of the amino acid from R to Q at position 506.
+The protein's natural variant, known as in colorectal cancer samples; somatic mutation;, features a modification of the amino acid from A to V at position 698.
+The protein's natural variant, known as in strain: pseudo8 and pseudo9, features a modification of the amino acid from G to S at position 171.
+The protein's natural variant, known as in equal amount, features a modification of the amino acid from L to I at position 1.
+The protein's natural variant, known as in ACADVLD, features a modification of the amino acid from T to N at position 158.
+The protein's natural variant, known as in ACADVLD;, features a modification of the amino acid from Q to R at position 159.
+The protein's natural variant, known as in ACADVLD;, features a modification of the amino acid from V to M at position 174.
+The protein's natural variant, known as in ACADVLD;, features a modification of the amino acid from G to S at position 185.
+The protein's natural variant, known as in ACADVLD;, features a modification of the amino acid from A to P at position 213.
+The protein's natural variant, known as in ACADVLD;, features a modification of the amino acid from E to K at position 218.
+The protein's natural variant, known as in ACADVLD, features a modification of the amino acid from L to R at position 243.
+The protein's natural variant, known as in ACADVLD;, features a modification of the amino acid from K to E at position 247.
+The protein's natural variant, known as in ACADVLD, features a modification of the amino acid from K to T at position 247.
+The protein's natural variant, known as in ACADVLD;, features a modification of the amino acid from T to M at position 260.
+The protein's natural variant, known as in ACADVLD, features a modification of the amino acid from A to D at position 281.
+The protein's natural variant, known as in ACADVLD;, features a modification of the amino acid from V to A at position 283.
+The protein's natural variant, known as in ACADVLD;, features a modification of the amino acid from G to D at position 290.
+The protein's natural variant, known as in ACADVLD;, features a modification of the amino acid from G to E at position 294.
+The protein's natural variant, known as in ACADVLD;, features a modification of the amino acid from K to N at position 299.
+The protein's natural variant, known as in ACADVLD;, features a modification of the amino acid from V to A at position 317.
+The protein's natural variant, known as in ACADVLD, features a modification of the amino acid from M to V at position 352.
+The protein's natural variant, known as in ACADVLD;, features a modification of the amino acid from R to C at position 366.
+The protein's natural variant, known as in ACADVLD;, features a modification of the amino acid from R to H at position 366.
+The protein's natural variant, known as in ACADVLD;, features a modification of the amino acid from K to Q at position 382.
+The protein's natural variant, known as in ACADVLD, features a modification of the amino acid from D to H at position 405.
+The protein's natural variant, known as in ACADVLD;, features a modification of the amino acid from G to D at position 441.
+The protein's natural variant, known as in ACADVLD;, features a modification of the amino acid from R to H at position 450.
+The protein's natural variant, known as in ACADVLD;, features a modification of the amino acid from R to Q at position 453.
+The protein's natural variant, known as in ACADVLD;, features a modification of the amino acid from D to N at position 454.
+The protein's natural variant, known as in ACADVLD;, features a modification of the amino acid from R to H at position 456.
+The protein's natural variant, known as in ACADVLD; loss of acyl-CoA dehydrogenase activity; Loss of FAD cofactor-binding;, features a modification of the amino acid from F to L at position 458.
+The protein's natural variant, known as in ACADVLD;, features a modification of the amino acid from R to W at position 459.
+The protein's natural variant, known as in ACADVLD;, features a modification of the amino acid from G to E at position 463.
+The protein's natural variant, known as in ACADVLD;, features a modification of the amino acid from R to Q at position 469.
+The protein's natural variant, known as in ACADVLD;, features a modification of the amino acid from R to W at position 469.
+The protein's natural variant, known as in ACADVLD; decreased association with mitochondrial inner membrane; may affect substrate specificity, possibly reducing the affinity for long-chain acyl-CoA substrates;, features a modification of the amino acid from A to P at position 490.
+The protein's natural variant, known as in ACADVLD; decreased association with mitochondrial inner membrane; decreased specific activity towards several substrates in vitro, features a modification of the amino acid from L to P at position 502.
+The protein's natural variant, known as in ACADVLD; unknown pathological significance;, features a modification of the amino acid from E to K at position 534.
+The protein's natural variant, known as in ACADVLD; Loss of homodimerization; loss of localization to mitochondrial inner membrane;, features a modification of the amino acid from S to W at position 583.
+The protein's natural variant, known as in ACADVLD, features a modification of the amino acid from L to I at position 602.
+The protein's natural variant, known as in ACADVLD;, features a modification of the amino acid from R to W at position 613.
+The protein's natural variant, known as in ACADVLD;, features a modification of the amino acid from R to Q at position 615.
+The protein's natural variant, known as in CALJA; absence from the plasma-membrane; exhibits no catalytic AMPase activity;, features a modification of the amino acid from C to Y at position 358.
+The natural variant of this protein is characterized by an amino acid alteration from D to G at position 58.
+The protein's natural variant, known as in strain: cv. Cvi-0, cv. Kas-0, cv. Landsberg erecta and cv. Mt-0, features a modification of the amino acid from E to V at position 14.
+The protein's natural variant, known as in strain: cv. Ang-0, cv. Bla-1, cv. Bur-0, cv. Ct-1, cv. Cvi-0, cv. Kas-0, cv. Landsberg erecta, cv. Mt-0, cv. Pog-0, cv. Tamm-17, cv. Tsu-0, cv. Wu-0, features a modification of the amino acid from N to K at position 47.
+The protein's natural variant, known as in strain: cv. Bur-0, features a modification of the amino acid from I to V at position 57.
+The protein's natural variant, known as in strain: cv. Cvi-0, cv. Kas-0, cv. Landsberg erecta and cv. Mt-0, features a modification of the amino acid from S to I at position 91.
+The protein's natural variant, known as in strain: cv. Cvi-0, cv. Kas-0, cv. Landsberg erecta and cv. Mt-0, features a modification of the amino acid from N to H at position 94.
+The protein's natural variant, known as in strain: cv. Cvi-0, cv. Kas-0, cv. Landsberg erecta and cv. Mt-0, features a modification of the amino acid from M to R at position 112.
+The protein's natural variant, known as in strain: cv. Cvi-0, cv. Kas-0, cv. Landsberg erecta and cv. Mt-0, features a modification of the amino acid from V to E at position 135.
+The protein's natural variant, known as in strain: cv. Cvi-0, cv. Kas-0, cv. Landsberg erecta and cv. Mt-0, features a modification of the amino acid from I to V at position 138.
+The protein's natural variant, known as in strain: cv. Cvi-0, cv. Kas-0, cv. Landsberg erecta and cv. Mt-0, features a modification of the amino acid from A to T at position 143.
+The protein's natural variant, known as in strain: cv. Bur-0, features a modification of the amino acid from D to N at position 165.
+The protein's natural variant, known as in strain: cv. Cvi-0, cv. Kas-0, cv. Landsberg erecta and cv. Mt-0, features a modification of the amino acid from K to R at position 226.
+The protein's natural variant, known as in strain: cv. Bur-0, features a modification of the amino acid from V to A at position 275.
+The protein's natural variant, known as in strain: cv. Cvi-0, cv. Kas-0, cv. Landsberg erecta and cv. Mt-0, features a modification of the amino acid from YPSG to FPNR at position 283.
+The protein's natural variant, known as in strain: cv. Ang-0 and cv. Tsu-0, features a modification of the amino acid from P to S at position 281.
+The protein's natural variant, known as in strain: cv. Cvi-0, cv. Kas-0, cv. Landsberg erecta and cv. Mt-0, features a modification of the amino acid from V to I at position 289.
+The protein's natural variant, known as in strain: cv. Ang-0, cv. Bla-1, cv. Bur-0, cv. Ct-1, cv. Cvi-0, cv. Kas-0, cv. Landsberg erecta, cv. Mt-0, cv. Pog-0, cv. Tamm-17, cv. Tsu-0, cv. Wu-0, features a modification of the amino acid from H to R at position 294.
+The protein's natural variant, known as in strain: cv. Cvi-0, cv. Kas-0, cv. Landsberg erecta and cv. Mt-0, features a modification of the amino acid from N to D at position 306.
+The protein's natural variant, known as in strain: cv. Cvi-0, cv. Kas-0, cv. Landsberg erecta and cv. Mt-0, features a modification of the amino acid from I to V at position 310.
+The protein's natural variant, known as in strain: cv. Cvi-0, cv. Kas-0, cv. Landsberg erecta and cv. Mt-0, features a modification of the amino acid from R to C at position 342.
+The protein's natural variant, known as in strain: cv. Cvi-0, cv. Kas-0, cv. Landsberg erecta and cv. Mt-0, features a modification of the amino acid from C to R at position 349.
+The protein's natural variant, known as in strain: cv. Cvi-0, cv. Kas-0, cv. Landsberg erecta and cv. Mt-0, features a modification of the amino acid from S to SS at position 380.
+The protein's natural variant, known as in strain: cv. Wu-0, features a modification of the amino acid from I to L at position 394.
+The protein's natural variant, known as in strain: cv. Cvi-0, cv. Kas-0, cv. Landsberg erecta and cv. Mt-0, features a modification of the amino acid from A to V at position 407.
+The protein's natural variant, known as in strain: cv. Ct-1 and cv. Tamm-17, features a modification of the amino acid from E to D at position 419.
+The protein's natural variant, known as in strain: cv. Bur-0, features a modification of the amino acid from E to K at position 435.
+The protein's natural variant, known as in strain: cv. Cvi-0, cv. Kas-0, cv. Landsberg erecta and cv. Mt-0, features a modification of the amino acid from A to T at position 468.
+The protein's natural variant, known as in strain: cv. Cvi-0, cv. Kas-0, cv. Landsberg erecta and cv. Mt-0, features a modification of the amino acid from V to F at position 473.
+The protein's natural variant, known as in strain: cv. Ang-0,, cv. Bla-1, cv. Bur-0, cv. Ct-1, cv. Cvi-0, cv. Kas-0, cv. Landsberg erecta, cv. Mt-0, cv. Pog-0, cv. Tamm-17, cv. Tsu-0, cv. Wu-0, features a modification of the amino acid from M to V at position 479.
+The protein's natural variant, known as in strain: cv. Cvi-0, cv. Kas-0, cv. Landsberg erecta and cv. Mt-0, features a modification of the amino acid from F to S at position 488.
+The protein's natural variant, known as in strain: cv. Cvi-0, cv. Kas-0, cv. Landsberg erecta and cv. Mt-0, features a modification of the amino acid from E to K at position 511.
+The protein's natural variant, known as in strain: cv. Cvi-0, cv. Kas-0, cv. Landsberg erecta and cv. Mt-0, features a modification of the amino acid from N to D at position 527.
+The protein's natural variant, known as in strain: cv. Cvi-0, cv. Kas-0, cv. Landsberg erecta and cv. Mt-0, features a modification of the amino acid from L to F at position 532.
+The protein's natural variant, known as in strain: cv. Bla-1, cv. Bur-0, cv. Cvi, cv. Kas-0, cv. Landsberg erecta, cv. Mt-0 and cv. Wu-0, features a modification of the amino acid from H to Q at position 607.
+The protein's natural variant, known as in strain: cv. Wu-0, features a modification of the amino acid from L to R at position 640.
+The protein's natural variant, known as in strain: cv. Cvi-0, cv. Kas-0, cv. Landsberg erecta and cv. Mt-0, features a modification of the amino acid from V to I at position 702.
+The protein's natural variant, known as in strain: cv. Cvi-0, cv. Kas-0, cv. Landsberg erecta and cv. Mt-0, features a modification of the amino acid from H to T at position 711.
+The protein's natural variant, known as in strain: cv. Cvi-0, cv. Kas-0, cv. Landsberg erecta and cv. Mt-0, features a modification of the amino acid from W to C at position 724.
+The protein's natural variant, known as in strain: cv. Cvi-0, cv. Kas-0, cv. Landsberg erecta and cv. Mt-0, features a modification of the amino acid from K to KK at position 730.
+The protein's natural variant, known as in strain: cv. Cvi-0, cv. Kas-0, cv. Landsberg erecta and cv. Mt-0, features a modification of the amino acid from K to N at position 734.
+The protein's natural variant, known as in strain: cv. Cvi-0, cv. Kas-0, cv. Landsberg erecta and cv. Mt-0, features a modification of the amino acid from N to S at position 739.
+The protein's natural variant, known as in strain: cv. Cvi-0, cv. Kas-0, cv. Landsberg erecta and cv. Mt-0, features a modification of the amino acid from I to L at position 782.
+The protein's natural variant, known as in strain: cv. Cvi-0, cv. Kas-0, cv. Landsberg erecta and cv. Mt-0, features a modification of the amino acid from A to V at position 789.
+The protein's natural variant, known as in strain: cv. Cvi-0, cv. Kas-0, cv. Landsberg erecta and cv. Mt-0, features a modification of the amino acid from Q to A at position 800.
+The protein's natural variant, known as in strain: cv. Bla-1 and cv. Bur-0, features a modification of the amino acid from K to T at position 846.
+The protein's natural variant, known as in strain: cv. Cvi-0 and cv. Mt-0, features a modification of the amino acid from SVVKVEEFV to VLSKLKNLS at position 855.
+The protein's natural variant, known as in strain: cv. Kas-0 and cv. Landsberg erecta, features a modification of the amino acid from QY to RH at position 876.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from R to G at position 877.
+The protein's natural variant, known as in strain: cv. Kas-0 and cv. Landsberg erecta, features a modification of the amino acid from T to S at position 881.
+The protein's natural variant, known as in Lig v 1.0102, features a modification of the amino acid from V to I at position 51.
+The protein's natural variant, known as in Lig v 1.0102, features a modification of the amino acid from K to R at position 60.
+The protein's natural variant, known as in Lig v 1.0102, features a modification of the amino acid from N to S at position 66.
+The protein's natural variant, known as in Lig v 1.0102, features a modification of the amino acid from I to L at position 83.
+The protein's natural variant, known as in Lig v 1.0102, features a modification of the amino acid from T to I at position 95.
+The protein's natural variant, known as in Lig v 1.0102, features a modification of the amino acid from V to M at position 106.
+The protein's natural variant, known as in Lig v 1.0102, features a modification of the amino acid from L to F at position 123.
+The protein's natural variant, known as in Lig v 1.0102, features a modification of the amino acid from V to A at position 127.
+The protein's natural variant, known as in MTDPS1;, features a modification of the amino acid from R to Q at position 44.
+The protein's natural variant, known as in MTDPS1;, features a modification of the amino acid from G to R at position 145.
+The protein's natural variant, known as in MTDPS1;, features a modification of the amino acid from G to S at position 153.
+The protein's natural variant, known as in MTDPS1;, features a modification of the amino acid from K to R at position 222.
+The protein's natural variant, known as in MTDPS1;, features a modification of the amino acid from E to A at position 289.
+The protein's natural variant, known as in strain: KIM5 and 91001, features a modification of the amino acid from N to K at position 504.
+The natural variant of this protein is characterized by an amino acid alteration from T to K at position 96.
+The natural variant of this protein is characterized by an amino acid alteration from R to C at position 319.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 335.
+The natural variant of this protein is characterized by an amino acid alteration from G to D at position 356.
+The natural variant of this protein is characterized by an amino acid alteration from I to L at position 365.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from E to Q at position 53.
+The natural variant of this protein is characterized by an amino acid alteration from G to A at position 48.
+The natural variant of this protein is characterized by an amino acid alteration from P to Q at position 160.
+The natural variant of this protein is characterized by an amino acid alteration from D to V at position 225.
+The protein's natural variant, known as in CPND;, features a modification of the amino acid from G to D at position 178.
+The protein's natural variant, known as in SPG86, features a modification of the amino acid from R to H at position 118.
+The protein's natural variant, known as in SPG86; unknown pathological significance, features a modification of the amino acid from N to I at position 121.
+The protein's natural variant, known as in SPG86; unknown pathological significance, features a modification of the amino acid from R to Q at position 252.
+The protein's natural variant, known as in SPG86; unknown pathological significance, features a modification of the amino acid from L to R at position 409.
+The protein's natural variant, known as in SPG86; no protein detected in homozygous patient cells; increased levels of phosphatidylserine and decreased levels of lysophosphatidylserine in homozygous patient cells, indicating loss of function in phosphatidylserine catabolism, features a modification of the amino acid from R to Q at position 457.
+The protein's natural variant, known as in CHNG2; loss of activity;, features a modification of the amino acid from R to H at position 31.
+The protein's natural variant, known as in CHNG2; loss of activity;, features a modification of the amino acid from Q to P at position 40.
+The protein's natural variant, known as in CHNG2; loss of activity;, features a modification of the amino acid from C to Y at position 57.
+The protein's natural variant, known as in CHNG2; loss of activity;, features a modification of the amino acid from L to R at position 62.
+The protein's natural variant, known as in CAND; <0.5% residual enzyme activity;, features a modification of the amino acid from I to T at position 16.
+The protein's natural variant, known as in CAND, features a modification of the amino acid from H to P at position 21.
+The protein's natural variant, known as in CAND;, features a modification of the amino acid from E to G at position 24.
+The protein's natural variant, known as in CAND; <1% residual enzyme activity, features a modification of the amino acid from E to K at position 24.
+The protein's natural variant, known as in CAND; 3% residual enzyme activity;, features a modification of the amino acid from G to R at position 27.
+The protein's natural variant, known as in CAND; <1% residual enzyme activity;, features a modification of the amino acid from L to P at position 30.
+The protein's natural variant, known as in CAND, features a modification of the amino acid from A to T at position 57.
+The protein's natural variant, known as in CAND; <1% residual enzyme activity;, features a modification of the amino acid from A to V at position 57.
+The protein's natural variant, known as in CAND; <1% residual enzyme activity;, features a modification of the amino acid from R to T at position 63.
+The protein's natural variant, known as in CAND, features a modification of the amino acid from D to A at position 68.
+The protein's natural variant, known as in CAND; <1% residual enzyme activity;, features a modification of the amino acid from L to R at position 69.
+The protein's natural variant, known as in CAND; <1% residual enzyme activity, features a modification of the amino acid from G to V at position 101.
+The protein's natural variant, known as in CAND; <0.5% residual enzyme activity, features a modification of the amino acid from D to E at position 114.
+The protein's natural variant, known as in CAND;, features a modification of the amino acid from D to Y at position 114.
+The protein's natural variant, known as in CAND; about 25% residual enzyme activity;, features a modification of the amino acid from G to E at position 123.
+The protein's natural variant, known as in CAND; <1% residual enzyme activity;, features a modification of the amino acid from E to K at position 129.
+The protein's natural variant, known as in CAND;, features a modification of the amino acid from I to T at position 143.
+The protein's natural variant, known as in CAND; loss of activity;, features a modification of the amino acid from C to R at position 152.
+The protein's natural variant, known as in CAND, features a modification of the amino acid from C to W at position 152.
+The protein's natural variant, known as in CAND; <0.5% residual enzyme activity, features a modification of the amino acid from C to Y at position 152.
+The protein's natural variant, known as in CAND; undetectable enzyme activity;, features a modification of the amino acid from R to C at position 168.
+The protein's natural variant, known as in CAND;, features a modification of the amino acid from R to H at position 168.
+The protein's natural variant, known as in CAND; 5.5% residual enzyme activity;, features a modification of the amino acid from I to T at position 170.
+The protein's natural variant, known as in CAND; Loss of catalytic activity, features a modification of the amino acid from I to T at position 177.
+The protein's natural variant, known as in CAND; <1% residual enzyme activity;, features a modification of the amino acid from G to V at position 180.
+The protein's natural variant, known as in CAND;, features a modification of the amino acid from P to T at position 181.
+The protein's natural variant, known as in CAND;, features a modification of the amino acid from P to H at position 183.
+The protein's natural variant, known as in CAND, features a modification of the amino acid from V to F at position 186.
+The protein's natural variant, known as in CAND, features a modification of the amino acid from M to R at position 195.
+The protein's natural variant, known as in CAND; 12% residual enzyme activity, features a modification of the amino acid from D to H at position 204.
+The protein's natural variant, known as in CAND;, features a modification of the amino acid from Y to C at position 231.
+The protein's natural variant, known as in CAND;, features a modification of the amino acid from H to R at position 244.
+The protein's natural variant, known as in CAND; <1% residual enzyme activity, features a modification of the amino acid from Q to R at position 248.
+The protein's natural variant, known as in CAND;, features a modification of the amino acid from D to V at position 249.
+The protein's natural variant, known as in CAND;, features a modification of the amino acid from G to R at position 274.
+The protein's natural variant, known as in CAND;, features a modification of the amino acid from P to L at position 280.
+The protein's natural variant, known as in CAND;, features a modification of the amino acid from P to S at position 280.
+The protein's natural variant, known as in CAND; predominant mutation in Ashkenazi Jewish population; 99% loss of activity;, features a modification of the amino acid from E to A at position 285.
+The protein's natural variant, known as in CAND; <1% residual enzyme activity;, features a modification of the amino acid from A to D at position 286.
+The protein's natural variant, known as in CAND;, features a modification of the amino acid from A to T at position 287.
+The protein's natural variant, known as in CAND, features a modification of the amino acid from F to S at position 295.
+The protein's natural variant, known as in CAND; pan-European origin; most prevalent among non-Jewish CAND patients; probably the most ancient mutation; loss of activity;, features a modification of the amino acid from A to E at position 305.
+The protein's natural variant, known as in TEL2-1; short telomere length, features a modification of the amino acid from S to R at position 129.
+The protein's natural variant, known as in strain: JEC20, features a modification of the amino acid from L to I at position 102.
+The protein's natural variant, known as in strain: JEC20, features a modification of the amino acid from A to V at position 107.
+The protein's natural variant, known as in PSORS2; reduces NF-kappa-B activation;, features a modification of the amino acid from R to W at position 69.
+The protein's natural variant, known as in PSORS2 and PRP; may result in altered splicing of exon 3; increases NF-kappaB transcription factor activity; enhances CBCL10-MALT1-CARD14 complex formation; enhances MALT1 protease activity;, features a modification of the amino acid from G to S at position 117.
+The protein's natural variant, known as in PRP, features a modification of the amino acid from C to S at position 127.
+The protein's natural variant, known as in PRP, features a modification of the amino acid from Q to L at position 136.
+The protein's natural variant, known as in PSORS2; increases NF-kappaB transcription factor activity; enhances CBCL10-MALT1-CARD14 complex formation; enhances MALT1 protease activity;, features a modification of the amino acid from E to A at position 138.
+The protein's natural variant, known as in PSORS2; increases NF-kappaB transcription factor activity;, features a modification of the amino acid from E to G at position 142.
+The protein's natural variant, known as in PSORS2; increases NF-kappaB transcription factor activity; enhances MALT1 protease activity;, features a modification of the amino acid from E to K at position 142.
+The protein's natural variant, known as in PSORS2; increases NF-kappaB transcription factor activity;, features a modification of the amino acid from L to R at position 150.
+The protein's natural variant, known as in PSORS2; unknown pathological significance; decreases NF-kappaB transcription factor activity;, features a modification of the amino acid from R to Q at position 151.
+The protein's natural variant, known as in PSORS2; unknown pathological significance; decreases NF-kappaB transcription factor activity;, features a modification of the amino acid from R to W at position 151.
+The protein's natural variant, known as in PRP;, features a modification of the amino acid from L to P at position 156.
+The protein's natural variant, known as may be associated with susceptibility to psoriasis; does not change MALT1 protease activity;, features a modification of the amino acid from H to N at position 171.
+The protein's natural variant, known as in PSORS2; increases NF-kappaB transcription factor activity;, features a modification of the amino acid from E to K at position 197.
+The protein's natural variant, known as in PSORS2; unknown pathological significance; no effect on NF-kappaB transcription factor activity, features a modification of the amino acid from L to P at position 209.
+The protein's natural variant, known as in PSORS2; unknown pathological significance; decreases NF-kappaB transcription factor activity;, features a modification of the amino acid from A to T at position 216.
+The protein's natural variant, known as unknown pathological significance; decreases NF-kappaB transcription factor activity;, features a modification of the amino acid from R to C at position 218.
+The protein's natural variant, known as may be associated with susceptibility to psoriasis;, features a modification of the amino acid from D to G at position 285.
+The protein's natural variant, known as unknown pathological significance; does not change NF-kappaB transcription factor activity;, features a modification of the amino acid from M to V at position 338.
+The natural variant of this protein is characterized by an amino acid alteration from L to P at position 357.
+The protein's natural variant, known as in PSORS2; unknown pathological significance; decreases NF-kappaB transcription factor activity;, features a modification of the amino acid from T to A at position 420.
+The protein's natural variant, known as in PSORS2; unknown pathological significance; does not change NF-kappaB transcription factor activity;, features a modification of the amino acid from S to L at position 602.
+The protein's natural variant, known as in PSORS2; unknown pathological significance; does not change NF-kappaB transcription factor activity, features a modification of the amino acid from A to G at position 639.
+The protein's natural variant, known as in CILD36; no effect on expression at protein level; almost complete loss of outer dynein arms and inner dynein arms in motor cilia; immotile cilia; abolishes interaction with DNAI2, features a modification of the amino acid from D to Y at position 133.
+The protein's natural variant, known as in strain: Reids2, features a modification of the amino acid from S to L at position 394.
+The protein's natural variant, known as in SPGF27; loss of protein expression in sperm cells, no effect in airway epithelial cells;, features a modification of the amino acid from L to P at position 673.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from S to G at position 490.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to C at position 609.
+The protein's natural variant, known as in strain: Awamori-1, AKU-4011, K1, K5, NRIC 23, NRIC 1413 and NRIC 1685, features a modification of the amino acid from A to T at position 118.
+The protein's natural variant, known as in strain: Pasteur Red, features a modification of the amino acid from I to V at position 199.
+The protein's natural variant, known as in strain: YJM326, features a modification of the amino acid from G to C at position 217.
+The protein's natural variant, known as in strain: Levuline ALS, Lalvin CY-3079, Cote des Blancs, I14, M1, M11, M12, M13, M15, M2, M20, M21, M22, M24, M29, M3, M30, M31, M32, M33, M34, M4, M5, M6, M7, M8, M9, NRRLY-1438, NRRLYB-1952, NRRLY-2411, Pasteur Red, UCD 51, UCD 2120, UCD 175, UCD 529, UCD 765, UCD 781, UCD 820, UCD 762, YJM269, YJM270, YJM308, YJM326, YJM434 and YJM1129, features a modification of the amino acid from T to S at position 253.
+The protein's natural variant, known as in strain: SK1, V1-09, YJM269, YJM270, YJM280, YJM320, YJM326, YJM339, YJM627 and YJM1129, features a modification of the amino acid from N to D at position 310.
+The protein's natural variant, known as in strain: YJM269 and YJM270, features a modification of the amino acid from I to V at position 541.
+The protein's natural variant, known as in IMD41;, features a modification of the amino acid from Y to S at position 41.
+The protein's natural variant, known as in IMD41; the receptor does not localize to the plasma membrane;, features a modification of the amino acid from S to N at position 166.
+The protein's natural variant, known as in IBD30; unknown pathological significance, features a modification of the amino acid from V to I at position 44.
+The protein's natural variant, known as in IBD30;, features a modification of the amino acid from F to I at position 102.
+The protein's natural variant, known as in strain: Isolate SAS-3, features a modification of the amino acid from G to S at position 16.
+The protein's natural variant, known as in strain: Isolate SAS-3, features a modification of the amino acid from I to V at position 156.
+The protein's natural variant, known as in GAMOS5;, features a modification of the amino acid from L to P at position 136.
+The protein's natural variant, known as in GAMOS5;, features a modification of the amino acid from Y to C at position 149.
+The protein's natural variant, known as decreased inosine transport;, features a modification of the amino acid from I to T at position 216.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from A to T at position 293.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from I to V at position 455.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from E to Q at position 110.
+The protein's natural variant, known as in SPGF66; unknown pathological significance;, features a modification of the amino acid from S to G at position 184.
+The protein's natural variant, known as in SPGF66; unknown pathological significance, features a modification of the amino acid from H to L at position 217.
+The protein's natural variant, known as in SPGF66; unknown pathological significance;, features a modification of the amino acid from G to S at position 225.
+The protein's natural variant, known as in SPGF66; unknown pathological significance, features a modification of the amino acid from N to S at position 252.
+The protein's natural variant, known as in SPGF66; unknown pathological significance, features a modification of the amino acid from I to T at position 287.
+The natural variant of this protein is characterized by an amino acid alteration from N to K at position 7.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 8.
+The natural variant of this protein is characterized by an amino acid alteration from V to M at position 223.
+The natural variant of this protein is characterized by an amino acid alteration from C to F at position 326.
+The protein's natural variant, known as in MCPH23; impairs mitotic chromosome compaction;, features a modification of the amino acid from P to L at position 243.
+The protein's natural variant, known as in GCCD4;, features a modification of the amino acid from S to N at position 193.
+The protein's natural variant, known as in GCCD4;, features a modification of the amino acid from T to A at position 357.
+The protein's natural variant, known as in GCCD4, features a modification of the amino acid from H to P at position 365.
+The protein's natural variant, known as in GCCD4;, features a modification of the amino acid from P to L at position 437.
+The protein's natural variant, known as in GCCD4;, features a modification of the amino acid from A to V at position 533.
+The protein's natural variant, known as in GCCD4;, features a modification of the amino acid from G to R at position 664.
+The protein's natural variant, known as in GCCD4, features a modification of the amino acid from G to R at position 678.
+The protein's natural variant, known as in GCCD4;, features a modification of the amino acid from G to D at position 862.
+The protein's natural variant, known as in GCCD4;, features a modification of the amino acid from L to P at position 977.
+The protein's natural variant, known as in GCCD4;, features a modification of the amino acid from A to P at position 1008.
+The protein's natural variant, known as in GCCD4;, features a modification of the amino acid from N to K at position 1009.
+The protein's natural variant, known as in strain: Czech II, features a modification of the amino acid from L to S at position 20.
+The protein's natural variant, known as in strain: Czech II, features a modification of the amino acid from P to L at position 32.
+The protein's natural variant, known as in strain: Czech II, features a modification of the amino acid from T to P at position 120.
+The protein's natural variant, known as in strain: Czech II, features a modification of the amino acid from P to L at position 330.
+The protein's natural variant, known as in CCF; reduces the ability to transactivate a luciferase reporter gene; suppresses wild-type activity in a dose-dependent manner;, features a modification of the amino acid from E to K at position 130.
+The protein's natural variant, known as in 50% of the molecules, features a modification of the amino acid from P to S at position 23.
+The protein's natural variant, known as in clone TM002, features a modification of the amino acid from CN to SS at position 73.
+The protein's natural variant, known as in clone TM002, features a modification of the amino acid from A to T at position 80.
+The protein's natural variant, known as rare variant; found in individuals suffering from stuttering; unknown pathological significance;, features a modification of the amino acid from H to Q at position 84.
+The protein's natural variant, known as rare variant; found in individuals suffering from stuttering; unknown pathological significance;, features a modification of the amino acid from R to C at position 328.
+The protein's natural variant, known as in SARCOS;, features a modification of the amino acid from V to F at position 71.
+The protein's natural variant, known as in SARCOS;, features a modification of the amino acid from P to L at position 287.
+The protein's natural variant, known as in MTDPS9; with progressive liver disease and recurrent hepatic failure;, features a modification of the amino acid from M to L at position 14.
+The protein's natural variant, known as in MTDPS9;, features a modification of the amino acid from G to A at position 85.
+The protein's natural variant, known as in MTDPS9;, features a modification of the amino acid from P to R at position 170.
+The protein's natural variant, known as almost no change in activity;, features a modification of the amino acid from S to A at position 152.
+The protein's natural variant, known as almost no change in activity;, features a modification of the amino acid from D to N at position 389.
+The protein's natural variant, known as in MYP22; reduced DNA polymerase and DNA primase activities; reduced DNA-binding;, features a modification of the amino acid from Y to D at position 89.
+The protein's natural variant, known as in strain: Mysore, features a modification of the amino acid from G to S at position 39.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from A to D at position 42.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from A to T at position 332.
+The protein's natural variant, known as in SPGF53; unknown pathological significance; reduces interaction with ACTL7A, features a modification of the amino acid from S to L at position 345.
+The protein's natural variant, known as in SPGF53; unknown pathological significance; reduces interaction with ACTL7A, features a modification of the amino acid from V to L at position 380.
+The protein's natural variant, known as in strain: YJM 421, features a modification of the amino acid from D to E at position 245.
+The protein's natural variant, known as in strain: YJM 280, YJM 320, YJM 326, YJM 627, YJM 789 and YJM 1129, features a modification of the amino acid from S to N at position 258.
+The protein's natural variant, known as in strain: SK1, YJM 269, YJM 270, YJM 280, YJM 320, YJM 326, YJM 339, YJM 421, YJM 627, YJM 789 and YJM 1129, features a modification of the amino acid from D to N at position 268.
+The protein's natural variant, known as in CSNU; unknown pathological significance, features a modification of the amino acid from V to M at position 40.
+The protein's natural variant, known as in CSNU; type I;, features a modification of the amino acid from I to T at position 44.
+The protein's natural variant, known as in CSNU; unknown pathological significance, features a modification of the amino acid from S to F at position 51.
+The protein's natural variant, known as in CSNU; impairs protein stability and dimer formation;, features a modification of the amino acid from P to L at position 52.
+The protein's natural variant, known as in CSNU;, features a modification of the amino acid from V to M at position 62.
+The protein's natural variant, known as in CSNU;, features a modification of the amino acid from G to R at position 63.
+The protein's natural variant, known as in CSNU, features a modification of the amino acid from W to L at position 69.
+The protein's natural variant, known as in CSNU; partial loss of amino acid transport activity;, features a modification of the amino acid from A to V at position 70.
+The protein's natural variant, known as in CSNU; unknown pathological significance, features a modification of the amino acid from Y to H at position 99.
+The protein's natural variant, known as in CSNU, features a modification of the amino acid from G to E at position 105.
+The protein's natural variant, known as in CSNU; type III; severe loss of amino acid transport activity;, features a modification of the amino acid from G to R at position 105.
+The protein's natural variant, known as in CSNU; unknown pathological significance, features a modification of the amino acid from W to R at position 114.
+The protein's natural variant, known as in CSNU; unknown pathological significance, features a modification of the amino acid from I to L at position 120.
+The protein's natural variant, known as in CSNU; partial loss of amino acid transport activity;, features a modification of the amino acid from T to M at position 123.
+The protein's natural variant, known as in CSNU;, features a modification of the amino acid from A to T at position 126.
+The protein's natural variant, known as no effect on amino acid transport activity;, features a modification of the amino acid from V to A at position 142.
+The protein's natural variant, known as in CSNU, features a modification of the amino acid from A to AA at position 158.
+The protein's natural variant, known as in CSNU; type III; severe loss of amino acid transport activity;, features a modification of the amino acid from V to M at position 170.
+The protein's natural variant, known as in CSNU; type III; partial loss of amino acid transport activity;, features a modification of the amino acid from A to T at position 182.
+The protein's natural variant, known as in CSNU;, features a modification of the amino acid from I to F at position 187.
+The protein's natural variant, known as in CSNU;, features a modification of the amino acid from V to M at position 188.
+The protein's natural variant, known as in CSNU, features a modification of the amino acid from I to II at position 193.
+The protein's natural variant, known as in CSNU; type III; decreased amino acid transport activity;, features a modification of the amino acid from G to R at position 195.
+The protein's natural variant, known as slightly decreased amino acid transport activity;, features a modification of the amino acid from L to M at position 223.
+The protein's natural variant, known as in CSNU; non-classic type I;, features a modification of the amino acid from A to V at position 224.
+The protein's natural variant, known as in CSNU; decreased amino acid transport activity, features a modification of the amino acid from N to D at position 227.
+The protein's natural variant, known as in CSNU; complete loss of amino acid transport activity, features a modification of the amino acid from W to R at position 230.
+The protein's natural variant, known as in CSNU;, features a modification of the amino acid from Y to C at position 232.
+The protein's natural variant, known as in CSNU;, features a modification of the amino acid from I to T at position 241.
+The protein's natural variant, known as in CSNU;, features a modification of the amino acid from R to K at position 250.
+The protein's natural variant, known as in CSNU; type III; impairs protein stability and dimer formation;, features a modification of the amino acid from G to R at position 259.
+The protein's natural variant, known as in CSNU; types I and III;, features a modification of the amino acid from P to L at position 261.
+The protein's natural variant, known as in CSNU;, features a modification of the amino acid from L to F at position 283.
+The protein's natural variant, known as in CSNU; unknown pathological significance;, features a modification of the amino acid from S to F at position 286.
+The protein's natural variant, known as in CSNU, features a modification of the amino acid from A to V at position 316.
+The protein's natural variant, known as in CSNU, features a modification of the amino acid from G to R at position 319.
+The protein's natural variant, known as in CSNU; unknown pathological significance, features a modification of the amino acid from A to E at position 324.
+The protein's natural variant, known as in CSNU; type III;, features a modification of the amino acid from V to M at position 330.
+The protein's natural variant, known as in CSNU; non-classic type I;, features a modification of the amino acid from A to V at position 331.
+The protein's natural variant, known as in CSNU; decreased amino acid transport activity;, features a modification of the amino acid from R to Q at position 333.
+The protein's natural variant, known as in CSNU; severe loss of amino acid transport activity;, features a modification of the amino acid from R to W at position 333.
+The protein's natural variant, known as in CSNU; type III; severe loss of amino acid transport activity;, features a modification of the amino acid from A to T at position 354.
+The protein's natural variant, known as in CSNU;, features a modification of the amino acid from S to R at position 379.
+The protein's natural variant, known as in CSNU; severe loss of amino acid transport activity;, features a modification of the amino acid from A to T at position 382.
+The protein's natural variant, known as in CSNU; unknown pathological significance;, features a modification of the amino acid from K to E at position 401.
+The protein's natural variant, known as in CSNU; unknown pathological significance, features a modification of the amino acid from L to P at position 426.
+The protein's natural variant, known as in CSNU; severe loss of amino acid transport activity; no effect on localization to the apical membrane;, features a modification of the amino acid from P to L at position 482.
+The protein's natural variant, known as in allele fen-1a', features a modification of the amino acid from V to I at position 33.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from L to S at position 120.
+The protein's natural variant, known as in AD; unknown pathological significance, features a modification of the amino acid from Y to C at position 141.
+The protein's natural variant, known as in AD; unknown pathological significance; loss of interaction with APP amyloid-beta peptides, hence reduced turnover of APP amyloid-beta peptides in cells, features a modification of the amino acid from G to R at position 511.
+The protein's natural variant, known as in AD; unknown pathological significance;, features a modification of the amino acid from N to S at position 924.
+The protein's natural variant, known as in AD; unknown pathological significance;, features a modification of the amino acid from N to S at position 1358.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from M to L at position 1581.
+The protein's natural variant, known as in AD; unknown pathological significance;, features a modification of the amino acid from G to D at position 1681.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from L to V at position 1972.
+The protein's natural variant, known as in NDMSBA;, features a modification of the amino acid from G to V at position 23.
+The protein's natural variant, known as in NDMSBA; no effect on protein stability; no effect on subcellular localization; decreased function in positive regulation of cytosolic phospholipase A2 activity; in patient cells homozygous for the mutation;, features a modification of the amino acid from L to F at position 752.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from I to V at position 572.
+The natural variant of this protein is characterized by an amino acid alteration from P to A at position 308.
+The protein's natural variant, known as in WRWF; no effect on subcellular localization; no loss of function; rescues interneurons differentiation when expressed in a zebrafish heterologous system;, features a modification of the amino acid from R to K at position 18.
+The protein's natural variant, known as in WRWF; causes a decrease in synapse number and density;, features a modification of the amino acid from V to L at position 63.
+The protein's natural variant, known as in WRWF; no effect on subcellular localization; partial loss of function; rescues partially interneurons differentiation when expressed in a zebrafish heterologous system;, features a modification of the amino acid from L to H at position 66.
+The protein's natural variant, known as in WRWF, features a modification of the amino acid from H to Q at position 70.
+The protein's natural variant, known as in WRWF; causes a decrease in synapse number and density;, features a modification of the amino acid from R to Q at position 198.
+The protein's natural variant, known as in WRWF;, features a modification of the amino acid from A to T at position 200.
+The protein's natural variant, known as in WRWF, features a modification of the amino acid from A to V at position 200.
+The protein's natural variant, known as in WRWF, features a modification of the amino acid from P to H at position 201.
+The protein's natural variant, known as in WRWF; causes a decrease in synapse number and density;, features a modification of the amino acid from P to S at position 201.
+The protein's natural variant, known as in WRWFFR, features a modification of the amino acid from C to S at position 203.
+The protein's natural variant, known as in WRWFFR;, features a modification of the amino acid from C to F at position 206.
+The protein's natural variant, known as in WRWF; increased cytoplasmic subcellular localization; partial loss of function; rescues partially interneurons differentiation when expressed in a zebrafish heterologous system;, features a modification of the amino acid from R to W at position 213.
+The protein's natural variant, known as in WRWF;, features a modification of the amino acid from K to R at position 217.
+The protein's natural variant, known as in patients with early-onset diabetes type 2; unknown pathological significance;, features a modification of the amino acid from M to R at position 330.
+The protein's natural variant, known as in patients with early-onset diabetes type 2; unknown pathological significance, features a modification of the amino acid from I to N at position 331.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from G to V at position 660.
+The protein's natural variant, known as in NEDDISH; unknown pathological significance;, features a modification of the amino acid from R to H at position 198.
+The protein's natural variant, known as in DEEAH; impaired TNFA-induced activation of the MAP kinases ERK1/2; enhanced susceptibility to TNFA-induced apoptosis; decreased EGF internalization, features a modification of the amino acid from S to F at position 257.
+The protein's natural variant, known as in DEEAH; impaired TNFA-induced activation of the MAP kinases ERK1/2; enhanced susceptibility to TNFA-induced apoptosis; decreased EGF internalization, features a modification of the amino acid from G to V at position 305.
+The protein's natural variant, known as in NEDDISH; unknown pathological significance;, features a modification of the amino acid from L to P at position 346.
+The protein's natural variant, known as in NEDDISH; impaired TNFA-induced activation of the MAP kinases ERK1/2; enhanced susceptibility to TNFA-induced apoptosis; decreased EGF internalization;, features a modification of the amino acid from P to L at position 354.
+The protein's natural variant, known as in DEEAH; unknown pathological significance;, features a modification of the amino acid from P to L at position 372.
+The protein's natural variant, known as in NEDDISH; unknown pathological significance, features a modification of the amino acid from L to P at position 945.
+The protein's natural variant, known as in DEEAH; impaired TNFA-induced activation of the MAP kinases ERK1/2; enhanced susceptibility to TNFA-induced apoptosis; decreased EGF internalization, features a modification of the amino acid from L to R at position 1040.
+The protein's natural variant, known as in NEDDISH; unknown pathological significance, features a modification of the amino acid from Y to S at position 1283.
+The protein's natural variant, known as in NEDDISH; unknown pathological significance, features a modification of the amino acid from W to R at position 1318.
+The protein's natural variant, known as in strain: cv. Borszczagowski, features a modification of the amino acid from I to T at position 83.
+The protein's natural variant, known as in PVNH2; unknown pathological significance;, features a modification of the amino acid from E to K at position 209.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from K to E at position 794.
+The protein's natural variant, known as in BROD;, features a modification of the amino acid from P to L at position 789.
+The protein's natural variant, known as resistance to EMB, features a modification of the amino acid from I to F at position 289.
+The protein's natural variant, known as resistance to EMB, features a modification of the amino acid from I to M at position 289.
+The protein's natural variant, known as resistance to EMB, features a modification of the amino acid from M to T at position 292.
+The protein's natural variant, known as in SCA34;, features a modification of the amino acid from L to F at position 168.
+The protein's natural variant, known as in RP35 and CORD10; heterozygous compound with C-350; loss of localization to cell membrane;, features a modification of the amino acid from D to H at position 345.
+The protein's natural variant, known as in RP35 and CORD10; heterozygous compound with H-345; loss of localization to cell membrane;, features a modification of the amino acid from F to C at position 350.
+The protein's natural variant, known as no effect on localization to cell membrane;, features a modification of the amino acid from R to Q at position 713.
+The protein's natural variant, known as in lexA3, resistant to cleavage. Increased sensitivity to hydroxyurea, features a modification of the amino acid from G to D at position 85.
+The protein's natural variant, known as in MDDGC5;, features a modification of the amino acid from R to W at position 54.
+The protein's natural variant, known as in MDDGC5;, features a modification of the amino acid from V to M at position 79.
+The protein's natural variant, known as in MDDGB5; unknown pathological significance;, features a modification of the amino acid from A to G at position 114.
+The protein's natural variant, known as in MDDGC5;, features a modification of the amino acid from R to W at position 134.
+The protein's natural variant, known as in MDDGC5;, features a modification of the amino acid from R to S at position 143.
+The protein's natural variant, known as in MDDGC5, features a modification of the amino acid from V to F at position 160.
+The protein's natural variant, known as in MDDGC5;, features a modification of the amino acid from Y to C at position 182.
+The protein's natural variant, known as in MDDGB5, features a modification of the amino acid from P to T at position 217.
+The protein's natural variant, known as in MDDGB5; severe form; brain involvement; intellectual disability and cerebellar cysts on cranial MRI; affects tetramer assembly; decreases the ribitol 5-phosphate transferase activity of about 95%.;, features a modification of the amino acid from S to R at position 221.
+The protein's natural variant, known as in MDDGC5; reduced secretion to the medium; localizes mainly to the Golgi apparatus; affects tetramer assembly; decreases the ribitol-5-phosphate transferase activity of about 50%.;, features a modification of the amino acid from L to I at position 276.
+The protein's natural variant, known as in MDDGC5, features a modification of the amino acid from T to I at position 293.
+The protein's natural variant, known as in MDDGC5;, features a modification of the amino acid from V to A at position 300.
+The protein's natural variant, known as in MDDGC5; unknown pathological significance;, features a modification of the amino acid from V to M at position 300.
+The protein's natural variant, known as in MDDGC5 and MDDGA5; muscle-eye-brain disease, decrease in ribitol-5-phosphate transferase activity.;, features a modification of the amino acid from Y to N at position 307.
+The protein's natural variant, known as in MDDGB5;, features a modification of the amino acid from Y to C at position 309.
+The protein's natural variant, known as in MDDGC5, features a modification of the amino acid from R to C at position 312.
+The protein's natural variant, known as in MDDGC5;, features a modification of the amino acid from T to M at position 314.
+The protein's natural variant, known as in MDDGB5; severe form; brain involvement; intellectual disability and cerebellar cysts on cranial MRI, features a modification of the amino acid from P to T at position 315.
+The protein's natural variant, known as in MDDGB5 and MDDGC5;, features a modification of the amino acid from P to R at position 316.
+The protein's natural variant, known as in MDDGC5;, features a modification of the amino acid from P to S at position 316.
+The protein's natural variant, known as in MDDGA5; severe Walker-Warburg syndrome;, features a modification of the amino acid from C to Y at position 318.
+The protein's natural variant, known as in MDDGB5, features a modification of the amino acid from Y to S at position 328.
+The protein's natural variant, known as in MDDGB5, features a modification of the amino acid from R to H at position 339.
+The protein's natural variant, known as in MDDGC5;, features a modification of the amino acid from R to L at position 339.
+The protein's natural variant, known as in MDDGC5; unknown pathological significance;, features a modification of the amino acid from P to L at position 358.
+The protein's natural variant, known as in MDDGC5;, features a modification of the amino acid from D to N at position 360.
+The protein's natural variant, known as in MDDGB5;, features a modification of the amino acid from D to N at position 401.
+The protein's natural variant, known as in MDDGB5; severe form; brain involvement; intellectual disability and cerebellar cysts on cranial MRI;, features a modification of the amino acid from V to L at position 405.
+The protein's natural variant, known as in MDDGB5; strongly reduced secretion to the medium; localizes mainly to the ER compartment;, features a modification of the amino acid from P to L at position 448.
+The protein's natural variant, known as in MDDGB5; severe form; brain involvement; intellectual disability and cerebellar cysts on cranial MRI;, features a modification of the amino acid from A to D at position 455.
+The protein's natural variant, known as in MDDGC5;, features a modification of the amino acid from P to S at position 462.
+The protein's natural variant, known as in MDDGB5;, features a modification of the amino acid from N to D at position 463.
+The protein's natural variant, known as in MDDGB5;, features a modification of the amino acid from Y to S at position 465.
+The protein's natural variant, known as in cataract, features a modification of the amino acid from R to W at position 340.
+The protein's natural variant, known as in XP-C; severe; does not affect interaction with KAT2A and transcription coactivator activity in absence of DNA damage;, features a modification of the amino acid from P to H at position 334.
+The protein's natural variant, known as in XP-C; diminishes repair activity and impairs DNA binding, features a modification of the amino acid from W to S at position 690.
+The protein's natural variant, known as in XP-C; mild, features a modification of the amino acid from V to VV at position 697.
+The protein's natural variant, known as in strain: L2/434/Bu, features a modification of the amino acid from A to V at position 190.
+The protein's natural variant, known as in SPG57; defective self-assembly into an oligomeric complex; impaired interaction with PDCD6; causes mitochondrial fragmentation;, features a modification of the amino acid from R to C at position 106.
+The protein's natural variant, known as in SPG57; causes mitochondrial fragmentation;, features a modification of the amino acid from R to H at position 106.
+The protein's natural variant, known as in SPG57; unknown pathological significance, features a modification of the amino acid from R to P at position 107.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from A to S at position 149.
+The protein's natural variant, known as in HMSNO; does not affect interaction with PDCD6;, features a modification of the amino acid from P to L at position 285.
+The protein's natural variant, known as in LEC4; loss of activity, features a modification of the amino acid from DIINGVQEKCVLPPMDGYPHC to VQHPNSIGWCCPHLEWVFPVS at position 155.
+The protein's natural variant, known as in LEC4A; loss of activity, features a modification of the amino acid from L to R at position 188.
+The protein's natural variant, known as found in a patient with congenital hyperinsulinism; markedly decreases transporter activity;, features a modification of the amino acid from A to G at position 268.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from V to A at position 43.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from P to L at position 58.
+The protein's natural variant, known as in a pancreatic ductal adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from R to Q at position 408.
+The protein's natural variant, known as in SQORD; severely decreased sulfide:quinone oxidoreductase activity; severely reduced protein levels in patient cells, features a modification of the amino acid from E to K at position 213.
+The protein's natural variant, known as found in individuals with para-Bombay phenotype; allele H4;, features a modification of the amino acid from D to Y at position 148.
+The protein's natural variant, known as found in individuals with Bombay phenotype, features a modification of the amino acid from Y to C at position 154.
+The protein's natural variant, known as found in individuals with para-Bombay phenotype; allele H5;, features a modification of the amino acid from Y to H at position 154.
+The protein's natural variant, known as found in individuals with para-Bombay phenotype;, features a modification of the amino acid from L to H at position 164.
+The protein's natural variant, known as found in individuals with Bombay phenotype, features a modification of the amino acid from W to C at position 171.
+The protein's natural variant, known as found in individuals with para-Bombay phenotype; allele H3;, features a modification of the amino acid from Y to H at position 241.
+The protein's natural variant, known as found in individuals with Bombay phenotype;, features a modification of the amino acid from L to R at position 242.
+The protein's natural variant, known as found in individuals with Bombay phenotype, features a modification of the amino acid from V to E at position 259.
+The protein's natural variant, known as found in individuals with Bombay phenotype, features a modification of the amino acid from A to V at position 315.
+The protein's natural variant, known as found in individuals with para-Bombay phenotype; allele H5;, features a modification of the amino acid from E to K at position 348.
+The protein's natural variant, known as found in individuals with Bombay phenotype;, features a modification of the amino acid from W to C at position 349.
+The protein's natural variant, known as found in a patient with autism spectrum disorder and no epileptic seizures; unknown pathological significance, features a modification of the amino acid from G to R at position 47.
+The protein's natural variant, known as in EPILX2, features a modification of the amino acid from T to M at position 166.
+The protein's natural variant, known as in EPILX2; unknown pathological significance, features a modification of the amino acid from Q to L at position 242.
+The protein's natural variant, known as in EPILX2; unknown pathological significance, features a modification of the amino acid from T to M at position 336.
+The protein's natural variant, known as in EPILX2, features a modification of the amino acid from Y to C at position 474.
+The protein's natural variant, known as in IMD100; results in increased 2'-5'-oligoadenylate synthetase activity leading to increased RNase L-mediated cellular RNA degradation, translational arrest and apoptosis, features a modification of the amino acid from A to V at position 76.
+The protein's natural variant, known as in IMD100; results in increased 2'-5'-oligoadenylate synthetase activity leading to increased RNase L-mediated cellular RNA degradation, translational arrest and apoptosis, features a modification of the amino acid from C to Y at position 109.
+The protein's natural variant, known as in IMD100; results in increased 2'-5'-oligoadenylate synthetase activity leading to increased RNase L-mediated cellular RNA degradation, translational arrest and apoptosis, features a modification of the amino acid from V to G at position 121.
+The protein's natural variant, known as in IMD100; results in increased 2'-5'-oligoadenylate synthetase activity leading to increased RNase L-mediated cellular RNA degradation, translational arrest and apoptosis, features a modification of the amino acid from L to V at position 198.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from G to V at position 346.
+The protein's natural variant, known as in CMTDIF; the mutant protein has impaired bradykinin-induced G-protein-coupled receptor intracellular signaling compared to the wild-type protein;, features a modification of the amino acid from G to D at position 53.
+The protein's natural variant, known as in CMTDIF; the mutant protein has impaired bradykinin-induced G-protein-coupled receptor intracellular signaling compared to the wild-type protein;, features a modification of the amino acid from K to E at position 89.
+The protein's natural variant, known as in CMS2A;, features a modification of the amino acid from L to M at position 285.
+The protein's natural variant, known as in CMS2A; slow-channel mutation; increases gating equilibrium constant by 33-fold, owing to increased opening rate and decreased closing rate; no effect on the choline dissociation rate constant, features a modification of the amino acid from V to A at position 289.
+The protein's natural variant, known as in CMS2A;, features a modification of the amino acid from V to M at position 289.
+The natural variant of this protein is characterized by an amino acid alteration from S to C at position 168.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from A to E at position 42.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from V to M at position 154.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from E to D at position 317.
+The protein's natural variant, known as in CLCD1, features a modification of the amino acid from Q to L at position 53.
+The protein's natural variant, known as in CLCD1; the patient also shows brachydactyly of hands and feet, features a modification of the amino acid from A to AAAAAAAAAAA at position 84.
+The protein's natural variant, known as in CLCD1; unchanged subcellular localization; decreased transactivation activity, features a modification of the amino acid from L to R at position 113.
+The protein's natural variant, known as in CLCD1, features a modification of the amino acid from S to N at position 118.
+The protein's natural variant, known as in CLCD1, features a modification of the amino acid from S to R at position 118.
+The protein's natural variant, known as in CLCD1, features a modification of the amino acid from F to C at position 121.
+The protein's natural variant, known as in CLCD1, features a modification of the amino acid from C to R at position 123.
+The protein's natural variant, known as in CLCD1, features a modification of the amino acid from R to C at position 131.
+The protein's natural variant, known as in CLCD1, features a modification of the amino acid from R to G at position 131.
+The protein's natural variant, known as in CLCD1, features a modification of the amino acid from R to S at position 131.
+The protein's natural variant, known as in CLCD1, features a modification of the amino acid from L to P at position 136.
+The protein's natural variant, known as in CLCD1, features a modification of the amino acid from V to D at position 156.
+The protein's natural variant, known as in CLCD1, features a modification of the amino acid from V to G at position 156.
+The protein's natural variant, known as in CLCD1;, features a modification of the amino acid from R to P at position 169.
+The protein's natural variant, known as in CLCD1;, features a modification of the amino acid from R to Q at position 169.
+The protein's natural variant, known as in CLCD1, features a modification of the amino acid from M to K at position 175.
+The protein's natural variant, known as in CLCD1; abolishes DNA binding;, features a modification of the amino acid from M to R at position 175.
+The protein's natural variant, known as in CLCD1;, features a modification of the amino acid from M to V at position 175.
+The protein's natural variant, known as in CLCD1; unchanged subcellular localization; decreased transactivation activity, features a modification of the amino acid from R to T at position 186.
+The protein's natural variant, known as in CLCD1, features a modification of the amino acid from F to S at position 187.
+The protein's natural variant, known as in CLCD1; abolishes DNA binding;, features a modification of the amino acid from R to Q at position 190.
+The protein's natural variant, known as in CLCD1; has severely impaired DNA binding and transactivation, features a modification of the amino acid from R to W at position 190.
+The protein's natural variant, known as in CLCD1; abolishes DNA binding;, features a modification of the amino acid from S to N at position 191.
+The protein's natural variant, known as in CLCD1, features a modification of the amino acid from R to C at position 193.
+The protein's natural variant, known as in CLCD1; unchanged subcellular localization; decreased transactivation activity, features a modification of the amino acid from R to G at position 193.
+The protein's natural variant, known as in CLCD1, features a modification of the amino acid from R to Q at position 193.
+The protein's natural variant, known as in CLCD1; retains heterodimerization activity together with a trace potential for DNA binding; retains a low but still substantial transactivation activity, features a modification of the amino acid from F to S at position 197.
+The protein's natural variant, known as in CLCD1; abolishes DNA binding, features a modification of the amino acid from L to F at position 199.
+The protein's natural variant, known as in CLCD1; mild; associated also with isolated dental anomalies; normal DNA binding;, features a modification of the amino acid from T to A at position 200.
+The protein's natural variant, known as in CLCD1, features a modification of the amino acid from T to I at position 200.
+The protein's natural variant, known as in CLCD1, features a modification of the amino acid from I to K at position 201.
+The protein's natural variant, known as in CLCD1, features a modification of the amino acid from T to R at position 205.
+The protein's natural variant, known as in CLCD1, features a modification of the amino acid from Q to H at position 209.
+The protein's natural variant, known as in CLCD1, features a modification of the amino acid from Q to R at position 209.
+The protein's natural variant, known as in CLCD1, features a modification of the amino acid from A to P at position 211.
+The protein's natural variant, known as in CLCD1, features a modification of the amino acid from K to E at position 218.
+The protein's natural variant, known as in CLCD1; has severely impaired DNA binding and transactivation;, features a modification of the amino acid from K to N at position 218.
+The protein's natural variant, known as in CLCD1, features a modification of the amino acid from K to Q at position 218.
+The protein's natural variant, known as in CLCD1; has severely impaired DNA binding and transactivation, features a modification of the amino acid from T to I at position 220.
+The protein's natural variant, known as in CLCD1, features a modification of the amino acid from R to L at position 225.
+The protein's natural variant, known as in CLCD1; interferes with nuclear localization; abolishes DNA binding;, features a modification of the amino acid from R to Q at position 225.
+The protein's natural variant, known as in CLCD1; interferes with nuclear localization; has severely impaired DNA binding and transactivation;, features a modification of the amino acid from R to W at position 225.
+The protein's natural variant, known as in CLCD1, features a modification of the amino acid from R to G at position 228.
+The protein's natural variant, known as in CLCD1, features a modification of the amino acid from K to R at position 233.
+The protein's natural variant, known as in CLCD1, features a modification of the amino acid from D to N at position 287.
+The protein's natural variant, known as in CLCD1, features a modification of the amino acid from A to V at position 362.
+The protein's natural variant, known as in CLCD1, features a modification of the amino acid from T to I at position 420.
+The protein's natural variant, known as in CLCD1, features a modification of the amino acid from T to N at position 420.
+The protein's natural variant, known as in COLACD;, features a modification of the amino acid from Q to H at position 268.
+The protein's natural variant, known as in COLACD;, features a modification of the amino acid from G to S at position 1363.
+The natural variant of this protein is characterized by an amino acid alteration from S to F at position 209.
+The protein's natural variant, known as in strain: B, features a modification of the amino acid from F to C at position 51.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation, features a modification of the amino acid from R to L at position 256.
+The protein's natural variant, known as in strain: Isolate BEMA8, features a modification of the amino acid from K to N at position 19.
+The protein's natural variant, known as in RPIAD;, features a modification of the amino acid from A to V at position 135.
+The natural variant of this protein is characterized by an amino acid alteration from S to C at position 333.
+The protein's natural variant, known as in strain: CCUG 18241, features a modification of the amino acid from SR to GQ at position 129.
+The protein's natural variant, known as in strain: CCUG 18241, features a modification of the amino acid from V to I at position 132.
+The protein's natural variant, known as found in a cutaneous malignant melanoma sample; somatic mutation, features a modification of the amino acid from P to L at position 57.
+The protein's natural variant, known as in FESD;, features a modification of the amino acid from P to R at position 79.
+The protein's natural variant, known as found in a patient with autism spectrum disorder; unknown pathological significance, features a modification of the amino acid from T to I at position 143.
+The protein's natural variant, known as found in a cutaneous malignant melanoma sample; somatic mutation; also found in a patient with benign epilepsy with centrotemporal spike;, features a modification of the amino acid from F to I at position 183.
+The protein's natural variant, known as in FESD; unknown pathological significance, features a modification of the amino acid from I to S at position 184.
+The protein's natural variant, known as found in a patient with schizophrenia; unknown pathological significance;, features a modification of the amino acid from T to N at position 189.
+The protein's natural variant, known as in FESD; unknown pathological significance, features a modification of the amino acid from C to Y at position 231.
+The protein's natural variant, known as in FESD; results in reduced high-affinity zinc mediated inhibition, features a modification of the amino acid from A to V at position 243.
+The protein's natural variant, known as found in a cutaneous malignant melanoma sample; somatic mutation;, features a modification of the amino acid from D to N at position 252.
+The natural variant of this protein is characterized by an amino acid alteration from K to E at position 270.
+The protein's natural variant, known as found in a cutaneous malignant melanoma sample; somatic mutation;, features a modification of the amino acid from S to F at position 278.
+The protein's natural variant, known as in FESD;, features a modification of the amino acid from A to V at position 290.
+The protein's natural variant, known as in FESD; unknown pathological significance;, features a modification of the amino acid from G to S at position 295.
+The protein's natural variant, known as found in a cutaneous malignant melanoma sample, features a modification of the amino acid from S to F at position 349.
+The protein's natural variant, known as in FESD;, features a modification of the amino acid from R to W at position 370.
+The protein's natural variant, known as found in a cutaneous malignant melanoma sample; somatic mutation;, features a modification of the amino acid from E to K at position 371.
+The protein's natural variant, known as found in a cutaneous malignant melanoma sample; somatic mutation, features a modification of the amino acid from E to K at position 373.
+The protein's natural variant, known as found in a patient with neonatal onset epileptic encephalopathy; unknown pathological significance;, features a modification of the amino acid from N to D at position 380.
+The protein's natural variant, known as in FESD; decreased protein abundance; loss of localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by increased glutamate potency and decreased glycine potency;, features a modification of the amino acid from C to R at position 436.
+The protein's natural variant, known as found in a cutaneous malignant melanoma sample; somatic mutation;, features a modification of the amino acid from G to E at position 449.
+The protein's natural variant, known as no effect on localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by increased glutamate potency;, features a modification of the amino acid from V to M at position 452.
+The protein's natural variant, known as found in a cutaneous malignant melanoma sample; somatic mutation, features a modification of the amino acid from F to S at position 459.
+The protein's natural variant, known as in FESD; decreased protein abundance; decreased localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by decreased glutamate potency, features a modification of the amino acid from G to R at position 483.
+The protein's natural variant, known as in FESD; decreased protein abundance; decreased localization to the cell membrane; no significant effect on calcium ion transmembrane import into cytosol;, features a modification of the amino acid from R to W at position 504.
+The protein's natural variant, known as in FESD; no effect on localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by increased glutamate potency;, features a modification of the amino acid from V to A at position 506.
+The protein's natural variant, known as in FESD; decreased protein abundance; decreased localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by affected receptor kinetics;, features a modification of the amino acid from R to H at position 518.
+The protein's natural variant, known as in FESD; decreased protein abundance; decreased localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by affected receptor kinetics;, features a modification of the amino acid from T to M at position 531.
+The protein's natural variant, known as in FESD; no effect on localization to the cell membrane; loss of glutamate-gated calcium ion channel activity, features a modification of the amino acid from A to T at position 548.
+The protein's natural variant, known as in FESD; no effect on localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by increased glutamate and glycine potency with delay in rise time and slower deactivation time course;, features a modification of the amino acid from P to R at position 552.
+The natural variant of this protein is characterized by an amino acid alteration from F to S at position 576.
+The protein's natural variant, known as found in a cutaneous malignant melanoma sample; somatic mutation;, features a modification of the amino acid from H to R at position 595.
+The protein's natural variant, known as found in a cutaneous malignant melanoma sample; somatic mutation, features a modification of the amino acid from S to F at position 598.
+The protein's natural variant, known as in FESD; the mutant receptor has decreased calcium permeability; shows a dominant-negative effect;, features a modification of the amino acid from N to K at position 615.
+The protein's natural variant, known as in FESD;, features a modification of the amino acid from L to V at position 649.
+The protein's natural variant, known as in FESD; affects receptor kinetics;, features a modification of the amino acid from F to V at position 652.
+The protein's natural variant, known as found in a cutaneous malignant melanoma sample; somatic mutation, features a modification of the amino acid from M to I at position 653.
+The protein's natural variant, known as in FESD; no effect on localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by increased glutamate and glycine potency, features a modification of the amino acid from K to N at position 669.
+The protein's natural variant, known as in FESD; decreased protein abundance; decreased localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by decreased glutamate potency;, features a modification of the amino acid from V to G at position 685.
+The protein's natural variant, known as in FESD; decreased protein abundance; decreased localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by decreased glutamate potency and decreased open probability, features a modification of the amino acid from I to T at position 694.
+The protein's natural variant, known as in FESD; no effect on localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by increased glutamate potency and decreased open probability;, features a modification of the amino acid from P to S at position 699.
+The protein's natural variant, known as in FESD; decreased localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by decreased glutamate potency and decreased open probability, features a modification of the amino acid from M to V at position 705.
+The protein's natural variant, known as found in a cutaneous malignant melanoma sample; somatic mutation;, features a modification of the amino acid from G to E at position 712.
+The protein's natural variant, known as in FESD; decreased protein abundance; no effect on localization to the cell membrane; no significant effect on calcium ion transmembrane import into cytosol, features a modification of the amino acid from E to K at position 714.
+The protein's natural variant, known as in FESD; unknown pathological significance;, features a modification of the amino acid from A to D at position 716.
+The protein's natural variant, known as in FESD; decreased protein abundance; decreased localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by decreased glutamate potency;, features a modification of the amino acid from A to T at position 716.
+The protein's natural variant, known as in FESD; decreased protein abundance; decreased localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by decreased glutamate potency and decreased open probability;, features a modification of the amino acid from A to T at position 727.
+The protein's natural variant, known as in FESD; decreased protein abundance; decreased localization to the cell membrane; decreased glutamate-gated calcium ion channel activity characterized by drastically decreased glutamate agonist potency, decreased glycine agonist potency, reduced amplitude of current response, shortened synaptic-like response time course, decreased channel open probability and enhanced sensitivity to negative allosteric modulators;, features a modification of the amino acid from D to N at position 731.
+The protein's natural variant, known as in FESD; no effect on localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by decreased glutamate potency, features a modification of the amino acid from V to L at position 734.
+The protein's natural variant, known as found in a cutaneous malignant melanoma sample; somatic mutation, features a modification of the amino acid from G to W at position 740.
+The protein's natural variant, known as found in a cutaneous malignant melanoma sample, features a modification of the amino acid from G to A at position 762.
+The protein's natural variant, known as in FESD; decreased protein abundance; decreased localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by decreased glutamate potency and decreased open probability, features a modification of the amino acid from K to E at position 772.
+The protein's natural variant, known as in FESD; increase in receptor response to agonists; decrease in the actions of endogenous negative modulators; increase in channel open probability; prolonged deactivation time course, features a modification of the amino acid from L to M at position 812.
+The protein's natural variant, known as in FESD; unknown pathological significance;, features a modification of the amino acid from I to T at position 814.
+The protein's natural variant, known as in FESD; gain-of-function characterized by enhanced agonist potency, reduced sensitivity to endogenous negative inhibitors, prolonged synaptic-like response time course, increased single-channel mean open time and increased channel open probability;, features a modification of the amino acid from M to V at position 817.
+The protein's natural variant, known as found in a patient with autism; unknown pathological significance;, features a modification of the amino acid from D to N at position 884.
+The protein's natural variant, known as found in a cutaneous malignant melanoma sample; somatic mutation, features a modification of the amino acid from G to E at position 889.
+The protein's natural variant, known as in FESD;, features a modification of the amino acid from I to F at position 904.
+The protein's natural variant, known as found in a cutaneous malignant melanoma sample; somatic mutation, features a modification of the amino acid from R to K at position 920.
+The protein's natural variant, known as found in a cutaneous malignant melanoma sample; somatic mutation;, features a modification of the amino acid from S to F at position 929.
+The protein's natural variant, known as in FESD; unknown pathological significance;, features a modification of the amino acid from D to N at position 933.
+The protein's natural variant, known as found in a cutaneous malignant melanoma sample; somatic mutation;, features a modification of the amino acid from E to K at position 962.
+The protein's natural variant, known as probable disease-associated variant found in a patient with schizophrenia, features a modification of the amino acid from A to T at position 968.
+The protein's natural variant, known as in FESD;, features a modification of the amino acid from N to S at position 976.
+The protein's natural variant, known as found in a patient with neonatal onset epileptic encephalopathy; unknown pathological significance;, features a modification of the amino acid from N to S at position 989.
+The protein's natural variant, known as found in a patient with schizophrenia; unknown pathological significance;, features a modification of the amino acid from V to M at position 998.
+The protein's natural variant, known as found in a cutaneous malignant melanoma sample; somatic mutation, features a modification of the amino acid from E to K at position 1073.
+The protein's natural variant, known as found in a cutaneous malignant melanoma sample; somatic mutation;, features a modification of the amino acid from P to L at position 1074.
+The protein's natural variant, known as found in a cutaneous malignant melanoma sample, features a modification of the amino acid from P to L at position 1132.
+The protein's natural variant, known as found in a cutaneous malignant melanoma sample, features a modification of the amino acid from P to S at position 1133.
+The protein's natural variant, known as found in a cutaneous malignant melanoma sample; somatic mutation;, features a modification of the amino acid from D to N at position 1153.
+The protein's natural variant, known as found in a cutaneous malignant melanoma sample; somatic mutation;, features a modification of the amino acid from E to K at position 1175.
+The protein's natural variant, known as found in a patient with schizophrenia; unknown pathological significance;, features a modification of the amino acid from T to S at position 1229.
+The protein's natural variant, known as in FESD, features a modification of the amino acid from D to N at position 1251.
+The protein's natural variant, known as found in a patient with continuous spike-wave discharges during slow-wave sleep; also found in a patient with drug-resistant focal epilepsy; also found in a cutaneous malignant melanoma sample as somatic mutation; unknown pathological significance;, features a modification of the amino acid from A to G at position 1276.
+The protein's natural variant, known as found in a cutaneous malignant melanoma sample; somatic mutation;, features a modification of the amino acid from R to K at position 1285.
+The protein's natural variant, known as found in a cutaneous malignant melanoma sample; somatic mutation;, features a modification of the amino acid from R to W at position 1318.
+The protein's natural variant, known as found in a cutaneous malignant melanoma sample; somatic mutation, features a modification of the amino acid from P to L at position 1366.
+The protein's natural variant, known as found in a cutaneous malignant melanoma sample; somatic mutation, features a modification of the amino acid from D to N at position 1421.
+The protein's natural variant, known as found in a cutaneous malignant melanoma sample; somatic mutation;, features a modification of the amino acid from S to L at position 1425.
+The protein's natural variant, known as found in a cutaneous malignant melanoma sample; somatic mutation;, features a modification of the amino acid from E to K at position 1426.
+The protein's natural variant, known as found in a cutaneous malignant melanoma sample; somatic mutation, features a modification of the amino acid from S to C at position 1462.
+The protein's natural variant, known as in PVNH1;, features a modification of the amino acid from A to G at position 39.
+The protein's natural variant, known as in PVNH1;, features a modification of the amino acid from E to V at position 82.
+The protein's natural variant, known as in PVNH1, features a modification of the amino acid from M to V at position 102.
+The protein's natural variant, known as in PVNH1;, features a modification of the amino acid from A to V at position 128.
+The protein's natural variant, known as in PVNH1, features a modification of the amino acid from S to F at position 149.
+The protein's natural variant, known as in OPD2;, features a modification of the amino acid from Q to P at position 170.
+The protein's natural variant, known as in OPD1, features a modification of the amino acid from L to F at position 172.
+The protein's natural variant, known as in OPD2; unknown pathological significance, features a modification of the amino acid from N to S at position 187.
+The protein's natural variant, known as in OPD2, features a modification of the amino acid from R to G at position 196.
+The protein's natural variant, known as in OPD1;, features a modification of the amino acid from R to W at position 196.
+The protein's natural variant, known as in OPD2, features a modification of the amino acid from A to S at position 200.
+The protein's natural variant, known as in OPD1;, features a modification of the amino acid from D to Y at position 203.
+The protein's natural variant, known as in OPD1;, features a modification of the amino acid from P to L at position 207.
+The protein's natural variant, known as in OPD2;, features a modification of the amino acid from C to F at position 210.
+The protein's natural variant, known as in OPD2;, features a modification of the amino acid from E to K at position 254.
+The protein's natural variant, known as in OPD1; unknown pathological significance, features a modification of the amino acid from A to T at position 267.
+The protein's natural variant, known as in OPD2, features a modification of the amino acid from A to P at position 273.
+The protein's natural variant, known as in CVDPX;, features a modification of the amino acid from G to R at position 288.
+The protein's natural variant, known as in OPD2;, features a modification of the amino acid from T to K at position 555.
+The protein's natural variant, known as found in a child with developmental disabilities; unknown pathological significance, features a modification of the amino acid from V to L at position 606.
+The protein's natural variant, known as in CVDPX;, features a modification of the amino acid from P to Q at position 637.
+The protein's natural variant, known as in PVNH1;, features a modification of the amino acid from L to F at position 656.
+The protein's natural variant, known as in CVDPX;, features a modification of the amino acid from V to D at position 711.
+The protein's natural variant, known as in OPD1; unknown pathological significance, features a modification of the amino acid from V to D at position 804.
+The protein's natural variant, known as in FMD1; unknown pathological significance, features a modification of the amino acid from D to V at position 1142.
+The protein's natural variant, known as in FMD1; does not inhibit interaction with MIS18BP1;, features a modification of the amino acid from D to A at position 1159.
+The protein's natural variant, known as in MNS; unknown pathological significance, features a modification of the amino acid from V to L at position 1163.
+The protein's natural variant, known as in MNS;, features a modification of the amino acid from D to E at position 1184.
+The protein's natural variant, known as in FMD1;, features a modification of the amino acid from S to L at position 1186.
+The protein's natural variant, known as in MNS; does not inhibit interaction with MIS18BP1;, features a modification of the amino acid from A to T at position 1188.
+The protein's natural variant, known as in MNS; does not inhibit interaction with MIS18BP1;, features a modification of the amino acid from S to L at position 1199.
+The protein's natural variant, known as in FGS2;, features a modification of the amino acid from P to L at position 1291.
+The protein's natural variant, known as in OPD2, features a modification of the amino acid from C to F at position 1645.
+The protein's natural variant, known as in FMD1;, features a modification of the amino acid from G to C at position 1728.
+The protein's natural variant, known as probable disease-associated variant found in a patient with macrothrombocytopenia;, features a modification of the amino acid from E to K at position 1803.
+The protein's natural variant, known as in FMD1; unknown pathological significance, features a modification of the amino acid from H to R at position 1840.
+The protein's natural variant, known as in OPD1; unknown pathological significance;, features a modification of the amino acid from R to H at position 2391.
+The protein's natural variant, known as in SBIDDS;, features a modification of the amino acid from R to T at position 32.
+The protein's natural variant, known as in SBIDDS;, features a modification of the amino acid from R to G at position 387.
+The protein's natural variant, known as in SBIDDS;, features a modification of the amino acid from W to R at position 494.
+The natural variant of this protein is characterized by an amino acid alteration from A to V at position 27.
+The protein's natural variant, known as in APLID;, features a modification of the amino acid from V to M at position 411.
+The protein's natural variant, known as in SCAR31; results in decreased LC3-I lipidation to form LC3-II, features a modification of the amino acid from P to T at position 234.
+The protein's natural variant, known as in SCAR31; unknown pathological significance, features a modification of the amino acid from Q to R at position 261.
+The protein's natural variant, known as in SCAR31; results in severely decreased LC3-I lipidation to form LC3-II, features a modification of the amino acid from G to D at position 511.
+The protein's natural variant, known as in SCAR31; in homozygous patient cells it results in diminished autophagic flux, features a modification of the amino acid from L to P at position 512.
+The protein's natural variant, known as in SCAR31; results in decreased LC3-I lipidation to form LC3-II, features a modification of the amino acid from R to H at position 576.
+The protein's natural variant, known as in SCAR31; results in severely decreased LC3-I lipidation to form LC3-II, features a modification of the amino acid from V to M at position 588.
+The protein's natural variant, known as in SCAR31; results in decreased LC3-I lipidation to form LC3-II, features a modification of the amino acid from H to Y at position 624.
+The protein's natural variant, known as associated with Ala-735; affects KIBRA lipid-binding specificity showing stronger interactions with PI(4)P and PI(5)P;, features a modification of the amino acid from M to I at position 734.
+The protein's natural variant, known as associated with Ile-734; affects KIBRA lipid-binding specificity showing stronger interactions with PI(4)P and PI(5)P;, features a modification of the amino acid from S to A at position 735.
+The protein's natural variant, known as in strain: Isolate B9 and Isolate D1, features a modification of the amino acid from F to S at position 167.
+The protein's natural variant, known as in strain: Isolate B9 and Isolate D1, features a modification of the amino acid from IF to L at position 232.
+The protein's natural variant, known as in strain: Isolate B9 and Isolate D1, features a modification of the amino acid from T to I at position 240.
+The natural variant of this protein is characterized by an amino acid alteration from L to S at position 48.
+The protein's natural variant, known as in DYTOABG; probably decreased protein abundance;, features a modification of the amino acid from G to E at position 232.
+The protein's natural variant, known as in DYTOABG;, features a modification of the amino acid from R to W at position 258.
+The protein's natural variant, known as in DYTOABG;, features a modification of the amino acid from Y to C at position 285.
+The protein's natural variant, known as in strain: C57BL/6, features a modification of the amino acid from R to Q at position 1051.
+The protein's natural variant, known as in CMS21;, features a modification of the amino acid from G to A at position 186.
+The protein's natural variant, known as in CMS21;, features a modification of the amino acid from D to H at position 398.
+The protein's natural variant, known as in strain: MAR001, features a modification of the amino acid from I to T at position 489.
+The protein's natural variant, known as in strain: MAR001, features a modification of the amino acid from V to A at position 497.
+The natural variant of this protein is characterized by an amino acid alteration from L to V at position 106.
+The natural variant of this protein is characterized by an amino acid alteration from Q to S at position 115.
+The protein's natural variant, known as in strain: cv. Bus-1, features a modification of the amino acid from S to P at position 3.
+The protein's natural variant, known as in strain: cv. Ag-0, cv. Bus-1, cv. Dra-0, cv. Hiroshima and cv. Kas-1, features a modification of the amino acid from T to P at position 5.
+The protein's natural variant, known as in strain: cv. Bus-1, features a modification of the amino acid from A to V at position 36.
+The protein's natural variant, known as in strain: cv. Bl-1 and cv. In-0, features a modification of the amino acid from S to A at position 73.
+The protein's natural variant, known as in strain: cv. Bl-1 and cv. In-0, features a modification of the amino acid from S to A at position 95.
+The protein's natural variant, known as in strain: cv. Bus-1 and cv. Kas-1, features a modification of the amino acid from V to I at position 99.
+The protein's natural variant, known as in strain: cv. Hiroshima, features a modification of the amino acid from K to E at position 105.
+The protein's natural variant, known as in strain: cv. Bl-1 and cv. In-0, features a modification of the amino acid from M to K at position 114.
+The protein's natural variant, known as in strain: cv. Nok-4, features a modification of the amino acid from E to D at position 119.
+The protein's natural variant, known as in strain: cv. Bus-1, features a modification of the amino acid from N to S at position 198.
+The protein's natural variant, known as in strain: cv. Cvi-0, features a modification of the amino acid from M to T at position 295.
+The protein's natural variant, known as in strain: cv. WS-0, features a modification of the amino acid from I to T at position 355.
+The protein's natural variant, known as in strain: cv. Pog-0, features a modification of the amino acid from L to F at position 431.
+The protein's natural variant, known as in strain: cv. In-0, features a modification of the amino acid from M to I at position 432.
+The protein's natural variant, known as in strain: cv. Ost-0, features a modification of the amino acid from H to Q at position 528.
+The protein's natural variant, known as in strain: Tai 255.1, features a modification of the amino acid from AA to TS at position 114.
+The protein's natural variant, known as in strain: DK20, features a modification of the amino acid from SL to FT at position 34.
+The protein's natural variant, known as in strain: DK20, features a modification of the amino acid from I to L at position 121.
+The protein's natural variant, known as in strain: DK20, features a modification of the amino acid from V to A at position 132.
+The protein's natural variant, known as in strain: DK20, features a modification of the amino acid from N to S at position 458.
+The protein's natural variant, known as in a hypereosinophilic syndrome sample; does not lead to constitutive kinase activation, features a modification of the amino acid from R to G at position 481.
+The protein's natural variant, known as in a hypereosinophilic syndrome sample; does not lead to constitutive kinase activation, features a modification of the amino acid from L to P at position 507.
+The protein's natural variant, known as in GISTPS; increased platelet-derived growth factor alpha-receptor activity; constitutively activated kinase;, features a modification of the amino acid from Y to C at position 555.
+The protein's natural variant, known as in a GIST sample; constitutively activated kinase;, features a modification of the amino acid from V to D at position 561.
+The protein's natural variant, known as in a hypereosinophilic syndrome sample; does not lead to constitutive kinase activation, features a modification of the amino acid from I to M at position 562.
+The protein's natural variant, known as in a hypereosinophilic syndrome sample; does not lead to constitutive kinase activation, features a modification of the amino acid from H to R at position 570.
+The protein's natural variant, known as in a hypereosinophilic syndrome sample; constitutively activated kinase, features a modification of the amino acid from H to Q at position 650.
+The protein's natural variant, known as in GISTPS; unknown pathological significance, features a modification of the amino acid from P to L at position 653.
+The protein's natural variant, known as in GIST sample; constitutively activated kinase;, features a modification of the amino acid from N to K at position 659.
+The protein's natural variant, known as in a hypereosinophilic syndrome sample; constitutively activated kinase, features a modification of the amino acid from N to S at position 659.
+The protein's natural variant, known as in a hypereosinophilic syndrome sample; does not lead to constitutive kinase activation, features a modification of the amino acid from L to P at position 705.
+The protein's natural variant, known as in a hypereosinophilic syndrome sample; constitutively activated kinase, features a modification of the amino acid from R to G at position 748.
+The protein's natural variant, known as in a glioblastoma multiforme sample; somatic mutation, features a modification of the amino acid from G to R at position 829.
+The protein's natural variant, known as in a GIST sample; imatinib resistant, constitutively activated kinase;, features a modification of the amino acid from D to V at position 842.
+The protein's natural variant, known as in a GIST sample; imatinib sensitive, constitutively activated kinase;, features a modification of the amino acid from D to Y at position 842.
+The protein's natural variant, known as in GISTPS; unknown pathological significance;, features a modification of the amino acid from D to Y at position 846.
+The protein's natural variant, known as in GIST, features a modification of the amino acid from Y to C at position 849.
+The protein's natural variant, known as in a hypereosinophilic syndrome sample; constitutively activated kinase, features a modification of the amino acid from Y to S at position 849.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation;, features a modification of the amino acid from E to K at position 996.
+The protein's natural variant, known as in a lung neuroendocrine carcinoma sample; somatic mutation;, features a modification of the amino acid from D to N at position 1071.
+The natural variant of this protein is characterized by an amino acid alteration from P to R at position 13.
+The natural variant of this protein is characterized by an amino acid alteration from A to G at position 16.
+The natural variant of this protein is characterized by an amino acid alteration from R to G at position 17.
+The natural variant of this protein is characterized by an amino acid alteration from S to L at position 25.
+The natural variant of this protein is characterized by an amino acid alteration from K to R at position 28.
+The protein's natural variant, known as in Yt(b) antigen;, features a modification of the amino acid from H to N at position 353.
+The protein's natural variant, known as in strain: 4091-5-8, features a modification of the amino acid from E to G at position 140.
+The protein's natural variant, known as in strain: 4091-5-8, features a modification of the amino acid from L to F at position 398.
+The protein's natural variant, known as in strain: cv. Sah-0, features a modification of the amino acid from M to T at position 3.
+The protein's natural variant, known as no effect on activity; increases secretion; rate of solubilization is 2.5-fold higher than wild-type;, features a modification of the amino acid from P to L at position 1228.
+The protein's natural variant, known as in strain: Petite Havana, allele 2, features a modification of the amino acid from R to G at position 214.
+The protein's natural variant, known as no effect on inhibition of NF-kappa-B activation; no effect on interaction with MYD88;, features a modification of the amino acid from I to V at position 5.
+The protein's natural variant, known as in IMD67; no effect on inhibition of NF-kappa-B complex activation; loss of interaction with MYD88; decreases protein stability;, features a modification of the amino acid from R to C at position 12.
+The protein's natural variant, known as increases inhibition of NF-kappa-B complex activation; decreases interaction with MYD88; decreases protein stability;, features a modification of the amino acid from R to W at position 20.
+The protein's natural variant, known as no effect on inhibition of NF-kappa-B activation; no effect on interaction with MYD88;, features a modification of the amino acid from I to T at position 26.
+The protein's natural variant, known as no effect on inhibition of NF-kappa-B activation; no effect on interaction with MYD88;, features a modification of the amino acid from I to V at position 39.
+The protein's natural variant, known as no effect on inhibition of NF-kappa-B activation; no effect on interaction with MYD88;, features a modification of the amino acid from S to R at position 98.
+The protein's natural variant, known as in IMD67; decreases inhibition of NF-kappa-B complex activation; impairs neutrophil migration and phagocytosis;, features a modification of the amino acid from G to D at position 298.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from F to I at position 60.
+The protein's natural variant, known as in NEDSFF; decreased function in diphthamide biosynthesis shown in a yeast assay system, features a modification of the amino acid from N to S at position 110.
+The protein's natural variant, known as in NEDSFF; results in multisystem abnormalities in a homozygous mouse knockin model; decreased function in diphthamide biosynthesis shown in a yeast assay system, features a modification of the amino acid from H to R at position 260.
+The protein's natural variant, known as in DFNY2; unknown pathological significance; increased protein degradation;, features a modification of the amino acid from D to V at position 69.
+The protein's natural variant, known as in BSS;, features a modification of the amino acid from L to F at position 73.
+The protein's natural variant, known as in BSS;, features a modification of the amino acid from C to R at position 81.
+The protein's natural variant, known as in BSS;, features a modification of the amino acid from L to P at position 145.
+The protein's natural variant, known as in Siba(+);, features a modification of the amino acid from T to M at position 161.
+The protein's natural variant, known as in BSS and BSSA2;, features a modification of the amino acid from A to V at position 172.
+The protein's natural variant, known as in BSS;, features a modification of the amino acid from C to S at position 225.
+The protein's natural variant, known as in VWDP;, features a modification of the amino acid from G to S at position 249.
+The protein's natural variant, known as in VWDP;, features a modification of the amino acid from G to V at position 249.
+The protein's natural variant, known as in VWDP; increased binding to vWF;, features a modification of the amino acid from M to V at position 255.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to W at position 627.
+The natural variant of this protein is characterized by an amino acid alteration from N to G at position 308.
+The protein's natural variant, known as in MT2881, features a modification of the amino acid from S to G at position 165.
+The natural variant of this protein is characterized by an amino acid alteration from D to E at position 78.
+The protein's natural variant, known as in strain: CWL029 and TW-183, features a modification of the amino acid from T to A at position 321.
+The protein's natural variant, known as in DEE24; likely benign variant;, features a modification of the amino acid from G to V at position 47.
+The protein's natural variant, known as in GEFSP10; unknown pathological significance, features a modification of the amino acid from E to A at position 85.
+The protein's natural variant, known as in DEE24; dominant-negative mutation resulting in gain of channel function;, features a modification of the amino acid from S to F at position 100.
+The protein's natural variant, known as in DEE24; unknown pathological significance, features a modification of the amino acid from F to Y at position 143.
+The protein's natural variant, known as in DEE24; affects channel gating properties; the half-activation voltage is shifted to the depolarizing direction; significantly faster activation and slower deactivation kinetics than wild-type channel;, features a modification of the amino acid from M to I at position 153.
+The protein's natural variant, known as in GEFSP10; unknown pathological significance; reduced current density; affects channel gating properties as the half-activation voltage is shifted to the depolarizing direction; neurons expressing mutant channels show increased excitability;, features a modification of the amino acid from L to V at position 157.
+The protein's natural variant, known as in GEFSP10; unknown pathological significance, features a modification of the amino acid from T to R at position 171.
+The protein's natural variant, known as in GEFSP10; unknown pathological significance, features a modification of the amino acid from T to P at position 172.
+The protein's natural variant, known as in GEFSP10; significantly decreased current densities;, features a modification of the amino acid from M to R at position 243.
+The protein's natural variant, known as in GEFSP10; unknown pathological significance, features a modification of the amino acid from T to I at position 260.
+The protein's natural variant, known as in DEE24; unknown pathological significance;, features a modification of the amino acid from K to E at position 261.
+The protein's natural variant, known as found in a patient with infantile-onset epilepsy; unknown pathological significance;, features a modification of the amino acid from S to C at position 264.
+The protein's natural variant, known as in DEE24; dominant-negative mutation resulting in loss of channel currents;, features a modification of the amino acid from S to P at position 272.
+The protein's natural variant, known as found in a patient with childhood focal epilepsy; unknown pathological significance, features a modification of the amino acid from I to T at position 275.
+The protein's natural variant, known as in DEE24; results in a gain of channel function;, features a modification of the amino acid from H to Y at position 279.
+The protein's natural variant, known as in DEE24; dominant-negative mutation resulting in loss of channel currents;, features a modification of the amino acid from R to T at position 297.
+The protein's natural variant, known as in DEE24; absence of hyperpolarization-activated currents; highly reduced amount of protein at the cell membrane;, features a modification of the amino acid from M to L at position 305.
+The protein's natural variant, known as in GEFSP10; decreased current density; voltage-dependence of activation as well as the activation and deactivation kinetics are not altered;, features a modification of the amino acid from C to S at position 329.
+The protein's natural variant, known as found in a patient with intellectual disability and language delay; unknown pathological significance, features a modification of the amino acid from M to R at position 379.
+The protein's natural variant, known as in GEFSP10; affects channel gating properties as the half-activation voltage is shifted to the hyperpolarizing direction, features a modification of the amino acid from G to C at position 391.
+The protein's natural variant, known as in DEE24; results in absence of hyperpolarization-activated currents; reduced amount of protein at the cell membrane;, features a modification of the amino acid from G to D at position 391.
+The protein's natural variant, known as in GEFSP10; affects channel gating properties as the half-activation voltage is shifted to the depolarizing direction; reduced amount of protein at the cell membrane;, features a modification of the amino acid from G to S at position 391.
+The protein's natural variant, known as in DEE24; the half-activation voltage is shifted to the depolarizing direction; reduced amount of protein at the cell membrane, features a modification of the amino acid from I to L at position 397.
+The protein's natural variant, known as in DEE24; results in absence of hyperpolarization-activated currents; reduced amount of protein at the cell membrane, features a modification of the amino acid from S to P at position 399.
+The protein's natural variant, known as in DEE24; results in a gain of channel function;, features a modification of the amino acid from D to H at position 401.
+The protein's natural variant, known as in GEFSP10; results in a depolarizing shift of the half-activation voltage and faster activation kinetics;, features a modification of the amino acid from V to M at position 414.
+The protein's natural variant, known as in GEFSP10; decreased current densities; half-activation voltage is slightly shifted to the hyperpolarizing direction;, features a modification of the amino acid from R to Q at position 590.
+The protein's natural variant, known as in GEFSP10; unknown pathological significance, features a modification of the amino acid from S to Y at position 680.
+The protein's natural variant, known as in GEFSP10; unknown pathological significance;, features a modification of the amino acid from R to G at position 715.
+The protein's natural variant, known as found in a patient with sinus bradychardia; unknown pathological significance; affects channel properties as it results in a negative shift in the threshold voltage of activation and slower activation kinetics compared to the wild-type, features a modification of the amino acid from P to A at position 851.
+The protein's natural variant, known as in strain: T1, features a modification of the amino acid from S to R at position 35.
+The protein's natural variant, known as in strain: T1, features a modification of the amino acid from L to A at position 493.
+The protein's natural variant, known as in strain: T1, features a modification of the amino acid from V to D at position 515.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 22.
+The natural variant of this protein is characterized by an amino acid alteration from G to R at position 24.
+The natural variant of this protein is characterized by an amino acid alteration from R to G at position 153.
+The natural variant of this protein is characterized by an amino acid alteration from Q to R at position 157.
+The natural variant of this protein is characterized by an amino acid alteration from I to T at position 268.
+The natural variant of this protein is characterized by an amino acid alteration from G to E at position 280.
+The natural variant of this protein is characterized by an amino acid alteration from V to A at position 339.
+The natural variant of this protein is characterized by an amino acid alteration from E to K at position 349.
+The natural variant of this protein is characterized by an amino acid alteration from G to R at position 358.
+The natural variant of this protein is characterized by an amino acid alteration from R to K at position 434.
+The natural variant of this protein is characterized by an amino acid alteration from G to D at position 458.
+The natural variant of this protein is characterized by an amino acid alteration from E to K at position 491.
+The natural variant of this protein is characterized by an amino acid alteration from G to R at position 514.
+The natural variant of this protein is characterized by an amino acid alteration from G to R at position 524.
+The natural variant of this protein is characterized by an amino acid alteration from E to K at position 531.
+The natural variant of this protein is characterized by an amino acid alteration from S to N at position 546.
+The natural variant of this protein is characterized by an amino acid alteration from A to T at position 548.
+The natural variant of this protein is characterized by an amino acid alteration from E to K at position 552.
+The natural variant of this protein is characterized by an amino acid alteration from E to K at position 636.
+The protein's natural variant, known as in strain: CWL029 and TW-183, features a modification of the amino acid from C to Y at position 577.
+The protein's natural variant, known as in strain: ECOR 4 and ECOR 10, features a modification of the amino acid from S to N at position 100.
+The protein's natural variant, known as in strain: cv. Haomuxi, features a modification of the amino acid from P to S at position 415.
+The protein's natural variant, known as in AHUS3;, features a modification of the amino acid from P to L at position 64.
+The protein's natural variant, known as in AHUS3 and ARMD13; the mutant is both expressed and secreted at lower levels than wild-type protein; mediates C3 degradation to a lesser extent than that of controls;, features a modification of the amino acid from G to R at position 119.
+The protein's natural variant, known as in AHUS3;, features a modification of the amino acid from H to R at position 183.
+The natural variant of this protein is characterized by an amino acid alteration from G to A at position 188.
+The protein's natural variant, known as in CFI deficiency;, features a modification of the amino acid from G to D at position 243.
+The protein's natural variant, known as in AHUS3;, features a modification of the amino acid from G to R at position 287.
+The protein's natural variant, known as in AHUS3;, features a modification of the amino acid from R to W at position 317.
+The protein's natural variant, known as in AHUS3;, features a modification of the amino acid from I to T at position 340.
+The protein's natural variant, known as in AHUS3;, features a modification of the amino acid from I to L at position 416.
+The protein's natural variant, known as in CFI deficiency;, features a modification of the amino acid from H to L at position 418.
+The protein's natural variant, known as in AHUS3;, features a modification of the amino acid from D to N at position 519.
+The protein's natural variant, known as in AHUS3, features a modification of the amino acid from K to T at position 522.
+The protein's natural variant, known as in AHUS3;, features a modification of the amino acid from D to V at position 524.
+The protein's natural variant, known as in a renal clear cell carcinoma sample; somatic mutation, features a modification of the amino acid from K to E at position 93.
+The protein's natural variant, known as in a breast infiltrating ductal carcinoma sample; somatic mutation;, features a modification of the amino acid from E to D at position 276.
+The protein's natural variant, known as in TCS2;, features a modification of the amino acid from E to K at position 47.
+The protein's natural variant, known as in TCS2, features a modification of the amino acid from T to I at position 50.
+The protein's natural variant, known as in TCS2;, features a modification of the amino acid from L to R at position 51.
+The protein's natural variant, known as in TCS2, features a modification of the amino acid from G to E at position 52.
+The protein's natural variant, known as in TCS2;, features a modification of the amino acid from R to C at position 56.
+The protein's natural variant, known as in TCS2, features a modification of the amino acid from L to S at position 82.
+The protein's natural variant, known as in TCS2, features a modification of the amino acid from G to S at position 99.
+The protein's natural variant, known as in NEDJED, features a modification of the amino acid from G to R at position 242.
+The protein's natural variant, known as in NEDJED, features a modification of the amino acid from R to W at position 363.
+The protein's natural variant, known as in NEDJED, features a modification of the amino acid from A to D at position 364.
+The protein's natural variant, known as in NEDJED, features a modification of the amino acid from A to T at position 365.
+The protein's natural variant, known as in NEDJED, features a modification of the amino acid from E to K at position 444.
+The protein's natural variant, known as in NEDJED, features a modification of the amino acid from R to L at position 447.
+The protein's natural variant, known as in NEDJED, features a modification of the amino acid from R to Q at position 447.
+The protein's natural variant, known as in strain: CWL029 and TW-183, features a modification of the amino acid from N to H at position 96.
+The protein's natural variant, known as associated with susceptibility to schizoaffective disorder;, features a modification of the amino acid from L to F at position 607.
+The natural variant of this protein is characterized by an amino acid alteration from M to T at position 20.
+The protein's natural variant, known as may be associated with infertility;, features a modification of the amino acid from K to R at position 27.
+The protein's natural variant, known as no effect on glucagon-elicited cAMP production;, features a modification of the amino acid from G to S at position 40.
+The protein's natural variant, known as in MVAH, features a modification of the amino acid from D to N at position 63.
+The protein's natural variant, known as no effect on glucagon-elicited cAMP production, features a modification of the amino acid from T to M at position 76.
+The protein's natural variant, known as in MVAH; abolishes glucagon binding, features a modification of the amino acid from P to S at position 86.
+The protein's natural variant, known as in MVAH; when associated in cis with M-368; decreased glucagon binding and decreased glucagon-elicited cAMP production; decreased localization to the cell membrane, features a modification of the amino acid from R to H at position 225.
+The protein's natural variant, known as no effect on glucagon-elicited cAMP production, features a modification of the amino acid from R to Q at position 336.
+The protein's natural variant, known as in MVAH; when associated in cis with H-225; decreased glucagon binding and decreased glucagon-elicited cAMP production; no effect on localization to the cell membrane, features a modification of the amino acid from V to M at position 368.
+The protein's natural variant, known as no effect on glucagon-elicited cAMP production, features a modification of the amino acid from R to H at position 414.
+The protein's natural variant, known as no effect on glucagon-elicited cAMP production, features a modification of the amino acid from H to R at position 416.
+The protein's natural variant, known as no effect on glucagon-elicited cAMP production, features a modification of the amino acid from R to Q at position 428.
+The protein's natural variant, known as no effect on glucagon-elicited cAMP production, features a modification of the amino acid from S to L at position 438.
+The protein's natural variant, known as no effect on glucagon-elicited cAMP production, features a modification of the amino acid from D to H at position 458.
+The protein's natural variant, known as no effect on glucagon-elicited cAMP production, features a modification of the amino acid from A to V at position 461.
+The protein's natural variant, known as no effect on glucagon-elicited cAMP production, features a modification of the amino acid from P to L at position 476.
+The protein's natural variant, known as in NEDCPMD; unknown pathological significance, features a modification of the amino acid from R to P at position 359.
+The protein's natural variant, known as in NEDCPMD; decreased protein abundance in patient-derived cells; decreased cell surface localization; unknown pathological significance, features a modification of the amino acid from V to E at position 1229.
+The protein's natural variant, known as in DEE34; results in reduced chloride transport; decreased localization at the cell surface;, features a modification of the amino acid from L to H at position 311.
+The protein's natural variant, known as in DEE34; results in loss of chloride transport; decreased localization at the cell surface;, features a modification of the amino acid from L to P at position 426.
+The protein's natural variant, known as in DEE34; results in loss of chloride transport; decreased localization at the cell surface;, features a modification of the amino acid from G to D at position 551.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from G to D at position 847.
+The protein's natural variant, known as in EIG14; rare variant associated with disease susceptibility; results in reduced chloride transport; decreased localization at the cell surface; unable to induce cortical dendritic spines formation;, features a modification of the amino acid from R to H at position 975.
+The protein's natural variant, known as in EIG14; rare variant associated with disease susceptibility; results in reduced chloride transport;, features a modification of the amino acid from R to C at position 1072.
+The natural variant of this protein is characterized by an amino acid alteration from F to V at position 4.
+The natural variant of this protein is characterized by an amino acid alteration from F to S at position 15.
+The natural variant of this protein is characterized by an amino acid alteration from L to Q at position 67.
+The natural variant of this protein is characterized by an amino acid alteration from T to A at position 84.
+The protein's natural variant, known as in strain: NCTC 4716, features a modification of the amino acid from V to I at position 100.
+The natural variant of this protein is characterized by an amino acid alteration from A to G at position 13.
+The natural variant of this protein is characterized by an amino acid alteration from N to S at position 141.
+The protein's natural variant, known as in strain: BP26; photosynthesis-deficient, features a modification of the amino acid from V to G at position 51.
+The protein's natural variant, known as in MECRCN, features a modification of the amino acid from L to P at position 20.
+The protein's natural variant, known as in MECRCN;, features a modification of the amino acid from L to R at position 20.
+The protein's natural variant, known as in MECRCN; unknown pathological significance;, features a modification of the amino acid from R to K at position 26.
+The protein's natural variant, known as in MECRCN; unknown pathological significance;, features a modification of the amino acid from T to P at position 74.
+The protein's natural variant, known as in MECRCN; unknown pathological significance, features a modification of the amino acid from G to C at position 89.
+The protein's natural variant, known as in MECRCN;, features a modification of the amino acid from G to R at position 154.
+The protein's natural variant, known as in MECRCN; unknown pathological significance, features a modification of the amino acid from T to I at position 236.
+The protein's natural variant, known as correlated with reduced enzyme activity; associated with increased risk for schizophrenia;, features a modification of the amino acid from A to S at position 72.
+The protein's natural variant, known as in allele COMT*2; associated with low enzyme activity and thermolability; may increase the tendency to develop high blood pressure and abdominal obesity;, features a modification of the amino acid from V to M at position 158.
+The protein's natural variant, known as found at heterozygosity in a patient with Bardet-Biedl syndrome also carrying BBS6 mutation A-57 in MKKS; hypomorphic variant, features a modification of the amino acid from D to A at position 155.
+The protein's natural variant, known as in a breast pleomorphic lobular carcinoma sample; somatic mutation;, features a modification of the amino acid from S to C at position 660.
+The protein's natural variant, known as in an ovarian papillary serous adenocarcinoma sample; somatic mutation, features a modification of the amino acid from S to Y at position 767.
+The protein's natural variant, known as in an ovarian serous carcinoma sample; somatic mutation, features a modification of the amino acid from Q to K at position 1138.
+The protein's natural variant, known as in an ovarian endometrioid sample; somatic mutation, features a modification of the amino acid from P to S at position 1185.
+The natural variant of this protein is characterized by an amino acid alteration from H to P at position 1313.
+The protein's natural variant, known as in strain: MA-1 / fabB3, features a modification of the amino acid from A to T at position 4.
+The protein's natural variant, known as in strain: K1060 / fabB5, features a modification of the amino acid from S to F at position 140.
+The protein's natural variant, known as in strain: MA-1 / fabB3, features a modification of the amino acid from G to S at position 299.
+The protein's natural variant, known as in strain: M5 / fabB15, features a modification of the amino acid from A to V at position 329.
+The protein's natural variant, known as in strain: AL847, features a modification of the amino acid from A to T at position 59.
+The protein's natural variant, known as in strain: AL845 and AL847; chloramphenicol-sensitive, features a modification of the amino acid from N to D at position 73.
+The protein's natural variant, known as in strain: cv. Se-0, features a modification of the amino acid from S to N at position 765.
+The protein's natural variant, known as in strain: Serovar 6B, features a modification of the amino acid from L to P at position 240.
+The protein's natural variant, known as in strain: Serovar 6B, features a modification of the amino acid from K to KNTNTNTNTNTNTNT at position 328.
+The protein's natural variant, known as in strain: Pu-60m, features a modification of the amino acid from R to K at position 25.
+The protein's natural variant, known as in strain: Pu-60m, features a modification of the amino acid from Q to H at position 120.
+The protein's natural variant, known as in allele b', features a modification of the amino acid from D to N at position 148.
+The protein's natural variant, known as in MC1DN17;, features a modification of the amino acid from D to V at position 69.
+The protein's natural variant, known as in MC1DN17;, features a modification of the amino acid from S to P at position 76.
+The protein's natural variant, known as in MC1DN17;, features a modification of the amino acid from Q to R at position 99.
+The protein's natural variant, known as in MC1DN17;, features a modification of the amino acid from I to T at position 124.
+The protein's natural variant, known as in MC1DN17;, features a modification of the amino acid from A to P at position 178.
+The protein's natural variant, known as in MC1DN17;, features a modification of the amino acid from H to D at position 269.
+The protein's natural variant, known as in MC1DN17;, features a modification of the amino acid from R to G at position 274.
+The protein's natural variant, known as in LCAEOD; affects microtubules polymerization;, features a modification of the amino acid from R to C at position 391.
+The protein's natural variant, known as in LCAEOD; affects microtubules polymerization;, features a modification of the amino acid from R to H at position 391.
+The protein's natural variant, known as in A2, features a modification of the amino acid from A to E at position 56.
+The protein's natural variant, known as in A2, features a modification of the amino acid from S to SS at position 80.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from E to K at position 181.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from I to V at position 229.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from E to G at position 230.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from K to E at position 233.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from E to G at position 254.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from K to R at position 265.
+The protein's natural variant, known as in IBGC1;, features a modification of the amino acid from I to L at position 11.
+The protein's natural variant, known as in IBGC1; Impairs phosphate transport; no effect on retroviral receptor function;, features a modification of the amino acid from D to N at position 28.
+The protein's natural variant, known as in IBGC1, features a modification of the amino acid from A to V at position 51.
+The protein's natural variant, known as in IBGC1, features a modification of the amino acid from L to P at position 62.
+The protein's natural variant, known as in IBGC1, features a modification of the amino acid from R to H at position 71.
+The protein's natural variant, known as in IBGC1; loss of sodium-dependent phosphate transport but no effect on cell membrane localization;, features a modification of the amino acid from T to M at position 115.
+The protein's natural variant, known as in IBGC1; unknown pathological significance, features a modification of the amino acid from P to L at position 184.
+The protein's natural variant, known as in IBGC1; unknown pathological significance;, features a modification of the amino acid from N to S at position 194.
+The protein's natural variant, known as in IBGC1;, features a modification of the amino acid from R to Q at position 382.
+The protein's natural variant, known as in IBGC1;, features a modification of the amino acid from S to W at position 434.
+The protein's natural variant, known as in IBGC1; substantially impaired phosphate transport, features a modification of the amino acid from G to R at position 498.
+The protein's natural variant, known as in IBGC1, features a modification of the amino acid from H to Q at position 502.
+The protein's natural variant, known as in IBGC1;, features a modification of the amino acid from P to L at position 568.
+The protein's natural variant, known as in IBGC1;, features a modification of the amino acid from G to S at position 571.
+The protein's natural variant, known as in IBGC1; substantially impaired phosphate transport;, features a modification of the amino acid from E to K at position 575.
+The protein's natural variant, known as in IBGC1; substantially impaired phosphate transport;, features a modification of the amino acid from T to M at position 595.
+The protein's natural variant, known as in IBGC1; substantially impaired phosphate transport;, features a modification of the amino acid from S to L at position 601.
+The protein's natural variant, known as in IBGC1; substantially impaired phosphate transport;, features a modification of the amino acid from S to W at position 601.
+The protein's natural variant, known as in IBGC1; unknown pathological significance; reduced sodium-dependent phosphate transport and cell membrane localization, features a modification of the amino acid from T to TWFVT at position 629.
+The protein's natural variant, known as in IBGC1; loss of sodium-dependent phosphate transport but no effect on cell membrane localization, features a modification of the amino acid from S to R at position 637.
+The natural variant of this protein is characterized by an amino acid alteration from G to R at position 103.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from N to D at position 62.
+The natural variant of this protein is characterized by an amino acid alteration from Q to R at position 100.
+The natural variant of this protein is characterized by an amino acid alteration from G to V at position 19.
+The natural variant of this protein is characterized by an amino acid alteration from V to M at position 77.
+The protein's natural variant, known as in JBTS32; decreased stability; no effect on nuclear and cytoplasmic localization; decreased interaction with GLI3; no effect on interaction with GLI1; decreased repression of the hedgehog/smoothened signaling pathway;, features a modification of the amino acid from H to R at position 176.
+The protein's natural variant, known as in JBTS32; decreased stability; forms cytoplasmic aggregates; decreased interaction with GLI3; no effect on interaction with GLI1; decreased repression of the hedgehog/smoothened signaling pathway;, features a modification of the amino acid from I to T at position 406.
+The natural variant of this protein is characterized by an amino acid alteration from S to N at position 481.
+The protein's natural variant, known as in strain: ATCC 43603, features a modification of the amino acid from N to K at position 214.
+The protein's natural variant, known as in strain: ATCC 43603, features a modification of the amino acid from L to V at position 235.
+The protein's natural variant, known as in strain: ATCC 43603, features a modification of the amino acid from S to N at position 327.
+The protein's natural variant, known as in strain: ATCC 43603, features a modification of the amino acid from A to S at position 339.
+The protein's natural variant, known as found in patients with late onset Alzheimer disease; unknown pathological significance; no effect on cell membrane localization;, features a modification of the amino acid from V to M at position 27.
+The protein's natural variant, known as found in patients with late onset Alzheimer disease; unknown pathological significance; increases cell membrane localization;, features a modification of the amino acid from A to V at position 28.
+The protein's natural variant, known as found in patients with late onset Alzheimer disease; unknown pathological significance; decreases cell membrane localization;, features a modification of the amino acid from S to F at position 31.
+The protein's natural variant, known as results in defective protein maturation and trafficking; loss of proteolytic cleavage by ADAM10 and ectodomain shedding; increases protein aggregation; decreases cell membrane localization; decreased phagocytosis; loss of LDL, CLU and APOE binding; greatly decreases LDL and CLU uptake into cells;, features a modification of the amino acid from Y to C at position 38.
+The protein's natural variant, known as found in patients with late onset Alzheimer disease; unknown pathological significance; decreases cell membrane localization;, features a modification of the amino acid from R to C at position 47.
+The protein's natural variant, known as found in patients with late onset Alzheimer disease; unknown pathological significance; no effect on cell membrane localization; no effect on autophagy in microglia; no effect on phagocystosis, including amyloid plaque clearance by microglia; reduces ectodomain shedding caused by proteolytic cleavage by ADAM10, while also reducing the oligomerization of the extracellular domain after shedding; decreases binding to and uptake of LDL and CLU into cells; decreases binding to APOE, phospholipids and oligomeric APP cleavage product beta-amyloid peptide 42;, features a modification of the amino acid from R to H at position 47.
+The protein's natural variant, known as does not affect protein structure; no effect on cell membrane localization; increases autophagy in microglia; decreases LDL, CLU and APOE binding; decreases LDL uptake into cells; no effect on CLU uptake into cells; decreases the uptake of APP-LDL complex in macrophages; decreases binding to oligomeric APP cleavage product beta-amyloid peptide 42;, features a modification of the amino acid from R to H at position 62.
+The protein's natural variant, known as results in defective protein maturation and trafficking; loss of proteolytic cleavage by ADAM10 and ectodomain shedding; increases protein aggregation; decreases cell membrane localization; decreases phagocytosis; loss of LDL, CLU and APOE binding; greatly decreases LDL and CLU uptake into cells;, features a modification of the amino acid from T to M at position 66.
+The protein's natural variant, known as decreases LDL, CLU and APOE binding; decreases LDL and CLU uptake into cells; no effect on cell membrane localization;, features a modification of the amino acid from D to N at position 87.
+The protein's natural variant, known as does not change protein structure; changes protein stability; increases binding to THP-1 cells;, features a modification of the amino acid from T to K at position 96.
+The protein's natural variant, known as in PLOSL2; results in defective protein maturation; increases protein aggregation; decreases cell membrane localization;, features a modification of the amino acid from V to G at position 126.
+The protein's natural variant, known as likely benign variant; no effect on protein expression and maturation, features a modification of the amino acid from A to S at position 130.
+The protein's natural variant, known as in PLOSL2; unknown pathological significance; decreased protein level;, features a modification of the amino acid from D to G at position 134.
+The protein's natural variant, known as found in patients with Alzheimer disease; unknown pathological significance; slightly decreases cell membrane localization;, features a modification of the amino acid from R to Q at position 136.
+The protein's natural variant, known as found in patients with Alzheimer disease; unknown pathological significance; decreases cell membrane localization;, features a modification of the amino acid from R to W at position 136.
+The protein's natural variant, known as found in patients with late onset Alzheimer disease; unknown pathological significance; decreases cell membrane localization;, features a modification of the amino acid from E to K at position 151.
+The protein's natural variant, known as may be associated with an increased risk for late-onset Alzheimer disease; accelerates ectodomain shedding but does not alter the cleavage site; decreases cell membrane localization; decreases phagocytosis;, features a modification of the amino acid from H to Y at position 157.
+The protein's natural variant, known as no effect on protein expression and maturation;, features a modification of the amino acid from S to R at position 162.
+The protein's natural variant, known as in PLOSL2; unknown pathological significance; increased localization at the cell membrane;, features a modification of the amino acid from K to N at position 186.
+The protein's natural variant, known as affects protein maturation;, features a modification of the amino acid from T to I at position 223.
+The protein's natural variant, known as found in a large family with autosomal dominant thrombocytopenia; unknown pathological significance; no effect on nuclear localization;, features a modification of the amino acid from E to D at position 167.
+The protein's natural variant, known as in SKDEAS; unknown pathological significance, features a modification of the amino acid from W to R at position 172.
+The protein's natural variant, known as in SKDEAS; unknown pathological significance, features a modification of the amino acid from L to P at position 215.
+The protein's natural variant, known as in SKDEAS; unknown pathological significance;, features a modification of the amino acid from S to R at position 254.
+The protein's natural variant, known as in SKDEAS; unknown pathological significance; slightly decreased protein expression;;, features a modification of the amino acid from D to N at position 284.
+The protein's natural variant, known as in a pancreatic ductal adenocarcinoma sample; somatic mutation, features a modification of the amino acid from N to H at position 305.
+The protein's natural variant, known as in COXPD16;, features a modification of the amino acid from L to R at position 156.
+The protein's natural variant, known as in HOPS, features a modification of the amino acid from S to F at position 17.
+The protein's natural variant, known as in HPPI; 7% of activity, features a modification of the amino acid from Y to C at position 28.
+The protein's natural variant, known as in HOPS; strongly reduced alkaline phosphatase activity;, features a modification of the amino acid from A to V at position 33.
+The protein's natural variant, known as in HOPS; 2% of activity;, features a modification of the amino acid from A to V at position 40.
+The protein's natural variant, known as in HOPS, features a modification of the amino acid from A to S at position 51.
+The protein's natural variant, known as in HOPS;, features a modification of the amino acid from A to V at position 51.
+The protein's natural variant, known as in HOPS; moderate; 27% of activity, features a modification of the amino acid from M to L at position 62.
+The protein's natural variant, known as in HOPS, features a modification of the amino acid from M to V at position 62.
+The protein's natural variant, known as in HOPS, features a modification of the amino acid from G to R at position 63.
+The protein's natural variant, known as in HOPS; loss of activity, features a modification of the amino acid from G to V at position 63.
+The protein's natural variant, known as in HPPC; severe allele, features a modification of the amino acid from T to M at position 68.
+The protein's natural variant, known as in HOPS; abolished alkaline phosphatase activity;, features a modification of the amino acid from R to C at position 71.
+The protein's natural variant, known as in HOPS; loss of alkaline phosphatase activity;, features a modification of the amino acid from R to H at position 71.
+The protein's natural variant, known as in HOPS; abolished alkaline phosphatase activity;, features a modification of the amino acid from R to P at position 71.
+The protein's natural variant, known as in HPPC; severe allele;, features a modification of the amino acid from R to S at position 71.
+The protein's natural variant, known as in HOPS; severe; 3.5% of activity;, features a modification of the amino acid from G to S at position 75.
+The protein's natural variant, known as in HOPS;, features a modification of the amino acid from Q to R at position 76.
+The protein's natural variant, known as in HOPS; dominant-negative mutant; abolished alkaline phosphatase activity, features a modification of the amino acid from G to R at position 82.
+The protein's natural variant, known as in HOPS; 0.4% of alkaline phosphatase activity; severe allele; no effect on subcellular location; fails to assemble into dimeric structure; dominant negative effect;, features a modification of the amino acid from P to L at position 108.
+The protein's natural variant, known as in HOPS; odonto; abolished alkaline phosphatase activity;, features a modification of the amino acid from A to T at position 111.
+The protein's natural variant, known as in HOPS, features a modification of the amino acid from A to G at position 114.
+The protein's natural variant, known as in HOPS; loss of alkaline phosphatase activity;, features a modification of the amino acid from A to T at position 116.
+The protein's natural variant, known as in HOPS;, features a modification of the amino acid from G to R at position 120.
+The protein's natural variant, known as in HOPS;, features a modification of the amino acid from V to M at position 128.
+The protein's natural variant, known as in HOPS, features a modification of the amino acid from G to R at position 129.
+The protein's natural variant, known as in HOPS; strongly reduced alkaline phosphatase activity, features a modification of the amino acid from A to V at position 132.
+The protein's natural variant, known as in HOPS; requires 2 nucleotide substitutions;, features a modification of the amino acid from T to H at position 134.
+The protein's natural variant, known as in HOPS; 9% of activity;, features a modification of the amino acid from T to N at position 134.
+The protein's natural variant, known as in HOPS; moderate; 33% of activity;, features a modification of the amino acid from R to H at position 136.
+The protein's natural variant, known as in HOPS;, features a modification of the amino acid from T to I at position 148.
+The protein's natural variant, known as in HOPS; unknown pathological significance, features a modification of the amino acid from R to C at position 152.
+The protein's natural variant, known as in HOPS; lethal form; benign variant;, features a modification of the amino acid from R to H at position 152.
+The protein's natural variant, known as in HOPS;, features a modification of the amino acid from G to S at position 162.
+The protein's natural variant, known as in HOPS; severe; 1% of activity;, features a modification of the amino acid from G to V at position 162.
+The protein's natural variant, known as in HOPS, features a modification of the amino acid from N to D at position 170.
+The protein's natural variant, known as in HOPS;, features a modification of the amino acid from H to R at position 171.
+The protein's natural variant, known as in HOPS; severe; 2% of activity, features a modification of the amino acid from H to Y at position 171.
+The protein's natural variant, known as in HOPS; 30% of alkaline phosphatase activity;, features a modification of the amino acid from A to T at position 176.
+The protein's natural variant, known as in HOPS and HPPC; moderate allele; normal alkaline phosphatase activity toward diphosphate and increased activity toward pyridoxal 5'-phosphate;, features a modification of the amino acid from A to T at position 177.
+The protein's natural variant, known as in HOPS; reduced alkaline phosphatase activity toward diphosphate and pyridoxal 5'-phosphate;, features a modification of the amino acid from A to T at position 179.
+The protein's natural variant, known as in HOPS; 1% of activity;, features a modification of the amino acid from S to L at position 181.
+The protein's natural variant, known as in HOPS; loss of activity;, features a modification of the amino acid from R to W at position 184.
+The protein's natural variant, known as in HOPS; unknown pathological significance, features a modification of the amino acid from S to P at position 188.
+The protein's natural variant, known as in HOPS, features a modification of the amino acid from D to E at position 189.
+The protein's natural variant, known as in HOPS; odonto; slightly reduced alkaline phosphatase activity, features a modification of the amino acid from E to G at position 191.
+The protein's natural variant, known as in HOPS; moderate; frequent mutation in European countries; slightly reduced alkaline phosphatase activity;, features a modification of the amino acid from E to K at position 191.
+The protein's natural variant, known as in HOPS; weak alkaline phosphatase activity; severely affects homodimerization; reduced cell surface expression, features a modification of the amino acid from C to Y at position 201.
+The protein's natural variant, known as in HOPS;, features a modification of the amino acid from Q to P at position 207.
+The protein's natural variant, known as in HOPS, features a modification of the amino acid from N to D at position 211.
+The protein's natural variant, known as in HOPS, features a modification of the amino acid from I to F at position 212.
+The protein's natural variant, known as in HOPS; unknown pathological significance, features a modification of the amino acid from I to S at position 218.
+The protein's natural variant, known as in HOPS, features a modification of the amino acid from G to A at position 220.
+The protein's natural variant, known as in HOPS; odonto, features a modification of the amino acid from G to V at position 220.
+The protein's natural variant, known as in HOPS;, features a modification of the amino acid from R to Q at position 223.
+The protein's natural variant, known as in HOPS and HPPC; severe allele; abolished alkaline phosphatase activity;, features a modification of the amino acid from R to W at position 223.
+The protein's natural variant, known as in HPPI; partial loss of activity;, features a modification of the amino acid from K to E at position 224.
+The protein's natural variant, known as in HOPS, features a modification of the amino acid from E to G at position 235.
+The protein's natural variant, known as in HOPS; 4% of activity;, features a modification of the amino acid from R to S at position 246.
+The protein's natural variant, known as in HOPS; partial loss of activity;, features a modification of the amino acid from G to V at position 249.
+The protein's natural variant, known as in HOPS; 6.8% of wild-type activity;, features a modification of the amino acid from R to H at position 272.
+The protein's natural variant, known as in HOPS;, features a modification of the amino acid from R to L at position 272.
+The protein's natural variant, known as in HPPC; severe allele;, features a modification of the amino acid from L to P at position 275.
+The protein's natural variant, known as in HOPS, features a modification of the amino acid from L to F at position 289.
+The protein's natural variant, known as in HOPS; moderate; 8% of activity;, features a modification of the amino acid from E to K at position 291.
+The protein's natural variant, known as in HOPS; 4% of wild-type activity;, features a modification of the amino acid from P to T at position 292.
+The protein's natural variant, known as in HOPS; reduced alkaline phosphatase toward diphosphate and pyridoxal 5'-phosphate;, features a modification of the amino acid from D to A at position 294.
+The protein's natural variant, known as in HOPS;, features a modification of the amino acid from D to Y at position 294.
+The protein's natural variant, known as in HOPS; 8.5% of wild-type activity;, features a modification of the amino acid from M to T at position 295.
+The protein's natural variant, known as in HOPS; 1.3% of wild-type activity, features a modification of the amino acid from Y to D at position 297.
+The protein's natural variant, known as in HPPI; does not affect alkaline phosphatase activity;, features a modification of the amino acid from E to K at position 298.
+The protein's natural variant, known as in HOPS, features a modification of the amino acid from L to P at position 299.
+The protein's natural variant, known as in HOPS, features a modification of the amino acid from D to V at position 306.
+The protein's natural variant, known as in HOPS;, features a modification of the amino acid from E to K at position 311.
+The protein's natural variant, known as in HOPS; in a patient carrying also K-291, features a modification of the amino acid from G to R at position 326.
+The protein's natural variant, known as in HOPS; requires 2 nucleotide substitutions, features a modification of the amino acid from F to G at position 327.
+The protein's natural variant, known as in HOPS and HPPI;, features a modification of the amino acid from F to L at position 327.
+The protein's natural variant, known as in HOPS; abolished alkaline phosphatase activity;, features a modification of the amino acid from G to D at position 334.
+The protein's natural variant, known as in HOPS; weak alkaline phosphatase activity, features a modification of the amino acid from G to R at position 334.
+The protein's natural variant, known as in HOPS; loss of alkaline phosphatase activity, features a modification of the amino acid from G to R at position 339.
+The protein's natural variant, known as in HOPS;, features a modification of the amino acid from A to T at position 348.
+The protein's natural variant, known as in HOPS;, features a modification of the amino acid from E to D at position 354.
+The protein's natural variant, known as in HOPS; strongly reduced alkaline phosphatase activity;, features a modification of the amino acid from D to V at position 378.
+The protein's natural variant, known as in HOPS, features a modification of the amino acid from H to R at position 381.
+The protein's natural variant, known as in HOPS; abolished alkaline phosphatase activity;, features a modification of the amino acid from V to I at position 382.
+The protein's natural variant, known as in HOPS; moderate; 4-10% of alkaline phosphatase activity;, features a modification of the amino acid from R to C at position 391.
+The protein's natural variant, known as in HPPC and HOPS; severe allele; loss of alkaline phosphatase activity;, features a modification of the amino acid from R to H at position 391.
+The protein's natural variant, known as in HOPS, features a modification of the amino acid from A to S at position 399.
+The protein's natural variant, known as in HOPS; 15% of activity, features a modification of the amino acid from D to G at position 406.
+The protein's natural variant, known as in HOPS; absence of residual enzymatic activity, features a modification of the amino acid from T to A at position 411.
+The protein's natural variant, known as in HOPS; loss of alkaline phosphatase activity, features a modification of the amino acid from L to M at position 414.
+The protein's natural variant, known as in HOPS; very low alkaline phosphatase activity; does not affect subcellular location; fails to assemble into dimeric structure;, features a modification of the amino acid from N to S at position 417.
+The protein's natural variant, known as in HOPS; very low alkaline phosphatase activity; does not affect subcellular location, features a modification of the amino acid from G to A at position 420.
+The protein's natural variant, known as in HOPS; very low alkaline phosphatase activity; does not affect subcellular location, features a modification of the amino acid from G to S at position 420.
+The protein's natural variant, known as in HOPS; 16% alkaline of phosphatase activity, features a modification of the amino acid from V to A at position 423.
+The protein's natural variant, known as in HPPI; partial loss of activity, features a modification of the amino acid from G to C at position 426.
+The protein's natural variant, known as in HOPS, features a modification of the amino acid from G to D at position 426.
+The protein's natural variant, known as in HOPS;, features a modification of the amino acid from Y to H at position 436.
+The protein's natural variant, known as in HOPS; severe; 2% of activity;, features a modification of the amino acid from S to P at position 445.
+The protein's natural variant, known as in HOPS; severe; 4% of activity;, features a modification of the amino acid from R to C at position 450.
+The protein's natural variant, known as in HOPS;, features a modification of the amino acid from R to H at position 450.
+The protein's natural variant, known as in HOPS; loss of alkaline phosphatase activity;, features a modification of the amino acid from E to K at position 452.
+The protein's natural variant, known as in HPPI and HOPS; strongly reduced alkaline phosphatase activity;, features a modification of the amino acid from G to R at position 456.
+The protein's natural variant, known as in HOPS; loss of alkaline phosphatase activity, features a modification of the amino acid from V to L at position 459.
+The protein's natural variant, known as in HPPI;, features a modification of the amino acid from V to M at position 459.
+The protein's natural variant, known as in HOPS;, features a modification of the amino acid from A to T at position 468.
+The protein's natural variant, known as in HOPS, features a modification of the amino acid from G to S at position 473.
+The protein's natural variant, known as in HOPS; loss of alkaline phosphatase activity, features a modification of the amino acid from E to A at position 476.
+The protein's natural variant, known as in HOPS, features a modification of the amino acid from E to K at position 476.
+The protein's natural variant, known as in HOPS; 9% of activity, features a modification of the amino acid from N to I at position 478.
+The protein's natural variant, known as in HOPS; reduces alkaline phosphatase activity, features a modification of the amino acid from C to S at position 489.
+The protein's natural variant, known as in HOPS; odonto; partial loss of activity, features a modification of the amino acid from I to F at position 490.
+The protein's natural variant, known as in HOPS;, features a modification of the amino acid from G to R at position 491.
+The protein's natural variant, known as in strain: 406 / Type 3, 19F and SP-VA96, features a modification of the amino acid from V to I at position 461.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from D to N at position 183.
+The natural variant of this protein is characterized by an amino acid alteration from D to A at position 212.
+The natural variant of this protein is characterized by an amino acid alteration from H to D at position 235.
+The natural variant of this protein is characterized by an amino acid alteration from D to N at position 27.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from H to L at position 129.
+The protein's natural variant, known as in strain: 21, features a modification of the amino acid from E to D at position 14.
+The protein's natural variant, known as in strain: 21, 30 and 1/1, features a modification of the amino acid from E to D at position 20.
+The protein's natural variant, known as in strain: 30, 56 and 1/1, features a modification of the amino acid from K to Q at position 60.
+The protein's natural variant, known as in strain: 92, features a modification of the amino acid from I to V at position 65.
+The protein's natural variant, known as in strain: 21, 56 and 1/1, features a modification of the amino acid from P to S at position 70.
+The protein's natural variant, known as in strain: 21, features a modification of the amino acid from I to L at position 74.
+The protein's natural variant, known as in strain: 30, features a modification of the amino acid from VA to AV at position 78.
+The protein's natural variant, known as in strain: 21, 56 and 1/1, features a modification of the amino acid from Q to H at position 81.
+The protein's natural variant, known as in strain: 21, features a modification of the amino acid from Q to H at position 91.
+The protein's natural variant, known as in strain: ATCC 49619, features a modification of the amino acid from A to D at position 92.
+The protein's natural variant, known as in strain: 21, features a modification of the amino acid from E to D at position 94.
+The protein's natural variant, known as in strain: 21, 30, 56 and 1/1, features a modification of the amino acid from I to L at position 100.
+The protein's natural variant, known as in strain: 56 and 1/1, features a modification of the amino acid from P to S at position 111.
+The protein's natural variant, known as in strain: 21, 30, 56 and 1/1, features a modification of the amino acid from L to F at position 135.
+The protein's natural variant, known as in strain: 56, features a modification of the amino acid from E to D at position 141.
+The protein's natural variant, known as in strain: 21, features a modification of the amino acid from FYA to SYT at position 149.
+The protein's natural variant, known as abolishes activity, features a modification of the amino acid from G to R at position 181.
+The protein's natural variant, known as found in a patient with neurodevelopmental disorder with absent speech, pyramidal signs and limb ataxia; probable disease-associated variant, features a modification of the amino acid from D to H at position 126.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from D to N at position 434.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from D to N at position 462.
+The protein's natural variant, known as in SPG72; abolishes REEP2 interaction with membranes; affects correct shaping of the endoplasmic reticulum;, features a modification of the amino acid from V to E at position 36.
+The protein's natural variant, known as in SPG72; reduces REEP2 interaction with membranes; affects correct shaping of the endoplasmic reticulum;, features a modification of the amino acid from F to Y at position 72.
+The protein's natural variant, known as in strain: Isolate SA 03, features a modification of the amino acid from I to T at position 323.
+The protein's natural variant, known as confers streptomycin resistance but not hyperaccurate translation, features a modification of the amino acid from K to R at position 43.
+The protein's natural variant, known as found in leukemia, features a modification of the amino acid from V to L at position 28.
+The protein's natural variant, known as in leukemia, features a modification of the amino acid from P to PQKP at position 232.
+The protein's natural variant, known as in IMD22;, features a modification of the amino acid from L to P at position 341.
+The protein's natural variant, known as found in leukemia, features a modification of the amino acid from A to V at position 353.
+The protein's natural variant, known as found in leukemia, features a modification of the amino acid from P to L at position 447.
+The protein's natural variant, known as in strain: Isolate FMNH 167358, features a modification of the amino acid from L to F at position 233.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from D to N at position 44.
+The protein's natural variant, known as in SCN1;, features a modification of the amino acid from A to V at position 25.
+The protein's natural variant, known as in SCN1, features a modification of the amino acid from P to L at position 42.
+The protein's natural variant, known as in SCN1 and CH, features a modification of the amino acid from F to L at position 43.
+The protein's natural variant, known as in SCN1, features a modification of the amino acid from M to R at position 44.
+The protein's natural variant, known as in SCN1, features a modification of the amino acid from V to E at position 45.
+The protein's natural variant, known as in CH, features a modification of the amino acid from V to L at position 45.
+The protein's natural variant, known as in SCN1, features a modification of the amino acid from S to C at position 46.
+The protein's natural variant, known as in CH and SCN1;, features a modification of the amino acid from S to F at position 46.
+The protein's natural variant, known as in SCN1;, features a modification of the amino acid from L to P at position 47.
+The protein's natural variant, known as in SCN1, features a modification of the amino acid from L to R at position 47.
+The protein's natural variant, known as in SCN1, features a modification of the amino acid from L to P at position 49.
+The protein's natural variant, known as in SCN1, features a modification of the amino acid from H to L at position 53.
+The protein's natural variant, known as in CH, features a modification of the amino acid from H to Q at position 53.
+The protein's natural variant, known as in SCN1;, features a modification of the amino acid from H to Y at position 53.
+The protein's natural variant, known as in SCN1, features a modification of the amino acid from C to S at position 55.
+The protein's natural variant, known as in SCN1, features a modification of the amino acid from C to Y at position 55.
+The protein's natural variant, known as in SCN1, features a modification of the amino acid from G to R at position 56.
+The protein's natural variant, known as in SCN1, features a modification of the amino acid from A to S at position 57.
+The protein's natural variant, known as in SCN1, features a modification of the amino acid from A to T at position 57.
+The protein's natural variant, known as in SCN1;, features a modification of the amino acid from A to V at position 57.
+The protein's natural variant, known as in SCN1, features a modification of the amino acid from L to P at position 59.
+The natural variant of this protein is characterized by an amino acid alteration from IA to R at position 61.
+The protein's natural variant, known as in SCN1, features a modification of the amino acid from I to T at position 60.
+The protein's natural variant, known as in SCN1 and CH;, features a modification of the amino acid from A to V at position 61.
+The protein's natural variant, known as in SCN1, features a modification of the amino acid from S to W at position 67.
+The protein's natural variant, known as in SCN1;, features a modification of the amino acid from C to F at position 71.
+The protein's natural variant, known as in SCN1;, features a modification of the amino acid from C to R at position 71.
+The protein's natural variant, known as in SCN1, features a modification of the amino acid from C to S at position 71.
+The protein's natural variant, known as in SCN1, features a modification of the amino acid from C to Y at position 71.
+The protein's natural variant, known as in SCN1, features a modification of the amino acid from V to G at position 72.
+The protein's natural variant, known as in SCN1, features a modification of the amino acid from V to G at position 80.
+The protein's natural variant, known as in SCN1 and CH, features a modification of the amino acid from R to P at position 81.
+The protein's natural variant, known as in SCN1 and CH, features a modification of the amino acid from V to M at position 82.
+The protein's natural variant, known as in SCN1;, features a modification of the amino acid from L to P at position 84.
+The protein's natural variant, known as in SCN1, features a modification of the amino acid from G to E at position 85.
+The protein's natural variant, known as in SCN1, features a modification of the amino acid from G to R at position 85.
+The protein's natural variant, known as in CH, features a modification of the amino acid from Q to L at position 97.
+The protein's natural variant, known as in SCN1; located on the same allele as L-101; reduces proteolytic enzyme activity by slightly less than half; together with L-101 shows an additive effect with minimal remaining enzyme activity;, features a modification of the amino acid from V to L at position 98.
+The protein's natural variant, known as in SCN1;, features a modification of the amino acid from V to M at position 98.
+The protein's natural variant, known as in SCN1; located on the same allele as L-98; reduces proteolytic enzyme activity by slightly less than half; together with L-98 shows an additive effect with minimal remaining enzyme activity;, features a modification of the amino acid from V to L at position 101.
+The protein's natural variant, known as in SCN1;, features a modification of the amino acid from V to M at position 101.
+The protein's natural variant, known as in SCN1;, features a modification of the amino acid from R to L at position 103.
+The protein's natural variant, known as in SCN1, features a modification of the amino acid from R to P at position 103.
+The protein's natural variant, known as in CH, features a modification of the amino acid from I to N at position 104.
+The protein's natural variant, known as in SCN1 and CH;, features a modification of the amino acid from I to F at position 120.
+The protein's natural variant, known as in SCN1, features a modification of the amino acid from I to N at position 120.
+The protein's natural variant, known as in SCN1, features a modification of the amino acid from I to S at position 120.
+The protein's natural variant, known as in SCN1, features a modification of the amino acid from L to P at position 121.
+The protein's natural variant, known as in SCN1, features a modification of the amino acid from L to H at position 123.
+The protein's natural variant, known as in SCN1, features a modification of the amino acid from L to PQL at position 123.
+The protein's natural variant, known as in SCN1, features a modification of the amino acid from N to I at position 124.
+The protein's natural variant, known as in SCN1 and CH;, features a modification of the amino acid from S to L at position 126.
+The protein's natural variant, known as in SCN1, features a modification of the amino acid from A to D at position 127.
+The protein's natural variant, known as in SCN1, features a modification of the amino acid from A to P at position 127.
+The protein's natural variant, known as in SCN1; unknown pathological significance;, features a modification of the amino acid from A to T at position 131.
+The protein's natural variant, known as in SCN1, features a modification of the amino acid from A to D at position 136.
+The protein's natural variant, known as in SCN1 and CH;, features a modification of the amino acid from P to L at position 139.
+The protein's natural variant, known as in SCN1, features a modification of the amino acid from P to R at position 139.
+The protein's natural variant, known as in CH; unknown pathological significance;, features a modification of the amino acid from R to H at position 143.
+The protein's natural variant, known as in SCN1;, features a modification of the amino acid from C to F at position 151.
+The protein's natural variant, known as in SCN1, features a modification of the amino acid from C to S at position 151.
+The protein's natural variant, known as in SCN1, features a modification of the amino acid from C to W at position 151.
+The protein's natural variant, known as in SCN1; unknown pathological significance;, features a modification of the amino acid from C to Y at position 151.
+The protein's natural variant, known as in SCN1, features a modification of the amino acid from L to P at position 152.
+The protein's natural variant, known as in SCN1, features a modification of the amino acid from A to D at position 153.
+The protein's natural variant, known as in SCN1, features a modification of the amino acid from A to P at position 153.
+The protein's natural variant, known as in SCN1, features a modification of the amino acid from W to C at position 156.
+The protein's natural variant, known as in SCN1, features a modification of the amino acid from W to R at position 156.
+The protein's natural variant, known as in SCN1; the patient also carries mutation Lys-116 in G6PC3;, features a modification of the amino acid from A to T at position 166.
+The protein's natural variant, known as in SCN1 and CH, features a modification of the amino acid from G to C at position 203.
+The protein's natural variant, known as in SCN1;, features a modification of the amino acid from G to R at position 203.
+The protein's natural variant, known as in SCN1;, features a modification of the amino acid from P to R at position 205.
+The protein's natural variant, known as in CH;, features a modification of the amino acid from L to F at position 206.
+The protein's natural variant, known as in SCN1, features a modification of the amino acid from L to S at position 206.
+The protein's natural variant, known as in SCN1, features a modification of the amino acid from C to G at position 208.
+The protein's natural variant, known as in CH, features a modification of the amino acid from N to I at position 209.
+The protein's natural variant, known as in SCN1, features a modification of the amino acid from G to V at position 210.
+The protein's natural variant, known as in CH, features a modification of the amino acid from G to W at position 210.
+The protein's natural variant, known as in SCN1, features a modification of the amino acid from G to E at position 214.
+The protein's natural variant, known as in SCN1;, features a modification of the amino acid from G to R at position 214.
+The protein's natural variant, known as in CH and SCN1; loss of interaction with NOTCH2NL and loss of NOTCH2NL and NOTCH2 proteolytic cleavage;, features a modification of the amino acid from R to Q at position 220.
+The protein's natural variant, known as in SCN1, features a modification of the amino acid from A to P at position 233.
+The protein's natural variant, known as in SCN1, features a modification of the amino acid from V to E at position 235.
+The protein's natural variant, known as in SCN1, features a modification of the amino acid from V to G at position 235.
+The protein's natural variant, known as found in patients with severe congenital or cyclic neutropenia;, features a modification of the amino acid from P to L at position 262.
+The protein's natural variant, known as minor, features a modification of the amino acid from D to E at position 52.
+The natural variant of this protein is characterized by an amino acid alteration from V to G at position 133.
+The protein's natural variant, known as found in a patient with Kleefstra syndrome; unknown pathological significance;, features a modification of the amino acid from F to S at position 247.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from Q to H at position 617.
+The natural variant of this protein is characterized by an amino acid alteration from R to Q at position 56.
+The natural variant of this protein is characterized by an amino acid alteration from T to S at position 340.
+The protein's natural variant, known as in DKCB3; disrupts telomerase localization to Cajal bodies resulting in misdirection of telomerase RNA to nucleoli;, features a modification of the amino acid from F to L at position 164.
+The protein's natural variant, known as in DKCB3; shortened telomeres; disrupts telomerase localization to Cajal bodies resulting in misdirection of telomerase RNA to nucleoli;, features a modification of the amino acid from H to Y at position 376.
+The protein's natural variant, known as in DKCB3; disrupts telomerase localization to Cajal bodies resulting in misdirection of telomerase RNA to nucleoli;, features a modification of the amino acid from R to W at position 398.
+The protein's natural variant, known as in DKCB3; shortened telomeres; disrupts telomerase localization to Cajal bodies resulting in misdirection of telomerase RNA to nucleoli;, features a modification of the amino acid from G to R at position 435.
+The protein's natural variant, known as in cv. Borszczagowski, features a modification of the amino acid from KYKNHLSVSAITAP to NIKTIKCKRNNRA at position 106.
+The protein's natural variant, known as in cv. Borszczagowski, features a modification of the amino acid from Q to P at position 125.
+The protein's natural variant, known as in cv. Borszczagowski, features a modification of the amino acid from Y to S at position 192.
+The protein's natural variant, known as in cv. Borszczagowski, features a modification of the amino acid from Y to C at position 225.
+The protein's natural variant, known as in cv. Borszczagowski, features a modification of the amino acid from S to P at position 317.
+The natural variant of this protein is characterized by an amino acid alteration from S to R at position 120.
+The protein's natural variant, known as in strain: YJM269, YJM270 and YJM1129, features a modification of the amino acid from N to S at position 162.
+The protein's natural variant, known as in strain: YJM269 and YJM270, features a modification of the amino acid from V to L at position 241.
+The protein's natural variant, known as in strain: YJM326, features a modification of the amino acid from E to G at position 331.
+The protein's natural variant, known as in strain: YJM269 and YJM270, features a modification of the amino acid from T to S at position 343.
+The protein's natural variant, known as in strain: YJM269, YJM270 and YJM1129, features a modification of the amino acid from T to I at position 386.
+The protein's natural variant, known as in strain: YJM269 and YJM270, features a modification of the amino acid from D to G at position 457.
+The protein's natural variant, known as in strain: YJM627, features a modification of the amino acid from S to P at position 530.
+The protein's natural variant, known as in strain: YJM627, features a modification of the amino acid from K to N at position 580.
+The protein's natural variant, known as in strain: YJM269 and YJM270, features a modification of the amino acid from A to T at position 621.
+The protein's natural variant, known as in strain: YJM627, features a modification of the amino acid from P to F at position 942.
+The protein's natural variant, known as in DSMA4; stability and intracellular location affected severely impairing the NF-kappa-B transduction pathway;, features a modification of the amino acid from F to S at position 647.
+The protein's natural variant, known as in CMTRIC; in vitro assay suggests a defect in activating the NF-kappa-B signaling pathway;, features a modification of the amino acid from T to M at position 663.
+The protein's natural variant, known as in CMTRIC; in vitro assay suggests a defect in activating the NF-kappa-B signaling pathway;, features a modification of the amino acid from G to R at position 820.
+The protein's natural variant, known as in TEBIVANED3; results in early developmental defects when expressed in zebrafish embryos, features a modification of the amino acid from K to T at position 32.
+The protein's natural variant, known as in TEBIVANED1, features a modification of the amino acid from P to A at position 33.
+The protein's natural variant, known as in TEBIVANED1, features a modification of the amino acid from P to L at position 33.
+The protein's natural variant, known as in TEBIVANED3; results in early developmental defects when expressed in zebrafish embryos, features a modification of the amino acid from P to R at position 33.
+The protein's natural variant, known as in TEBIVANED3; results in early developmental defects when expressed in zebrafish embryos, features a modification of the amino acid from R to W at position 36.
+The protein's natural variant, known as in TEBIVANED3; results in early developmental defects when expressed in zebrafish embryos, features a modification of the amino acid from L to P at position 38.
+The protein's natural variant, known as in TEBIVANED2 and TEBIVANED3; unknown pathological significance; does not affect early development when expressed in zebrafish embryos, features a modification of the amino acid from R to C at position 41.
+The protein's natural variant, known as found in a patient with a neurodevelopmental disorder; unknown pathological significance; results in early developmental defects when expressed in zebrafish embryos, features a modification of the amino acid from R to H at position 41.
+The protein's natural variant, known as in TEBIVANED4; results in early developmental defects when expressed in zebrafish embryos, features a modification of the amino acid from R to L at position 41.
+The protein's natural variant, known as in TEBIVANED3, features a modification of the amino acid from R to C at position 46.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from E to Q at position 64.
+The protein's natural variant, known as in TEBIVANED4; results in severe early developmental defects when expressed in zebrafish embryos, features a modification of the amino acid from H to R at position 76.
+The protein's natural variant, known as in TEBIVANED2; results in severe early developmental defects when expressed in zebrafish embryos, features a modification of the amino acid from K to E at position 92.
+The protein's natural variant, known as in TEBIVANED1; results in severe early developmental defects when expressed in zebrafish embryos; results in defective cell cycle progression when expressed in zebrafish embryos, features a modification of the amino acid from K to Q at position 92.
+The protein's natural variant, known as in TEBIVANED1; results in severe early developmental defects when expressed in zebrafish embryos; results in defective cell cycle progression when expressed in zebrafish embryos, features a modification of the amino acid from K to R at position 92.
+The protein's natural variant, known as found in a patient with a neurodevelopmental disorder; unknown pathological significance, features a modification of the amino acid from G to R at position 95.
+The protein's natural variant, known as in TEBIVANED3; results in early developmental defects when expressed in zebrafish embryos, features a modification of the amino acid from Y to H at position 99.
+The protein's natural variant, known as in TALDOD, features a modification of the amino acid from R to C at position 192.
+The protein's natural variant, known as in strain: EG5144, features a modification of the amino acid from Q to P at position 21.
+The protein's natural variant, known as in strain: EG5144, features a modification of the amino acid from N to D at position 97.
+The protein's natural variant, known as in strain: EG5144, features a modification of the amino acid from I to V at position 289.
+The protein's natural variant, known as in strain: EG5144, features a modification of the amino acid from F to S at position 352.
+The protein's natural variant, known as in strain: EG5144, features a modification of the amino acid from VYL to IYF at position 419.
+The protein's natural variant, known as in strain: EG5144, features a modification of the amino acid from S to G at position 451.
+The protein's natural variant, known as in strain: EG5144, features a modification of the amino acid from L to I at position 590.
+The protein's natural variant, known as in strain: EG5144, features a modification of the amino acid from K to I at position 600.
+The protein's natural variant, known as in strain: EG5144, features a modification of the amino acid from K to T at position 624.
+The protein's natural variant, known as in SIDBA2;, features a modification of the amino acid from G to E at position 130.
+The protein's natural variant, known as in SIDBA2, features a modification of the amino acid from R to H at position 134.
+The protein's natural variant, known as in SIDBA2;, features a modification of the amino acid from R to P at position 187.
+The protein's natural variant, known as in SIDBA2;, features a modification of the amino acid from D to H at position 209.
+The protein's natural variant, known as in CGD1;, features a modification of the amino acid from R to Q at position 42.
+The protein's natural variant, known as may influence susceptibility to systemic lupus erythematosus;, features a modification of the amino acid from R to H at position 90.
+The natural variant of this protein is characterized by an amino acid alteration from T to S at position 160.
+The natural variant of this protein is characterized by an amino acid alteration from K to E at position 258.
+The protein's natural variant, known as in strain: 41, features a modification of the amino acid from V to M at position 10.
+The protein's natural variant, known as in strain: 41, features a modification of the amino acid from A to T at position 59.
+The protein's natural variant, known as in strain: 41, features a modification of the amino acid from H to R at position 116.
+The protein's natural variant, known as in strain: O42B, features a modification of the amino acid from ALSR to GFPV at position 198.
+The protein's natural variant, known as display properties similar to those of the wild-type receptor;, features a modification of the amino acid from Y to H at position 192.
+The protein's natural variant, known as in BESC2; hypoactive mutation resulting in reduction of protein expression and a significant decrease of amiloride-sensitive sodium currents;, features a modification of the amino acid from F to L at position 61.
+The protein's natural variant, known as in BESC2; hyperactive mutation resulting in a significant increase of amiloride-sensitive sodium currents;, features a modification of the amino acid from V to I at position 114.
+The protein's natural variant, known as significant increase of amiloride-sensitive sodium currents;, features a modification of the amino acid from R to W at position 181.
+The protein's natural variant, known as in PHA1B1; results in a significant reduction of channel function as compared to wild-type; significantly lowers both Li+ and Na+ ion currents;, features a modification of the amino acid from G to C at position 327.
+The protein's natural variant, known as significant decrease of amiloride-sensitive sodium currents;, features a modification of the amino acid from A to T at position 334.
+The protein's natural variant, known as in LIDLS3; increased channel activity;, features a modification of the amino acid from C to R at position 479.
+The protein's natural variant, known as results in a 4-fold increase of amiloride-sensitive sodium currents; found in BESC2 patients at higher frequency than in controls; associated with an increased risk for ischemic cerebrovascular events;, features a modification of the amino acid from W to R at position 493.
+The protein's natural variant, known as in PHA1B1;, features a modification of the amino acid from S to L at position 562.
+The protein's natural variant, known as in strain: MT1131, features a modification of the amino acid from A to P at position 57.
+The protein's natural variant, known as in strain: MT1131, features a modification of the amino acid from G to R at position 66.
+The protein's natural variant, known as in strain: MT1131, features a modification of the amino acid from L to V at position 96.
+The protein's natural variant, known as in strain: MT1131, features a modification of the amino acid from N to K at position 250.
+The protein's natural variant, known as in strain: 133, features a modification of the amino acid from S to T at position 171.
+The protein's natural variant, known as in strain: 133, features a modification of the amino acid from VFA to FSP at position 191.
+The protein's natural variant, known as in GURDP; unknown pathological significance;, features a modification of the amino acid from S to P at position 111.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from H to Q at position 442.
+The protein's natural variant, known as in GURDP; unknown pathological significance;, features a modification of the amino acid from R to H at position 485.
+The protein's natural variant, known as in GURDP; decreased protein expression, if any, in platelets from homozygous patients;, features a modification of the amino acid from D to H at position 575.
+The natural variant of this protein is characterized by an amino acid alteration from F to S at position 100.
+The protein's natural variant, known as in strain: BB399V12, features a modification of the amino acid from T to P at position 706.
+The protein's natural variant, known as in strain: BB270V15, features a modification of the amino acid from E to K at position 840.
+The protein's natural variant, known as in strain: NOD and NOR, features a modification of the amino acid from E to K at position 5.
+The protein's natural variant, known as in strain: NOD and NOR, features a modification of the amino acid from R to W at position 29.
+The protein's natural variant, known as in strain: NOD and NOR, features a modification of the amino acid from E to Q at position 32.
+The protein's natural variant, known as in strain: NOD and NOR, features a modification of the amino acid from R to G at position 35.
+The protein's natural variant, known as in strain: NOD and NOR, features a modification of the amino acid from L to F at position 45.
+The protein's natural variant, known as in strain: NOD and NOR, features a modification of the amino acid from T to I at position 60.
+The protein's natural variant, known as in strain: NOD and NOR, features a modification of the amino acid from K to Q at position 79.
+The protein's natural variant, known as in strain: NOD and NOR, features a modification of the amino acid from Y to S at position 132.
+The protein's natural variant, known as in strain: NOD and NOR, features a modification of the amino acid from L to F at position 189.
+The natural variant of this protein is characterized by an amino acid alteration from M to I at position 55.
+The protein's natural variant, known as in AM, features a modification of the amino acid from R to W at position 227.
+The protein's natural variant, known as found in WKY/NCrl rat, a rat model of attention deficit hyperactive disorder. Always found associated with R-534. 2-fold increase in binding CHP1; when associated with R-534, features a modification of the amino acid from V to G at position 512.
+The protein's natural variant, known as found in WKY/NCrl rat, a rat model of attention deficit hyperactive disorder. Always found associated with G-512. 2-fold increase in binding CHP1; when associated with G-512, features a modification of the amino acid from K to R at position 534.
+The protein's natural variant, known as in LMPHM10; unknown pathological significance; results in increased lymphangiogenesis; decreased interaction with ITGA5; no effect on protein abundance; no effect on secretion; no effect on interaction with TEK;, features a modification of the amino acid from T to M at position 299.
+The protein's natural variant, known as in LMPHM10; unknown pathological significance; no effect on protein abundance; reduced secretion; reduced glycosylation; no effect on interaction with TEK;, features a modification of the amino acid from N to K at position 304.
+The protein's natural variant, known as in LMPHM10; no effect on protein abundance; mutant protein is not secreted; loss of interaction with TEK, features a modification of the amino acid from C to S at position 435.
+The protein's natural variant, known as in LMPHM10; unknown pathological significance; no effect on protein abundance; severely decreased secretion, features a modification of the amino acid from R to Q at position 492.
+The natural variant of this protein is characterized by an amino acid alteration from I to Q at position 58.
+The protein's natural variant, known as in DDD4;, features a modification of the amino acid from G to E at position 170.
+The protein's natural variant, known as in LGMDR21; reduced glucosyltransferase and xylosyltransferase activities; impaired Notch signaling;, features a modification of the amino acid from D to E at position 233.
+The protein's natural variant, known as in DDD4, features a modification of the amino acid from C to Y at position 286.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation, features a modification of the amino acid from R to I at position 503.
+The protein's natural variant, known as in IHPRF3;, features a modification of the amino acid from R to H at position 511.
+The protein's natural variant, known as in IHPRF3, features a modification of the amino acid from L to P at position 551.
+The protein's natural variant, known as in a head & Neck squamous cell carcinoma sample; somatic mutation, features a modification of the amino acid from I to V at position 806.
+The protein's natural variant, known as in strain: ZW104, features a modification of the amino acid from G to D at position 81.
+The protein's natural variant, known as in strain: ZW141, features a modification of the amino acid from A to T at position 95.
+The protein's natural variant, known as in a lung neuroendocrine carcinoma sample; somatic mutation, features a modification of the amino acid from H to Y at position 684.
+The protein's natural variant, known as in a lung small cell carcinoma sample; somatic mutation, features a modification of the amino acid from V to L at position 860.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from D to N at position 294.
+The protein's natural variant, known as increased guanidino hydrolase activity toward taurocyamine; can hydrolyze guanidinopropanoate with low efficiency; inactive toward L-arginine;, features a modification of the amino acid from G to R at position 105.
+The protein's natural variant, known as in coumermycin A1 mutant, features a modification of the amino acid from G to S at position 124.
+The protein's natural variant, known as in coumermycin A1 mutant, features a modification of the amino acid from R to Q at position 184.
+The protein's natural variant, known as in coumermycin A1 mutant, features a modification of the amino acid from T to A at position 214.
+The protein's natural variant, known as in coumermycin A1 mutant, features a modification of the amino acid from T to I at position 214.
+The protein's natural variant, known as in LADD3;, features a modification of the amino acid from C to F at position 106.
+The protein's natural variant, known as in LADD3;, features a modification of the amino acid from I to R at position 156.
+The protein's natural variant, known as in MYP27; unknown pathological significance, features a modification of the amino acid from D to Y at position 1275.
+The protein's natural variant, known as in strain: CC-503, features a modification of the amino acid from T to A at position 8.
+The protein's natural variant, known as associated with susceptibility to SLE; associated with resistance to malaria; found at an increased frequency in African and Asian populations from areas where malaria is endemic; enhances phagocytosis of Plasmodium falciparum-infected erythrocytes in vitro;, features a modification of the amino acid from I to T at position 232.
+The protein's natural variant, known as in LQT15; reduction in calcium affinity; highly decreased calcium-dependent inactivation of L-type calcium channel; increased action potential duration; not changed protein abundance; not changed structure; increased thermal stability in absence of calcium; decreased thermal stability in presence of calcium; significantly increased RYR2 interaction; increased ryanodine-sensitive calcium-release channel activity; decreased of KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane;, features a modification of the amino acid from D to V at position 96.
+The protein's natural variant, known as in LQT15; reduction in calcium affinity;, features a modification of the amino acid from N to I at position 98.
+The protein's natural variant, known as in LQT15; the mutant has significantly reduced calcium affinity compared to wild-type; calmodulin-RYR2 interaction is defective at low intracellular Ca(2+) concentrations and restored at moderate to high Ca(2+) concentrations; increased RYR2 calcium-release channel activity; decreased calcium-dependent inactivation of L-type calcium channel; not changed protein abundance; not changed structure; significantly reduced ryanodine-sensitive calcium-release channel activity; decreased of KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane;, features a modification of the amino acid from N to S at position 98.
+The protein's natural variant, known as in LQT15; reduction in calcium affinity; not changed protein abundance; not changed structure; significantly decreased thermal stability in presence of calcium; significantly decreased RYR2 interaction; increased ryanodine-sensitive calcium-release channel activity; decreased of KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane;, features a modification of the amino acid from D to G at position 130.
+The protein's natural variant, known as in LQT15, features a modification of the amino acid from D to V at position 130.
+The protein's natural variant, known as in LQT15; reduction in calcium affinity;, features a modification of the amino acid from D to E at position 132.
+The protein's natural variant, known as in LQT15; reduction in calcium affinity;, features a modification of the amino acid from D to H at position 134.
+The protein's natural variant, known as in LQT15; reduction in calcium affinity;, features a modification of the amino acid from Q to P at position 136.
+The natural variant of this protein is characterized by an amino acid alteration from G to S at position 601.
+The protein's natural variant, known as in DEE61; unknown pathological significance; loss of interaction with LGI1; no effect on DLG4-binding, nor on subcellular location;, features a modification of the amino acid from C to Y at position 401.
+The protein's natural variant, known as found in a case of cancer of unknown primary origin; the mutated receptor is still functional and can sustain the transformed phenotype; somatic mutation;, features a modification of the amino acid from H to Y at position 150.
+The protein's natural variant, known as found in a case of cancer of unknown primary origin; the mutated receptor is still functional and can sustain the transformed phenotype; somatic mutation;, features a modification of the amino acid from E to D at position 168.
+The protein's natural variant, known as found in lung cancer also including cases carrying EGFR mutations; unknown pathological significance; decreased hepatocyte growth factor-activated receptor activity; decreased interaction with HGF;, features a modification of the amino acid from N to K at position 375.
+The protein's natural variant, known as found in a case of cancer of unknown primary origin; the mutated receptor is still functional and can sustain the transformed phenotype; somatic mutation;, features a modification of the amino acid from C to Y at position 385.
+The protein's natural variant, known as in gastric cancer;, features a modification of the amino acid from P to L at position 773.
+The protein's natural variant, known as in DFNB97;, features a modification of the amino acid from F to V at position 841.
+The protein's natural variant, known as in gastric cancer; prolonged tyrosine phosphorylation in response to HGF/SF; transforming activity in athymic nude mice;, features a modification of the amino acid from P to S at position 991.
+The protein's natural variant, known as found in a case of cancer of unknown primary origin; the mutated receptor is still functional and can sustain the transformed phenotype; somatic mutation;, features a modification of the amino acid from T to I at position 992.
+The protein's natural variant, known as probable disease-associated variant found in lesional sample from a patient with sporadically occurring, unilateral osteofibrous dysplasia; somatic mutation; complete loss of ligand-induced CBL-mediated ubiquitination, resulting in protein stabilization, features a modification of the amino acid from Y to S at position 1003.
+The protein's natural variant, known as in RCCP; constitutive autophosphorylation;, features a modification of the amino acid from V to I at position 1092.
+The protein's natural variant, known as in RCCP; constitutive autophosphorylation; causes malignant transformation in cell lines, features a modification of the amino acid from H to L at position 1094.
+The protein's natural variant, known as in RCCP; causes malignant transformation in cell lines;, features a modification of the amino acid from H to R at position 1094.
+The protein's natural variant, known as in RCCP; constitutive autophosphorylation; causes malignant transformation in cell lines;, features a modification of the amino acid from H to Y at position 1094.
+The protein's natural variant, known as in RCCP; constitutive autophosphorylation; causes malignant transformation in cell lines, features a modification of the amino acid from H to D at position 1106.
+The protein's natural variant, known as in RCCP; germline mutation;, features a modification of the amino acid from M to T at position 1131.
+The protein's natural variant, known as in HCC;, features a modification of the amino acid from T to I at position 1173.
+The protein's natural variant, known as in RCCP; germline mutation;, features a modification of the amino acid from V to L at position 1188.
+The protein's natural variant, known as in RCCP; somatic mutation;, features a modification of the amino acid from L to V at position 1195.
+The protein's natural variant, known as in RCCP; germline mutation;, features a modification of the amino acid from V to I at position 1220.
+The protein's natural variant, known as in RCCP; somatic mutation;, features a modification of the amino acid from D to H at position 1228.
+The protein's natural variant, known as in RCCP; germline mutation;, features a modification of the amino acid from D to N at position 1228.
+The protein's natural variant, known as in RCCP; germline mutation;, features a modification of the amino acid from Y to C at position 1230.
+The protein's natural variant, known as in RCCP; constitutive autophosphorylation; causes malignant transformation in cell lines, features a modification of the amino acid from Y to D at position 1230.
+The protein's natural variant, known as in RCCP; somatic mutation;, features a modification of the amino acid from Y to H at position 1230.
+The protein's natural variant, known as in DA11; not phosphorylated in reponse to HGF; severely decreased tyrosin kinase activity;, features a modification of the amino acid from Y to C at position 1234.
+The protein's natural variant, known as in HCC;, features a modification of the amino acid from K to R at position 1244.
+The protein's natural variant, known as in HCC;, features a modification of the amino acid from M to I at position 1250.
+The protein's natural variant, known as in RCCP; somatic mutation;, features a modification of the amino acid from M to T at position 1250.
+The protein's natural variant, known as found in a case of cancer of unknown primary origin; the mutated receptor is still functional and can sustain the transformed phenotype; somatic mutation;, features a modification of the amino acid from V to I at position 1294.
+The protein's natural variant, known as in HIES2;, features a modification of the amino acid from K to R at position 473.
+The natural variant of this protein is characterized by an amino acid alteration from M to I at position 98.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from R to G at position 955.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from D to N at position 202.
+The natural variant of this protein is characterized by an amino acid alteration from G to A at position 110.
+The natural variant of this protein is characterized by an amino acid alteration from TV to YI at position 59.
+The protein's natural variant, known as in strain: HF116, features a modification of the amino acid from A to G at position 50.
+The protein's natural variant, known as in strain: HF116, features a modification of the amino acid from G to A at position 57.
+The protein's natural variant, known as in strain: HF116, features a modification of the amino acid from V to T at position 60.
+The protein's natural variant, known as in strain: HF116, features a modification of the amino acid from A to T at position 65.
+The protein's natural variant, known as in strain: HF116, features a modification of the amino acid from L to W at position 100.
+The protein's natural variant, known as in strain: cv. Kas-0, features a modification of the amino acid from R to S at position 78.
+The protein's natural variant, known as in strain: cv. Bu-0, features a modification of the amino acid from Y to H at position 114.
+The protein's natural variant, known as in strain: cv. Bretagny, features a modification of the amino acid from E to G at position 120.
+The protein's natural variant, known as in strain: cv. Kas-0, features a modification of the amino acid from M to K at position 122.
+The protein's natural variant, known as in strain: cv. Bu-0, features a modification of the amino acid from I to T at position 141.
+The protein's natural variant, known as in strain: cv. Kent, features a modification of the amino acid from K to E at position 161.
+The protein's natural variant, known as in strain: cv. Kent and cv. Wassilewskija, features a modification of the amino acid from E to K at position 176.
+The protein's natural variant, known as in strain: cv. Bu-0, cv. Landsberg erecta, cv. Li-8 and cv. NL2, features a modification of the amino acid from R to K at position 182.
+The protein's natural variant, known as in strain: cv. NL2, features a modification of the amino acid from K to R at position 184.
+The protein's natural variant, known as in strain: cv. Wassilewskija, features a modification of the amino acid from T to I at position 186.
+The protein's natural variant, known as in strain: cv. Co-1, features a modification of the amino acid from V to I at position 195.
+The protein's natural variant, known as in strain: cv. Kent, features a modification of the amino acid from D to N at position 196.
+The protein's natural variant, known as in strain: cv. Bu-2, features a modification of the amino acid from Q to QL at position 205.
+The protein's natural variant, known as in strain: cv. Li-3, features a modification of the amino acid from L to F at position 209.
+The protein's natural variant, known as in strain: cv. Bla-1, cv. Bretagny, cv. Bs-0, cv. Bu-0, cv. Bu-2, cv. Co-1, cv. Kas-0, cv. Kent, cv. Landsberg erecta, cv. Li-3, cv. Li-8, cv. Nd-0, cv. NL2 and cv. Wassilewskija, features a modification of the amino acid from E to G at position 228.
+The protein's natural variant, known as in strain: cv. Bu-2, features a modification of the amino acid from N to D at position 238.
+The protein's natural variant, known as in strain: cv. NL2, features a modification of the amino acid from Y to C at position 249.
+The protein's natural variant, known as in DYT24;, features a modification of the amino acid from W to C at position 490.
+The protein's natural variant, known as in DYT24;, features a modification of the amino acid from R to W at position 494.
+The protein's natural variant, known as in DYT24;, features a modification of the amino acid from S to G at position 685.
+The protein's natural variant, known as in DYT24;, features a modification of the amino acid from K to N at position 862.
+The protein's natural variant, known as in a lung neuroendocrine carcinoma sample; somatic mutation;, features a modification of the amino acid from P to S at position 333.
+The protein's natural variant, known as in a lung large cell carcinoma sample; somatic mutation, features a modification of the amino acid from P to T at position 411.
+The protein's natural variant, known as in PPA-10; quinolone-resistant, features a modification of the amino acid from A to S at position 67.
+The protein's natural variant, known as in NAL-97; quinolone-resistant, features a modification of the amino acid from G to C at position 81.
+The protein's natural variant, known as in NAL-51, NAL-112, NAL-118, NAL-119 and strains 58, 158, 218, 231 and 235; quinolone-resistant, features a modification of the amino acid from S to L at position 83.
+The protein's natural variant, known as in PPA-18 and strains 233 and 227; quinolone-resistant, features a modification of the amino acid from S to W at position 83.
+The protein's natural variant, known as in PPA-05; quinolone-resistant, features a modification of the amino acid from A to P at position 84.
+The protein's natural variant, known as in NAL-113 and OV6; quinolone-resistant, features a modification of the amino acid from D to N at position 87.
+The protein's natural variant, known as in strain: 202; partially quinolone-resistant, features a modification of the amino acid from D to V at position 87.
+The protein's natural variant, known as in NAL-89; quinolone-resistant, features a modification of the amino acid from Q to H at position 106.
+The protein's natural variant, known as in strain: 227, features a modification of the amino acid from D to E at position 678.
+The protein's natural variant, known as in strain: OV6; quinolone-resistant, features a modification of the amino acid from I to IMMI at position 798.
+The protein's natural variant, known as in strain: 227, features a modification of the amino acid from A to S at position 828.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from E to V at position 85.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from A to S at position 273.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from N to K at position 347.
+The protein's natural variant, known as may influence susceptibility to juvenile rheumatoid arthritis; increased adenosine deaminase activity and decreased adenosine phosphorylase activity; reduced ability to promote pattern recognition receptor (PRR)-induced cytokines; reduced NOD2-induced signaling; does not change interaction with FASN;, features a modification of the amino acid from I to V at position 254.
+The protein's natural variant, known as in JUVAR; unknown pathological significance, features a modification of the amino acid from A to P at position 278.
+The protein's natural variant, known as in JUVAR; reduced NOD2-induced signaling;, features a modification of the amino acid from C to R at position 284.
+The protein's natural variant, known as in PEE5;, features a modification of the amino acid from K to E at position 317.
+The protein's natural variant, known as in PEE5;, features a modification of the amino acid from S to G at position 472.
+The natural variant of this protein is characterized by an amino acid alteration from R to H at position 535.
+The protein's natural variant, known as in a renal papillary sample; somatic mutation, features a modification of the amino acid from L to F at position 16.
+The protein's natural variant, known as in EKVP1;, features a modification of the amino acid from G to D at position 12.
+The protein's natural variant, known as in EKVP1;, features a modification of the amino acid from G to R at position 12.
+The protein's natural variant, known as in EKVP1;, features a modification of the amino acid from R to P at position 42.
+The protein's natural variant, known as in EKVP1;, features a modification of the amino acid from C to S at position 86.
+The protein's natural variant, known as in EKVP1, features a modification of the amino acid from F to L at position 137.
+The protein's natural variant, known as in DFNA2B;, features a modification of the amino acid from I to V at position 141.
+The protein's natural variant, known as in DFNA2B; unknown pathological significance;, features a modification of the amino acid from E to K at position 183.
+The protein's natural variant, known as in strain: M1-106, features a modification of the amino acid from R to K at position 84.
+The protein's natural variant, known as in strain: B-3501, features a modification of the amino acid from K to R at position 222.
+The protein's natural variant, known as in strain: B-3501, features a modification of the amino acid from D to S at position 231.
+The protein's natural variant, known as in strain: B-3501 and M1-106, features a modification of the amino acid from IE to SR at position 234.
+The protein's natural variant, known as in strain: B-3501, features a modification of the amino acid from P to H at position 236.
+The protein's natural variant, known as in strain: M1-106, features a modification of the amino acid from A to S at position 371.
+The protein's natural variant, known as in strain: M1-106, features a modification of the amino acid from A to S at position 404.
+The protein's natural variant, known as in strain: M1-106, features a modification of the amino acid from DKTEKG to EKSDGKS at position 445.
+The protein's natural variant, known as in allotype C4A3a, allotype C4A6;, features a modification of the amino acid from S to Y at position 347.
+The protein's natural variant, known as in allotype C4A4, features a modification of the amino acid from V to A at position 418.
+The protein's natural variant, known as in allotype C4A6, features a modification of the amino acid from R to W at position 477.
+The protein's natural variant, known as in allotype C4A3a;, features a modification of the amino acid from P to L at position 726.
+The natural variant of this protein is characterized by an amino acid alteration from D to N at position 727.
+The protein's natural variant, known as in allotype C4A1, allotype C4A2;, features a modification of the amino acid from D to G at position 1073.
+The protein's natural variant, known as in allotype C4A1;, features a modification of the amino acid from N to S at position 1176.
+The protein's natural variant, known as in allotype C4A4, features a modification of the amino acid from T to S at position 1201.
+The protein's natural variant, known as in allotype C4A1, allotype C4A13;, features a modification of the amino acid from V to A at position 1207.
+The protein's natural variant, known as in allotype C4A1, allotype C4A13;, features a modification of the amino acid from L to R at position 1210.
+The protein's natural variant, known as in allotype C4A1, allotype C4A3a, allotype C4A6;, features a modification of the amino acid from S to A at position 1286.
+The protein's natural variant, known as in some primary melanomas and melanoma cell lines, features a modification of the amino acid from P to L at position 126.
+The protein's natural variant, known as in HMN9; decreased tryptophan-tRNA ligase activity; dominant negative effect; decreased general protein synthesis; decreased cell viability; no effect on homodimerization, features a modification of the amino acid from H to R at position 257.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from E to D at position 455.
+The protein's natural variant, known as in SCA49; results in motor and sensory impairments when expressed in zebrafish, features a modification of the amino acid from S to L at position 626.
+The protein's natural variant, known as in ATXPC and M7MLS1;, features a modification of the amino acid from H to Q at position 880.
+The protein's natural variant, known as in M7MLS1, features a modification of the amino acid from R to C at position 986.
+The protein's natural variant, known as in ATXPC; unknown pathological significance;, features a modification of the amino acid from C to S at position 1196.
+The protein's natural variant, known as in M7MLS1, features a modification of the amino acid from R to K at position 1281.
+The protein's natural variant, known as in M7MLS1, features a modification of the amino acid from V to A at position 1512.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from S to F at position 254.
+The natural variant of this protein is characterized by an amino acid alteration from F to L at position 206.
+The protein's natural variant, known as associated with exfoliation syndrome in the presence of D-153;, features a modification of the amino acid from R to L at position 141.
+The protein's natural variant, known as associated with exfoliation syndrome in the presence of L-141;, features a modification of the amino acid from G to D at position 153.
+The protein's natural variant, known as in EDSPD2;, features a modification of the amino acid from C to R at position 294.
+The natural variant of this protein is characterized by an amino acid alteration from L to V at position 130.
+The protein's natural variant, known as in COXPD45; MRPL12 steady state level are reduced in patient fibroblasts; results in defective mt-LSU assembly; reduced mitochondrial translation with a significant decrease of synthesis of COXI, COXII and COXIII subunits;, features a modification of the amino acid from A to V at position 181.
+The protein's natural variant, known as in strain: C57BL/6J, features a modification of the amino acid from A to E at position 319.
+The protein's natural variant, known as in strain: C57BL/6J, features a modification of the amino acid from G to D at position 346.
+The protein's natural variant, known as in allele 6M1-3*02; decreased response to C3HEX;, features a modification of the amino acid from T to A at position 113.
+The protein's natural variant, known as in allele 6M1-3*02; decreased response to C3HEX;, features a modification of the amino acid from R to Q at position 226.
+The protein's natural variant, known as in allele 6M1-3*03;, features a modification of the amino acid from V to I at position 228.
+The protein's natural variant, known as in allele 6M1-3*03 and allele 6M1-3*04;, features a modification of the amino acid from I to M at position 261.
+The protein's natural variant, known as requires 2 nucleotide substitutions;, features a modification of the amino acid from P to I at position 252.
+The protein's natural variant, known as in a mutant strain; shows symptoms similar to the motor neuron disease, agrin-associated congenital myasthenic syndrome (CMS) with progressive degradation of the neuromuscular junction, decreased acetylcholine receptor (AChR) density and increased subsynaptic reticulum. Synapses eventually denervate and muscles atrophy. There is decreased glycosylation and proteolytic processing is altered due to changes in sensitivity to neurotrypsin, features a modification of the amino acid from F to S at position 1061.
+The protein's natural variant, known as in BDPLT18; prevents Rap1 activation upon calcium stimulation; reduces platelet adhesion and spreading;, features a modification of the amino acid from G to W at position 248.
+The protein's natural variant, known as in BDPLT18; lack of mutant protein in platelets from a patient homozygous for the mutation, features a modification of the amino acid from C to Y at position 296.
+The protein's natural variant, known as in BDPLT18, features a modification of the amino acid from G to D at position 305.
+The protein's natural variant, known as in BDPLT18; loss of guanyl-nucleotide exchange factor activity;, features a modification of the amino acid from S to F at position 381.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to H at position 215.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from R to Q at position 352.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from D to H at position 391.
+The natural variant of this protein is characterized by an amino acid alteration from L to F at position 18.
+The natural variant of this protein is characterized by an amino acid alteration from I to N at position 787.
+The protein's natural variant, known as found in a renal cell carcinoma sample; somatic mutation;, features a modification of the amino acid from V to M at position 216.
+The natural variant of this protein is characterized by an amino acid alteration from D to E at position 360.
+The natural variant of this protein is characterized by an amino acid alteration from C to S at position 1041.
+The protein's natural variant, known as in HHF2;, features a modification of the amino acid from R to H at position 34.
+The protein's natural variant, known as in PNDM2;, features a modification of the amino acid from F to L at position 35.
+The protein's natural variant, known as in PNDM2;, features a modification of the amino acid from F to V at position 35.
+The protein's natural variant, known as in HHF2;, features a modification of the amino acid from G to D at position 40.
+The protein's natural variant, known as in TNDM3; increased spontaneous open probability; reduced ATP sensitivity; reduced expression at the cell surface of the functional ATP-sensitive form;, features a modification of the amino acid from C to R at position 42.
+The protein's natural variant, known as in PNDM2, features a modification of the amino acid from H to Y at position 46.
+The protein's natural variant, known as in PNDM2; decreased inhibition by ATP; enhanced activation by Mg(2+); increased current;, features a modification of the amino acid from R to P at position 50.
+The protein's natural variant, known as in PNDM2; decreased inhibition by ATP; enhanced activation by Mg(2+); increased current;, features a modification of the amino acid from R to Q at position 50.
+The protein's natural variant, known as in PNDM2; with neurologic features; produces larger current and more change in ATP sensitivity than mutation associated with mild disease C-201;, features a modification of the amino acid from Q to R at position 52.
+The protein's natural variant, known as in PNDM2; with neurologic features;, features a modification of the amino acid from G to D at position 53.
+The protein's natural variant, known as in TNDM3; reduction in the sensitivity to ATP when compared with wild-type;, features a modification of the amino acid from G to R at position 53.
+The protein's natural variant, known as in TNDM3; reduction in the sensitivity to ATP when compared with wild-type;, features a modification of the amino acid from G to S at position 53.
+The protein's natural variant, known as in HHF2; does neither affect channel expression nor channel response to MgADP;, features a modification of the amino acid from F to L at position 55.
+The protein's natural variant, known as in PNDM2; with neurologic features; produces larger current and more change in ATP sensitivity than mutation associated with mild disease C-201; decreases ATP sensitivity indirectly by favoring the open conformation of the channel;, features a modification of the amino acid from V to G at position 59.
+The protein's natural variant, known as in PNDM2; with neurologic features;, features a modification of the amino acid from V to M at position 59.
+The protein's natural variant, known as in PNDM2; found in a patient who also carries L-64 in cis; thought to be the pathogenic mutation in this double allele; displays gain of function; increases the intrinsic channel open probability and decreases sensitivity toward ATP inhibition; variant L-64 associated in cis is thought to ameliorate the effect of the Y-60 mutation on the channel ATP sensitivity;, features a modification of the amino acid from F to Y at position 60.
+The protein's natural variant, known as in PNDM2; found in a patient who also carries Y-60 in cis; unknown pathological significance; only subtle effects, if any, on channel ATP sensitivity; thought to attenuate the deleterious effect of the Y-60 mutation associated in cis on the channel ATP sensitivity;, features a modification of the amino acid from V to L at position 64.
+The protein's natural variant, known as in HHF2;, features a modification of the amino acid from K to N at position 67.
+The protein's natural variant, known as in HHF2, features a modification of the amino acid from W to R at position 91.
+The protein's natural variant, known as in HHF2;, features a modification of the amino acid from A to D at position 101.
+The protein's natural variant, known as in HHF2;, features a modification of the amino acid from S to P at position 116.
+The protein's natural variant, known as in HHF2, features a modification of the amino acid from G to A at position 134.
+The protein's natural variant, known as in HHF2;, features a modification of the amino acid from R to L at position 136.
+The protein's natural variant, known as in HHF2;, features a modification of the amino acid from L to P at position 147.
+The natural variant of this protein is characterized by an amino acid alteration from I to S at position 148.
+The protein's natural variant, known as in HHF2;, features a modification of the amino acid from G to R at position 156.
+The protein's natural variant, known as in PNDM2, features a modification of the amino acid from L to P at position 164.
+The protein's natural variant, known as in PNDM2; individual also diagnosed with West syndrome;, features a modification of the amino acid from C to Y at position 166.
+The protein's natural variant, known as in PNDM2; has severely impaired sensitivity to ATP and markedly increases open channel probability;, features a modification of the amino acid from I to L at position 167.
+The protein's natural variant, known as in PNDM2;, features a modification of the amino acid from K to N at position 170.
+The protein's natural variant, known as in PNDM2;, features a modification of the amino acid from K to R at position 170.
+The protein's natural variant, known as in PNDM2, features a modification of the amino acid from K to T at position 170.
+The protein's natural variant, known as in TNDM3; reduction in the sensitivity to ATP when compared with wild-type;, features a modification of the amino acid from I to V at position 182.
+The protein's natural variant, known as in PNDM2; with neurologic features; produces smaller current and less change in ATP sensitivity than mutations associated with severe disease R-52 and G-59;, features a modification of the amino acid from R to C at position 201.
+The protein's natural variant, known as in PNDM2; ability of ATP to block mutant channels greatly reduced;, features a modification of the amino acid from R to H at position 201.
+The protein's natural variant, known as in PNDM2;, features a modification of the amino acid from R to L at position 201.
+The protein's natural variant, known as in HHF2;, features a modification of the amino acid from D to E at position 204.
+The protein's natural variant, known as in MODY13;, features a modification of the amino acid from E to K at position 227.
+The protein's natural variant, known as in HHF2; impairs trafficking of the mutant channel;, features a modification of the amino acid from P to L at position 254.
+The protein's natural variant, known as in HHF2; impairs trafficking and abolishes channel function;, features a modification of the amino acid from H to R at position 259.
+The protein's natural variant, known as in HHF2;, features a modification of the amino acid from P to L at position 266.
+The protein's natural variant, known as in HHF2; prevents the ER export and surface expression of the channel;, features a modification of the amino acid from E to K at position 282.
+The protein's natural variant, known as in PNDM2; with neurologic features;, features a modification of the amino acid from I to L at position 296.
+The protein's natural variant, known as in HHF2;, features a modification of the amino acid from R to H at position 301.
+The protein's natural variant, known as in PNDM2;, features a modification of the amino acid from E to K at position 322.
+The protein's natural variant, known as in PNDM2;, features a modification of the amino acid from Y to C at position 330.
+The protein's natural variant, known as in PNDM2, features a modification of the amino acid from Y to S at position 330.
+The protein's natural variant, known as in PNDM2; alters gating characteristics; decreases sensitivity to inhibition by ATP and increases intrinsic open probability;, features a modification of the amino acid from F to I at position 333.
+The protein's natural variant, known as in NIDDM; Afro-Caribbean;, features a modification of the amino acid from L to P at position 355.
+The protein's natural variant, known as in NIDDM, features a modification of the amino acid from P to PKP at position 380.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from S to C at position 8.
+The protein's natural variant, known as in strain: 1479, features a modification of the amino acid from R to H at position 6.
+The protein's natural variant, known as in strain: 1479, features a modification of the amino acid from V to I at position 14.
+The protein's natural variant, known as in strain: 1479, features a modification of the amino acid from VGS to ITH at position 19.
+The protein's natural variant, known as in strain: 1479, features a modification of the amino acid from A to V at position 21.
+The protein's natural variant, known as in strain: 1479, features a modification of the amino acid from R to H at position 79.
+The protein's natural variant, known as in strain: 1479, features a modification of the amino acid from T to A at position 129.
+The protein's natural variant, known as in strain: 1479, features a modification of the amino acid from A to G at position 160.
+The protein's natural variant, known as in strain: 1479, features a modification of the amino acid from A to T at position 237.
+The protein's natural variant, known as in strain: 1479, features a modification of the amino acid from S to N at position 322.
+The protein's natural variant, known as in strain: 1479, features a modification of the amino acid from A to V at position 326.
+The protein's natural variant, known as in strain: 1479, features a modification of the amino acid from A to S at position 328.
+The protein's natural variant, known as in NEDDFSA; leads to altered positioning of pyramidal neurons;, features a modification of the amino acid from K to R at position 91.
+The protein's natural variant, known as in NEDDFSA; unknown pathological significance, features a modification of the amino acid from A to T at position 287.
+The protein's natural variant, known as in NEDDFSA, features a modification of the amino acid from T to I at position 296.
+The protein's natural variant, known as in NEDDFSA;, features a modification of the amino acid from T to K at position 296.
+The protein's natural variant, known as in NEDDFSA;, features a modification of the amino acid from T to I at position 298.
+The protein's natural variant, known as in NEDDFSA; leads to altered positioning of pyramidal neurons; decreased transcription coactivator activity; does not affect nuclear localization;, features a modification of the amino acid from T to M at position 300.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from L to V at position 551.
+The protein's natural variant, known as probable disease-associated variant found in a patient with infantile onset epileptic encephalopathy and autism spectrum disorder, features a modification of the amino acid from S to R at position 36.
+The protein's natural variant, known as probable disease-associated variant found in a patient with infantile onset epileptic encephalopathy and autism spectrum disorder;, features a modification of the amino acid from C to R at position 39.
+The natural variant of this protein is characterized by an amino acid alteration from T to I at position 236.
+The protein's natural variant, known as in IMD20; loss of interaction with CD2;, features a modification of the amino acid from L to H at position 66.
+The protein's natural variant, known as shows a higher binding capacity for IgG1, IgG3 and IgG4;, features a modification of the amino acid from F to V at position 176.
+The protein's natural variant, known as enables membrane anchoring via glycosylphosphatidylinositol; disrupts transmembrane anchoring;, features a modification of the amino acid from F to S at position 203.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from V to L at position 181.
+The protein's natural variant, known as found in a patient with congenital cataract;, features a modification of the amino acid from E to K at position 41.
+The protein's natural variant, known as in BOR1, features a modification of the amino acid from P to S at position 95.
+The protein's natural variant, known as in BOR1, features a modification of the amino acid from G to S at position 140.
+The protein's natural variant, known as in BOS1;, features a modification of the amino acid from S to G at position 242.
+The protein's natural variant, known as in ASA;, features a modification of the amino acid from E to K at position 363.
+The protein's natural variant, known as in BOR1, features a modification of the amino acid from E to V at position 363.
+The protein's natural variant, known as in BOR1; with cataract;, features a modification of the amino acid from G to S at position 426.
+The protein's natural variant, known as in BOR1, features a modification of the amino acid from D to G at position 429.
+The protein's natural variant, known as in BOR1;, features a modification of the amino acid from R to Q at position 440.
+The protein's natural variant, known as in BOR1;, features a modification of the amino acid from S to P at position 487.
+The protein's natural variant, known as in BOR1;, features a modification of the amino acid from L to R at position 505.
+The protein's natural variant, known as in BOR1;, features a modification of the amino acid from L to P at position 514.
+The protein's natural variant, known as in BOR1, features a modification of the amino acid from Y to C at position 527.
+The protein's natural variant, known as in ASA; with cataract;, features a modification of the amino acid from R to G at position 547.
+The protein's natural variant, known as in BOR1, features a modification of the amino acid from M to T at position 569.
+The protein's natural variant, known as in BOR1;, features a modification of the amino acid from L to P at position 583.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from T to A at position 1186.
+The protein's natural variant, known as in JBTS27;, features a modification of the amino acid from Y to C at position 32.
+The protein's natural variant, known as in JBTS27;, features a modification of the amino acid from R to Q at position 156.
+The protein's natural variant, known as in LMPHM12; unknown pathological significance, features a modification of the amino acid from F to L at position 244.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from S to L at position 1306.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from A to T at position 1445.
+The protein's natural variant, known as found in a renal cell carcinoma sample; somatic mutation, features a modification of the amino acid from Q to K at position 1566.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from V to M at position 1598.
+The protein's natural variant, known as found in a patient with a neurodevelopmental disorder; unknown pathological significance;, features a modification of the amino acid from N to S at position 441.
+The protein's natural variant, known as found in a patient with a neurodevelopmental disorder; unknown pathological significance;, features a modification of the amino acid from R to P at position 776.
+The protein's natural variant, known as in strain: Guyane 11, features a modification of the amino acid from H to R at position 152.
+The protein's natural variant, known as in strain: Guyane 11, features a modification of the amino acid from D to G at position 263.
+The protein's natural variant, known as in CSNBAD3;, features a modification of the amino acid from G to D at position 38.
+The protein's natural variant, known as in CSNB1G;, features a modification of the amino acid from D to G at position 129.
+The protein's natural variant, known as in CSNBAD3;, features a modification of the amino acid from Q to E at position 200.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from V to I at position 90.
+The protein's natural variant, known as in MCOPS12; increased transcriptional response to retinoic acid ligands, features a modification of the amino acid from L to P at position 220.
+The protein's natural variant, known as in MCOPS12; increased transcriptional response to retinoic acid ligands, features a modification of the amino acid from G to A at position 303.
+The protein's natural variant, known as in MCOPS12; increased transcriptional response to retinoic acid ligands, features a modification of the amino acid from R to C at position 394.
+The protein's natural variant, known as in MCOPS12; increases transcriptional response to retinoic acid, features a modification of the amino acid from R to S at position 394.
+The natural variant of this protein is characterized by an amino acid alteration from R to K at position 152.
+The protein's natural variant, known as decreased transport activity;, features a modification of the amino acid from P to T at position 155.
+The protein's natural variant, known as decreased transport activity;, features a modification of the amino acid from E to G at position 156.
+The protein's natural variant, known as decreased transport activity;, features a modification of the amino acid from V to A at position 174.
+The protein's natural variant, known as strongly decreases expression at the plasma membrane; abolishes transport activity;, features a modification of the amino acid from L to R at position 193.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation, features a modification of the amino acid from Q to R at position 2.
+The protein's natural variant, known as in a renal clear cell carcinoma sample; somatic mutation, features a modification of the amino acid from A to G at position 248.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from R to L at position 275.
+The protein's natural variant, known as in HCI; associated with disease susceptibility; expression of FLT1 in hemangioma endothelial cells is markedly reduced and KDR activity is increased compared to controls; low FLT1 expression in hemangioma cells is caused by reduced activity of a pathway involving ITGB1, ANTXR1, KDR and NFATC2IP; the mutation predicts to result in loss-of-function and disruption of the normal association of these molecules;, features a modification of the amino acid from C to R at position 482.
+The protein's natural variant, known as strongly reduced autophosphorylation and kinase activity;, features a modification of the amino acid from V to E at position 848.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from G to R at position 873.
+The protein's natural variant, known as in HCI; somatic mutation;, features a modification of the amino acid from P to S at position 1147.
+The protein's natural variant, known as in lst; abolishes DNA binding and transcriptional activation, features a modification of the amino acid from R to Q at position 206.
+The natural variant of this protein is characterized by an amino acid alteration from D to E at position 79.
+The natural variant of this protein is characterized by an amino acid alteration from Y to F at position 100.
+The protein's natural variant, known as in strain: cv. Little Marvel, features a modification of the amino acid from A to W at position 35.
+The protein's natural variant, known as found in parathyroid adenoma samples; somatic mutation; parathyroid adenoma samples are from a patient with isolated hyperparathyroidism who also carries germline mutation P-91, features a modification of the amino acid from A to S at position 2.
+The protein's natural variant, known as found in a clear cell renal carcinoma sample; somatic mutation; unlike wild-type protein the mutant is defective in suppressing CCND1 expression in vivo, features a modification of the amino acid from K to Q at position 34.
+The protein's natural variant, known as found in a parathyroid carcinoma sample; somatic mutation, features a modification of the amino acid from S to F at position 59.
+The protein's natural variant, known as in HRPT1; unknown pathological significance;, features a modification of the amino acid from L to P at position 63.
+The protein's natural variant, known as in HRPT1; does not affect interaction with the Pfa1 complex;, features a modification of the amino acid from L to P at position 64.
+The protein's natural variant, known as found in a patient with isolated hyperparathyroidism and parathyroid adenomas, features a modification of the amino acid from R to P at position 91.
+The protein's natural variant, known as in HRPT1; unknown pathological significance; found as somatic mutation in a parathyroid adenoma sample from a patient who also carries a germline frameshift mutation, features a modification of the amino acid from L to P at position 95.
+The protein's natural variant, known as found in a parathyroid adenoma sample;, features a modification of the amino acid from N to S at position 272.
+The protein's natural variant, known as found in a Wilms tumor sample; somatic mutation, features a modification of the amino acid from R to K at position 292.
+The protein's natural variant, known as in HRPT2;, features a modification of the amino acid from D to N at position 379.
+The protein's natural variant, known as in GA2A; impaired protein stability and loss of electron transfer activity;, features a modification of the amino acid from G to R at position 116.
+The protein's natural variant, known as in GA2A;, features a modification of the amino acid from V to G at position 157.
+The protein's natural variant, known as decreased protein stability;, features a modification of the amino acid from T to I at position 171.
+The protein's natural variant, known as in GA2A; decreased electron transfer activity;, features a modification of the amino acid from T to M at position 266.
+The natural variant of this protein is characterized by an amino acid alteration from S to T at position 170.
+The natural variant of this protein is characterized by an amino acid alteration from A to V at position 221.
+The natural variant of this protein is characterized by an amino acid alteration from P to H at position 282.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from D to N at position 360.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from A to P at position 603.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from R to Q at position 719.
+The protein's natural variant, known as in an ovarian mucinous carcinoma sample; somatic mutation, features a modification of the amino acid from P to S at position 743.
+The natural variant of this protein is characterized by an amino acid alteration from R to H at position 813.
+The protein's natural variant, known as in a glioblastoma multiforme sample; somatic mutation, features a modification of the amino acid from E to K at position 875.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from D to G at position 930.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 993.
+The protein's natural variant, known as in SPG35; patients present spastic paraparesis associated with leukodystrophy and dystonia;, features a modification of the amino acid from D to Y at position 35.
+The protein's natural variant, known as in SPG35;, features a modification of the amino acid from R to C at position 154.
+The protein's natural variant, known as in SPG35; significantly reduced enzymatic function;, features a modification of the amino acid from R to C at position 235.
+The protein's natural variant, known as in a patient with amyotrophic lateral sclerosis;, features a modification of the amino acid from H to Y at position 69.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from L to V at position 226.
+The protein's natural variant, known as in a patient with amyotrophic lateral sclerosis;, features a modification of the amino acid from E to G at position 272.
+The protein's natural variant, known as in a renal hypodysplasia patient;, features a modification of the amino acid from L to F at position 43.
+The protein's natural variant, known as in a renal hypodysplasia patient;, features a modification of the amino acid from P to L at position 241.
+The protein's natural variant, known as in a renal hypodysplasia patient;, features a modification of the amino acid from D to N at position 276.
+The protein's natural variant, known as in RP12;, features a modification of the amino acid from C to F at position 27.
+The protein's natural variant, known as in RP12;, features a modification of the amino acid from C to W at position 45.
+The protein's natural variant, known as in LCA8;, features a modification of the amino acid from F to V at position 144.
+The protein's natural variant, known as in RP12, features a modification of the amino acid from C to S at position 157.
+The protein's natural variant, known as in RP12;, features a modification of the amino acid from A to V at position 161.
+The protein's natural variant, known as in PPCRA;, features a modification of the amino acid from V to M at position 162.
+The protein's natural variant, known as in RP12;, features a modification of the amino acid from C to F at position 195.
+The protein's natural variant, known as in LCA8; unknown pathological significance;, features a modification of the amino acid from I to T at position 205.
+The protein's natural variant, known as in RP12;, features a modification of the amino acid from C to W at position 250.
+The protein's natural variant, known as rare variant found in patients with retinal dystrophy; does not segregate with the disease in a family; unlikely to be pathogenic;, features a modification of the amino acid from T to M at position 289.
+The protein's natural variant, known as probable disease-associated variant found in patients with early-onset retinal dystrophy;, features a modification of the amino acid from C to Y at position 310.
+The protein's natural variant, known as in RP12, features a modification of the amino acid from N to K at position 312.
+The protein's natural variant, known as in LCA8;, features a modification of the amino acid from G to D at position 333.
+The protein's natural variant, known as in LCA8;, features a modification of the amino acid from C to Y at position 383.
+The protein's natural variant, known as in RP12;, features a modification of the amino acid from Y to C at position 433.
+The protein's natural variant, known as in LCA8;, features a modification of the amino acid from C to Y at position 438.
+The protein's natural variant, known as in LCA8;, features a modification of the amino acid from G to R at position 454.
+The protein's natural variant, known as probable disease-associated variant found in patients with rod-cone retinal dystrophy;, features a modification of the amino acid from L to P at position 479.
+The protein's natural variant, known as in LCA8, features a modification of the amino acid from C to G at position 480.
+The protein's natural variant, known as in LCA8;, features a modification of the amino acid from C to R at position 480.
+The protein's natural variant, known as found in a patient with early-onset retinal dystrophy; unknown pathological significance;, features a modification of the amino acid from D to V at position 491.
+The protein's natural variant, known as in RP12, features a modification of the amino acid from K to N at position 534.
+The protein's natural variant, known as in LCA8;, features a modification of the amino acid from L to P at position 535.
+The protein's natural variant, known as in LCA8, features a modification of the amino acid from D to Y at position 564.
+The protein's natural variant, known as in RP12;, features a modification of the amino acid from V to E at position 578.
+The protein's natural variant, known as in LCA8;, features a modification of the amino acid from D to Y at position 584.
+The protein's natural variant, known as in RP12;, features a modification of the amino acid from C to Y at position 587.
+The protein's natural variant, known as in LCA8; unknown pathological significance, features a modification of the amino acid from S to P at position 635.
+The protein's natural variant, known as in RP12, features a modification of the amino acid from W to C at position 675.
+The protein's natural variant, known as in LCA8;, features a modification of the amino acid from C to Y at position 681.
+The protein's natural variant, known as in LCA8;, features a modification of the amino acid from E to Q at position 710.
+The protein's natural variant, known as in RP12;, features a modification of the amino acid from E to V at position 710.
+The protein's natural variant, known as in RP12;, features a modification of the amino acid from S to F at position 740.
+The protein's natural variant, known as in LCA8; also found in patients with early-onset rod-cone retinal dystrophy;, features a modification of the amino acid from M to T at position 741.
+The protein's natural variant, known as in RP12 and LCA8;, features a modification of the amino acid from T to M at position 745.
+The protein's natural variant, known as in LCA8;, features a modification of the amino acid from L to P at position 753.
+The protein's natural variant, known as in RP12 and LCA8;, features a modification of the amino acid from R to C at position 764.
+The protein's natural variant, known as found in a patient with early-onset retinal dystrophy; unknown pathological significance;, features a modification of the amino acid from R to H at position 764.
+The natural variant of this protein is characterized by an amino acid alteration from R to Q at position 769.
+The protein's natural variant, known as in RP12;, features a modification of the amino acid from P to T at position 836.
+The protein's natural variant, known as in RP12; located on the same allele as T-1354;, features a modification of the amino acid from D to H at position 837.
+The protein's natural variant, known as in RP12;, features a modification of the amino acid from G to R at position 846.
+The protein's natural variant, known as in RP12 and LCA8;, features a modification of the amino acid from G to S at position 850.
+The protein's natural variant, known as in LCA8;, features a modification of the amino acid from I to T at position 852.
+The protein's natural variant, known as in RP12; without preservation of the paraarteriolar retinal pigment epithelium;, features a modification of the amino acid from C to G at position 891.
+The protein's natural variant, known as found in patients with retinitis pigmentosa; unknown pathological significance; heterozygous;, features a modification of the amino acid from N to S at position 894.
+The protein's natural variant, known as in RP12; unknown pathological significance, features a modification of the amino acid from V to I at position 901.
+The protein's natural variant, known as probable disease-associated variant found in patients with rod-cone retinal dystrophy, features a modification of the amino acid from A to P at position 921.
+The protein's natural variant, known as in LCA8; unknown pathological significance;, features a modification of the amino acid from A to T at position 937.
+The protein's natural variant, known as in LCA8;, features a modification of the amino acid from C to Y at position 939.
+The protein's natural variant, known as in LCA8;, features a modification of the amino acid from C to R at position 948.
+The protein's natural variant, known as in RP12 and LCA8; without preservation of the paraarteriolar retinal pigment epithelium;, features a modification of the amino acid from C to Y at position 948.
+The protein's natural variant, known as in RP12; unknown pathological significance;, features a modification of the amino acid from G to S at position 959.
+The protein's natural variant, known as in RP12, features a modification of the amino acid from N to I at position 986.
+The protein's natural variant, known as in LCA8, features a modification of the amino acid from I to T at position 989.
+The protein's natural variant, known as in LCA8;, features a modification of the amino acid from I to T at position 1003.
+The protein's natural variant, known as in RP12, features a modification of the amino acid from L to S at position 1012.
+The protein's natural variant, known as in LCA8;, features a modification of the amino acid from S to I at position 1025.
+The protein's natural variant, known as in RP12, features a modification of the amino acid from S to N at position 1025.
+The protein's natural variant, known as probable disease-associated variant found in patients with rod-cone retinal dystrophy, features a modification of the amino acid from D to N at position 1031.
+The protein's natural variant, known as in RP12;, features a modification of the amino acid from M to T at position 1041.
+The protein's natural variant, known as in RP12;, features a modification of the amino acid from L to P at position 1071.
+The protein's natural variant, known as in RP12, features a modification of the amino acid from T to K at position 1099.
+The protein's natural variant, known as in LCA8;, features a modification of the amino acid from I to R at position 1100.
+The protein's natural variant, known as in RP12;, features a modification of the amino acid from I to T at position 1100.
+The protein's natural variant, known as in LCA8 and RP12;, features a modification of the amino acid from G to R at position 1103.
+The protein's natural variant, known as in LCA8;, features a modification of the amino acid from L to P at position 1107.
+The protein's natural variant, known as in LCA8 and RP12;, features a modification of the amino acid from L to R at position 1107.
+The protein's natural variant, known as in LCA8;, features a modification of the amino acid from Y to C at position 1161.
+The protein's natural variant, known as in RP12;, features a modification of the amino acid from C to W at position 1165.
+The protein's natural variant, known as in LCA8 and RP12;, features a modification of the amino acid from C to G at position 1174.
+The protein's natural variant, known as in RP12;, features a modification of the amino acid from C to R at position 1181.
+The protein's natural variant, known as probable disease-associated variant found in patients with early-onset retinal dystrophy, features a modification of the amino acid from Y to C at position 1198.
+The protein's natural variant, known as in LCA8;, features a modification of the amino acid from G to R at position 1205.
+The protein's natural variant, known as in LCA8, features a modification of the amino acid from C to F at position 1218.
+The protein's natural variant, known as probable disease-associated variant found in patients with early-onset retinal dystrophy, features a modification of the amino acid from C to S at position 1223.
+The protein's natural variant, known as in RP12;, features a modification of the amino acid from P to L at position 1305.
+The protein's natural variant, known as in LCA8;, features a modification of the amino acid from N to H at position 1317.
+The protein's natural variant, known as in LCA8; also early onset RP without preservation of the paraarteriolar retinal pigment epithelium;, features a modification of the amino acid from C to S at position 1321.
+The protein's natural variant, known as in LCA8;, features a modification of the amino acid from C to F at position 1332.
+The protein's natural variant, known as in RP12; located on the same allele as H-837;, features a modification of the amino acid from A to T at position 1354.
+The protein's natural variant, known as probable disease-associated variant found in patients with early-onset retinal dystrophy, features a modification of the amino acid from A to D at position 1365.
+The protein's natural variant, known as in LCA8, features a modification of the amino acid from P to L at position 1381.
+The protein's natural variant, known as in RP12;, features a modification of the amino acid from R to H at position 1383.
+The natural variant of this protein is characterized by an amino acid alteration from E to Q at position 72.
+The natural variant of this protein is characterized by an amino acid alteration from S to L at position 158.
+The natural variant of this protein is characterized by an amino acid alteration from D to N at position 166.
+The protein's natural variant, known as in XLID96;, features a modification of the amino acid from G to R at position 217.
+The protein's natural variant, known as in XLID96; unknown pathological significance, features a modification of the amino acid from D to E at position 277.
+The protein's natural variant, known as in XLID96; unknown pathological significance;, features a modification of the amino acid from G to S at position 293.
+The protein's natural variant, known as in allele HOP1-628; TS, features a modification of the amino acid from S to N at position 595.
+The protein's natural variant, known as in MRD51; unknown pathological significance;, features a modification of the amino acid from W to S at position 264.
+The protein's natural variant, known as in MRD51; unknown pathological significance;, features a modification of the amino acid from A to V at position 513.
+The protein's natural variant, known as in MRD51; unknown pathological significance;, features a modification of the amino acid from R to Q at position 540.
+The protein's natural variant, known as in PKD7; unable to rescue defective PKD1 glycosylation and maturation in ALG5-deficient cells, features a modification of the amino acid from R to H at position 208.
+The protein's natural variant, known as in PKD7; unable to rescue defective PKD1 glycosylation and maturation in ALG5-deficient cells, features a modification of the amino acid from R to H at position 212.
+The natural variant of this protein is characterized by an amino acid alteration from K to P at position 31.
+The protein's natural variant, known as in GRIDHH;, features a modification of the amino acid from V to G at position 370.
+The protein's natural variant, known as in GRIDHH;, features a modification of the amino acid from P to L at position 437.
+The natural variant of this protein is characterized by an amino acid alteration from M to I at position 769.
+The protein's natural variant, known as in GRIDHH;, features a modification of the amino acid from N to D at position 992.
+The protein's natural variant, known as in GRIDHH;, features a modification of the amino acid from I to N at position 1174.
+The natural variant of this protein is characterized by an amino acid alteration from S to T at position 16.
+The protein's natural variant, known as in DDVIBA; unknown pathological significance, features a modification of the amino acid from K to E at position 512.
+The protein's natural variant, known as in DDVIBA; unknown pathological significance, features a modification of the amino acid from P to L at position 1557.
+The protein's natural variant, known as in DDVIBA; unknown pathological significance, features a modification of the amino acid from K to R at position 1710.
+The protein's natural variant, known as in DDVIBA, features a modification of the amino acid from H to Y at position 1909.
+The protein's natural variant, known as in DDVIBA; unknown pathological significance, features a modification of the amino acid from P to L at position 1937.
+The protein's natural variant, known as in DDVIBA; unknown pathological significance, features a modification of the amino acid from P to H at position 1942.
+The protein's natural variant, known as in SPCH1; reduced interaction with TBR1;, features a modification of the amino acid from R to H at position 553.
+The protein's natural variant, known as in strain: Isolate 3, features a modification of the amino acid from V to I at position 118.
+The protein's natural variant, known as in strain: Isolate 3, features a modification of the amino acid from RA to QT at position 314.
+The protein's natural variant, known as in XLID50; results in reduced synaptic vesicle mobility, increased clustering of synaptic vesicles at presynatptic terminals and increased frequency of miniature excitatory postsynaptic currents;, features a modification of the amino acid from S to W at position 79.
+The protein's natural variant, known as in XLID50; unknown pathological significance; no effect on phosphorylation by CaMK2 and MAPK1; has no effect on axon elongation when tested in SYN1-knockout mouse neurons; slightly reduced protein targeting to presynapse;, features a modification of the amino acid from A to T at position 550.
+The protein's natural variant, known as no effect on phosphorylation by CaMK2 and MAPK1; has no effect on axon elongation when tested in SYN1-knockout mouse neurons; slightly reduced protein targeting to presynapse;, features a modification of the amino acid from T to A at position 567.
+The protein's natural variant, known as in CSCSC1; disrupts heterodimer assembly and microtubule dynamics;, features a modification of the amino acid from Q to K at position 15.
+The protein's natural variant, known as in CSCSC1; disrupts heterodimer assembly and microtubule dynamics;, features a modification of the amino acid from Y to F at position 222.
+The protein's natural variant, known as in CDCBM6; decreases the ability of the protein to assemble into tubulin heterodimers;, features a modification of the amino acid from M to V at position 299.
+The protein's natural variant, known as in CDCBM6; does not affect the ability of the mutant polypeptides to assemble into heterodimers and incorporate into microtubules;, features a modification of the amino acid from V to I at position 353.
+The protein's natural variant, known as in CDCBM6; arrests the assembly pathway of alpha/beta-tubulin; the mutant protein is unable to coassemble into a tubulin heterodimer but is instead distributed throughout the cytoplasm;, features a modification of the amino acid from E to K at position 401.
+The protein's natural variant, known as in allele CYP2A13*2;, features a modification of the amino acid from R to Q at position 25.
+The protein's natural variant, known as in allele CYP2A13*4;, features a modification of the amino acid from R to Q at position 101.
+The protein's natural variant, known as in allele CYP2A13*3, features a modification of the amino acid from T to TT at position 134.
+The protein's natural variant, known as in allele CYP2A13*3 and allele CYP2A13*8;, features a modification of the amino acid from D to E at position 158.
+The protein's natural variant, known as in allele CYP2A13*2;, features a modification of the amino acid from R to C at position 257.
+The protein's natural variant, known as in allele CYP2A13*9, features a modification of the amino acid from V to L at position 323.
+The protein's natural variant, known as in allele CYP2A13*5;, features a modification of the amino acid from F to Y at position 453.
+The protein's natural variant, known as in allele CYP2A13*6;, features a modification of the amino acid from R to C at position 494.
+The protein's natural variant, known as in CMD1M; unknown pathological significance; decreases interaction with TCAP;, features a modification of the amino acid from W to R at position 4.
+The protein's natural variant, known as in CMH12; decreases PKC/PRKCA activity;, features a modification of the amino acid from L to P at position 44.
+The protein's natural variant, known as in CMH12; decreases PKC/PRKCA activity;, features a modification of the amino acid from SE to RG at position 55.
+The protein's natural variant, known as in CMH12; decreases interaction with NRAP and ACTN2, decreases zinc-binding and impairs protein stability, decreases PKC/PRKCA activity;, features a modification of the amino acid from C to G at position 58.
+The protein's natural variant, known as in CMD1M; unknown pathological significance; increases PKC/PRKCA activity;, features a modification of the amino acid from G to R at position 72.
+The protein's natural variant, known as in MKS3; unknown pathological significance;, features a modification of the amino acid from Y to C at position 54.
+The protein's natural variant, known as in JBTS6; unknown pathological significance;, features a modification of the amino acid from P to R at position 82.
+The protein's natural variant, known as in JBTS6; unknown pathological significance;, features a modification of the amino acid from P to S at position 82.
+The protein's natural variant, known as probable disease-associated variant found in Joubert syndrome-related disorder, features a modification of the amino acid from N to K at position 90.
+The protein's natural variant, known as in COACH1; unknown pathological significance;, features a modification of the amino acid from K to N at position 99.
+The protein's natural variant, known as probable disease-associated variant found in Joubert syndrome-related disorder;, features a modification of the amino acid from E to K at position 124.
+The protein's natural variant, known as in COACH1;, features a modification of the amino acid from P to R at position 130.
+The protein's natural variant, known as in COACH1; does not affect protein abundance; fails to rescue the hydrocephalus phenotype in a zebrafish model;, features a modification of the amino acid from G to A at position 132.
+The protein's natural variant, known as in COACH1; unknown pathological significance;, features a modification of the amino acid from R to Q at position 172.
+The protein's natural variant, known as in COACH1 and JBTS6, features a modification of the amino acid from N to S at position 242.
+The protein's natural variant, known as in MKS3; unknown pathological significance;, features a modification of the amino acid from S to F at position 245.
+The protein's natural variant, known as in MKS3, JBTS6 and COACH1; loss of interaction with WNT5A;, features a modification of the amino acid from M to T at position 252.
+The protein's natural variant, known as in COACH1; unknown pathological significance;, features a modification of the amino acid from M to V at position 257.
+The protein's natural variant, known as in NPHP11;, features a modification of the amino acid from W to L at position 290.
+The protein's natural variant, known as in MKS3; unknown pathological significance;, features a modification of the amino acid from W to C at position 296.
+The protein's natural variant, known as probable disease-associated variant found in Joubert syndrome-related disorder;, features a modification of the amino acid from D to E at position 301.
+The protein's natural variant, known as is a modifier of Bardet-Biedl syndrome; found in a BBS14 patient also carrying a homozygous truncating mutation of the CEP290 gene;, features a modification of the amino acid from S to C at position 320.
+The protein's natural variant, known as in COACH1 and MKS3; loss of interaction with WNT5A;, features a modification of the amino acid from L to S at position 349.
+The protein's natural variant, known as in COACH1 and JBTS6; found in a patient with Joubert syndrome that also carries mutation 1329-R--S-1332 Del in KIF7;, features a modification of the amino acid from P to L at position 358.
+The protein's natural variant, known as does not affect Wnt signaling regulation; when expressed in TMEM67-null cells it induces ROR2 phosphorylation upon stimulation by WNT5A, features a modification of the amino acid from D to E at position 359.
+The protein's natural variant, known as in COACH1;, features a modification of the amino acid from T to K at position 372.
+The protein's natural variant, known as in COACH1;, features a modification of the amino acid from Q to E at position 376.
+The protein's natural variant, known as in MKS3; leads to endoplasmic reticulum retention and prevents localization at the cell membrane; decreased function in non-canonical Wnt signaling activation; when expressed in TMEM67-null cells does not induce ROR2 phosphorylation upon stimulation by WNT5A; loss of interaction with WNT5A;, features a modification of the amino acid from Q to P at position 376.
+The protein's natural variant, known as in RHYNS; may result in exon 13 skipping, features a modification of the amino acid from D to G at position 430.
+The protein's natural variant, known as in MKS3 and COACH1; loss of interaction with WNT5A; affects Wnt signaling regulation; when expressed in TMEM67-null cells does not rescue increased canonical Wnt signaling;, features a modification of the amino acid from R to Q at position 440.
+The protein's natural variant, known as in COACH1; unknown pathological significance;, features a modification of the amino acid from R to C at position 441.
+The protein's natural variant, known as in MKS3;, features a modification of the amino acid from R to L at position 441.
+The protein's natural variant, known as in COACH1; unknown pathological significance;, features a modification of the amino acid from P to S at position 485.
+The protein's natural variant, known as in JBTS6, MKS3 and COACH1;, features a modification of the amino acid from Y to C at position 513.
+The protein's natural variant, known as in JBTS6;, features a modification of the amino acid from G to E at position 545.
+The protein's natural variant, known as in MKS3; affects Wnt signaling regulation; when expressed in TMEM67-null cells does not rescue increased canonical Wnt signaling, features a modification of the amino acid from R to C at position 549.
+The protein's natural variant, known as probable disease-associated variant found in Joubert syndrome-related disorder;, features a modification of the amino acid from G to D at position 569.
+The protein's natural variant, known as in COACH1;, features a modification of the amino acid from F to S at position 590.
+The protein's natural variant, known as in MKS3, COACH1 and NPHP11; affects Wnt signaling regulation; when expressed in TMEM67-null cells does not rescue increased canonical Wnt signaling;, features a modification of the amino acid from C to R at position 615.
+The protein's natural variant, known as probable disease-associated variant found in Joubert syndrome-related disorder;, features a modification of the amino acid from A to V at position 616.
+The protein's natural variant, known as in COACH1; unknown pathological significance;, features a modification of the amino acid from F to L at position 637.
+The protein's natural variant, known as in MKS3;, features a modification of the amino acid from W to R at position 668.
+The protein's natural variant, known as in JBTS6;, features a modification of the amino acid from D to A at position 711.
+The protein's natural variant, known as in COACH1, features a modification of the amino acid from S to G at position 728.
+The protein's natural variant, known as probable disease-associated variant found in Joubert syndrome-related disorder, features a modification of the amino acid from L to R at position 739.
+The protein's natural variant, known as in COACH1; decreased function in non-canonical Wnt signaling activation; when expressed in TMEM67-null cells does not induce ROR2 phosphorylation upon stimulation by WNT5A;, features a modification of the amino acid from H to R at position 782.
+The protein's natural variant, known as in MKS3, features a modification of the amino acid from G to A at position 786.
+The protein's natural variant, known as in MKS3; decreased function in non-canonical Wnt signaling activation; when expressed in TMEM67-null cells does not induce ROR2 phosphorylation upon stimulation by WNT5A;, features a modification of the amino acid from G to E at position 786.
+The protein's natural variant, known as in COACH1, features a modification of the amino acid from R to S at position 820.
+The protein's natural variant, known as in NPHP11;, features a modification of the amino acid from G to R at position 821.
+The protein's natural variant, known as in NPHP11;, features a modification of the amino acid from G to S at position 821.
+The protein's natural variant, known as in COACH1 and JBTS6; found in a patient with Joubert syndrome that also carries mutation 1329-R--S-1332 Del in KIF7;, features a modification of the amino acid from I to T at position 833.
+The protein's natural variant, known as in COACH1; unknown pathological significance;, features a modification of the amino acid from Q to P at position 841.
+The protein's natural variant, known as in MKS3;, features a modification of the amino acid from Y to C at position 843.
+The protein's natural variant, known as in COACH1; unknown pathological significance;, features a modification of the amino acid from F to C at position 942.
+The protein's natural variant, known as in MKS3;, features a modification of the amino acid from L to P at position 966.
+The protein's natural variant, known as not associated with susceptibility to breast cancer;, features a modification of the amino acid from A to T at position 348.
+The protein's natural variant, known as in BC; results in reduced DSB repair efficiency; primarily localizes to the cytoplasm and has reduced nuclear localization; does not affect interaction with BRCA1; results in highly reduced interaction with UIMC1/RAP80;, features a modification of the amino acid from R to Q at position 361.
+The protein's natural variant, known as not associated with susceptibility to breast cancer;, features a modification of the amino acid from D to N at position 373.
+The protein's natural variant, known as in TTD7; loss of protein stability; loss of threonine-tRNA ligase activity, features a modification of the amino acid from L to P at position 227.
+The protein's natural variant, known as in TTD7, features a modification of the amino acid from K to E at position 276.
+The protein's natural variant, known as in strain: Zimbabwe 53, features a modification of the amino acid from Y to F at position 148.
+The protein's natural variant, known as in strain: Japan, features a modification of the amino acid from H to Y at position 182.
+The protein's natural variant, known as in strain: Oregon-R, features a modification of the amino acid from Y to L at position 200.
+The protein's natural variant, known as in strain: Oregon-R, SP1 and w1118iso, features a modification of the amino acid from L to I at position 277.
+The protein's natural variant, known as in 02E11, features a modification of the amino acid from P to A at position 47.
+The protein's natural variant, known as in 10F07, features a modification of the amino acid from L to M at position 73.
+The protein's natural variant, known as in 10F07, features a modification of the amino acid from M to L at position 109.
+The protein's natural variant, known as in 10F07, features a modification of the amino acid from PPM to APL at position 121.
+The protein's natural variant, known as in 10F07, features a modification of the amino acid from APL to PPM at position 133.
+The protein's natural variant, known as in 02E11, features a modification of the amino acid from G to GAA at position 223.
+The protein's natural variant, known as in 10F07, features a modification of the amino acid from G to GAAA at position 223.
+The protein's natural variant, known as found in a patient with intellectual disability; unknown pathological significance, features a modification of the amino acid from S to N at position 51.
+The natural variant of this protein is characterized by an amino acid alteration from P to L at position 251.
+The natural variant of this protein is characterized by an amino acid alteration from ML to II at position 337.
+The natural variant of this protein is characterized by an amino acid alteration from A to D at position 470.
+The natural variant of this protein is characterized by an amino acid alteration from E to G at position 479.
+The protein's natural variant, known as in strain: ICMP 2844, features a modification of the amino acid from V to A at position 265.
+The protein's natural variant, known as in THPH10; Oslo; decreased affinity for dermatan sulfate;, features a modification of the amino acid from R to H at position 208.
+The protein's natural variant, known as in THPH10;, features a modification of the amino acid from E to K at position 447.
+The protein's natural variant, known as in THPH10; Tokushima; impaired secretion of the mutant molecules;, features a modification of the amino acid from P to L at position 462.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from G to C at position 123.
+The protein's natural variant, known as in strain: Nv2001_f0696, NVIII-46 and NVIII-24, features a modification of the amino acid from A to V at position 2.
+The protein's natural variant, known as in strain: NVIII-46 and NVIII-24, features a modification of the amino acid from P to Q at position 169.
+The protein's natural variant, known as in COXPD39;, features a modification of the amino acid from Y to S at position 92.
+The protein's natural variant, known as in COXPD39;, features a modification of the amino acid from R to Q at position 190.
+The protein's natural variant, known as in COXPD39; unknown pathological significance; may affect splicing, features a modification of the amino acid from D to E at position 576.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from K to N at position 204.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from S to Y at position 497.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from R to Q at position 626.
+The protein's natural variant, known as in a colon cancer sample; somatic mutation;, features a modification of the amino acid from R to C at position 214.
+The protein's natural variant, known as in a colon cancer sample; somatic mutation;, features a modification of the amino acid from Q to P at position 276.
+The protein's natural variant, known as in strain: B28, features a modification of the amino acid from E to G at position 189.
+The protein's natural variant, known as in strain: Z(H)1, features a modification of the amino acid from I to N at position 194.
+The protein's natural variant, known as in strain: 122, features a modification of the amino acid from R to G at position 262.
+The protein's natural variant, known as in strain: FrV3-1, features a modification of the amino acid from K to R at position 489.
+The protein's natural variant, known as in strain: 56H8, features a modification of the amino acid from V to D at position 567.
+The protein's natural variant, known as in strain: 122, features a modification of the amino acid from D to G at position 573.
+The protein's natural variant, known as in strain: B28, features a modification of the amino acid from P to R at position 636.
+The protein's natural variant, known as in allele LYB-2A.2, features a modification of the amino acid from E to EYLSDAPQ at position 279.
+The protein's natural variant, known as in MC1DN4;, features a modification of the amino acid from E to K at position 214.
+The protein's natural variant, known as in MC1DN4;, features a modification of the amino acid from A to V at position 341.
+The protein's natural variant, known as in MC1DN4;, features a modification of the amino acid from T to M at position 423.
+The protein's natural variant, known as in FAP2; also found in multiple polyposis, colorectal and lung cancer cases; unknown pathological significance; decreased function in DNA repair;, features a modification of the amino acid from P to L at position 18.
+The protein's natural variant, known as does not affect function in DNA repair;, features a modification of the amino acid from V to M at position 22.
+The protein's natural variant, known as does not affect function in DNA repair;, features a modification of the amino acid from G to D at position 25.
+The protein's natural variant, known as likely benign variant; does not affect DNA glycosylase activity, features a modification of the amino acid from V to E at position 72.
+The protein's natural variant, known as found in sporadic hepatocellular carcinoma; unknown pathological significance; loss of function in DNA repair;, features a modification of the amino acid from W to R at position 100.
+The protein's natural variant, known as found in multiple polyposis and sporadic colorectal cancer cases; unknown pathological significance; does not affect DNA glycosylase activity; does not affect function in DNA repair;, features a modification of the amino acid from D to N at position 102.
+The protein's natural variant, known as likely benign variant; does not affect DNA glycosylase activity; does not affect function in DNA repair, features a modification of the amino acid from D to G at position 121.
+The protein's natural variant, known as in FAP2; decreased function in DNA repair, features a modification of the amino acid from Y to H at position 125.
+The protein's natural variant, known as in FAP2; loss of function in DNA repair;, features a modification of the amino acid from W to R at position 128.
+The protein's natural variant, known as in FAP2; reduced DNA glycosylase activity; decreased DNA binding; loss of function in DNA repair, features a modification of the amino acid from G to GIW at position 148.
+The protein's natural variant, known as in FAP2; decreased function in DNA repair;, features a modification of the amino acid from P to L at position 154.
+The protein's natural variant, known as in FAP2; loss of DNA glycosylase activity; decreased DNA binding; loss of function in DNA repair;, features a modification of the amino acid from Y to C at position 176.
+The protein's natural variant, known as in FAP2, features a modification of the amino acid from Y to S at position 177.
+The protein's natural variant, known as in FAP2; also found in multiple polyposis and colorectal cancer cases; loss of function in DNA repair;, features a modification of the amino acid from R to C at position 179.
+The protein's natural variant, known as in FAP2; loss of DNA glycosylase activity; loss of function in DNA repair;, features a modification of the amino acid from R to H at position 179.
+The protein's natural variant, known as in FAP2; loss of function in DNA repair;, features a modification of the amino acid from R to Q at position 182.
+The protein's natural variant, known as in FAP2; loss of DNA glycosylase activity; loss of DNA binding; loss of function in DNA repair;, features a modification of the amino acid from R to W at position 182.
+The protein's natural variant, known as in FAP2; decreased function in DNA repair;, features a modification of the amino acid from G to E at position 186.
+The protein's natural variant, known as in FAP2;, features a modification of the amino acid from G to E at position 213.
+The protein's natural variant, known as in FAP2; also found in multiple polyposis case; unknown pathological significance; reduced DNA glycosylase activity; no effect on function in DNA repair;, features a modification of the amino acid from I to V at position 220.
+The protein's natural variant, known as decreased function in DNA repair;, features a modification of the amino acid from A to V at position 224.
+The protein's natural variant, known as probable disease-associated variant found in a case of familial colorectal cancer; no significant effect on DNA glycosylase activity; slightly decreased function in DNA repair;, features a modification of the amino acid from V to M at position 231.
+The protein's natural variant, known as in FAP2; loss of DNA glycosylase activity; loss of function in DNA repair;, features a modification of the amino acid from N to S at position 235.
+The protein's natural variant, known as in FAP2; also found in a case of sporadic colorectal cancer; unknown pathological significance; decreased function in DNA repair;, features a modification of the amino acid from R to W at position 238.
+The protein's natural variant, known as probable disease-associated variant found in multiple polyposis cases; decreased function in DNA repair;, features a modification of the amino acid from R to C at position 242.
+The protein's natural variant, known as in FAP2; loss of function in DNA repair;, features a modification of the amino acid from R to H at position 242.
+The protein's natural variant, known as does not affect function;, features a modification of the amino acid from V to F at position 243.
+The protein's natural variant, known as reduced DNA glycosylase activity; decreased function in DNA repair;, features a modification of the amino acid from R to G at position 244.
+The protein's natural variant, known as in FAP2; loss of function in DNA repair;, features a modification of the amino acid from R to W at position 271.
+The protein's natural variant, known as in FAP2; reduced DNA glycosylase activity;, features a modification of the amino acid from M to V at position 280.
+The protein's natural variant, known as in FAP2; also found in a patient with multiple polyps; unknown pathological significance; does not affect function in DNA repair;, features a modification of the amino acid from G to E at position 283.
+The protein's natural variant, known as found in a case of sporadic lung cancer; unknown pathological significance; loss of function in DNA repair, features a modification of the amino acid from C to W at position 287.
+The protein's natural variant, known as in FAP2; also found in multiple polyposis cases; loss of function in DNA repair;, features a modification of the amino acid from P to L at position 292.
+The protein's natural variant, known as in FAP2; also found in multiple polyposis cases; unknown pathological significance; does not affect DNA glycosylase activity; slightly decreased function in DNA repair;, features a modification of the amino acid from R to C at position 306.
+The protein's natural variant, known as does not affect DNA glycosylase activity; does not affect function in DNA repair;, features a modification of the amino acid from S to N at position 319.
+The protein's natural variant, known as does not affect function in DNA repair;, features a modification of the amino acid from Q to H at position 335.
+The protein's natural variant, known as found in a family with non-polyposis colorectal cancer-like syndrome; unknown pathological significance; does not affect function in DNA repair;, features a modification of the amino acid from Q to R at position 335.
+The protein's natural variant, known as does not affect DNA glycosylase activity;, features a modification of the amino acid from A to V at position 370.
+The protein's natural variant, known as in FAP2; decreased function in DNA repair, features a modification of the amino acid from P to T at position 377.
+The protein's natural variant, known as in FAP2; also found in multiple polyposis cases; loss of DNA glycosylase activity; loss of function in DNA repair;, features a modification of the amino acid from L to P at position 385.
+The protein's natural variant, known as in FAP2; reduced DNA glycosylase activity; decreased DNA binding; decreased function in DNA repair;, features a modification of the amino acid from G to D at position 393.
+The protein's natural variant, known as in FAP2; also found in multiple polyposis and colorectal cancer cases; loss of DNA glycosylase activity; loss of function in DNA repair;, features a modification of the amino acid from P to L at position 402.
+The protein's natural variant, known as in GASC; sporadic; decreased function in DNA repair;, features a modification of the amino acid from P to S at position 402.
+The protein's natural variant, known as in GASC; sporadic; unknown pathological significance; does not affect function in DNA repair;, features a modification of the amino acid from Q to R at position 411.
+The protein's natural variant, known as in FAP2; also found in patient with multiple polyps and in a family with non-polyposis colorectal cancer-like syndrome; unknown pathological significance; does not affect function in DNA repair;, features a modification of the amino acid from L to M at position 417.
+The protein's natural variant, known as in FAP2; unknown pathological significance; does not affect function in DNA repair;, features a modification of the amino acid from R to C at position 423.
+The protein's natural variant, known as found in sporadic colorectal cancer cases; unknown pathological significance; decreased function in DNA repair, features a modification of the amino acid from R to P at position 434.
+The protein's natural variant, known as does not affect function in DNA repair;, features a modification of the amino acid from R to Q at position 434.
+The protein's natural variant, known as in FAP2; loss of function in DNA repair;, features a modification of the amino acid from A to D at position 470.
+The protein's natural variant, known as found in patient with multiple polyposis; unknown pathological significance; does not affect function in DNA repair;, features a modification of the amino acid from A to T at position 470.
+The protein's natural variant, known as in FAP2; unknown pathological significance;, features a modification of the amino acid from T to M at position 474.
+The protein's natural variant, known as in FAP2; decreased function in DNA repair;, features a modification of the amino acid from A to T at position 486.
+The protein's natural variant, known as in FAP2; found also in sporadic colorectal cancer cases; unknown pathological significance; decreased function in DNA repair;, features a modification of the amino acid from V to F at position 490.
+The protein's natural variant, known as decreased function in DNA repair;, features a modification of the amino acid from G to E at position 500.
+The protein's natural variant, known as does not affect DNA glycosylase activity; does not affect function in DNA repair;, features a modification of the amino acid from S to F at position 512.
+The protein's natural variant, known as does not affect function in DNA repair;, features a modification of the amino acid from P to L at position 513.
+The protein's natural variant, known as does not affect DNA glycosylase activity; does not affect function in DNA repair;, features a modification of the amino acid from R to H at position 520.
+The protein's natural variant, known as does not affect function in DNA repair;, features a modification of the amino acid from L to M at position 526.
+The protein's natural variant, known as does not affect function in DNA repair;, features a modification of the amino acid from R to Q at position 531.
+The protein's natural variant, known as does not affect DNA glycosylase activity; does not affect function in DNA repair;, features a modification of the amino acid from T to A at position 536.
+The protein's natural variant, known as in HPE9; unknown pathological significance;, features a modification of the amino acid from R to G at position 479.
+The protein's natural variant, known as in CJS; loss of DNA-binding; loss of transcription factor activity, features a modification of the amino acid from R to P at position 516.
+The protein's natural variant, known as in CJS;, features a modification of the amino acid from P to L at position 608.
+The protein's natural variant, known as in HPE9; unknown pathological significance;, features a modification of the amino acid from P to S at position 932.
+The protein's natural variant, known as likely benign variant; associated with N-1520 in Culler-Jones syndrome; decreased transcription factor activity when associated with N-1520;, features a modification of the amino acid from M to V at position 1352.
+The protein's natural variant, known as in CJS; unknown pathological significance; decreased transcription factor activity, features a modification of the amino acid from ML to IF at position 1445.
+The protein's natural variant, known as likely benign variant; associated with V-1352 in Culler-Jones syndrome; decreased transcription factor activity when associated with V-1352;, features a modification of the amino acid from D to N at position 1520.
+The protein's natural variant, known as no effect on transcription factor activity;, features a modification of the amino acid from R to H at position 1543.
+The protein's natural variant, known as in HPE9; unknown pathological significance;, features a modification of the amino acid from P to L at position 1554.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from L to H at position 455.
+The protein's natural variant, known as in subunit alpha-2 and subunit alpha-3, features a modification of the amino acid from S to F at position 6.
+The protein's natural variant, known as in subunit alpha-3, features a modification of the amino acid from I to T at position 91.
+The protein's natural variant, known as in subunit alpha-4, features a modification of the amino acid from R to G at position 154.
+The protein's natural variant, known as in alpha-2, features a modification of the amino acid from D to G at position 115.
+The protein's natural variant, known as in DFNA7; unknown pathological significance, features a modification of the amino acid from C to S at position 97.
+The protein's natural variant, known as in DFNA7, features a modification of the amino acid from V to L at position 241.
+The protein's natural variant, known as found in autosomal recessive sensorineural hearing loss; unknown pathological significance, features a modification of the amino acid from I to T at position 369.
+The protein's natural variant, known as in CDLS2;, features a modification of the amino acid from F to V at position 133.
+The protein's natural variant, known as in CDLS2;, features a modification of the amino acid from E to K at position 141.
+The protein's natural variant, known as in CDLS2;, features a modification of the amino acid from R to H at position 196.
+The protein's natural variant, known as in CDLS2, features a modification of the amino acid from R to G at position 398.
+The protein's natural variant, known as in CDLS2;, features a modification of the amino acid from R to Q at position 398.
+The protein's natural variant, known as in CDLS2; affects the affinity of SMC hinge dimers for DNA; mutated hinge dimers bind DNA with higher affinity than wild-type proteins;, features a modification of the amino acid from E to A at position 493.
+The protein's natural variant, known as in CDLS2; affects the affinity of SMC hinge dimers for DNA; mutated hinge dimers bind DNA with higher affinity than wild-type proteins;, features a modification of the amino acid from R to C at position 496.
+The protein's natural variant, known as in CDLS2; affects the affinity of SMC hinge dimers for DNA; mutated hinge dimers bind DNA with higher affinity than wild-type proteins;, features a modification of the amino acid from R to H at position 496.
+The protein's natural variant, known as in CDLS2; unknown pathological significance, features a modification of the amino acid from V to M at position 651.
+The protein's natural variant, known as in CDLS2, features a modification of the amino acid from R to G at position 693.
+The protein's natural variant, known as in CDLS2;, features a modification of the amino acid from R to Q at position 693.
+The protein's natural variant, known as in CDLS2;, features a modification of the amino acid from R to Q at position 711.
+The protein's natural variant, known as in CDLS2;, features a modification of the amino acid from R to W at position 711.
+The protein's natural variant, known as in CDLS2, features a modification of the amino acid from C to F at position 781.
+The protein's natural variant, known as in CDLS2;, features a modification of the amino acid from I to T at position 784.
+The protein's natural variant, known as in CDLS2;, features a modification of the amino acid from R to Q at position 790.
+The protein's natural variant, known as in CDLS2, features a modification of the amino acid from R to G at position 816.
+The protein's natural variant, known as in DEE85;, features a modification of the amino acid from R to G at position 895.
+The protein's natural variant, known as in CDLS2;, features a modification of the amino acid from R to Q at position 1049.
+The protein's natural variant, known as in CDLS2;, features a modification of the amino acid from Y to C at position 1085.
+The protein's natural variant, known as in CDLS2, features a modification of the amino acid from F to L at position 1122.
+The protein's natural variant, known as in CDLS2, features a modification of the amino acid from R to W at position 1123.
+The protein's natural variant, known as in CDLS2; unknown pathological significance;, features a modification of the amino acid from N to T at position 1166.
+The protein's natural variant, known as in CDLS2; unknown pathological significance, features a modification of the amino acid from L to F at position 1189.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from R to Q at position 127.
+The protein's natural variant, known as in TDH5; unknown pathological significance; impairs hydrogen peroxide metabolic process, features a modification of the amino acid from I to M at position 26.
+The protein's natural variant, known as in IMD15A; gain-of-function mutation resulting in increased activation of NF-kappa-B signaling pathway;, features a modification of the amino acid from V to I at position 203.
+The protein's natural variant, known as in breast cancer samples; infiltrating ductal carcinoma; somatic mutation, features a modification of the amino acid from A to S at position 360.
+The natural variant of this protein is characterized by an amino acid alteration from N to D at position 217.
+The natural variant of this protein is characterized by an amino acid alteration from K to R at position 231.
+The natural variant of this protein is characterized by an amino acid alteration from V to M at position 268.
+The protein's natural variant, known as in HMSN6C; decreased pyridoxal kinase activity;, features a modification of the amino acid from R to Q at position 220.
+The protein's natural variant, known as in HMSN6C; decreased pyridoxal kinase activity; decreased affinity for ATP; decreased affinity for pyridoxal 5'-phosphate; no effect on protein abundance;, features a modification of the amino acid from A to T at position 228.
+The protein's natural variant, known as in isoform 1B, features a modification of the amino acid from V to A at position 38.
+The protein's natural variant, known as in isoform 1B, features a modification of the amino acid from I to S at position 63.
+The protein's natural variant, known as in isoform 1B, features a modification of the amino acid from K to E at position 133.
+The protein's natural variant, known as in alpha-1, features a modification of the amino acid from G to D at position 20.
+The protein's natural variant, known as in GABATD; 25% reduction in 4-aminobutyrate aminotransferase activity;, features a modification of the amino acid from R to K at position 220.
+The protein's natural variant, known as lower Vmax; increase in substrate affinity and increase in the affinity for the nucleoside phosphonate analogs cidofovir, adefovir and tenofovir;, features a modification of the amino acid from R to H at position 50.
+The protein's natural variant, known as increase in substrate affinity;, features a modification of the amino acid from R to W at position 293.
+The protein's natural variant, known as in PAIS;, features a modification of the amino acid from E to K at position 2.
+The protein's natural variant, known as in prostate cancer, features a modification of the amino acid from L to S at position 54.
+The protein's natural variant, known as in prostate cancer;, features a modification of the amino acid from L to Q at position 57.
+The protein's natural variant, known as in prostate cancer, features a modification of the amino acid from Q to R at position 64.
+The protein's natural variant, known as in prostate cancer, features a modification of the amino acid from Q to H at position 114.
+The protein's natural variant, known as in prostate cancer, features a modification of the amino acid from K to R at position 182.
+The protein's natural variant, known as in AIS, features a modification of the amino acid from Q to R at position 196.
+The protein's natural variant, known as 20% lower transactivation capacity;, features a modification of the amino acid from G to R at position 216.
+The protein's natural variant, known as in AIS, features a modification of the amino acid from L to P at position 257.
+The protein's natural variant, known as in prostate cancer, features a modification of the amino acid from M to T at position 268.
+The protein's natural variant, known as in prostate cancer, features a modification of the amino acid from P to S at position 271.
+The protein's natural variant, known as in prostate cancer;, features a modification of the amino acid from P to L at position 342.
+The protein's natural variant, known as in AIS;, features a modification of the amino acid from P to R at position 392.
+The protein's natural variant, known as in AIS;, features a modification of the amino acid from P to S at position 392.
+The protein's natural variant, known as in AIS; unknown pathological significance;, features a modification of the amino acid from Q to R at position 445.
+The protein's natural variant, known as in AIS, features a modification of the amino acid from G to S at position 492.
+The protein's natural variant, known as in prostate cancer, features a modification of the amino acid from D to G at position 529.
+The protein's natural variant, known as in PAIS;, features a modification of the amino acid from L to F at position 548.
+The protein's natural variant, known as in AIS;, features a modification of the amino acid from P to S at position 549.
+The protein's natural variant, known as in AIS, features a modification of the amino acid from C to Y at position 560.
+The protein's natural variant, known as in a patient with isolated hypospadias, features a modification of the amino acid from G to V at position 569.
+The protein's natural variant, known as in PAIS;, features a modification of the amino acid from G to W at position 569.
+The protein's natural variant, known as in AIS, features a modification of the amino acid from Y to C at position 572.
+The protein's natural variant, known as in AIS, features a modification of the amino acid from A to D at position 574.
+The protein's natural variant, known as in prostate cancer, features a modification of the amino acid from L to P at position 575.
+The protein's natural variant, known as in prostate cancer, features a modification of the amino acid from T to A at position 576.
+The protein's natural variant, known as in AIS, features a modification of the amino acid from C to F at position 577.
+The protein's natural variant, known as in AIS, features a modification of the amino acid from C to R at position 577.
+The protein's natural variant, known as in AIS; reduced transcription and DNA binding;, features a modification of the amino acid from C to F at position 580.
+The protein's natural variant, known as in AIS;, features a modification of the amino acid from C to Y at position 580.
+The protein's natural variant, known as in prostate cancer, features a modification of the amino acid from K to R at position 581.
+The protein's natural variant, known as in AIS, features a modification of the amino acid from V to F at position 582.
+The protein's natural variant, known as in PAIS, features a modification of the amino acid from F to S at position 583.
+The protein's natural variant, known as in PAIS;, features a modification of the amino acid from F to Y at position 583.
+The protein's natural variant, known as in AIS, features a modification of the amino acid from R to K at position 586.
+The protein's natural variant, known as in prostate cancer; somatic mutation, features a modification of the amino acid from A to V at position 587.
+The protein's natural variant, known as in prostate cancer; somatic mutation, features a modification of the amino acid from A to S at position 588.
+The protein's natural variant, known as in AIS; abolishes dimerization;, features a modification of the amino acid from A to T at position 597.
+The protein's natural variant, known as in PAIS; associated with P-618 in a PAIS patient; normal androgen binding; does not activate transcription; impairs DNA binding;, features a modification of the amino acid from S to G at position 598.
+The protein's natural variant, known as in a patient with severe hypospadias, features a modification of the amino acid from S to T at position 598.
+The protein's natural variant, known as in AIS, features a modification of the amino acid from C to F at position 602.
+The protein's natural variant, known as in PAIS, features a modification of the amino acid from D to Y at position 605.
+The protein's natural variant, known as in PAIS and breast cancer;, features a modification of the amino acid from R to Q at position 608.
+The protein's natural variant, known as in PAIS and breast cancer; defective nuclear localization;, features a modification of the amino acid from R to K at position 609.
+The protein's natural variant, known as in PAIS, features a modification of the amino acid from N to T at position 611.
+The protein's natural variant, known as in AIS, features a modification of the amino acid from C to Y at position 612.
+The protein's natural variant, known as in AIS and PAIS;, features a modification of the amino acid from R to H at position 616.
+The protein's natural variant, known as in AIS, features a modification of the amino acid from R to P at position 616.
+The protein's natural variant, known as in AIS;, features a modification of the amino acid from L to P at position 617.
+The protein's natural variant, known as in PAIS, features a modification of the amino acid from L to R at position 617.
+The protein's natural variant, known as in AIS and PAIS; associated with G-598 in a PAIS patient; loss of DNA-binding activity, features a modification of the amino acid from R to P at position 618.
+The protein's natural variant, known as in prostate cancer; loss of DNA binding; somatic mutation, features a modification of the amino acid from C to Y at position 620.
+The protein's natural variant, known as in prostate cancer;, features a modification of the amino acid from R to Q at position 630.
+The protein's natural variant, known as in prostate cancer, features a modification of the amino acid from K to T at position 631.
+The protein's natural variant, known as in prostate cancer;, features a modification of the amino acid from S to N at position 648.
+The protein's natural variant, known as in AIS and PAIS, features a modification of the amino acid from I to N at position 665.
+The protein's natural variant, known as in prostate cancer, features a modification of the amino acid from Q to R at position 671.
+The protein's natural variant, known as in PAIS, features a modification of the amino acid from P to H at position 672.
+The protein's natural variant, known as in prostate cancer, features a modification of the amino acid from I to T at position 673.
+The protein's natural variant, known as in AIS;, features a modification of the amino acid from L to P at position 678.
+The protein's natural variant, known as in AIS;, features a modification of the amino acid from E to K at position 682.
+The protein's natural variant, known as in PAIS, features a modification of the amino acid from P to T at position 683.
+The protein's natural variant, known as in prostate cancer, features a modification of the amino acid from G to A at position 684.
+The protein's natural variant, known as in AIS;, features a modification of the amino acid from V to I at position 685.
+The protein's natural variant, known as in PAIS, features a modification of the amino acid from C to R at position 687.
+The protein's natural variant, known as in PAIS, features a modification of the amino acid from A to V at position 688.
+The protein's natural variant, known as in AIS, features a modification of the amino acid from G to E at position 689.
+The protein's natural variant, known as in AIS, features a modification of the amino acid from D to H at position 696.
+The protein's natural variant, known as in AIS; almost complete loss of androgen binding and transcription activation;, features a modification of the amino acid from D to N at position 696.
+The protein's natural variant, known as in AIS, features a modification of the amino acid from D to V at position 696.
+The protein's natural variant, known as in AIS, features a modification of the amino acid from L to M at position 701.
+The protein's natural variant, known as in AIS;, features a modification of the amino acid from L to F at position 702.
+The protein's natural variant, known as in AIS and prostate cancer;, features a modification of the amino acid from L to H at position 702.
+The protein's natural variant, known as in AIS, features a modification of the amino acid from S to A at position 703.
+The protein's natural variant, known as in AIS, features a modification of the amino acid from S to C at position 704.
+The protein's natural variant, known as in PAIS and AIS, features a modification of the amino acid from S to G at position 704.
+The protein's natural variant, known as in AIS;, features a modification of the amino acid from N to S at position 706.
+The protein's natural variant, known as in AIS, features a modification of the amino acid from N to Y at position 706.
+The protein's natural variant, known as in AIS;, features a modification of the amino acid from L to R at position 708.
+The protein's natural variant, known as in PAIS, features a modification of the amino acid from G to A at position 709.
+The protein's natural variant, known as in AIS, features a modification of the amino acid from G to V at position 709.
+The protein's natural variant, known as in AIS, features a modification of the amino acid from R to T at position 711.
+The protein's natural variant, known as in PAIS, features a modification of the amino acid from Q to E at position 712.
+The protein's natural variant, known as in PAIS;, features a modification of the amino acid from L to F at position 713.
+The protein's natural variant, known as in prostate cancer; gain in function;, features a modification of the amino acid from V to M at position 716.
+The protein's natural variant, known as in prostate cancer, features a modification of the amino acid from K to E at position 718.
+The protein's natural variant, known as in prostate cancer; found in bone metastases, features a modification of the amino acid from K to E at position 721.
+The protein's natural variant, known as in prostate cancer; somatic mutation;, features a modification of the amino acid from A to T at position 722.
+The protein's natural variant, known as in AIS, features a modification of the amino acid from L to F at position 723.
+The protein's natural variant, known as in AIS, features a modification of the amino acid from P to S at position 724.
+The protein's natural variant, known as in AIS and prostate cancer, features a modification of the amino acid from G to D at position 725.
+The protein's natural variant, known as in a patient with severe hypospadias;, features a modification of the amino acid from F to L at position 726.
+The protein's natural variant, known as in prostate cancer;, features a modification of the amino acid from R to L at position 727.
+The protein's natural variant, known as in AIS;, features a modification of the amino acid from N to K at position 728.
+The protein's natural variant, known as in PAIS, features a modification of the amino acid from L to S at position 729.
+The protein's natural variant, known as in prostate cancer; increases transcription activation;, features a modification of the amino acid from V to M at position 731.
+The protein's natural variant, known as in AIS, features a modification of the amino acid from D to N at position 733.
+The protein's natural variant, known as in AIS, features a modification of the amino acid from D to Y at position 733.
+The protein's natural variant, known as in PAIS, features a modification of the amino acid from Q to H at position 734.
+The protein's natural variant, known as in PAIS, features a modification of the amino acid from I to T at position 738.
+The protein's natural variant, known as in AIS, features a modification of the amino acid from W to R at position 742.
+The protein's natural variant, known as in PAIS, features a modification of the amino acid from M to I at position 743.
+The protein's natural variant, known as in PAIS, features a modification of the amino acid from M to V at position 743.
+The protein's natural variant, known as in AIS;, features a modification of the amino acid from G to E at position 744.
+The protein's natural variant, known as in PAIS and AIS;, features a modification of the amino acid from G to V at position 744.
+The protein's natural variant, known as in AIS and prostate cancer, features a modification of the amino acid from L to F at position 745.
+The protein's natural variant, known as in PAIS, features a modification of the amino acid from M to T at position 746.
+The protein's natural variant, known as in PAIS, features a modification of the amino acid from V to M at position 747.
+The protein's natural variant, known as in PAIS, features a modification of the amino acid from A to D at position 749.
+The protein's natural variant, known as in prostate cancer, features a modification of the amino acid from A to T at position 749.
+The protein's natural variant, known as in prostate cancer, features a modification of the amino acid from A to V at position 749.
+The protein's natural variant, known as in prostate cancer, features a modification of the amino acid from M to I at position 750.
+The protein's natural variant, known as in PAIS and AIS;, features a modification of the amino acid from M to V at position 750.
+The protein's natural variant, known as in AIS; loss of androgen binding, features a modification of the amino acid from G to D at position 751.
+The protein's natural variant, known as in prostate cancer, features a modification of the amino acid from G to S at position 751.
+The protein's natural variant, known as in AIS, features a modification of the amino acid from W to R at position 752.
+The protein's natural variant, known as in AIS;, features a modification of the amino acid from R to Q at position 753.
+The protein's natural variant, known as in PAIS and prostate cancer, features a modification of the amino acid from F to L at position 755.
+The protein's natural variant, known as in AIS, features a modification of the amino acid from F to V at position 755.
+The protein's natural variant, known as in prostate cancer, features a modification of the amino acid from T to A at position 756.
+The protein's natural variant, known as in PAIS;, features a modification of the amino acid from N to S at position 757.
+The protein's natural variant, known as in prostate cancer, features a modification of the amino acid from V to A at position 758.
+The protein's natural variant, known as in PAIS; 50% reduction in transactivation, features a modification of the amino acid from N to T at position 759.
+The protein's natural variant, known as in AIS, features a modification of the amino acid from S to F at position 760.
+The protein's natural variant, known as in prostate cancer, features a modification of the amino acid from S to P at position 760.
+The protein's natural variant, known as in AIS; loss of androgen binding, features a modification of the amino acid from L to F at position 763.
+The protein's natural variant, known as in PAIS and prostate cancer; partial loss of androgen binding;, features a modification of the amino acid from Y to C at position 764.
+The protein's natural variant, known as in AIS, features a modification of the amino acid from Y to H at position 764.
+The protein's natural variant, known as in AIS, features a modification of the amino acid from F to L at position 765.
+The protein's natural variant, known as in AIS; loss of androgen binding;, features a modification of the amino acid from A to T at position 766.
+The protein's natural variant, known as in AIS, features a modification of the amino acid from A to V at position 766.
+The protein's natural variant, known as in AIS, features a modification of the amino acid from P to S at position 767.
+The protein's natural variant, known as in AIS, features a modification of the amino acid from D to E at position 768.
+The protein's natural variant, known as in AIS, features a modification of the amino acid from L to P at position 769.
+The protein's natural variant, known as in PAIS;, features a modification of the amino acid from N to H at position 772.
+The protein's natural variant, known as in PAIS, features a modification of the amino acid from E to A at position 773.
+The protein's natural variant, known as in PAIS, features a modification of the amino acid from E to G at position 773.
+The protein's natural variant, known as in AIS; frequent mutation; loss of androgen binding;, features a modification of the amino acid from R to C at position 775.
+The protein's natural variant, known as in AIS and PAIS; almost complete loss of androgen binding;, features a modification of the amino acid from R to H at position 775.
+The protein's natural variant, known as in AIS, features a modification of the amino acid from R to W at position 780.
+The protein's natural variant, known as in PAIS and AIS;, features a modification of the amino acid from M to I at position 781.
+The protein's natural variant, known as in prostate cancer; somatic mutation, features a modification of the amino acid from S to N at position 783.
+The protein's natural variant, known as in AIS; loss of androgen binding and of transactivation, features a modification of the amino acid from C to Y at position 785.
+The protein's natural variant, known as in AIS;, features a modification of the amino acid from M to V at position 788.
+The protein's natural variant, known as in AIS;, features a modification of the amino acid from R to S at position 789.
+The protein's natural variant, known as in AIS, features a modification of the amino acid from L to F at position 791.
+The protein's natural variant, known as in prostate cancer, features a modification of the amino acid from S to P at position 792.
+The protein's natural variant, known as in AIS, features a modification of the amino acid from F to S at position 795.
+The protein's natural variant, known as in PAIS, AIS and prostate cancer; reduced transcription activation;, features a modification of the amino acid from Q to E at position 799.
+The protein's natural variant, known as in PAIS;, features a modification of the amino acid from C to Y at position 807.
+The protein's natural variant, known as in AIS; loss of transactivation, features a modification of the amino acid from M to R at position 808.
+The protein's natural variant, known as in PAIS;, features a modification of the amino acid from M to T at position 808.
+The protein's natural variant, known as in AIS; 25% androgen binding, features a modification of the amino acid from M to V at position 808.
+The protein's natural variant, known as in AIS;, features a modification of the amino acid from L to F at position 813.
+The protein's natural variant, known as in AIS and PAIS, features a modification of the amino acid from S to N at position 815.
+The protein's natural variant, known as in AIS, features a modification of the amino acid from G to A at position 821.
+The protein's natural variant, known as in PAIS, features a modification of the amino acid from L to V at position 822.
+The protein's natural variant, known as in PAIS, features a modification of the amino acid from F to V at position 828.
+The protein's natural variant, known as in prostate cancer, features a modification of the amino acid from L to P at position 831.
+The protein's natural variant, known as in AIS, features a modification of the amino acid from R to L at position 832.
+The protein's natural variant, known as in AIS; loss of androgen binding;, features a modification of the amino acid from R to Q at position 832.
+The protein's natural variant, known as in AIS; loss of androgen binding;, features a modification of the amino acid from Y to C at position 835.
+The protein's natural variant, known as in AIS;, features a modification of the amino acid from R to C at position 841.
+The protein's natural variant, known as in PAIS, features a modification of the amino acid from R to G at position 841.
+The protein's natural variant, known as in AIS;, features a modification of the amino acid from R to H at position 841.
+The protein's natural variant, known as in PAIS, features a modification of the amino acid from R to S at position 841.
+The protein's natural variant, known as in PAIS, features a modification of the amino acid from I to S at position 842.
+The protein's natural variant, known as in AIS;, features a modification of the amino acid from I to T at position 843.
+The protein's natural variant, known as in prostate cancer, features a modification of the amino acid from R to G at position 847.
+The protein's natural variant, known as in PAIS, features a modification of the amino acid from R to K at position 855.
+The protein's natural variant, known as in AIS;, features a modification of the amino acid from R to C at position 856.
+The protein's natural variant, known as in AIS; strongly reduced transcription activation;, features a modification of the amino acid from R to H at position 856.
+The protein's natural variant, known as in AIS;, features a modification of the amino acid from F to L at position 857.
+The protein's natural variant, known as in AIS, features a modification of the amino acid from L to R at position 864.
+The protein's natural variant, known as in AIS, features a modification of the amino acid from D to G at position 865.
+The protein's natural variant, known as in AIS; loss of androgen binding;, features a modification of the amino acid from D to N at position 865.
+The protein's natural variant, known as in AIS;, features a modification of the amino acid from S to P at position 866.
+The protein's natural variant, known as in AIS, features a modification of the amino acid from V to E at position 867.
+The protein's natural variant, known as in PAIS;, features a modification of the amino acid from V to L at position 867.
+The protein's natural variant, known as in AIS and prostate cancer;, features a modification of the amino acid from V to M at position 867.
+The protein's natural variant, known as in PAIS;, features a modification of the amino acid from I to M at position 870.
+The protein's natural variant, known as in PAIS, features a modification of the amino acid from A to G at position 871.
+The protein's natural variant, known as in PAIS;, features a modification of the amino acid from A to V at position 871.
+The protein's natural variant, known as in AIS, features a modification of the amino acid from R to G at position 872.
+The protein's natural variant, known as in AIS, features a modification of the amino acid from H to R at position 875.
+The protein's natural variant, known as in prostate cancer; increases affinity for testosterone and androgen sensitivity; increased transcription activation;, features a modification of the amino acid from H to Y at position 875.
+The protein's natural variant, known as in prostate cancer; found in bone metastases; alters receptor specificity so that transcription is activated by antiandrogens such as cyproterone acetate;, features a modification of the amino acid from T to A at position 878.
+The protein's natural variant, known as in prostate cancer;, features a modification of the amino acid from T to S at position 878.
+The protein's natural variant, known as in AIS, features a modification of the amino acid from D to Y at position 880.
+The protein's natural variant, known as in prostate cancer, features a modification of the amino acid from L to Q at position 881.
+The protein's natural variant, known as in AIS, features a modification of the amino acid from L to V at position 882.
+The protein's natural variant, known as in AIS;, features a modification of the amino acid from M to V at position 887.
+The protein's natural variant, known as in AIS and PAIS;, features a modification of the amino acid from V to M at position 890.
+The protein's natural variant, known as in prostate cancer, features a modification of the amino acid from D to N at position 891.
+The protein's natural variant, known as in prostate cancer, features a modification of the amino acid from F to L at position 892.
+The protein's natural variant, known as in AIS, features a modification of the amino acid from P to L at position 893.
+The protein's natural variant, known as in AIS; low androgen binding and transactivation, features a modification of the amino acid from M to T at position 896.
+The protein's natural variant, known as in prostate cancer, features a modification of the amino acid from A to T at position 897.
+The protein's natural variant, known as in AIS;, features a modification of the amino acid from I to T at position 899.
+The protein's natural variant, known as in prostate cancer;, features a modification of the amino acid from Q to R at position 903.
+The protein's natural variant, known as in PAIS, features a modification of the amino acid from V to M at position 904.
+The protein's natural variant, known as in AIS, features a modification of the amino acid from P to H at position 905.
+The protein's natural variant, known as in AIS, features a modification of the amino acid from P to S at position 905.
+The protein's natural variant, known as in AIS; almost complete loss of transcription activation, features a modification of the amino acid from L to F at position 908.
+The protein's natural variant, known as in prostate cancer, features a modification of the amino acid from G to E at position 910.
+The protein's natural variant, known as in PAIS, features a modification of the amino acid from G to R at position 910.
+The protein's natural variant, known as in prostate cancer, features a modification of the amino acid from K to R at position 911.
+The protein's natural variant, known as in PAIS, features a modification of the amino acid from V to L at position 912.
+The protein's natural variant, known as in PAIS, features a modification of the amino acid from P to S at position 914.
+The protein's natural variant, known as in AIS, features a modification of the amino acid from F to L at position 917.
+The protein's natural variant, known as in AIS, features a modification of the amino acid from H to R at position 918.
+The protein's natural variant, known as in prostate cancer, features a modification of the amino acid from Q to R at position 920.
+The protein's natural variant, known as in SP mutation, features a modification of the amino acid from P to L at position 76.
+The protein's natural variant, known as in strain: P1 / 1029/N5, features a modification of the amino acid from R to Q at position 81.
+The protein's natural variant, known as in strain: P1 / 1029/N5, features a modification of the amino acid from R to Q at position 118.
+The protein's natural variant, known as in strain: P1 / 1029/N5, features a modification of the amino acid from G to E at position 123.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from P to L at position 339.
+The protein's natural variant, known as in NPHS3; gives rise to focal segmental glomerulosclerosis rather than diffuse mesangial sclerosis;, features a modification of the amino acid from S to L at position 1484.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from C to G at position 196.
+The protein's natural variant, known as in strain: ATCCVR-358 /Fuller / CIP 107027, features a modification of the amino acid from R to RCQL at position 103.
+The protein's natural variant, known as in DFNA41; found in heterozygous status in patients; abolished ATP-stimulated permeability;, features a modification of the amino acid from V to L at position 60.
+The protein's natural variant, known as in DFNA41;, features a modification of the amino acid from G to R at position 353.
+The protein's natural variant, known as in CMT2M;, features a modification of the amino acid from G to R at position 358.
+The protein's natural variant, known as in CNM1;, features a modification of the amino acid from E to K at position 368.
+The protein's natural variant, known as in CNM1, features a modification of the amino acid from E to Q at position 368.
+The protein's natural variant, known as in CNM1;, features a modification of the amino acid from R to Q at position 369.
+The protein's natural variant, known as in CNM1; reduced association with the centrosome;, features a modification of the amino acid from R to W at position 369.
+The protein's natural variant, known as in LCCS5; hypomorphic mutation impacting on endocytosis;, features a modification of the amino acid from F to V at position 379.
+The protein's natural variant, known as in CNM1; reduced association with the centrosome; COS7 cells show a reduced uptake of transferrin and low-density lipoprotein complex;, features a modification of the amino acid from R to W at position 465.
+The protein's natural variant, known as in CNM1;, features a modification of the amino acid from R to C at position 522.
+The protein's natural variant, known as in CNM1;, features a modification of the amino acid from R to H at position 522.
+The protein's natural variant, known as in CNM1;, features a modification of the amino acid from R to G at position 523.
+The protein's natural variant, known as in CMT2M;, features a modification of the amino acid from G to C at position 537.
+The protein's natural variant, known as in CNM1;, features a modification of the amino acid from E to K at position 560.
+The protein's natural variant, known as in CMTDIB; with neutropenia; COS7 cells show a reduced uptake of transferrin and low-density lipoprotein complex;, features a modification of the amino acid from K to E at position 562.
+The protein's natural variant, known as in CMT2M;, features a modification of the amino acid from L to H at position 570.
+The protein's natural variant, known as in CNM1;, features a modification of the amino acid from A to D at position 618.
+The protein's natural variant, known as in CNM1; severe;, features a modification of the amino acid from A to T at position 618.
+The protein's natural variant, known as in CNM1; severe;, features a modification of the amino acid from S to L at position 619.
+The protein's natural variant, known as in CNM1; severe;, features a modification of the amino acid from S to W at position 619.
+The protein's natural variant, known as in CNM1; centronuclear myopathy with cataracts;, features a modification of the amino acid from L to P at position 621.
+The protein's natural variant, known as in CNM1, features a modification of the amino acid from P to H at position 627.
+The protein's natural variant, known as in CNM1;, features a modification of the amino acid from P to R at position 627.
+The protein's natural variant, known as in CNM1; COS7 cells show a reduced uptake of transferrin and low-density lipoprotein complex, features a modification of the amino acid from E to K at position 650.
+The protein's natural variant, known as in strain: DL42 and RM 7004, features a modification of the amino acid from K to N at position 29.
+The protein's natural variant, known as in strain: DL42 and RM 7004, features a modification of the amino acid from F to L at position 106.
+The protein's natural variant, known as in strain: DL42 and RM 7004, features a modification of the amino acid from Q to R at position 151.
+The protein's natural variant, known as in strain: RM 7004, features a modification of the amino acid from S to P at position 256.
+The protein's natural variant, known as in strain: RM 7004, features a modification of the amino acid from N to D at position 274.
+The protein's natural variant, known as in protamine-M7, features a modification of the amino acid from E to Q at position 6.
+The natural variant of this protein is characterized by an amino acid alteration from I to M at position 22.
+The protein's natural variant, known as in strain: Isolate TK 17308, features a modification of the amino acid from T to P at position 176.
+The protein's natural variant, known as in strain: Isolate TK 17308, features a modification of the amino acid from HLP to LLL at position 198.
+The protein's natural variant, known as in strain: Isolate TK 17308, features a modification of the amino acid from A to S at position 240.
+The protein's natural variant, known as in strain: Isolate TK 17308, features a modification of the amino acid from T to P at position 264.
+The protein's natural variant, known as in strain: Isolate TK 17308, features a modification of the amino acid from H to Y at position 267.
+The protein's natural variant, known as in strain: Isolate TK 17308, features a modification of the amino acid from P to T at position 270.
+The protein's natural variant, known as in strain: Isolate TK 17308, features a modification of the amino acid from T to V at position 356.
+The protein's natural variant, known as in BPL_1D, BPL_2B, BPL_3E, BPL_3F, BPL_5A, BPL_5D, BPL_5F, BPL_6D, BPL_6E, BPL_7F, BPL_8A, BPL_8C, BPL_9H, BPL_10D, BPL_10G, BPL_11D, BPL_12B, BPL_13A, BPL_13F, Florida1Slow and Paris, features a modification of the amino acid from QN to G at position 29.
+The protein's natural variant, known as in strain: AfricaFast, BPL_1A, BPL_1B, BPL_1D, BPL_1G, BPL_2A, BPL_2B, BPL_2C, BPL_2D, BPL_2E, BPL_2G, BPL_2H, BPL_3B, BPL_3C, BPL_3D, BPL_3E, BPL_3F, BPL_4A, BPL_4C, BPL_4E, BPL_4G, BPL_5A, BPL_5D, BPL_5F, BPL_5G, BPL_5H, BPL_6A, BPL_6B, BPL_6D, BPL_6E, BPL_6F, BPL_6H, BPL_7C, BPL_7E, BPL_7F, BPL_8A, BPL_8C, BPL_8D, BPL_8E, BPL_8F, BPL_9A, BPL_9C, BPL_9F, BPL_9H, BPL_10C, BPL_10D, BPL_10E, BPL_10G, BPL_11B, BPL_11C, BPL_11D, BPL_11E, BPL_11F, BPL_11G, BPL_11H, BPL_12A, BPL_12B, BPL_12C, BPL_13A, BPL_13D, BPL_13F, FloridaFast, Florida1Slow, Paris and WashingtonFast, features a modification of the amino acid from I to A at position 32.
+The protein's natural variant, known as in strain: JapanSlow, features a modification of the amino acid from I to M at position 32.
+The protein's natural variant, known as in strain: BPL_1D, BPL_2B, BPL_3E, BPL_3F, BPL_9H, BPL_10D, BPL_10G, BPL_11D, BPL_12B and BPL_13A, features a modification of the amino acid from I to V at position 32.
+The protein's natural variant, known as in strain: AfricaFast, BPL_10C, BPL_10D, BPL_10E, BPL_10G, BPL_11B, BPL_11C, BPL_11D, BPL_11E, BPL_11F, BPL_11G, BPL_11H, BPL_12A, BPL_12B, BPL_12C, BPL_13A, BPL_13D, BPL_13F, BPL_1A, BPL_1B, BPL_1D, BPL_1G, BPL_2A, BPL_2B, BPL_2C, BPL_2D, BPL_2E, BPL_2G, BPL_2H, BPL_3A, BPL_3B, BPL_3C, BPL_3D, BPL_3E, BPL_3F, BPL_4A, BPL_4C, BPL_4E, BPL_4G, BPL_5A, BPL_5D, BPL_5F, BPL_5G, BPL_5H, BPL_6A, BPL_6B, BPL_6D, BPL_6E, BPL_6F, BPL_6H, BPL_7C, BPL_7E, BPL_7F, BPL_8A, BPL_8C, BPL_8D, BPL_8E, BPL_8F, BPL_9A, BPL_9C, BPL_9F, BPL_9H, Florida1Slow, FloridaFast, JapanSlow, Oregon-R, Paris and WashingtonFast, features a modification of the amino acid from Q to L at position 43.
+The protein's natural variant, known as in strain: BPL_1A, BPL_1G, BPL_2A, BPL_2G, BPL_2H, BPL_3C, BPL_4A, BPL_4C, BPL_4G, BPL_5H, BPL_6H, BPL_7C, BPL_10E, BPL_11C, BPL_11H, BPL_12A and WashingtonFast, features a modification of the amino acid from D to Y at position 60.
+The protein's natural variant, known as in strain: BPL_1B, BPL_9F and BPL_13D, features a modification of the amino acid from C to R at position 79.
+The protein's natural variant, known as in strain: BPL_10C, BPL_10D, BPL_10E, BPL_10G, BPL_10H, BPL_11B, BPL_11C, BPL_11D, BPL_11F, BPL_11G, BPL_11H, BPL_12A, BPL_12B, BPL_12C, BPL_13A, BPL_13C, BPL_13D, BPL_13F, BPL_1A, BPL_1B, BPL_1C, BPL_1D, BPL_1E, BPL_1G, BPL_1H, BPL_2A, BPL_2B, BPL_2C, BPL_2D, BPL_2E, BPL_2G, BPL_2H, BPL_3A, BPL_3B, BPL_3C, BPL_3D, BPL_3E, BPL_3F, BPL_3G, BPL_3H, BPL_4A, BPL_4B, BPL_4C, BPL_4E, BPL_4G, BPL_5A, BPL_5D, BPL_5E, BPL_5F, BPL_5G, BPL_5H, BPL_6A, BPL_6B, BPL_6D, BPL_6E, BPL_6F, BPL_6H, BPL_7B, BPL_7C, BPL_7E, BPL_7F, BPL_7H, BPL_8A, BPL_8C, BPL_8D, BPL_8E, BPL_8F, BPL_8G, BPL_9A, BPL_9C, BPL_9F, BPL_9H, FrenchSlow and Paris, features a modification of the amino acid from T to S at position 231.
+The protein's natural variant, known as in strain: BPL_7A, BPL_9D, BPL_10A and BPL_11E, features a modification of the amino acid from A to D at position 247.
+The protein's natural variant, known as in strain: BPL_1E, features a modification of the amino acid from A to V at position 274.
+The protein's natural variant, known as in strain: BPL_3G, features a modification of the amino acid from V to D at position 290.
+The protein's natural variant, known as in strain: AfricaFast, AfricaSlow, BPL_10A, BPL_10C, BPL_10D, BPL_10E, BPL_10G, BPL_10H, BPL_11B, BPL_11C, BPL_11D, BPL_11E, BPL_11F, BPL_11G, BPL_11H, BPL_12A, BPL_12B, BPL_12C, BPL_12F, BPL_13A, BPL_13B, BPL_13C, BPL_13D, BPL_13F, BPL_1A, BPL_1B, BPL_1C, BPL_1D, BPL_1E, BPL_1F, BPL_1G, BPL_1H, BPL_2A, BPL_2B, BPL_2C, BPL_2D, BPL_2E, BPL_2F, BPL_2G, BPL_2H, BPL_3A, BPL_3B, BPL_3C, BPL_3D, BPL_3E, BPL_3F, BPL_3G, BPL_3H, BPL_4A, BPL_4B, BPL_4C, BPL_4E, BPL_4G, BPL_5A, BPL_5B, BPL_5D, BPL_5E, BPL_5F, BPL_5G, BPL_5H, BPL_6A, BPL_6B, BPL_6D, BPL_6E, BPL_6F, BPL_6H, BPL_7A, BPL_7B, BPL_7C, BPL_7E, BPL_7F, BPL_7G, BPL_7H, BPL_8A, BPL_8B, BPL_8C, BPL_8D, BPL_8E, BPL_8F, BPL_8G, BPL_8H, BPL_9A, BPL_9B, BPL_9C, BPL_9D, BPL_9F, BPL_9H, Florida1Slow, Florida2Slow, FloridaFast, FrenchFast, FrenchSlow, JapanFast, JapanSlow, Paris and WashingtonFast, features a modification of the amino acid from S to R at position 331.
+The protein's natural variant, known as in strain: BPL_6H, BPL_7C, BPL_11F and BPL_12A, features a modification of the amino acid from S to L at position 356.
+The protein's natural variant, known as in strain: BPL_1C, features a modification of the amino acid from Q to E at position 389.
+The protein's natural variant, known as in strain: BPL_1H, BPL_3H, BPL_4B, BPL_5E, BPL_7B, BPL_7H, BPL_8G, BPL_10H and BPL_13C, features a modification of the amino acid from P to L at position 393.
+The protein's natural variant, known as in strain: FrenchSlow, features a modification of the amino acid from P to S at position 397.
+The protein's natural variant, known as in strain: FrenchFast, features a modification of the amino acid from K to M at position 432.
+The protein's natural variant, known as in strain: BPL_3B and BPL_8F, features a modification of the amino acid from R to I at position 444.
+The protein's natural variant, known as in strain: AfricaSlow, AfricaFast, FloridaFast, Florida1Slow, Florida2Slow, FrenchSlow, JapanSlow, Paris and WashingtonFast, features a modification of the amino acid from D to E at position 542.
+The protein's natural variant, known as in IMGTALLELEIGLC7*01, features a modification of the amino acid from N to Y at position 34.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from Q to R at position 636.
+The protein's natural variant, known as in CLSS; abolishes the antagonistic effect of LRP4 on LRP6-mediated activation of Wnt signaling;, features a modification of the amino acid from D to N at position 137.
+The protein's natural variant, known as in CLSS; abolishes the antagonistic effect of LRP4 on LRP6-mediated activation of Wnt signaling;, features a modification of the amino acid from C to Y at position 160.
+The protein's natural variant, known as in CLSS; abolishes the antagonistic effect of LRP4 on LRP6-mediated activation of Wnt signaling;, features a modification of the amino acid from D to N at position 449.
+The protein's natural variant, known as in CLSS;, features a modification of the amino acid from T to P at position 461.
+The protein's natural variant, known as in CLSS; abolishes the antagonistic effect of LRP4 on LRP6-mediated activation of Wnt signaling, features a modification of the amino acid from L to F at position 473.
+The protein's natural variant, known as in CLSS; abolishes the antagonistic effect of LRP4 on LRP6-mediated activation of Wnt signaling;, features a modification of the amino acid from D to N at position 529.
+The protein's natural variant, known as in CLSS, features a modification of the amino acid from C to R at position 1017.
+The protein's natural variant, known as in SOST2; impairs the interaction with SOST; loss of function as facilitator of SOST-mediated inhibition of Wnt signaling; has no effect on AGRN-mediated MUSK signaling; retains the ability to bind AGRN and MUSK;, features a modification of the amino acid from R to W at position 1170.
+The protein's natural variant, known as in SOST2; impairs the interaction with SOST; loss of function as facilitator of SOST-mediated inhibition of Wnt signaling; has no effect on AGRN-mediated MUSK signaling; retains the ability to bind AGRN and MUSK;, features a modification of the amino acid from W to S at position 1186.
+The protein's natural variant, known as in CMS17; decreases binding affinity for AGRN and MUSK proteins; does not enhance downstream activation of the MUSK signaling pathway thus impairing clustering of AChRs;, features a modification of the amino acid from E to K at position 1233.
+The protein's natural variant, known as in CMS17; decreases binding affinity for AGRN and MUSK proteins; does not enhance downstream activation of the MUSK signaling pathway thus impairing clustering of AChRs;, features a modification of the amino acid from R to H at position 1277.
+The protein's natural variant, known as in strain: CAST/EiJ, features a modification of the amino acid from E to K at position 3.
+The protein's natural variant, known as in strain: PWK/PhJ, features a modification of the amino acid from F to Y at position 88.
+The protein's natural variant, known as in strain: CAST/EiJ, DBA/2J and PWK/PhJ, features a modification of the amino acid from E to G at position 112.
+The protein's natural variant, known as in strain: PWK/PhJ, features a modification of the amino acid from Q to R at position 227.
+The protein's natural variant, known as in strain: CAST/EiJ, DBA/2J and PWK/PhJ, features a modification of the amino acid from G to E at position 256.
+The protein's natural variant, known as in strain: DBA/2J, features a modification of the amino acid from R to Q at position 291.
+The protein's natural variant, known as in strain: PWK/PhJ, features a modification of the amino acid from K to N at position 337.
+The protein's natural variant, known as in strain: DBA/2J and CAST/EiJ, features a modification of the amino acid from S to G at position 484.
+The protein's natural variant, known as in strain: PWK/PhJ, features a modification of the amino acid from V to M at position 541.
+The protein's natural variant, known as in strain: AKR/J, features a modification of the amino acid from R to H at position 660.
+The protein's natural variant, known as in strain: PWK/PhJ, features a modification of the amino acid from L to I at position 664.
+The protein's natural variant, known as in strain: DBA/2J, features a modification of the amino acid from G to D at position 705.
+The protein's natural variant, known as in strain: PWK/PhJ, features a modification of the amino acid from D to N at position 857.
+The protein's natural variant, known as in strain: PWK/PhJ, features a modification of the amino acid from N to S at position 975.
+The protein's natural variant, known as in strain: DBA/2J, features a modification of the amino acid from R to Q at position 1030.
+The protein's natural variant, known as in strain: CAST/EiJ, features a modification of the amino acid from I to F at position 1043.
+The protein's natural variant, known as in strain: DBA/2J, features a modification of the amino acid from P to S at position 1110.
+The protein's natural variant, known as in strain: CAST/EiJ and DBA/2J, features a modification of the amino acid from K to R at position 1181.
+The protein's natural variant, known as in strain: Sing, TL and TS, features a modification of the amino acid from P to T at position 15.
+The protein's natural variant, known as in strain: Sing, features a modification of the amino acid from D to E at position 30.
+The protein's natural variant, known as in strain: Sing, features a modification of the amino acid from V to T at position 130.
+The protein's natural variant, known as in strain: TL, features a modification of the amino acid from D to N at position 202.
+The protein's natural variant, known as in strain: Sing, features a modification of the amino acid from KS to QN at position 347.
+The protein's natural variant, known as in strain: Sing, features a modification of the amino acid from I to T at position 371.
+The protein's natural variant, known as in strain: TS, features a modification of the amino acid from K to N at position 424.
+The protein's natural variant, known as in strain: TS, features a modification of the amino acid from K to R at position 450.
+The protein's natural variant, known as in strain: TS, features a modification of the amino acid from G to R at position 678.
+The protein's natural variant, known as in ADRP, features a modification of the amino acid from T to R at position 4.
+The protein's natural variant, known as in COXPD54; results in decreased mitochondrial tRNA 5'-end processing as shown by assays with mitochondrial ribonuclease P complex reconstituted in vitro, features a modification of the amino acid from N to S at position 412.
+The protein's natural variant, known as in COXPD54; unknown pathological significance, features a modification of the amino acid from R to C at position 421.
+The protein's natural variant, known as in COXPD54; unknown pathological significance, features a modification of the amino acid from A to D at position 434.
+The protein's natural variant, known as in COXPD54; results in decreased mitochondrial tRNA 5'-end processing as shown by assays with mitochondrial ribonuclease P complex reconstituted in vitro, features a modification of the amino acid from R to Q at position 445.
+The protein's natural variant, known as in COXPD54; decreased protein levels in homozygous patient cells; impaired mitochondrial RNA processing in homozygous patient cells, features a modification of the amino acid from A to V at position 485.
+The protein's natural variant, known as in PKND;, features a modification of the amino acid from G to E at position 79.
+The protein's natural variant, known as in PKND, features a modification of the amino acid from R to P at position 122.
+The protein's natural variant, known as in PKND;, features a modification of the amino acid from G to R at position 146.
+The protein's natural variant, known as in PKND;, features a modification of the amino acid from A to V at position 277.
+The protein's natural variant, known as in PKND; does not affect protein level; does not detect cysteine-type endopeptidase activity, features a modification of the amino acid from Y to C at position 283.
+The protein's natural variant, known as in PKND;, features a modification of the amino acid from L to P at position 309.
+The protein's natural variant, known as associated with higher levels of pregnenolone production by lymphomonocytes and with increased plasma levels of cholesterol-rich low density lipoprotein;, features a modification of the amino acid from T to A at position 147.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from H to R at position 439.
+The protein's natural variant, known as found in a lung cancer cell line, features a modification of the amino acid from V to L at position 49.
+The protein's natural variant, known as found in a brain cancer cell line;, features a modification of the amino acid from T to A at position 56.
+The protein's natural variant, known as found in a colon cancer cell line;, features a modification of the amino acid from R to G at position 66.
+The protein's natural variant, known as found in a bladder cancer cell line, features a modification of the amino acid from Q to E at position 90.
+The protein's natural variant, known as found in a malignant melanoma cell line, features a modification of the amino acid from Y to F at position 144.
+The protein's natural variant, known as found in a malignant melanoma cell line, features a modification of the amino acid from E to A at position 160.
+The protein's natural variant, known as found in a endometrial cancer cell line;, features a modification of the amino acid from R to C at position 202.
+The protein's natural variant, known as found in hematopoietic and lymphoid cancer cell lines;, features a modification of the amino acid from E to K at position 206.
+The protein's natural variant, known as found in hematopoietic and lymphoid cancer cell lines, features a modification of the amino acid from E to G at position 226.
+The protein's natural variant, known as found in a breast cancer cell line;, features a modification of the amino acid from I to V at position 228.
+The protein's natural variant, known as found in a case of clear cell renal carcinoma; somatic mutation, features a modification of the amino acid from T to P at position 232.
+The protein's natural variant, known as found in a renal carcinoma cell line, features a modification of the amino acid from I to T at position 233.
+The protein's natural variant, known as found in an ovary carcinoma cell line;, features a modification of the amino acid from A to T at position 256.
+The protein's natural variant, known as found in a malignant melanoma cell line;, features a modification of the amino acid from G to A at position 340.
+The protein's natural variant, known as found in a case of clear cell renal carcinoma; somatic mutation, features a modification of the amino acid from M to I at position 523.
+The protein's natural variant, known as found in a case of clear cell renal carcinoma; somatic mutation, features a modification of the amino acid from R to S at position 540.
+The protein's natural variant, known as found in a case of clear cell renal carcinoma; somatic mutation, features a modification of the amino acid from A to D at position 597.
+The protein's natural variant, known as found in a case of clear cell renal carcinoma; somatic mutation, features a modification of the amino acid from K to E at position 621.
+The protein's natural variant, known as found in a case of clear cell renal carcinoma; somatic mutation, features a modification of the amino acid from K to N at position 661.
+The protein's natural variant, known as found in a case of clear cell renal carcinoma; somatic mutation, features a modification of the amino acid from D to E at position 674.
+The protein's natural variant, known as found in hematopoietic, lymphoid, lung and liver cancer cell lines;, features a modification of the amino acid from Y to C at position 893.
+The protein's natural variant, known as found in a lung cancer cell line, features a modification of the amino acid from T to S at position 895.
+The protein's natural variant, known as found in a breast cancer cell line, features a modification of the amino acid from E to Q at position 922.
+The protein's natural variant, known as found in a colon cancer cell line, features a modification of the amino acid from K to Q at position 925.
+The protein's natural variant, known as requires 2 nucleotide substitutions; found in a colon cancer cell line, features a modification of the amino acid from P to Y at position 1079.
+The protein's natural variant, known as found in hematopoietic and lymphoid cancer cell lines;, features a modification of the amino acid from A to S at position 1098.
+The protein's natural variant, known as found in hematopoietic and lymphoid cancer cell lines;, features a modification of the amino acid from R to Q at position 1120.
+The protein's natural variant, known as found in a kidney cancer cell line, features a modification of the amino acid from G to S at position 1177.
+The protein's natural variant, known as found in a case of clear cell renal carcinoma; somatic mutation, features a modification of the amino acid from H to P at position 1204.
+The protein's natural variant, known as found in a breast cancer cell line, features a modification of the amino acid from E to Q at position 1287.
+The protein's natural variant, known as found in a lung cancer cell line, features a modification of the amino acid from G to E at position 1414.
+The protein's natural variant, known as found in a stomach cancer cell line, features a modification of the amino acid from G to C at position 1503.
+The protein's natural variant, known as found in an endometrial cancer cell line, features a modification of the amino acid from Q to H at position 1560.
+The protein's natural variant, known as found in a case of clear cell renal carcinoma; somatic mutation, features a modification of the amino acid from I to N at position 1614.
+The protein's natural variant, known as found in a breast cancer cell line;, features a modification of the amino acid from R to C at position 1647.
+The protein's natural variant, known as in 1/3 of the chains, features a modification of the amino acid from I to V at position 78.
+The protein's natural variant, known as in 1/3 of the chains, features a modification of the amino acid from V to I at position 112.
+The natural variant of this protein is characterized by an amino acid alteration from A to G at position 616.
+The protein's natural variant, known as in MMIHS2, features a modification of the amino acid from R to H at position 677.
+The protein's natural variant, known as in VSCM2; unknown pathological significance, features a modification of the amino acid from L to V at position 1555.
+The protein's natural variant, known as in AAT4;, features a modification of the amino acid from R to Q at position 1758.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from K to T at position 772.
+The protein's natural variant, known as rifampicin resistant, features a modification of the amino acid from S to P at position 549.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from S to C at position 904.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from P to S at position 1017.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from R to W at position 1794.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from D to N at position 1918.
+The protein's natural variant, known as in DEE5; could form a heterodimer with SPTBN1 but the heterodimer is thermally unstable; suggests a dominant negative effect, features a modification of the amino acid from M to MRM at position 2304.
+The protein's natural variant, known as in OOMD2; loss of function in oocyte maturation; decreased alpha/beta-tubulin heterodimer assembly;, features a modification of the amino acid from R to K at position 2.
+The protein's natural variant, known as in OOMD2; loss of function in meiotic spindle assembly and oocyte maturation; when expressed in mouse oocytes it leads to abnormal spindle structure and maturation arrest;, features a modification of the amino acid from A to V at position 54.
+The protein's natural variant, known as in OOMD2; loss of function in oocyte maturation; loss of function in meiotic spindle assembly; decreased alpha/beta-tubulin heterodimer assembly;, features a modification of the amino acid from S to L at position 176.
+The protein's natural variant, known as in OOMD2; decreased alpha/beta-tubulin heterodimer assembly; loss of function in meiotic spindle assembly;, features a modification of the amino acid from I to V at position 210.
+The protein's natural variant, known as in OOMD2; loss of function in oocyte maturation; decreased alpha/beta-tubulin heterodimer assembly;, features a modification of the amino acid from V to A at position 229.
+The protein's natural variant, known as in OOMD2; decreased alpha/beta-tubulin heterodimer assembly; loss of function in meiotic spindle assembly;, features a modification of the amino acid from T to M at position 238.
+The protein's natural variant, known as in OOMD2; loss of function in meiotic spindle assembly;, features a modification of the amino acid from V to M at position 255.
+The protein's natural variant, known as in OOMD2; loss of function in oocyte maturation; decreased alpha/beta-tubulin heterodimer assembly;, features a modification of the amino acid from R to Q at position 262.
+The protein's natural variant, known as in OOMD2; decreased alpha/beta-tubulin heterodimer assembly; does not affect function in meiotic spindle assembly;, features a modification of the amino acid from R to W at position 262.
+The protein's natural variant, known as in OOMD2; loss of function in meiotic spindle assembly, features a modification of the amino acid from T to P at position 285.
+The protein's natural variant, known as in OOMD2; loss of function in oocyte maturation; decreased alpha/beta-tubulin heterodimer assembly;, features a modification of the amino acid from M to I at position 300.
+The protein's natural variant, known as in OOMD2; loss of function in meiotic spindle assembly and oocyte maturation; when expressed in mouse oocytes it leads to abnormal spindle structure and maturation arrest, features a modification of the amino acid from R to H at position 320.
+The protein's natural variant, known as in OOMD2; loss of function in meiotic spindle assembly;, features a modification of the amino acid from N to S at position 348.
+The protein's natural variant, known as in OOMD2; loss of function in oocyte maturation; decreased alpha/beta-tubulin heterodimer assembly;, features a modification of the amino acid from M to T at position 363.
+The protein's natural variant, known as in OOMD2; loss of function in oocyte maturation; loss of function in meiotic spindle assembly; decreased alpha/beta-tubulin heterodimer assembly;, features a modification of the amino acid from D to N at position 417.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from C to F at position 512.
+The protein's natural variant, known as does not affect octanoyltransferase activity;, features a modification of the amino acid from T to A at position 46.
+The protein's natural variant, known as associated with susceptibility to infection with Mycobacterium ulcerans;, features a modification of the amino acid from D to N at position 543.
+The protein's natural variant, known as probable disease-associated variant found in a patient with early infantile epileptic encephalopathy;, features a modification of the amino acid from R to Q at position 571.
+The protein's natural variant, known as in Lp3.1b, features a modification of the amino acid from E to G at position 57.
+The protein's natural variant, known as in strain: ATCC 32354 / B311, features a modification of the amino acid from C to W at position 219.
+The protein's natural variant, known as in strain: ATCC 32354 / B311, features a modification of the amino acid from L to P at position 248.
+The protein's natural variant, known as in strain: ATCC 32354 / B311, features a modification of the amino acid from L to S at position 332.
+The protein's natural variant, known as in strain: ATCC 32354 / B311, features a modification of the amino acid from T to A at position 352.
+The protein's natural variant, known as in strain: GR4, features a modification of the amino acid from A to V at position 13.
+The protein's natural variant, known as in allele TAP2*01F, allele TAP2*01G, allele TAP2*01H, allele TAP2*02B and allele TAP2*02D;, features a modification of the amino acid from A to T at position 374.
+The protein's natural variant, known as in allele TAP2*01D, allele TAP2*01E, allele TAP2*01G, allele TAP2*02C and allele TAP2*02F;, features a modification of the amino acid from V to I at position 379.
+The protein's natural variant, known as in allele TAP2*01F and allele TAP2*02D;, features a modification of the amino acid from V to I at position 467.
+The protein's natural variant, known as variant of uncertain significance, features a modification of the amino acid from A to S at position 513.
+The protein's natural variant, known as in allele TAP2*01:02, allele TAP2*01D, allele TAP2*02E and allele TAP2*02F;, features a modification of the amino acid from A to T at position 565.
+The protein's natural variant, known as in allele TAP2*BKY2;, features a modification of the amino acid from M to V at position 577.
+The protein's natural variant, known as in allele TAP2*01:03 and allele TAP2*01G;, features a modification of the amino acid from R to C at position 651.
+The protein's natural variant, known as in allele TAP2*02:01, allele TAP2*02B, allele TAP2*02C, allele TAP2*02D, allele TAP2*02E, allele TAP2*02F, allele TAP2*04A and allele TAP2*Bky2;, features a modification of the amino acid from T to A at position 665.
+The protein's natural variant, known as in allele TAP2*02:01, allele TAP2*02B, allele TAP2*02C, allele TAP2*02D, allele TAP2*02E, allele TAP2*02F, allele TAP2*03A and allele TAP2*BKY2, features a modification of the amino acid from L to LQEGQDLYSRLVQQRLMD at position 686.
+The protein's natural variant, known as in strain: C57BL/6, features a modification of the amino acid from K to E at position 41.
+The protein's natural variant, known as in strain: C57BL/6, features a modification of the amino acid from V to A at position 51.
+The protein's natural variant, known as in HLD18; unknown pathological significance, features a modification of the amino acid from M to T at position 37.
+The protein's natural variant, known as in HLD18; decreased function in sphingolipid biosynthetic process, features a modification of the amino acid from N to D at position 113.
+The protein's natural variant, known as in HLD18; unknown pathological significance, features a modification of the amino acid from H to R at position 132.
+The protein's natural variant, known as in HLD18, features a modification of the amino acid from R to W at position 133.
+The protein's natural variant, known as in HLD18; unknown pathological significance, features a modification of the amino acid from N to D at position 189.
+The protein's natural variant, known as in HLD18; decreased function in sphingolipid biosynthetic process, features a modification of the amino acid from N to S at position 255.
+The protein's natural variant, known as in HLD18; decreased function in sphingolipid biosynthetic process; reduced protein levels; increased protein degradation, features a modification of the amino acid from A to V at position 280.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from I to M at position 1684.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from T to A at position 1860.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from Q to R at position 1900.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from Q to R at position 1915.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from S to G at position 1917.
+The natural variant of this protein is characterized by an amino acid alteration from K to I at position 106.
+The natural variant of this protein is characterized by an amino acid alteration from L to P at position 206.
+The natural variant of this protein is characterized by an amino acid alteration from L to P at position 218.
+The natural variant of this protein is characterized by an amino acid alteration from I to T at position 289.
+The natural variant of this protein is characterized by an amino acid alteration from S to P at position 295.
+The protein's natural variant, known as have ligand binding and signaling properties similar to wild-type;, features a modification of the amino acid from V to I at position 44.
+The protein's natural variant, known as associated with susceptibility to obesity; completely lacks signaling in response to agonist stimulation; coexpression of the wild-type and the mutant receptor shows that it does not exert dominant-negative activity on wild-type;, features a modification of the amino acid from I to N at position 146.
+The protein's natural variant, known as associated with susceptibility to obesity; in vitro expression studies demonstrate that the mutation causes complete loss of function; transfected cells show diffuse cytoplasmic staining indicating intracellular retention of the receptor;, features a modification of the amino acid from I to S at position 298.
+The natural variant of this protein is characterized by an amino acid alteration from CR to W at position 81.
+The protein's natural variant, known as in allele A2;, features a modification of the amino acid from P to L at position 156.
+The protein's natural variant, known as in allele Aw08;, features a modification of the amino acid from T to M at position 163.
+The protein's natural variant, known as in allele Aw08 and allele Bw08;, features a modification of the amino acid from R to G at position 176.
+The protein's natural variant, known as in allele Aw07, features a modification of the amino acid from R to W at position 198.
+The protein's natural variant, known as in allele Bel01; loss of manganese binding and reduced catalytic activity, features a modification of the amino acid from M to R at position 214.
+The protein's natural variant, known as in allele B106, features a modification of the amino acid from E to D at position 223.
+The protein's natural variant, known as in group B transferase; lower-level protein expression and intracellular cytoplasmic mislocation, features a modification of the amino acid from G to R at position 230.
+The protein's natural variant, known as in allele B(A), features a modification of the amino acid from P to A at position 234.
+The protein's natural variant, known as in allele Bw08;, features a modification of the amino acid from G to S at position 235.
+The protein's natural variant, known as in allele Bw08;, features a modification of the amino acid from L to M at position 266.
+The protein's natural variant, known as in allele Bw08;, features a modification of the amino acid from G to A at position 268.
+The protein's natural variant, known as in allele Aw08;, features a modification of the amino acid from G to R at position 268.
+The natural variant of this protein is characterized by an amino acid alteration from M to R at position 288.
+The protein's natural variant, known as in allele B104, features a modification of the amino acid from D to N at position 291.
+The protein's natural variant, known as in allele Bw08, features a modification of the amino acid from K to M at position 346.
+The protein's natural variant, known as in allele A107, features a modification of the amino acid from R to G at position 352.
+The protein's natural variant, known as in allele A106 and allele B3, features a modification of the amino acid from R to W at position 352.
+The protein's natural variant, known as in DEE60; unknown pathological significance;, features a modification of the amino acid from G to R at position 125.
+The protein's natural variant, known as in strain: Guyane 11, features a modification of the amino acid from KR to NG at position 546.
+The natural variant of this protein is characterized by an amino acid alteration from K to E at position 309.
+The natural variant of this protein is characterized by an amino acid alteration from S to G at position 590.
+The natural variant of this protein is characterized by an amino acid alteration from K to E at position 731.
+The natural variant of this protein is characterized by an amino acid alteration from G to E at position 1100.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from A to T at position 105.
+The natural variant of this protein is characterized by an amino acid alteration from N to D at position 109.
+The protein's natural variant, known as in HLD8, features a modification of the amino acid from L to F at position 104.
+The protein's natural variant, known as in HLD8, features a modification of the amino acid from S to G at position 268.
+The protein's natural variant, known as in CMT1I; affects RNA polymerase III assembly; no effect on nuclear localization, features a modification of the amino acid from E to K at position 363.
+The protein's natural variant, known as in CMT1I; affects RNA polymerase III assembly; no effect on nuclear localization;, features a modification of the amino acid from A to V at position 365.
+The protein's natural variant, known as in CMT1I; affects RNA polymerase III assembly; no effect on nuclear localization, features a modification of the amino acid from D to V at position 375.
+The protein's natural variant, known as in CMT1I; affects RNA polymerase III assembly; no effect on nuclear localization;, features a modification of the amino acid from L to S at position 426.
+The protein's natural variant, known as in HLD8;, features a modification of the amino acid from R to C at position 442.
+The protein's natural variant, known as in CMT1I; affects RNA polymerase III assembly; no effect on nuclear localization;, features a modification of the amino acid from T to R at position 462.
+The protein's natural variant, known as in HLD8;, features a modification of the amino acid from T to K at position 503.
+The protein's natural variant, known as in HLD8;, features a modification of the amino acid from V to E at position 523.
+The protein's natural variant, known as in HLD8, features a modification of the amino acid from C to R at position 527.
+The protein's natural variant, known as in HLD8;, features a modification of the amino acid from R to H at position 768.
+The protein's natural variant, known as in HLD8;, features a modification of the amino acid from D to E at position 926.
+The protein's natural variant, known as in CMT1I; affects RNA polymerase III assembly; no effect on nuclear localization;, features a modification of the amino acid from R to H at position 1046.
+The protein's natural variant, known as in DIAR10;, features a modification of the amino acid from L to P at position 34.
+The protein's natural variant, known as in TDH4; strongly reduces activity; does not respond to the increase of flavin mononucleotide concentration;, features a modification of the amino acid from R to W at position 101.
+The protein's natural variant, known as in TDH4; strongly reduces activity; does not respond to the increase of flavin mononucleotide concentration, features a modification of the amino acid from FI to L at position 106.
+The protein's natural variant, known as in TDH4; strongly reduces activity; marginally respond to the increase of flavin mononucleotide concentration; reduces protein stability;, features a modification of the amino acid from I to T at position 116.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from Y to H at position 531.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from D to N at position 573.
+The protein's natural variant, known as in allele Adh-UF, features a modification of the amino acid from N to V at position 9.
+The protein's natural variant, known as in allele Adh-UF, features a modification of the amino acid from A to D at position 46.
+The protein's natural variant, known as in strain: NC16, features a modification of the amino acid from A to V at position 46.
+The protein's natural variant, known as in allele Adh-F', features a modification of the amino acid from A to E at position 52.
+The protein's natural variant, known as in strain: NC16, features a modification of the amino acid from A to S at position 71.
+The protein's natural variant, known as in allele Adh-F, allele Adh-F-CHD, allele Adh-71K, allele Adh-JA-F and in strain: Berkeley, features a modification of the amino acid from K to T at position 193.
+The protein's natural variant, known as in allele Adh-F-CHD and allele Adh-71K, features a modification of the amino acid from P to S at position 215.
+The natural variant of this protein is characterized by an amino acid alteration from L to F at position 194.
+The protein's natural variant, known as found in a patient with progressive myoclonus epilepsy and dementia; unknown pathological significance;, features a modification of the amino acid from V to A at position 142.
+The protein's natural variant, known as found in a patient with late onset progressive myoclonus epilepsy; unknown pathological significance;, features a modification of the amino acid from M to I at position 342.
+The protein's natural variant, known as found in a patient with complex IV deficiency and non-lethal infantile mitochondrial disease; unknown pathological significance, features a modification of the amino acid from D to Y at position 436.
+The protein's natural variant, known as found in a patient with complex IV deficiency and non-lethal infantile mitochondrial disease; unknown pathological significance, features a modification of the amino acid from L to F at position 441.
+The protein's natural variant, known as in a patient with amyotrophic lateral sclerosis;, features a modification of the amino acid from Q to P at position 362.
+The protein's natural variant, known as in CTRCT19;, features a modification of the amino acid from F to V at position 105.
+The natural variant of this protein is characterized by an amino acid alteration from S to G at position 162.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to H at position 121.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from G to R at position 291.
+The protein's natural variant, known as in NAFLD1; unknown pathological significance;, features a modification of the amino acid from A to T at position 76.
+The protein's natural variant, known as in NAFLD1; unknown pathological significance, features a modification of the amino acid from A to V at position 104.
+The protein's natural variant, known as associated with increased hepatic fat content and serum aspartate aminotransferase concentrations; probable gain-of-function variant; 2-fold increase in 1-acylglycerol-3-phosphate O-acyltransferase/lysophosphatidic acid acyltransferase activity; results on glycerolipid hydrolysis activity are controversial with reduction in triacylglycerol, diacylglycerol and monoacylglycerol hydrolase activity or no effect compared to wild-type in which this activity may be very low; does not affect subcellular location, nor association with lipid droplets;, features a modification of the amino acid from I to M at position 148.
+The protein's natural variant, known as in NAFLD1; unknown pathological significance;, features a modification of the amino acid from T to M at position 200.
+The protein's natural variant, known as associated with lower hepatic fat content in African Americans;, features a modification of the amino acid from S to I at position 453.
+The protein's natural variant, known as in EA6;, features a modification of the amino acid from P to R at position 290.
+The protein's natural variant, known as in strain: PCI 219, features a modification of the amino acid from M to V at position 96.
+The protein's natural variant, known as in strain: PAI, features a modification of the amino acid from M to I at position 295.
+The protein's natural variant, known as in strain: PAI, features a modification of the amino acid from N to D at position 392.
+The protein's natural variant, known as in Sverdlovsk sample, features a modification of the amino acid from F to L at position 560.
+The protein's natural variant, known as in strain: BA1024, features a modification of the amino acid from P to S at position 565.
+The protein's natural variant, known as in strain: BA1024, V770-NP1-R, Carbosap and Ferrara, features a modification of the amino acid from A to V at position 600.
+The protein's natural variant, known as in allele ADH3*2/gamma-2;, features a modification of the amino acid from R to Q at position 272.
+The protein's natural variant, known as in allele ADH3*2/gamma-2;, features a modification of the amino acid from I to V at position 350.
+The protein's natural variant, known as in a glioblastoma multiforme sample; somatic mutation, features a modification of the amino acid from G to D at position 243.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from E to K at position 117.
+The protein's natural variant, known as in DEDHIL, features a modification of the amino acid from T to A at position 416.
+The protein's natural variant, known as in DEDHIL, features a modification of the amino acid from T to I at position 416.
+The protein's natural variant, known as in DEDHIL, features a modification of the amino acid from H to L at position 420.
+The protein's natural variant, known as in DEDHIL; no effect on protein abundance; changed proteasome-mediated ubiquitin-dependent protein catabolic process, features a modification of the amino acid from G to R at position 423.
+The protein's natural variant, known as in DEDHIL, features a modification of the amino acid from R to G at position 441.
+The protein's natural variant, known as in DEDHIL, features a modification of the amino acid from S to P at position 462.
+The protein's natural variant, known as in an acute lymphoblastic leukemia cell line; loss of interaction with substrate; does not affect interaction with SKP1 or STYX;, features a modification of the amino acid from R to C at position 465.
+The protein's natural variant, known as in DEDHIL; also found in a colorectal cancer sample;, features a modification of the amino acid from R to H at position 465.
+The protein's natural variant, known as in DEDHIL, features a modification of the amino acid from R to Q at position 479.
+The protein's natural variant, known as in DEDHIL; no effect on protein abundance; changed proteasome-mediated ubiquitin-dependent protein catabolic process, features a modification of the amino acid from D to G at position 480.
+The protein's natural variant, known as in DEDHIL, features a modification of the amino acid from R to H at position 505.
+The protein's natural variant, known as in an ovarian cancer cell line;, features a modification of the amino acid from R to L at position 505.
+The protein's natural variant, known as in DEDHIL; no effect on protein abundance; changed on proteasome-mediated ubiquitin-dependent protein catabolic process, features a modification of the amino acid from V to G at position 544.
+The protein's natural variant, known as in DEDHIL, features a modification of the amino acid from H to Y at position 580.
+The protein's natural variant, known as in DEDHIL, features a modification of the amino acid from S to A at position 582.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from S to L at position 582.
+The protein's natural variant, known as in DEDHIL, features a modification of the amino acid from A to V at position 599.
+The protein's natural variant, known as in DEDHIL; unknown pathological significance, features a modification of the amino acid from I to V at position 608.
+The protein's natural variant, known as in DEDHIL, features a modification of the amino acid from A to V at position 626.
+The protein's natural variant, known as in DEDHIL; no effect on protein abundance; changed proteasome-mediated ubiquitin-dependent protein catabolic process, features a modification of the amino acid from S to R at position 640.
+The protein's natural variant, known as in DEDHIL; no effect on protein abundance; changed on proteasome-mediated ubiquitin-dependent protein catabolic process, features a modification of the amino acid from R to P at position 674.
+The protein's natural variant, known as in DEDHIL; no effect on protein abundance; changed proteasome-mediated ubiquitin-dependent protein catabolic process, features a modification of the amino acid from R to W at position 674.
+The protein's natural variant, known as in DEDHIL; decreased protein abundance; no effect on proteasome-mediated ubiquitin-dependent protein catabolic process, features a modification of the amino acid from R to Q at position 689.
+The protein's natural variant, known as in DEDHIL, features a modification of the amino acid from R to W at position 689.
+The protein's natural variant, known as in MSD; loss of activity;, features a modification of the amino acid from L to F at position 20.
+The protein's natural variant, known as in MSD; loss of enzyme activity;, features a modification of the amino acid from S to P at position 155.
+The protein's natural variant, known as in MSD; loss of activity; decreases its specific enzyme activity to less than 1%; does not affect localization of the protein in the endoplasmic reticulum of MSD fibroblasts; protein stability is almost comparable to wild-type, features a modification of the amino acid from A to P at position 177.
+The protein's natural variant, known as in MSD; decreases its specific enzyme activity to less than 3%; does not affect localization of the protein in the endoplasmic reticulum of MSD fibroblasts; protein stability is almost comparable to wild-type;, features a modification of the amino acid from W to S at position 179.
+The protein's natural variant, known as in MSD; loss of activity;, features a modification of the amino acid from C to Y at position 218.
+The protein's natural variant, known as in MSD; loss of activity;, features a modification of the amino acid from R to W at position 224.
+The protein's natural variant, known as in MSD;, features a modification of the amino acid from G to R at position 247.
+The protein's natural variant, known as in MSD; loss of activity;, features a modification of the amino acid from N to I at position 259.
+The protein's natural variant, known as in MSD; mild phenotype; reduced but not abolished activity;, features a modification of the amino acid from G to V at position 263.
+The protein's natural variant, known as in MSD; retains some activity;, features a modification of the amino acid from P to L at position 266.
+The protein's natural variant, known as in MSD; loss of activity; decreases its specific enzyme activity to about 23%; does not affect localization of the protein in the endoplasmic reticulum of MSD fibroblasts; protein stability is decreased;, features a modification of the amino acid from A to V at position 279.
+The protein's natural variant, known as in MSD; loss of activity;, features a modification of the amino acid from C to R at position 336.
+The protein's natural variant, known as in MSD; reduced but not abolished activity;, features a modification of the amino acid from R to C at position 345.
+The protein's natural variant, known as in MSD; loss of activity;, features a modification of the amino acid from A to P at position 348.
+The protein's natural variant, known as in MSD; loss of activity;, features a modification of the amino acid from R to Q at position 349.
+The protein's natural variant, known as in MSD; loss of activity; decreases its specific enzyme activity to less than 1%; does not affect localization of the protein in the endoplasmic reticulum of MSD fibroblasts; protein stability is severely decreased;, features a modification of the amino acid from R to W at position 349.
+The protein's natural variant, known as in COXPD56; unknown pathological significance; compared to wild-type, only partly rescues the growth defect in deficient yeast, when tested on respiratory media at 36 degrees Celsius;, features a modification of the amino acid from S to P at position 86.
+The protein's natural variant, known as in COXPD56; unknown pathological significance; contrary to wild-type, unable to complement the growth defect in deficient yeast, features a modification of the amino acid from Y to C at position 110.
+The protein's natural variant, known as in COXPD56; unknown pathological significance; contrary to wild-type, unable to complement the growth defect in deficient yeast;, features a modification of the amino acid from P to L at position 137.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation, features a modification of the amino acid from Q to K at position 405.
+The protein's natural variant, known as in an ovarian serous carcinoma sample; somatic mutation;, features a modification of the amino acid from E to Q at position 604.
+The natural variant of this protein is characterized by an amino acid alteration from M to V at position 381.
+The protein's natural variant, known as in strain: Netherlands line N22, features a modification of the amino acid from L to Q at position 16.
+The protein's natural variant, known as in strain: Netherlands line N02 and Netherlands line N30, features a modification of the amino acid from P to T at position 142.
+The protein's natural variant, known as in strain: Netherlands line N02, Netherlands line N07, Netherlands line N17 and Netherlands line N30, features a modification of the amino acid from P to L at position 213.
+The protein's natural variant, known as in strain: Netherlands line N02 and Netherlands line N30, features a modification of the amino acid from A to V at position 292.
+The protein's natural variant, known as in strain: Netherlands line N22, features a modification of the amino acid from K to I at position 399.
+The protein's natural variant, known as in strain: Netherlands line N02 and Netherlands line N30, features a modification of the amino acid from E to G at position 404.
+The protein's natural variant, known as in strain: Netherlands line N22, features a modification of the amino acid from A to G at position 408.
+The protein's natural variant, known as in strain: Netherlands line N22, features a modification of the amino acid from H to N at position 479.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to R at position 22.
+The protein's natural variant, known as in OI2; rare variant; unknown pathological significance;, features a modification of the amino acid from P to T at position 146.
+The protein's natural variant, known as in OIEDS1; decreased N-terminal propeptide processing;, features a modification of the amino acid from G to D at position 188.
+The protein's natural variant, known as in OIEDS1; severely decreased cleavage of N-terminal propeptide; affects collagen fibril organization; collagen dermal fibrils in patients have smaller diameters than in age-matched controls;, features a modification of the amino acid from G to D at position 191.
+The protein's natural variant, known as in OI1;, features a modification of the amino acid from G to R at position 194.
+The protein's natural variant, known as in OI4, features a modification of the amino acid from G to R at position 197.
+The protein's natural variant, known as in OI1; patient diagnosed with OI1/OI4;, features a modification of the amino acid from G to V at position 200.
+The protein's natural variant, known as in OIEDS1, features a modification of the amino acid from G to C at position 203.
+The protein's natural variant, known as in OI3 and OIEDS1; small decrease of N-terminal propeptide; affects collagen fibril organization; collagen dermal fibrils in patients have smaller diameters than in age-matched controls;, features a modification of the amino acid from G to V at position 203.
+The protein's natural variant, known as in OIEDS1; small decrease of N-terminal propeptide; affects collagen fibril organization; collagen dermal fibrils in patients have smaller diameters than in age-matched controls;, features a modification of the amino acid from G to R at position 212.
+The protein's natural variant, known as in OI1; mild form;, features a modification of the amino acid from G to C at position 221.
+The protein's natural variant, known as in OI1; mild phenotype;, features a modification of the amino acid from G to C at position 224.
+The protein's natural variant, known as in OI;, features a modification of the amino acid from G to D at position 242.
+The protein's natural variant, known as in OIEDS1; affects collagen fibril organization; collagen dermal fibrils in patients have smaller diameters than in age-matched controls;, features a modification of the amino acid from G to E at position 254.
+The protein's natural variant, known as in OI4;, features a modification of the amino acid from G to R at position 257.
+The protein's natural variant, known as in OI1; mild form;, features a modification of the amino acid from G to R at position 263.
+The protein's natural variant, known as in OI1; mild form;, features a modification of the amino acid from G to V at position 263.
+The protein's natural variant, known as in OI1 and OIEDS1; affects collagen fibril organization; collagen dermal fibrils in patients have smaller diameters than in age-matched controls;, features a modification of the amino acid from G to E at position 266.
+The protein's natural variant, known as in OI1;, features a modification of the amino acid from G to C at position 272.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to D at position 275.
+The protein's natural variant, known as in OI1;, features a modification of the amino acid from G to S at position 287.
+The protein's natural variant, known as in OI1; the patient also has mutation Glu-1219; unknown pathological significance;, features a modification of the amino acid from E to K at position 288.
+The protein's natural variant, known as in OI2; rare variant; unknown pathological significance, features a modification of the amino acid from E to V at position 288.
+The protein's natural variant, known as in EDSCL1;, features a modification of the amino acid from R to C at position 312.
+The protein's natural variant, known as in OI1;, features a modification of the amino acid from G to V at position 320.
+The protein's natural variant, known as in OI3; mild to moderate form;, features a modification of the amino acid from G to R at position 332.
+The protein's natural variant, known as in OI4;, features a modification of the amino acid from G to C at position 338.
+The protein's natural variant, known as in OI1;, features a modification of the amino acid from V to F at position 349.
+The protein's natural variant, known as in OI3;, features a modification of the amino acid from G to R at position 350.
+The protein's natural variant, known as in OI4;, features a modification of the amino acid from G to C at position 353.
+The protein's natural variant, known as in OI2, features a modification of the amino acid from G to D at position 353.
+The protein's natural variant, known as in OI4;, features a modification of the amino acid from G to S at position 353.
+The protein's natural variant, known as in OI4; mild form;, features a modification of the amino acid from G to C at position 356.
+The protein's natural variant, known as in OI2, features a modification of the amino acid from G to V at position 368.
+The protein's natural variant, known as in OI4;, features a modification of the amino acid from G to C at position 383.
+The protein's natural variant, known as in OI; moderate form;, features a modification of the amino acid from G to C at position 389.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to R at position 389.
+The protein's natural variant, known as in OI2; rare variant; unknown pathological significance;, features a modification of the amino acid from A to T at position 390.
+The protein's natural variant, known as in OI4;, features a modification of the amino acid from G to A at position 398.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to D at position 398.
+The protein's natural variant, known as in OI4;, features a modification of the amino acid from G to C at position 401.
+The protein's natural variant, known as in OI; moderate form;, features a modification of the amino acid from G to C at position 404.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to C at position 422.
+The protein's natural variant, known as in OI2; lethal form;, features a modification of the amino acid from G to S at position 425.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to V at position 434.
+The protein's natural variant, known as in OI2, features a modification of the amino acid from G to D at position 455.
+The protein's natural variant, known as in OI2, features a modification of the amino acid from G to V at position 470.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to R at position 476.
+The protein's natural variant, known as in OI2, features a modification of the amino acid from G to V at position 509.
+The protein's natural variant, known as in OI4;, features a modification of the amino acid from G to C at position 527.
+The protein's natural variant, known as in OI2, OI3 and OI4; mild to lethal form;, features a modification of the amino acid from G to S at position 530.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to D at position 533.
+The protein's natural variant, known as in OI2, features a modification of the amino acid from G to A at position 548.
+The protein's natural variant, known as in OI1;, features a modification of the amino acid from P to R at position 555.
+The protein's natural variant, known as in OI4;, features a modification of the amino acid from G to C at position 560.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to R at position 560.
+The protein's natural variant, known as in OI4;, features a modification of the amino acid from G to S at position 560.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to R at position 569.
+The protein's natural variant, known as found in a patient with isolated osteopenia and vascular rupture; unknown pathological significance;, features a modification of the amino acid from R to C at position 574.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to R at position 581.
+The protein's natural variant, known as in OI3 and OI4;, features a modification of the amino acid from G to C at position 593.
+The protein's natural variant, known as in OI2 and OI3; moderate to lethal form;, features a modification of the amino acid from G to S at position 593.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to R at position 602.
+The protein's natural variant, known as in OI2, features a modification of the amino acid from G to D at position 605.
+The protein's natural variant, known as in OI2, features a modification of the amino acid from G to R at position 614.
+The protein's natural variant, known as in OI1;, features a modification of the amino acid from G to S at position 647.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to S at position 656.
+The protein's natural variant, known as in OI4;, features a modification of the amino acid from G to S at position 683.
+The protein's natural variant, known as in OI4;, features a modification of the amino acid from G to C at position 701.
+The protein's natural variant, known as in OI3;, features a modification of the amino acid from G to C at position 704.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to D at position 719.
+The protein's natural variant, known as in OI3;, features a modification of the amino acid from G to S at position 719.
+The protein's natural variant, known as in OI1;, features a modification of the amino acid from G to S at position 722.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to R at position 728.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to V at position 734.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to D at position 737.
+The protein's natural variant, known as in OI2, features a modification of the amino acid from G to R at position 740.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to S at position 743.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to V at position 743.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to V at position 764.
+The protein's natural variant, known as in OI3; severe;, features a modification of the amino acid from G to S at position 767.
+The protein's natural variant, known as in OI2; de novo mutation, features a modification of the amino acid from G to C at position 773.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to S at position 776.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to S at position 809.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to V at position 815.
+The protein's natural variant, known as in OI3;, features a modification of the amino acid from G to S at position 821.
+The protein's natural variant, known as in OI2, features a modification of the amino acid from G to R at position 824.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to D at position 833.
+The protein's natural variant, known as in OI2; mild to moderate form;, features a modification of the amino acid from G to S at position 839.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to R at position 842.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to R at position 845.
+The protein's natural variant, known as in OI2, features a modification of the amino acid from G to R at position 848.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to D at position 851.
+The protein's natural variant, known as in OI2; rare variant; unknown pathological significance, features a modification of the amino acid from N to H at position 855.
+The protein's natural variant, known as in OI3 and OI2;, features a modification of the amino acid from G to S at position 866.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to C at position 869.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to S at position 875.
+The protein's natural variant, known as in OI2 and OI3; extremely severe form;, features a modification of the amino acid from G to S at position 884.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to C at position 896.
+The protein's natural variant, known as in OI2, features a modification of the amino acid from G to D at position 896.
+The protein's natural variant, known as found in a patient with mild osteogenesis imperfecta; uncertain pathological significance;, features a modification of the amino acid from G to S at position 906.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to C at position 926.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to C at position 947.
+The protein's natural variant, known as in OI2, features a modification of the amino acid from G to D at position 977.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to V at position 980.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to C at position 1001.
+The protein's natural variant, known as in OI4;, features a modification of the amino acid from G to S at position 1010.
+The protein's natural variant, known as in CAFYD;, features a modification of the amino acid from R to C at position 1014.
+The protein's natural variant, known as in OI3; severe form;, features a modification of the amino acid from G to S at position 1022.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to V at position 1022.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to R at position 1025.
+The protein's natural variant, known as in OI2 and OI3; moderate to lethal form;, features a modification of the amino acid from G to S at position 1040.
+The protein's natural variant, known as in OI2, features a modification of the amino acid from G to S at position 1043.
+The protein's natural variant, known as in OI3;, features a modification of the amino acid from G to S at position 1049.
+The protein's natural variant, known as in OI2, features a modification of the amino acid from G to GAPG at position 1052.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to D at position 1055.
+The protein's natural variant, known as in OI3 and OI4; mild form;, features a modification of the amino acid from G to S at position 1058.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to D at position 1061.
+The protein's natural variant, known as in OI4;, features a modification of the amino acid from G to S at position 1061.
+The protein's natural variant, known as in OIEDS1; affects dimer formation, helix stability and organization of collagen fibrils;, features a modification of the amino acid from R to C at position 1066.
+The protein's natural variant, known as in OI3; severe form;, features a modification of the amino acid from G to S at position 1076.
+The protein's natural variant, known as in OI1 and OI2; mild to moderate form;, features a modification of the amino acid from G to S at position 1079.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to C at position 1082.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to A at position 1088.
+The protein's natural variant, known as in OI1; de novo mutation; unknown pathological significance, features a modification of the amino acid from G to E at position 1088.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to S at position 1091.
+The protein's natural variant, known as found in a patient with isolated osteopenia and vascular rupture; unknown pathological significance;, features a modification of the amino acid from R to C at position 1093.
+The protein's natural variant, known as in OI2, features a modification of the amino acid from G to S at position 1094.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to D at position 1100.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to A at position 1106.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to C at position 1124.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to S at position 1142.
+The protein's natural variant, known as in OI3;, features a modification of the amino acid from G to S at position 1151.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to V at position 1151.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to R at position 1154.
+The protein's natural variant, known as in OI1;, features a modification of the amino acid from G to D at position 1157.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to C at position 1166.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to D at position 1172.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to S at position 1181.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to V at position 1184.
+The protein's natural variant, known as in OI2 and OI3; extremely severe form;, features a modification of the amino acid from G to S at position 1187.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from G to V at position 1187.
+The protein's natural variant, known as in OI1; mild form;, features a modification of the amino acid from G to C at position 1195.
+The protein's natural variant, known as in OI1;, features a modification of the amino acid from D to E at position 1219.
+The protein's natural variant, known as found in a patient with mild osteogenesis imperfecta associated with increased bone mineral density; results in defective type I procollagen processing; incorporation of the immature procollagen into the matrix leads to increased bone matrix mineralization and altered collagen fibril structure;, features a modification of the amino acid from D to N at position 1219.
+The protein's natural variant, known as in OI2; impaired pro-alpha chain association;, features a modification of the amino acid from D to H at position 1277.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from W to C at position 1312.
+The protein's natural variant, known as in OI2; impaired pro-alpha chain association;, features a modification of the amino acid from L to R at position 1388.
+The protein's natural variant, known as in OI2;, features a modification of the amino acid from D to N at position 1413.
+The protein's natural variant, known as in OI3;, features a modification of the amino acid from L to P at position 1464.
+The protein's natural variant, known as in strain: HG84, Singapore and w cv, features a modification of the amino acid from M to MDMGMGM at position 7.
+The protein's natural variant, known as in strain: HG84, Singapore and w cv, features a modification of the amino acid from F to I at position 12.
+The protein's natural variant, known as in strain: Shanghai and Tananarive, features a modification of the amino acid from L to M at position 348.
+The protein's natural variant, known as in ALGS1, features a modification of the amino acid from A to V at position 31.
+The protein's natural variant, known as in ALGS1, features a modification of the amino acid from G to D at position 33.
+The protein's natural variant, known as in ALGS1;, features a modification of the amino acid from G to S at position 33.
+The protein's natural variant, known as in ALGS1, features a modification of the amino acid from G to V at position 33.
+The protein's natural variant, known as in ALGS1; the mutant is unable to activate Notch signaling;, features a modification of the amino acid from L to S at position 37.
+The protein's natural variant, known as in ALGS1, features a modification of the amino acid from I to S at position 39.
+The protein's natural variant, known as in ALGS1, features a modification of the amino acid from L to P at position 40.
+The protein's natural variant, known as in biliary atresia; extrahepatic;, features a modification of the amino acid from V to L at position 45.
+The protein's natural variant, known as in biliary atresia; extrahepatic, features a modification of the amino acid from N to D at position 53.
+The protein's natural variant, known as in biliary atresia; extrahepatic, features a modification of the amino acid from K to M at position 65.
+The protein's natural variant, known as in ALGS1, features a modification of the amino acid from F to S at position 75.
+The protein's natural variant, known as in ALGS1;, features a modification of the amino acid from C to S at position 78.
+The protein's natural variant, known as in ALGS1, features a modification of the amino acid from L to H at position 79.
+The protein's natural variant, known as in ALGS1, features a modification of the amino acid from C to R at position 92.
+The protein's natural variant, known as in ALGS1, features a modification of the amino acid from C to Y at position 92.
+The protein's natural variant, known as in ALGS1, features a modification of the amino acid from I to N at position 120.
+The protein's natural variant, known as in ALGS1;, features a modification of the amino acid from P to S at position 123.
+The protein's natural variant, known as in ALGS1;, features a modification of the amino acid from A to T at position 127.
+The protein's natural variant, known as in ALGS1;, features a modification of the amino acid from P to R at position 129.
+The protein's natural variant, known as in ALGS1, features a modification of the amino acid from I to T at position 152.
+The protein's natural variant, known as in ALGS1, features a modification of the amino acid from A to P at position 155.
+The protein's natural variant, known as in ALGS1, features a modification of the amino acid from P to L at position 163.
+The protein's natural variant, known as in ALGS1;, features a modification of the amino acid from P to R at position 163.
+The protein's natural variant, known as in ALGS1, features a modification of the amino acid from Y to N at position 181.
+The protein's natural variant, known as in ALGS1;, features a modification of the amino acid from R to C at position 184.
+The protein's natural variant, known as in ALGS1, features a modification of the amino acid from R to G at position 184.
+The protein's natural variant, known as in ALGS1; loss of expression at the cell membrane;, features a modification of the amino acid from R to H at position 184.
+The protein's natural variant, known as in ALGS1, features a modification of the amino acid from R to L at position 184.
+The protein's natural variant, known as in ALGS1, features a modification of the amino acid from C to S at position 187.
+The protein's natural variant, known as in ALGS1, features a modification of the amino acid from C to Y at position 187.
+The protein's natural variant, known as in biliary atresia; extrahepatic, features a modification of the amino acid from R to K at position 203.
+The protein's natural variant, known as in ALGS1, features a modification of the amino acid from C to F at position 220.
+The protein's natural variant, known as in ALGS1, features a modification of the amino acid from W to C at position 224.
+The protein's natural variant, known as in ALGS1, features a modification of the amino acid from C to G at position 229.
+The protein's natural variant, known as in ALGS1, features a modification of the amino acid from C to Y at position 229.
+The protein's natural variant, known as in DCHE; the mutant is unable to activate Notch signaling;, features a modification of the amino acid from C to Y at position 234.
+The protein's natural variant, known as in ALGS1, features a modification of the amino acid from R to G at position 252.
+The protein's natural variant, known as in ALGS1, features a modification of the amino acid from G to S at position 256.
+The protein's natural variant, known as in ALGS1;, features a modification of the amino acid from P to L at position 269.
+The protein's natural variant, known as in ALGS1, features a modification of the amino acid from C to R at position 271.
+The protein's natural variant, known as in TOF; temperature sensitive mutation; the protein is abnormally glycosylated and retained intracellularly; unable to activate Notch signaling;, features a modification of the amino acid from G to D at position 274.
+The protein's natural variant, known as in ALGS1;, features a modification of the amino acid from C to F at position 284.
+The protein's natural variant, known as in ALGS1, features a modification of the amino acid from W to C at position 288.
+The protein's natural variant, known as in ALGS1;, features a modification of the amino acid from G to R at position 386.
+The protein's natural variant, known as in ALGS1, features a modification of the amino acid from C to W at position 436.
+The protein's natural variant, known as in ALGS1, features a modification of the amino acid from C to F at position 438.
+The protein's natural variant, known as in ALGS1;, features a modification of the amino acid from N to S at position 504.
+The protein's natural variant, known as in CMT2HH; decreased glycosylation; decreased expression at the cell membrane due to partial retention in the endoplasmic reticulum, features a modification of the amino acid from S to R at position 577.
+The protein's natural variant, known as in CMT2HH; decreased glycosylation; decreased expression at the cell membrane due to partial retention in the endoplasmic reticulum, features a modification of the amino acid from S to P at position 650.
+The protein's natural variant, known as found in a patient with pulmonary stenosis; unknown pathological significance; the mutant is able to activate Notch signaling, features a modification of the amino acid from C to S at position 664.
+The protein's natural variant, known as in biliary atresia; extrahepatic, features a modification of the amino acid from Y to D at position 690.
+The protein's natural variant, known as in ALGS1;, features a modification of the amino acid from C to Y at position 693.
+The protein's natural variant, known as in ALGS1, features a modification of the amino acid from C to Y at position 714.
+The protein's natural variant, known as in ALGS1, features a modification of the amino acid from C to S at position 731.
+The protein's natural variant, known as in ALGS1, features a modification of the amino acid from C to R at position 740.
+The protein's natural variant, known as in ALGS1, features a modification of the amino acid from C to R at position 753.
+The protein's natural variant, known as in TOF; the mutant is unable to activate Notch signaling;, features a modification of the amino acid from P to L at position 810.
+The natural variant of this protein is characterized by an amino acid alteration from R to K at position 818.
+The protein's natural variant, known as in biliary atresia; extrahepatic;, features a modification of the amino acid from P to R at position 871.
+The protein's natural variant, known as in ALGS1; unknown pathological significance;, features a modification of the amino acid from R to Q at position 889.
+The protein's natural variant, known as in ALGS1;, features a modification of the amino acid from C to S at position 902.
+The protein's natural variant, known as in biliary atresia; extrahepatic, features a modification of the amino acid from H to Q at position 908.
+The protein's natural variant, known as in ALGS1, features a modification of the amino acid from C to Y at position 911.
+The protein's natural variant, known as in ALGS1, features a modification of the amino acid from S to R at position 913.
+The protein's natural variant, known as in biliary atresia; extrahepatic;, features a modification of the amino acid from L to P at position 921.
+The protein's natural variant, known as likely benign variant; the mutant is able to activate Notch signaling;, features a modification of the amino acid from R to Q at position 937.
+The protein's natural variant, known as in ALGS1, features a modification of the amino acid from VR to G at position 1056.
+The protein's natural variant, known as found in patient with tetralogy of Fallot and pulmonary stenosis; unknown pathological significance;, features a modification of the amino acid from H to Q at position 1104.
+The protein's natural variant, known as in biliary atresia; extrahepatic;, features a modification of the amino acid from R to Q at position 1213.
+The protein's natural variant, known as in plasmid pCP301, features a modification of the amino acid from V to A at position 385.
+The protein's natural variant, known as in plasmid pCHL1, features a modification of the amino acid from N to D at position 56.
+The protein's natural variant, known as in plasmid pCHL1, features a modification of the amino acid from L to S at position 90.
+The protein's natural variant, known as in DEE2; causes mislocalization of the protein in the cytoplasm;, features a modification of the amino acid from A to V at position 40.
+The protein's natural variant, known as in DEE2;, features a modification of the amino acid from I to N at position 72.
+The protein's natural variant, known as in DEE2;, features a modification of the amino acid from I to T at position 72.
+The protein's natural variant, known as in DEE2;, features a modification of the amino acid from H to R at position 127.
+The protein's natural variant, known as in DEE2; unknown pathological significance, features a modification of the amino acid from H to Y at position 145.
+The protein's natural variant, known as in DEE2; affect activity; causes mislocalization of the protein in the cytoplasm;, features a modification of the amino acid from C to F at position 152.
+The protein's natural variant, known as in DEE2; affect activity; does not affect the cellular distribution of the protein;, features a modification of the amino acid from R to S at position 175.
+The protein's natural variant, known as in DEE2;, features a modification of the amino acid from R to P at position 178.
+The protein's natural variant, known as in DEE2;, features a modification of the amino acid from R to Q at position 178.
+The protein's natural variant, known as in DEE2;, features a modification of the amino acid from R to W at position 178.
+The protein's natural variant, known as in DEE2;, features a modification of the amino acid from P to L at position 180.
+The protein's natural variant, known as in DEE2, features a modification of the amino acid from L to P at position 182.
+The protein's natural variant, known as in DEE2;, features a modification of the amino acid from S to L at position 196.
+The protein's natural variant, known as in DEE2, features a modification of the amino acid from G to E at position 207.
+The protein's natural variant, known as in DEE2; causes mislocalization of the protein in the cytoplasm;, features a modification of the amino acid from L to P at position 220.
+The protein's natural variant, known as in DEE2;, features a modification of the amino acid from T to I at position 288.
+The protein's natural variant, known as in DEE2;, features a modification of the amino acid from C to Y at position 291.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from N to H at position 368.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation, features a modification of the amino acid from A to T at position 374.
+The protein's natural variant, known as in DEE2;, features a modification of the amino acid from N to T at position 399.
+The protein's natural variant, known as in an ovarian serous carcinoma sample; somatic mutation;, features a modification of the amino acid from P to Q at position 574.
+The protein's natural variant, known as in DEE2; unknown pathological significance, features a modification of the amino acid from H to Y at position 581.
+The protein's natural variant, known as probable disease-associated variant found in a patient with autism spectrum disorder, features a modification of the amino acid from P to L at position 647.
+The protein's natural variant, known as in DEE2;, features a modification of the amino acid from V to M at position 718.
+The protein's natural variant, known as in DEE2; unknown pathological significance;, features a modification of the amino acid from V to A at position 793.
+The protein's natural variant, known as in DEE2; unknown pathological significance;, features a modification of the amino acid from R to C at position 858.
+The protein's natural variant, known as in PARK2;, features a modification of the amino acid from V to M at position 15.
+The protein's natural variant, known as in PARK2;, features a modification of the amino acid from R to Q at position 33.
+The protein's natural variant, known as in PARK2;, features a modification of the amino acid from P to L at position 37.
+The protein's natural variant, known as in PARK2 and PARK; induces a conformational change in the PSMD4-binding site of Ubl resulting in impaired proteasomal binding; decreases ubiquitination and degradation; increased aggregation; impairs the ability to ubiquitinate and degrade SYT11;, features a modification of the amino acid from R to P at position 42.
+The protein's natural variant, known as in PARK2, features a modification of the amino acid from A to P at position 46.
+The protein's natural variant, known as in PARK2;, features a modification of the amino acid from V to E at position 56.
+The protein's natural variant, known as in PARK2;, features a modification of the amino acid from A to E at position 82.
+The protein's natural variant, known as in PARK2;, features a modification of the amino acid from A to V at position 92.
+The protein's natural variant, known as in PARK2; severely compromises the mitochondrial localization; fails to stabilize BCL2; decreased binding to the TP53 promoter; abolishes TP53 transcriptional repression;, features a modification of the amino acid from K to N at position 161.
+The protein's natural variant, known as in PARK2; unknown pathological significance;, features a modification of the amino acid from M to L at position 192.
+The protein's natural variant, known as in PARK2; unknown pathological significance;, features a modification of the amino acid from M to V at position 192.
+The protein's natural variant, known as in PARK2; severely compromises the mitochondrial localization; fails to stabilize BCL2;, features a modification of the amino acid from K to N at position 211.
+The protein's natural variant, known as in PARK2;, features a modification of the amino acid from C to Y at position 212.
+The protein's natural variant, known as in PARK2;, features a modification of the amino acid from T to M at position 240.
+The protein's natural variant, known as in PARK2; impairs the ability to ubiquitinate SNCAIP and BCL2; loss of UBE2L3 binding; severely compromises the mitochondrial localization;, features a modification of the amino acid from T to R at position 240.
+The protein's natural variant, known as in PARK; late onset;, features a modification of the amino acid from C to Y at position 253.
+The protein's natural variant, known as in PARK2 and PARK; at heterozygosity it is associated with late onset Parkinson disease; impairs the ability to ubiquitinate SNCAIP and ZNF746; decreased binding to the TP53 promoter; abolishes TP53 transcriptional repression;, features a modification of the amino acid from R to C at position 256.
+The protein's natural variant, known as in PARK2 and PARK; at heterozygosity it is associated with late onset Parkinson disease; impairs the ability to ubiquitinate SNCAIP; abolishes p53/TP53 transcriptional repression; impairs the ability to ubiquitinate and degrade SYT11;, features a modification of the amino acid from R to W at position 275.
+The protein's natural variant, known as in PARK; does not affect PINK-1 dependent localization to depolarized mitochondria;, features a modification of the amino acid from D to N at position 280.
+The protein's natural variant, known as in PARK2;, features a modification of the amino acid from G to R at position 284.
+The protein's natural variant, known as in PARK2; increased aggregation; fails to ubiquitinate SYT11; loses ability to bind SYT11; impaired relocalization to damaged mitochondria; loss of function in mitophagy;, features a modification of the amino acid from C to G at position 289.
+The protein's natural variant, known as in a patient with Parkinson disease; unknown pathological significance, features a modification of the amino acid from Q to R at position 311.
+The protein's natural variant, known as in PARK2; does not affect PINK-1 dependent localization to depolarized mitochondria, features a modification of the amino acid from G to E at position 328.
+The protein's natural variant, known as in PARK2; impairs folding of IBR domain;, features a modification of the amino acid from T to P at position 351.
+The protein's natural variant, known as in a patient with Parkinson disease; unknown pathological significance, features a modification of the amino acid from A to T at position 371.
+The protein's natural variant, known as in PARK2;, features a modification of the amino acid from R to C at position 402.
+The protein's natural variant, known as in PARK2; impairs the ability to ubiquitinate SNCAIP; does not affect turnover of CDCRE1; impairs PINK1-dependent localization to dysfunctional depolarized mitochondria;, features a modification of the amino acid from T to N at position 415.
+The protein's natural variant, known as in PARK2; decreased binding to the TP53 promoter; abolishes TP53 transcriptional repression; fails to ubiquitinate SYT11 but does not loose ability to bind SYT11;, features a modification of the amino acid from C to R at position 418.
+The protein's natural variant, known as in PARK2; impairs PINK1-dependent localization to dysfunctional depolarized mitochondria; impaired E3 ubiquitin-protein ligase toward ZNF746;, features a modification of the amino acid from G to D at position 430.
+The protein's natural variant, known as in PARK2; impaired E3 ubiquitin-protein ligase toward ZNF746 and BCL2;, features a modification of the amino acid from C to F at position 431.
+The protein's natural variant, known as in PARK2; impaired E3 ubiquitin-protein ligase toward BCL2;, features a modification of the amino acid from P to L at position 437.
+The protein's natural variant, known as in PARK2; decreased binding to the TP53 promoter; abolishes TP53 transcriptional repression;, features a modification of the amino acid from C to R at position 441.
+The protein's natural variant, known as in strain: cv. Ag-0, features a modification of the amino acid from SF to TS at position 625.
+The protein's natural variant, known as in strain: cv. C24, features a modification of the amino acid from FSS to SSI at position 627.
+The protein's natural variant, known as in strain: cv. Br-0, cv. Ct-1, cv. Edi-0, cv. Ga-0, cv. Landsberg erecta, cv. Ll-0, cv. Lz-0, cv. Ms-0, cv. Sorbo, cv. Tu-1, cv. Wa-1 and cv. Wassilewskija, features a modification of the amino acid from F to S at position 625.
+The protein's natural variant, known as in strain: cv. Nd-1, features a modification of the amino acid from S to L at position 630.
+The natural variant of this protein is characterized by an amino acid alteration from Y to F at position 38.
+The protein's natural variant, known as in MC4DN16; decreased COX4I1 protein levels, features a modification of the amino acid from KT to NS at position 102.
+The protein's natural variant, known as in MC4DN16, features a modification of the amino acid from P to T at position 152.
+The protein's natural variant, known as in strain: NC-066, features a modification of the amino acid from E to Q at position 46.
+The protein's natural variant, known as in strain: NC-036 and NC-123, features a modification of the amino acid from E to V at position 49.
+The protein's natural variant, known as in strain: CA-002, CA-008, CA-009, CA-011, CA-013, CA-015, CA-026, CA-031, CA-033, CA-034, CA-035, CA-037, CA-040, CA-048, CA-052, CA-055, CA-057, CA-060, CA-061, CA-063, CA-064, CA-065, CA-069, CA-072, CA-073, CA-075, CA-088, CA-090, CA-093, CA-096, CA-100, CA-114, CA-120, CA-127, CA-129, CA-132, CA-133, CA-140, CA-142, CA-145, CA-147, NC-003, NC-006, NC-010, NC-011, NC-014, NC-015, NC-021, NC-033, NC-034, NC-036, NC-040, NC-042, NC-044, NC-046, NC-047, NC-051, NC-052, NC-054, NC-057, NC-066, NC-069, NC-071, NC-073, NC-081, NC-084, NC-086, NC-089, NC-092, NC-094, NC-096, NC-097, NC-101, NC-103, NC-104, NC-107, NC-108, NC-118, NC-119, NC-121, NC-123, NC-127, NC-128, NC-129, NC-134, NC-136, NC-137, NC-138, NC-141, NC-144 and NC-148, features a modification of the amino acid from D to E at position 51.
+The protein's natural variant, known as in strain: NC-103 and NC-118, features a modification of the amino acid from D to E at position 52.
+The protein's natural variant, known as in strain: NC-061, features a modification of the amino acid from A to G at position 54.
+The protein's natural variant, known as in strain: NC-012, NC-023, NC-037, NC-038, NC-039, NC-124 and NC-131, features a modification of the amino acid from S to T at position 76.
+The protein's natural variant, known as in strain: CA-008, CA-009, CA-013, CA-026, CA-031, CA-033, CA-035, CA-037, CA-040, CA-048, CA-052, CA-057, CA-060, CA-061, CA-063, CA-065, CA-072, CA-073, CA-088, CA-093, CA-096, CA-100, CA-114, CA-120, CA-129, CA-132, CA-133, CA-140, CA-147, NC-011, NC-015, NC-021, NC-033, NC-034, NC-040, NC-042, NC-044, NC-046, NC-047, NC-051, NC-052, NC-054, NC-057, NC-069, NC-084, NC-089, NC-092, NC-094, NC-097, NC-103, NC-107, NC-119, NC-121, NC-127, NC-128, NC-129, NC-134, NC-137, NC-138, NC-141, NC-144 and NC-148, features a modification of the amino acid from S to T at position 86.
+The protein's natural variant, known as in strain: CA-030, CA-068, CA-091, NC-008, NC-025, NC-043, NC-048, NC-060, NC-075, NC-088, NC-091, NC-114, NC-116 and NC-135, features a modification of the amino acid from P to Q at position 91.
+The protein's natural variant, known as in strain: CA-008, CA-009, CA-011, CA-013, CA-015, CA-026, CA-031, CA-033, CA-034, CA-035, CA-037, CA-040, CA-048, CA-052, CA-055, CA-057, CA-060, CA-061, CA-063, CA-064, CA-065, CA-069, CA-072, CA-073, CA-075, CA-088, CA-090, CA-093, CA-095, CA-096, CA-100, CA-114, CA-120, CA-129, CA-132, CA-133, CA-140, CA-147, NC-010, NC-011, NC-012, NC-014, NC-015, NC-021, NC-023, NC-033, NC-034, NC-036, NC-037, NC-038, NC-039, NC-040, NC-042, NC-044, NC-046, NC-047, NC-051, NC-052, NC-054, NC-057, NC-066, NC-069, NC-073, NC-081, NC-084, NC-086, NC-089, NC-092, NC-094, NC-096, NC-097, NC-101, NC-103, NC-104, NC-107, NC-108, NC-118, NC-119, NC-121, NC-123, NC-124, NC-127, NC-128, NC-129, NC-131, NC-134, NC-136, NC-137, NC-138, NC-141, NC-144, NC-148 and Oregon-R, features a modification of the amino acid from V to A at position 96.
+The protein's natural variant, known as in strain: CA-064, features a modification of the amino acid from A to T at position 143.
+The protein's natural variant, known as in strain: CA-008, CA-026, CA-033, CA-035, CA-037, CA-048, CA-052, CA-057, CA-060, CA-063, CA-065, CA-072, CA-088, CA-090, CA-096, CA-100, CA-114, CA-120, CA-132, CA-140, CA-147, NC-011, NC-014, NC-033, NC-034, NC-040, NC-042, NC-044, NC-046, NC-047, NC-051, NC-052, NC-054, NC-057, NC-069, NC-084, NC-092, NC-094, NC-096, NC-103, NC-105, NC-107, NC-108, NC-118, NC-119, NC-121, NC-125, NC-126, NC-127, NC-129, NC-138, NC-144 and NC-148, features a modification of the amino acid from S to T at position 146.
+The protein's natural variant, known as in strain: CA-008, CA-009, CA-026, CA-031, CA-033, CA-035, CA-037, CA-048, CA-052, CA-057, CA-060, CA-061, CA-063, CA-065, CA-072, CA-088, CA-096, CA-100, CA-114, CA-120, CA-132, CA-140, CA-147, NC-011, NC-034, NC-040, NC-042, NC-044, NC-046, NC-047, NC-051, NC-052, NC-054, NC-057, NC-069, NC-084, NC-092, NC-094, NC-103, NC-107, NC-119, NC-121, NC-127, NC-129, NC-138, NC-144 and NC-148, features a modification of the amino acid from A to V at position 171.
+The protein's natural variant, known as in strain: NC-066, features a modification of the amino acid from G to D at position 182.
+The protein's natural variant, known as in strain: NC-086, NC-104 and NC-010, features a modification of the amino acid from D to Y at position 184.
+The protein's natural variant, known as in strain: NC-114, features a modification of the amino acid from S to N at position 196.
+The protein's natural variant, known as in strain: CA-001, CA-009, CA-011, CA-013, CA-015, CA-026, CA-030, CA-031, CA-033, CA-034, CA-035, CA-037, CA-040, CA-046, CA-048, CA-052, CA-055, CA-057, CA-060, CA-061, CA-063, CA-065, CA-066, CA-068, CA-069, CA-072, CA-073, CA-075, CA-088, CA-090, CA-091, CA-093, CA-095, CA-096, CA-100, CA-114, CA-120, CA-132, CA-133, CA-140, CA-147, NC-008, NC-011, NC-014, NC-015, NC-025, NC-034, NC-040, NC-042, NC-043, NC-044, NC-046, NC-047, NC-048, NC-051, NC-052, NC-054, NC-057, NC-060, NC-066, NC-069, NC-073, NC-075, NC-081, NC-084, NC-088, NC-091, NC-092, NC-094, NC-096, NC-101, NC-103, NC-107, NC-108, NC-110, NC-113, NC-114, NC-115, NC-116, NC-118, NC-119, NC-121, NC-123, NC-127, NC-128, NC-129, NC-135, NC-136, NC-137, NC-138, NC-139, NC-142, NC-144, NC-146, NC-148 and Oregon-R, features a modification of the amino acid from Q to H at position 198.
+The protein's natural variant, known as in strain: CA-015, features a modification of the amino acid from S to G at position 213.
+The protein's natural variant, known as in strain: NC-104, features a modification of the amino acid from Q to L at position 531.
+The protein's natural variant, known as in strain: CA-011, CA-017, CA-018, CA-062, CA-130, NC-118, NC-022, NC-026, NC-049 and NC-073, features a modification of the amino acid from T to A at position 536.
+The protein's natural variant, known as in strain: CA-013, CA-026 and CA-093, features a modification of the amino acid from APSG to GPMGPL at position 550.
+The protein's natural variant, known as in strain: CA-002, CA-003, CA-008, CA-011, CA-012, CA-015, CA-023, CA-027, CA-030, CA-031, CA-034, CA-035, CA-037, CA-043, CA-044, CA-045, CA-046, CA-048, CA-052, CA-055, CA-057, CA-058, CA-063, CA-064, CA-065, CA-066, CA-068, CA-070, CA-072, CA-073, CA-075, CA-081, CA-083, CA-087, CA-088, CA-089, CA-091, CA-096, CA-100, CA-105, CA-114, CA-120, CA-123, CA-128, CA-129, CA-133, CA-140, CA-145, CA-147, CA-148, NC-001, NC-002, NC-003, NC-010, NC-011, NC-012, NC-013, NC-015, NC-023, NC-024, NC-025, NC-027, NC-028, NC-029, NC-030, NC-032, NC-033, NC-034, NC-036, NC-040, NC-041, NC-042, NC-043, NC-044, NC-046, NC-047, NC-048, NC-050, NC-051, NC-052, NC-054, NC-057, NC-059, NC-060, NC-061, NC-066, NC-069, NC-071, NC-072, NC-074, NC-075, NC-077, NC-079, NC-080, NC-081, NC-084, NC-086, NC-087, NC-088, NC-089, NC-091, NC-092, NC-094, NC-098, NC-101, NC-103, NC-104, NC-107, NC-109, NC-110, NC-111, NC-112, NC-113, NC-114, NC-115, NC-116, NC-119, NC-121, NC-124, NC-127, NC-128, NC-129, NC-131, NC-133, NC-134, NC-135, NC-136, NC-137, NC-138, NC-144, NC-146, NC-147, NC-148 and NC-149, features a modification of the amino acid from E to V at position 571.
+The protein's natural variant, known as in strain: NC-026, features a modification of the amino acid from T to K at position 585.
+The protein's natural variant, known as in strain: Berkeley, CA-009, CA-010, CA-013, CA-026, CA-041, CA-060, CA-063, CA-066, CA-086, CA-093, CA-113, CA-137, CA-145, NC-006, NC-008, NC-021, NC-064, NC-067, NC-123, NC-142 and NC-150, features a modification of the amino acid from T to M at position 588.
+The protein's natural variant, known as in strain: CA-040, CA-056, CA-115, CA-118, CA-126, CA-132, CA-142, NC-005, NC-037, NC-038, NC-039, NC-053, NC-068, NC-095, NC-100, NC-105, NC-125, NC-126 and NC-139, features a modification of the amino acid from T to R at position 589.
+The protein's natural variant, known as in strain: CA-023, CA-048, NC-015, NC-110, NC-128, NC-133 and NC-137, features a modification of the amino acid from A to V at position 648.
+The protein's natural variant, known as in strain: CA-130, features a modification of the amino acid from Q to P at position 657.
+The protein's natural variant, known as in strain: CA-043, CA-058 and CA-105, features a modification of the amino acid from S to W at position 682.
+The protein's natural variant, known as in strain: CA-088, features a modification of the amino acid from T to I at position 688.
+The protein's natural variant, known as in strain: NC-104, features a modification of the amino acid from S to T at position 692.
+The protein's natural variant, known as in strain: NC-001, features a modification of the amino acid from P to T at position 706.
+The protein's natural variant, known as in strain: NC-032, features a modification of the amino acid from Q to H at position 716.
+The protein's natural variant, known as in strain: NC-047, features a modification of the amino acid from Q to QH at position 716.
+The protein's natural variant, known as in strain: CA-069, NC-096 and NC-108, features a modification of the amino acid from QQQ to H at position 719.
+The protein's natural variant, known as in PDA3; unknown pathological significance;, features a modification of the amino acid from C to S at position 263.
+The protein's natural variant, known as in PDA3;, features a modification of the amino acid from Q to R at position 462.
+The protein's natural variant, known as in PDA3;, features a modification of the amino acid from R to Q at position 549.
+The natural variant of this protein is characterized by an amino acid alteration from K to D at position 64.
+The protein's natural variant, known as in strain: KK/HLJ, features a modification of the amino acid from D to N at position 94.
+The protein's natural variant, known as in strain: A/J, BALB/cJ, P/J, SODL/EI, SEA/GNJ, NZW/LACJ and VM/DK, features a modification of the amino acid from M to I at position 209.
+The protein's natural variant, known as in strain: SEA/GNJ, features a modification of the amino acid from D to G at position 219.
+The protein's natural variant, known as in strain: A/J, BALB/cJ and SEA/GNJ, features a modification of the amino acid from V to I at position 254.
+The protein's natural variant, known as in strain: SEA/GNJ, features a modification of the amino acid from Q to L at position 423.
+The protein's natural variant, known as in strain: P/J, features a modification of the amino acid from A to S at position 477.
+The protein's natural variant, known as in strain: LP/J, features a modification of the amino acid from T to A at position 516.
+The protein's natural variant, known as in strain: A/J, BALB/cJ, P/J, SODL/EI, SEA/GNJ, NZW/LACJ and VM/DK, features a modification of the amino acid from E to D at position 593.
+The protein's natural variant, known as in strain: KK/HLJ, features a modification of the amino acid from N to I at position 600.
+The protein's natural variant, known as in strain: P/J, features a modification of the amino acid from A to V at position 607.
+The protein's natural variant, known as in strain: P/J, features a modification of the amino acid from V to I at position 637.
+The protein's natural variant, known as in Lps-tolerant mice, features a modification of the amino acid from P to H at position 712.
+The protein's natural variant, known as in strain: A/J, BALB/cJ, SODL/EI, SEA/GNJ, NZW/LACJ and VM/DK, features a modification of the amino acid from R to H at position 761.
+The protein's natural variant, known as in strain: P/J, features a modification of the amino acid from N to K at position 811.
+The protein's natural variant, known as in CONRIBA; strongly slowed gating and increased current amplitudes;, features a modification of the amino acid from Y to C at position 553.
+The protein's natural variant, known as in strain: UCD932, features a modification of the amino acid from S to N at position 504.
+The protein's natural variant, known as decreased interaction with GATA4; decreased synergistic activation of GATA4 target genes transcription; detrimental effect on cardiomyocyte differentiation, features a modification of the amino acid from P to L at position 496.
+The protein's natural variant, known as in SCCD, features a modification of the amino acid from A to T at position 97.
+The protein's natural variant, known as in SCCD, features a modification of the amino acid from G to S at position 98.
+The protein's natural variant, known as in SCCD; reduced menaquinone-4 (MK-4) synthesis; does not affect coenzyme Q10 synthesis;, features a modification of the amino acid from N to S at position 102.
+The protein's natural variant, known as in SCCD; does not affect coenzyme Q10 synthesis;, features a modification of the amino acid from D to G at position 112.
+The protein's natural variant, known as in SCCD; reduced menaquinone-4 (MK-4) synthesis, features a modification of the amino acid from D to N at position 112.
+The protein's natural variant, known as in SCCD, features a modification of the amino acid from D to G at position 118.
+The protein's natural variant, known as in SCCD;, features a modification of the amino acid from R to G at position 119.
+The protein's natural variant, known as in SCCD, features a modification of the amino acid from L to F at position 121.
+The protein's natural variant, known as in SCCD, features a modification of the amino acid from V to E at position 122.
+The protein's natural variant, known as in SCCD, features a modification of the amino acid from V to G at position 122.
+The protein's natural variant, known as in SCCD;, features a modification of the amino acid from S to P at position 171.
+The protein's natural variant, known as in SCCD;, features a modification of the amino acid from T to I at position 175.
+The protein's natural variant, known as in SCCD; reduced menaquinone-4 (MK-4) synthesis;, features a modification of the amino acid from G to E at position 177.
+The protein's natural variant, known as in SCCD; reduced menaquinone-4 (MK-4) synthesis;, features a modification of the amino acid from G to R at position 177.
+The protein's natural variant, known as in SCCD;, features a modification of the amino acid from G to R at position 186.
+The protein's natural variant, known as in SCCD, features a modification of the amino acid from L to H at position 188.
+The protein's natural variant, known as in SCCD;, features a modification of the amino acid from N to S at position 232.
+The protein's natural variant, known as in SCCD;, features a modification of the amino acid from D to E at position 236.
+The protein's natural variant, known as in SCCD;, features a modification of the amino acid from D to N at position 240.
+The protein's natural variant, known as in strain: m104, features a modification of the amino acid from I to V at position 210.
+The protein's natural variant, known as in strain: cv. Ts-1 and cv. No-0, features a modification of the amino acid from R to RTQLKQWTKGAKTIDDYMQG at position 129.
+The protein's natural variant, known as in VISS; very low protein expression levels, if any, in either patient's fibroblasts or patient's Epstein-Barr virus-immortalized B cell lines;, features a modification of the amino acid from D to N at position 88.
+The protein's natural variant, known as in VISS; unknown pathological significance, features a modification of the amino acid from Y to C at position 317.
+The protein's natural variant, known as in VISS; undetectable protein expression levels in either patient's fibroblasts or patient's Epstein-Barr virus-immortalized B cell lines, features a modification of the amino acid from C to R at position 749.
+The protein's natural variant, known as in VISS; very low protein expression levels, if any, in either patient's fibroblasts or patient's Epstein-Barr virus-immortalized B cell lines;, features a modification of the amino acid from R to W at position 834.
+The protein's natural variant, known as in allele C8A*B;, features a modification of the amino acid from Q to K at position 93.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from Y to C at position 785.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from L to V at position 183.
+The protein's natural variant, known as in THES2; abolished ATPase activity;, features a modification of the amino acid from V to G at position 341.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from M to I at position 765.
+The protein's natural variant, known as very rare variant found in a family with neuronal ceroid lipofuscinosis carrying a causative mutation in DNAJC5; uncertain role as a disease phenotype modifier;, features a modification of the amino acid from N to S at position 477.
+The protein's natural variant, known as in RP60; impaired function in pre-mRNA splicing; mislocalized in Cajal bodies; partial loss of localization in splicing speckles;, features a modification of the amino acid from R to W at position 729.
+The protein's natural variant, known as associated with 1/3 to 2/3 the enzyme activity of the wild-type;, features a modification of the amino acid from R to C at position 18.
+The protein's natural variant, known as in CBSD; decreased expression; no effect on cystathionine beta-synthase activity; increased homotetramer formation;, features a modification of the amino acid from P to L at position 49.
+The protein's natural variant, known as in CBSD; linked with V-114; 18% of activity;, features a modification of the amino acid from R to W at position 58.
+The protein's natural variant, known as in CBSD; decreased cystathionine beta-synthase activity; inhibited by AdoMet and AdoHcy; decreased homotetramer formation;, features a modification of the amino acid from H to R at position 65.
+The protein's natural variant, known as in CBSD; severe form; associated in cis with N-102; decreased cystathionine beta-synthase activity; decreased homotetramer formation;, features a modification of the amino acid from P to R at position 78.
+The protein's natural variant, known as in CBSD; loss of cystathionine beta-synthase activity;, features a modification of the amino acid from G to R at position 85.
+The protein's natural variant, known as in CBSD; decreased cystathionine beta-synthase activity; increased aggregation, features a modification of the amino acid from T to N at position 87.
+The protein's natural variant, known as in CBSD, features a modification of the amino acid from P to S at position 88.
+The protein's natural variant, known as in CBSD; common mutation in Irish population; loss of activity;, features a modification of the amino acid from L to P at position 101.
+The protein's natural variant, known as in CBSD; associated in cis with R-78; decreased cystathionine beta-synthase activity; decreased homotetramer formation;, features a modification of the amino acid from K to N at position 102.
+The protein's natural variant, known as in CBSD; loss of activity;, features a modification of the amino acid from C to R at position 109.
+The protein's natural variant, known as in CBSD; mild form; when linked with W-58 severe form; decreased cystathionine beta-synthase activity; decreases homotetramer formation by promoting formation of larger aggregates;, features a modification of the amino acid from A to V at position 114.
+The protein's natural variant, known as in CBSD;, features a modification of the amino acid from G to R at position 116.
+The protein's natural variant, known as in CBSD;, features a modification of the amino acid from R to C at position 121.
+The protein's natural variant, known as in CBSD;, features a modification of the amino acid from R to H at position 121.
+The protein's natural variant, known as in CBSD; mild form;, features a modification of the amino acid from R to L at position 121.
+The protein's natural variant, known as in CBSD, features a modification of the amino acid from R to P at position 125.
+The protein's natural variant, known as in CBSD; severe form; when linked with D-131 moderate form; loss of cystathionine beta-synthase activity; decreased homotetramer formation;, features a modification of the amino acid from R to Q at position 125.
+The protein's natural variant, known as in CBSD; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure;, features a modification of the amino acid from R to W at position 125.
+The protein's natural variant, known as in CBSD; loss of activity, features a modification of the amino acid from M to V at position 126.
+The protein's natural variant, known as in CBSD;, features a modification of the amino acid from E to D at position 128.
+The protein's natural variant, known as in CBSD; linked with Q-125; loss of activity;, features a modification of the amino acid from E to D at position 131.
+The protein's natural variant, known as in CBSD; mild form;, features a modification of the amino acid from G to R at position 139.
+The protein's natural variant, known as in CBSD; 4% of activity; stable;, features a modification of the amino acid from I to M at position 143.
+The protein's natural variant, known as in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; decreased homotetramer formation;, features a modification of the amino acid from E to K at position 144.
+The protein's natural variant, known as in CBSD;, features a modification of the amino acid from P to L at position 145.
+The protein's natural variant, known as in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; loss of homotetramer formation;, features a modification of the amino acid from G to R at position 148.
+The protein's natural variant, known as in CBSD;, features a modification of the amino acid from G to R at position 151.
+The protein's natural variant, known as in CBSD; severe form, features a modification of the amino acid from I to M at position 152.
+The protein's natural variant, known as in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity, features a modification of the amino acid from L to Q at position 154.
+The protein's natural variant, known as in CBSD; complete loss of activity; severely affects homotetramer formation by promoting formation of larger aggregates;, features a modification of the amino acid from A to T at position 155.
+The protein's natural variant, known as in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity, features a modification of the amino acid from A to V at position 155.
+The protein's natural variant, known as in CBSD; severe form; protein expression is comparable to wild-type; loss of cystathionine beta-synthase activity; no effect on homotetramer formation;, features a modification of the amino acid from C to Y at position 165.
+The protein's natural variant, known as in CBSD, features a modification of the amino acid from V to A at position 168.
+The protein's natural variant, known as in CBSD;, features a modification of the amino acid from V to M at position 168.
+The protein's natural variant, known as in CBSD; presents 40% of the wild-type activity; highly reduced capacity to form multimeric quaternary structure, features a modification of the amino acid from M to V at position 173.
+The protein's natural variant, known as in CBSD; severe form; loss of cystathionine beta-synthase activity; inhibited by AdoMet; severely decreases homotetramer formation by promoting formation of larger aggregates;, features a modification of the amino acid from E to K at position 176.
+The protein's natural variant, known as in CBSD; decreased cystathionine beta-synthase activity; decreases homotetramer formation;, features a modification of the amino acid from V to A at position 180.
+The protein's natural variant, known as in CBSD; moderate and severe forms; loss of cystathionine beta-synthase activity; absent capacity to form multimeric quaternary structure;, features a modification of the amino acid from T to M at position 191.
+The protein's natural variant, known as in CBSD, features a modification of the amino acid from D to V at position 198.
+The protein's natural variant, known as in CBSD;, features a modification of the amino acid from P to L at position 200.
+The protein's natural variant, known as in CBSD;, features a modification of the amino acid from R to H at position 224.
+The protein's natural variant, known as in CBSD; presents 20% of the wild-type activity; dramatically reduced capacity to form multimeric quaternary structure;, features a modification of the amino acid from A to T at position 226.
+The protein's natural variant, known as in CBSD; loss of cystathionine beta-synthase activity; decreased homotetramer formation;, features a modification of the amino acid from N to K at position 228.
+The protein's natural variant, known as in CBSD; has significantly decreased levels of enzyme activity;, features a modification of the amino acid from N to S at position 228.
+The protein's natural variant, known as in CBSD; has significantly decreased levels of enzyme activity, features a modification of the amino acid from A to P at position 231.
+The protein's natural variant, known as in CBSD; decreased cystathionine beta-synthase activity; changed localization; decreased interaction with pyridoxal 5'-phosphate; no effect on homotetramer formation;, features a modification of the amino acid from D to N at position 234.
+The protein's natural variant, known as in CBSD, features a modification of the amino acid from E to K at position 239.
+The protein's natural variant, known as in CBSD; moderate to severe form; protein expression is comparable to wild-type; significant decrease of enzyme activity;, features a modification of the amino acid from T to M at position 257.
+The protein's natural variant, known as in CBSD; moderate form;, features a modification of the amino acid from T to M at position 262.
+The protein's natural variant, known as in CBSD; severe form; loss of cystathionine beta-synthase activity; loss of homotetramer formation, features a modification of the amino acid from T to R at position 262.
+The protein's natural variant, known as in CBSD, features a modification of the amino acid from R to G at position 266.
+The protein's natural variant, known as in CBSD; mild form; decreased cystathionine beta-synthase activity; decreased homotetramer formation; no effect on heme-binding; decreased stability;, features a modification of the amino acid from R to K at position 266.
+The protein's natural variant, known as in CBSD; severe form; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure, features a modification of the amino acid from C to Y at position 275.
+The protein's natural variant, known as in CBSD; loss of activity, features a modification of the amino acid from I to S at position 278.
+The protein's natural variant, known as in CBSD; mild to severe form; common mutation; decreased expression; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; severely affects homotetramer formation by promoting formation of larger aggregates;, features a modification of the amino acid from I to T at position 278.
+The protein's natural variant, known as in CBSD; loss of activity, features a modification of the amino acid from D to N at position 281.
+The protein's natural variant, known as in CBSD, features a modification of the amino acid from A to P at position 288.
+The protein's natural variant, known as in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity;, features a modification of the amino acid from A to T at position 288.
+The protein's natural variant, known as in CBSD;, features a modification of the amino acid from P to L at position 290.
+The protein's natural variant, known as in CBSD; no effect on cystathionine beta-synthase activity; inhibited by AdoHcy and impaired activation by AdoMet; no effect on homotetramer formation;, features a modification of the amino acid from E to K at position 302.
+The protein's natural variant, known as in CBSD; loss of cystathionine beta-synthase activity; no effect on homotetramer formation, features a modification of the amino acid from G to R at position 305.
+The protein's natural variant, known as in CBSD; moderate to severe form; linked with D-534; common mutation; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; no effect on homotetramer formation;, features a modification of the amino acid from G to S at position 307.
+The protein's natural variant, known as in CBSD; has 36% of wild-type enzyme activity;, features a modification of the amino acid from V to A at position 320.
+The protein's natural variant, known as in CBSD; loss of activity, features a modification of the amino acid from D to V at position 321.
+The protein's natural variant, known as in CBSD;, features a modification of the amino acid from A to E at position 331.
+The protein's natural variant, known as in CBSD;, features a modification of the amino acid from A to V at position 331.
+The protein's natural variant, known as in CBSD; protein expression is comparable to wild-type; loss of activity; absent capacity to form multimeric quaternary structure;, features a modification of the amino acid from R to C at position 336.
+The protein's natural variant, known as in CBSD; mild form; no effect on expression; exhibits an activity lower than 4% of the wild-type enzyme; altered stimulation by AdoMet; absent capacity to form multimeric quaternary structure;, features a modification of the amino acid from R to H at position 336.
+The protein's natural variant, known as in CBSD; severe form; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure, features a modification of the amino acid from L to P at position 338.
+The protein's natural variant, known as in CBSD; protein expression is comparable to wild-type; loss of activity;, features a modification of the amino acid from G to S at position 347.
+The protein's natural variant, known as in CBSD; severe form; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure, features a modification of the amino acid from S to N at position 349.
+The protein's natural variant, known as in CBSD, features a modification of the amino acid from S to N at position 352.
+The protein's natural variant, known as in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity;, features a modification of the amino acid from T to M at position 353.
+The protein's natural variant, known as in CBSD;, features a modification of the amino acid from V to M at position 354.
+The protein's natural variant, known as in CBSD;, features a modification of the amino acid from A to P at position 355.
+The protein's natural variant, known as in CBSD;, features a modification of the amino acid from A to T at position 361.
+The protein's natural variant, known as in CBSD; when linked with C-491 severe form; decreased cystathionine beta-synthase activity; decreased homotetramer formation;, features a modification of the amino acid from R to C at position 369.
+The protein's natural variant, known as in CBSD;, features a modification of the amino acid from R to H at position 369.
+The protein's natural variant, known as in CBSD;, features a modification of the amino acid from C to Y at position 370.
+The protein's natural variant, known as in CBSD;, features a modification of the amino acid from V to M at position 371.
+The protein's natural variant, known as in CBSD; has significantly decreased levels of enzyme activity;, features a modification of the amino acid from D to N at position 376.
+The protein's natural variant, known as in CBSD; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure;, features a modification of the amino acid from R to Q at position 379.
+The protein's natural variant, known as in CBSD;, features a modification of the amino acid from R to W at position 379.
+The protein's natural variant, known as in CBSD; severe form;, features a modification of the amino acid from K to E at position 384.
+The protein's natural variant, known as in CBSD; moderate form, features a modification of the amino acid from K to N at position 384.
+The protein's natural variant, known as in CBSD, features a modification of the amino acid from M to I at position 391.
+The protein's natural variant, known as in CBSD; changed cystathionine beta-synthase activity; impaired stimulation by AdoMet; does not affect homotetramer formation;, features a modification of the amino acid from P to L at position 422.
+The protein's natural variant, known as in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet;, features a modification of the amino acid from P to L at position 427.
+The protein's natural variant, known as in CBSD;, features a modification of the amino acid from T to N at position 434.
+The protein's natural variant, known as in CBSD; no effect on cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; does not affect homotetramer formation, features a modification of the amino acid from I to T at position 435.
+The protein's natural variant, known as in CBSD; no effect on cystathionine beta-synthase activity; increased homotetramer formation;, features a modification of the amino acid from R to Q at position 439.
+The protein's natural variant, known as in CBSD; decreased expression; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet; increased homotetramer formation;, features a modification of the amino acid from D to N at position 444.
+The protein's natural variant, known as in CBSD, features a modification of the amino acid from A to S at position 446.
+The protein's natural variant, known as in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet, features a modification of the amino acid from V to G at position 449.
+The protein's natural variant, known as in CBSD, features a modification of the amino acid from V to E at position 454.
+The protein's natural variant, known as in CBSD; severe; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure, features a modification of the amino acid from L to P at position 456.
+The protein's natural variant, known as in CBSD; increased cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; decreased homotetramer formation;, features a modification of the amino acid from S to L at position 466.
+The protein's natural variant, known as in CBSD; linked with C-369;, features a modification of the amino acid from R to C at position 491.
+The protein's natural variant, known as in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet;, features a modification of the amino acid from S to L at position 500.
+The protein's natural variant, known as in CBSD; has significantly decreased levels of enzyme activity, features a modification of the amino acid from Q to K at position 526.
+The protein's natural variant, known as in CBSD; linked with S-307, features a modification of the amino acid from V to D at position 534.
+The protein's natural variant, known as in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; loss of homotetramer formation;, features a modification of the amino acid from L to S at position 539.
+The protein's natural variant, known as in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet, features a modification of the amino acid from L to Q at position 540.
+The protein's natural variant, known as presents 60% of the wild-type activity; highly reduced capacity to form multimeric quaternary structure;, features a modification of the amino acid from R to Q at position 548.
+The protein's natural variant, known as in HP3;, features a modification of the amino acid from C to G at position 257.
+The protein's natural variant, known as in HP3;, features a modification of the amino acid from G to V at position 287.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from K to R at position 388.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from G to D at position 466.
+The protein's natural variant, known as in strain: PA011 and PA103, features a modification of the amino acid from D to E at position 56.
+The protein's natural variant, known as in strain: PA011, features a modification of the amino acid from N to S at position 342.
+The protein's natural variant, known as in strain: cv. Sha, features a modification of the amino acid from F to I at position 55.
+The protein's natural variant, known as in strain: cv. SF-2, features a modification of the amino acid from L to I at position 79.
+The protein's natural variant, known as in strain: cv. Edi-0, features a modification of the amino acid from G to E at position 146.
+The protein's natural variant, known as in strain: cv. Edi-0, features a modification of the amino acid from M to I at position 148.
+The protein's natural variant, known as in FECD8; decreased TCF4-binding;, features a modification of the amino acid from C to S at position 1036.
+The protein's natural variant, known as found in a child with sporadic epilepsy; unknown pathological significance, features a modification of the amino acid from R to T at position 467.
+The protein's natural variant, known as in CSNB1B; abolishes expression at the cell membrane;, features a modification of the amino acid from P to L at position 46.
+The protein's natural variant, known as in CSNB1B; abolishes expression at the cell membrane;, features a modification of the amino acid from G to R at position 58.
+The protein's natural variant, known as no effect on location at the cell membrane;, features a modification of the amino acid from Q to P at position 59.
+The protein's natural variant, known as in CSNB1B; abolishes expression at the cell membrane;, features a modification of the amino acid from G to S at position 150.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from S to F at position 191.
+The protein's natural variant, known as in CSNB1B; abolishes expression at the cell membrane;, features a modification of the amino acid from I to T at position 405.
+The protein's natural variant, known as in CSNB1B; abolishes expression at the cell membrane;, features a modification of the amino acid from C to Y at position 522.
+The protein's natural variant, known as in CSNB1B; abolishes expression at the cell membrane;, features a modification of the amino acid from E to K at position 781.
+The protein's natural variant, known as in allele ALS6-2, features a modification of the amino acid from L to S at position 70.
+The protein's natural variant, known as in allele ALS6-2, features a modification of the amino acid from S to L at position 856.
+The protein's natural variant, known as in allele ALS6-2, features a modification of the amino acid from I to V at position 907.
+The protein's natural variant, known as in allele ALS6-2, features a modification of the amino acid from D to G at position 1230.
+The protein's natural variant, known as in allele ALS6-2, features a modification of the amino acid from N to S at position 1238.
+The protein's natural variant, known as in allele ALS6-2, features a modification of the amino acid from M to T at position 1302.
+The protein's natural variant, known as in allele ALS6-2, features a modification of the amino acid from I to M at position 1310.
+The protein's natural variant, known as in strain: FU02472, features a modification of the amino acid from A to S at position 90.
+The protein's natural variant, known as in strain: FU02472, features a modification of the amino acid from N to K at position 210.
+The protein's natural variant, known as in strain: FU02472, features a modification of the amino acid from S to F at position 343.
+The protein's natural variant, known as in CsEv3A, features a modification of the amino acid from N to K at position 26.
+The protein's natural variant, known as in CsEv3A, features a modification of the amino acid from T to D at position 29.
+The protein's natural variant, known as in CsEv3B*, features a modification of the amino acid from C to Y at position 35.
+The protein's natural variant, known as in CsEv3A, features a modification of the amino acid from K to T at position 46.
+The protein's natural variant, known as in EXT2, features a modification of the amino acid from C to R at position 85.
+The protein's natural variant, known as in SSMS; decreased protein abundance; levels of the EXT2-interacting protein NDST1 are abolished in patient cells;, features a modification of the amino acid from M to R at position 87.
+The protein's natural variant, known as in SSMS; decreased protein abundance; levels of the EXT2-interacting protein NDST1 are abolished in patient cells;, features a modification of the amino acid from R to C at position 95.
+The protein's natural variant, known as in EXT2, features a modification of the amino acid from L to R at position 152.
+The protein's natural variant, known as in EXT2, features a modification of the amino acid from R to S at position 179.
+The protein's natural variant, known as in EXT2;, features a modification of the amino acid from A to V at position 202.
+The protein's natural variant, known as in EXT2;, features a modification of the amino acid from R to P at position 223.
+The protein's natural variant, known as in EXT2; no effect on oligomeric complex formation with EXT1;, features a modification of the amino acid from D to N at position 227.
+The protein's natural variant, known as in EXT2, features a modification of the amino acid from I to T at position 380.
+The protein's natural variant, known as in osteochondroma;, features a modification of the amino acid from E to K at position 576.
+The protein's natural variant, known as in strain: 11, 35, 7725 and Robertson, features a modification of the amino acid from A to D at position 21.
+The protein's natural variant, known as in strain: Praslin, features a modification of the amino acid from S to I at position 26.
+The natural variant of this protein is characterized by an amino acid alteration from P to A at position 8.
+The natural variant of this protein is characterized by an amino acid alteration from N to K at position 22.
+The protein's natural variant, known as in RILDBC2; unknown pathological significance;, features a modification of the amino acid from F to L at position 256.
+The protein's natural variant, known as in RILDBC2; unknown pathological significance;, features a modification of the amino acid from N to K at position 410.
+The protein's natural variant, known as in CHOPS;, features a modification of the amino acid from T to A at position 254.
+The protein's natural variant, known as in CHOPS;, features a modification of the amino acid from T to S at position 254.
+The protein's natural variant, known as in CHOPS;, features a modification of the amino acid from R to W at position 258.
+The protein's natural variant, known as found in a clear cell renal carcinoma case; somatic mutation, features a modification of the amino acid from S to T at position 757.
+The protein's natural variant, known as in allele PRH1-PIF, allele PRH1-PA and allele PRH1-DB;, features a modification of the amino acid from D to N at position 20.
+The protein's natural variant, known as in allele PRH1-PA and allele PRH1-DB;, features a modification of the amino acid from I to L at position 42.
+The protein's natural variant, known as in allele PRH2-2;, features a modification of the amino acid from N to D at position 66.
+The protein's natural variant, known as in allele PRH1-DB, features a modification of the amino acid from Q to QGGQQQQGPPPPQGKPQGPPQQ at position 97.
+The protein's natural variant, known as in allele PRH1-PA; interferes with proteolytic cleavage at Arg-122;, features a modification of the amino acid from R to C at position 119.
+The protein's natural variant, known as in allele PRH2-3;, features a modification of the amino acid from Q to K at position 163.
+The protein's natural variant, known as in strain: ATCC 33303 / B10, features a modification of the amino acid from W to R at position 265.
+The protein's natural variant, known as in strain: ATCC 33303 / B10, features a modification of the amino acid from R to A at position 285.
+The protein's natural variant, known as in strain: ATCC 33303 / B10, features a modification of the amino acid from QL to HV at position 290.
+The protein's natural variant, known as in strain: ATCC 33303 / B10, features a modification of the amino acid from R to A at position 423.
+The protein's natural variant, known as in ARJPKD, features a modification of the amino acid from G to V at position 448.
+The protein's natural variant, known as in strain: SI-LI2, features a modification of the amino acid from D to H at position 57.
+The protein's natural variant, known as in strain: SI-K1, SI-K2, SI-LI1 and SI-LI2, features a modification of the amino acid from T to A at position 68.
+The protein's natural variant, known as in strain: SI-K1, features a modification of the amino acid from T to A at position 77.
+The protein's natural variant, known as in strain: SI-LI1 and SI-LI2, features a modification of the amino acid from T to S at position 165.
+The protein's natural variant, known as in strain: SI-LI1, features a modification of the amino acid from I to M at position 230.
+The protein's natural variant, known as in strain: SI-K2, features a modification of the amino acid from G to A at position 311.
+The protein's natural variant, known as in strain: Merano 7, Merano 8 and Kenscoff, features a modification of the amino acid from N to T at position 634.
+The protein's natural variant, known as in strain: Merano 8, features a modification of the amino acid from TNS to N at position 638.
+The protein's natural variant, known as in strain: Merano 7 and Kenscoff, features a modification of the amino acid from NS to GN at position 638.
+The protein's natural variant, known as in strain: Merano 7, Merano 8 and Kenscoff, features a modification of the amino acid from GT to NS at position 642.
+The protein's natural variant, known as in strain: Merano 8 and Kenscoff, features a modification of the amino acid from S to T at position 646.
+The protein's natural variant, known as in strain: Merano 7 and Merano 8, features a modification of the amino acid from T to A at position 653.
+The protein's natural variant, known as in strain: Merano 7 and Merano 8, features a modification of the amino acid from I to V at position 655.
+The protein's natural variant, known as in strain: cv. Cvi-0, features a modification of the amino acid from Q to E at position 75.
+The protein's natural variant, known as in strain: cv. C24, features a modification of the amino acid from I to V at position 84.
+The protein's natural variant, known as in strain: cv. C24, features a modification of the amino acid from K to E at position 257.
+The protein's natural variant, known as in strain: cv. C24, features a modification of the amino acid from N to D at position 266.
+The protein's natural variant, known as in strain: cv. Cvi-0, features a modification of the amino acid from S to T at position 297.
+The protein's natural variant, known as in strain: cv. C24, features a modification of the amino acid from L to F at position 299.
+The protein's natural variant, known as in isoform A and isoform H, features a modification of the amino acid from ANLP to GDLL at position 39.
+The protein's natural variant, known as in isoform A and isoform H, features a modification of the amino acid from E to D at position 55.
+The protein's natural variant, known as in isoform D, features a modification of the amino acid from D to G at position 56.
+The protein's natural variant, known as in isoform A and isoform B, features a modification of the amino acid from V to I at position 115.
+The protein's natural variant, known as in isoform H, features a modification of the amino acid from E to L at position 134.
+The protein's natural variant, known as in isoform H, features a modification of the amino acid from T to R at position 138.
+The protein's natural variant, known as in isoform H, features a modification of the amino acid from N to D at position 184.
+The protein's natural variant, known as in isoform H, features a modification of the amino acid from M to E at position 195.
+The protein's natural variant, known as in isoform H, features a modification of the amino acid from K to R at position 254.
+The protein's natural variant, known as in strain: cv. Cvi-0, features a modification of the amino acid from G to S at position 105.
+The protein's natural variant, known as in strain: cv. Cvi-0, features a modification of the amino acid from L to F at position 184.
+The protein's natural variant, known as in strain: cv. Cvi-0, features a modification of the amino acid from P to H at position 218.
+The protein's natural variant, known as in strain: cv. Cvi-0, features a modification of the amino acid from G to E at position 254.
+The protein's natural variant, known as in strain: cv. Cvi-0, features a modification of the amino acid from R to I at position 288.
+The protein's natural variant, known as in MDDGA13; no effect on Golgi localization; loss of beta-1,4-glucuronyltransferase activity;, features a modification of the amino acid from N to D at position 390.
+The protein's natural variant, known as in MDDGA13; no effect on Golgi localization; loss of beta-1,4-glucuronyltransferase activity;, features a modification of the amino acid from A to V at position 406.
+The protein's natural variant, known as in Japanese subjects with maturity-onset diabetes of the young; unknown pathological significance;, features a modification of the amino acid from A to V at position 328.
+The natural variant of this protein is characterized by an amino acid alteration from I to T at position 143.
+The protein's natural variant, known as in variant C, features a modification of the amino acid from E to D at position 27.
+The protein's natural variant, known as in variant C, features a modification of the amino acid from Q to H at position 86.
+The protein's natural variant, known as in NTD; unknown pathological significance;, features a modification of the amino acid from S to L at position 83.
+The protein's natural variant, known as in NTD; unknown pathological significance, features a modification of the amino acid from F to S at position 153.
+The protein's natural variant, known as in NTD; unknown pathological significance;, features a modification of the amino acid from R to Q at position 181.
+The protein's natural variant, known as in NTD; unknown pathological significance, features a modification of the amino acid from L to F at position 202.
+The protein's natural variant, known as in SDAM; abolishes ability to interact with DVL1, DVL2 and DVL3;, features a modification of the amino acid from V to I at position 239.
+The protein's natural variant, known as in NTD; does not abolish ability to interact with DVL1, DVL2 and DVL3;, features a modification of the amino acid from R to Q at position 274.
+The protein's natural variant, known as in NTD; does not abolish ability to interact with DVL1, DVL2 and DVL3;, features a modification of the amino acid from M to T at position 328.
+The protein's natural variant, known as in NTD; unknown pathological significance;, features a modification of the amino acid from A to S at position 404.
+The natural variant of this protein is characterized by an amino acid alteration from D to E at position 468.
+The protein's natural variant, known as in strain: cv. Alaska, features a modification of the amino acid from D to G at position 107.
+The protein's natural variant, known as in strain: cv. Alaska, features a modification of the amino acid from V to G at position 127.
+The protein's natural variant, known as in strain: cv. Alaska, features a modification of the amino acid from L to P at position 150.
+The protein's natural variant, known as in strain: cv. Alaska, features a modification of the amino acid from L to P at position 250.
+The protein's natural variant, known as in strain: cv. Alaska, features a modification of the amino acid from QQ to HK at position 327.
+The protein's natural variant, known as in strain: Kinshu, features a modification of the amino acid from G to R at position 23.
+The protein's natural variant, known as in MPS3D, features a modification of the amino acid from S to I at position 94.
+The protein's natural variant, known as in MPS3D, features a modification of the amino acid from K to R at position 340.
+The protein's natural variant, known as in MPS3D, features a modification of the amino acid from G to E at position 418.
+The protein's natural variant, known as probable disease-associated variant found in a family with congenital cataract; impaired interaction with PEX7; impaired ability to mediate peroxisomal import of proteins containing a C-terminal PTS2-type targeting signal without affecting import of proteins with a PTS1 targeting signal, features a modification of the amino acid from F to S at position 218.
+The protein's natural variant, known as in PBD2B; neonatal adrenoleukodystrophy; strongly affects peroxisomal protein import containing a C-terminal PTS1-type targeting signal without affecting import of proteins with a PTS2 targeting signal;, features a modification of the amino acid from N to K at position 526.
+The protein's natural variant, known as in PBD2B; infantile Refsum disease; mildly affects peroxisomal protein import, features a modification of the amino acid from S to W at position 600.
+The protein's natural variant, known as in RTD;, features a modification of the amino acid from T to M at position 282.
+The protein's natural variant, known as in Sc7 antigen;, features a modification of the amino acid from G to S at position 35.
+The protein's natural variant, known as in Sc5 antigen;, features a modification of the amino acid from E to K at position 47.
+The protein's natural variant, known as in Sc2 antigen;, features a modification of the amino acid from G to R at position 57.
+The protein's natural variant, known as in Sc4 antigen;, features a modification of the amino acid from P to A at position 60.
+The protein's natural variant, known as in Sc6 antigen;, features a modification of the amino acid from R to Q at position 81.
+The protein's natural variant, known as in Sc-3 allele, features a modification of the amino acid from DAQEGSVTLQI to CPRGKCHSADP at position 113.
+The protein's natural variant, known as in HH4; phenotype consistent with Kallmann syndrome;, features a modification of the amino acid from A to P at position 24.
+The protein's natural variant, known as in HH4; phenotype consistent with Kallmann syndrome;, features a modification of the amino acid from G to R at position 32.
+The protein's natural variant, known as in HH4; totally abolished intracellular calcium mobilization;, features a modification of the amino acid from C to Y at position 34.
+The protein's natural variant, known as in HH4;, features a modification of the amino acid from C to Y at position 46.
+The protein's natural variant, known as in HH4; no effect on intracellular calcium mobilization;, features a modification of the amino acid from I to M at position 50.
+The protein's natural variant, known as in HH4; phenotype consistent with Kallmann syndrome; impaired calcium mobilization;, features a modification of the amino acid from R to C at position 73.
+The protein's natural variant, known as in VWM;, features a modification of the amino acid from R to Q at position 209.
+The protein's natural variant, known as in VWM;, features a modification of the amino acid from A to V at position 228.
+The protein's natural variant, known as in VWM;, features a modification of the amino acid from L to R at position 269.
+The protein's natural variant, known as in VWM;, features a modification of the amino acid from R to Q at position 357.
+The protein's natural variant, known as in VWM;, features a modification of the amino acid from R to C at position 374.
+The protein's natural variant, known as in VWM; with ovarian failure;, features a modification of the amino acid from C to R at position 465.
+The protein's natural variant, known as in VWM; with ovarian failure;, features a modification of the amino acid from Y to H at position 489.
+The protein's natural variant, known as in allele TUM-, features a modification of the amino acid from A to T at position 154.
+The protein's natural variant, known as in MGC1;, features a modification of the amino acid from C to F at position 260.
+The protein's natural variant, known as in strain: FVB/N, features a modification of the amino acid from M to V at position 73.
+The protein's natural variant, known as in strain: P/J, features a modification of the amino acid from Y to F at position 111.
+The protein's natural variant, known as in GSD9B;, features a modification of the amino acid from A to P at position 118.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from L to V at position 867.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from G to R at position 877.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from R to G at position 9.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from K to R at position 13.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from E to G at position 17.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from E to G at position 21.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from Y to C at position 31.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from K to G at position 41.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from Q to R at position 46.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from E to G at position 50.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from Q to R at position 54.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from E to G at position 57.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from K to R at position 59.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from T to A at position 70.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from M to V at position 80.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from E to G at position 84.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from I to V at position 86.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from E to G at position 91.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from E to G at position 96.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from N to G at position 101.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from R to G at position 107.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from S to G at position 113.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from S to G at position 116.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from N to S at position 130.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from E to G at position 132.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from S to G at position 135.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from D to G at position 138.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from S to G at position 139.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from S to G at position 141.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from K to R at position 163.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from K to G at position 164.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from K to G at position 183.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from E to G at position 190.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from N to G at position 193.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from T to A at position 196.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from H to R at position 200.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from Y to C at position 205.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from K to G at position 207.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from T to A at position 213.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from E to G at position 218.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from K to G at position 220.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from Q to R at position 225.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from Y to C at position 265.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from K to R at position 275.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from K to G at position 298.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from H to R at position 299.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from T to A at position 302.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from Q to R at position 311.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from K to G at position 314.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from K to R at position 319.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from K to E at position 321.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from Q to R at position 322.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from T to A at position 328.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from K to R at position 354.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from N to S at position 355.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from K to G at position 368.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from E to G at position 381.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from I to V at position 383.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from T to A at position 389.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from N to S at position 393.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from E to G at position 396.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from E to G at position 398.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from T to A at position 400.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from K to R at position 406.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from K to E at position 409.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from S to G at position 430.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from H to R at position 431.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from S to G at position 433.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from N to S at position 437.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from M to V at position 444.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from E to G at position 453.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from E to G at position 456.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from Y to C at position 482.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from S to G at position 490.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from E to G at position 492.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from Q to R at position 493.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from S to G at position 497.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from T to A at position 510.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from Y to C at position 513.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from Q to R at position 516.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from R to G at position 520.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from Y to C at position 521.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from Q to R at position 525.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from N to G at position 540.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from Y to E at position 551.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from P to R at position 552.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from G to F at position 553.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from S to E at position 554.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from S to I at position 555.
+The protein's natural variant, known as in strain: CWL029 and TW-183, features a modification of the amino acid from S to A at position 30.
+The protein's natural variant, known as in strain: NC322, NC358 and NC359, features a modification of the amino acid from T to A at position 105.
+The protein's natural variant, known as in strain: NC390, features a modification of the amino acid from R to C at position 126.
+The protein's natural variant, known as in strain: MW25, features a modification of the amino acid from T to S at position 134.
+The natural variant of this protein is characterized by an amino acid alteration from K to E at position 225.
+The protein's natural variant, known as in MCPH16; unknown pathological significance;, features a modification of the amino acid from A to V at position 8.
+The protein's natural variant, known as in MCPH16; unknown pathological significance, features a modification of the amino acid from A to G at position 27.
+The protein's natural variant, known as in MCPH16, features a modification of the amino acid from A to P at position 109.
+The protein's natural variant, known as in MCPH16;, features a modification of the amino acid from G to W at position 201.
+The protein's natural variant, known as in MCPH16; unknown pathological significance; severe loss of VRK1 nuclear localization in non-dividing cells, features a modification of the amino acid from V to G at position 229.
+The protein's natural variant, known as in MCPH16; unknown pathological significance;, features a modification of the amino acid from R to C at position 536.
+The protein's natural variant, known as in MCPH16; unknown pathological significance;, features a modification of the amino acid from L to V at position 573.
+The protein's natural variant, known as in MCPH16; unknown pathological significance, features a modification of the amino acid from G to V at position 585.
+The protein's natural variant, known as in PCH13; impaired association with VPS50 and VPS53 subunits; reduced levels of assembled GARP and EARP complexes;, features a modification of the amino acid from R to C at position 490.
+The protein's natural variant, known as in mutant HO1; lacks DNA-binding activity, features a modification of the amino acid from P to S at position 115.
+The protein's natural variant, known as in strain: IFO 13350, features a modification of the amino acid from G to E at position 171.
+The protein's natural variant, known as in strain: IFO 13350, features a modification of the amino acid from AATDSGS to PTSEGGT at position 235.
+The protein's natural variant, known as in strain: IFO 13350, features a modification of the amino acid from GA to VT at position 256.
+The protein's natural variant, known as in strain: IFO 13350, features a modification of the amino acid from V to I at position 274.
+The protein's natural variant, known as in strain: Carmody, K2 and B33, features a modification of the amino acid from G to GG at position 246.
+The protein's natural variant, known as in MCAHS3; flow cytometric analysis of patient granulocytes and monocytes show decreased amounts of GPI-anchored proteins CD16B and CD59 compared to controls;, features a modification of the amino acid from T to P at position 183.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from T to M at position 467.
+The protein's natural variant, known as in strain: ECOR 1, ECOR 10, ECOR 11, ECOR 12, ECOR 13, ECOR 14, ECOR 15, ECOR 16, ECOR 17, ECOR 18, ECOR 19, ECOR 2, ECOR 20, ECOR 21, ECOR 22, ECOR 24, ECOR 25, ECOR 26, ECOR 27, ECOR 3, ECOR 30, ECOR 33, ECOR 34, ECOR 35, ECOR 36, ECOR 37, ECOR 38, ECOR 4, ECOR 40, ECOR 41, ECOR 42, ECOR 43, ECOR 44, ECOR 45, ECOR 46, ECOR 47, ECOR 48, ECOR 5, ECOR 50, ECOR 51, ECOR 52, ECOR 53, ECOR 54, ECOR 55, ECOR 56, ECOR 57, ECOR 59, ECOR 6, ECOR 60, ECOR 61, ECOR 62, ECOR 63, ECOR 64, ECOR 65, ECOR 66, ECOR 67, ECOR 68, ECOR 69, ECOR 7, ECOR 70, ECOR 71, ECOR 72, ECOR 8 and ECOR 9, features a modification of the amino acid from S to G at position 29.
+The protein's natural variant, known as in strain: ECOR 35, ECOR 36, ECOR 38, ECOR 40, ECOR 41, ECOR 51, ECOR 52, ECOR 53, ECOR 54, ECOR 55, ECOR 56, ECOR 57, ECOR 59, ECOR 60, ECOR 61, ECOR 62, ECOR 63 and ECOR 64, ECOR 65 and ECOR 66, features a modification of the amino acid from T to S at position 31.
+The protein's natural variant, known as in strain: ECOR 51, ECOR 52, ECOR 53, ECOR 54, ECOR 55, ECOR 56, ECOR 57, ECOR 59, ECOR 60, ECOR 61, ECOR 62, ECOR 63 and ECOR 64, features a modification of the amino acid from I to N at position 128.
+The protein's natural variant, known as in strain: ECOR 19, features a modification of the amino acid from V to L at position 129.
+The protein's natural variant, known as in strain: ECOR 44, ECOR 48, ECOR 50, ECOR 51, ECOR 52, ECOR 53, ECOR 54, ECOR 55, ECOR 56, ECOR 57, ECOR 59, ECOR 60, ECOR 61, ECOR 62, ECOR 63, ECOR 64 and ECOR 72, features a modification of the amino acid from G to S at position 144.
+The protein's natural variant, known as in strain: ECOR 27, features a modification of the amino acid from R to P at position 207.
+The protein's natural variant, known as in strain: ECOR 27, features a modification of the amino acid from Y to F at position 214.
+The protein's natural variant, known as in OI5; correlates with reduced expression and barely detectable secretion of SERPINF1;, features a modification of the amino acid from S to L at position 40.
+The protein's natural variant, known as in strain: DC-4, features a modification of the amino acid from Y to F at position 128.
+The protein's natural variant, known as in CDGF2; unknown pathological significance;, features a modification of the amino acid from S to P at position 223.
+The protein's natural variant, known as in CDGF2; unknown pathological significance;, features a modification of the amino acid from R to C at position 683.
+The protein's natural variant, known as in CDGF2; unknown pathological significance;, features a modification of the amino acid from K to Q at position 994.
+The protein's natural variant, known as associated with resistance to multiple myeloma;, features a modification of the amino acid from A to V at position 3.
+The protein's natural variant, known as associated with resistance to multiple myeloma;, features a modification of the amino acid from T to I at position 9.
+The protein's natural variant, known as in LIG4S and leukemia; impairs activity;, features a modification of the amino acid from R to H at position 278.
+The protein's natural variant, known as in LIG4S;, features a modification of the amino acid from G to E at position 469.
+The protein's natural variant, known as found in a patient with microcephalic primordial dwarfism; unknown pathological significance;, features a modification of the amino acid from L to P at position 774.
+The protein's natural variant, known as in PRLTS3;, features a modification of the amino acid from T to P at position 145.
+The protein's natural variant, known as in PRLTS3;, features a modification of the amino acid from C to S at position 147.
+The protein's natural variant, known as in PRLTS3, features a modification of the amino acid from Y to D at position 229.
+The protein's natural variant, known as in RP82; drastic decrease ARL2-binding, diffuse cytoplasmic localization, no enrichement at cilia basal body;, features a modification of the amino acid from M to R at position 45.
+The protein's natural variant, known as in strain: cv. Cardinal; clone 910, features a modification of the amino acid from M to I at position 76.
+The protein's natural variant, known as in strain: cv. Cardinal; clone 910, features a modification of the amino acid from L to P at position 97.
+The protein's natural variant, known as in strain: cv. Cardinal; clone 910, features a modification of the amino acid from R to G at position 146.
+The protein's natural variant, known as in strain: cv. Cardinal; clone 910, features a modification of the amino acid from D to E at position 150.
+The protein's natural variant, known as in strain: cv. Cardinal; clone 386, features a modification of the amino acid from S to P at position 190.
+The protein's natural variant, known as in strain: cv. Cardinal; clones 386 and 910, features a modification of the amino acid from S to P at position 195.
+The protein's natural variant, known as in strain: cv. Cardinal; clone 386, features a modification of the amino acid from P to L at position 223.
+The protein's natural variant, known as in strain: cv. Cardinal; clone 910, features a modification of the amino acid from I to N at position 245.
+The protein's natural variant, known as in strain: cv. Cardinal; clone 386, features a modification of the amino acid from I to S at position 245.
+The protein's natural variant, known as in strain: cv. Bengal and cv. Strawhull, features a modification of the amino acid from A to T at position 11.
+The protein's natural variant, known as in strain: cv. Strawhull; resistant to imidazolinone and sulfonylurea herbicides; when associated with T-11; R-293; E-390; D-401; D-604; N-627 and P-636, features a modification of the amino acid from S to P at position 160.
+The protein's natural variant, known as in strain: cv. Bengal and cv. Strawhull, features a modification of the amino acid from W to R at position 293.
+The protein's natural variant, known as in strain: cv. Strawhull; resistant to imidazolinone and sulfonylurea herbicides; when associated with T-11; P-160; R-293; D-401, D-604; N-627 and P-636, features a modification of the amino acid from K to E at position 390.
+The protein's natural variant, known as in strain: cv. Bengal and cv. Strawhull, features a modification of the amino acid from Q to D at position 401.
+The protein's natural variant, known as in strain: cv. Japonica /Kinmaze; resistant to imidazolinone and sulfonylurea herbicides; when associated with I-627, features a modification of the amino acid from W to L at position 548.
+The protein's natural variant, known as in strain: cv. Strawhull, features a modification of the amino acid from E to D at position 604.
+The protein's natural variant, known as in strain: cv. Japonica /Kinmaze; resistant to imidazolinone and sulfonylurea herbicides; when associated with L-548, features a modification of the amino acid from S to I at position 627.
+The protein's natural variant, known as in strain: cv. Strawhull; resistant to imidazolinone and sulfonylurea herbicides; when associated with T-11; P-160; R-293; E-390; D-401; D-604 and P-636, features a modification of the amino acid from S to N at position 627.
+The protein's natural variant, known as in strain: cv. Strawhull; resistant to imidazolinone and sulfonylurea herbicides; when associated with T-11, P-160; R-293; E-390; D-401; D-604 and N-627, features a modification of the amino acid from L to P at position 636.
+The protein's natural variant, known as in PDB6; unknown pathological significance;, features a modification of the amino acid from S to I at position 242.
+The protein's natural variant, known as in PDB6; enhances nuclear localization; increases expression levels; R-937 containing osteoclasts induced by treatment of peripheral blood mononuclear cells with CSF1 and TNFSF11 exhibit a greater number of nuclei, as well as a larger surface area than did those from the control individuals;, features a modification of the amino acid from P to R at position 937.
+The natural variant of this protein is characterized by an amino acid alteration from T to A at position 10.
+The natural variant of this protein is characterized by an amino acid alteration from F to C at position 94.
+The protein's natural variant, known as in CRC; displays steady-state catalytic activity linked to proton pumping that is approximately 34% of wild-type; an intrinsic proton leak is find in the enzyme, which will lead to decreased overall energy-conversion efficiency of the respiratory chain, perturbing transport processes such as protein, ion and metabolite trafficking;, features a modification of the amino acid from G to D at position 125.
+The protein's natural variant, known as in MT-C4D; significant decrease in enzyme activity;, features a modification of the amino acid from S to F at position 142.
+The protein's natural variant, known as in MT-C4D;, features a modification of the amino acid from L to I at position 196.
+The natural variant of this protein is characterized by an amino acid alteration from G to A at position 224.
+The protein's natural variant, known as found in two patients with acquired idiopathic sideroblastic anemia;, features a modification of the amino acid from M to T at position 273.
+The protein's natural variant, known as found in two patients with acquired idiopathic sideroblastic anemia;, features a modification of the amino acid from I to T at position 280.
+The protein's natural variant, known as in CRC; the mutant is probably not expressed, indicating that the amino acid substitution results in a severely altered overall structure of the enzyme;, features a modification of the amino acid from S to P at position 458.
+The protein's natural variant, known as in LHON; secondary mutation; does not seem to directly cause the disease, features a modification of the amino acid from S to SKQK at position 513.
+The protein's natural variant, known as in a cutaneous metastatic melanoma sample; somatic mutation;, features a modification of the amino acid from P to S at position 170.
+The protein's natural variant, known as in a cutaneous metastatic melanoma sample; somatic mutation, features a modification of the amino acid from V to G at position 284.
+The protein's natural variant, known as in a cutaneous metastatic melanoma sample; somatic mutation;, features a modification of the amino acid from M to I at position 344.
+The protein's natural variant, known as in a cutaneous metastatic melanoma sample; somatic mutation, features a modification of the amino acid from M to K at position 362.
+The protein's natural variant, known as in a cutaneous metastatic melanoma sample; somatic mutation, features a modification of the amino acid from S to L at position 536.
+The protein's natural variant, known as in strain: SHR, SHRSP and Wistar Kyoto, features a modification of the amino acid from G to C at position 583.
+The protein's natural variant, known as in strain: K289-3A, features a modification of the amino acid from Y to F at position 181.
+The protein's natural variant, known as in strain: K289-3A, features a modification of the amino acid from H to R at position 328.
+The natural variant of this protein is characterized by an amino acid alteration from R to H at position 5.
+The natural variant of this protein is characterized by an amino acid alteration from Y to H at position 231.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 322.
+The natural variant of this protein is characterized by an amino acid alteration from S to R at position 371.
+The natural variant of this protein is characterized by an amino acid alteration from S to G at position 615.
+The natural variant of this protein is characterized by an amino acid alteration from D to A at position 626.
+The protein's natural variant, known as in PVHH, features a modification of the amino acid from R to H at position 84.
+The protein's natural variant, known as in PVHH, features a modification of the amino acid from NIF to I at position 112.
+The protein's natural variant, known as in PVHH;, features a modification of the amino acid from P to R at position 280.
+The protein's natural variant, known as in PVHH;, features a modification of the amino acid from A to V at position 326.
+The protein's natural variant, known as in PVHH, features a modification of the amino acid from T to R at position 352.
+The protein's natural variant, known as in PVHH;, features a modification of the amino acid from L to V at position 398.
+The protein's natural variant, known as in PVHH, features a modification of the amino acid from G to R at position 412.
+The protein's natural variant, known as in PVHH;, features a modification of the amino acid from T to M at position 430.
+The protein's natural variant, known as in PVHH;, features a modification of the amino acid from T to R at position 430.
+The protein's natural variant, known as in CCMS; expression of the protein is reduced, features a modification of the amino acid from N to S at position 55.
+The protein's natural variant, known as in CCMS, features a modification of the amino acid from N to T at position 55.
+The protein's natural variant, known as in CCMS, features a modification of the amino acid from S to R at position 56.
+The protein's natural variant, known as in CCMS, features a modification of the amino acid from S to W at position 56.
+The protein's natural variant, known as in IMD103; reduced cytokine production in response to C.albicans infection; impaired NF-kappa-B transcriptional activity, features a modification of the amino acid from R to W at position 18.
+The protein's natural variant, known as in IMD103; abolished homooligomerization and formation of BCL10-nucleating filaments; reduced cytokine production in response to C.albicans infection; reduced production IgG antibodies in response to C.albicans infection;, features a modification of the amino acid from R to Q at position 35.
+The protein's natural variant, known as in IMD103; reduced cytokine production in response to C.albicans infection;, features a modification of the amino acid from R to H at position 57.
+The protein's natural variant, known as in IMD103; reduced cytokine production in response to C.albicans infection; impaired NF-kappa-B transcriptional activity; reduced production IgG antibodies in response to C.albicans infection;, features a modification of the amino acid from R to W at position 70.
+The protein's natural variant, known as in IMD103;, features a modification of the amino acid from G to S at position 72.
+The protein's natural variant, known as in IMD103; does not affect formation of the CBM complex but impairs formation of a complex with RASGRF1;, features a modification of the amino acid from Y to H at position 91.
+The protein's natural variant, known as in IMD103;, features a modification of the amino acid from R to C at position 101.
+The protein's natural variant, known as in IMD103, features a modification of the amino acid from R to L at position 101.
+The protein's natural variant, known as in IMD103; reduced cytokine production in response to C.albicans infection; does not affect NF-kappa-B transcriptional activity;, features a modification of the amino acid from K to E at position 196.
+The protein's natural variant, known as in IMD103; reduced cytokine production in response to C.albicans infection; does not affect NF-kappa-B transcriptional activity;, features a modification of the amino acid from R to P at position 373.
+The protein's natural variant, known as in IMD103, features a modification of the amino acid from A to P at position 380.
+The protein's natural variant, known as in allele F1, features a modification of the amino acid from D to N at position 104.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from Q to H at position 664.
+The protein's natural variant, known as in strain: C57BL/6 and Leaden XA1, features a modification of the amino acid from M to L at position 61.
+The protein's natural variant, known as in strain: C57BL/6 and Leaden XA1, features a modification of the amino acid from T to I at position 160.
+The protein's natural variant, known as in strain: C57BL/6 and Leaden XA1, features a modification of the amino acid from E to KK at position 246.
+The protein's natural variant, known as in allele HB-1Y; loss of CTL recognition for epitope HB-1. No influence on HLA-B/HLA-B44 binding, nor on the processing by the proteasome;, features a modification of the amino acid from H to Y at position 16.
+The protein's natural variant, known as in strain: 777-3A, features a modification of the amino acid from G to V at position 269.
+The protein's natural variant, known as in strain: 777-3A, features a modification of the amino acid from D to N at position 350.
+The protein's natural variant, known as in strain: 777-3A, features a modification of the amino acid from E to K at position 412.
+The protein's natural variant, known as in strain: 777-3A, features a modification of the amino acid from Q to M at position 434.
+The protein's natural variant, known as in strain: 777-3A, features a modification of the amino acid from S to N at position 437.
+The protein's natural variant, known as in strain: 777-3A, features a modification of the amino acid from TQ to NN at position 452.
+The protein's natural variant, known as in strain: 777-3A, features a modification of the amino acid from TDK to MNE at position 458.
+The protein's natural variant, known as in strain: 777-3A, features a modification of the amino acid from R to K at position 463.
+The protein's natural variant, known as in strain: 777-3A, features a modification of the amino acid from G to D at position 471.
+The protein's natural variant, known as in strain: 777-3A, features a modification of the amino acid from P to S at position 515.
+The natural variant of this protein is characterized by an amino acid alteration from A to R at position 392.
+The natural variant of this protein is characterized by an amino acid alteration from T to V at position 441.
+The natural variant of this protein is characterized by an amino acid alteration from A to E at position 446.
+The natural variant of this protein is characterized by an amino acid alteration from EEILA to TELLN at position 453.
+The natural variant of this protein is characterized by an amino acid alteration from K to KEELL at position 456.
+The protein's natural variant, known as in strain: 3CPA2, features a modification of the amino acid from R to G at position 69.
+The protein's natural variant, known as in strain: FrV3-1, features a modification of the amino acid from Y to S at position 441.
+The protein's natural variant, known as in strain: QD18, features a modification of the amino acid from K to T at position 495.
+The protein's natural variant, known as in strain: 122, features a modification of the amino acid from L to M at position 593.
+The protein's natural variant, known as in strain: QD18, features a modification of the amino acid from P to R at position 636.
+The protein's natural variant, known as in a gastric adenocarcinoma sample; somatic mutation, features a modification of the amino acid from A to V at position 51.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation, features a modification of the amino acid from P to R at position 322.
+The protein's natural variant, known as no effect on secretion; no effect on proglucagon processing;, features a modification of the amino acid from A to D at position 77.
+The protein's natural variant, known as decreased secretion; reduced proglucagon processing;, features a modification of the amino acid from A to T at position 267.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from D to N at position 424.
+The protein's natural variant, known as no effect on secretion; no effect on proglucagon processing;, features a modification of the amino acid from R to W at position 430.
+The protein's natural variant, known as no effect on secretion; no effect on proglucagon processing;, features a modification of the amino acid from M to V at position 525.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from I to V at position 155.
+The protein's natural variant, known as allele ADA*2; found in about 10% of the population; affects duration and intensity of deep sleep; enhances negative effects of sleep loss during sleep deprivation; may have a protective role against male infertility; 20% to 30% decrease in activity;, features a modification of the amino acid from D to N at position 8.
+The protein's natural variant, known as in ADASCID; loss of activity;, features a modification of the amino acid from H to D at position 15.
+The protein's natural variant, known as in ADASCID; loss of activity;, features a modification of the amino acid from G to R at position 20.
+The protein's natural variant, known as in ADASCID; delayed-onset;, features a modification of the amino acid from G to C at position 74.
+The protein's natural variant, known as in ADASCID;, features a modification of the amino acid from R to W at position 76.
+The protein's natural variant, known as in ADASCID; loss of activity;, features a modification of the amino acid from A to D at position 83.
+The protein's natural variant, known as in ADASCID; unknown pathological significance; loss of activity on its own; total loss of activity; when associated with V-106;, features a modification of the amino acid from Y to C at position 97.
+The protein's natural variant, known as in ADASCID;, features a modification of the amino acid from R to L at position 101.
+The protein's natural variant, known as in ADASCID; loss of activity;, features a modification of the amino acid from R to Q at position 101.
+The protein's natural variant, known as in ADASCID;, features a modification of the amino acid from R to W at position 101.
+The protein's natural variant, known as in ADASCID; unknown pathological significance; 30% of activity; total loss of activity; when associated with C-97;, features a modification of the amino acid from L to V at position 106.
+The protein's natural variant, known as in ADASCID;, features a modification of the amino acid from L to P at position 107.
+The protein's natural variant, known as in ADASCID; delayed-onset;, features a modification of the amino acid from V to M at position 129.
+The protein's natural variant, known as in ADASCID;, features a modification of the amino acid from G to E at position 140.
+The protein's natural variant, known as in a pancreatic ductal adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from R to Q at position 142.
+The protein's natural variant, known as in ADASCID;, features a modification of the amino acid from R to Q at position 149.
+The protein's natural variant, known as in ADASCID;, features a modification of the amino acid from R to W at position 149.
+The protein's natural variant, known as in an individual with partial ADA deficiency but no immunodeficiency; 1,5% of activity;, features a modification of the amino acid from L to M at position 152.
+The protein's natural variant, known as in ADASCID;, features a modification of the amino acid from R to C at position 156.
+The protein's natural variant, known as in ADASCID; loss of activity;, features a modification of the amino acid from R to H at position 156.
+The protein's natural variant, known as in ADASCID; loss of activity;, features a modification of the amino acid from V to M at position 177.
+The protein's natural variant, known as in ADASCID; loss of activity;, features a modification of the amino acid from A to D at position 179.
+The protein's natural variant, known as in ADASCID; delayed-onset;, features a modification of the amino acid from Q to P at position 199.
+The protein's natural variant, known as in ADASCID; late onset; 4% of activity;, features a modification of the amino acid from R to C at position 211.
+The protein's natural variant, known as in ADASCID;, features a modification of the amino acid from R to H at position 211.
+The protein's natural variant, known as in ADASCID; 8% of activity;, features a modification of the amino acid from A to T at position 215.
+The protein's natural variant, known as in ADASCID; severe;, features a modification of the amino acid from G to R at position 216.
+The protein's natural variant, known as in an individual with partial ADA deficiency but no immunodeficiency; 20% of activity;, features a modification of the amino acid from T to I at position 233.
+The protein's natural variant, known as in ADASCID;, features a modification of the amino acid from P to L at position 274.
+The protein's natural variant, known as in ADASCID;, features a modification of the amino acid from S to L at position 291.
+The protein's natural variant, known as in ADASCID;, features a modification of the amino acid from P to Q at position 297.
+The protein's natural variant, known as in ADASCID; loss of activity;, features a modification of the amino acid from L to R at position 304.
+The protein's natural variant, known as in ADASCID;, features a modification of the amino acid from A to V at position 329.
+The protein's natural variant, known as in FA12D; Tenri; inactive;, features a modification of the amino acid from Y to C at position 53.
+The protein's natural variant, known as in FA12D; CRM-negative phenotype; low levels of accumulation in the cell; not secreted, features a modification of the amino acid from R to P at position 142.
+The protein's natural variant, known as in HAE3;, features a modification of the amino acid from T to K at position 328.
+The protein's natural variant, known as in HAE3;, features a modification of the amino acid from T to R at position 328.
+The protein's natural variant, known as in FA12D; Locarno; inactive;, features a modification of the amino acid from R to P at position 372.
+The protein's natural variant, known as in FA12D; Shizuoka; CRM-negative phenotype; transcribed and synthesized at wild-type levels; not secreted;, features a modification of the amino acid from A to T at position 411.
+The protein's natural variant, known as in FA12D; CRM-negative phenotype, features a modification of the amino acid from L to M at position 414.
+The protein's natural variant, known as in FA12D; CRM-negative phenotype;, features a modification of the amino acid from R to Q at position 417.
+The protein's natural variant, known as in FA12D; CRM-negative phenotype; accumulation in the cell; low secretion, features a modification of the amino acid from Q to K at position 440.
+The protein's natural variant, known as in FA12D; CRM-positive phenotype, features a modification of the amino acid from D to N at position 461.
+The protein's natural variant, known as in FA12D; CRM-negative phenotype; transcribed and synthesized at wild-type levels; not secreted, features a modification of the amino acid from W to C at position 505.
+The protein's natural variant, known as in FA12D; CRM-positive phenotype;, features a modification of the amino acid from G to R at position 589.
+The protein's natural variant, known as in FA12D; Washington D.C.; inactive;, features a modification of the amino acid from C to S at position 590.
+The protein's natural variant, known as in EMARDD; unknown pathological significance;, features a modification of the amino acid from R to W at position 71.
+The protein's natural variant, known as in EMARDD; slightly decreased tyrosine phosphorylation; slightly reduced apoptotic cell engulfement by astrocytes; no effect on cell membrane location; no effect on binding to C1q; no effect on myoblasts migration and proliferation; no effect on interaction with NOTCH1;, features a modification of the amino acid from C to R at position 326.
+The protein's natural variant, known as in EMARDD; also found in a patient with MEGF10 myopathy; impairs tyrosine phosphorylation; no effect on cell membrane location; impairs binding to C1q; reduced apoptotic cell engulfement by astrocytes by 50%; reduced myoblast migration and proliferation; decreased interaction with NOTCH1; no effect on NOTCH1 nuclear location;, features a modification of the amino acid from C to R at position 774.
+The protein's natural variant, known as probable disease-associated variant found in a patient with MEGF10 myopathy;, features a modification of the amino acid from Y to C at position 1030.
+The protein's natural variant, known as in MPSVII; loss of activity, features a modification of the amino acid from R to H at position 166.
+The natural variant of this protein is characterized by an amino acid alteration from I to F at position 317.
+The protein's natural variant, known as in ADHD8; decreased propeptide cleavage, features a modification of the amino acid from H to Y at position 150.
+The protein's natural variant, known as in ACOGS; unknown pathological significance, features a modification of the amino acid from V to D at position 162.
+The protein's natural variant, known as in ARVD14; unknown pathological significance, features a modification of the amino acid from Q to P at position 229.
+The protein's natural variant, known as in ACOGS; decreased function in cell-cell adhesion;, features a modification of the amino acid from D to N at position 353.
+The protein's natural variant, known as in ARVD14; unknown pathological significance;, features a modification of the amino acid from D to N at position 407.
+The protein's natural variant, known as in ACOGS; unknown pathological significance, features a modification of the amino acid from D to G at position 525.
+The protein's natural variant, known as in ACOGS; decreased function in cell-cell adhesion;, features a modification of the amino acid from D to N at position 597.
+The protein's natural variant, known as in ACOGS;, features a modification of the amino acid from D to Y at position 597.
+The protein's natural variant, known as in ACOGS; decreased function in cell-cell adhesion;, features a modification of the amino acid from N to T at position 601.
+The protein's natural variant, known as in ACOGS; unknown pathological significance, features a modification of the amino acid from P to S at position 603.
+The protein's natural variant, known as in ACOGS; decreased function in cell-cell adhesion;, features a modification of the amino acid from C to W at position 613.
+The protein's natural variant, known as in ACOGS; decreased function in cell-cell adhesion;, features a modification of the amino acid from D to G at position 627.
+The protein's natural variant, known as in ACOGS; decreased function in cell-cell adhesion;, features a modification of the amino acid from Y to C at position 676.
+The protein's natural variant, known as risk factor for type 2 diabetes;, features a modification of the amino acid from C to R at position 18.
+The protein's natural variant, known as risk factor for type 2 diabetes;, features a modification of the amino acid from Q to L at position 59.
+The protein's natural variant, known as risk factor for type 2 diabetes;, features a modification of the amino acid from D to N at position 76.
+The protein's natural variant, known as risk factor for type 2 diabetes;, features a modification of the amino acid from R to H at position 197.
+The protein's natural variant, known as risk factor for type 2 diabetes, features a modification of the amino acid from P to PP at position 243.
+The protein's natural variant, known as in FCT, features a modification of the amino acid from L to P at position 131.
+The protein's natural variant, known as in BFPP; abolishes interaction with COL3A1;, features a modification of the amino acid from R to Q at position 38.
+The protein's natural variant, known as in BFPP; abolishes interaction with COL3A1; reduces cell surface localization;, features a modification of the amino acid from R to W at position 38.
+The protein's natural variant, known as in BFPP; abolishes interaction with COL3A1; reduces cell surface localization;, features a modification of the amino acid from Y to C at position 88.
+The protein's natural variant, known as in BFPP; abolishes interaction with COL3A1; reduces cell surface localization;, features a modification of the amino acid from C to S at position 91.
+The protein's natural variant, known as in BFPP; abolishes autoproteolytic cleavage; reduces cell surface localization;, features a modification of the amino acid from C to S at position 346.
+The protein's natural variant, known as in BFPP; abolishes autoproteolytic cleavage; reduces cell surface localization, features a modification of the amino acid from W to S at position 349.
+The protein's natural variant, known as in BFPP; reduces cell surface localization;, features a modification of the amino acid from E to K at position 496.
+The protein's natural variant, known as in BFPP; reduces cell surface localization;, features a modification of the amino acid from R to W at position 565.
+The protein's natural variant, known as in BFPP; unclear effects on cell surface localization; blocks downstream RhoA activation, features a modification of the amino acid from L to R at position 640.
+The protein's natural variant, known as in LCCS3; loss of activity;, features a modification of the amino acid from D to N at position 253.
+The protein's natural variant, known as in MPS3C; shows practically no enzyme activity, features a modification of the amino acid from A to V at position 82.
+The protein's natural variant, known as in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum; loss of intralysosomal proteolytic cleavage, features a modification of the amino acid from C to F at position 104.
+The protein's natural variant, known as in MPS3C; shows practically no enzyme activity, features a modification of the amino acid from L to P at position 141.
+The protein's natural variant, known as in RP73, features a modification of the amino acid from R to W at position 152.
+The protein's natural variant, known as in RP73, features a modification of the amino acid from G to A at position 161.
+The protein's natural variant, known as in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum, features a modification of the amino acid from L to P at position 165.
+The protein's natural variant, known as likely benign variant; does not influence stability; does not influence activity; does not influence cellular localization of the enzyme, features a modification of the amino acid from P to Q at position 265.
+The protein's natural variant, known as in MPS3C, features a modification of the amino acid from I to R at position 280.
+The protein's natural variant, known as in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum, features a modification of the amino acid from G to R at position 290.
+The protein's natural variant, known as in MPS3C; retained in the endoplasmic reticulum; loss of enzymatic activity, features a modification of the amino acid from N to K at position 301.
+The protein's natural variant, known as in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum, features a modification of the amino acid from P to L at position 311.
+The protein's natural variant, known as in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum, features a modification of the amino acid from R to C at position 372.
+The protein's natural variant, known as in MPS3C; retained in the endoplasmic reticulum; loss of enzymatic activity, features a modification of the amino acid from R to H at position 372.
+The protein's natural variant, known as in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum, features a modification of the amino acid from W to C at position 431.
+The protein's natural variant, known as in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum, features a modification of the amino acid from G to S at position 452.
+The protein's natural variant, known as in MPS3C; shows practically no enzyme activity, features a modification of the amino acid from G to V at position 452.
+The protein's natural variant, known as in MPS3C; shows practically no enzyme activity, features a modification of the amino acid from L to P at position 473.
+The protein's natural variant, known as in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum, features a modification of the amino acid from E to K at position 499.
+The protein's natural variant, known as likely benign variant; no loss of enzymatic activity, features a modification of the amino acid from V to L at position 509.
+The protein's natural variant, known as in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum, features a modification of the amino acid from M to K at position 510.
+The protein's natural variant, known as in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum, features a modification of the amino acid from G to E at position 514.
+The protein's natural variant, known as in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum, features a modification of the amino acid from A to E at position 517.
+The protein's natural variant, known as in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum, features a modification of the amino acid from S to F at position 546.
+The protein's natural variant, known as no loss of enzymatic activity;, features a modification of the amino acid from K to Q at position 551.
+The protein's natural variant, known as in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum, features a modification of the amino acid from S to C at position 567.
+The protein's natural variant, known as in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity, features a modification of the amino acid from S to L at position 569.
+The protein's natural variant, known as in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity, features a modification of the amino acid from D to V at position 590.
+The protein's natural variant, known as in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity, features a modification of the amino acid from P to L at position 599.
+The protein's natural variant, known as in RP73 and MPS3C; unknown pathological significance; may act as a modifier of disease severity in patients with retinitis pigmentosa; has a negligible effect on the enzyme expression; moderately reduced enzyme activity;, features a modification of the amino acid from A to T at position 643.
+The protein's natural variant, known as found in an oligozoospermic man; unknown pathological significance, features a modification of the amino acid from D to G at position 136.
+The protein's natural variant, known as in CORD16 and BBS21; does not affect interaction with FAM161A.;, features a modification of the amino acid from R to W at position 177.
+The protein's natural variant, known as in RP64; does not affect interaction with FAM161A.;, features a modification of the amino acid from Q to R at position 182.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to H at position 530.
+The protein's natural variant, known as in RP66; abolishes secretion; results in mis-folded insoluble complexes degraded via the ER-associated protein catabolic process;, features a modification of the amino acid from D to N at position 1080.
+The protein's natural variant, known as in strain: PS246, features a modification of the amino acid from V to F at position 34.
+The protein's natural variant, known as in strain: PS230, features a modification of the amino acid from V to I at position 68.
+The protein's natural variant, known as in strain: PS295, features a modification of the amino acid from K to R at position 185.
+The protein's natural variant, known as in strain: 4aRR, PEST, features a modification of the amino acid from L to V at position 7.
+The protein's natural variant, known as in strain: 4aRR, PEST, features a modification of the amino acid from D to V at position 19.
+The protein's natural variant, known as in strain: L3-5, features a modification of the amino acid from E to K at position 28.
+The protein's natural variant, known as in strain: L3-5, features a modification of the amino acid from P to S at position 37.
+The protein's natural variant, known as in strain: Yaounde Yd41, features a modification of the amino acid from K to Q at position 55.
+The protein's natural variant, known as in strain: Yaounde Yd21, Yaounde Yd35, Yaounde Yd41, features a modification of the amino acid from A to S at position 73.
+The protein's natural variant, known as in strain: G3, features a modification of the amino acid from A to V at position 88.
+The protein's natural variant, known as in strain: 4aRR, PEST, features a modification of the amino acid from P to S at position 89.
+The protein's natural variant, known as in strain: CWL029 and TW-183, features a modification of the amino acid from L to F at position 186.
+The protein's natural variant, known as in HH9; phenotype consistent with Kallmann syndrome; the patient also carries a mutation in FGFR1;, features a modification of the amino acid from R to H at position 196.
+The protein's natural variant, known as in HH9; sporadic case;, features a modification of the amino acid from T to A at position 480.
+The protein's natural variant, known as in HNPCC7;, features a modification of the amino acid from Q to E at position 24.
+The protein's natural variant, known as in HNPCC7;, features a modification of the amino acid from N to S at position 499.
+The protein's natural variant, known as in HNPCC7;, features a modification of the amino acid from E to Q at position 624.
+The protein's natural variant, known as in HNPCC7;, features a modification of the amino acid from R to C at position 647.
+The protein's natural variant, known as in HNPCC7;, features a modification of the amino acid from S to G at position 817.
+The protein's natural variant, known as in HNPCC7;, features a modification of the amino acid from G to S at position 981.
+The protein's natural variant, known as in HNPCC7;, features a modification of the amino acid from N to S at position 1007.
+The natural variant of this protein is characterized by an amino acid alteration from G to R at position 1319.
+The protein's natural variant, known as in HNPCC7;, features a modification of the amino acid from A to T at position 1394.
+The protein's natural variant, known as in HNPCC7;, features a modification of the amino acid from E to K at position 1451.
+The protein's natural variant, known as in MCPHSBA;, features a modification of the amino acid from L to P at position 371.
+The natural variant of this protein is characterized by an amino acid alteration from R to Z at position 30.
+The protein's natural variant, known as in DFNB37;, features a modification of the amino acid from E to V at position 216.
+The protein's natural variant, known as in DFNHCM;, features a modification of the amino acid from H to R at position 246.
+The protein's natural variant, known as in DFNA22, features a modification of the amino acid from C to Y at position 442.
+The protein's natural variant, known as in strain: EFB1, features a modification of the amino acid from E to D at position 103.
+The protein's natural variant, known as in strain: MS11 / V18, features a modification of the amino acid from SED to MLKA at position 4.
+The protein's natural variant, known as in strain: MS11 / V18, features a modification of the amino acid from V to M at position 234.
+The protein's natural variant, known as in ST; causes an absence of mature T-cells due to thymocyte development being arrested at the CD4+CD8+ stage, features a modification of the amino acid from R to C at position 464.
+The protein's natural variant, known as in pyrimethamine resistance, features a modification of the amino acid from S to N at position 110.
+The protein's natural variant, known as in pyrimethamine resistance, features a modification of the amino acid from S to F at position 177.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from P to S at position 140.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from G to R at position 286.
+The protein's natural variant, known as found in a patient with schizophrenia; unknown pathological significance, features a modification of the amino acid from L to V at position 466.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from E to G at position 527.
+The protein's natural variant, known as found in a patient with autism spectrum disorder; unknown pathological significance, features a modification of the amino acid from M to L at position 592.
+The protein's natural variant, known as in DEE46; gain-of-function mutation that potentiates ionotropic glutamate receptor signaling; mutant receptors are activated by lower concentrations of glutamate and glycine and show slower deactivation after agonist removal as well as decreased sensitivity to allosteric inhibitors indicating that NMDA glutamate receptor activity is changed;, features a modification of the amino acid from V to I at position 667.
+The protein's natural variant, known as found in a patient with schizophrenia; unknown pathological significance, features a modification of the amino acid from M to V at position 733.
+The protein's natural variant, known as found in a patient with schizophrenia; unknown pathological significance;, features a modification of the amino acid from R to H at position 872.
+The protein's natural variant, known as found in patients with schizophrenia; unknown pathological significance;, features a modification of the amino acid from A to V at position 922.
+The protein's natural variant, known as found in a patient with autism spectrum disorder; unknown pathological significance, features a modification of the amino acid from A to T at position 926.
+The protein's natural variant, known as in KTS; in 5 patients; displays a stronger angiogenic activity;, features a modification of the amino acid from E to K at position 133.
+The protein's natural variant, known as confirmed at protein level;, features a modification of the amino acid from G to D at position 284.
+The protein's natural variant, known as in DRS1; hypomorphic mutation;, features a modification of the amino acid from C to S at position 83.
+The protein's natural variant, known as in DRS1; unknown pathological significance, features a modification of the amino acid from S to C at position 160.
+The protein's natural variant, known as in DRS1, features a modification of the amino acid from C to CGC at position 164.
+The protein's natural variant, known as in DRS1; hypomorphic mutation;, features a modification of the amino acid from C to R at position 182.
+The protein's natural variant, known as in SCA50; unknown pathological significance, features a modification of the amino acid from R to L at position 143.
+The protein's natural variant, known as in SCA50; unknown pathological significance; abolishes secretion; loss of multimerization ability, features a modification of the amino acid from E to G at position 327.
+The protein's natural variant, known as in SCA50, features a modification of the amino acid from Q to R at position 370.
+The protein's natural variant, known as in SCA50; does not affect secretion; does not affect multimerization, features a modification of the amino acid from G to R at position 389.
+The protein's natural variant, known as in 40% of the molecules, features a modification of the amino acid from A to S at position 109.
+The protein's natural variant, known as in 3MC2; unknown pathological significance, features a modification of the amino acid from A to T at position 166.
+The protein's natural variant, known as in 3MC2; no effect on homotrimerization; loss of calcium-binding; loss of carbohydrate-binding probably due to the inability to bind calcium; not secreted probably due to degradation early after biosynthesis;, features a modification of the amino acid from S to P at position 169.
+The protein's natural variant, known as in 3MC2; no effect on homotrimerization; loss of calcium-binding; loss of carbohydrate-binding probably due to the inability to bind calcium; not secreted probably due to degradation early after biosynthesis;, features a modification of the amino acid from G to S at position 204.
+The natural variant of this protein is characterized by an amino acid alteration from Q to H at position 34.
+The natural variant of this protein is characterized by an amino acid alteration from P to L at position 38.
+The natural variant of this protein is characterized by an amino acid alteration from L to F at position 384.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 199.
+The protein's natural variant, known as in DYT11, features a modification of the amino acid from T to R at position 36.
+The protein's natural variant, known as in DYT11; affects protein stability; the mutant undergoes endoplasmic reticulum-associated degradation, features a modification of the amino acid from H to P at position 60.
+The protein's natural variant, known as in DYT11; affects protein stability; the mutant undergoes endoplasmic reticulum-associated degradation, features a modification of the amino acid from H to R at position 60.
+The protein's natural variant, known as in DYT11; results in gain-of-glycosylation; the mutant is targeted to the plasma membrane at reduced levels compared to wild-type, features a modification of the amino acid from M to T at position 92.
+The protein's natural variant, known as in DYT11, features a modification of the amino acid from W to G at position 100.
+The protein's natural variant, known as in DYT11, features a modification of the amino acid from G to R at position 112.
+The protein's natural variant, known as in DYT11; affects protein stability; the mutant undergoes endoplasmic reticulum-associated degradation, features a modification of the amino acid from Y to C at position 115.
+The protein's natural variant, known as in DYT11, features a modification of the amino acid from L to S at position 175.
+The protein's natural variant, known as in DYT11, features a modification of the amino acid from S to C at position 177.
+The protein's natural variant, known as in DYT11; affects protein stability; the mutant undergoes endoplasmic reticulum-associated degradation;, features a modification of the amino acid from L to P at position 184.
+The protein's natural variant, known as in DYT11;, features a modification of the amino acid from L to R at position 196.
+The protein's natural variant, known as in DYT11; affects protein stability; the mutant undergoes endoplasmic reticulum-associated degradation, features a modification of the amino acid from W to R at position 270.
+The protein's natural variant, known as in DYT11; affects protein stability; the mutant undergoes endoplasmic reticulum-associated degradation;, features a modification of the amino acid from C to Y at position 271.
+The protein's natural variant, known as in BLM;, features a modification of the amino acid from Q to R at position 672.
+The protein's natural variant, known as in BLM;, features a modification of the amino acid from I to T at position 841.
+The protein's natural variant, known as in BLM;, features a modification of the amino acid from T to I at position 843.
+The protein's natural variant, known as in BLM, features a modification of the amino acid from C to R at position 878.
+The protein's natural variant, known as in BLM;, features a modification of the amino acid from G to E at position 891.
+The protein's natural variant, known as in BLM;, features a modification of the amino acid from C to Y at position 901.
+The protein's natural variant, known as in BLM;, features a modification of the amino acid from C to F at position 1036.
+The protein's natural variant, known as in BLM;, features a modification of the amino acid from C to S at position 1055.
+The protein's natural variant, known as in GLCC; unknown pathological significance;, features a modification of the amino acid from E to K at position 184.
+The protein's natural variant, known as may be associated with increased risk for prostate cancer; results in decreased affinity for laminin;, features a modification of the amino acid from D to N at position 1675.
+The natural variant of this protein is characterized by an amino acid alteration from R to F at position 22.
+The natural variant of this protein is characterized by an amino acid alteration from F to G at position 41.
+The protein's natural variant, known as in strain: Isolate LSUMZ 36303, features a modification of the amino acid from S to P at position 345.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from L to V at position 290.
+The protein's natural variant, known as in MCPH7;, features a modification of the amino acid from L to W at position 798.
+The natural variant of this protein is characterized by an amino acid alteration from P to R at position 1012.
+The protein's natural variant, known as in RP44;, features a modification of the amino acid from S to R at position 66.
+The protein's natural variant, known as in DFNA76, features a modification of the amino acid from F to S at position 128.
+The protein's natural variant, known as in DFNA76, features a modification of the amino acid from L to R at position 238.
+The protein's natural variant, known as in DFNA76, features a modification of the amino acid from E to K at position 269.
+The protein's natural variant, known as in DFNA76, features a modification of the amino acid from L to F at position 363.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from E to D at position 277.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from P to L at position 705.
+The protein's natural variant, known as in strain: BO, DJI, Harare, Martinique, Recife, Supercar, TemR and Trans; confers resistance to insecticides, features a modification of the amino acid from G to S at position 97.
+The protein's natural variant, known as in strain: TemR and Trans, features a modification of the amino acid from A to T at position 114.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from G to D at position 572.
+The protein's natural variant, known as in MC4DN5;, features a modification of the amino acid from A to V at position 354.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from E to Q at position 106.
+The protein's natural variant, known as in strain: Isolate LVT 3645, features a modification of the amino acid from T to A at position 23.
+The protein's natural variant, known as in strain: Isolate LVT 3645, features a modification of the amino acid from I to M at position 60.
+The protein's natural variant, known as in strain: Isolate LVT 3645, features a modification of the amino acid from M to I at position 118.
+The protein's natural variant, known as in strain: Isolate LVT 3645, features a modification of the amino acid from T to S at position 159.
+The protein's natural variant, known as in strain: Isolate LVT 3645, features a modification of the amino acid from F to L at position 226.
+The protein's natural variant, known as in strain: Isolate LVT 3645, features a modification of the amino acid from S to T at position 241.
+The protein's natural variant, known as in strain: Isolate LVT 3645, features a modification of the amino acid from V to I at position 295.
+The protein's natural variant, known as in strain: Isolate LVT 3645, features a modification of the amino acid from F to L at position 333.
+The protein's natural variant, known as in strain: Isolate LVT 3645, features a modification of the amino acid from V to I at position 353.
+The protein's natural variant, known as in strain: Isolate LVT 3645, features a modification of the amino acid from F to L at position 365.
+The protein's natural variant, known as in strain: Isolate LVT 3645, features a modification of the amino acid from I to V at position 368.
+The protein's natural variant, known as in strain: Isolate LVT 3645, features a modification of the amino acid from V to I at position 376.
+The protein's natural variant, known as in lau; allele tb233c; semicircular canal defects, features a modification of the amino acid from I to N at position 963.
+The protein's natural variant, known as in lau; allele tk256a; semicircular canal defects, features a modification of the amino acid from P to L at position 969.
+The protein's natural variant, known as in Le(-);, features a modification of the amino acid from L to R at position 20.
+The protein's natural variant, known as in Le(-);, features a modification of the amino acid from W to R at position 68.
+The protein's natural variant, known as in Le(+);, features a modification of the amino acid from Q to K at position 102.
+The protein's natural variant, known as in Le(-);, features a modification of the amino acid from T to M at position 105.
+The protein's natural variant, known as in Le(+);, features a modification of the amino acid from S to A at position 124.
+The protein's natural variant, known as in Le(-); about 20% of alpha (1,3/1,4)fucosyltransferase activity;, features a modification of the amino acid from D to N at position 162.
+The protein's natural variant, known as in Le(-); completely inactive;, features a modification of the amino acid from G to S at position 170.
+The protein's natural variant, known as in Le(-); Loss of alpha (1,3/1,4)fucosyltransferase activity.;, features a modification of the amino acid from G to R at position 223.
+The protein's natural variant, known as in Le(-); Loss of alpha (1,3/1,4)fucosyltransferase activity.;, features a modification of the amino acid from V to M at position 270.
+The protein's natural variant, known as in Le(-);, features a modification of the amino acid from D to A at position 336.
+The protein's natural variant, known as in Le(-); less than 10% reduction in activity;, features a modification of the amino acid from I to K at position 356.
+The protein's natural variant, known as in minor component, features a modification of the amino acid from A to I at position 35.
+The natural variant of this protein is characterized by an amino acid alteration from S to SS at position 150.
+The protein's natural variant, known as in Raleigh; O(2) affinity down;, features a modification of the amino acid from V to A at position 2.
+The protein's natural variant, known as in Graz;, features a modification of the amino acid from H to L at position 3.
+The protein's natural variant, known as in Okayama; O(2) affinity up;, features a modification of the amino acid from H to Q at position 3.
+The protein's natural variant, known as in Deer Lodge; O(2) affinity up;, features a modification of the amino acid from H to R at position 3.
+The protein's natural variant, known as in Fukuoka;, features a modification of the amino acid from H to Y at position 3.
+The protein's natural variant, known as in Warwickshire;, features a modification of the amino acid from P to R at position 6.
+The protein's natural variant, known as in G-Makassar;, features a modification of the amino acid from E to A at position 7.
+The protein's natural variant, known as in Hb C; confers resistance to severe malaria;, features a modification of the amino acid from E to K at position 7.
+The protein's natural variant, known as in Machida;, features a modification of the amino acid from E to Q at position 7.
+The protein's natural variant, known as in SKCA; Hb S; at heterozygosity confers resistance to malaria;, features a modification of the amino acid from E to V at position 7.
+The protein's natural variant, known as in G-San Jose; mildly unstable;, features a modification of the amino acid from E to G at position 8.
+The protein's natural variant, known as in G-Siriraj;, features a modification of the amino acid from E to K at position 8.
+The protein's natural variant, known as in N-Timone;, features a modification of the amino acid from K to E at position 9.
+The protein's natural variant, known as in J-Luhe;, features a modification of the amino acid from K to Q at position 9.
+The protein's natural variant, known as in Rio Grande;, features a modification of the amino acid from K to T at position 9.
+The protein's natural variant, known as in Porto Alegre; O(2) affinity up;, features a modification of the amino acid from S to C at position 10.
+The protein's natural variant, known as in Ankara;, features a modification of the amino acid from A to D at position 11.
+The protein's natural variant, known as in Iraq-Halabja;, features a modification of the amino acid from A to V at position 11.
+The protein's natural variant, known as in Windsor; O(2) affinity up; unstable;, features a modification of the amino acid from V to D at position 12.
+The protein's natural variant, known as in Hamilton;, features a modification of the amino acid from V to I at position 12.
+The protein's natural variant, known as in J-Lens;, features a modification of the amino acid from A to D at position 14.
+The protein's natural variant, known as in Saki; unstable;, features a modification of the amino acid from L to P at position 15.
+The protein's natural variant, known as in Soegn; unstable;, features a modification of the amino acid from L to R at position 15.
+The protein's natural variant, known as in Randwick; unstable;, features a modification of the amino acid from W to G at position 16.
+The protein's natural variant, known as in Belfast; O(2) affinity up; unstable;, features a modification of the amino acid from W to R at position 16.
+The protein's natural variant, known as in J-Baltimore/J-Trinidad/J-Ireland/J-Georgia/N-New Haven;, features a modification of the amino acid from G to D at position 17.
+The protein's natural variant, known as in D-Bushman;, features a modification of the amino acid from G to R at position 17.
+The protein's natural variant, known as in Nagasaki;, features a modification of the amino acid from K to E at position 18.
+The protein's natural variant, known as in J-Amiens;, features a modification of the amino acid from K to N at position 18.
+The protein's natural variant, known as in Nikosia;, features a modification of the amino acid from K to Q at position 18.
+The protein's natural variant, known as in Baden; slightly unstable;, features a modification of the amino acid from V to M at position 19.
+The protein's natural variant, known as in Alamo;, features a modification of the amino acid from N to D at position 20.
+The protein's natural variant, known as in D-Ouleh RABAH;, features a modification of the amino acid from N to K at position 20.
+The protein's natural variant, known as in Malay;, features a modification of the amino acid from N to S at position 20.
+The protein's natural variant, known as in Olympia; O(2) affinity up;, features a modification of the amino acid from V to M at position 21.
+The protein's natural variant, known as in Connecticut; O(2) affinity down;, features a modification of the amino acid from D to G at position 22.
+The protein's natural variant, known as in Karlskoga;, features a modification of the amino acid from D to H at position 22.
+The protein's natural variant, known as in Cocody;, features a modification of the amino acid from D to N at position 22.
+The protein's natural variant, known as in Yusa;, features a modification of the amino acid from D to Y at position 22.
+The protein's natural variant, known as in G-Coushatta/G-Saskatoon/G-Taegu/Hsin Chu;, features a modification of the amino acid from E to A at position 23.
+The protein's natural variant, known as in G-Taipei;, features a modification of the amino acid from E to G at position 23.
+The protein's natural variant, known as in E-Saskatoon;, features a modification of the amino acid from E to K at position 23.
+The protein's natural variant, known as in D-Iran;, features a modification of the amino acid from E to Q at position 23.
+The protein's natural variant, known as in D-Granada;, features a modification of the amino acid from E to V at position 23.
+The protein's natural variant, known as in Strasbourg; O(2) affinity up;, features a modification of the amino acid from V to D at position 24.
+The protein's natural variant, known as in Palmerston North; O(2) affinity up; unstable;, features a modification of the amino acid from V to F at position 24.
+The protein's natural variant, known as in Miyashiro; O(2) affinity up; unstable;, features a modification of the amino acid from V to G at position 24.
+The protein's natural variant, known as in Moscva; O(2) affinity down; unstable;, features a modification of the amino acid from G to D at position 25.
+The protein's natural variant, known as in Riverdale-Bronx; O(2) affinity up; unstable;, features a modification of the amino acid from G to R at position 25.
+The protein's natural variant, known as in Savannah; unstable;, features a modification of the amino acid from G to V at position 25.
+The protein's natural variant, known as in J-Auckland; unstable; O(2) affinity down;, features a modification of the amino acid from G to D at position 26.
+The protein's natural variant, known as in G-Taiwan Ami;, features a modification of the amino acid from G to R at position 26.
+The protein's natural variant, known as in B-THAL; Hb E; confers resistance to severe malaria;, features a modification of the amino acid from E to K at position 27.
+The protein's natural variant, known as in Henri Mondor; slightly unstable;, features a modification of the amino acid from E to V at position 27.
+The protein's natural variant, known as in Volga/Drenthe; unstable;, features a modification of the amino acid from A to D at position 28.
+The protein's natural variant, known as in Knossos;, features a modification of the amino acid from A to S at position 28.
+The protein's natural variant, known as in Grange-blanche; O(2) affinity up;, features a modification of the amino acid from A to V at position 28.
+The protein's natural variant, known as in Genova/Hyogo; unstable;, features a modification of the amino acid from L to P at position 29.
+The protein's natural variant, known as in St Louis;, features a modification of the amino acid from L to Q at position 29.
+The protein's natural variant, known as in Lufkin; unstable;, features a modification of the amino acid from G to D at position 30.
+The protein's natural variant, known as in Tacoma; unstable;, features a modification of the amino acid from R to S at position 31.
+The protein's natural variant, known as in Yokohama; unstable;, features a modification of the amino acid from L to P at position 32.
+The protein's natural variant, known as in Castilla; unstable;, features a modification of the amino acid from L to R at position 33.
+The protein's natural variant, known as in Muscat; slightly unstable;, features a modification of the amino acid from L to V at position 33.
+The protein's natural variant, known as in Santander; unstable;, features a modification of the amino acid from V to D at position 35.
+The protein's natural variant, known as in Pitie-Salpetriere; O(2) affinity up;, features a modification of the amino acid from V to F at position 35.
+The protein's natural variant, known as in Nantes; increased oxygen affinity;, features a modification of the amino acid from V to L at position 35.
+The protein's natural variant, known as in Philly; O(2) affinity up; unstable;, features a modification of the amino acid from Y to F at position 36.
+The protein's natural variant, known as in Sunnybrook;, features a modification of the amino acid from P to R at position 37.
+The protein's natural variant, known as in North Chicago; O(2) affinity up;, features a modification of the amino acid from P to S at position 37.
+The protein's natural variant, known as in Linkoping/Finlandia; O(2) affinity up;, features a modification of the amino acid from P to T at position 37.
+The protein's natural variant, known as in Howick;, features a modification of the amino acid from W to G at position 38.
+The protein's natural variant, known as in Rothschild; O(2) affinity down;, features a modification of the amino acid from W to R at position 38.
+The protein's natural variant, known as in Hirose; O(2) affinity up;, features a modification of the amino acid from W to S at position 38.
+The protein's natural variant, known as in Hinwil; O(2) affinity up;, features a modification of the amino acid from T to N at position 39.
+The protein's natural variant, known as in Vaasa; unstable;, features a modification of the amino acid from Q to E at position 40.
+The protein's natural variant, known as in Alabama;, features a modification of the amino acid from Q to K at position 40.
+The protein's natural variant, known as in Tianshui;, features a modification of the amino acid from Q to R at position 40.
+The protein's natural variant, known as in Mequon;, features a modification of the amino acid from F to Y at position 42.
+The protein's natural variant, known as in Louisville; unstable;, features a modification of the amino acid from F to L at position 43.
+The protein's natural variant, known as in Hammersmith;, features a modification of the amino acid from F to S at position 43.
+The protein's natural variant, known as in Hoshida/Chaya;, features a modification of the amino acid from E to Q at position 44.
+The protein's natural variant, known as in Mississippi;, features a modification of the amino acid from S to C at position 45.
+The protein's natural variant, known as in Cheverly; unstable;, features a modification of the amino acid from F to S at position 46.
+The protein's natural variant, known as in K-Ibadan;, features a modification of the amino acid from G to E at position 47.
+The protein's natural variant, known as in Avicenna;, features a modification of the amino acid from D to A at position 48.
+The protein's natural variant, known as in Gavello;, features a modification of the amino acid from D to G at position 48.
+The protein's natural variant, known as in Maputo;, features a modification of the amino acid from D to Y at position 48.
+The protein's natural variant, known as in Bab-Saadoum; slightly unstable;, features a modification of the amino acid from L to P at position 49.
+The protein's natural variant, known as in Las Palmas; slightly unstable;, features a modification of the amino acid from S to F at position 50.
+The protein's natural variant, known as in Edmonton, features a modification of the amino acid from T to K at position 51.
+The protein's natural variant, known as in Willamette; O(2) affinity up; unstable;, features a modification of the amino acid from P to R at position 52.
+The protein's natural variant, known as in Ocho Rios;, features a modification of the amino acid from D to A at position 53.
+The protein's natural variant, known as in Summer Hill;, features a modification of the amino acid from D to H at position 53.
+The protein's natural variant, known as in Jacksonville; O(2) affinity up; unstable;, features a modification of the amino acid from V to D at position 55.
+The protein's natural variant, known as in Matera; unstable;, features a modification of the amino acid from M to K at position 56.
+The protein's natural variant, known as in Hamadan;, features a modification of the amino acid from G to R at position 57.
+The protein's natural variant, known as in G-ferrara; unstable;, features a modification of the amino acid from N to K at position 58.
+The protein's natural variant, known as in Dhofar/Yukuhashi;, features a modification of the amino acid from P to R at position 59.
+The protein's natural variant, known as in I-High Wycombe;, features a modification of the amino acid from K to E at position 60.
+The protein's natural variant, known as in Collingwood; unstable;, features a modification of the amino acid from V to A at position 61.
+The protein's natural variant, known as in N-Seatlle;, features a modification of the amino acid from K to E at position 62.
+The protein's natural variant, known as in Bologna; O(2) affinity down;, features a modification of the amino acid from K to M at position 62.
+The protein's natural variant, known as in Hikari;, features a modification of the amino acid from K to N at position 62.
+The protein's natural variant, known as in J-Europa;, features a modification of the amino acid from A to D at position 63.
+The protein's natural variant, known as in Duarte; unstable;, features a modification of the amino acid from A to P at position 63.
+The protein's natural variant, known as in M-Saskatoon; O(2) affinity up;, features a modification of the amino acid from H to Y at position 64.
+The protein's natural variant, known as in J-Antakya;, features a modification of the amino acid from K to M at position 66.
+The protein's natural variant, known as in J-Sicilia;, features a modification of the amino acid from K to N at position 66.
+The protein's natural variant, known as in J-Cairo;, features a modification of the amino acid from K to Q at position 66.
+The protein's natural variant, known as in Vigo; O(2) affinity down, features a modification of the amino acid from K to I at position 67.
+The protein's natural variant, known as in Chico; O(2) affinity down;, features a modification of the amino acid from K to T at position 67.
+The protein's natural variant, known as in Sydney; unstable;, features a modification of the amino acid from V to A at position 68.
+The protein's natural variant, known as in Bristol, features a modification of the amino acid from V to D at position 68.
+The protein's natural variant, known as in non-spherocytic haemolytic anemia; Manukau;, features a modification of the amino acid from V to G at position 68.
+The protein's natural variant, known as in Alesha; unstable;, features a modification of the amino acid from V to M at position 68.
+The protein's natural variant, known as in Brisbane; O(2) affinity up;, features a modification of the amino acid from L to H at position 69.
+The protein's natural variant, known as in Mizuho; unstable;, features a modification of the amino acid from L to P at position 69.
+The protein's natural variant, known as in Rambam;, features a modification of the amino acid from G to D at position 70.
+The protein's natural variant, known as in Kenitra;, features a modification of the amino acid from G to R at position 70.
+The protein's natural variant, known as in City of Hope;, features a modification of the amino acid from G to S at position 70.
+The protein's natural variant, known as in Seattle; O(2) affinity down; unstable;, features a modification of the amino acid from A to D at position 71.
+The protein's natural variant, known as in Christchurch; unstable;, features a modification of the amino acid from F to S at position 72.
+The protein's natural variant, known as in Tilburg; O(2) affinity down;, features a modification of the amino acid from D to G at position 74.
+The protein's natural variant, known as in Mobile; O(2) affinity down;, features a modification of the amino acid from D to V at position 74.
+The protein's natural variant, known as in Vancouver; O(2) affinity down;, features a modification of the amino acid from D to Y at position 74.
+The protein's natural variant, known as in Aalborg; unstable;, features a modification of the amino acid from G to R at position 75.
+The protein's natural variant, known as in Bushwick; unstable;, features a modification of the amino acid from G to V at position 75.
+The protein's natural variant, known as in Atlanta; unstable;, features a modification of the amino acid from L to P at position 76.
+The protein's natural variant, known as in Pasadena; O(2) affinity up; unstable;, features a modification of the amino acid from L to R at position 76.
+The protein's natural variant, known as in J-Chicago;, features a modification of the amino acid from A to D at position 77.
+The protein's natural variant, known as in J-Iran;, features a modification of the amino acid from H to D at position 78.
+The protein's natural variant, known as in Costa Rica;, features a modification of the amino acid from H to R at position 78.
+The protein's natural variant, known as in Fukuyama;, features a modification of the amino acid from H to Y at position 78.
+The protein's natural variant, known as in Quin-hai;, features a modification of the amino acid from L to R at position 79.
+The protein's natural variant, known as in Tampa;, features a modification of the amino acid from D to Y at position 80.
+The protein's natural variant, known as in G-Szuhu/Gifu;, features a modification of the amino acid from N to K at position 81.
+The protein's natural variant, known as in La Roche-sur-Yon; unstable and O(2) affinity up;, features a modification of the amino acid from L to H at position 82.
+The protein's natural variant, known as in Baylor; unstable;, features a modification of the amino acid from L to R at position 82.
+The protein's natural variant, known as in Helsinki; O(2) affinity up;, features a modification of the amino acid from K to M at position 83.
+The protein's natural variant, known as in Providence;, features a modification of the amino acid from K to N at position 83.
+The protein's natural variant, known as in Pyrgos;, features a modification of the amino acid from G to D at position 84.
+The protein's natural variant, known as in Muskegon;, features a modification of the amino acid from G to R at position 84.
+The protein's natural variant, known as in Kofu;, features a modification of the amino acid from T to I at position 85.
+The protein's natural variant, known as in Olomouc; O(2) affinity up;, features a modification of the amino acid from A to D at position 87.
+The protein's natural variant, known as in Quebec-Chori;, features a modification of the amino acid from T to I at position 88.
+The protein's natural variant, known as in D-Ibadan;, features a modification of the amino acid from T to K at position 88.
+The protein's natural variant, known as in Valletta;, features a modification of the amino acid from T to P at position 88.
+The protein's natural variant, known as in Santa Ana; unstable;, features a modification of the amino acid from L to P at position 89.
+The protein's natural variant, known as in Boras; unstable;, features a modification of the amino acid from L to R at position 89.
+The protein's natural variant, known as in Creteil; O(2) affinity up;, features a modification of the amino acid from S to N at position 90.
+The protein's natural variant, known as in Vanderbilt; O(2) affinity up;, features a modification of the amino acid from S to R at position 90.
+The protein's natural variant, known as in Pierre-Benite; O(2) affinity up;, features a modification of the amino acid from E to D at position 91.
+The protein's natural variant, known as in Agenogi; O(2) affinity down;, features a modification of the amino acid from E to K at position 91.
+The protein's natural variant, known as in Sabine; unstable;, features a modification of the amino acid from L to P at position 92.
+The protein's natural variant, known as in Caribbean; O(2) affinity down; unstable;, features a modification of the amino acid from L to R at position 92.
+The protein's natural variant, known as in J-Altgelds Gardens; unstable;, features a modification of the amino acid from H to D at position 93.
+The protein's natural variant, known as in Isehara; unstable;, features a modification of the amino acid from H to N at position 93.
+The protein's natural variant, known as in Newcastle and Duino; associated with S-104 in Duino; unstable;, features a modification of the amino acid from H to P at position 93.
+The protein's natural variant, known as in Istambul; unstable;, features a modification of the amino acid from H to Q at position 93.
+The protein's natural variant, known as in Okazaki; O(2) affinity up; unstable;, features a modification of the amino acid from C to R at position 94.
+The protein's natural variant, known as in Chandigarh;, features a modification of the amino acid from D to G at position 95.
+The protein's natural variant, known as in Barcelona; O(2) affinity up;, features a modification of the amino acid from D to H at position 95.
+The protein's natural variant, known as in Bunbury; O(2) affinity up;, features a modification of the amino acid from D to N at position 95.
+The protein's natural variant, known as in J-Cordoba;, features a modification of the amino acid from K to M at position 96.
+The protein's natural variant, known as in Detroit;, features a modification of the amino acid from K to N at position 96.
+The protein's natural variant, known as in Debrousse; unstable; O(2) affinity up;, features a modification of the amino acid from L to P at position 97.
+The protein's natural variant, known as in Regina; O(2) affinity up;, features a modification of the amino acid from L to V at position 97.
+The protein's natural variant, known as in Wood; O(2) affinity up;, features a modification of the amino acid from H to L at position 98.
+The protein's natural variant, known as in Nagoya; O(2) affinity up; unstable;, features a modification of the amino acid from H to P at position 98.
+The protein's natural variant, known as in Malmoe; O(2) affinity up;, features a modification of the amino acid from H to Q at position 98.
+The protein's natural variant, known as in Moriguchi;, features a modification of the amino acid from H to Y at position 98.
+The protein's natural variant, known as in Nottingham; unstable;, features a modification of the amino acid from V to G at position 99.
+The protein's natural variant, known as in Coimbra; O(2) affinity up;, features a modification of the amino acid from D to E at position 100.
+The protein's natural variant, known as in Brigham; O(2) affinity up;, features a modification of the amino acid from P to L at position 101.
+The protein's natural variant, known as in New Mexico;, features a modification of the amino acid from P to R at position 101.
+The protein's natural variant, known as in Potomac; O(2) affinity up;, features a modification of the amino acid from E to D at position 102.
+The protein's natural variant, known as in Alberta; O(2) affinity up;, features a modification of the amino acid from E to G at position 102.
+The protein's natural variant, known as in British Columbia; O(2) affinity up;, features a modification of the amino acid from E to K at position 102.
+The protein's natural variant, known as in Rush; unstable;, features a modification of the amino acid from E to Q at position 102.
+The protein's natural variant, known as in Beth Israel; O(2) affinity down; unstable;, features a modification of the amino acid from N to S at position 103.
+The protein's natural variant, known as in St Mande; O(2) affinity down;, features a modification of the amino acid from N to Y at position 103.
+The protein's natural variant, known as in Heathrow; O(2) affinity up;, features a modification of the amino acid from F to L at position 104.
+The protein's natural variant, known as in Camperdown and Duino; associated with P-92 in Duino; unstable;, features a modification of the amino acid from R to S at position 105.
+The protein's natural variant, known as in Sherwood Forest;, features a modification of the amino acid from R to T at position 105.
+The protein's natural variant, known as in Burke; O(2) affinity down; unstable;, features a modification of the amino acid from G to R at position 108.
+The protein's natural variant, known as in Presbyterian; O(2) affinity down; unstable;, features a modification of the amino acid from N to K at position 109.
+The protein's natural variant, known as in San Diego; O(2) affinity up;, features a modification of the amino acid from V to M at position 110.
+The protein's natural variant, known as in Showa-Yakushiji;, features a modification of the amino acid from L to P at position 111.
+The protein's natural variant, known as in Stanmore; O(2) affinity down; unstable;, features a modification of the amino acid from V to A at position 112.
+The protein's natural variant, known as in Canterbury;, features a modification of the amino acid from C to F at position 113.
+The protein's natural variant, known as in Indianapolis;, features a modification of the amino acid from C to R at position 113.
+The protein's natural variant, known as in Yahata;, features a modification of the amino acid from C to Y at position 113.
+The protein's natural variant, known as in Zengcheng;, features a modification of the amino acid from L to M at position 115.
+The protein's natural variant, known as in B-THAL; Durham-N.C./Brescia;, features a modification of the amino acid from L to P at position 115.
+The protein's natural variant, known as in B-THAL; Hradec Kralove; unstable;, features a modification of the amino acid from A to D at position 116.
+The protein's natural variant, known as in Madrid; unstable;, features a modification of the amino acid from A to P at position 116.
+The protein's natural variant, known as in Vexin; increased oxygen affinity;, features a modification of the amino acid from H to L at position 117.
+The protein's natural variant, known as in Hafnia;, features a modification of the amino acid from H to Q at position 117.
+The protein's natural variant, known as in Saitama; unstable;, features a modification of the amino acid from H to P at position 118.
+The protein's natural variant, known as in P-Galveston;, features a modification of the amino acid from H to R at position 118.
+The protein's natural variant, known as in Tsukumi;, features a modification of the amino acid from H to Y at position 118.
+The protein's natural variant, known as in Iowa;, features a modification of the amino acid from G to A at position 120.
+The protein's natural variant, known as in Hijiyama;, features a modification of the amino acid from K to E at position 121.
+The protein's natural variant, known as in Jianghua;, features a modification of the amino acid from K to I at position 121.
+The protein's natural variant, known as in Takamatsu;, features a modification of the amino acid from K to Q at position 121.
+The protein's natural variant, known as in D-Neath;, features a modification of the amino acid from E to A at position 122.
+The protein's natural variant, known as in St Francis;, features a modification of the amino acid from E to G at position 122.
+The protein's natural variant, known as in O-Arab;, features a modification of the amino acid from E to K at position 122.
+The protein's natural variant, known as in D-Los Angeles/D-Punjab/D-Portugal/D-Chicago/D-Oak Ridge;, features a modification of the amino acid from E to Q at position 122.
+The protein's natural variant, known as in D-Camperdown/Beograd;, features a modification of the amino acid from E to V at position 122.
+The protein's natural variant, known as in Villejuif; asymptomatic variant;, features a modification of the amino acid from T to I at position 124.
+The protein's natural variant, known as in Ty Gard; O(2) affinity up;, features a modification of the amino acid from P to Q at position 125.
+The protein's natural variant, known as in Khartoum; unstable;, features a modification of the amino acid from P to R at position 125.
+The protein's natural variant, known as in Tunis;, features a modification of the amino acid from P to S at position 125.
+The protein's natural variant, known as in Beirut;, features a modification of the amino acid from V to A at position 127.
+The protein's natural variant, known as in Hofu; unstable;, features a modification of the amino acid from V to E at position 127.
+The protein's natural variant, known as in B-THAL; Dhonburi/Neapolis; unstable;, features a modification of the amino acid from V to G at position 127.
+The protein's natural variant, known as in Complutense;, features a modification of the amino acid from Q to E at position 128.
+The protein's natural variant, known as in Brest; unstable;, features a modification of the amino acid from Q to K at position 128.
+The protein's natural variant, known as in J-Guantanamo; unstable;, features a modification of the amino acid from A to D at position 129.
+The protein's natural variant, known as in Crete; O(2) affinity up; unstable;, features a modification of the amino acid from A to P at position 130.
+The protein's natural variant, known as in La Desirade; O(2) affinity down; unstable;, features a modification of the amino acid from A to V at position 130.
+The protein's natural variant, known as in Wien; unstable;, features a modification of the amino acid from Y to D at position 131.
+The protein's natural variant, known as in Nevers;, features a modification of the amino acid from Y to S at position 131.
+The protein's natural variant, known as in Camden/Tokuchi/Motown;, features a modification of the amino acid from Q to E at position 132.
+The protein's natural variant, known as in Shelby/Leslie/Deaconess; unstable;, features a modification of the amino acid from Q to K at position 132.
+The protein's natural variant, known as in Shangai; unstable;, features a modification of the amino acid from Q to P at position 132.
+The protein's natural variant, known as in Sarrebourg; unstable;, features a modification of the amino acid from Q to R at position 132.
+The protein's natural variant, known as in Yamagata; O(2) affinity down;, features a modification of the amino acid from K to N at position 133.
+The protein's natural variant, known as in K-Woolwich;, features a modification of the amino acid from K to Q at position 133.
+The protein's natural variant, known as in Extredemura;, features a modification of the amino acid from V to L at position 134.
+The protein's natural variant, known as in North Shore-Caracas; unstable;, features a modification of the amino acid from V to E at position 135.
+The protein's natural variant, known as in Beckman; originally reported as E-136; O(2) affinity down; unstable;, features a modification of the amino acid from A to D at position 136.
+The protein's natural variant, known as in Altdorf; O(2) affinity up; unstable;, features a modification of the amino acid from A to P at position 136.
+The protein's natural variant, known as in Hope; O(2) affinity down; unstable;, features a modification of the amino acid from G to D at position 137.
+The protein's natural variant, known as in Brockton; unstable;, features a modification of the amino acid from A to P at position 139.
+The protein's natural variant, known as in Geelong; unstable;, features a modification of the amino acid from N to D at position 140.
+The protein's natural variant, known as in Hinsdale; O(2) affinity down;, features a modification of the amino acid from N to K at position 140.
+The protein's natural variant, known as in S-Wake; associated with V-6, features a modification of the amino acid from N to S at position 140.
+The protein's natural variant, known as in Aurora; O(2) affinity up;, features a modification of the amino acid from N to Y at position 140.
+The protein's natural variant, known as in Himeji; unstable; O(2) affinity down;, features a modification of the amino acid from A to D at position 141.
+The protein's natural variant, known as in St Jacques; O(2) affinity up;, features a modification of the amino acid from A to T at position 141.
+The protein's natural variant, known as in Puttelange; polycythemia; O(2) affinity up;, features a modification of the amino acid from A to V at position 141.
+The protein's natural variant, known as in Olmsted; unstable;, features a modification of the amino acid from L to R at position 142.
+The protein's natural variant, known as in Ohio; O(2) affinity up;, features a modification of the amino acid from A to D at position 143.
+The protein's natural variant, known as in Rancho Mirage;, features a modification of the amino acid from H to D at position 144.
+The protein's natural variant, known as in Syracuse; O(2) affinity up;, features a modification of the amino acid from H to P at position 144.
+The protein's natural variant, known as in Little Rock; O(2) affinity up;, features a modification of the amino acid from H to Q at position 144.
+The protein's natural variant, known as in Abruzzo; O(2) affinity up;, features a modification of the amino acid from H to R at position 144.
+The protein's natural variant, known as in Mito; O(2) affinity up;, features a modification of the amino acid from K to E at position 145.
+The protein's natural variant, known as in Rainier; O(2) affinity up;, features a modification of the amino acid from Y to C at position 146.
+The protein's natural variant, known as in Bethesda; O(2) affinity up;, features a modification of the amino acid from Y to H at position 146.
+The protein's natural variant, known as in Hiroshima; O(2) affinity up;, features a modification of the amino acid from H to D at position 147.
+The protein's natural variant, known as in Cowtown; O(2) affinity up;, features a modification of the amino acid from H to L at position 147.
+The protein's natural variant, known as in York; O(2) affinity up;, features a modification of the amino acid from H to P at position 147.
+The protein's natural variant, known as in Kodaira; O(2) affinity up;, features a modification of the amino acid from H to Q at position 147.
+The protein's natural variant, known as might contribute to non-insulin dependent diabetes mellitus susceptibility in some populations;, features a modification of the amino acid from A to T at position 4.
+The protein's natural variant, known as in a patient with hypertrophic cardiomyopathy and profound hearing loss;, features a modification of the amino acid from Y to C at position 30.
+The protein's natural variant, known as in LHON; secondary mutation; unknown pathological significance;, features a modification of the amino acid from Y to H at position 30.
+The protein's natural variant, known as in MELAS;, features a modification of the amino acid from M to T at position 31.
+The protein's natural variant, known as in AD-MT; may be associated with disease susceptibility;, features a modification of the amino acid from M to V at position 31.
+The protein's natural variant, known as in LHON; primary mutation; medium severity; some vision recovery; 80% reduction in rotenone-sensitive and ubiquinone-dependent electron transfer activity, whereas the proximal NADH dehydrogenase activity of the complex is unaffected;, features a modification of the amino acid from A to T at position 52.
+The natural variant of this protein is characterized by an amino acid alteration from S to P at position 205.
+The protein's natural variant, known as found in a patient with epileptic encephalopathy evolving to Lennox-Gastaut syndrome; unknown pathological significance;, features a modification of the amino acid from E to K at position 214.
+The natural variant of this protein is characterized by an amino acid alteration from Y to C at position 255.
+The protein's natural variant, known as in LHON; secondary mutation; unknown pathological significance;, features a modification of the amino acid from L to P at position 285.
+The natural variant of this protein is characterized by an amino acid alteration from L to P at position 288.
+The protein's natural variant, known as in LHON; secondary mutation; unknown pathological significance;, features a modification of the amino acid from Y to H at position 304.
+The protein's natural variant, known as in allele B, features a modification of the amino acid from E to G at position 196.
+The natural variant of this protein is characterized by an amino acid alteration from R to G at position 163.
+The protein's natural variant, known as in strain: MS11, features a modification of the amino acid from P to R at position 57.
+The protein's natural variant, known as associated with susceptibility to drug abuse; the mutant enzyme is more sensitive to proteolytic degradation; displays reduced cellular expression probably due to a post-translational mechanism preceding productive folding;, features a modification of the amino acid from P to T at position 129.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from A to D at position 345.
+The protein's natural variant, known as in strain: 97-337, features a modification of the amino acid from F to S at position 131.
+The protein's natural variant, known as in strain: 97-337, features a modification of the amino acid from K to R at position 236.
+The protein's natural variant, known as in strain: Isolate S60, features a modification of the amino acid from L to M at position 306.
+The protein's natural variant, known as in strain: Isolate S60, features a modification of the amino acid from I to T at position 360.
+The natural variant of this protein is characterized by an amino acid alteration from T to M at position 6.
+The protein's natural variant, known as in NPC2;, features a modification of the amino acid from V to M at position 30.
+The protein's natural variant, known as in NPC2; results in the synthesis of functional recombinant proteins correctly targeted to lysosomes;, features a modification of the amino acid from V to M at position 39.
+The protein's natural variant, known as in NPC2; leads to the synthesis of misfolded recombinant proteins that colocalized with an endoplasmic reticulum marker; normally secreted but unable to correct cholesterol storage in NPC2-deficient cells;, features a modification of the amino acid from C to F at position 47.
+The protein's natural variant, known as in NPC2; leads to the synthesis of misfolded recombinant proteins that colocalized with an endoplasmic reticulum marker; normally secreted but unable to correct cholesterol storage in NPC2-deficient cells;, features a modification of the amino acid from S to P at position 67.
+The protein's natural variant, known as in NPC2; leads to the synthesis of misfolded recombinant proteins that colocalized with an endoplasmic reticulum marker; normally secreted but unable to correct cholesterol storage in NPC2-deficient cells;, features a modification of the amino acid from C to F at position 93.
+The protein's natural variant, known as in NPC2; leads to the synthesis of misfolded recombinant proteins that colocalized with an endoplasmic reticulum marker; normally secreted but unable to correct cholesterol storage in NPC2-deficient cells;, features a modification of the amino acid from C to R at position 99.
+The protein's natural variant, known as in NPC2; unable to bind cholesterol;, features a modification of the amino acid from P to S at position 120.
+The protein's natural variant, known as in allele TED7-2/TED7B, features a modification of the amino acid from P to H at position 4.
+The protein's natural variant, known as in allele TED7-2/TED7B, features a modification of the amino acid from V to L at position 9.
+The protein's natural variant, known as in allele TED7-2/TED7B, features a modification of the amino acid from SPPHPVSPPP to LPPHSVPPPS at position 73.
+The protein's natural variant, known as in allele TED7-2/TED7B, features a modification of the amino acid from F to S at position 102.
+The protein's natural variant, known as in allele TED7-2/TED7B, features a modification of the amino acid from HFVPPPPNM to PHHVSPPPHT at position 122.
+The protein's natural variant, known as in allele TED7-2/TED7B, features a modification of the amino acid from PHANPPPPPPPHS to HF at position 141.
+The protein's natural variant, known as in allele TED7-2/TED7B, features a modification of the amino acid from HTVPPPPPPPHIIPPPAHALSPPPPH to NTVPPPPAPHFVPPPPPPY at position 172.
+The protein's natural variant, known as in allele TED7-2/TED7B, features a modification of the amino acid from Q to R at position 221.
+The protein's natural variant, known as in allele TED7-2/TED7B, features a modification of the amino acid from LEN to IED at position 269.
+The protein's natural variant, known as in lah, features a modification of the amino acid from E to V at position 228.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from D to E at position 385.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from P to L at position 400.
+The protein's natural variant, known as in PCH1F; decreased protein abundance, features a modification of the amino acid from S to L at position 35.
+The protein's natural variant, known as in a lung small cell carcinoma sample; somatic mutation, features a modification of the amino acid from G to V at position 234.
+The protein's natural variant, known as in a lung small cell carcinoma sample; somatic mutation, features a modification of the amino acid from K to N at position 347.
+The protein's natural variant, known as in a lung small cell carcinoma sample; somatic mutation;, features a modification of the amino acid from R to Q at position 379.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation, features a modification of the amino acid from W to C at position 389.
+The protein's natural variant, known as in a lung large cell carcinoma sample; somatic mutation;, features a modification of the amino acid from T to M at position 590.
+The protein's natural variant, known as in a lung squamous cell carcinoma sample; somatic mutation, features a modification of the amino acid from A to G at position 835.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation, features a modification of the amino acid from R to L at position 1095.
+The protein's natural variant, known as in a lung small cell carcinoma sample; somatic mutation;, features a modification of the amino acid from R to Q at position 1195.
+The protein's natural variant, known as in a lung large cell carcinoma sample; somatic mutation, features a modification of the amino acid from P to Q at position 1238.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation, features a modification of the amino acid from P to T at position 1238.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation, features a modification of the amino acid from E to K at position 1708.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation, features a modification of the amino acid from E to D at position 1715.
+The protein's natural variant, known as in a lung small cell carcinoma sample; somatic mutation, features a modification of the amino acid from A to E at position 1970.
+The protein's natural variant, known as in a lung small cell carcinoma sample; somatic mutation, features a modification of the amino acid from G to C at position 2295.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from R to H at position 2381.
+The protein's natural variant, known as in a lung large cell carcinoma sample; somatic mutation;, features a modification of the amino acid from D to E at position 2554.
+The protein's natural variant, known as in CLN3;, features a modification of the amino acid from L to P at position 101.
+The protein's natural variant, known as in CLN3;, features a modification of the amino acid from C to R at position 134.
+The protein's natural variant, known as in CLN3; Decreases synthesis of bis(monoacylglycerol)phosphate.;, features a modification of the amino acid from L to P at position 170.
+The protein's natural variant, known as in CLN3;, features a modification of the amino acid from G to A at position 187.
+The protein's natural variant, known as in CLN3;, features a modification of the amino acid from G to R at position 189.
+The protein's natural variant, known as in CLN3; the mutant is located to vesicles clustered in a perinuclear region. Does not affect protein synthesis and maturation. Does not affect lysosomal localization.;, features a modification of the amino acid from E to K at position 295.
+The protein's natural variant, known as in CLN3;, features a modification of the amino acid from V to F at position 330.
+The protein's natural variant, known as in CLN3; Does not affect lysosomal localization. Does not affect lysosomal protein catabolic process. Does not affect lysosomal pH;, features a modification of the amino acid from R to C at position 334.
+The protein's natural variant, known as in CLN3;, features a modification of the amino acid from R to H at position 334.
+The protein's natural variant, known as in VRNI; largely mislocalized to the cytoplasm whereas the wild-type protein is localized near the cell surface;, features a modification of the amino acid from R to L at position 243.
+The protein's natural variant, known as in VRNI; largely mislocalized to the cytoplasm whereas the wild-type protein is localized near the cell surface;, features a modification of the amino acid from L to P at position 244.
+The natural variant of this protein is characterized by an amino acid alteration from G to D at position 81.
+The natural variant of this protein is characterized by an amino acid alteration from G to D at position 83.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 152.
+The natural variant of this protein is characterized by an amino acid alteration from P to A at position 164.
+The natural variant of this protein is characterized by an amino acid alteration from K to I at position 198.
+The natural variant of this protein is characterized by an amino acid alteration from L to W at position 334.
+The protein's natural variant, known as in strain: BALB/c, C3H and ICR, features a modification of the amino acid from QV to KA at position 250.
+The protein's natural variant, known as in tufB; in strain: 2457T, features a modification of the amino acid from G to S at position 394.
+The protein's natural variant, known as in CTRCT6; retained in the cytoplasm and constitutively active it alters EPHA2 signaling;, features a modification of the amino acid from R to Q at position 721.
+The protein's natural variant, known as in a gastric adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from G to S at position 777.
+The protein's natural variant, known as in CTRCT6; reduced protein stability and reduced ability to stimulate cell migration in absence of its ephrin ligand;, features a modification of the amino acid from T to I at position 940.
+The protein's natural variant, known as in CTRCT6; reduced protein stability and reduced ability to stimulate cell migration in absence of its ephrin ligand;, features a modification of the amino acid from G to W at position 948.
+The protein's natural variant, known as unknown pathological significance; found in patients with intellectual disability and microcephaly; impaired interaction with TRMT112, features a modification of the amino acid from G to D at position 61.
+The protein's natural variant, known as found in a family with intellectual disability; unknown pathological significance;, features a modification of the amino acid from S to P at position 57.
+The natural variant of this protein is characterized by an amino acid alteration from V to A at position 54.
+The protein's natural variant, known as in TYRSN1; loss of activity;, features a modification of the amino acid from N to I at position 16.
+The protein's natural variant, known as in TYRSN1; atypical mild phenotype, features a modification of the amino acid from A to T at position 35.
+The protein's natural variant, known as in TYRSN1; loss of activity, features a modification of the amino acid from F to C at position 62.
+The protein's natural variant, known as in TYRSN1;, features a modification of the amino acid from Q to H at position 64.
+The protein's natural variant, known as in TYRSN1; loss of activity;, features a modification of the amino acid from A to D at position 134.
+The protein's natural variant, known as in TYRSN1, features a modification of the amino acid from G to D at position 158.
+The protein's natural variant, known as in TYRSN1;, features a modification of the amino acid from V to G at position 166.
+The protein's natural variant, known as in TYRSN1; loss of activity, features a modification of the amino acid from C to R at position 193.
+The protein's natural variant, known as in TYRSN1;, features a modification of the amino acid from G to D at position 207.
+The protein's natural variant, known as in TYRSN1; loss of activity;, features a modification of the amino acid from D to V at position 233.
+The protein's natural variant, known as in TYRSN1; loss of activity;, features a modification of the amino acid from W to G at position 234.
+The protein's natural variant, known as in TYRSN1, features a modification of the amino acid from P to T at position 249.
+The protein's natural variant, known as in TYRSN1;, features a modification of the amino acid from P to L at position 261.
+The protein's natural variant, known as in TYRSN1; may affect splicing resulting in skipping of exon 8 alone or together with exon 9; lower activity as compared to wild type;, features a modification of the amino acid from Q to R at position 279.
+The protein's natural variant, known as in TYRSN1;, features a modification of the amino acid from T to P at position 294.
+The protein's natural variant, known as in TYRSN1;, features a modification of the amino acid from G to S at position 337.
+The protein's natural variant, known as does not cause a clinically relevant phenotype; results in lower enzyme activity;, features a modification of the amino acid from R to W at position 341.
+The protein's natural variant, known as in TYRSN1; loss of activity;, features a modification of the amino acid from P to L at position 342.
+The protein's natural variant, known as in TYRSN1, features a modification of the amino acid from G to V at position 369.
+The protein's natural variant, known as in TYRSN1; loss of activity;, features a modification of the amino acid from R to G at position 381.
+The protein's natural variant, known as in TYRSN1; requires 2 nucleotide substitutions, features a modification of the amino acid from F to H at position 405.
+The protein's natural variant, known as in strain: TRC11; Ty38c-resistant mutant strain lacking Rv3406, but sensitive to moxifloxacin, features a modification of the amino acid from G to C at position 17.
+The protein's natural variant, known as in a spontaneous TCA1-resistant mutant strain, but sensitive to BTZ, features a modification of the amino acid from Y to C at position 314.
+The protein's natural variant, known as in strain: TRC12; Ty38c-resistant mutant strain lacking Rv3406, but sensitive to moxifloxacin, features a modification of the amino acid from L to P at position 368.
+The protein's natural variant, known as in strain: NTB9; BTZ043-resistant, features a modification of the amino acid from C to G at position 387.
+The protein's natural variant, known as in strain: NTB1; BTZ043-resistant, features a modification of the amino acid from C to S at position 387.
+The protein's natural variant, known as in allele NKG2-E*01 and allele NKG2-E*03; requires 2 nucleotide substitutions;, features a modification of the amino acid from W to P at position 19.
+The protein's natural variant, known as in allele NKG2-E*02;, features a modification of the amino acid from W to R at position 19.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from K to E at position 679.
+The protein's natural variant, known as in AGOTC;, features a modification of the amino acid from F to S at position 113.
+The protein's natural variant, known as found in a patient with non-syndromic ventricular septal defect; unknown pathological significance; loss of function in negative regulation of transcription from E-cadherin promoter;, features a modification of the amino acid from G to S at position 83.
+The protein's natural variant, known as no effect on negative regulation of transcription from E-cadherin promoter;, features a modification of the amino acid from S to G at position 95.
+The protein's natural variant, known as in SWCOS;, features a modification of the amino acid from E to G at position 117.
+The protein's natural variant, known as in SWCOS;, features a modification of the amino acid from E to V at position 117.
+The protein's natural variant, known as in SCS;, features a modification of the amino acid from Q to P at position 119.
+The protein's natural variant, known as in SCS;, features a modification of the amino acid from L to P at position 131.
+The protein's natural variant, known as in SCS, features a modification of the amino acid from I to IAALRKII at position 135.
+The protein's natural variant, known as in SCS, features a modification of the amino acid from P to PKIIPTLP at position 139.
+The protein's natural variant, known as in SCS; variant form with features overlapping Baller-Gerold syndrome;, features a modification of the amino acid from I to V at position 156.
+The protein's natural variant, known as in CRS1;, features a modification of the amino acid from A to T at position 186.
+The protein's natural variant, known as in CRS1;, features a modification of the amino acid from S to L at position 188.
+The natural variant of this protein is characterized by an amino acid alteration from K to R at position 132.
+The natural variant of this protein is characterized by an amino acid alteration from G to A at position 154.
+The protein's natural variant, known as in allele UGT1A8*2;, features a modification of the amino acid from A to G at position 173.
+The natural variant of this protein is characterized by an amino acid alteration from T to A at position 202.
+The protein's natural variant, known as in allele UGT1A8*3; dramatic reduction in catalytic activity;, features a modification of the amino acid from C to Y at position 277.
+The protein's natural variant, known as in ACL1.C2, features a modification of the amino acid from A to V at position 17.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation, features a modification of the amino acid from S to F at position 253.
+The protein's natural variant, known as associated with susceptibility to mastitis, features a modification of the amino acid from G to GG at position 116.
+The protein's natural variant, known as in spd, features a modification of the amino acid from A to S at position 80.
+The protein's natural variant, known as in SGYMR;, features a modification of the amino acid from M to V at position 617.
+The protein's natural variant, known as in strain: CEN.PK 113-7D, features a modification of the amino acid from V to I at position 48.
+The protein's natural variant, known as in strain: CEN.PK 113-7D, features a modification of the amino acid from L to S at position 59.
+The protein's natural variant, known as in strain: CEN.PK 113-7D, features a modification of the amino acid from I to N at position 69.
+The protein's natural variant, known as in rec30; DNA-repair deficient, features a modification of the amino acid from G to S at position 224.
+The protein's natural variant, known as in allele CYP2F1*4;, features a modification of the amino acid from S to P at position 38.
+The protein's natural variant, known as in allele CYP2F1*6;, features a modification of the amino acid from R to P at position 98.
+The protein's natural variant, known as in allele CYP2F1*3 and in allele CYP2F1*4;, features a modification of the amino acid from D to N at position 218.
+The protein's natural variant, known as in allele CYP2F1*3;, features a modification of the amino acid from Q to H at position 266.
+The protein's natural variant, known as in allele CYP2F1*5A and in allele CYP2F1*5B;, features a modification of the amino acid from L to P at position 391.
+The protein's natural variant, known as in allele CYP2F1*3;, features a modification of the amino acid from P to L at position 490.
+The protein's natural variant, known as in HLD1;, features a modification of the amino acid from P to L at position 15.
+The protein's natural variant, known as in SPG2; partially retained in the endoplasmic reticulum; does not induce unfolded protein response, features a modification of the amino acid from A to P at position 30.
+The protein's natural variant, known as in HLD1, features a modification of the amino acid from L to P at position 31.
+The protein's natural variant, known as in HLD1, features a modification of the amino acid from F to L at position 32.
+The protein's natural variant, known as in HLD1, features a modification of the amino acid from F to V at position 32.
+The protein's natural variant, known as in HLD1;, features a modification of the amino acid from C to Y at position 33.
+The protein's natural variant, known as in HLD1, features a modification of the amino acid from C to R at position 35.
+The protein's natural variant, known as in HLD1, features a modification of the amino acid from C to Y at position 35.
+The protein's natural variant, known as in HLD1, features a modification of the amino acid from A to T at position 39.
+The protein's natural variant, known as in HLD1;, features a modification of the amino acid from T to I at position 43.
+The protein's natural variant, known as in HLD1, features a modification of the amino acid from L to P at position 46.
+The protein's natural variant, known as in HLD1, features a modification of the amino acid from L to R at position 46.
+The protein's natural variant, known as in HLD1, features a modification of the amino acid from Y to C at position 50.
+The protein's natural variant, known as in HLD1, features a modification of the amino acid from F to S at position 51.
+The protein's natural variant, known as in HLD1, features a modification of the amino acid from Y to C at position 60.
+The protein's natural variant, known as in HLD1;, features a modification of the amino acid from G to R at position 74.
+The protein's natural variant, known as in HLD1, features a modification of the amino acid from A to P at position 76.
+The protein's natural variant, known as in HLD1, features a modification of the amino acid from T to K at position 116.
+The protein's natural variant, known as in SPG2;, features a modification of the amino acid from H to Y at position 130.
+The protein's natural variant, known as in SPG2;, features a modification of the amino acid from R to W at position 137.
+The protein's natural variant, known as in SPG2;, features a modification of the amino acid from H to Y at position 140.
+The protein's natural variant, known as in HLD1 and SPG2, features a modification of the amino acid from H to Y at position 148.
+The protein's natural variant, known as in HLD1, features a modification of the amino acid from K to N at position 151.
+The protein's natural variant, known as in HLD1;, features a modification of the amino acid from T to I at position 156.
+The protein's natural variant, known as in HLD1, features a modification of the amino acid from V to E at position 162.
+The protein's natural variant, known as in HLD1;, features a modification of the amino acid from W to R at position 163.
+The protein's natural variant, known as in HLD1, features a modification of the amino acid from V to E at position 166.
+The protein's natural variant, known as probable disease-associated variant found in Pelizaeus-Merzbacher disease/X-linked spastic paraplegia, features a modification of the amino acid from V to G at position 166.
+The protein's natural variant, known as in HLD1, features a modification of the amino acid from C to R at position 169.
+The protein's natural variant, known as in SPG2;, features a modification of the amino acid from S to F at position 170.
+The protein's natural variant, known as in HLD1, features a modification of the amino acid from S to P at position 170.
+The protein's natural variant, known as in HLD1, features a modification of the amino acid from V to A at position 172.
+The protein's natural variant, known as in HLD1, features a modification of the amino acid from P to S at position 173.
+The protein's natural variant, known as in HLD1, features a modification of the amino acid from Y to C at position 175.
+The protein's natural variant, known as in HLD1, features a modification of the amino acid from W to C at position 181.
+The protein's natural variant, known as in HLD1;, features a modification of the amino acid from T to P at position 182.
+The protein's natural variant, known as in HLD1, features a modification of the amino acid from T to N at position 183.
+The protein's natural variant, known as in SPG2;, features a modification of the amino acid from I to T at position 187.
+The protein's natural variant, known as in HLD1, features a modification of the amino acid from D to E at position 203.
+The protein's natural variant, known as in HLD1, features a modification of the amino acid from D to G at position 203.
+The protein's natural variant, known as in HLD1;, features a modification of the amino acid from D to H at position 203.
+The protein's natural variant, known as in HLD1;, features a modification of the amino acid from D to N at position 203.
+The protein's natural variant, known as in HLD1, features a modification of the amino acid from D to V at position 203.
+The protein's natural variant, known as in HLD1, features a modification of the amino acid from R to G at position 205.
+The protein's natural variant, known as in HLD1, features a modification of the amino acid from Y to C at position 207.
+The protein's natural variant, known as in HLD1, features a modification of the amino acid from V to D at position 209.
+The protein's natural variant, known as in HLD1, features a modification of the amino acid from L to H at position 210.
+The protein's natural variant, known as in HLD1, features a modification of the amino acid from P to L at position 211.
+The protein's natural variant, known as in HLD1, features a modification of the amino acid from W to R at position 212.
+The protein's natural variant, known as in HLD1, features a modification of the amino acid from P to A at position 216.
+The protein's natural variant, known as in SPG2, features a modification of the amino acid from P to L at position 216.
+The protein's natural variant, known as in HLD1;, features a modification of the amino acid from P to S at position 216.
+The protein's natural variant, known as in HLD1, features a modification of the amino acid from G to S at position 217.
+The protein's natural variant, known as in HLD1;, features a modification of the amino acid from V to F at position 219.
+The protein's natural variant, known as in HLD1, features a modification of the amino acid from C to Y at position 220.
+The protein's natural variant, known as in HLD1;, features a modification of the amino acid from G to C at position 221.
+The protein's natural variant, known as probable disease-associated variant found in Pelizaeus-Merzbacher disease/X-linked spastic paraplegia, features a modification of the amino acid from L to I at position 224.
+The protein's natural variant, known as in HLD1;, features a modification of the amino acid from L to P at position 224.
+The protein's natural variant, known as in HLD1, features a modification of the amino acid from L to P at position 225.
+The protein's natural variant, known as in SPG2, features a modification of the amino acid from S to P at position 226.
+The protein's natural variant, known as in HLD1;, features a modification of the amino acid from C to Y at position 228.
+The protein's natural variant, known as in HLD1, features a modification of the amino acid from Q to P at position 234.
+The protein's natural variant, known as in SPG2;, features a modification of the amino acid from F to S at position 237.
+The protein's natural variant, known as in HLD1, features a modification of the amino acid from L to P at position 239.
+The protein's natural variant, known as in HLD1, features a modification of the amino acid from A to P at position 242.
+The protein's natural variant, known as in HLD1, features a modification of the amino acid from A to E at position 243.
+The protein's natural variant, known as in HLD1, features a modification of the amino acid from A to V at position 243.
+The protein's natural variant, known as in HLD1;, features a modification of the amino acid from G to A at position 246.
+The protein's natural variant, known as in HLD1, features a modification of the amino acid from G to E at position 246.
+The protein's natural variant, known as in HLD1;, features a modification of the amino acid from A to T at position 247.
+The protein's natural variant, known as in HLD1, features a modification of the amino acid from A to E at position 248.
+The protein's natural variant, known as in HLD1, features a modification of the amino acid from A to P at position 249.
+The protein's natural variant, known as in HLD1, features a modification of the amino acid from S to F at position 253.
+The natural variant of this protein is characterized by an amino acid alteration from Y to H at position 169.
+The protein's natural variant, known as in CPVT3; unknown pathological significance;, features a modification of the amino acid from R to Q at position 196.
+The protein's natural variant, known as unknown pathological significance;, features a modification of the amino acid from R to W at position 289.
+The protein's natural variant, known as in ARWH1;, features a modification of the amino acid from D to V at position 63.
+The protein's natural variant, known as in ARWH1;, features a modification of the amino acid from I to F at position 188.
+The protein's natural variant, known as in ARWH1;, features a modification of the amino acid from E to K at position 189.
+The protein's natural variant, known as in strain: cv. Bla-6, cv. Et-0, cv. Li-5:3, cv. Mt-0, cv. Pa-2 and cv. Tsu-1, features a modification of the amino acid from H to D at position 231.
+The protein's natural variant, known as in NGPS; shows a dramatic reduction in BANF1 protein levels indicating that the mutation impairs protein stability;, features a modification of the amino acid from A to T at position 12.
+The protein's natural variant, known as in allotype C6 A;, features a modification of the amino acid from A to E at position 119.
+The protein's natural variant, known as in IMGT allele IGHV3-20*02, features a modification of the amino acid from C to F at position 41.
+The protein's natural variant, known as in CDCBM2; the mutation results in a significant decrease of excitatory post-synaptic currents when expressed in cultured primary hippocampal neurons; decreased localization to distal regions of dendrites; accumulates in dendrite cell body;, features a modification of the amino acid from E to K at position 237.
+The protein's natural variant, known as in CDCBM2; the mutant protein has a complete loss of ATP hydrolysis activity; colocalizes with microtubules throughout the cell but does not appear as puncta or accumulates in cortical clusters as does the wild-type protein;, features a modification of the amino acid from E to V at position 237.
+The protein's natural variant, known as in MRT2;, features a modification of the amino acid from C to R at position 391.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to W at position 62.
+The protein's natural variant, known as in CDCBM5; abolishes coassembly with tubulin subunits and incorporation into the microtubule polymer network;, features a modification of the amino acid from N to K at position 247.
+The protein's natural variant, known as in CDCBM5; reduces coassembly with tubulin subunits and incorporation into the microtubule polymer network;, features a modification of the amino acid from A to V at position 248.
+The protein's natural variant, known as in strain: 3CPA86, features a modification of the amino acid from D to E at position 43.
+The protein's natural variant, known as in strain: FrV3-1, features a modification of the amino acid from P to S at position 60.
+The protein's natural variant, known as in Z(S)29, features a modification of the amino acid from A to P at position 67.
+The protein's natural variant, known as in Z(S)2, features a modification of the amino acid from I to T at position 71.
+The protein's natural variant, known as in strain: IS2, IS3, IS4, IS5, IS25 and QD18, features a modification of the amino acid from K to N at position 187.
+The protein's natural variant, known as in strain: ZZ30, features a modification of the amino acid from F to L at position 195.
+The protein's natural variant, known as in strain: Z(H)1, features a modification of the amino acid from E to D at position 241.
+The protein's natural variant, known as in strain: Z(H)1, features a modification of the amino acid from E to D at position 350.
+The protein's natural variant, known as in strain: Z(H)1, features a modification of the amino acid from S to A at position 430.
+The protein's natural variant, known as in strain: IS4 and IS5, features a modification of the amino acid from S to P at position 437.
+The protein's natural variant, known as in strain: B28, features a modification of the amino acid from M to I at position 516.
+The protein's natural variant, known as in strain: B28, features a modification of the amino acid from A to V at position 524.
+The protein's natural variant, known as in strain: Z(S)24 and Z(S)49, features a modification of the amino acid from V to I at position 544.
+The protein's natural variant, known as in strain: 3CPA126, features a modification of the amino acid from K to T at position 606.
+The protein's natural variant, known as in strain: Z(S)30A, features a modification of the amino acid from M to V at position 607.
+The protein's natural variant, known as in some hepatocellular carcinoma, features a modification of the amino acid from N to S at position 260.
+The protein's natural variant, known as found in a patient with familial intrahepatic cholestasis; unknown pathological significance, features a modification of the amino acid from E to G at position 235.
+The protein's natural variant, known as in RP14;, features a modification of the amino acid from A to V at position 245.
+The protein's natural variant, known as in RP14, features a modification of the amino acid from K to T at position 261.
+The protein's natural variant, known as in LCA15;, features a modification of the amino acid from G to W at position 368.
+The protein's natural variant, known as in RP14;, features a modification of the amino acid from R to H at position 378.
+The protein's natural variant, known as in RP14;, features a modification of the amino acid from F to S at position 382.
+The protein's natural variant, known as in LCA15;, features a modification of the amino acid from R to W at position 400.
+The protein's natural variant, known as in RP14; no effect on RPE phagocytosis;, features a modification of the amino acid from R to P at position 420.
+The protein's natural variant, known as in RP14;, features a modification of the amino acid from T to M at position 454.
+The protein's natural variant, known as in RP14; no effect on RPE phagocytosis;, features a modification of the amino acid from I to K at position 459.
+The protein's natural variant, known as in RP14;, features a modification of the amino acid from R to W at position 482.
+The protein's natural variant, known as in RP14; abolishes RPE phagocytosis;, features a modification of the amino acid from K to R at position 489.
+The protein's natural variant, known as in RP14; abolishes RPE phagocytosis;, features a modification of the amino acid from F to L at position 491.
+The protein's natural variant, known as in RP14; unknown pathological significance;, features a modification of the amino acid from A to T at position 496.
+The protein's natural variant, known as in LCA15, features a modification of the amino acid from A to AFA at position 529.
+The natural variant of this protein is characterized by an amino acid alteration from L to V at position 33.
+The natural variant of this protein is characterized by an amino acid alteration from N to D at position 43.
+The natural variant of this protein is characterized by an amino acid alteration from S to A at position 48.
+The natural variant of this protein is characterized by an amino acid alteration from D to E at position 71.
+The protein's natural variant, known as in SESAMES; no effect on localization to the basolateral membrane in kidney cells;, features a modification of the amino acid from R to P at position 65.
+The protein's natural variant, known as in SESAMES, features a modification of the amino acid from L to P at position 68.
+The protein's natural variant, known as in SESAMES; important loss of localization to the basolateral membrane in kidney cells; in non-tubular cells, does not form functional channels;, features a modification of the amino acid from G to R at position 77.
+The protein's natural variant, known as in SESAMES;, features a modification of the amino acid from I to V at position 129.
+The protein's natural variant, known as in SESAMES; loss of localization to the basolateral membrane in kidney cells; in non-tubular cells, does not form functional channels;, features a modification of the amino acid from C to R at position 140.
+The protein's natural variant, known as in SESAMES; no effect on localization to the basolateral membrane in kidney cells;, features a modification of the amino acid from T to I at position 164.
+The protein's natural variant, known as in SESAMES; loss of localization to the basolateral membrane in kidney cells; in non-tubular cells, forms functional channels; important loss of MAGI1-binding when transfected in tubular MDCKII cells, but not in non-tubular HEK293T cells;, features a modification of the amino acid from A to V at position 167.
+The protein's natural variant, known as in SESAMES; no effect on localization to the basolateral membrane in kidney cells;, features a modification of the amino acid from R to C at position 297.
+The protein's natural variant, known as found in a colon cancer sample; somatic mutation, features a modification of the amino acid from K to T at position 14.
+The protein's natural variant, known as found in a multiple myeloma sample; somatic mutation;, features a modification of the amino acid from R to C at position 21.
+The protein's natural variant, known as in GASC; somatic mutation; impairs CASP10-mediated apoptosis;, features a modification of the amino acid from M to T at position 147.
+The protein's natural variant, known as in ALPS2A;, features a modification of the amino acid from L to F at position 285.
+The protein's natural variant, known as found in a T-acute lymphoblastic leukemia sample; somatic mutation, features a modification of the amino acid from L to P at position 285.
+The protein's natural variant, known as the mutant protein has defective apoptosis and exerts a dominant-negative effect when cotransfected with the wild-type protein;, features a modification of the amino acid from I to L at position 406.
+The protein's natural variant, known as does not interfere with apoptosis in a dominant negative manner;, features a modification of the amino acid from V to I at position 410.
+The protein's natural variant, known as in NHL; somatic mutation;, features a modification of the amino acid from A to V at position 414.
+The protein's natural variant, known as associated with ALPS2A; does not interfere with apoptosis in a dominant negative manner;, features a modification of the amino acid from Y to C at position 446.
+The protein's natural variant, known as in strain: FVB/N, features a modification of the amino acid from G to S at position 374.
+The protein's natural variant, known as in BTD deficiency;, features a modification of the amino acid from F to V at position 128.
+The protein's natural variant, known as in BTD deficiency;, features a modification of the amino acid from A to T at position 171.
+The protein's natural variant, known as in BTD deficiency;, features a modification of the amino acid from D to Y at position 228.
+The protein's natural variant, known as in BTD deficiency; partial;, features a modification of the amino acid from H to R at position 323.
+The protein's natural variant, known as in BTD deficiency; profound and partial; 52% decrease in biotinyl-transferase activity;, features a modification of the amino acid from D to H at position 444.
+The protein's natural variant, known as in BTD deficiency; partial;, features a modification of the amino acid from G to D at position 451.
+The protein's natural variant, known as in BTD deficiency;, features a modification of the amino acid from Q to H at position 456.
+The protein's natural variant, known as in BTD deficiency;, features a modification of the amino acid from T to M at position 532.
+The protein's natural variant, known as in BTD deficiency; not detectable protein levels; loss of biotinyl-transferase activity;, features a modification of the amino acid from R to C at position 538.
+The protein's natural variant, known as in strain: cv. Ag-0, cv. Br-0, cv. C24, cv. Ct-1, cv. Edi-0, cv. Kas-1, cv. Kin-0, cv. Landsberg erecta, cv. Ll-0, cv. Lz-0, cv. Ms-0, cv. Mt-0, cv. Nd-1, cv. Nok-3, cv. Oy-0, cv. Sorbo, cv. Van-0, cv. Wa-1 and cv. Wassilewskija, features a modification of the amino acid from C to R at position 43.
+The protein's natural variant, known as in strain: cv. Se-0, features a modification of the amino acid from A to G at position 83.
+The protein's natural variant, known as in strain: cv. Br-0 and cv. Mt-0, features a modification of the amino acid from I to T at position 120.
+The protein's natural variant, known as in strain: cv. Ag-0, cv. Cvi-1, cv. Edi-0, cv. Ll-0 and cv. Nok-3, features a modification of the amino acid from V to F at position 154.
+The protein's natural variant, known as in strain: cv. Ag-0, cv. Br-0, cv. Cvi-1, cv. Edi-0, cv. Ll-0, cv. Lz-0, cv. Mt-0, cv. Nok-3 and cv. Van-0, features a modification of the amino acid from K to N at position 158.
+The protein's natural variant, known as in strain: cv. Nd-1, features a modification of the amino acid from M to I at position 159.
+The protein's natural variant, known as in strain: cv. Lz-0 and cv. Van-0, features a modification of the amino acid from E to K at position 161.
+The protein's natural variant, known as in strain: cv. Kin-0, features a modification of the amino acid from R to W at position 192.
+The protein's natural variant, known as in strain: cv. Ll-0, features a modification of the amino acid from G to V at position 222.
+The protein's natural variant, known as in AMD1;, features a modification of the amino acid from P to T at position 32.
+The protein's natural variant, known as in SNSK; loss of C-type natriuretic peptide-induced signaling; dominant negative effect; loss of localization to the plasma membrane;, features a modification of the amino acid from S to P at position 76.
+The protein's natural variant, known as in SNSK; loss of C-type natriuretic peptide-induced signaling; dominant negative effect; retained in the endoplasmic reticulum;, features a modification of the amino acid from R to C at position 110.
+The protein's natural variant, known as in AMD1; markedly deficient activity;, features a modification of the amino acid from W to G at position 115.
+The protein's natural variant, known as in AMD1;, features a modification of the amino acid from D to E at position 176.
+The protein's natural variant, known as does not affect C-type natriuretic peptide-induced signaling;, features a modification of the amino acid from V to I at position 187.
+The protein's natural variant, known as in SNSK; loss of C-type natriuretic peptide-induced signaling; dominant negative effect; loss of localization to the plasma membrane;, features a modification of the amino acid from R to P at position 263.
+The protein's natural variant, known as in AMD1; markedly deficient activity;, features a modification of the amino acid from T to M at position 297.
+The protein's natural variant, known as in AMD1;, features a modification of the amino acid from Y to C at position 338.
+The protein's natural variant, known as in AMD1, features a modification of the amino acid from A to T at position 409.
+The protein's natural variant, known as in AMD1; markedly deficient activity, features a modification of the amino acid from G to E at position 413.
+The protein's natural variant, known as in SNSK; loss of C-type natriuretic peptide-induced signaling; dominant negative effect; no effect on cell surface expression;, features a modification of the amino acid from Q to E at position 417.
+The protein's natural variant, known as in ECDM; mutant and wild-type alleles have similar expression levels; the mutation results in increased guanylate cyclase activity;, features a modification of the amino acid from A to P at position 488.
+The protein's natural variant, known as in ECDM; the mutation results in increased guanylate cyclase activity;, features a modification of the amino acid from R to C at position 655.
+The protein's natural variant, known as in AMD1; no effect on subcellular location; changed glycosylation; no effect on C-type natriuretic peptide binding; decreased guanylate cyclase activity; loss of natriuretic peptide receptor activity; dominant negative effect;, features a modification of the amino acid from L to F at position 658.
+The protein's natural variant, known as in AMD1; no effect on subcellular location; changed glycosylation; no effect on C-type natriuretic peptide binding; decreased guanylate cyclase activity;, features a modification of the amino acid from Y to C at position 708.
+The protein's natural variant, known as in AMD1; no effect on subcellular location; changed glycosylation; no effect on C-type natriuretic peptide binding; decreased guanylate cyclase activity;, features a modification of the amino acid from R to W at position 776.
+The protein's natural variant, known as in SNSK; loss of C-type natriuretic peptide-induced signaling; dominant negative effect; no effect on cell surface expression;, features a modification of the amino acid from R to C at position 819.
+The protein's natural variant, known as in ECDM; the mutation results in higher guanylate cyclase activity; causes a 15-fold increase in basal Vmax; has higher affinity for GTP than wild-type in the presence of NPPC; might lead to a structural change that locks the enzyme in a conformation mimicking the ATP-bound state, features a modification of the amino acid from V to M at position 882.
+The protein's natural variant, known as in AMD1;, features a modification of the amino acid from R to C at position 957.
+The protein's natural variant, known as in AMD1; no effect on subcellular location; changed glycosylation; no effect on C-type natriuretic peptide binding; decreased guanylate cyclase activity, features a modification of the amino acid from G to A at position 959.
+The protein's natural variant, known as in NS14; results in loss of MAPK down-regulation; increased protein degradation; properly targeted to the cell membrane; loss of interaction with NF1, features a modification of the amino acid from L to P at position 100.
+The protein's natural variant, known as in PHPX; reduced transcriptional activity and impaired nuclear localization, features a modification of the amino acid from A to AAAAAAAA at position 248.
+The protein's natural variant, known as in MRXGH, features a modification of the amino acid from A to AAAAAAAAAAAA at position 248.
+The protein's natural variant, known as in strain: L2, features a modification of the amino acid from V to A at position 334.
+The protein's natural variant, known as in strain: L2, features a modification of the amino acid from A to S at position 342.
+The protein's natural variant, known as in strain: W, features a modification of the amino acid from T to A at position 210.
+The protein's natural variant, known as in clone CORA 1/11, features a modification of the amino acid from V to A at position 8.
+The protein's natural variant, known as in clone CORA 1/11, features a modification of the amino acid from P to T at position 11.
+The protein's natural variant, known as in clone CORA 1/16, features a modification of the amino acid from P to S at position 15.
+The protein's natural variant, known as in clone CORA 1/16, features a modification of the amino acid from E to G at position 46.
+The protein's natural variant, known as in clone CORA 1/6 and 1/16, features a modification of the amino acid from T to K at position 81.
+The protein's natural variant, known as in clone CORA 1/6 and 1/16, features a modification of the amino acid from H to S at position 101.
+The protein's natural variant, known as in clone CORA 1/16, features a modification of the amino acid from I to T at position 114.
+The protein's natural variant, known as in clone CORA 1/11, features a modification of the amino acid from M to I at position 134.
+The protein's natural variant, known as in strain: ECOR 30, features a modification of the amino acid from TKV to VKI at position 7.
+The protein's natural variant, known as in strain: ECOR 30, features a modification of the amino acid from K to M at position 38.
+The protein's natural variant, known as in strain: ECOR 30, features a modification of the amino acid from R to K at position 57.
+The protein's natural variant, known as in strain: ECOR 30, features a modification of the amino acid from L to I at position 68.
+The protein's natural variant, known as in strain: ECOR 30, features a modification of the amino acid from N to G at position 78.
+The protein's natural variant, known as in strain: ECOR 30, features a modification of the amino acid from R to Q at position 88.
+The protein's natural variant, known as in strain: ECOR 30, features a modification of the amino acid from A to R at position 92.
+The protein's natural variant, known as in strain: ECOR 30, features a modification of the amino acid from D to E at position 96.
+The protein's natural variant, known as in strain: ECOR 30, features a modification of the amino acid from N to D at position 100.
+The protein's natural variant, known as in strain: ECOR 30, features a modification of the amino acid from G to A at position 106.
+The protein's natural variant, known as in strain: ECOR 30, features a modification of the amino acid from R to A at position 125.
+The protein's natural variant, known as in strain: ECOR 30, features a modification of the amino acid from QKM to GKI at position 144.
+The protein's natural variant, known as in strain: ECOR 30, features a modification of the amino acid from AQIREEG to SQIKVKD at position 158.
+The protein's natural variant, known as in strain: cv. cv. Ag-0, cv. Bay-0, cv. C24, cv. Ct-0, cv. Cvi-0, cv. Kas-2, cv. Mrk-0, cv. Ms-0, cv. Mt-0, cv. Nok-3, cv. Oy-0, cv. Sorbo, cv. Wa-1, cv. Wei-0 and cv. Wt-5, features a modification of the amino acid from S to T at position 305.
+The protein's natural variant, known as in VUR2;, features a modification of the amino acid from I to T at position 945.
+The protein's natural variant, known as in VUR2;, features a modification of the amino acid from A to T at position 1236.
+The protein's natural variant, known as in AD9;, features a modification of the amino acid from R to Q at position 880.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from I to M at position 330.
+The protein's natural variant, known as in strain: MT8148 / Serotype c, features a modification of the amino acid from T to A at position 88.
+The protein's natural variant, known as in strain: cv. Desiree, cv. ND860-2 and cv. Russet Burbank-1, features a modification of the amino acid from T to A at position 5.
+The protein's natural variant, known as in strain: cv. Desiree, cv. ND860-2 and cv. Russet Burbank-1, features a modification of the amino acid from E to D at position 30.
+The protein's natural variant, known as in strain: cv. Desiree, cv. ND860-2 and cv. Russet Burbank-1, features a modification of the amino acid from K to N at position 82.
+The protein's natural variant, known as in strain: cv. Desiree, cv. ND860-2 and cv. Russet Burbank-1, features a modification of the amino acid from K to E at position 445.
+The protein's natural variant, known as in strain: cv. Desiree, cv. ND860-2 and cv. Russet Burbank-1, features a modification of the amino acid from V to I at position 450.
+The natural variant of this protein is characterized by an amino acid alteration from S to T at position 525.
+The protein's natural variant, known as in SCAR22;, features a modification of the amino acid from K to T at position 622.
+The protein's natural variant, known as in strain: cv. Ag-0, features a modification of the amino acid from K to R at position 142.
+The protein's natural variant, known as in strain: cv. Br-0 and cv. Cal-0, features a modification of the amino acid from R to K at position 143.
+The protein's natural variant, known as in strain: cv. Cvi-0 and cv. Cvi-1, features a modification of the amino acid from L to F at position 170.
+The protein's natural variant, known as in strain: cv. An-1, cv. Bl-0, cv. Bla-10, cv. C24, cv. Br-0, cv. Cal-0, cv. Can-0, cv. Cnt-1, cv. Kon, cv. Ct-1, cv. Cvi-0, cv. Cvi-1, cv. Di-1, cv. Di-G, cv. Edi-0, cv. Ema-1, cv. Ga-0, cv. Hodja-Obi-Garm, cv. Ka-0, cv. Kas-1, cv. Kil-1, cv. Landsberg erecta, cv. Lip-0, cv. Ll-0, cv. Lz-0, cv. Mr-0, cv. Mrk-0, cv. Ms-0, cv. Nd-1, cv. No-0, cv. Nok-3, cv. Oy-0, cv. Pa-1, cv. Per-1, cv. Petergof, cv. Pi-0, cv. Pla-0, cv, cv. Se-0. Sei-0, cv. Sorbo, cv. Su-0, cv. Tac-0, cv. Tsu-1, cv. Van-0, cv. Wa-1, cv. Wl-0, cv. Wassilewskija and cv. Yo-0, features a modification of the amino acid from K to N at position 222.
+The protein's natural variant, known as in strain: cv. Cvi-0 and cv. Cvi-1, features a modification of the amino acid from I to V at position 245.
+The protein's natural variant, known as in HLD13;, features a modification of the amino acid from V to L at position 54.
+The protein's natural variant, known as in a patient with amyotrophic lateral sclerosis;, features a modification of the amino acid from R to C at position 65.
+The protein's natural variant, known as in a patient with amyotrophic lateral sclerosis;, features a modification of the amino acid from A to V at position 103.
+The protein's natural variant, known as in a patient with amyotrophic lateral sclerosis;, features a modification of the amino acid from G to R at position 113.
+The protein's natural variant, known as in a patient with amyotrophic lateral sclerosis;, features a modification of the amino acid from R to W at position 246.
+The protein's natural variant, known as in a patient with amyotrophic lateral sclerosis;, features a modification of the amino acid from E to Q at position 367.
+The protein's natural variant, known as in less than 10% of the chains, features a modification of the amino acid from L to F at position 4.
+The protein's natural variant, known as in less than 10% of the chains, features a modification of the amino acid from V to A at position 6.
+The protein's natural variant, known as in less than 10% of the chains, features a modification of the amino acid from L to F at position 11.
+The protein's natural variant, known as in less than 10% of the chains, features a modification of the amino acid from A to V at position 22.
+The protein's natural variant, known as in less than 10% of the chains, features a modification of the amino acid from A to S at position 49.
+The protein's natural variant, known as in less than 10% of the chains, features a modification of the amino acid from S to Q at position 52.
+The protein's natural variant, known as in less than 10% of the chains, features a modification of the amino acid from Y to F at position 67.
+The protein's natural variant, known as in less than 10% of the chains, features a modification of the amino acid from D to G at position 89.
+The protein's natural variant, known as in less than 10% of the chains, features a modification of the amino acid from E to D at position 97.
+The protein's natural variant, known as in less than 10% of the chains, features a modification of the amino acid from K to E at position 108.
+The protein's natural variant, known as in less than 10% of the chains, features a modification of the amino acid from Q to R at position 112.
+The protein's natural variant, known as in less than 10% of the chains, features a modification of the amino acid from L to H at position 113.
+The protein's natural variant, known as in less than 10% of the chains, features a modification of the amino acid from K to Q at position 120.
+The protein's natural variant, known as in AI1E;, features a modification of the amino acid from W to S at position 4.
+The protein's natural variant, known as in AI1E, features a modification of the amino acid from ILFA to T at position 8.
+The protein's natural variant, known as in AI1E;, features a modification of the amino acid from T to I at position 37.
+The protein's natural variant, known as in AI1E;, features a modification of the amino acid from P to T at position 56.
+The protein's natural variant, known as in DEE69;, features a modification of the amino acid from L to P at position 228.
+The protein's natural variant, known as in DEE69, features a modification of the amino acid from G to R at position 348.
+The protein's natural variant, known as in DEE69;, features a modification of the amino acid from G to R at position 352.
+The protein's natural variant, known as in DEE69; gain-of-function variant affecting channel activity; results in hyperpolarizing shift in half activation voltage;, features a modification of the amino acid from I to L at position 603.
+The protein's natural variant, known as in DEE69;, features a modification of the amino acid from G to D at position 690.
+The protein's natural variant, known as in DEE69; gain-of-function variant affecting channel activity; shifts the voltage dependence of activation toward more negative potentials and slows the fast inactivation time course;, features a modification of the amino acid from F to S at position 698.
+The protein's natural variant, known as in DEE69, features a modification of the amino acid from A to T at position 700.
+The protein's natural variant, known as in DEE69; gain-of-function variant affecting channel activity; shifts the voltage dependence of activation toward more negative potentials and slows the fast inactivation time course;, features a modification of the amino acid from I to V at position 701.
+The protein's natural variant, known as in DEE69;, features a modification of the amino acid from A to P at position 702.
+The protein's natural variant, known as in DEE69; gain-of-function variant affecting channel activity; shifts the voltage dependence of activation toward more negative potentials and slows the fast inactivation time course;, features a modification of the amino acid from A to T at position 702.
+The protein's natural variant, known as in DEE69, features a modification of the amino acid from I to F at position 1422.
+The protein's natural variant, known as in DEE69, features a modification of the amino acid from T to N at position 1425.
+The protein's natural variant, known as in DEE69;, features a modification of the amino acid from G to R at position 1430.
+The protein's natural variant, known as in DEE69, features a modification of the amino acid from A to G at position 1720.
+The protein's natural variant, known as in LSMFLAD; decreased protein stability; decreased affinity for FMN; reduced Vmax; decreased FMN adenylyltransferase activity;, features a modification of the amino acid from R to C at position 530.
+The protein's natural variant, known as in IDLDP, features a modification of the amino acid from C to Y at position 280.
+The protein's natural variant, known as in IDLDP; unknown pathological significance, features a modification of the amino acid from F to S at position 286.
+The protein's natural variant, known as in IDLDP, features a modification of the amino acid from C to Y at position 305.
+The protein's natural variant, known as in IDLDP, features a modification of the amino acid from R to Q at position 319.
+The protein's natural variant, known as in IDLDP; unknown pathological significance, features a modification of the amino acid from C to F at position 323.
+The protein's natural variant, known as in IDLDP; unknown pathological significance, features a modification of the amino acid from D to G at position 392.
+The protein's natural variant, known as in strain: Adelaide-1, features a modification of the amino acid from A to T at position 582.
+The protein's natural variant, known as in strain: Adelaide-1, features a modification of the amino acid from A to S at position 606.
+The protein's natural variant, known as loss of function associated with defective cofactor binding and accelerated proteasomal degradation;, features a modification of the amino acid from P to S at position 187.
+The protein's natural variant, known as in mf, features a modification of the amino acid from C to Y at position 450.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from D to A at position 162.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from S to G at position 208.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from E to D at position 354.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from N to D at position 899.
+The protein's natural variant, known as in OOHE; unknown pathological significance;, features a modification of the amino acid from R to W at position 98.
+The protein's natural variant, known as in OOHE; unknown pathological significance, features a modification of the amino acid from G to V at position 343.
+The protein's natural variant, known as in OOHE; unknown pathological significance;, features a modification of the amino acid from V to D at position 438.
+The protein's natural variant, known as in OOHE; unknown pathological significance;, features a modification of the amino acid from S to L at position 893.
+The protein's natural variant, known as in OOHE; unknown pathological significance, features a modification of the amino acid from C to G at position 927.
+The natural variant of this protein is characterized by an amino acid alteration from A to G at position 19.
+The protein's natural variant, known as in 3M1; unknown pathological significance;, features a modification of the amino acid from L to R at position 1014.
+The protein's natural variant, known as in 3M1; requires 2 nucleotide substitutions, features a modification of the amino acid from Q to G at position 1246.
+The protein's natural variant, known as in 3M1; impairs the ability to interact with RBX1, thus hampers the assembly of polyubiquitin chains;, features a modification of the amino acid from H to P at position 1464.
+The protein's natural variant, known as in 3M1;, features a modification of the amino acid from L to P at position 1588.
+The natural variant of this protein is characterized by an amino acid alteration from S to L at position 125.
+The natural variant of this protein is characterized by an amino acid alteration from T to A at position 529.
+The natural variant of this protein is characterized by an amino acid alteration from G to S at position 262.
+The natural variant of this protein is characterized by an amino acid alteration from P to S at position 98.
+The protein's natural variant, known as in strain: K12 / MC4100; inactive, features a modification of the amino acid from R to C at position 298.
+The protein's natural variant, known as found in patients with Barrett esophagus;, features a modification of the amino acid from Q to P at position 44.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from S to N at position 77.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from N to S at position 149.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from I to F at position 353.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from F to S at position 682.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from S to F at position 707.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from I to T at position 770.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from N to S at position 811.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from D to NDNNN at position 852.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from N to NN at position 887.
+The protein's natural variant, known as in acute lymphoblastic leukemia patients and acute myelogenous leukemia patients; somatic mutation; constitutively activated;, features a modification of the amino acid from D to E at position 835.
+The protein's natural variant, known as in acute lymphoblastic leukemia patients and in acute myelogenous leukemia patients; somatic mutation; constitutively activated;, features a modification of the amino acid from D to H at position 835.
+The protein's natural variant, known as in acute lymphoblastic leukemia patients and in acute myelogenous leukemia patients; somatic mutation; constitutively activated;, features a modification of the amino acid from D to N at position 835.
+The protein's natural variant, known as in acute lymphoblastic leukemia patients and in acute myelogenous leukemia patients; somatic mutation; constitutively activated;, features a modification of the amino acid from D to V at position 835.
+The protein's natural variant, known as in acute lymphoblastic leukemia patients and in acute myelogenous leukemia patients; somatic mutation; constitutively activated;, features a modification of the amino acid from D to Y at position 835.
+The protein's natural variant, known as in acute lymphoblastic leukemia patients; somatic mutation;, features a modification of the amino acid from I to M at position 836.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from V to M at position 133.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from P to S at position 24.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 329.
+The protein's natural variant, known as in AI2A5; autosomal recessive;, features a modification of the amino acid from A to V at position 146.
+The protein's natural variant, known as in AI2A5; autosomal recessive;, features a modification of the amino acid from S to C at position 499.
+The protein's natural variant, known as prevents G1 cell cycle arrest; reduced protein phosphorylation;, features a modification of the amino acid from S to F at position 135.
+The protein's natural variant, known as prevents G1 cell cycle arrest; reduced protein phosphorylation;, features a modification of the amino acid from A to S at position 137.
+The protein's natural variant, known as in BC; unknown pathological significance;, features a modification of the amino acid from S to F at position 4.
+The protein's natural variant, known as in BC and BROVCA1, features a modification of the amino acid from E to K at position 10.
+The protein's natural variant, known as found in breast-ovarian cancer patients; unknown pathological significance;, features a modification of the amino acid from V to A at position 11.
+The protein's natural variant, known as in BC; unknown pathological significance;, features a modification of the amino acid from M to T at position 18.
+The protein's natural variant, known as found in breast-ovarian cancer patients; unknown pathological significance;, features a modification of the amino acid from I to V at position 21.
+The protein's natural variant, known as in BC;, features a modification of the amino acid from L to S at position 22.
+The protein's natural variant, known as in BC and BROVCA1, features a modification of the amino acid from E to K at position 23.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from L to F at position 30.
+The protein's natural variant, known as in BC; unknown pathological significance; functionally neutral in vitro;, features a modification of the amino acid from K to Q at position 45.
+The protein's natural variant, known as in BC and ovarian cancer; no interaction with BAP1;, features a modification of the amino acid from C to G at position 61.
+The protein's natural variant, known as in BC; no interaction with BAP1;, features a modification of the amino acid from C to G at position 64.
+The protein's natural variant, known as in BC; unknown pathological significance; functionally neutral in vitro;, features a modification of the amino acid from D to Y at position 67.
+The protein's natural variant, known as in BC; unknown pathological significance;, features a modification of the amino acid from R to K at position 71.
+The protein's natural variant, known as in BC; unknown pathological significance; functionally neutral in vitro;, features a modification of the amino acid from N to K at position 132.
+The protein's natural variant, known as in BC; unknown pathological significance; functionally neutral in vitro;, features a modification of the amino acid from P to H at position 142.
+The protein's natural variant, known as in BC; unknown pathological significance; functionally neutral in vitro;, features a modification of the amino acid from L to F at position 147.
+The protein's natural variant, known as in BC; unknown pathological significance; functionally neutral in vitro, features a modification of the amino acid from L to P at position 165.
+The protein's natural variant, known as in BC; unknown pathological significance; functionally neutral in vitro;, features a modification of the amino acid from R to W at position 170.
+The protein's natural variant, known as in BC; unknown pathological significance; functionally neutral in vitro;, features a modification of the amino acid from S to Y at position 186.
+The protein's natural variant, known as in BC; unknown pathological significance; functionally neutral in vitro;, features a modification of the amino acid from V to I at position 191.
+The protein's natural variant, known as in ovarian cancer; unknown pathological significance, features a modification of the amino acid from E to K at position 227.
+The protein's natural variant, known as in BC; unknown pathological significance; functionally neutral in vitro;, features a modification of the amino acid from T to M at position 231.
+The protein's natural variant, known as in BC; unknown pathological significance; functionally neutral in vitro;, features a modification of the amino acid from D to V at position 245.
+The protein's natural variant, known as in BC; unknown pathological significance; functionally neutral in vitro;, features a modification of the amino acid from L to V at position 246.
+The protein's natural variant, known as in BC; unknown pathological significance; functionally neutral in vitro;, features a modification of the amino acid from V to L at position 271.
+The protein's natural variant, known as in BC;, features a modification of the amino acid from V to M at position 271.
+The protein's natural variant, known as in BC; unknown pathological significance;, features a modification of the amino acid from P to S at position 346.
+The protein's natural variant, known as in BC;, features a modification of the amino acid from F to L at position 461.
+The protein's natural variant, known as in BC;, features a modification of the amino acid from Y to D at position 465.
+The protein's natural variant, known as found in breast-ovarian cancer patients; unknown pathological significance;, features a modification of the amino acid from R to I at position 507.
+The protein's natural variant, known as in BC;, features a modification of the amino acid from G to V at position 552.
+The natural variant of this protein is characterized by an amino acid alteration from N to I at position 656.
+The protein's natural variant, known as in BC; unknown pathological significance; functionally neutral in vitro;, features a modification of the amino acid from L to F at position 668.
+The protein's natural variant, known as in BC; unknown pathological significance; functionally neutral in vitro;, features a modification of the amino acid from D to N at position 695.
+The protein's natural variant, known as in BC;, features a modification of the amino acid from D to Y at position 749.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from L to F at position 758.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from G to C at position 778.
+The protein's natural variant, known as in BC; unknown pathological significance; functionally neutral in vitro;, features a modification of the amino acid from P to L at position 798.
+The protein's natural variant, known as in BC; unknown pathological significance; functionally neutral in vitro;, features a modification of the amino acid from N to Y at position 810.
+The protein's natural variant, known as in BC; unknown pathological significance; functionally neutral in vitro;, features a modification of the amino acid from T to K at position 826.
+The protein's natural variant, known as in BROVCA1; unknown pathological significance;, features a modification of the amino acid from H to Y at position 835.
+The protein's natural variant, known as in BC; unknown pathological significance; functionally neutral in vitro;, features a modification of the amino acid from R to Q at position 841.
+The protein's natural variant, known as in BROVCA1; unknown pathological significance;, features a modification of the amino acid from R to W at position 841.
+The protein's natural variant, known as in a patient with sporadic breast cancer; unknown pathological significance;, features a modification of the amino acid from Y to H at position 856.
+The protein's natural variant, known as in BC; unknown pathological significance, features a modification of the amino acid from R to Q at position 866.
+The protein's natural variant, known as in BC; unknown pathological significance;, features a modification of the amino acid from H to Y at position 888.
+The protein's natural variant, known as in BC;, features a modification of the amino acid from L to S at position 892.
+The protein's natural variant, known as in BC;, features a modification of the amino acid from G to D at position 960.
+The protein's natural variant, known as in BC;, features a modification of the amino acid from T to I at position 1025.
+The protein's natural variant, known as in BC;, features a modification of the amino acid from V to A at position 1047.
+The protein's natural variant, known as in BC; unknown pathological significance; functionally neutral in vitro;, features a modification of the amino acid from S to N at position 1101.
+The protein's natural variant, known as in BC; unknown pathological significance;, features a modification of the amino acid from S to I at position 1139.
+The protein's natural variant, known as in BC; unknown pathological significance; functionally neutral in vitro;, features a modification of the amino acid from S to G at position 1140.
+The protein's natural variant, known as in BC; unknown pathological significance; functionally neutral in vitro, features a modification of the amino acid from S to N at position 1140.
+The protein's natural variant, known as in BC;, features a modification of the amino acid from P to S at position 1150.
+The protein's natural variant, known as in BC and BROVCA1, features a modification of the amino acid from S to I at position 1187.
+The protein's natural variant, known as in BC and BROVCA1;, features a modification of the amino acid from Q to H at position 1200.
+The protein's natural variant, known as in BC, features a modification of the amino acid from R to I at position 1204.
+The protein's natural variant, known as in BC, features a modification of the amino acid from K to N at position 1207.
+The protein's natural variant, known as in BC; unknown pathological significance;, features a modification of the amino acid from E to G at position 1210.
+The protein's natural variant, known as in BC; unknown pathological significance; functionally neutral in vitro;, features a modification of the amino acid from E to K at position 1214.
+The protein's natural variant, known as in BC and BROVCA1, features a modification of the amino acid from S to Y at position 1217.
+The protein's natural variant, known as found in breast-ovarian cancer patients; unknown pathological significance;, features a modification of the amino acid from E to D at position 1219.
+The protein's natural variant, known as in BROVCA1, features a modification of the amino acid from F to L at position 1226.
+The protein's natural variant, known as in BC; unknown pathological significance; functionally neutral in vitro;, features a modification of the amino acid from N to K at position 1236.
+The protein's natural variant, known as in BROVCA1, features a modification of the amino acid from R to G at position 1243.
+The protein's natural variant, known as in BC; unknown pathological significance; functionally neutral in vitro;, features a modification of the amino acid from L to S at position 1267.
+The protein's natural variant, known as in BC; unknown pathological significance; functionally neutral in vitro;, features a modification of the amino acid from E to V at position 1282.
+The protein's natural variant, known as in BC; unknown pathological significance;, features a modification of the amino acid from S to P at position 1297.
+The protein's natural variant, known as in BC; unknown pathological significance; functionally neutral in vitro;, features a modification of the amino acid from S to R at position 1301.
+The protein's natural variant, known as in BC; unknown pathological significance; functionally neutral in vitro;, features a modification of the amino acid from E to K at position 1346.
+The protein's natural variant, known as in BC; unknown pathological significance; functionally neutral in vitro;, features a modification of the amino acid from V to I at position 1378.
+The protein's natural variant, known as in BC; unknown pathological significance; functionally neutral in vitro;, features a modification of the amino acid from M to V at position 1400.
+The protein's natural variant, known as in BC; unknown pathological significance; functionally neutral in vitro;, features a modification of the amino acid from L to P at position 1407.
+The protein's natural variant, known as in BC and ovarian cancer; unknown pathological significance; decreased interaction with PALB2;, features a modification of the amino acid from M to T at position 1411.
+The natural variant of this protein is characterized by an amino acid alteration from S to P at position 1431.
+The protein's natural variant, known as in BC; unknown pathological significance; functionally neutral in vitro;, features a modification of the amino acid from R to G at position 1443.
+The protein's natural variant, known as in BC; unknown pathological significance; functionally neutral in vitro;, features a modification of the amino acid from S to G at position 1448.
+The protein's natural variant, known as in BC; unknown pathological significance; functionally neutral in vitro;, features a modification of the amino acid from S to C at position 1486.
+The protein's natural variant, known as in BC; unknown pathological significance;, features a modification of the amino acid from R to M at position 1495.
+The protein's natural variant, known as in BC; unknown pathological significance; functionally neutral in vitro;, features a modification of the amino acid from V to M at position 1534.
+The protein's natural variant, known as found in breast cancer; unknown pathological significance;, features a modification of the amino acid from T to I at position 1561.
+The protein's natural variant, known as in BC; unknown pathological significance; functionally neutral in vitro, features a modification of the amino acid from R to P at position 1589.
+The protein's natural variant, known as found in breast cancer; unknown pathological significance;, features a modification of the amino acid from K to E at position 1606.
+The protein's natural variant, known as could be associated with cancer susceptibility; major splicing aberration identified with this mutant;, features a modification of the amino acid from A to G at position 1623.
+The protein's natural variant, known as in some patients with sporadic breast cancer; unknown pathological significance;, features a modification of the amino acid from M to T at position 1628.
+The protein's natural variant, known as found in breast and ovarian cancer patients; unknown pathological significance;, features a modification of the amino acid from M to V at position 1628.
+The protein's natural variant, known as in ovarian cancer; unknown pathological significance;, features a modification of the amino acid from A to P at position 1641.
+The protein's natural variant, known as in BC; unknown pathological significance;, features a modification of the amino acid from S to F at position 1651.
+The protein's natural variant, known as in BC; unknown pathological significance;, features a modification of the amino acid from S to P at position 1651.
+The protein's natural variant, known as in BC; unknown pathological significance; functionally impaired in vitro;, features a modification of the amino acid from S to F at position 1655.
+The protein's natural variant, known as in BC; unknown pathological significance;, features a modification of the amino acid from T to A at position 1685.
+The protein's natural variant, known as could be associated with cancer susceptibility; multifactorial likelihood analysis provides evidence for pathogenicity;, features a modification of the amino acid from T to I at position 1685.
+The protein's natural variant, known as in BC; unknown pathological significance; functionally impaired in vitro;, features a modification of the amino acid from H to Q at position 1686.
+The protein's natural variant, known as in BC; unknown pathological significance; functionally impaired in vitro;, features a modification of the amino acid from H to R at position 1686.
+The protein's natural variant, known as in BC; unknown pathological significance;, features a modification of the amino acid from M to R at position 1689.
+The protein's natural variant, known as in some patients with sporadic breast cancer; unknown pathological significance;, features a modification of the amino acid from K to Q at position 1690.
+The protein's natural variant, known as in BC; unknown pathological significance; functionally impaired in vitro;, features a modification of the amino acid from T to I at position 1691.
+The protein's natural variant, known as in ovarian cancer; unknown pathological significance;, features a modification of the amino acid from D to N at position 1692.
+The protein's natural variant, known as in ovarian cancer;, features a modification of the amino acid from C to R at position 1697.
+The protein's natural variant, known as in BC; unknown pathological significance; strongly reduces affinity for a BRIP1 phosphopeptide; functionally impaired in vitro;, features a modification of the amino acid from R to Q at position 1699.
+The protein's natural variant, known as in BC, ovarian cancer and FANCS; impairs protein stability; functionally impaired in vitro;, features a modification of the amino acid from R to W at position 1699.
+The protein's natural variant, known as in BC; unknown pathological significance;, features a modification of the amino acid from G to A at position 1706.
+The protein's natural variant, known as in BC; unknown pathological significance;, features a modification of the amino acid from G to E at position 1706.
+The protein's natural variant, known as in BC; abolishes ACACA binding;, features a modification of the amino acid from A to E at position 1708.
+The natural variant of this protein is characterized by an amino acid alteration from V to G at position 1713.
+The protein's natural variant, known as in BC; unknown pathological significance;, features a modification of the amino acid from S to R at position 1715.
+The protein's natural variant, known as in BC; unknown pathological significance; functionally impaired in vitro;, features a modification of the amino acid from W to C at position 1718.
+The protein's natural variant, known as in BC; unknown pathological significance; functionally neutral in vitro; no effect on in vitro phosphorylation by ATR;, features a modification of the amino acid from T to A at position 1720.
+The protein's natural variant, known as in BC; unknown pathological significance;, features a modification of the amino acid from E to K at position 1735.
+The protein's natural variant, known as in BC and FANCS; unknown pathological significance; Decreased localization to DNA damage sites and reduced interaction with UIMC1/RAP80;, features a modification of the amino acid from V to A at position 1736.
+The protein's natural variant, known as in BC; unknown pathological significance;, features a modification of the amino acid from G to R at position 1738.
+The protein's natural variant, known as in BC; unknown pathological significance; functionally impaired in vitro;, features a modification of the amino acid from D to G at position 1739.
+The protein's natural variant, known as in BC; unknown pathological significance; functionally impaired in vitro;, features a modification of the amino acid from D to V at position 1739.
+The protein's natural variant, known as in BC; unknown pathological significance;, features a modification of the amino acid from H to Q at position 1746.
+The protein's natural variant, known as in ovarian cancer; unknown pathological significance; abolishes ACACA binding and strongly reduces BRIP1 binding;, features a modification of the amino acid from P to R at position 1749.
+The protein's natural variant, known as in BC; unknown pathological significance;, features a modification of the amino acid from R to T at position 1753.
+The protein's natural variant, known as in BC; unknown pathological significance; functionally impaired in vitro;, features a modification of the amino acid from L to P at position 1764.
+The protein's natural variant, known as in BC; unknown pathological significance;, features a modification of the amino acid from I to S at position 1766.
+The protein's natural variant, known as in BC; unknown pathological significance; functionally neutral in vitro;, features a modification of the amino acid from C to S at position 1767.
+The protein's natural variant, known as in BC; unknown pathological significance; functionally impaired in vitro;, features a modification of the amino acid from G to V at position 1770.
+The protein's natural variant, known as in BC; strongly reduced transcription transactivation; abolishes interaction with BRIP1 and RBBP8;, features a modification of the amino acid from M to K at position 1775.
+The protein's natural variant, known as in BC; alters protein stability and abolishes ACACA and BRIP1 binding;, features a modification of the amino acid from M to R at position 1775.
+The protein's natural variant, known as in ovarian cancer; unknown pathological significance;, features a modification of the amino acid from P to S at position 1776.
+The protein's natural variant, known as in BC, BROVCA1 and OC; unknown pathological significance;, features a modification of the amino acid from L to P at position 1780.
+The protein's natural variant, known as in BC; unknown pathological significance; functionally neutral in vitro, features a modification of the amino acid from W to C at position 1782.
+The protein's natural variant, known as in BROVCA1; unknown pathological significance;, features a modification of the amino acid from L to P at position 1786.
+The protein's natural variant, known as in BC; unknown pathological significance;, features a modification of the amino acid from G to V at position 1788.
+The protein's natural variant, known as in BC; unknown pathological significance; functionally impaired in vitro;, features a modification of the amino acid from A to T at position 1789.
+The protein's natural variant, known as in BC; unknown pathological significance; functionally neutral in vitro;, features a modification of the amino acid from E to D at position 1794.
+The protein's natural variant, known as in BC; unknown pathological significance; functionally neutral in vitro;, features a modification of the amino acid from V to D at position 1804.
+The protein's natural variant, known as in BC; unknown pathological significance; functionally neutral in vitro, features a modification of the amino acid from P to R at position 1812.
+The protein's natural variant, known as in ovarian cancer; unknown pathological significance;, features a modification of the amino acid from P to S at position 1812.
+The protein's natural variant, known as in BC; unknown pathological significance; functionally impaired in vitro;, features a modification of the amino acid from W to R at position 1837.
+The protein's natural variant, known as in BC; unknown pathological significance; functionally neutral in vitro;, features a modification of the amino acid from H to L at position 1862.
+The protein's natural variant, known as in KPD; associated with disease susceptibility, features a modification of the amino acid from R to W at position 45.
+The protein's natural variant, known as in T2D; associated with disease susceptibility;, features a modification of the amino acid from R to W at position 129.
+The protein's natural variant, known as in KPD; associated with disease susceptibility;, features a modification of the amino acid from R to W at position 141.
+The protein's natural variant, known as in MODY9; the mutant sequence represses the activity of the insulin and glucagon promoters by only 35% compared to 50% and 57% respectively with wild-type sequence, features a modification of the amino acid from R to W at position 172.
+The protein's natural variant, known as in strain: Breinl, features a modification of the amino acid from V to A at position 257.
+The protein's natural variant, known as in strain: Breinl, features a modification of the amino acid from Y to D at position 1010.
+The protein's natural variant, known as in strain: Breinl, features a modification of the amino acid from A to S at position 1450.
+The protein's natural variant, known as in strain: CWL029 and TW-183, features a modification of the amino acid from K to Q at position 257.
+The natural variant of this protein is characterized by an amino acid alteration from L to P at position 11.
+The natural variant of this protein is characterized by an amino acid alteration from L to V at position 12.
+The natural variant of this protein is characterized by an amino acid alteration from K to R at position 46.
+The natural variant of this protein is characterized by an amino acid alteration from G to D at position 107.
+The natural variant of this protein is characterized by an amino acid alteration from A to V at position 114.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 229.
+The protein's natural variant, known as in strain: TN106, features a modification of the amino acid from F to L at position 72.
+The protein's natural variant, known as in strain: TN106, features a modification of the amino acid from G to C at position 104.
+The protein's natural variant, known as in strain: TN106, features a modification of the amino acid from V to G at position 116.
+The protein's natural variant, known as in strain: TN106, features a modification of the amino acid from S to F at position 167.
+The protein's natural variant, known as in strain: TN106, features a modification of the amino acid from T to M at position 252.
+The protein's natural variant, known as in 40% of the molecules, features a modification of the amino acid from A to S at position 97.
+The protein's natural variant, known as requires 2 nucleotide substitutions, features a modification of the amino acid from K to P at position 115.
+The natural variant of this protein is characterized by an amino acid alteration from V to G at position 167.
+The natural variant of this protein is characterized by an amino acid alteration from PL to GE at position 180.
+The natural variant of this protein is characterized by an amino acid alteration from S to D at position 51.
+The protein's natural variant, known as in strain: Isolate FMNH 128675 and Isolate FMNH 128718, features a modification of the amino acid from V to I at position 14.
+The protein's natural variant, known as in strain: Isolate FMNH 128713, Isolate TK 4728, Isolate TK 86578 and Isolate TK 86579, features a modification of the amino acid from A to T at position 23.
+The protein's natural variant, known as in strain: Isolate TK 9251 and Isolate TK 11040, features a modification of the amino acid from S to N at position 26.
+The protein's natural variant, known as in strain: Isolate MVZ 185575, features a modification of the amino acid from V to A at position 39.
+The protein's natural variant, known as in strain: Isolate FMNH 128718, features a modification of the amino acid from V to M at position 39.
+The protein's natural variant, known as in strain: Isolate TK 4728 and Isolate TK 9251, features a modification of the amino acid from V to M at position 78.
+The protein's natural variant, known as in strain: Isolate FMNH 128676, Isolate FMNH 128713, Isolate FMNH 128718 and Isolate TK 43208, features a modification of the amino acid from T to M at position 108.
+The protein's natural variant, known as in strain: Isolate TK 4728, features a modification of the amino acid from S to L at position 110.
+The protein's natural variant, known as in strain: Isolate TK 13173, features a modification of the amino acid from L to M at position 119.
+The protein's natural variant, known as in strain: Isolate MVZ 185583, features a modification of the amino acid from F to L at position 121.
+The protein's natural variant, known as in strain: Isolate TK 15194, features a modification of the amino acid from V to D at position 132.
+The protein's natural variant, known as in strain: Isolate MVZ 185566, features a modification of the amino acid from V to I at position 132.
+The protein's natural variant, known as in strain: Isolate TK 15194, features a modification of the amino acid from I to N at position 156.
+The protein's natural variant, known as in strain: Isolate FMNH 128676, Isolate FMNH 128713, Isolate FMNH 128718, Isolate MVZ 185583, Isolate TK 4728, Isolate TK 9251, Isolate TK 11040, Isolate TK 13173, Isolate TK 13594, Isolate TK 14159, Isolate TK 34707, Isolate TK 41573, Isolate TK 43138, Isolate TK 43178, Isolate TK 43189, Isolate TK 43208, Isolate USNM578997, Isolate USNM579009 and Isolate USNM579010, features a modification of the amino acid from T to M at position 158.
+The protein's natural variant, known as in strain: Isolate TK 22631, features a modification of the amino acid from Q to H at position 162.
+The protein's natural variant, known as in strain: Isolate TK 15194, features a modification of the amino acid from T to K at position 176.
+The protein's natural variant, known as in strain: Isolate TK 4728 and Isolate TK 86578, features a modification of the amino acid from F to L at position 185.
+The protein's natural variant, known as in strain: Isolate TK 41573, Isolate TK 86578, Isolate USNM578997, Isolate USNM579009 and Isolate USNM579010, features a modification of the amino acid from S to P at position 215.
+The protein's natural variant, known as in strain: Isolate FMNH 128676, features a modification of the amino acid from L to P at position 236.
+The protein's natural variant, known as in strain: Isolate TK 41573, features a modification of the amino acid from L to I at position 249.
+The protein's natural variant, known as in strain: Isolate FMNH 128676, features a modification of the amino acid from M to V at position 257.
+The protein's natural variant, known as in strain: Isolate TK 15194, features a modification of the amino acid from Y to F at position 273.
+The protein's natural variant, known as in strain: Isolate TK 15194, Isolate TK 22602, Isolate TK 22631, Isolate TK 25071, Isolate TK 56869, Isolate USNM578997, Isolate USNM579009 and Isolate USNM579010, features a modification of the amino acid from I to V at position 303.
+The protein's natural variant, known as in strain: Isolate FMNH 128676, features a modification of the amino acid from I to F at position 331.
+The protein's natural variant, known as in strain: Isolate FMNH 128718, features a modification of the amino acid from I to V at position 338.
+The protein's natural variant, known as in strain: Isolate TK 15154, Isolate TK 15194, Isolate TK 17544, Isolate TK 25071 and Isolate TK 25212, features a modification of the amino acid from V to I at position 356.
+The protein's natural variant, known as in strain: Isolate TK 86578, features a modification of the amino acid from L to S at position 360.
+The protein's natural variant, known as in strain: Isolate FMNH 128676, features a modification of the amino acid from IL to TQ at position 363.
+The protein's natural variant, known as in strain: Isolate TK 17544, features a modification of the amino acid from V to I at position 364.
+The protein's natural variant, known as in strain: Isolate TK 43189, features a modification of the amino acid from V to I at position 369.
+The protein's natural variant, known as in strain: Isolate FMNH 128676, Isolate FMNH 128713, Isolate FMNH 128718, Isolate TK 4728, Isolate TK 9251, Isolate TK 11040, Isolate TK 13173, Isolate TK 13594, Isolate TK 14159, Isolate TK 34707, Isolate TK 41573, Isolate TK 43138, Isolate TK 43178, Isolate TK 43189, Isolate TK 43208, Isolate USNM578997, Isolate USNM579009 and Isolate USNM579010, features a modification of the amino acid from Y to H at position 375.
+The protein's natural variant, known as in Malaysia;, features a modification of the amino acid from G to C at position 2.
+The protein's natural variant, known as in Meinohama;, features a modification of the amino acid from E to G at position 6.
+The protein's natural variant, known as in Auckland;, features a modification of the amino acid from D to N at position 8.
+The protein's natural variant, known as in Albaicin;, features a modification of the amino acid from K to E at position 9.
+The protein's natural variant, known as in Albaicin;, features a modification of the amino acid from K to Q at position 9.
+The protein's natural variant, known as in Heather;, features a modification of the amino acid from T to R at position 13.
+The protein's natural variant, known as in Catalonia;, features a modification of the amino acid from W to R at position 16.
+The protein's natural variant, known as in Melbourne;, features a modification of the amino acid from G to R at position 17.
+The protein's natural variant, known as in Clamart;, features a modification of the amino acid from K to N at position 18.
+The protein's natural variant, known as in Ouled Rabah;, features a modification of the amino acid from N to K at position 20.
+The protein's natural variant, known as in Bron;, features a modification of the amino acid from V to A at position 21.
+The protein's natural variant, known as in Saskatoon;, features a modification of the amino acid from E to K at position 22.
+The protein's natural variant, known as in Fuchu;, features a modification of the amino acid from E to Q at position 22.
+The protein's natural variant, known as in Urumqi;, features a modification of the amino acid from D to G at position 23.
+The protein's natural variant, known as in Granada;, features a modification of the amino acid from D to V at position 23.
+The protein's natural variant, known as in Cosenza;, features a modification of the amino acid from G to E at position 26.
+The protein's natural variant, known as in Oakland;, features a modification of the amino acid from E to K at position 27.
+The protein's natural variant, known as in Tokyo;, features a modification of the amino acid from V to I at position 35.
+The protein's natural variant, known as in Bonheiden; causes severe hereditary hemolytic anemia;, features a modification of the amino acid from T to P at position 39.
+The protein's natural variant, known as in Veleta;, features a modification of the amino acid from R to G at position 41.
+The protein's natural variant, known as in Austell;, features a modification of the amino acid from R to K at position 41.
+The protein's natural variant, known as in TNCY; hemoglobin Cincinnati;, features a modification of the amino acid from F to S at position 42.
+The protein's natural variant, known as in Lodz;, features a modification of the amino acid from S to R at position 45.
+The protein's natural variant, known as in Kingston;, features a modification of the amino acid from M to R at position 56.
+The protein's natural variant, known as in Emirates;, features a modification of the amino acid from K to E at position 60.
+The protein's natural variant, known as in Sacromonte;, features a modification of the amino acid from K to Q at position 60.
+The protein's natural variant, known as in TNCY; hemoglobin M-Circleville, features a modification of the amino acid from H to L at position 64.
+The protein's natural variant, known as in TNCY; hemoglobin Osaka; the presence of a tyrosine causes the formation of a covalent link with heme iron, so that the iron is stabilized in the ferric form; when this occurs methemoglobin is formed, oxygen can no longer bind to heme and cyanosis occurs;, features a modification of the amino acid from H to Y at position 64.
+The protein's natural variant, known as in Clarke;, features a modification of the amino acid from K to N at position 66.
+The protein's natural variant, known as in Brooklyn;, features a modification of the amino acid from K to Q at position 67.
+The protein's natural variant, known as in Shanghai;, features a modification of the amino acid from K to R at position 67.
+The protein's natural variant, known as in TNCY; hemoglobin Toms River; the side chain of methionine decreases both the affinity of oxygen for binding to the mutant hemoglobin subunit via steric hindrance and the rate at which it does so; the mutant methionine is converted to aspartic acid post-translationally;, features a modification of the amino acid from V to M at position 68.
+The protein's natural variant, known as in Minoo;, features a modification of the amino acid from G to R at position 73.
+The protein's natural variant, known as in LesVos/Waynesboro/Charlotte;, features a modification of the amino acid from I to T at position 76.
+The protein's natural variant, known as in Coigneres;, features a modification of the amino acid from I to V at position 76.
+The protein's natural variant, known as in Kennestone;, features a modification of the amino acid from H to R at position 78.
+The protein's natural variant, known as in Marietta;, features a modification of the amino acid from D to N at position 81.
+The protein's natural variant, known as in TNCY; hemoglobin Fort Ripley;, features a modification of the amino acid from H to Y at position 93.
+The protein's natural variant, known as in Columbus-Ga;, features a modification of the amino acid from D to N at position 95.
+The protein's natural variant, known as in La Grange;, features a modification of the amino acid from E to K at position 102.
+The protein's natural variant, known as in Macedonia-II;, features a modification of the amino acid from K to N at position 105.
+The protein's natural variant, known as in TNCY; hemoglobin F-Brugine/Feldkirch; lowered affinity for oxygen, features a modification of the amino acid from L to H at position 106.
+The protein's natural variant, known as in Malta-1;, features a modification of the amino acid from H to R at position 118.
+The protein's natural variant, known as in Calabria;, features a modification of the amino acid from F to L at position 119.
+The protein's natural variant, known as in Caltech;, features a modification of the amino acid from K to Q at position 121.
+The protein's natural variant, known as in Carlton;, features a modification of the amino acid from E to K at position 122.
+The protein's natural variant, known as in Port-Royal;, features a modification of the amino acid from E to A at position 126.
+The protein's natural variant, known as in Poole; unstable;, features a modification of the amino acid from W to G at position 131.
+The protein's natural variant, known as in Onoda; O(2) affinity up;, features a modification of the amino acid from H to Y at position 147.
+The protein's natural variant, known as in DENBA, features a modification of the amino acid from W to R at position 123.
+The protein's natural variant, known as in DENBA; unknown pathological significance, features a modification of the amino acid from E to K at position 178.
+The protein's natural variant, known as in DENBA; unknown pathological significance, features a modification of the amino acid from W to R at position 193.
+The protein's natural variant, known as in DENBA; unknown pathological significance;, features a modification of the amino acid from K to E at position 274.
+The protein's natural variant, known as in DENBA; unknown pathological significance, features a modification of the amino acid from Q to E at position 326.
+The protein's natural variant, known as in DENBA; unknown pathological significance, features a modification of the amino acid from M to R at position 479.
+The protein's natural variant, known as in DENBA, features a modification of the amino acid from R to H at position 483.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from K to N at position 57.
+The protein's natural variant, known as in strain: cv. Nona Bokra and cv. Pokkali; higher sodium transport activity, features a modification of the amino acid from R to H at position 184.
+The protein's natural variant, known as in strain: cv. Nona Bokra and cv. Pokkali; higher sodium transport activity, features a modification of the amino acid from H to D at position 332.
+The protein's natural variant, known as in strain: cv. Nona Bokra and cv. Pokkali; higher sodium transport activity, features a modification of the amino acid from L to V at position 395.
+The protein's natural variant, known as in strain: Isolate IZEA-6137, features a modification of the amino acid from S to N at position 16.
+The protein's natural variant, known as in strain: Isolate IZEA-6137, features a modification of the amino acid from A to T at position 122.
+The protein's natural variant, known as in strain: Isolate IZEA-5339, features a modification of the amino acid from G to A at position 194.
+The protein's natural variant, known as in strain: Isolate IZEA-5326, Isolate IZEA-5381 and Isolate IZEA-5561, features a modification of the amino acid from L to F at position 234.
+The protein's natural variant, known as in strain: Isolate IZEA-3303, Isolate IZEA-5326, Isolate IZEA-5339, Isolate IZEA-5381, Isolate IZEA-5561, Isolate San Rhemy and Isolate SI-91.4, features a modification of the amino acid from T to A at position 238.
+The protein's natural variant, known as in strain: Isolate IZEA-2887, Isolate IZEA-3303, Isolate IZEA-3383, Isolate IZEA-5326, Isolate IZEA-5339, Isolate IZEA-5381, Isolate IZEA-5561, Isolate IZEA-6137, Isolate JS3032, Isolate JZ665, Isolate JZ835, Isolate San Rhemy and Isolate SI-91.4, features a modification of the amino acid from M to T at position 257.
+The protein's natural variant, known as in strain: Isolate IZEA-2887, Isolate IZEA-3303, Isolate IZEA-3383, Isolate IZEA-IZEA-5326, Isolate IZEA-5339, Isolate IZEA-5381, Isolate IZEA-5561, Isolate IZEA-6137, Isolate JS3032, Isolate JZ665, Isolate JZ835, Isolate San Rhemy and Isolate SI-91.4, features a modification of the amino acid from A to V at position 295.
+The protein's natural variant, known as in strain: Isolate IZEA-5381 and Isolate JS3032, features a modification of the amino acid from W to WK at position 379.
+The protein's natural variant, known as in DEE51; severe defects in aerobic respiration, when assayed in a heterologous system;, features a modification of the amino acid from G to R at position 37.
+The protein's natural variant, known as in DEE51; decreased protein abundance; strong decrease in malate dehydrogenase activity; severe defects in aerobic respiration, when assayed in a heterologous system;, features a modification of the amino acid from P to L at position 133.
+The protein's natural variant, known as in DEE51; decreased protein abundance; strong decrease in malate dehydrogenase activity; severe defects in aerobic respiration, when assayed in a heterologous system;, features a modification of the amino acid from P to L at position 207.
+The natural variant of this protein is characterized by an amino acid alteration from S to T at position 91.
+The natural variant of this protein is characterized by an amino acid alteration from M to I at position 59.
+The natural variant of this protein is characterized by an amino acid alteration from T to A at position 4.
+The protein's natural variant, known as in strain: ECOR 70, features a modification of the amino acid from Y to I at position 43.
+The protein's natural variant, known as in strain: E830587, features a modification of the amino acid from G to D at position 266.
+The protein's natural variant, known as in strain: E2666-74, features a modification of the amino acid from E to A at position 267.
+The protein's natural variant, known as found in a patient with Parkinson disease;, features a modification of the amino acid from I to M at position 241.
+The protein's natural variant, known as found in a patient with Parkinson disease;, features a modification of the amino acid from P to S at position 316.
+The protein's natural variant, known as found in a consanguineous family with intellectual disability; unknown pathological significance, features a modification of the amino acid from Q to P at position 469.
+The protein's natural variant, known as found in a patient with Parkinson disease;, features a modification of the amino acid from R to W at position 524.
+The protein's natural variant, known as in PARK17; decreases interaction with WASHC2C, FKBP15 and the WASH complex; impairs recruitment of the WASH complex to endosomes; shows reduced retrograde transport of selective cargo between lysosomes and the Golgi apparatus; shows a progressive reduction in neurite length and branching;, features a modification of the amino acid from D to N at position 620.
+The protein's natural variant, known as in CTRCT18;, features a modification of the amino acid from L to P at position 1376.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation, features a modification of the amino acid from E to G at position 150.
+The protein's natural variant, known as in a lung large cell carcinoma sample; somatic mutation;, features a modification of the amino acid from I to M at position 469.
+The protein's natural variant, known as in SRTD20; unknown pathological significance; impairs recruitment of IFT43 to the basal body, but no effect on subcellular location, when tested in a heterologous system;, features a modification of the amino acid from E to A at position 500.
+The protein's natural variant, known as in an ovarian cancer cell line;, features a modification of the amino acid from Q to R at position 438.
+The protein's natural variant, known as in a melanoma cell line, features a modification of the amino acid from S to F at position 460.
+The protein's natural variant, known as in a melanoma cell line, features a modification of the amino acid from N to Y at position 1028.
+The protein's natural variant, known as found in a renal cell carcinoma sample; somatic mutation, features a modification of the amino acid from V to D at position 1222.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from K to R at position 179.
+The protein's natural variant, known as detected only in flower DNA, features a modification of the amino acid from N to D at position 70.
+The protein's natural variant, known as detected only in flower DNA, features a modification of the amino acid from K to T at position 138.
+The protein's natural variant, known as detected only in flower DNA, features a modification of the amino acid from K to R at position 321.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation; abolishes strongly phosphorylation, features a modification of the amino acid from Q to H at position 5.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation; reduces interaction with ZNF385A, features a modification of the amino acid from S to L at position 6.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from D to H at position 7.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from P to S at position 8.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from V to I at position 10.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from E to K at position 11.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from E to Q at position 11.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from S to R at position 15.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from Q to L at position 16.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from E to D at position 17.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from K to N at position 24.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from E to A at position 28.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from NN to KD at position 30.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from V to I at position 31.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from S to T at position 33.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from P to L at position 34.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from L to F at position 35.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from P to L at position 36.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from S to P at position 37.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from S to T at position 37.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from A to P at position 39.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from A to V at position 39.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from D to Y at position 42.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from L to S at position 43.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from M to I at position 44.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from M to T at position 44.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from M to V at position 44.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from L to M at position 45.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from S to F at position 46.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from S to P at position 46.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from P to L at position 47.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from D to G at position 48.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from D to H at position 49.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from D to N at position 49.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from D to Y at position 49.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from Q to H at position 52.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from W to C at position 53.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from W to G at position 53.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from F to L at position 54.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from F to Y at position 54.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from E to K at position 56.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from E to V at position 56.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from P to Q at position 58.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from P to T at position 58.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from G to C at position 59.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from G to D at position 59.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from G to N at position 59.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from P to L at position 60.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from P to Q at position 60.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from P to S at position 60.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from D to G at position 61.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from D to N at position 61.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from E to D at position 62.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from A to T at position 63.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from A to V at position 63.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from R to T at position 65.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from M to I at position 66.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from M to R at position 66.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from P to L at position 67.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from P to R at position 67.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from P to S at position 67.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from E to G at position 68.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from E to Q at position 68.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from A to D at position 69.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from A to G at position 69.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from A to T at position 69.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from A to V at position 69.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from A to T at position 70.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from P to T at position 71.
+The protein's natural variant, known as in sporadic cancers; somatic mutation; requires 2 nucleotide substitutions;, features a modification of the amino acid from P to C at position 72.
+The protein's natural variant, known as in sporadic cancers; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from P to G at position 72.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from P to H at position 72.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from P to L at position 72.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from V to E at position 73.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from V to L at position 73.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from V to M at position 73.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from A to T at position 74.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from P to L at position 75.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from P to R at position 75.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from P to S at position 75.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from A to G at position 76.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from A to T at position 76.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from P to A at position 77.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from A to V at position 78.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from A to G at position 79.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from A to T at position 79.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from A to V at position 79.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from P to L at position 80.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from P to S at position 80.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from T to I at position 81.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from P to L at position 82.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from P to S at position 82.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from A to E at position 83.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from A to V at position 83.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from A to G at position 84.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from A to V at position 84.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from P to L at position 85.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from P to S at position 85.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from A to V at position 86.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from P to Q at position 87.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from A to T at position 88.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from A to V at position 88.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from P to L at position 89.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from P to S at position 89.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from S to F at position 90.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from S to Y at position 90.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from W to C at position 91.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from P to A at position 92.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from P to L at position 92.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from P to S at position 92.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from L to M at position 93.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from L to P at position 93.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from S to L at position 94.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from S to T at position 94.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from S to F at position 95.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from S to T at position 95.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from S to C at position 96.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from S to F at position 96.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from S to P at position 96.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from V to A at position 97.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from V to F at position 97.
+The protein's natural variant, known as in familial cancer not matching LFS; germline mutation and in a sporadic cancer; somatic mutation;, features a modification of the amino acid from V to I at position 97.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from P to L at position 98.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from P to S at position 98.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from S to F at position 99.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from S to P at position 99.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from Q to R at position 100.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from K to N at position 101.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from K to R at position 101.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from T to I at position 102.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from Q to H at position 104.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from Q to L at position 104.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation, features a modification of the amino acid from G to C at position 105.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from G to D at position 105.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from G to R at position 105.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from G to S at position 105.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from G to V at position 105.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from S to G at position 106.
+The protein's natural variant, known as in a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from S to R at position 106.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from Y to C at position 107.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from Y to D at position 107.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from Y to H at position 107.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from G to D at position 108.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from G to S at position 108.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from F to C at position 109.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from F to L at position 109.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from F to S at position 109.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to C at position 110.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from R to G at position 110.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to H at position 110.
+The protein's natural variant, known as in a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation; does not induce SNAI1 degradation;, features a modification of the amino acid from R to L at position 110.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to P at position 110.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from R to S at position 110.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from L to M at position 111.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from L to P at position 111.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from L to Q at position 111.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from L to R at position 111.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from G to D at position 112.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from G to S at position 112.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from F to C at position 113.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from F to G at position 113.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from F to I at position 113.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from F to L at position 113.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from F to S at position 113.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from F to V at position 113.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from H to Y at position 115.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from S to C at position 116.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from S to F at position 116.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from S to P at position 116.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from G to E at position 117.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from G to R at position 117.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from T to A at position 118.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from T to I at position 118.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from T to R at position 118.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from A to D at position 119.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from A to T at position 119.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from K to E at position 120.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from K to M at position 120.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from K to Q at position 120.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from K to R at position 120.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from S to F at position 121.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from V to L at position 122.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from T to I at position 123.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from T to N at position 123.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from C to G at position 124.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from C to R at position 124.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from C to S at position 124.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from C to W at position 124.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from C to Y at position 124.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from T to A at position 125.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from T to K at position 125.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from T to M at position 125.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from T to P at position 125.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from T to R at position 125.
+The protein's natural variant, known as in a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from Y to C at position 126.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from Y to D at position 126.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from Y to F at position 126.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from Y to G at position 126.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from Y to H at position 126.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from Y to N at position 126.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from Y to S at position 126.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from S to C at position 127.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from S to F at position 127.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from S to P at position 127.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from S to T at position 127.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from S to Y at position 127.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from P to A at position 128.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from P to L at position 128.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from P to R at position 128.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from P to S at position 128.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from A to D at position 129.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from A to G at position 129.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from A to T at position 129.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from A to V at position 129.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from L to F at position 130.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from L to H at position 130.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from L to I at position 130.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from L to P at position 130.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from L to R at position 130.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from L to V at position 130.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from N to D at position 131.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from N to H at position 131.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from N to I at position 131.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from N to K at position 131.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from N to S at position 131.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from N to T at position 131.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from N to Y at position 131.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from KM to NL at position 133.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from K to E at position 132.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from K to L at position 132.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from K to M at position 132.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from K to N at position 132.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from K to Q at position 132.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from K to R at position 132.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from K to T at position 132.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from K to W at position 132.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from M to I at position 133.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from M to K at position 133.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from M to L at position 133.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation, features a modification of the amino acid from M to R at position 133.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from M to T at position 133.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from M to V at position 133.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from F to C at position 134.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from F to I at position 134.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from F to L at position 134.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from F to S at position 134.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from F to V at position 134.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from C to F at position 135.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from C to G at position 135.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from C to R at position 135.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from C to S at position 135.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from C to T at position 135.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from C to W at position 135.
+The protein's natural variant, known as in sporadic cancers; somatic mutation; decreased E6-mediated binding to E6-AP;, features a modification of the amino acid from C to Y at position 135.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from Q to E at position 136.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from Q to H at position 136.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from Q to K at position 136.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from Q to P at position 136.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from Q to R at position 136.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from L to M at position 137.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from L to P at position 137.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from L to Q at position 137.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from L to V at position 137.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from A to D at position 138.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from A to P at position 138.
+The protein's natural variant, known as in LFS; germline mutation, features a modification of the amino acid from A to S at position 138.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from A to T at position 138.
+The protein's natural variant, known as in sporadic cancers; somatic mutation; no effect on susceptibility to calpain;, features a modification of the amino acid from A to V at position 138.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from K to E at position 139.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from K to N at position 139.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from K to Q at position 139.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from K to R at position 139.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from K to T at position 139.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from T to A at position 140.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from T to I at position 140.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from T to N at position 140.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from T to P at position 140.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from T to S at position 140.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from C to A at position 141.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from C to F at position 141.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from C to G at position 141.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from C to R at position 141.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from C to S at position 141.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from C to W at position 141.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from C to Y at position 141.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from P to A at position 142.
+The protein's natural variant, known as in sporadic cancers; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from P to F at position 142.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from P to H at position 142.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from P to L at position 142.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from P to R at position 142.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from P to S at position 142.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from P to T at position 142.
+The protein's natural variant, known as in sporadic cancers; somatic mutation; strong DNA binding ability at 32.5 degrees Celsius; strong reduction of transcriptional activity at 37.5 degrees Celsius; severely represses interaction with ZNF385A, features a modification of the amino acid from V to A at position 143.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from V to E at position 143.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from V to G at position 143.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from V to L at position 143.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from V to M at position 143.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from Q to H at position 144.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from Q to K at position 144.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from Q to L at position 144.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from Q to P at position 144.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from Q to R at position 144.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from L to M at position 145.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from L to P at position 145.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from L to Q at position 145.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from L to R at position 145.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from L to V at position 145.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from W to C at position 146.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from W to G at position 146.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from W to L at position 146.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from W to R at position 146.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from W to S at position 146.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from V to A at position 147.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from V to D at position 147.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from V to E at position 147.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from V to F at position 147.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from V to G at position 147.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from V to I at position 147.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from D to A at position 148.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from D to E at position 148.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from D to G at position 148.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from D to N at position 148.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from D to V at position 148.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from D to Y at position 148.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from S to F at position 149.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from S to P at position 149.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from S to T at position 149.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from T to A at position 150.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from T to I at position 150.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from T to K at position 150.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from T to N at position 150.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from T to P at position 150.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from T to R at position 150.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from P to A at position 151.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from P to H at position 151.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from P to L at position 151.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from P to R at position 151.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from P to S at position 151.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from P to T at position 151.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from P to A at position 152.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from P to L at position 152.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from P to Q at position 152.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from P to R at position 152.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from P to S at position 152.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from P to T at position 152.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from P to A at position 153.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from P to F at position 153.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from P to H at position 153.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from P to L at position 153.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from P to R at position 153.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from P to S at position 153.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from P to T at position 153.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from G to A at position 154.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from G to C at position 154.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from G to D at position 154.
+The protein's natural variant, known as in sporadic cancers; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from G to I at position 154.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from G to S at position 154.
+The protein's natural variant, known as in a brain tumor with no family history; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from G to V at position 154.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from T to A at position 155.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from T to I at position 155.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from T to M at position 155.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from T to N at position 155.
+The protein's natural variant, known as in sporadic cancers; somatic mutation; does not induce SNAI1 degradation, features a modification of the amino acid from T to P at position 155.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from T to S at position 155.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to C at position 156.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from R to G at position 156.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to H at position 156.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from R to L at position 156.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from R to P at position 156.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from R to S at position 156.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from V to A at position 157.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from V to D at position 157.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from V to F at position 157.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from V to G at position 157.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from V to I at position 157.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from V to L at position 157.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to C at position 158.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from R to F at position 158.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation, features a modification of the amino acid from R to G at position 158.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to H at position 158.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from R to L at position 158.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to P at position 158.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from R to Q at position 158.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from R to S at position 158.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from R to Y at position 158.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from A to D at position 159.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation; requires 2 nucleotide substitutions;, features a modification of the amino acid from A to F at position 159.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from A to G at position 159.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from A to P at position 159.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from A to S at position 159.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from A to T at position 159.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from A to V at position 159.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from MA to IP at position 161.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from MA to IS at position 161.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from MA to IT at position 161.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from M to I at position 160.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from M to K at position 160.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from M to T at position 160.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from M to V at position 160.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from A to D at position 161.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from A to F at position 161.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from A to G at position 161.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from A to P at position 161.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from A to S at position 161.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from A to T at position 161.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from A to V at position 161.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from I to F at position 162.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from I to M at position 162.
+The protein's natural variant, known as in a breast cancer with no family history; germline mutation and in sporadic cancers; somatic mutation, features a modification of the amino acid from I to N at position 162.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from I to S at position 162.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from I to T at position 162.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from I to V at position 162.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from Y to C at position 163.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from Y to D at position 163.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from Y to F at position 163.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from Y to H at position 163.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from Y to N at position 163.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from Y to S at position 163.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from K to E at position 164.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from K to M at position 164.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from K to N at position 164.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from K to Q at position 164.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from K to R at position 164.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from K to T at position 164.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from Q to E at position 165.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from Q to H at position 165.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from Q to L at position 165.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from Q to P at position 165.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from Q to R at position 165.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from S to A at position 166.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from S to G at position 166.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from S to L at position 166.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from S to P at position 166.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from S to T at position 166.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from QH to HD at position 168.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from QH to YL at position 168.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from Q to H at position 167.
+The protein's natural variant, known as in LFS; germline mutation and in a sporadic cancer; somatic mutation, features a modification of the amino acid from Q to K at position 167.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from Q to L at position 167.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from Q to R at position 167.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from HM to LI at position 169.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from H to D at position 168.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from H to L at position 168.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from H to N at position 168.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from H to P at position 168.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from H to Q at position 168.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from H to R at position 168.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from H to V at position 168.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from H to Y at position 168.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from MT to IS at position 170.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from M to I at position 169.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from M to K at position 169.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from M to T at position 169.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from M to V at position 169.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from T to A at position 170.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from T to K at position 170.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from T to M at position 170.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from T to P at position 170.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from T to S at position 170.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from E to A at position 171.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from E to D at position 171.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from E to G at position 171.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from E to K at position 171.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from E to Q at position 171.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from E to V at position 171.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from V to A at position 172.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from V to D at position 172.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from V to F at position 172.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from V to G at position 172.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from V to I at position 172.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from V to A at position 173.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from V to E at position 173.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from V to G at position 173.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from V to L at position 173.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from V to M at position 173.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from V to W at position 173.
+The protein's natural variant, known as in LFS; germline mutation and in a sporadic cancer; somatic mutation;, features a modification of the amino acid from R to G at position 174.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to K at position 174.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from R to M at position 174.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from R to S at position 174.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from R to T at position 174.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from R to W at position 174.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to C at position 175.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to G at position 175.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation; does not induce SNAI1 degradation; reduces interaction with ZNF385A; loss of susceptibility to calpain;, features a modification of the amino acid from R to H at position 175.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to L at position 175.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from R to P at position 175.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from R to Q at position 175.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from R to S at position 175.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from CP to FS at position 177.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from C to F at position 176.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from C to G at position 176.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from C to R at position 176.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from C to S at position 176.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from C to W at position 176.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from C to Y at position 176.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from P to A at position 177.
+The protein's natural variant, known as in sporadic cancers; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from P to F at position 177.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from P to H at position 177.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from P to I at position 177.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from P to L at position 177.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from P to R at position 177.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from P to S at position 177.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from P to T at position 177.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from HH to QS at position 179.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from H to D at position 178.
+The protein's natural variant, known as in a Burkitt lymphoma, features a modification of the amino acid from H to HPHP at position 178.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from H to L at position 178.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from H to N at position 178.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from H to P at position 178.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from H to Q at position 178.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from H to R at position 178.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from H to Y at position 178.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from H to D at position 179.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from H to L at position 179.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from H to N at position 179.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from H to P at position 179.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from H to Q at position 179.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from H to R at position 179.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from H to Y at position 179.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from E to A at position 180.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from E to D at position 180.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from E to G at position 180.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from E to K at position 180.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from E to Q at position 180.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from E to V at position 180.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to C at position 181.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from R to G at position 181.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to H at position 181.
+The protein's natural variant, known as in a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to L at position 181.
+The protein's natural variant, known as in a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation, features a modification of the amino acid from R to P at position 181.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to S at position 181.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from C to R at position 182.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from C to S at position 182.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from C to Y at position 182.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from S to L at position 183.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from S to P at position 183.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from D to G at position 184.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from D to H at position 184.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from D to N at position 184.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from D to V at position 184.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from D to Y at position 184.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from S to C at position 185.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from S to G at position 185.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from S to I at position 185.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from S to N at position 185.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from S to R at position 185.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from S to T at position 185.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from D to E at position 186.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from D to G at position 186.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from D to H at position 186.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from D to N at position 186.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from D to V at position 186.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from D to Y at position 186.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from G to C at position 187.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from G to D at position 187.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from G to N at position 187.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from G to R at position 187.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from G to S at position 187.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from G to V at position 187.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from L to P at position 188.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from L to V at position 188.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from A to D at position 189.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from A to G at position 189.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from A to P at position 189.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from A to S at position 189.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from A to T at position 189.
+The protein's natural variant, known as in a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from A to V at position 189.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from P to A at position 190.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from P to H at position 190.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from P to L at position 190.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from P to R at position 190.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from P to S at position 190.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from P to T at position 190.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from P to H at position 191.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from P to L at position 191.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from P to R at position 191.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from P to S at position 191.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from P to T at position 191.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from QH to HN at position 193.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from QH to HY at position 193.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from Q to H at position 192.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from Q to K at position 192.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from Q to L at position 192.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from Q to P at position 192.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from Q to R at position 192.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from H to D at position 193.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from H to L at position 193.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from H to N at position 193.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from H to P at position 193.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from H to Q at position 193.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from H to R at position 193.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from H to Y at position 193.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from L to F at position 194.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from L to H at position 194.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from L to I at position 194.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from L to P at position 194.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from L to R at position 194.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from L to V at position 194.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from I to F at position 195.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from I to L at position 195.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from I to N at position 195.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from I to S at position 195.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from I to T at position 195.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from I to V at position 195.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from I to Y at position 195.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to G at position 196.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to L at position 196.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to P at position 196.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to Q at position 196.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from R to S at position 196.
+The protein's natural variant, known as in a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation, features a modification of the amino acid from V to E at position 197.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from V to G at position 197.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from V to L at position 197.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from V to M at position 197.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from E to D at position 198.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from E to G at position 198.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from E to K at position 198.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from E to Q at position 198.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from E to V at position 198.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from G to A at position 199.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from G to E at position 199.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from G to R at position 199.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from G to V at position 199.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from N to D at position 200.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from N to I at position 200.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from N to K at position 200.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from N to P at position 200.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from N to S at position 200.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from N to T at position 200.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from LR to FC at position 202.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from L to F at position 201.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from L to P at position 201.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from L to S at position 201.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to C at position 202.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to G at position 202.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to H at position 202.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to L at position 202.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from R to P at position 202.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from R to S at position 202.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from VE to LV at position 204.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from V to A at position 203.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from V to E at position 203.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from V to L at position 203.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from V to M at position 203.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from V to W at position 203.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from E to A at position 204.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from E to D at position 204.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from E to G at position 204.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from E to K at position 204.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from E to Q at position 204.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from E to V at position 204.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from Y to C at position 205.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from Y to D at position 205.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from Y to F at position 205.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from Y to H at position 205.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from Y to N at position 205.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from Y to S at position 205.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from L to F at position 206.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from L to M at position 206.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from DD to EY at position 208.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from D to E at position 207.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from D to G at position 207.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from D to H at position 207.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from D to N at position 207.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from D to V at position 207.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from D to Y at position 207.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from D to E at position 208.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from D to G at position 208.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from D to H at position 208.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from D to I at position 208.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from D to N at position 208.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from D to V at position 208.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from D to Y at position 208.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from R to I at position 209.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from R to K at position 209.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from R to S at position 209.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from R to T at position 209.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from N to D at position 210.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from N to H at position 210.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from N to I at position 210.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from N to K at position 210.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from N to S at position 210.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from N to T at position 210.
+The protein's natural variant, known as in a familial cancer not matching LFS; germline mutation;, features a modification of the amino acid from N to Y at position 210.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from T to A at position 211.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from T to I at position 211.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from T to N at position 211.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from T to P at position 211.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from T to S at position 211.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from F to I at position 212.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from F to L at position 212.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from F to S at position 212.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from F to V at position 212.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from F to Y at position 212.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to G at position 213.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to L at position 213.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to P at position 213.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to Q at position 213.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from R to W at position 213.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from H to D at position 214.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from H to P at position 214.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from H to Q at position 214.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from H to R at position 214.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from H to Y at position 214.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from S to C at position 215.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from S to G at position 215.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from S to I at position 215.
+The protein's natural variant, known as in sporadic cancers; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from S to K at position 215.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from S to N at position 215.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from S to R at position 215.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from S to T at position 215.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from V to A at position 216.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from V to E at position 216.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from V to G at position 216.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from V to L at position 216.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from V to M at position 216.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from V to W at position 216.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from V to A at position 217.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from V to E at position 217.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from V to G at position 217.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from V to I at position 217.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from V to L at position 217.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from V to A at position 218.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from V to E at position 218.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from V to G at position 218.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from V to L at position 218.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from V to M at position 218.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from P to C at position 219.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from P to H at position 219.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from P to L at position 219.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from P to R at position 219.
+The protein's natural variant, known as in a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from P to S at position 219.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from P to T at position 219.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from Y to C at position 220.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from Y to D at position 220.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from Y to F at position 220.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from Y to H at position 220.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from Y to N at position 220.
+The protein's natural variant, known as in a brain tumor with no family history; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from Y to S at position 220.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from E to A at position 221.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from E to D at position 221.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from E to G at position 221.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from E to K at position 221.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from E to Q at position 221.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from P to A at position 222.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from P to L at position 222.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from P to Q at position 222.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from P to R at position 222.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from P to S at position 222.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from P to T at position 222.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from P to A at position 223.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from P to H at position 223.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from P to L at position 223.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from P to R at position 223.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from P to S at position 223.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from P to T at position 223.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from E to D at position 224.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from E to G at position 224.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from E to K at position 224.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from E to V at position 224.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from V to A at position 225.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from V to D at position 225.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from V to F at position 225.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from V to G at position 225.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from V to I at position 225.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from V to L at position 225.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from G to A at position 226.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from G to D at position 226.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from G to N at position 226.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from G to S at position 226.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from G to V at position 226.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from S to C at position 227.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from S to F at position 227.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from S to P at position 227.
+The protein's natural variant, known as in LFS; germline mutation and in a sporadic cancer; somatic mutation, features a modification of the amino acid from S to T at position 227.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from D to A at position 228.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from D to E at position 228.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from D to G at position 228.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from D to H at position 228.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from D to N at position 228.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from D to P at position 228.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from D to V at position 228.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from D to Y at position 228.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from C to G at position 229.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from C to N at position 229.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from C to R at position 229.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from C to S at position 229.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from C to Y at position 229.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from T to A at position 230.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from T to I at position 230.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from T to N at position 230.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from T to P at position 230.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from T to S at position 230.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from T to A at position 231.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from T to I at position 231.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from T to N at position 231.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from T to S at position 231.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from I to F at position 232.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from I to L at position 232.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from I to N at position 232.
+The protein's natural variant, known as in sporadic cancers; somatic mutation; does not induce SNAI1 degradation, features a modification of the amino acid from I to S at position 232.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from I to T at position 232.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from I to V at position 232.
+The protein's natural variant, known as in LFS; germline mutation and in a sporadic cancer; somatic mutation, features a modification of the amino acid from H to D at position 233.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from H to L at position 233.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from H to P at position 233.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from H to Q at position 233.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from H to R at position 233.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from H to Y at position 233.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from Y to C at position 234.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from Y to D at position 234.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from Y to F at position 234.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from Y to H at position 234.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from Y to K at position 234.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from Y to N at position 234.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from Y to Q at position 234.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from Y to S at position 234.
+The protein's natural variant, known as in an adrenocortical carcinoma with no family history; germline mutation and in sporadic cancers; somatic mutation, features a modification of the amino acid from N to D at position 235.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from N to H at position 235.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from N to I at position 235.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from N to M at position 235.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from N to S at position 235.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from N to T at position 235.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from N to Y at position 235.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from Y to C at position 236.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from Y to D at position 236.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from Y to F at position 236.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from Y to H at position 236.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from Y to N at position 236.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from Y to S at position 236.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation; no effect on susceptibility to calpain;, features a modification of the amino acid from M to I at position 237.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from M to K at position 237.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from M to L at position 237.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from M to R at position 237.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from M to T at position 237.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from M to V at position 237.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from C to F at position 238.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from C to G at position 238.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from C to H at position 238.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from C to R at position 238.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from C to S at position 238.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from C to W at position 238.
+The protein's natural variant, known as in a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from C to Y at position 238.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from N to D at position 239.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from N to H at position 239.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from N to I at position 239.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from N to K at position 239.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from N to S at position 239.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from N to T at position 239.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from N to Y at position 239.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from S to C at position 240.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from S to G at position 240.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from S to I at position 240.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from S to N at position 240.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from S to P at position 240.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from S to R at position 240.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from S to T at position 240.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from S to A at position 241.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from S to C at position 241.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from S to F at position 241.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from S to P at position 241.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation, features a modification of the amino acid from S to T at position 241.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from S to Y at position 241.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from C to F at position 242.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from C to G at position 242.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from C to R at position 242.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from C to S at position 242.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from C to W at position 242.
+The protein's natural variant, known as in a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from C to Y at position 242.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from MG to IC at position 244.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from MG to IS at position 244.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from M to I at position 243.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from M to K at position 243.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from M to L at position 243.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from M to R at position 243.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from M to T at position 243.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from M to V at position 243.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from G to A at position 244.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from G to C at position 244.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from G to D at position 244.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from G to E at position 244.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from G to R at position 244.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from G to S at position 244.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from G to V at position 244.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from G to A at position 245.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from G to C at position 245.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from G to D at position 245.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from G to E at position 245.
+The protein's natural variant, known as in sporadic cancers; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from G to F at position 245.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from G to H at position 245.
+The protein's natural variant, known as in sporadic cancers; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from G to L at position 245.
+The protein's natural variant, known as in sporadic cancers; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from G to N at position 245.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from G to R at position 245.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from G to S at position 245.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from G to V at position 245.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from M to I at position 246.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from M to K at position 246.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from M to L at position 246.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from M to R at position 246.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from M to T at position 246.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from M to V at position 246.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from NR to IP at position 248.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from NR to KW at position 248.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from N to D at position 247.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from N to F at position 247.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from N to I at position 247.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from N to K at position 247.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from N to S at position 247.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from N to T at position 247.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from N to Y at position 247.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from R to C at position 248.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to G at position 248.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to L at position 248.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to P at position 248.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to Q at position 248.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation; no effect on susceptibility to calpain;, features a modification of the amino acid from R to W at position 248.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from RP to SA at position 250.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from RP to SS at position 250.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to G at position 249.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from R to I at position 249.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to K at position 249.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to M at position 249.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from R to N at position 249.
+The protein's natural variant, known as in sporadic cancers; somatic mutation; does not induce SNAI1 degradation;, features a modification of the amino acid from R to S at position 249.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to T at position 249.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to W at position 249.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from P to A at position 250.
+The protein's natural variant, known as in sporadic cancers; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from P to F at position 250.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from P to H at position 250.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from P to L at position 250.
+The protein's natural variant, known as in sporadic cancers; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from P to N at position 250.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from P to Q at position 250.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from P to S at position 250.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from P to T at position 250.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from I to F at position 251.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from I to L at position 251.
+The protein's natural variant, known as in LFS; germline mutation;, features a modification of the amino acid from I to M at position 251.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from I to N at position 251.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from I to S at position 251.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from I to T at position 251.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from I to V at position 251.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from L to F at position 252.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from L to H at position 252.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from L to I at position 252.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from L to P at position 252.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from L to V at position 252.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from T to A at position 253.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from T to I at position 253.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from T to N at position 253.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from T to P at position 253.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from T to S at position 253.
+The protein's natural variant, known as in sporadic cancers; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from I to D at position 254.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from I to F at position 254.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from I to L at position 254.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from I to M at position 254.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from I to N at position 254.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from I to S at position 254.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from I to T at position 254.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from I to V at position 254.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from I to F at position 255.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from I to M at position 255.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from I to N at position 255.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from I to S at position 255.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from I to T at position 255.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from I to V at position 255.
+The protein's natural variant, known as in a brain tumor with no family history; germline mutation and in sporadic cancers; somatic mutation, features a modification of the amino acid from T to I at position 256.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from T to K at position 256.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from T to P at position 256.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from T to S at position 256.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from L to P at position 257.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from L to Q at position 257.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from L to R at position 257.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from L to V at position 257.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from E to A at position 258.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from E to D at position 258.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from E to G at position 258.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from E to K at position 258.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from E to L at position 258.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from E to Q at position 258.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from E to V at position 258.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from D to A at position 259.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from D to E at position 259.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from D to G at position 259.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from D to H at position 259.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from D to N at position 259.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from D to P at position 259.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from D to S at position 259.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from D to V at position 259.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from D to Y at position 259.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from S to A at position 260.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from S to C at position 260.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from S to F at position 260.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from S to P at position 260.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from S to T at position 260.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from S to Y at position 260.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from S to C at position 261.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from S to G at position 261.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from S to I at position 261.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from S to N at position 261.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from S to R at position 261.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from GN to PD at position 263.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from G to C at position 262.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from G to D at position 262.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from G to H at position 262.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from G to S at position 262.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from G to V at position 262.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from N to D at position 263.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from N to H at position 263.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from N to I at position 263.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from N to K at position 263.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from N to S at position 263.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from L to I at position 264.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from L to P at position 264.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from L to Q at position 264.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from L to R at position 264.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from L to V at position 264.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from L to M at position 265.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from L to P at position 265.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from L to Q at position 265.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from L to R at position 265.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from G to A at position 266.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from G to E at position 266.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from G to R at position 266.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from G to V at position 266.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from R to G at position 267.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from R to H at position 267.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to P at position 267.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to Q at position 267.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to W at position 267.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from N to F at position 268.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from N to H at position 268.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from N to I at position 268.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from N to K at position 268.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from N to S at position 268.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from N to Y at position 268.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from S to C at position 269.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from S to G at position 269.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from S to I at position 269.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from S to N at position 269.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from S to R at position 269.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from S to T at position 269.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from F to C at position 270.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from F to I at position 270.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from F to L at position 270.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from F to S at position 270.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from F to V at position 270.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from F to Y at position 270.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from E to A at position 271.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from E to D at position 271.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from E to G at position 271.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from E to K at position 271.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from E to P at position 271.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from E to Q at position 271.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from E to R at position 271.
+The protein's natural variant, known as in an osteosarcoma with no family history; germline mutation and in sporadic cancers; somatic mutation, features a modification of the amino acid from E to V at position 271.
+The protein's natural variant, known as in a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation, features a modification of the amino acid from V to A at position 272.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from V to E at position 272.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from V to G at position 272.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from V to L at position 272.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from V to M at position 272.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to C at position 273.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation, features a modification of the amino acid from R to G at position 273.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation; abolishes sequence-specific DNA binding; does not induce SNAI1 degradation;, features a modification of the amino acid from R to H at position 273.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to L at position 273.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from R to N at position 273.
+The protein's natural variant, known as in sporadic cancers; somatic mutation; no effect on susceptibility to calpain;, features a modification of the amino acid from R to P at position 273.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from R to Q at position 273.
+The protein's natural variant, known as in a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to S at position 273.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from R to Y at position 273.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from V to A at position 274.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from V to D at position 274.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from V to F at position 274.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from V to G at position 274.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from V to I at position 274.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from V to L at position 274.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from C to F at position 275.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from C to G at position 275.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from C to R at position 275.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from C to S at position 275.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from C to W at position 275.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from C to Y at position 275.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from A to D at position 276.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from A to G at position 276.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from A to P at position 276.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from A to S at position 276.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from A to T at position 276.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from A to V at position 276.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from C to F at position 277.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from C to G at position 277.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from C to R at position 277.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from C to S at position 277.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from C to W at position 277.
+The protein's natural variant, known as in an osteosarcoma with no family history; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from C to Y at position 277.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from P to A at position 278.
+The protein's natural variant, known as in sporadic cancers; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from P to F at position 278.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from P to H at position 278.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from P to L at position 278.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from P to R at position 278.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from P to S at position 278.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from P to T at position 278.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from G to E at position 279.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from G to R at position 279.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from G to V at position 279.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from G to W at position 279.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to G at position 280.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to I at position 280.
+The protein's natural variant, known as in a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation; no effect on interaction with CCAR2;, features a modification of the amino acid from R to K at position 280.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from R to P at position 280.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from R to S at position 280.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to T at position 280.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from DR to EW at position 282.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from D to A at position 281.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from D to E at position 281.
+The protein's natural variant, known as in a brain tumor with no family history; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from D to G at position 281.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from D to H at position 281.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from D to N at position 281.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from D to R at position 281.
+The protein's natural variant, known as in a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from D to V at position 281.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from D to Y at position 281.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to G at position 282.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from R to H at position 282.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to L at position 282.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to P at position 282.
+The protein's natural variant, known as in a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to Q at position 282.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation; does not induce SNAI1 degradation;, features a modification of the amino acid from R to W at position 282.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to C at position 283.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from R to G at position 283.
+The protein's natural variant, known as in a brain tumor with no family history; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to H at position 283.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from R to L at position 283.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from R to P at position 283.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from R to S at position 283.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from T to A at position 284.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from T to I at position 284.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from T to K at position 284.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from T to P at position 284.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from E to A at position 285.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from E to D at position 285.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from E to G at position 285.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from E to K at position 285.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation, features a modification of the amino acid from E to Q at position 285.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from E to V at position 285.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from E to A at position 286.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from E to D at position 286.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from E to G at position 286.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from E to K at position 286.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from E to L at position 286.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from E to Q at position 286.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from E to V at position 286.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from E to A at position 287.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from E to D at position 287.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from E to G at position 287.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from E to K at position 287.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from E to V at position 287.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from N to D at position 288.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from N to K at position 288.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from N to S at position 288.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from N to T at position 288.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from N to Y at position 288.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from L to F at position 289.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from L to H at position 289.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from L to P at position 289.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from L to R at position 289.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from L to V at position 289.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to C at position 290.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to H at position 290.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation, features a modification of the amino acid from R to L at position 290.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from K to E at position 291.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from K to M at position 291.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from K to N at position 291.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from K to Q at position 291.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from K to R at position 291.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from K to T at position 291.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from K to E at position 292.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from K to G at position 292.
+The protein's natural variant, known as in LFS; germline mutation and in a sporadic cancer; somatic mutation;, features a modification of the amino acid from K to I at position 292.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from K to N at position 292.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from K to Q at position 292.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from K to R at position 292.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from K to T at position 292.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from G to A at position 293.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from G to R at position 293.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from G to V at position 293.
+The protein's natural variant, known as in a brain tumor with no family history; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from G to W at position 293.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from E to A at position 294.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from E to D at position 294.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from E to G at position 294.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from E to K at position 294.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from E to Q at position 294.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from E to V at position 294.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from P to H at position 295.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from P to L at position 295.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from P to R at position 295.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from P to S at position 295.
+The protein's natural variant, known as in sporadic cancers; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from H to C at position 296.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from H to D at position 296.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from H to L at position 296.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from H to N at position 296.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from H to P at position 296.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from H to Q at position 296.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from H to R at position 296.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from H to Y at position 296.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from H to D at position 297.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from H to N at position 297.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from H to P at position 297.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from H to R at position 297.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from H to Y at position 297.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from E to A at position 298.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from E to D at position 298.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from E to K at position 298.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from E to Q at position 298.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from E to V at position 298.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from L to P at position 299.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from L to Q at position 299.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from L to R at position 299.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from L to V at position 299.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from P to A at position 300.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from P to L at position 300.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from P to R at position 300.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from P to S at position 300.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from P to A at position 301.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from P to L at position 301.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from P to Q at position 301.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from P to S at position 301.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from P to T at position 301.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from G to A at position 302.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from G to E at position 302.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from G to R at position 302.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from G to V at position 302.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from S to C at position 303.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from S to I at position 303.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from S to N at position 303.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from S to T at position 303.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from T to A at position 304.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from T to I at position 304.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from T to N at position 304.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from T to S at position 304.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from K to E at position 305.
+The protein's natural variant, known as in a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation, features a modification of the amino acid from K to M at position 305.
+The protein's natural variant, known as in sporadic cancers; somatic mutation; loss of nuclear localization, features a modification of the amino acid from K to N at position 305.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from K to R at position 305.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from K to T at position 305.
+The protein's natural variant, known as in LFS; germline mutation and in a sporadic cancer; somatic mutation, features a modification of the amino acid from R to P at position 306.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to Q at position 306.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from A to P at position 307.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from A to S at position 307.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from A to T at position 307.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from L to M at position 308.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from L to V at position 308.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from P to R at position 309.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from P to S at position 309.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from N to I at position 310.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from N to T at position 310.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from N to H at position 311.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from N to K at position 311.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from N to S at position 311.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from N to T at position 311.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from T to I at position 312.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from T to S at position 312.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from S to C at position 313.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from S to I at position 313.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from S to N at position 313.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from S to R at position 313.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from S to F at position 314.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from S to C at position 315.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from S to F at position 315.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from S to P at position 315.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from P to L at position 316.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from P to T at position 316.
+The protein's natural variant, known as in a kidney cancer with no family history; germline mutation and in a sporadic cancer; somatic mutation;, features a modification of the amino acid from Q to H at position 317.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from Q to K at position 317.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from Q to L at position 317.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from Q to P at position 317.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from Q to R at position 317.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from P to L at position 318.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from K to E at position 319.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from K to N at position 319.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from K to R at position 319.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from K to N at position 320.
+The protein's natural variant, known as in kidney cancer; germline mutation, features a modification of the amino acid from K to E at position 321.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from K to R at position 321.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from P to L at position 322.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from P to R at position 322.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from L to G at position 323.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from L to M at position 323.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from L to P at position 323.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from L to R at position 323.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from L to V at position 323.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from D to E at position 324.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from D to S at position 324.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from D to Y at position 324.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from G to A at position 325.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from G to E at position 325.
+The protein's natural variant, known as in LFS; germline mutation;, features a modification of the amino acid from G to V at position 325.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from E to G at position 326.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from Y to H at position 327.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from Y to S at position 327.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from F to L at position 328.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from F to S at position 328.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from F to V at position 328.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from T to I at position 329.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from T to S at position 329.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from L to H at position 330.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from L to P at position 330.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from L to R at position 330.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from Q to H at position 331.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from Q to P at position 331.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from Q to R at position 331.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from I to V at position 332.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from G to V at position 334.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from G to W at position 334.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from R to G at position 335.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from R to H at position 335.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from R to L at position 335.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to C at position 337.
+The protein's natural variant, known as in LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to H at position 337.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to L at position 337.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to P at position 337.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from F to I at position 338.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from F to L at position 338.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from E to K at position 339.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from E to Q at position 339.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from F to C at position 341.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from R to L at position 342.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to P at position 342.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to Q at position 342.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from E to G at position 343.
+The protein's natural variant, known as in LFS; germline mutation and in a sporadic cancer; somatic mutation;, features a modification of the amino acid from L to P at position 344.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from L to R at position 344.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from E to A at position 346.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from A to G at position 347.
+The protein's natural variant, known as in sporadic cancers; somatic mutation, features a modification of the amino acid from A to T at position 347.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from L to F at position 348.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from L to S at position 348.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from E to D at position 349.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from D to H at position 352.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from A to T at position 353.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from Q to E at position 354.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from Q to K at position 354.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from Q to R at position 354.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from G to A at position 356.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from G to W at position 356.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from E to D at position 358.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from E to K at position 358.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from G to V at position 360.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from R to K at position 363.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from A to P at position 364.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from A to T at position 364.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from A to V at position 364.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from H to R at position 365.
+The protein's natural variant, known as in a familial cancer not matching LFS; germline mutation and in a sporadic cancer; somatic mutation;, features a modification of the amino acid from H to Y at position 365.
+The protein's natural variant, known as in a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation;, features a modification of the amino acid from S to A at position 366.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from K to Q at position 370.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from S to A at position 376.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from S to T at position 376.
+The protein's natural variant, known as in sporadic cancers; somatic mutation;, features a modification of the amino acid from R to H at position 379.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from F to L at position 385.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation;, features a modification of the amino acid from G to W at position 389.
+The protein's natural variant, known as in a sporadic cancer; somatic mutation, features a modification of the amino acid from S to L at position 392.
+The protein's natural variant, known as in CRC; likely involved in disease pathogenesis; shows an increase in lipid kinase activity; may disrupt the interaction between the PI3K-ABD domain and the N-terminal lobe of PI3K/PI4K kinase domain possibly affecting the conformation of the kinase domain;, features a modification of the amino acid from R to H at position 38.
+The protein's natural variant, known as in MCAP;, features a modification of the amino acid from E to K at position 81.
+The protein's natural variant, known as in CLAPO; unknown pathological significance; somatic mutation;, features a modification of the amino acid from F to S at position 83.
+The protein's natural variant, known as in MCAP; also found in a glioblastoma multiforme sample;, features a modification of the amino acid from R to Q at position 88.
+The protein's natural variant, known as in CRC; likely involved in disease pathogenesis; shows an increase in lipid kinase activity;, features a modification of the amino acid from G to V at position 106.
+The protein's natural variant, known as in MCAP; increased phosphatidylinositol 3-kinase signaling; decreased interaction with p85 regulatory subunit; no effect on protein abundance;, features a modification of the amino acid from I to N at position 112.
+The protein's natural variant, known as in CLAPO and MADAC; unknown pathological significance; somatic mutation in CLAPO and MADAC patients, features a modification of the amino acid from R to P at position 115.
+The protein's natural variant, known as in CWS5;, features a modification of the amino acid from G to D at position 118.
+The protein's natural variant, known as in CWS5;, features a modification of the amino acid from E to K at position 135.
+The protein's natural variant, known as in CWS5;, features a modification of the amino acid from E to K at position 218.
+The protein's natural variant, known as found in a cancer sample; unknown pathological significance, features a modification of the amino acid from Y to C at position 343.
+The protein's natural variant, known as in CWS5;, features a modification of the amino acid from V to I at position 356.
+The protein's natural variant, known as in MCAP;, features a modification of the amino acid from G to R at position 364.
+The protein's natural variant, known as in MCAP;, features a modification of the amino acid from E to K at position 365.
+The protein's natural variant, known as in MCAP;, features a modification of the amino acid from C to Y at position 378.
+The protein's natural variant, known as in CWS5;, features a modification of the amino acid from R to K at position 382.
+The protein's natural variant, known as in CLOVE, CRC and CLAPO; unknown pathological significance; somatic mutation in CLAPO patients; shows an increase in lipid kinase activity; may increase the affinity for lipid membranes;, features a modification of the amino acid from C to R at position 420.
+The protein's natural variant, known as in CRC; likely involved in disease pathogenesis; shows an increase in lipid kinase activity; may disrupt the interaction of the C2 PI3K-type domain with the iSH2 region of the p85 regulatory subunit;, features a modification of the amino acid from E to Q at position 453.
+The protein's natural variant, known as in CLOVE, KERSEB, CRC, BC, CLAPO, MADAC and CCM4; also found in glioblastoma multiforme and endometrial carcinoma; somatic mutation; shows an increase in lipid kinase activity; oncogenic in vivo; occurs in the interface between the PI3K helical domain and the nSH2 (N-terminal SH2) region of the p85 regulatory subunit and may reduce the inhibitory effect of p85; requires interaction with RAS to induce cellular transformation;, features a modification of the amino acid from E to K at position 542.
+The protein's natural variant, known as found in an endometrial carcinoma sample; unknown pathological significance;, features a modification of the amino acid from E to Q at position 542.
+The protein's natural variant, known as in BC; unknown pathological significance;, features a modification of the amino acid from E to V at position 542.
+The protein's natural variant, known as in CWS5 and HCC; also found in a glioblastoma multiforme sample;, features a modification of the amino acid from E to A at position 545.
+The protein's natural variant, known as in KERSEB; also found in an endometrial carcinoma sample;, features a modification of the amino acid from E to G at position 545.
+The protein's natural variant, known as in MCAP, KERSEB, CRC and BC; shows an increase in lipid kinase activity; oncogenic in vivo; occurs in the interface between the PI3K helical domain and the nSH2 (N-terminal SH2) region of the p85 regulatory subunit and may reduce the inhibitory effect of p85; requires interaction with RAS to induce cellular transformation; enhances invadopodia-mediated extracellular matrix degradation and invasion in breast cancer cells;, features a modification of the amino acid from E to K at position 545.
+The protein's natural variant, known as in BC; unknown pathological significance;, features a modification of the amino acid from Q to E at position 546.
+The protein's natural variant, known as in OC; unknown pathological significance;, features a modification of the amino acid from Q to K at position 546.
+The protein's natural variant, known as found in an anaplastic astrocytoma sample; unknown pathological significance;, features a modification of the amino acid from Q to P at position 546.
+The protein's natural variant, known as in BC; unknown pathological significance;, features a modification of the amino acid from Q to R at position 546.
+The protein's natural variant, known as in MCAP;, features a modification of the amino acid from E to K at position 726.
+The protein's natural variant, known as in MCAP;, features a modification of the amino acid from G to R at position 914.
+The protein's natural variant, known as found in an endometrial carcinoma sample; unknown pathological significance, features a modification of the amino acid from G to R at position 1007.
+The protein's natural variant, known as in MCAP; also found in an endometrial carcinoma sample;, features a modification of the amino acid from Y to C at position 1021.
+The protein's natural variant, known as found in an endometrial carcinoma sample; unknown pathological significance, features a modification of the amino acid from Y to H at position 1021.
+The protein's natural variant, known as found in a glioblastoma multiforme sample; unknown pathological significance, features a modification of the amino acid from Y to N at position 1021.
+The protein's natural variant, known as in CRC; unknown pathological significance, features a modification of the amino acid from R to Q at position 1023.
+The protein's natural variant, known as in MCAP;, features a modification of the amino acid from T to A at position 1025.
+The protein's natural variant, known as found in a glioblastoma multiforme sample; unknown pathological significance, features a modification of the amino acid from T to N at position 1025.
+The protein's natural variant, known as in MCAP; also found in an endometrial carcinoma sample;, features a modification of the amino acid from A to V at position 1035.
+The protein's natural variant, known as in MCAP and CRC; also found in an endometrial carcinoma sample; shows an increase in lipid kinase activity;, features a modification of the amino acid from M to I at position 1043.
+The protein's natural variant, known as in BC, CLAPO, MADAC and CCM4; somatic mutation;, features a modification of the amino acid from H to L at position 1047.
+The protein's natural variant, known as in CLOVE, KERSEB, CRC, BC, OC, MADAC and CCM4; also found in an endometrial carcinoma sample; somatic mutation; shows an increase in lipid kinase activity; oncogenic in vivo; requires binding to p85 regulatory subunit to induce cellular transformation but not interaction with RAS; may mimic the conformatitonal change triggered by the interaction with RAS; enhances invadopodia-mediated extracellular matrix degradation and invasion in breast cancer cells; may alter the interaction of the PI3K/PI4K kinase domain with the cell membrane;, features a modification of the amino acid from H to R at position 1047.
+The protein's natural variant, known as in MCAP; also found in an endometrial carcinoma sample;, features a modification of the amino acid from H to Y at position 1047.
+The protein's natural variant, known as in MCAP;, features a modification of the amino acid from G to S at position 1049.
+The protein's natural variant, known as found in an endometrial carcinoma sample; unknown pathological significance, features a modification of the amino acid from G to D at position 1050.
+The protein's natural variant, known as found in an endometrial carcinoma sample; unknown pathological significance, features a modification of the amino acid from T to K at position 1052.
+The protein's natural variant, known as found in an endometrial carcinoma sample; unknown pathological significance;, features a modification of the amino acid from H to L at position 1065.
+The protein's natural variant, known as found in brain tumors; unknown pathological significance, features a modification of the amino acid from H to Y at position 1065.
+The protein's natural variant, known as in MC1DN24;, features a modification of the amino acid from L to P at position 64.
+The protein's natural variant, known as in MALNS, features a modification of the amino acid from R to C at position 38.
+The protein's natural variant, known as in MALNS, features a modification of the amino acid from R to P at position 54.
+The protein's natural variant, known as in MALNS;, features a modification of the amino acid from L to P at position 60.
+The protein's natural variant, known as in MALNS, features a modification of the amino acid from R to P at position 116.
+The protein's natural variant, known as in MALNS;, features a modification of the amino acid from R to P at position 121.
+The protein's natural variant, known as in MALNS, features a modification of the amino acid from K to E at position 125.
+The protein's natural variant, known as in strain: cv. An-2, features a modification of the amino acid from E to D at position 395.
+The protein's natural variant, known as in allele DRA*01:01;, features a modification of the amino acid from L to V at position 242.
+The protein's natural variant, known as in a hepatocellular carcinoma sample; somatic mutation, features a modification of the amino acid from S to F at position 306.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from M to I at position 356.
+The protein's natural variant, known as in MCOPS3; unknown pathological significance, features a modification of the amino acid from W to R at position 51.
+The protein's natural variant, known as in MCOPS3; unknown pathological significance;, features a modification of the amino acid from R to P at position 74.
+The protein's natural variant, known as in MCOPS3; unknown pathological significance, features a modification of the amino acid from W to S at position 79.
+The protein's natural variant, known as in a lung squamous cell carcinoma sample; somatic mutation, features a modification of the amino acid from V to L at position 243.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation, features a modification of the amino acid from G to R at position 410.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from E to Q at position 203.
+The protein's natural variant, known as found in individuals with Sd(a-) phenotype;, features a modification of the amino acid from Q to R at position 436.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from P to H at position 459.
+The protein's natural variant, known as found in individuals with Sd(a-) phenotype;, features a modification of the amino acid from C to R at position 466.
+The protein's natural variant, known as found in individuals with Sd(a-) phenotype;, features a modification of the amino acid from R to W at position 523.
+The protein's natural variant, known as in strain: DSM 65, features a modification of the amino acid from A to V at position 40.
+The protein's natural variant, known as in strain: DSM 65, features a modification of the amino acid from D to G at position 70.
+The protein's natural variant, known as in strain: DSM 65, features a modification of the amino acid from A to T at position 74.
+The protein's natural variant, known as in strain: DSM 65, features a modification of the amino acid from E to D at position 79.
+The protein's natural variant, known as in strain: DSM 65, features a modification of the amino acid from Q to R at position 264.
+The protein's natural variant, known as in strain: CC-503, features a modification of the amino acid from R to Q at position 290.
+The protein's natural variant, known as in strain: cv. Wassilewskija, features a modification of the amino acid from S to N at position 93.
+The protein's natural variant, known as in strain: cv. Wassilewskija, features a modification of the amino acid from A to T at position 96.
+The protein's natural variant, known as in strain: cv. Wassilewskija, features a modification of the amino acid from S to W at position 268.
+The protein's natural variant, known as in strain: cv. Wassilewskija, features a modification of the amino acid from Q to P at position 406.
+The protein's natural variant, known as in MTPD, features a modification of the amino acid from G to D at position 59.
+The protein's natural variant, known as in MTPD;, features a modification of the amino acid from R to C at position 61.
+The protein's natural variant, known as in MTPD;, features a modification of the amino acid from R to H at position 61.
+The protein's natural variant, known as in MTPD, features a modification of the amino acid from R to G at position 117.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from A to V at position 119.
+The protein's natural variant, known as in MTPD;, features a modification of the amino acid from L to P at position 121.
+The protein's natural variant, known as in MTPD;, features a modification of the amino acid from T to P at position 133.
+The protein's natural variant, known as in MTPD;, features a modification of the amino acid from D to G at position 242.
+The protein's natural variant, known as in MTPD;, features a modification of the amino acid from R to H at position 247.
+The protein's natural variant, known as in MTPD;, features a modification of the amino acid from D to G at position 263.
+The protein's natural variant, known as in MTPD;, features a modification of the amino acid from G to D at position 280.
+The protein's natural variant, known as in MTPD, features a modification of the amino acid from P to L at position 294.
+The protein's natural variant, known as in MTPD;, features a modification of the amino acid from P to R at position 294.
+The protein's natural variant, known as in MTPD;, features a modification of the amino acid from G to S at position 301.
+The protein's natural variant, known as in MTPD;, features a modification of the amino acid from R to K at position 444.
+The protein's natural variant, known as in colorectal cancer;, features a modification of the amino acid from C to R at position 32.
+The natural variant of this protein is characterized by an amino acid alteration from M to I at position 36.
+The natural variant of this protein is characterized by an amino acid alteration from I to T at position 61.
+The protein's natural variant, known as in LHON; possible rare primary mutation;, features a modification of the amino acid from V to A at position 65.
+The protein's natural variant, known as in CMH16;, features a modification of the amino acid from S to P at position 48.
+The protein's natural variant, known as in CMH16;, features a modification of the amino acid from I to M at position 246.
+The protein's natural variant, known as in CsE9, features a modification of the amino acid from M to I at position 6.
+The protein's natural variant, known as in CsE9, features a modification of the amino acid from K to M at position 38.
+The protein's natural variant, known as in CsE9, features a modification of the amino acid from N to K at position 50.
+The protein's natural variant, known as in URDS;, features a modification of the amino acid from C to G at position 311.
+The natural variant of this protein is characterized by an amino acid alteration from L to M at position 195.
+The natural variant of this protein is characterized by an amino acid alteration from P to L at position 287.
+The natural variant of this protein is characterized by an amino acid alteration from E to K at position 335.
+The natural variant of this protein is characterized by an amino acid alteration from G to A at position 352.
+The natural variant of this protein is characterized by an amino acid alteration from E to K at position 354.
+The protein's natural variant, known as in strain: 357A, 774A and 786A, features a modification of the amino acid from C to G at position 7.
+The protein's natural variant, known as in strain: 357A, 774A and 786A, features a modification of the amino acid from F to L at position 13.
+The protein's natural variant, known as in strain: 868A, features a modification of the amino acid from D to G at position 22.
+The protein's natural variant, known as in strain: 315A, 765A, 822A and 832A, features a modification of the amino acid from A to D at position 39.
+The protein's natural variant, known as in strain: 318A, 319A, 399A and 732A, features a modification of the amino acid from F to L at position 44.
+The protein's natural variant, known as in strain: 306A, 313A, 358A, 359A, 390A, 773A, 813A and 868A, features a modification of the amino acid from K to T at position 54.
+The protein's natural variant, known as in strain: 774A and 786A, features a modification of the amino acid from T to I at position 72.
+The protein's natural variant, known as in strain: 774A and 786A, features a modification of the amino acid from Q to H at position 79.
+The protein's natural variant, known as in strain: 313A, 737A, 820A and 907A, features a modification of the amino acid from K to T at position 92.
+The protein's natural variant, known as in strain: 307A, 318A, 390A, 705A, 707A, 732A, 736A, 797A and 868A, features a modification of the amino acid from D to H at position 115.
+The protein's natural variant, known as in strain: 705A, 740A and 907A, features a modification of the amino acid from E to D at position 126.
+The protein's natural variant, known as in strain: 740A, features a modification of the amino acid from HK to Q at position 128.
+The protein's natural variant, known as found in a family with autosomal recessive infantile-onset neurodegenerative disease; unknown pathological significance; loss of axonal outgrowth;, features a modification of the amino acid from V to I at position 1043.
+The protein's natural variant, known as in strain: Ds-NA, features a modification of the amino acid from V to M at position 142.
+The protein's natural variant, known as in MRD58;, features a modification of the amino acid from W to G at position 95.
+The protein's natural variant, known as in MRD58;, features a modification of the amino acid from H to Y at position 118.
+The natural variant of this protein is characterized by an amino acid alteration from E to H at position 31.
+The protein's natural variant, known as in strain: Czech II, features a modification of the amino acid from N to Y at position 65.
+The protein's natural variant, known as in strain: Czech II, features a modification of the amino acid from I to V at position 208.
+The protein's natural variant, known as in strain: Czech II, features a modification of the amino acid from T to K at position 226.
+The protein's natural variant, known as in strain: Czech II, features a modification of the amino acid from G to E at position 397.
+The protein's natural variant, known as in strain: Czech II, features a modification of the amino acid from D to A at position 458.
+The protein's natural variant, known as in strain: Czech II, features a modification of the amino acid from A to T at position 486.
+The protein's natural variant, known as in strain: Czech II, features a modification of the amino acid from I to V at position 527.
+The protein's natural variant, known as in strain: Czech II, features a modification of the amino acid from V to I at position 553.
+The protein's natural variant, known as in CDG2P;, features a modification of the amino acid from A to G at position 7.
+The protein's natural variant, known as in CDG2P;, features a modification of the amino acid from A to P at position 14.
+The protein's natural variant, known as in CDG2P;, features a modification of the amino acid from R to P at position 31.
+The protein's natural variant, known as in AHO;, features a modification of the amino acid from L to P at position 99.
+The protein's natural variant, known as in AHO/PHP1A, features a modification of the amino acid from I to S at position 106.
+The protein's natural variant, known as in AHO;, features a modification of the amino acid from P to L at position 115.
+The protein's natural variant, known as in PHP1A, features a modification of the amino acid from D to N at position 156.
+The protein's natural variant, known as in PHP1A, features a modification of the amino acid from V to M at position 159.
+The protein's natural variant, known as in AHO;, features a modification of the amino acid from R to C at position 165.
+The protein's natural variant, known as in MAS; also found in somatotrophinoma;, features a modification of the amino acid from R to C at position 201.
+The protein's natural variant, known as in MAS;, features a modification of the amino acid from R to G at position 201.
+The protein's natural variant, known as in MAS and AIMAH1; also found in somatotrophinoma;, features a modification of the amino acid from R to H at position 201.
+The protein's natural variant, known as in non-MAS endocrine tumors;, features a modification of the amino acid from R to L at position 201.
+The protein's natural variant, known as in AIMAH1; also found in pituitary tumor and polyostotic fibrous dysplasia;, features a modification of the amino acid from R to S at position 201.
+The protein's natural variant, known as in pituitary adenomas; also found in a patient with severe Cushing syndrome;, features a modification of the amino acid from Q to H at position 227.
+The protein's natural variant, known as in somatotrophinoma;, features a modification of the amino acid from Q to R at position 227.
+The protein's natural variant, known as in AHO; impairs the ability to mediate hormonal stimulation;, features a modification of the amino acid from R to H at position 231.
+The protein's natural variant, known as in AHO, features a modification of the amino acid from T to I at position 242.
+The protein's natural variant, known as in AHO, features a modification of the amino acid from F to S at position 246.
+The protein's natural variant, known as in AHO; may alter guanine nucleotide binding which could lead to thermolability and impaired function;, features a modification of the amino acid from S to R at position 250.
+The protein's natural variant, known as in AHO; defective GDP binding resulting in increased thermolability and decreased activation;, features a modification of the amino acid from R to W at position 258.
+The protein's natural variant, known as in AHO, features a modification of the amino acid from E to V at position 259.
+The protein's natural variant, known as in PHP1A, features a modification of the amino acid from R to G at position 280.
+The protein's natural variant, known as in PHP1A, features a modification of the amino acid from R to K at position 280.
+The protein's natural variant, known as in POH, features a modification of the amino acid from W to R at position 281.
+The protein's natural variant, known as in PHP1A, features a modification of the amino acid from K to N at position 338.
+The protein's natural variant, known as in PHP1A; the patient also shows testotoxicosis; constitutively activates adenylyl cyclase in vitro; rapidly degraded at 37 degrees resulting in loss of Gs activity;, features a modification of the amino acid from A to S at position 366.
+The protein's natural variant, known as in AHO; uncouples receptors from adenylyl cyclases, features a modification of the amino acid from R to H at position 385.
+The protein's natural variant, known as in PHP1C; significantly reduces receptor-mediated activation; displays normal receptor-independent activation;, features a modification of the amino acid from L to R at position 388.
+The protein's natural variant, known as in PHP1C; significantly reduces receptor-mediated activation; displays normal receptor-independent activation;, features a modification of the amino acid from E to K at position 392.
+The protein's natural variant, known as in NEDLDS; unknown pathological significance, features a modification of the amino acid from R to C at position 23.
+The protein's natural variant, known as in NEDLDS; unknown pathological significance, features a modification of the amino acid from G to V at position 328.
+The protein's natural variant, known as in NEDLDS; unknown pathological significance, features a modification of the amino acid from G to R at position 382.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to C at position 678.
+The protein's natural variant, known as in NEDLDS; unknown pathological significance, features a modification of the amino acid from L to F at position 862.
+The protein's natural variant, known as in a colorectal cancer sample and NEDLDS; somatic mutation; unknown pathological significance;, features a modification of the amino acid from A to V at position 1339.
+The protein's natural variant, known as in NEDLDS; unknown pathological significance, features a modification of the amino acid from A to E at position 1547.
+The protein's natural variant, known as in strain: HB19, features a modification of the amino acid from R to I at position 18.
+The protein's natural variant, known as in strain: HB19, features a modification of the amino acid from D to Y at position 119.
+The protein's natural variant, known as in strain: HB19, features a modification of the amino acid from V to I at position 174.
+The protein's natural variant, known as in strain: HB19, features a modification of the amino acid from N to S at position 192.
+The protein's natural variant, known as in strain: Silvio, features a modification of the amino acid from K to N at position 95.
+The protein's natural variant, known as in strain: Silvio, features a modification of the amino acid from E to A at position 140.
+The protein's natural variant, known as in strain: Silvio, features a modification of the amino acid from N to H at position 156.
+The protein's natural variant, known as in strain: Silvio, features a modification of the amino acid from N to T at position 353.
+The protein's natural variant, known as in strain: Silvio, features a modification of the amino acid from NI to KV at position 403.
+The protein's natural variant, known as in strain: Silvio, features a modification of the amino acid from V to I at position 441.
+The protein's natural variant, known as in strain: Isolate S11, features a modification of the amino acid from T to S at position 17.
+The protein's natural variant, known as in GAN1; no effect on binding to TBCB;, features a modification of the amino acid from R to S at position 15.
+The protein's natural variant, known as in GAN1;, features a modification of the amino acid from A to P at position 51.
+The protein's natural variant, known as in GAN1;, features a modification of the amino acid from S to G at position 52.
+The protein's natural variant, known as in GAN1;, features a modification of the amino acid from S to L at position 79.
+The protein's natural variant, known as in GAN1; no effect on binding to TBCB;, features a modification of the amino acid from V to F at position 82.
+The protein's natural variant, known as in GAN1;, features a modification of the amino acid from I to F at position 86.
+The protein's natural variant, known as in GAN1;, features a modification of the amino acid from Y to C at position 89.
+The protein's natural variant, known as probable disease-associated variant found in hereditary motor and sensory neuropathy;, features a modification of the amino acid from I to T at position 102.
+The protein's natural variant, known as in GAN1;, features a modification of the amino acid from R to H at position 138.
+The protein's natural variant, known as in GAN1;, features a modification of the amino acid from V to F at position 195.
+The protein's natural variant, known as in GAN1;, features a modification of the amino acid from R to Q at position 269.
+The protein's natural variant, known as in GAN1;, features a modification of the amino acid from L to R at position 309.
+The protein's natural variant, known as in GAN1;, features a modification of the amino acid from P to L at position 315.
+The protein's natural variant, known as in GAN1;, features a modification of the amino acid from G to R at position 368.
+The protein's natural variant, known as in GAN1;, features a modification of the amino acid from I to T at position 423.
+The protein's natural variant, known as probable disease-associated variant found in hereditary motor and sensory neuropathy;, features a modification of the amino acid from V to I at position 438.
+The protein's natural variant, known as in GAN1;, features a modification of the amino acid from G to R at position 474.
+The protein's natural variant, known as in GAN1;, features a modification of the amino acid from E to K at position 486.
+The protein's natural variant, known as in GAN1; complete loss of binding to TBCB;, features a modification of the amino acid from R to C at position 545.
+The protein's natural variant, known as in GAN1;, features a modification of the amino acid from R to H at position 545.
+The protein's natural variant, known as in GAN1;, features a modification of the amino acid from C to Y at position 570.
+The natural variant of this protein is characterized by an amino acid alteration from T to A at position 124.
+The natural variant of this protein is characterized by an amino acid alteration from K to Q at position 146.
+The protein's natural variant, known as associated with lymphedema in a small family;, features a modification of the amino acid from H to P at position 19.
+The protein's natural variant, known as in SPG44; does not form functional homotypic channels;, features a modification of the amino acid from I to M at position 36.
+The protein's natural variant, known as in LMPHM3;, features a modification of the amino acid from S to L at position 48.
+The protein's natural variant, known as in HLD2;, features a modification of the amino acid from P to S at position 90.
+The protein's natural variant, known as associated with lymphedema in a small family, features a modification of the amino acid from R to Q at position 125.
+The protein's natural variant, known as associated with lymphedema in a small family;, features a modification of the amino acid from G to S at position 149.
+The protein's natural variant, known as in LMPHM3;, features a modification of the amino acid from R to C at position 260.
+The protein's natural variant, known as in HLD2;, features a modification of the amino acid from Y to D at position 272.
+The protein's natural variant, known as in HLD2;, features a modification of the amino acid from M to T at position 286.
+The protein's natural variant, known as associated with lymphedema in a small family;, features a modification of the amino acid from P to L at position 316.
+The protein's natural variant, known as in AIFBL1; increases inflammatory cytokine secretion; increases NF-kappaB signaling, features a modification of the amino acid from C to Y at position 243.
+The natural variant of this protein is characterized by an amino acid alteration from R to I at position 73.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from L to V at position 19.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation; diminishes enzymatic activity;, features a modification of the amino acid from G to R at position 82.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from Y to S at position 117.
+The protein's natural variant, known as abolishes enzymatic activity;, features a modification of the amino acid from R to C at position 206.
+The protein's natural variant, known as found in a patient with hyperekplexia; unknown pathological significance; does not disrupt GLRB-GPHN interactions; does not affect the structural lattices formed by GPHN;, features a modification of the amino acid from N to Y at position 10.
+The protein's natural variant, known as in MOCODC; patient phenotype resembling Dravet syndrome; abolishes postsynaptic clustering of GPHN; decreases cell-surface expression of GABA receptors; impairs postsynaptic currents; catalytically inactive; decreases binding affinity toward GABRA3; decreases binding affinity toward GLRB, features a modification of the amino acid from G to D at position 375.
+The protein's natural variant, known as in MOCODC; lacks molybdenum cofactor synthesis activity;, features a modification of the amino acid from D to A at position 580.
+The protein's natural variant, known as in IMD97; loss-of-function variant unable to rescue reduced T-cell activation when expressed in Jurkat PIK3CG-deficient cells, features a modification of the amino acid from R to S at position 49.
+The protein's natural variant, known as in IMD97; loss of phosphatidylinositol-3,4-bisphosphate 5-kinase activity, features a modification of the amino acid from R to P at position 1021.
+The protein's natural variant, known as in IMD97; loss-of-function variant unable to rescue reduced T-cell activation when expressed in Jurkat PIK3CG-deficient cells, features a modification of the amino acid from N to S at position 1085.
+The protein's natural variant, known as in strain: Isolate DUPC 6271m and Isolate FMNH 85134, features a modification of the amino acid from T to A at position 191.
+The protein's natural variant, known as in strain: Isolate DUPC 6271m and Isolate FMNH 85134, features a modification of the amino acid from S to T at position 257.
+The protein's natural variant, known as in strain: Isolate FMNH 85134, features a modification of the amino acid from V to M at position 295.
+The protein's natural variant, known as in VWS2;, features a modification of the amino acid from R to H at position 298.
+The protein's natural variant, known as in VWS2;, features a modification of the amino acid from R to C at position 391.
+The protein's natural variant, known as in VWS2;, features a modification of the amino acid from R to Q at position 520.
+The protein's natural variant, known as in PC3;, features a modification of the amino acid from R to P at position 164.
+The protein's natural variant, known as in PC3;, features a modification of the amino acid from Q to P at position 166.
+The protein's natural variant, known as in PC3;, features a modification of the amino acid from I to N at position 167.
+The protein's natural variant, known as in PC3;, features a modification of the amino acid from L to F at position 170.
+The protein's natural variant, known as in PC3;, features a modification of the amino acid from N to D at position 171.
+The protein's natural variant, known as in PC3;, features a modification of the amino acid from N to K at position 171.
+The protein's natural variant, known as in PC3;, features a modification of the amino acid from N to S at position 171.
+The protein's natural variant, known as in PC3;, features a modification of the amino acid from N to Y at position 171.
+The protein's natural variant, known as in PC3;, features a modification of the amino acid from F to C at position 174.
+The protein's natural variant, known as in PC3;, features a modification of the amino acid from F to S at position 174.
+The protein's natural variant, known as in PC3;, features a modification of the amino acid from F to V at position 174.
+The protein's natural variant, known as in PC3;, features a modification of the amino acid from S to P at position 176.
+The protein's natural variant, known as in PC3;, features a modification of the amino acid from I to N at position 178.
+The protein's natural variant, known as in PC3;, features a modification of the amino acid from I to N at position 462.
+The protein's natural variant, known as in PC3;, features a modification of the amino acid from I to S at position 462.
+The protein's natural variant, known as in PC3;, features a modification of the amino acid from A to P at position 463.
+The protein's natural variant, known as in PC3;, features a modification of the amino acid from T to P at position 464.
+The protein's natural variant, known as in PC3;, features a modification of the amino acid from Y to H at position 465.
+The protein's natural variant, known as in PC3, features a modification of the amino acid from Y to S at position 465.
+The protein's natural variant, known as in PC3;, features a modification of the amino acid from L to P at position 468.
+The protein's natural variant, known as in PC3;, features a modification of the amino acid from L to Q at position 468.
+The protein's natural variant, known as in PC3;, features a modification of the amino acid from L to P at position 469.
+The protein's natural variant, known as in PC3;, features a modification of the amino acid from L to R at position 469.
+The protein's natural variant, known as in PC3;, features a modification of the amino acid from E to K at position 472.
+The protein's natural variant, known as does not affect catalytic activity;, features a modification of the amino acid from G to S at position 55.
+The protein's natural variant, known as does not affect catalytic activity;, features a modification of the amino acid from V to A at position 82.
+The protein's natural variant, known as does not affect catalytic activity;, features a modification of the amino acid from G to A at position 112.
+The protein's natural variant, known as in WT5, features a modification of the amino acid from Q to H at position 192.
+The protein's natural variant, known as in breast cancer; loss of CDK6 interaction;, features a modification of the amino acid from A to P at position 72.
+The protein's natural variant, known as in sti; homozygous mice display an unkempt sticky appearance of fur and show cerebellar Purkinje cell loss and ataxia; defects are caused by impaired ability to edit incorrectly charged tRNA, resulting in formation of ubiquitinated protein aggregates in cerebellar Purkinje cells and degeneration of these neurons, features a modification of the amino acid from A to E at position 734.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from P to L at position 574.
+The protein's natural variant, known as in FECD6; no effect on protein expression; no effect on nuclear localization;, features a modification of the amino acid from N to T at position 78.
+The protein's natural variant, known as found in a patient with FECD6, features a modification of the amino acid from G to E at position 525.
+The protein's natural variant, known as in FECD6; down-regulation of several collagen genes expression;, features a modification of the amino acid from Q to H at position 640.
+The protein's natural variant, known as in FECD6; no effect on protein expression; no effect on nuclear localization;, features a modification of the amino acid from P to A at position 649.
+The protein's natural variant, known as in FECD6; no effect on protein expression; no effect on nuclear localization;, features a modification of the amino acid from N to S at position 696.
+The protein's natural variant, known as in FECD6; no effect on protein expression; no effect on nuclear localization;, features a modification of the amino acid from Q to P at position 810.
+The protein's natural variant, known as in FECD6; no effect on protein expression; no effect on nuclear localization;, features a modification of the amino acid from Q to P at position 840.
+The protein's natural variant, known as in FECD6; no effect on protein expression; no effect on nuclear localization;, features a modification of the amino acid from A to G at position 905.
+The protein's natural variant, known as in FECD6, features a modification of the amino acid from A to T at position 905.
+The protein's natural variant, known as in a lung neuroendocrine carcinoma sample; somatic mutation, features a modification of the amino acid from P to L at position 127.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from A to T at position 182.
+The natural variant of this protein is characterized by an amino acid alteration from L to V at position 477.
+The protein's natural variant, known as in R biotype, features a modification of the amino acid from T to I at position 239.
+The protein's natural variant, known as in I biotype, features a modification of the amino acid from M to T at position 268.
+The protein's natural variant, known as in allele roan, features a modification of the amino acid from A to D at position 218.
+The protein's natural variant, known as in MC1DN34; unknown pathological significance;, features a modification of the amino acid from F to L at position 55.
+The protein's natural variant, known as in strain: B, features a modification of the amino acid from Q to E at position 29.
+The protein's natural variant, known as in GS3; abolishes RAB27A binding;, features a modification of the amino acid from R to W at position 35.
+The natural variant of this protein is characterized by an amino acid alteration from M to Q at position 89.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from F to L at position 8.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from I to V at position 35.
+The protein's natural variant, known as probable disease-associated variant found in patients with microcephaly and intellectual disability; disrupts interaction with CEP63; no effect on interaction with PCM1;, features a modification of the amino acid from E to Q at position 89.
+The protein's natural variant, known as in JBTS33; loss of function in ciliogenesis;, features a modification of the amino acid from R to Q at position 405.
+The protein's natural variant, known as in JBTS33; loss of function in ciliogenesis;, features a modification of the amino acid from D to A at position 637.
+The protein's natural variant, known as in strain: C57BL/6J, features a modification of the amino acid from I to V at position 69.
+The protein's natural variant, known as in strain: ML2, features a modification of the amino acid from P to S at position 24.
+The protein's natural variant, known as in strain: ML2, features a modification of the amino acid from D to E at position 52.
+The protein's natural variant, known as in strain: ML2, features a modification of the amino acid from I to V at position 59.
+The protein's natural variant, known as in strain: ML2, features a modification of the amino acid from F to Y at position 88.
+The protein's natural variant, known as in strain: ML2, features a modification of the amino acid from V to I at position 92.
+The protein's natural variant, known as increased protein half-life; reduced interaction with AREL1;, features a modification of the amino acid from S to N at position 52.
+The natural variant of this protein is characterized by an amino acid alteration from S to T at position 44.
+The protein's natural variant, known as may be associated with an increased risk for multiple sclerosis; homozygous patients express higher levels of CD24 on peripheral blood T-cells than homozygous controls;, features a modification of the amino acid from A to V at position 57.
+The protein's natural variant, known as in isozyme PB2, features a modification of the amino acid from S to G at position 303.
+The protein's natural variant, known as in isozyme PB2, features a modification of the amino acid from AE to TV at position 322.
+The protein's natural variant, known as in isozyme PB2, features a modification of the amino acid from L to P at position 337.
+The protein's natural variant, known as in isozyme PB2, features a modification of the amino acid from T to S at position 339.
+The protein's natural variant, known as in isozyme PB2, features a modification of the amino acid from S to T at position 344.
+The natural variant of this protein is characterized by an amino acid alteration from A to S at position 461.
+The natural variant of this protein is characterized by an amino acid alteration from S to A at position 519.
+The natural variant of this protein is characterized by an amino acid alteration from M to T at position 941.
+The natural variant of this protein is characterized by an amino acid alteration from R to W at position 977.
+The natural variant of this protein is characterized by an amino acid alteration from K to N at position 978.
+The natural variant of this protein is characterized by an amino acid alteration from Y to C at position 993.
+The natural variant of this protein is characterized by an amino acid alteration from D to E at position 994.
+The natural variant of this protein is characterized by an amino acid alteration from E to Q at position 1005.
+The natural variant of this protein is characterized by an amino acid alteration from D to Y at position 1007.
+The natural variant of this protein is characterized by an amino acid alteration from L to P at position 1008.
+The natural variant of this protein is characterized by an amino acid alteration from T to A at position 1018.
+The protein's natural variant, known as in USRISD; does not rescue morphological defects in a zebrafish animal model, features a modification of the amino acid from R to Q at position 15.
+The protein's natural variant, known as in USRISD; does not rescue morphological defects in a zebrafish animal model, features a modification of the amino acid from R to Q at position 35.
+The protein's natural variant, known as in USRISD; does not rescue morphological defects in a zebrafish animal model, features a modification of the amino acid from R to W at position 35.
+The protein's natural variant, known as in USRISR; does not fully rescue morphological defects in a zebrafish animal model; affects trafficking of transferrin from early to recycling endosomes; no effect on subcellular location in the perinuclear region; does not affect interaction with AP-1 complex subunits AP1B1, AP1M1 and AP1S1, features a modification of the amino acid from P to H at position 243.
+The protein's natural variant, known as in USRISR; does not fully rescue morphological defects in a zebrafish animal model; affects trafficking of transferrin from recycling endosomes to plasma membrane; no effect on subcellular location in the perinuclear region; does not affect interaction with AP-1 complex subunits AP1B1, AP1M1 and AP1S1, features a modification of the amino acid from M to V at position 366.
+The protein's natural variant, known as in USRISD; does not fully rescue morphological defects in a zebrafish animal model, features a modification of the amino acid from P to R at position 817.
+The natural variant of this protein is characterized by an amino acid alteration from T to K at position 29.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from A to V at position 8.
+The protein's natural variant, known as in LGMDR5, features a modification of the amino acid from G to D at position 69.
+The protein's natural variant, known as in LGMDR5, features a modification of the amino acid from G to R at position 69.
+The protein's natural variant, known as in LGMDR5;, features a modification of the amino acid from L to S at position 71.
+The protein's natural variant, known as in LGMDR5;, features a modification of the amino acid from C to Y at position 283.
+The natural variant of this protein is characterized by an amino acid alteration from L to V at position 85.
+The protein's natural variant, known as in allele Aldh2*2 and allele Aldh2*3; in strains UChA and UChB, features a modification of the amino acid from Q to R at position 86.
+The protein's natural variant, known as in allele Aldh2*3; in strain: UChB, features a modification of the amino acid from E to K at position 498.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from E to Q at position 23.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from G to D at position 446.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from D to E at position 780.
+The protein's natural variant, known as in strain: O44:K74, features a modification of the amino acid from P to L at position 247.
+The protein's natural variant, known as in MRT64;, features a modification of the amino acid from Y to C at position 288.
+The protein's natural variant, known as in MRT64;, features a modification of the amino acid from R to H at position 290.
+The protein's natural variant, known as in strain: Pasteur, features a modification of the amino acid from L to S at position 27.
+The protein's natural variant, known as in strain: Pasteur, features a modification of the amino acid from G to S at position 311.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from A to P at position 150.
+The protein's natural variant, known as in colorectal cancer and glioma samples; glioblastoma multiforme; somatic mutation; found in patients with cartilaginous tumors; abolishes magnesium binding and alters enzyme activity so that isocitrate is no longer converted to alpha-ketoglutarate but instead alpha-ketoglutarate is converted to R(-)-2-hydroxyglutarate; induces histone methylation; enhances expression of chondrocyte-related genes; disturbs the formation of cartilaginous matrix; inhibits osteogenic differentiation;, features a modification of the amino acid from R to C at position 132.
+The protein's natural variant, known as in a glioma sample; glioblastoma multiforme; somatic mutation; found in patients with cartilaginous tumors;, features a modification of the amino acid from R to G at position 132.
+The protein's natural variant, known as in a glioma sample; glioblastoma multiforme; somatic mutation; found in patients with cartilaginous tumors; abolishes magnesium binding and alters enzyme activity so that isocitrate is no longer converted to alpha-ketoglutarate but instead alpha-ketoglutarate is converted to R(-)-2-hydroxyglutarate;, features a modification of the amino acid from R to H at position 132.
+The protein's natural variant, known as in a glioma sample; glioblastoma multiforme; somatic mutation; abolishes magnesium binding and alters enzyme activity so that isocitrate is no longer converted to alpha-ketoglutarate but instead alpha-ketoglutarate is converted to R(-)-2-hydroxyglutarate;, features a modification of the amino acid from R to L at position 132.
+The protein's natural variant, known as in a glioma sample; glioblastoma multiforme; somatic mutation; abolishes magnesium binding and alters enzyme activity so that isocitrate is no longer converted to alpha-ketoglutarate but instead alpha-ketoglutarate is converted to R(-)-2-hydroxyglutarate;, features a modification of the amino acid from R to S at position 132.
+The protein's natural variant, known as in DEE65;, features a modification of the amino acid from R to C at position 87.
+The protein's natural variant, known as in DEE65;, features a modification of the amino acid from R to L at position 87.
+The protein's natural variant, known as in DEE65;, features a modification of the amino acid from R to P at position 87.
+The protein's natural variant, known as in RNA edited version;, features a modification of the amino acid from K to E at position 320.
+The protein's natural variant, known as in LIS6;, features a modification of the amino acid from G to W at position 33.
+The protein's natural variant, known as in LIS6; causes reduced interaction with KATNA1 and NDEL1;, features a modification of the amino acid from S to L at position 535.
+The protein's natural variant, known as in LIS6;, features a modification of the amino acid from L to R at position 540.
+The protein's natural variant, known as found in a patient with atrial septal defects; unknown pathological significance;, features a modification of the amino acid from K to E at position 139.
+The protein's natural variant, known as found in a patient with atrial septal defects; unknown pathological significance;, features a modification of the amino acid from A to P at position 171.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from F to C at position 80.
+The protein's natural variant, known as in MC5DN2, features a modification of the amino acid from T to P at position 210.
+The protein's natural variant, known as in strain: cv. CL2l, features a modification of the amino acid from F to L at position 33.
+The protein's natural variant, known as in strain: cv. CL2, features a modification of the amino acid from S to P at position 53.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from G to R at position 58.
+The natural variant of this protein is characterized by an amino acid alteration from R to W at position 178.
+The protein's natural variant, known as in a patient with bronchiectasis;, features a modification of the amino acid from G to S at position 183.
+The protein's natural variant, known as in a patient with bronchiectasis;, features a modification of the amino acid from E to K at position 197.
+The natural variant of this protein is characterized by an amino acid alteration from A to P at position 502.
+The natural variant of this protein is characterized by an amino acid alteration from A to S at position 614.
+The natural variant of this protein is characterized by an amino acid alteration from I to N at position 546.
+The protein's natural variant, known as in RSTS1, features a modification of the amino acid from Y to F at position 650.
+The protein's natural variant, known as in RSTS1;, features a modification of the amino acid from A to T at position 789.
+The protein's natural variant, known as in RSTS1; incomplete;, features a modification of the amino acid from T to A at position 910.
+The protein's natural variant, known as in RSTS1; mild form; impairs binding to ASF1A and acetylated histone H3;, features a modification of the amino acid from Y to C at position 1175.
+The protein's natural variant, known as in RSTS1, features a modification of the amino acid from E to A at position 1278.
+The protein's natural variant, known as in RSTS1; abolishes acetyltransferase activity;, features a modification of the amino acid from E to K at position 1278.
+The protein's natural variant, known as in RSTS1; abolishes acetyltransferase activity and the ability of transactivate CREB;, features a modification of the amino acid from R to P at position 1378.
+The protein's natural variant, known as in RSTS1;, features a modification of the amino acid from D to Y at position 1406.
+The protein's natural variant, known as in RSTS1, features a modification of the amino acid from Q to P at position 1415.
+The protein's natural variant, known as in RSTS1, features a modification of the amino acid from T to I at position 1447.
+The protein's natural variant, known as in RSTS1;, features a modification of the amino acid from Y to H at position 1450.
+The protein's natural variant, known as in RSTS1;, features a modification of the amino acid from H to R at position 1470.
+The protein's natural variant, known as in RSTS1, features a modification of the amino acid from P to T at position 1475.
+The protein's natural variant, known as in RSTS1, features a modification of the amino acid from Y to F at position 1503.
+The protein's natural variant, known as in RSTS1;, features a modification of the amino acid from L to P at position 1507.
+The protein's natural variant, known as in RSTS1, features a modification of the amino acid from D to N at position 1543.
+The protein's natural variant, known as in RSTS1; abolishes acetyltransferase activity;, features a modification of the amino acid from R to H at position 1664.
+The protein's natural variant, known as in MKHK1;, features a modification of the amino acid from C to R at position 1710.
+The protein's natural variant, known as in MKHK1, features a modification of the amino acid from H to D at position 1719.
+The protein's natural variant, known as in MKHK1;, features a modification of the amino acid from E to K at position 1724.
+The protein's natural variant, known as in MKHK1, features a modification of the amino acid from L to R at position 1747.
+The protein's natural variant, known as in MKHK1;, features a modification of the amino acid from A to V at position 1782.
+The protein's natural variant, known as in MKHK1, features a modification of the amino acid from R to P at position 1786.
+The protein's natural variant, known as in MKHK1, features a modification of the amino acid from C to F at position 1819.
+The protein's natural variant, known as in MKHK1, features a modification of the amino acid from C to W at position 1826.
+The protein's natural variant, known as in MKHK1, features a modification of the amino acid from H to D at position 1829.
+The protein's natural variant, known as in MKHK1, features a modification of the amino acid from C to Y at position 1838.
+The protein's natural variant, known as in MKHK1, features a modification of the amino acid from MR to I at position 1866.
+The protein's natural variant, known as in MKHK1;, features a modification of the amino acid from R to Q at position 1867.
+The protein's natural variant, known as in MKHK1, features a modification of the amino acid from R to W at position 1867.
+The protein's natural variant, known as in MKHK1;, features a modification of the amino acid from R to Q at position 1868.
+The protein's natural variant, known as in MKHK1;, features a modification of the amino acid from R to W at position 1868.
+The protein's natural variant, known as in MKHK1, features a modification of the amino acid from A to P at position 1870.
+The protein's natural variant, known as in MKHK1;, features a modification of the amino acid from M to V at position 1872.
+The protein's natural variant, known as in HALD2; increased voltage-gated chloride currents due to higher channel open probabilities at physiological cell membrane potentials;, features a modification of the amino acid from M to K at position 22.
+The protein's natural variant, known as in HALD2; increased voltage-gated chloride currents; increased aldosterone synthase expression;, features a modification of the amino acid from G to D at position 24.
+The protein's natural variant, known as in HALD2; increased voltage-gated chloride currents due to higher channel open probabilitiesat at physiological cell membrane potentials;, features a modification of the amino acid from Y to N at position 26.
+The protein's natural variant, known as reduces channel activity;, features a modification of the amino acid from P to R at position 48.
+The protein's natural variant, known as reduces channel activity;, features a modification of the amino acid from R to H at position 68.
+The protein's natural variant, known as in HALD2; increased voltage-gated chloride currents due to higher channel open probabilities at physiological cell membrane potentials; increased aldosterone synthase expression;, features a modification of the amino acid from R to Q at position 172.
+The protein's natural variant, known as no effect;, features a modification of the amino acid from G to A at position 199.
+The protein's natural variant, known as in EJM8; associated with disease susceptibility; the mutant channel has accelerated deactivation rates compared to wild-type, but normal activation and peak current;, features a modification of the amino acid from R to Q at position 235.
+The protein's natural variant, known as in LKPAT; loss of function mutation; the mutant protein is restricted to the endoplasmic reticulum and hardly reaches the plasma membrane; lower amounts of the mutant protein compared to wild-type;, features a modification of the amino acid from A to V at position 500.
+The protein's natural variant, known as in EIG11; associated with disease susceptibility; the mutant channel has accelerated deactivation rates compared to wild-type, but normal activation and peak current;, features a modification of the amino acid from R to Q at position 577.
+The protein's natural variant, known as no effect;, features a modification of the amino acid from R to C at position 644.
+The protein's natural variant, known as reduces channel activity;, features a modification of the amino acid from R to Q at position 646.
+The protein's natural variant, known as in JAE2; unknown pathological significance;, features a modification of the amino acid from G to E at position 715.
+The protein's natural variant, known as found in a patient with childhood absence epilepsy; unknown pathological significance;, features a modification of the amino acid from S to L at position 719.
+The protein's natural variant, known as slightly faster channel activation;, features a modification of the amino acid from R to W at position 725.
+The protein's natural variant, known as slightly faster channel activation;, features a modification of the amino acid from R to H at position 747.
+The protein's natural variant, known as in HALD2; increased voltage-gated chloride currents due to higher channel open probabilities at physiological cell membrane potentials;, features a modification of the amino acid from S to R at position 865.
+The protein's natural variant, known as in MTDPS18; loss of 2-oxoglutarate transporter activity;, features a modification of the amino acid from K to R at position 232.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from K to M at position 58.
+The protein's natural variant, known as in SCAR25; reduced conjugation to ATG12; decrease in autophagy activity;, features a modification of the amino acid from E to D at position 122.
+The protein's natural variant, known as in EA1;, features a modification of the amino acid from V to F at position 174.
+The protein's natural variant, known as in EA1, features a modification of the amino acid from I to R at position 177.
+The protein's natural variant, known as in EA1; alters voltage dependence and kinetics of activation though not of C-type inactivation;, features a modification of the amino acid from F to C at position 184.
+The protein's natural variant, known as in EA1;, features a modification of the amino acid from T to A at position 226.
+The protein's natural variant, known as in MK1; induces a reduced efflux of potassium ions during depolarization which results in increased muscle cell activity; coexpression studies of the mutant protein with the wild-type protein produces significantly reduced currents suggesting a severe effect of the mutation;, features a modification of the amino acid from T to K at position 226.
+The protein's natural variant, known as in EA1;, features a modification of the amino acid from T to M at position 226.
+The protein's natural variant, known as in EA1; yields currents with a largely reduced amplitude;, features a modification of the amino acid from T to R at position 226.
+The protein's natural variant, known as in EA1;, features a modification of the amino acid from R to S at position 239.
+The protein's natural variant, known as in MK1; 10% reduction of mean peak current amplitudes compared to wil-dtype; mutant and wild-type expression together is consistent with a loss-of-function effect of the mutation;, features a modification of the amino acid from A to P at position 242.
+The protein's natural variant, known as in MK1; does not affect channel activity;, features a modification of the amino acid from P to H at position 244.
+The protein's natural variant, known as in EA1;, features a modification of the amino acid from F to I at position 249.
+The protein's natural variant, known as in MK1; strongly reduces the activity of homomeric channels with dominant negative effects on wild-type channels;, features a modification of the amino acid from N to D at position 255.
+The protein's natural variant, known as in EA1; results in non-functional homomeric channels; accelerates recovery from N-type inactivation due to interaction with KCNAB1; slows down N-type inactivation of heteromeric channels formed by KCNA1 and KCNA4;, features a modification of the amino acid from E to D at position 325.
+The protein's natural variant, known as in EA1, features a modification of the amino acid from L to I at position 329.
+The protein's natural variant, known as in EA1; phenotype without myokymia, features a modification of the amino acid from S to I at position 342.
+The protein's natural variant, known as in EA1; results in slower channel activation compared to wild-type; slows down N-type inactivation of heteromeric channels formed by KCNA1 and KCNA4;, features a modification of the amino acid from V to I at position 404.
+The protein's natural variant, known as probable disease-associated variant found in a patient with neonatal onset epileptic encephalopathy;, features a modification of the amino acid from P to L at position 405.
+The protein's natural variant, known as in EA1; channels have voltage dependence similar to that of wild-type channels but with faster kinetics and increased C-type inactivation; accelerates recovery from N-type inactivation due to interaction with KCNAB1; slows down N-type inactivation of heteromeric channels formed by KCNA1 and KCNA4;, features a modification of the amino acid from V to A at position 408.
+The protein's natural variant, known as in PCH14; unknown pathological significance; strongly reduced protein levels compared to wild-type after transfection in HEK293T cell line, features a modification of the amino acid from Y to C at position 78.
+The protein's natural variant, known as in PCH14; unknown pathological significance; strongly reduced protein levels compared to wild-type after transfection in HEK293T cell line, features a modification of the amino acid from F to S at position 82.
+The protein's natural variant, known as in PCH14; strongly reduced interaction with SNW1; strongly reduced protein levels in homozygous patient's fibroblasts compared to heterozygous or wild-type cells; in transgenic knockin mice, produces a pontocerebellar hypoplasia-like phenotype;, features a modification of the amino acid from A to T at position 99.
+The protein's natural variant, known as in PCH14; unknown pathological significance; strongly reduced protein levels compared to wild-type after transfection in HEK293T cell line, features a modification of the amino acid from D to DANAGPD at position 106.
+The protein's natural variant, known as in PCH14; unknown pathological significance; reduced interaction with SNW1; no effect on protein expression level, but shows reduced thermal stability and increased aggregation propensity in vitro, features a modification of the amino acid from T to A at position 107.
+The protein's natural variant, known as in PCH14; unknown pathological significance, features a modification of the amino acid from G to C at position 109.
+The protein's natural variant, known as in PCH14; reduced protein levels in homozygous patient's fibroblasts compared to heterozygous or wild-type cells;, features a modification of the amino acid from T to A at position 127.
+The protein's natural variant, known as in PCH14; strongly reduced interaction with SNW1; slightly reduced protein levels compared to wild-type, after transfection in HEK293T cell line, reduced thermal stability and increased aggregation propensity in vitro; in transgenic knockin mice, produces a pontocerebellar hypoplasia-like phenotype;, features a modification of the amino acid from R to Q at position 131.
+The protein's natural variant, known as in PEBAS; unknown pathological significance;, features a modification of the amino acid from A to V at position 627.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from E to Q at position 717.
+The protein's natural variant, known as in CONDMIM; decreased function in mitochondrial potassium ion transmembrane transport; does not fully rescue defective proton/potassium exchange in letm1-deficient yeast, features a modification of the amino acid from I to N at position 293.
+The protein's natural variant, known as in CONDMIM; decreased function in mitochondrial potassium ion transmembrane transport; does not fully rescue defective proton/potassium exchange in letm1-deficient yeast, features a modification of the amino acid from R to Q at position 294.
+The protein's natural variant, known as in CONDMIM; homozygous patient cells show altered levels of components of the oxidative phosphorylation machinery; decreased function in mitochondrial potassium ion transmembrane transport; does not fully rescue defective proton/potassium exchange in letm1-deficient yeast, features a modification of the amino acid from P to S at position 300.
+The protein's natural variant, known as no effect on mitochondrial potassium ion transmembrane transport; it fully rescues defective proton/potassium exchange in letm1-deficient yeast, features a modification of the amino acid from I to L at position 305.
+The protein's natural variant, known as in CONDMIM; homozygous patient cells show abnormal mitochondrial morphology and altered levels of components of the oxidative phosphorylation machinery; loss of function in mitochondrial potassium ion transmembrane transport; does not rescue defective proton/potassium exchange in letm1-deficient yeast, features a modification of the amino acid from D to N at position 358.
+The protein's natural variant, known as in CONDMIM; unknown pathological significance; decreased function in mitochondrial potassium ion transmembrane transport; does not fully rescue defective proton/potassium exchange in letm1-deficient yeast, features a modification of the amino acid from R to P at position 380.
+The protein's natural variant, known as in CONDMIM; unknown pathological significance, features a modification of the amino acid from R to H at position 393.
+The protein's natural variant, known as benign variant; no effect on mitochondrial potassium ion transmembrane transport; it fully rescues defective proton/potassium exchange in letm1-deficient yeast, features a modification of the amino acid from K to R at position 587.
+The protein's natural variant, known as in MRD56;, features a modification of the amino acid from P to L at position 890.
+The protein's natural variant, known as in MRD56; unknown pathological significance;, features a modification of the amino acid from L to P at position 1047.
+The protein's natural variant, known as in MRD56; unknown pathological significance, features a modification of the amino acid from W to R at position 1108.
+The protein's natural variant, known as in DYT30;, features a modification of the amino acid from N to K at position 52.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from S to G at position 516.
+The protein's natural variant, known as in SCZD; associated with disease susceptibility; unable to mediate down-regulation of axonal growth; decreased interaction with MAG and OMG; no effect on interaction with RTN4;, features a modification of the amino acid from R to W at position 119.
+The protein's natural variant, known as in SCZD; associated with disease susceptibility; unable to mediate down-regulation of axonal growth; does not affect interaction with MAG, RTN4 and OMG;, features a modification of the amino acid from R to H at position 196.
+The protein's natural variant, known as in SCZD; unknown pathological significance;, features a modification of the amino acid from R to C at position 227.
+The protein's natural variant, known as in SCZD; associated with disease susceptibility; unable to mediate down-regulation of axonal growth;, features a modification of the amino acid from R to H at position 292.
+The protein's natural variant, known as in SCZD; associated with disease susceptibility; unable to mediate down-regulation of axonal growth; does not affect interaction with MAG, RTN4, OMG, NGFR and LINGO1;, features a modification of the amino acid from R to Q at position 377.
+The protein's natural variant, known as in SCZD; associated with disease susceptibility; unable to mediate down-regulation of axonal growth; does not affect interaction with MAG, RTN4, OMG, NGFR and LINGO1;, features a modification of the amino acid from R to W at position 377.
+The protein's natural variant, known as in SCZD; unknown pathological significance;, features a modification of the amino acid from R to W at position 399.
+The protein's natural variant, known as in His; reduced stability, features a modification of the amino acid from R to Q at position 322.
+The protein's natural variant, known as in allele DPA1*02:02, allele DPA1*02:04, allele DPA1*03:01, allele DPA1*03:02 and allele DPA1*03:03; requires 2 nucleotide substitutions;, features a modification of the amino acid from A to M at position 42.
+The protein's natural variant, known as in allele DPA1*04:01;, features a modification of the amino acid from P to T at position 49.
+The protein's natural variant, known as in allele DPA1*01:09;, features a modification of the amino acid from M to T at position 54.
+The protein's natural variant, known as in allele DPA1*01:04, allele DPA1*01:08, allele DPA1*03:03 and allele DPA1*04:01;, features a modification of the amino acid from E to D at position 59.
+The protein's natural variant, known as in allele DPA1*01:06, allele DPA1*02:01, allele DPA1*02:02 and allele DPA1*02:04; requires 2 nucleotide substitutions;, features a modification of the amino acid from M to Q at position 62.
+The protein's natural variant, known as in allele DPA1*01:10;, features a modification of the amino acid from W to C at position 74.
+The protein's natural variant, known as in allele DPA1*01:08, allele DPA1*02:01, allele DPA1*02:02, allele DPA1*02:03, allele DPA1*02:04 and allele DPA1*04:01;, features a modification of the amino acid from Q to R at position 81.
+The protein's natural variant, known as in allele DPA1*01:07;, features a modification of the amino acid from A to T at position 82.
+The protein's natural variant, known as in allele DPA1*03:01 and allele DPA1*03:03;, features a modification of the amino acid from L to S at position 97.
+The protein's natural variant, known as in allele DPA1*02:04;, features a modification of the amino acid from N to D at position 100.
+The protein's natural variant, known as in allele DPA1*04:01;, features a modification of the amino acid from T to I at position 103.
+The protein's natural variant, known as in allele DPA1*04:01; requires 2 nucleotide substitutions, features a modification of the amino acid from L to A at position 104.
+The protein's natural variant, known as in allele DPA1*01:05, allele DPA1*02:01, allele DPA1*02:02, allele DPA1*02:03, allele DPA1*02:04 and allele DPA1*04:01;, features a modification of the amino acid from T to A at position 114.
+The protein's natural variant, known as in allele DPA1*04:01;, features a modification of the amino acid from P to A at position 127.
+The protein's natural variant, known as in allele DPA1*02:01 and allele DPA1*02:02;, features a modification of the amino acid from K to R at position 142.
+The protein's natural variant, known as in allele DPA1*02:01, allele DPA1*02:02 and allele DPA1*04:01;, features a modification of the amino acid from L to P at position 158.
+The protein's natural variant, known as in allele DPA1*02:01, allele DPA1*02:02 and allele DPA1*04:01;, features a modification of the amino acid from F to V at position 191.
+The protein's natural variant, known as in allele DPA1*04:01;, features a modification of the amino acid from T to A at position 221.
+The protein's natural variant, known as in allele DPA1*02:01, allele DPA1*02:02 and allele DPA1*04:01;, features a modification of the amino acid from T to P at position 259.
+The protein's natural variant, known as in variant D, features a modification of the amino acid from E to Q at position 61.
+The protein's natural variant, known as in variant W, features a modification of the amino acid from I to L at position 72.
+The protein's natural variant, known as in variant C; found only in the Jersey breed, features a modification of the amino acid from Q to H at position 75.
+The protein's natural variant, known as in variant A, features a modification of the amino acid from G to D at position 80.
+The protein's natural variant, known as in variant A, features a modification of the amino acid from A to V at position 134.
+The natural variant of this protein is characterized by an amino acid alteration from F to S at position 35.
+The protein's natural variant, known as in LHON; secondary mutation; does not seem to directly cause the disease;, features a modification of the amino acid from G to S at position 78.
+The natural variant of this protein is characterized by an amino acid alteration from Q to R at position 177.
+The protein's natural variant, known as in LHON; possible rare primary mutation;, features a modification of the amino acid from A to T at position 200.
+The protein's natural variant, known as found in two patients with a diagnosis of mitochondrial encephalomyopathy with lactic acidosis and stroke-like episodes syndrome; unknown pathological significance;, features a modification of the amino acid from F to L at position 251.
+The protein's natural variant, known as in plasmid pMYSH6000 and plasmid pCP301, features a modification of the amino acid from T to A at position 18.
+The protein's natural variant, known as in NLSDM;, features a modification of the amino acid from P to L at position 195.
+The protein's natural variant, known as in strain: C57BL/6, C57BL/6J and FVB/N, features a modification of the amino acid from D to A at position 124.
+The protein's natural variant, known as in HPMRS3;, features a modification of the amino acid from R to W at position 16.
+The protein's natural variant, known as in HPMRS3;, features a modification of the amino acid from Y to C at position 99.
+The protein's natural variant, known as in HPMRS3;, features a modification of the amino acid from L to S at position 127.
+The protein's natural variant, known as in HPMRS3;, features a modification of the amino acid from T to I at position 160.
+The protein's natural variant, known as in HPMRS3;, features a modification of the amino acid from R to P at position 177.
+The natural variant of this protein is characterized by an amino acid alteration from G to A at position 163.
+The protein's natural variant, known as in a patient with amyotrophic lateral sclerosis, features a modification of the amino acid from E to V at position 32.
+The protein's natural variant, known as in a patient with amyotrophic lateral sclerosis;, features a modification of the amino acid from P to S at position 229.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from S to P at position 331.
+The protein's natural variant, known as in IMD49; loss of stimulation of T-lymphocyte development; dominant negative loss of activation of IL2 expression; results in reduced binding to known canonical promoters and abnormal binding to novel DNA sites not recognized by the wild-type protein; no effect on interaction with EP300;, features a modification of the amino acid from N to K at position 441.
+The protein's natural variant, known as in IMD49;, features a modification of the amino acid from N to K at position 807.
+The protein's natural variant, known as in strain: AW1 and ACH0158, features a modification of the amino acid from L to A at position 92.
+The protein's natural variant, known as in strain: AW1 and ACH0158, features a modification of the amino acid from I to V at position 100.
+The protein's natural variant, known as in strain: ACH0158, features a modification of the amino acid from H to G at position 185.
+The protein's natural variant, known as in strain: AW1, features a modification of the amino acid from H to R at position 185.
+The protein's natural variant, known as in strain: AW1 and ACH0158, features a modification of the amino acid from T to S at position 206.
+The protein's natural variant, known as in strain: AW1 and ACH0158, features a modification of the amino acid from M to L at position 247.
+The protein's natural variant, known as in strain: AW1 and ACH0158, features a modification of the amino acid from T to A at position 262.
+The protein's natural variant, known as in strain: ACH0158, features a modification of the amino acid from N to S at position 264.
+The protein's natural variant, known as in strain: AW1 and ACH0158, features a modification of the amino acid from I to N at position 314.
+The protein's natural variant, known as in strain: AW1 and ACH0158, features a modification of the amino acid from S to A at position 329.
+The protein's natural variant, known as in strain: AW1 and ACH0158, features a modification of the amino acid from V to A at position 347.
+The protein's natural variant, known as in FFM;, features a modification of the amino acid from L to P at position 11.
+The protein's natural variant, known as in STGD1; unknown pathological significance, features a modification of the amino acid from N to K at position 14.
+The protein's natural variant, known as in STGD1; unknown pathological significance, features a modification of the amino acid from R to P at position 18.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from R to W at position 18.
+The protein's natural variant, known as in STGD1; unknown pathological significance;, features a modification of the amino acid from R to H at position 24.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from C to Y at position 54.
+The protein's natural variant, known as in CORD3; unknown pathological significance, features a modification of the amino acid from H to R at position 55.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from N to K at position 58.
+The protein's natural variant, known as in STGD1, features a modification of the amino acid from A to E at position 60.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from A to T at position 60.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from A to V at position 60.
+The protein's natural variant, known as in CORD3; unknown pathological significance, features a modification of the amino acid from S to P at position 63.
+The protein's natural variant, known as in STGD1 and CORD3;, features a modification of the amino acid from G to E at position 65.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from P to L at position 68.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from P to R at position 68.
+The protein's natural variant, known as in STGD1; does not affect intracellular vesicle localization; does not affect solubility; significantly reduces N-Ret-PE binding; drastically reduces basal ATPase activity with little or no all trans retinal stimulation;, features a modification of the amino acid from G to R at position 72.
+The protein's natural variant, known as in STGD1; unknown pathological significance, features a modification of the amino acid from G to V at position 72.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from C to G at position 75.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from V to E at position 77.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from N to D at position 96.
+The protein's natural variant, known as in STGD1; unknown pathological significance;, features a modification of the amino acid from N to H at position 96.
+The protein's natural variant, known as in STGD1; unknown pathological significance;, features a modification of the amino acid from N to K at position 96.
+The protein's natural variant, known as in STGD1; unknown pathological significance;, features a modification of the amino acid from Y to C at position 97.
+The protein's natural variant, known as in STGD1; highly decreased protein abundance; highly decreased ATPase activity; highly decreased phospholipid translocase activity;, features a modification of the amino acid from S to P at position 100.
+The protein's natural variant, known as in STGD1; unknown pathological significance, features a modification of the amino acid from D to V at position 108.
+The protein's natural variant, known as in STGD1; unknown pathological significance;, features a modification of the amino acid from P to L at position 143.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from R to Q at position 152.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from I to V at position 156.
+The protein's natural variant, known as in STGD1; unknown pathological significance;, features a modification of the amino acid from G to S at position 172.
+The protein's natural variant, known as in STGD1; unknown pathological significance, features a modification of the amino acid from S to F at position 184.
+The protein's natural variant, known as in STGD1; unknown pathological significance, features a modification of the amino acid from S to R at position 184.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from Q to H at position 190.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from A to T at position 192.
+The protein's natural variant, known as in STGD1; reduced basal and retinal-stimulated ATP-hydrolysis;, features a modification of the amino acid from S to R at position 206.
+The protein's natural variant, known as in STGD1 and CORD3; common mutation in southern Europe; reduced ATP-binding capacity;, features a modification of the amino acid from R to C at position 212.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from R to H at position 212.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from R to C at position 220.
+The protein's natural variant, known as in STGD1; unknown pathological significance;, features a modification of the amino acid from K to Q at position 223.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from T to M at position 224.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from C to S at position 230.
+The protein's natural variant, known as in STGD1; unknown pathological significance;, features a modification of the amino acid from I to R at position 240.
+The protein's natural variant, known as in STGD1; unknown pathological significance, features a modification of the amino acid from E to D at position 241.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from L to P at position 244.
+The protein's natural variant, known as in STGD1; unknown pathological significance, features a modification of the amino acid from A to T at position 246.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from N to S at position 247.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from D to G at position 249.
+The protein's natural variant, known as in STGD1; unknown pathological significance;, features a modification of the amino acid from R to W at position 290.
+The protein's natural variant, known as in STGD1; unknown pathological significance;, features a modification of the amino acid from P to L at position 291.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from T to N at position 300.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from P to R at position 309.
+The protein's natural variant, known as in CORD3; unknown pathological significance, features a modification of the amino acid from S to C at position 320.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from E to V at position 328.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from R to W at position 333.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from S to C at position 336.
+The protein's natural variant, known as in FFM;, features a modification of the amino acid from W to G at position 339.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from Y to D at position 340.
+The protein's natural variant, known as in STGD1; unknown pathological significance, features a modification of the amino acid from Y to S at position 345.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from N to K at position 380.
+The protein's natural variant, known as in STGD1 and CORD3;, features a modification of the amino acid from A to V at position 407.
+The protein's natural variant, known as in STGD1; unknown pathological significance, features a modification of the amino acid from I to T at position 410.
+The protein's natural variant, known as in STGD1; unknown pathological significance, features a modification of the amino acid from N to K at position 415.
+The protein's natural variant, known as in STGD1; unknown pathological significance;, features a modification of the amino acid from F to S at position 418.
+The protein's natural variant, known as benign variant;, features a modification of the amino acid from H to R at position 423.
+The protein's natural variant, known as in STGD1 and RP19; unknown pathological significance, features a modification of the amino acid from V to A at position 424.
+The protein's natural variant, known as in CORD3; unknown pathological significance;, features a modification of the amino acid from Y to C at position 440.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from S to R at position 445.
+The protein's natural variant, known as in RP19; unknown pathological significance;, features a modification of the amino acid from L to M at position 455.
+The protein's natural variant, known as in ARMD2 and STGD1; unknown pathological significance; ATP-binding capacity and retinal stimulation as in wild-type;, features a modification of the amino acid from E to K at position 471.
+The protein's natural variant, known as in STGD1; unknown pathological significance, features a modification of the amino acid from D to E at position 498.
+The protein's natural variant, known as in STGD1; unknown pathological significance;, features a modification of the amino acid from R to C at position 508.
+The protein's natural variant, known as in STGD1; unknown pathological significance;, features a modification of the amino acid from R to C at position 511.
+The protein's natural variant, known as in STGD1; unknown pathological significance;, features a modification of the amino acid from C to R at position 519.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from D to E at position 523.
+The protein's natural variant, known as in STGD1, features a modification of the amino acid from F to C at position 525.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from R to C at position 537.
+The protein's natural variant, known as in STGD1, FFM and CORD3; reduced ATP-binding capacity; abolishes retinal-stimulated ATP hydrolysis; does not affect solubility; does not affect intracellular vesicle localization; significantly reduces substrate binding; drastically reduces basal ATPase activity with little or no substrate stimulation;, features a modification of the amino acid from L to P at position 541.
+The protein's natural variant, known as in STGD1; unknown pathological significance, features a modification of the amino acid from W to R at position 548.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from A to P at position 549.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from G to R at position 550.
+The protein's natural variant, known as in RP19; unknown pathological significance;, features a modification of the amino acid from V to I at position 552.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from R to P at position 572.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from R to Q at position 572.
+The protein's natural variant, known as found in a patient with pattern dystrophy; unknown pathological significance;, features a modification of the amino acid from D to H at position 576.
+The protein's natural variant, known as in STGD1; unknown pathological significance, features a modification of the amino acid from P to L at position 593.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from R to Q at position 602.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from R to W at position 602.
+The protein's natural variant, known as in STGD1; unknown pathological significance, features a modification of the amino acid from Y to C at position 603.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from G to R at position 607.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from G to W at position 607.
+The protein's natural variant, known as in STGD1; moderately decreased protein abundance; highly decreased ATPase activity; highly decreased phospholipid translocase activity;, features a modification of the amino acid from F to I at position 608.
+The protein's natural variant, known as in STGD1; unknown pathological significance;, features a modification of the amino acid from E to K at position 616.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from Q to K at position 635.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from Q to H at position 636.
+The protein's natural variant, known as in CORD3; unknown pathological significance, features a modification of the amino acid from Q to K at position 636.
+The protein's natural variant, known as in STGD1; unknown pathological significance;, features a modification of the amino acid from P to L at position 640.
+The protein's natural variant, known as in STGD1; unknown pathological significance;, features a modification of the amino acid from C to S at position 641.
+The protein's natural variant, known as in CORD3; unknown pathological significance;, features a modification of the amino acid from V to G at position 643.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from V to M at position 643.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from D to N at position 645.
+The protein's natural variant, known as in STGD1; does not affect solubility; does not affect location in cytoplasmic vesicle; does not affect both basal and N-Ret-PE-stimulated ATPase activity; very low substrate binding;, features a modification of the amino acid from R to C at position 653.
+The protein's natural variant, known as in STGD1; unknown pathological significance; does not affect solubility; does not affect location in cytoplasmic vesicle; does not affect both basal and N-Ret-PE-stimulated ATPase activity; very low substrate binding;, features a modification of the amino acid from R to H at position 653.
+The protein's natural variant, known as in CORD3; unknown pathological significance; severely decreases solubility; loss of cytoplasmic vesicle localization;decreases basal ATPase activity below 50%; loss of N-Ret-PE-induced stimulation in ATPase activity; very low substrate binding, features a modification of the amino acid from L to R at position 661.
+The protein's natural variant, known as in STGD1; severely decreases solubility; loss of cytoplasmic vesicle localization;decreases basal ATPase activity below 50%; loss of N-Ret-PE-induced stimulation in ATPase activity; very low substrate binding;, features a modification of the amino acid from L to S at position 686.
+The protein's natural variant, known as in STGD1; unknown pathological significance; severely decreases solubility; loss of cytoplasmic vesicle localization; very low substrate binding, features a modification of the amino acid from G to V at position 690.
+The protein's natural variant, known as in STGD1; does not affect solubility; does not affect location in cytoplasmic vesicle; does not affect both basal and N-Ret-PE-stimulated ATPase activity; decreases N-Ret-PE binding in the range of 40-70%;, features a modification of the amino acid from T to M at position 716.
+The protein's natural variant, known as in STGD1; unknown pathological significance, features a modification of the amino acid from F to S at position 754.
+The protein's natural variant, known as in ARMD2, features a modification of the amino acid from A to E at position 762.
+The protein's natural variant, known as in STGD1; does not affect solubility; does not affect location in cytoplasmic vesicle; does not affect both basal and N-Ret-PE-stimulated ATPase activity; decreases N-Ret-PE binding in the range of 40-70%;, features a modification of the amino acid from C to Y at position 764.
+The protein's natural variant, known as in STGD1; severely decreases solubility; loss of cytoplasmic vesicle localization;decreases basal ATPase activity below 50%; loss of N-Ret-PE-induced stimulation in ATPase activity; very low substrate binding;, features a modification of the amino acid from S to N at position 765.
+The protein's natural variant, known as in STGD1; severely decreases solubility; loss of cytoplasmic vesicle localization;decreases basal ATPase activity below 50%; loss of N-Ret-PE-induced stimulation in ATPase activity; very low substrate binding;, features a modification of the amino acid from S to R at position 765.
+The protein's natural variant, known as in STGD1; also found in a patient with macular dystrophy; severely decreases solubility; loss of cytoplasmic vesicle localization; decreases basal ATPase activity below 50%; severely decreases N-Ret-PE-stimulated ATPase activity; very low substrate binding;, features a modification of the amino acid from V to D at position 767.
+The protein's natural variant, known as in STGD1; severely decreases solubility; loss of cytoplasmic vesicle localization;decreases basal ATPase activity below 50%; loss of N-Ret-PE-induced stimulation in ATPase activity; very low substrate binding;, features a modification of the amino acid from L to P at position 797.
+The protein's natural variant, known as in STGD1; unknown pathological significance, features a modification of the amino acid from G to V at position 816.
+The protein's natural variant, known as in ARMD2 and STGD1; reduced ATP-binding capacity; moderately decreases solubility; loss of cytoplasmic vesicle localization; decreases ATPase activity between 50% and 80%; decreases modestly N-Ret-PE-stimulated ATPase; very low substrate binding;, features a modification of the amino acid from G to E at position 818.
+The protein's natural variant, known as in STGD1; moderately decreases solubility; loss of cytoplasmic vesicle localization; decreases ATPase activity between 50% and 80%; decreases modestly N-Ret-PE-stimulated ATPase; very low substrate binding;, features a modification of the amino acid from W to R at position 821.
+The protein's natural variant, known as in STGD1; moderately decreases solubility; loss of cytoplasmic vesicle localization; decreases ATPase activity between 50% and 80%; decreases modestly N-Ret-PE-stimulated ATPase; very low substrate binding, features a modification of the amino acid from I to T at position 824.
+The protein's natural variant, known as in STGD1; unknown pathological significance; severely decreases solubility; loss of cytoplasmic vesicle localization;decreases basal ATPase activity below 50%; loss of N-Ret-PE-induced stimulation in ATPase activity; very low substrate binding, features a modification of the amino acid from M to R at position 840.
+The protein's natural variant, known as severely decreases solubility; loss of cytoplasmic vesicle localization; decreases basal ATPase activity below 50%; severely decreases N-Ret-PE-stimulated ATPase activity; very low substrate binding;, features a modification of the amino acid from D to H at position 846.
+The protein's natural variant, known as in STGD1; does not affect solubility; does not affect location in cytoplasmic vesicle; does not affect both basal and N-Ret-PE-stimulated ATPase activity; decreases N-Ret-PE binding in the range of 40-70%;, features a modification of the amino acid from V to A at position 849.
+The protein's natural variant, known as in STGD1; highly reduced ATP-binding capacity; severely decreases solubility; loss of cytoplasmic vesicle localization;decreases basal ATPase activity below 50%; loss of N-Ret-PE-induced stimulation in ATPase activity; very low substrate binding;, features a modification of the amino acid from G to D at position 851.
+The protein's natural variant, known as in STGD1; does not affect solubility; does not affect location in cytoplasmic vesicle; decreases ATPase activity between 50% and 80%; decreases modestly N-Ret-PE-stimulated ATPase; decreases N-Ret-PE binding in the range of 40-70%;, features a modification of the amino acid from A to T at position 854.
+The protein's natural variant, known as in STGD1, FFM and CORD3; also found in a patient with bull's eye maculopathy; mild alteration probably leading to disease phenotype only in combination with a more severe allele; frequent mutation in northern Europe in linkage disequilibrium with the polymorphic variant Q-943; reduced ATP-binding capacity and retinal-stimulated ATP hydrolysis; significantly attenuates 11-cis-retinal binding; decreases about 80% the N-retinylidene-phosphatidylethanolamine transport activity; stimulates modestely the retinal-stimulated ATPase activity; does not affect ATP-independent N-retinylidene-phosphatidylethanolamine binding. Does not affect ATP-dependent release of N-retinylidene-phosphatidylethanolamine; significantly reduces phosphatidylethanolamine flippase activity;, features a modification of the amino acid from G to A at position 863.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from F to L at position 873.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from T to I at position 897.
+The natural variant of this protein is characterized by an amino acid alteration from H to R at position 914.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from V to M at position 931.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from V to A at position 935.
+The protein's natural variant, known as in linkage disequilibrium with A-863 in the European population and STGD1; found in a patient with macular dystrophy; unknown pathological significance; decreases 11-cis-Retinal binding affinity by 100-fold;, features a modification of the amino acid from R to Q at position 943.
+The protein's natural variant, known as in STGD1 and FFM;, features a modification of the amino acid from R to W at position 943.
+The protein's natural variant, known as in STGD1; unknown pathological significance;, features a modification of the amino acid from Y to D at position 954.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from Q to R at position 957.
+The protein's natural variant, known as in STGD1; moderately decreased protein abundance; highly decreased ATPase activity; highly decreased phospholipid translocase activity;, features a modification of the amino acid from T to I at position 959.
+The protein's natural variant, known as in STGD1; reduced retinal-stimulated ATP hydrolysis; moderately decreased protein abundance; highly decreased ATPase activity; highly decreased phospholipid translocase activity; decreases about 60% the N-retinylidene-phosphatidylethanolamine transfer activity; stimulates modestly the retinal-stimulated ATPase activity; does not affect ATP-independent N-retinylidene-phosphatidylethanolamine binding; does not affect ATP-dependent release of N-retinylidene-phosphatidylethanolamine; significantly reduces phosphatidylethanolamine flippase activity;, features a modification of the amino acid from N to S at position 965.
+The protein's natural variant, known as in STGD1; unknown pathological significance, features a modification of the amino acid from N to Y at position 965.
+The protein's natural variant, known as in STGD1; unknown pathological significance;, features a modification of the amino acid from T to P at position 970.
+The protein's natural variant, known as in STGD1; highly reduced ATP-binding capacity; abolishes retinal-stimulated ATP hydrolysis;, features a modification of the amino acid from T to N at position 971.
+The protein's natural variant, known as in STGD1; unknown pathological significance;, features a modification of the amino acid from T to N at position 972.
+The protein's natural variant, known as in STGD1; unknown pathological significance, features a modification of the amino acid from L to S at position 973.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from S to P at position 974.
+The protein's natural variant, known as in STGD1; unknown pathological significance, features a modification of the amino acid from T to P at position 977.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from G to C at position 978.
+The protein's natural variant, known as in STGD1; unknown pathological significance;, features a modification of the amino acid from G to D at position 978.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from V to A at position 989.
+The protein's natural variant, known as in FFM and STGD1;, features a modification of the amino acid from G to R at position 991.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from L to R at position 1014.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from T to A at position 1019.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from T to M at position 1019.
+The protein's natural variant, known as in STGD1; unknown pathological significance, features a modification of the amino acid from E to G at position 1022.
+The protein's natural variant, known as in STGD1; unknown pathological significance;, features a modification of the amino acid from E to K at position 1022.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from K to E at position 1031.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from E to K at position 1036.
+The protein's natural variant, known as in STGD1, FFM and CORD3; frequent mutation; reduced ATP-binding and retinal-stimulated ATP hydrolysis; decreases solubility at 70%; does not affect intracellular vesicle localization; significantly reduces substrate binding in the absence of ATP; reduces basal ATPase activity;, features a modification of the amino acid from A to V at position 1038.
+The protein's natural variant, known as in STGD1; unknown pathological significance;, features a modification of the amino acid from G to D at position 1050.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from R to W at position 1055.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from S to P at position 1063.
+The protein's natural variant, known as in STGD1; reduced ATP-binding capacity;, features a modification of the amino acid from S to L at position 1071.
+The protein's natural variant, known as in STGD1, features a modification of the amino acid from V to A at position 1072.
+The protein's natural variant, known as in STGD1; unknown pathological significance, features a modification of the amino acid from I to L at position 1074.
+The protein's natural variant, known as in STGD1; unknown pathological significance, features a modification of the amino acid from G to E at position 1078.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from E to D at position 1087.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from E to K at position 1087.
+The protein's natural variant, known as in FFM and STGD1; decreases solubilized at 70%; does not affect intracellular vesicle localization; does not affect substrate binding; drastically reduces basal ATPase activity with little or no substrate stimulation;, features a modification of the amino acid from G to E at position 1091.
+The protein's natural variant, known as in STGD1; unknown pathological significance, features a modification of the amino acid from P to T at position 1094.
+The protein's natural variant, known as in STGD1, features a modification of the amino acid from R to C at position 1097.
+The protein's natural variant, known as in STGD1; unknown pathological significance, features a modification of the amino acid from R to S at position 1097.
+The protein's natural variant, known as in STGD1; unknown pathological significance;, features a modification of the amino acid from R to C at position 1098.
+The protein's natural variant, known as in STGD1; unknown pathological significance;, features a modification of the amino acid from S to P at position 1099.
+The protein's natural variant, known as in STGD1 and FFM; reduced ATP-binding capacity;, features a modification of the amino acid from R to C at position 1108.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from R to H at position 1108.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from R to L at position 1108.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from T to N at position 1112.
+The protein's natural variant, known as in STGD1 and CORD3;, features a modification of the amino acid from E to K at position 1122.
+The protein's natural variant, known as in STGD1; may predispose to develop retinal toxicity after treatment with chloroquine and hydroxychloroquine;, features a modification of the amino acid from R to C at position 1129.
+The protein's natural variant, known as in ARMD2 and STGD1; also found in patients with fundus flavimaculatus; reduced ATP-binding capacity;, features a modification of the amino acid from R to L at position 1129.
+The protein's natural variant, known as in STGD1; unknown pathological significance;, features a modification of the amino acid from I to T at position 1130.
+The protein's natural variant, known as in STGD1; unknown pathological significance, features a modification of the amino acid from C to W at position 1140.
+The protein's natural variant, known as in CORD3; unknown pathological significance, features a modification of the amino acid from L to H at position 1145.
+The natural variant of this protein is characterized by an amino acid alteration from K to T at position 1148.
+The protein's natural variant, known as in STGD1; unknown pathological significance;, features a modification of the amino acid from L to S at position 1159.
+The protein's natural variant, known as in STGD1; unknown pathological significance;, features a modification of the amino acid from R to H at position 1161.
+The protein's natural variant, known as in CORD3; unknown pathological significance;, features a modification of the amino acid from G to C at position 1183.
+The protein's natural variant, known as in STGD1; may predispose to develop retinal toxicity after treatment with chloroquine and hydroxychloroquine;, features a modification of the amino acid from L to R at position 1201.
+The protein's natural variant, known as in STGD1, features a modification of the amino acid from G to D at position 1203.
+The protein's natural variant, known as in CORD3; unknown pathological significance;, features a modification of the amino acid from G to E at position 1203.
+The protein's natural variant, known as in STGD1; unknown pathological significance, features a modification of the amino acid from G to R at position 1203.
+The protein's natural variant, known as in STGD1; found in a patient with age-related macular degeneration; unknown pathological significance;, features a modification of the amino acid from D to N at position 1204.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from L to P at position 1250.
+The protein's natural variant, known as in FFM; unknown pathological significance;, features a modification of the amino acid from T to M at position 1253.
+The protein's natural variant, known as in STGD1; unknown pathological significance;, features a modification of the amino acid from R to Q at position 1300.
+The protein's natural variant, known as in CORD3; unknown pathological significance;, features a modification of the amino acid from R to C at position 1368.
+The protein's natural variant, known as in STGD1; unknown pathological significance, features a modification of the amino acid from K to N at position 1371.
+The protein's natural variant, known as in STGD1; also found in a patient with chorioretinal atrophy; reduced ATP-binding capacity; moderately decreases solubility; loss of cytoplasmic vesicle localization; decreases ATPase activity between 50% and 80%; decreases modestly N-Ret-PE-stimulated ATPase;, features a modification of the amino acid from P to L at position 1380.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from L to P at position 1388.
+The protein's natural variant, known as in STGD1; does not affect solubility; does not affect location in cytoplasmic vesicle; does not affect both basal and N-Ret-PE-stimulated ATPase activity; increases N-Ret-PE binding;, features a modification of the amino acid from E to K at position 1399.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from H to Y at position 1406.
+The protein's natural variant, known as in STGD1; does not affect secondary structure; decreases structural flexibility; significantly decreases all-trans-retinal binding;, features a modification of the amino acid from W to L at position 1408.
+The protein's natural variant, known as in STGD1; reduced retinal-stimulated ATP hydrolysis;, features a modification of the amino acid from W to R at position 1408.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from V to A at position 1429.
+The protein's natural variant, known as in STGD1, features a modification of the amino acid from L to P at position 1430.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from V to I at position 1433.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from G to D at position 1439.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from F to S at position 1440.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from F to V at position 1440.
+The protein's natural variant, known as in STGD1; unknown pathological significance;, features a modification of the amino acid from N to K at position 1442.
+The protein's natural variant, known as in STGD1; loss of the majority of alpha-helical secondary structure; does not bind all-trans-retinal; does not affect conformational change;, features a modification of the amino acid from R to H at position 1443.
+The protein's natural variant, known as in STGD1; unknown pathological significance, features a modification of the amino acid from P to S at position 1484.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from P to L at position 1486.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from C to F at position 1488.
+The protein's natural variant, known as in STGD1 and FFM; also found in a patient with chorioretinal atrophy; reduced retinal-stimulated ATP hydrolysis; does not affect secondary structure; oss of structural flexibility; significantly decreases all-trans-retinal binding;, features a modification of the amino acid from C to R at position 1488.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from C to Y at position 1488.
+The protein's natural variant, known as in STGD1 and CORD3; reduced retinal-stimulated ATP hydrolysis;, features a modification of the amino acid from C to Y at position 1490.
+The protein's natural variant, known as in STGD1; unknown pathological significance, features a modification of the amino acid from P to L at position 1503.
+The protein's natural variant, known as in FFM, features a modification of the amino acid from G to C at position 1508.
+The protein's natural variant, known as in STGD1; unknown pathological significance;, features a modification of the amino acid from P to H at position 1511.
+The protein's natural variant, known as in STGD1; unknown pathological significance;, features a modification of the amino acid from P to R at position 1512.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from Q to R at position 1513.
+The protein's natural variant, known as in ARMD2;, features a modification of the amino acid from R to S at position 1517.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from L to P at position 1525.
+The protein's natural variant, known as in STGD1; also found in a patient with chorioretinal atrophy; reduced retinal-stimulated ATP hydrolysis;, features a modification of the amino acid from T to M at position 1526.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from D to N at position 1532.
+The protein's natural variant, known as in STGD1; moderately decreased protein abundance; moderately decreased ATPase activity; moderately decreased phospholipid translocase activity;, features a modification of the amino acid from T to M at position 1537.
+The protein's natural variant, known as in STGD1; unknown pathological significance, features a modification of the amino acid from R to T at position 1556.
+The protein's natural variant, known as found in a patient with chorioretinal atrophy; unknown pathological significance;, features a modification of the amino acid from Y to C at position 1557.
+The protein's natural variant, known as in STGD1, FFM, ARMD2 and CORD3; found in a patient with bull's eye maculopathy; unknown pathological significance;, features a modification of the amino acid from I to T at position 1562.
+The protein's natural variant, known as in ARMD2;, features a modification of the amino acid from G to R at position 1578.
+The protein's natural variant, known as in STGD1; also found in a patient with macular dystrophy; unknown pathological significance;, features a modification of the amino acid from G to R at position 1591.
+The protein's natural variant, known as in CORD3 and STGD1; unknown pathological significance;, features a modification of the amino acid from A to D at position 1598.
+The protein's natural variant, known as unknown pathological significance;, features a modification of the amino acid from G to V at position 1623.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from L to P at position 1631.
+The protein's natural variant, known as in STGD1, FFM and CORD3;, features a modification of the amino acid from R to Q at position 1640.
+The protein's natural variant, known as in STGD1 and CORD3;, features a modification of the amino acid from R to W at position 1640.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from Y to D at position 1652.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from S to P at position 1689.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from V to I at position 1693.
+The protein's natural variant, known as in STGD1; unknown pathological significance; does not affect solubility; does not affect location in cytoplasmic vesicle; does not affect both basal and N-Ret-PE-stimulated ATPase activity; increases N-Ret-PE binding;, features a modification of the amino acid from S to N at position 1696.
+The protein's natural variant, known as in STGD1; unknown pathological significance; does not affect solubility; does not affect location in cytoplasmic vesicle;decreases basal ATPase activity below 50%; loss of N-Ret-PE-induced stimulation in ATPase activity;, features a modification of the amino acid from Q to E at position 1703.
+The protein's natural variant, known as in STGD1; moderately decreases solubility; loss of cytoplasmic vesicle localization;decreases basal ATPase activity below 50%; loss of N-Ret-PE-induced stimulation in ATPase activity, features a modification of the amino acid from Q to K at position 1703.
+The protein's natural variant, known as in STGD1; moderately decreases solubility; loss of cytoplasmic vesicle localization; decreases ATPase activity between 50% and 80%; decreases modestly N-Ret-PE-stimulated ATPase;, features a modification of the amino acid from R to L at position 1705.
+The protein's natural variant, known as in STGD1; unknown pathological significance;, features a modification of the amino acid from R to Q at position 1705.
+The protein's natural variant, known as in ARMD2, features a modification of the amino acid from W to C at position 1724.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from L to P at position 1729.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from M to T at position 1733.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from S to P at position 1736.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from G to R at position 1748.
+The protein's natural variant, known as in STGD1; unknown pathological significance, features a modification of the amino acid from Y to D at position 1754.
+The protein's natural variant, known as in STGD1; unknown pathological significance;, features a modification of the amino acid from A to D at position 1762.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from L to P at position 1763.
+The protein's natural variant, known as found in a patient with chorioretinal atrophy; unknown pathological significance; severely decreases solubility; loss of cytoplasmic vesicle localization; decreases basal ATPase activity below 50%; loss of N-Ret-PE-induced stimulation in ATPase activity, features a modification of the amino acid from A to E at position 1773.
+The protein's natural variant, known as in STGD1; unknown pathological significance; severely decreases solubility; loss of cytoplasmic vesicle localization; decreases basal ATPase activity below 50%; loss of N-Ret-PE-induced stimulation in ATPase activity;, features a modification of the amino acid from A to V at position 1773.
+The protein's natural variant, known as in STGD1; unknown pathological significance;, features a modification of the amino acid from I to N at position 1775.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from P to L at position 1776.
+The protein's natural variant, known as in STGD1; unknown pathological significance, features a modification of the amino acid from Y to H at position 1779.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from P to A at position 1780.
+The protein's natural variant, known as in STGD1; also found in a patient with bull's eye maculopathy; unknown pathological significance; moderately decreases solubility; loss of cytoplasmic vesicle localization; decreases basal ATPase activity below 50%; severely decreases N-Ret-PE-stimulated ATPase activity;, features a modification of the amino acid from A to D at position 1794.
+The protein's natural variant, known as in STGD1; unknown pathological significance; loss of cytoplasmic vesicle localization; decreases ATPase activity between 50% and 80%; decreases modestly N-Ret-PE-stimulated ATPase; decreases solubility below 50%; significantly reduces N-Ret-PE binding in the absence of ATP;, features a modification of the amino acid from A to P at position 1794.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from N to D at position 1799.
+The protein's natural variant, known as in STGD1; does not affect solubility; does not affect location in cytoplasmic vesicle; decreases ATPase activity between 50% and 80%; decreases modestly N-Ret-PE-stimulated ATPase;, features a modification of the amino acid from N to D at position 1805.
+The natural variant of this protein is characterized by an amino acid alteration from E to D at position 1817.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from R to P at position 1820.
+The protein's natural variant, known as in STGD1; unknown pathological significance; moderately decreases solubility; loss of cytoplasmic vesicle localization; decreases basal ATPase activity below 50%; decreases modestly N-Ret-PE-stimulated ATPase;, features a modification of the amino acid from H to D at position 1838.
+The protein's natural variant, known as in STGD1; unknown pathological significance; does not affect solubility; does not affect location in cytoplasmic vesicle; decreases basal ATPase activity between 50% and 80%; decreases modestly N-Ret-PE-stimulated ATPase;, features a modification of the amino acid from H to N at position 1838.
+The protein's natural variant, known as in STGD1; moderately decreases solubility; loss of cytoplasmic vesicle localization; decreases basal ATPase activity below 50%; severely decreases N-Ret-PE-stimulated ATPase activity;, features a modification of the amino acid from H to Y at position 1838.
+The protein's natural variant, known as in STGD1; does not affect solubility; does not affect location in cytoplasmic vesicle; decreases ATPase activity between 50% and 80%; decreases modestly N-Ret-PE-stimulated ATPase; does not affect N-Ret-PE binding;, features a modification of the amino acid from R to W at position 1843.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from I to T at position 1846.
+The protein's natural variant, known as in STGD1; slightly reduced retinal-stimulated ATP hydrolysis; does not affect solubility; does not affect location in cytoplasmic vesicle; does not affect both basal and N-Ret-PE-stimulated ATPase activity; does not affect N-Ret-PE binding;, features a modification of the amino acid from N to I at position 1868.
+The protein's natural variant, known as in CORD3; unknown pathological significance;, features a modification of the amino acid from M to I at position 1882.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from V to E at position 1884.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from E to K at position 1885.
+The protein's natural variant, known as in STGD1; highly reduced ATP-binding capacity;, features a modification of the amino acid from G to E at position 1886.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from V to D at position 1896.
+The protein's natural variant, known as does not affect solubility; does not affect location in cytoplasmic vesicle; does not affect both basal and N-Ret-PE-stimulated ATPase activity;, features a modification of the amino acid from R to C at position 1898.
+The protein's natural variant, known as in STGD1 and ARMD2; does not affect solubility; does not affect location in cytoplasmic vesicle; does not affect both basal and N-Ret-PE-stimulated ATPase activity; Increases N-Ret-PE binding;, features a modification of the amino acid from R to H at position 1898.
+The protein's natural variant, known as in STGD1; unknown pathological significance, features a modification of the amino acid from V to G at position 1921.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from V to M at position 1921.
+The protein's natural variant, known as in STGD1 and FFM;, features a modification of the amino acid from L to P at position 1940.
+The protein's natural variant, known as in STGD1; unknown pathological significance;, features a modification of the amino acid from E to Q at position 1942.
+The natural variant of this protein is characterized by an amino acid alteration from P to S at position 1948.
+The protein's natural variant, known as in STGD1, FFM and CORD3; also found patients with cone dystrophy and with macular dystrophy; frequent mutation; may be associated with ARMD2; inhibition of ATP hydrolysis by retinal;, features a modification of the amino acid from G to E at position 1961.
+The protein's natural variant, known as in STGD1; unknown pathological significance;, features a modification of the amino acid from G to R at position 1961.
+The protein's natural variant, known as in ARMD2, FFM and STGD1; also found in a patient with cone dystrophy;, features a modification of the amino acid from L to F at position 1970.
+The protein's natural variant, known as in FFM; highly reduced ATP-binding capacity; abolishes basal and retinal-stimulated ATP hydrolysis;, features a modification of the amino acid from L to R at position 1971.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from G to R at position 1975.
+The protein's natural variant, known as in STGD1 and ARMD2; highly reduced ATP-binding capacity; inhibition of ATP hydrolysis by retinal;, features a modification of the amino acid from G to S at position 1977.
+The protein's natural variant, known as in STGD1; unknown pathological significance, features a modification of the amino acid from C to Y at position 2017.
+The protein's natural variant, known as in STGD1; unknown pathological significance;, features a modification of the amino acid from I to T at position 2023.
+The protein's natural variant, known as in STGD1 and FFM; also found in a patient with chorioretinal atrophy; highly reduced ATP-binding capacity;, features a modification of the amino acid from L to F at position 2027.
+The protein's natural variant, known as in STGD1 and FFM;, features a modification of the amino acid from R to Q at position 2030.
+The protein's natural variant, known as in STGD1; unknown pathological significance;, features a modification of the amino acid from H to R at position 2032.
+The protein's natural variant, known as in STGD1; unknown pathological significance;, features a modification of the amino acid from L to R at position 2033.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from L to P at position 2035.
+The protein's natural variant, known as in STGD1; highly reduced ATP-binding capacity;, features a modification of the amino acid from R to W at position 2038.
+The protein's natural variant, known as in STGD1; unknown pathological significance;, features a modification of the amino acid from R to Q at position 2040.
+The protein's natural variant, known as in STGD1; unknown pathological significance, features a modification of the amino acid from V to G at position 2042.
+The protein's natural variant, known as in CORD3; unknown pathological significance;, features a modification of the amino acid from P to S at position 2043.
+The protein's natural variant, known as in ARMD2, features a modification of the amino acid from I to N at position 2047.
+The protein's natural variant, known as in STGD1 and CORD3; may act as a modifier of macular dystrophy in patients who also have a Trp-172 mutation in PRPH2;, features a modification of the amino acid from V to L at position 2050.
+The natural variant of this protein is characterized by an amino acid alteration from G to A at position 2059.
+The protein's natural variant, known as in CORD3;, features a modification of the amino acid from L to R at position 2060.
+The protein's natural variant, known as in STGD1; unknown pathological significance;, features a modification of the amino acid from A to T at position 2064.
+The protein's natural variant, known as in STGD1, features a modification of the amino acid from Y to F at position 2071.
+The protein's natural variant, known as in STGD1; unknown pathological significance;, features a modification of the amino acid from G to V at position 2074.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from R to G at position 2077.
+The protein's natural variant, known as in STGD1; highly reduced ATP-binding capacity; decreases solubility at 50 %; loss of intracellular vesicle localization; drastically reduced basal activity with little or no substrate stimulation;, features a modification of the amino acid from R to W at position 2077.
+The protein's natural variant, known as in STGD1; unknown pathological significance, features a modification of the amino acid from K to E at position 2078.
+The protein's natural variant, known as in STGD1; inhibition of ATP hydrolysis by retinal;, features a modification of the amino acid from E to K at position 2096.
+The protein's natural variant, known as in STGD1; unknown pathological significance;, features a modification of the amino acid from P to S at position 2097.
+The protein's natural variant, known as in STGD1 and FFM; reduced ATP-binding capacity;, features a modification of the amino acid from R to C at position 2106.
+The protein's natural variant, known as in STGD1; found in a patient with bull's eye maculopathy; unknown pathological significance;, features a modification of the amino acid from R to C at position 2107.
+The protein's natural variant, known as in STGD1 and CORD3; may predispose to develop retinal toxicity after treatment with chloroquine and hydroxychloroquine;, features a modification of the amino acid from R to H at position 2107.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from H to R at position 2128.
+The protein's natural variant, known as in STGD1; unknown pathological significance;, features a modification of the amino acid from E to K at position 2131.
+The protein's natural variant, known as in ARMD2, features a modification of the amino acid from C to Y at position 2137.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from R to W at position 2139.
+The protein's natural variant, known as in STGD1; unknown pathological significance;, features a modification of the amino acid from L to Q at position 2140.
+The protein's natural variant, known as in CORD3;, features a modification of the amino acid from G to D at position 2146.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from R to L at position 2149.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from C to R at position 2150.
+The protein's natural variant, known as in STGD1 and CORD3;, features a modification of the amino acid from C to Y at position 2150.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from K to R at position 2160.
+The protein's natural variant, known as in CORD3, ARMD2 and STGD1; unknown pathological significance; increased retinal-stimulated ATP hydrolysis;, features a modification of the amino acid from D to N at position 2177.
+The protein's natural variant, known as in STGD1; unknown pathological significance;, features a modification of the amino acid from F to S at position 2188.
+The protein's natural variant, known as in STGD1; unknown pathological significance, features a modification of the amino acid from L to P at position 2221.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from L to P at position 2229.
+The protein's natural variant, known as in STGD1; unknown pathological significance, features a modification of the amino acid from T to P at position 2237.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from L to V at position 2241.
+The protein's natural variant, known as benign variant;, features a modification of the amino acid from S to I at position 2255.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from R to L at position 2263.
+The protein's natural variant, known as in LEUDEN; unknown pathological significance; reduced phosphorylation of eukaryotic translation initiation factor 2-alpha in patient cells, features a modification of the amino acid from M to L at position 11.
+The protein's natural variant, known as in LEUDEN; unknown pathological significance, features a modification of the amino acid from N to S at position 32.
+The protein's natural variant, known as in DYT33; unknown pathological significance; gain-of-function variant resulting in increased levels of phosphorylated EIF2AK2 and EIF2A in patient cells compared to controls, features a modification of the amino acid from N to T at position 32.
+The protein's natural variant, known as in LEUDEN; unknown pathological significance, features a modification of the amino acid from S to F at position 97.
+The protein's natural variant, known as in LEUDEN; unknown pathological significance, features a modification of the amino acid from A to S at position 109.
+The protein's natural variant, known as in LEUDEN; unknown pathological significance, features a modification of the amino acid from A to V at position 109.
+The protein's natural variant, known as found in a patient with dysmorphic facies, syndactyly, congenital microcephaly and global developmental delay; unknown pathological significance, features a modification of the amino acid from L to Q at position 114.
+The protein's natural variant, known as in DYT33; gain-of-function variant resulting in increased levels of phosphorylated EIF2AK2 and EIF2A in patient cells compared to controls, features a modification of the amino acid from G to R at position 130.
+The protein's natural variant, known as in LEUDEN; unknown pathological significance; reduced phosphorylation of eukaryotic translation initiation factor 2-alpha in patient cells, features a modification of the amino acid from Y to F at position 133.
+The protein's natural variant, known as in DYT33; unknown pathological significance, features a modification of the amino acid from G to A at position 138.
+The protein's natural variant, known as in LEUDEN; unknown pathological significance, features a modification of the amino acid from G to S at position 325.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation, features a modification of the amino acid from L to V at position 439.
+The protein's natural variant, known as in LEUDEN; unknown pathological significance; reduced phosphorylation of eukaryotic translation initiation factor 2-alpha in patient cells, features a modification of the amino acid from S to C at position 461.
+The protein's natural variant, known as in strain: Isolate #5800, features a modification of the amino acid from I to V at position 39.
+The protein's natural variant, known as in CIRRH;, features a modification of the amino acid from G to V at position 53.
+The protein's natural variant, known as in CIRRH, features a modification of the amino acid from Y to C at position 54.
+The protein's natural variant, known as in CIRRH;, features a modification of the amino acid from G to C at position 62.
+The natural variant of this protein is characterized by an amino acid alteration from S to G at position 417.
+The protein's natural variant, known as in serotype 8, features a modification of the amino acid from M to A at position 61.
+The protein's natural variant, known as in serotype 8, features a modification of the amino acid from M to T at position 91.
+The protein's natural variant, known as in serotype 8, features a modification of the amino acid from GM to DV at position 126.
+The protein's natural variant, known as in serotype 8, features a modification of the amino acid from S to N at position 213.
+The protein's natural variant, known as in serotype 8, features a modification of the amino acid from T to A at position 416.
+The protein's natural variant, known as in serotype 8, features a modification of the amino acid from F to K at position 469.
+The protein's natural variant, known as in serotype 8, features a modification of the amino acid from L to Q at position 606.
+The protein's natural variant, known as in serotype 8, features a modification of the amino acid from S to R at position 638.
+The protein's natural variant, known as in strain: USDA 6, features a modification of the amino acid from P to H at position 98.
+The protein's natural variant, known as in strain: USDA 142, USDA 136 and USDA 122, features a modification of the amino acid from P to L at position 98.
+The protein's natural variant, known as confers novobiocin resistance, features a modification of the amino acid from S to L at position 127.
+The protein's natural variant, known as in DYTSPG, features a modification of the amino acid from N to K at position 106.
+The protein's natural variant, known as in CMT4F;, features a modification of the amino acid from D to N at position 651.
+The natural variant of this protein is characterized by an amino acid alteration from K to E at position 935.
+The protein's natural variant, known as found in a patient with a complex hereditary motor and sensory neuropathy form associated with dysarthria, joints hypermobility and cerebellar signs; unknown pathological significance;, features a modification of the amino acid from R to Q at position 1335.
+The protein's natural variant, known as in DEE94;, features a modification of the amino acid from W to R at position 548.
+The protein's natural variant, known as in DEE94;, features a modification of the amino acid from L to P at position 823.
+The protein's natural variant, known as in a patient with amyotrophic lateral sclerosis;, features a modification of the amino acid from R to L at position 209.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from V to I at position 63.
+The protein's natural variant, known as in strain: Isolate MSB 65041/NK 19644, features a modification of the amino acid from S to N at position 129.
+The protein's natural variant, known as found in a consanguineous family with intellectual disability; unknown pathological significance;, features a modification of the amino acid from R to Q at position 180.
+The protein's natural variant, known as in an asymptomatic patient with ALAD deficiency; also found in a hereditary coproporphyria patient carrying the R-279 mutation in CPOX; hexamer with almost no residual activity;, features a modification of the amino acid from F to L at position 12.
+The protein's natural variant, known as allele ALAD*2; ALAD*2 heterozygous or homozygous carriers have significantly higher blood lead levels than ALAD*1 homozygotes when exposed to environmental lead; fully active octamer;, features a modification of the amino acid from K to N at position 59.
+The protein's natural variant, known as in AHEPP; mixture of about 50% hexamer and 50% octamer; about 10% residual activity;, features a modification of the amino acid from G to R at position 133.
+The protein's natural variant, known as in AHEPP; about 95% octamer; about 40% residual activity;, features a modification of the amino acid from V to M at position 153.
+The protein's natural variant, known as in AHEPP; mixture of about 80% hexamer and 20% octamer; about 4% residual activity;, features a modification of the amino acid from R to W at position 240.
+The protein's natural variant, known as in AHEPP; mixture of about 14% hexamer and 86% octamer; about 20% enzyme residual activity;, features a modification of the amino acid from A to T at position 274.
+The protein's natural variant, known as in AHEPP; mainly octamer; reduced activity;, features a modification of the amino acid from V to M at position 275.
+The protein's natural variant, known as in strain: PI 595203, features a modification of the amino acid from T to P at position 81.
+The protein's natural variant, known as in NEDHYMS; unknown pathological significance; mild decreased editing activity, features a modification of the amino acid from K to E at position 127.
+The protein's natural variant, known as in NEDHYMS; unknown pathological significance; mild decreased editing activity, features a modification of the amino acid from K to N at position 367.
+The protein's natural variant, known as in NEDHYMS; unknown pathological significance; altered ratio of alternative splicing, features a modification of the amino acid from T to A at position 498.
+The protein's natural variant, known as in NEDHYMS; decreased protein stability; strong decreased editing activity, features a modification of the amino acid from R to Q at position 603.
+The protein's natural variant, known as in NEDHYMS; unknown pathological significance; mild decreased editing activity, features a modification of the amino acid from A to V at position 722.
+The natural variant of this protein is characterized by an amino acid alteration from K to R at position 63.
+The protein's natural variant, known as in CSNB1E;, features a modification of the amino acid from D to H at position 126.
+The protein's natural variant, known as in CSNB1E;, features a modification of the amino acid from Y to C at position 220.
+The protein's natural variant, known as in CSNB1E;, features a modification of the amino acid from G to D at position 455.
+The protein's natural variant, known as in CSNB1E;, features a modification of the amino acid from H to Y at position 603.
+The protein's natural variant, known as in strain: ATCC 21705, features a modification of the amino acid from I to T at position 68.
+The protein's natural variant, known as in strain: ATCC 21705, features a modification of the amino acid from L to A at position 70.
+The protein's natural variant, known as in strain: ATCC 21705, features a modification of the amino acid from T to A at position 76.
+The natural variant of this protein is characterized by an amino acid alteration from T to R at position 296.
+The protein's natural variant, known as in CDG1G;, features a modification of the amino acid from T to M at position 67.
+The protein's natural variant, known as in CDG1G;, features a modification of the amino acid from G to R at position 101.
+The protein's natural variant, known as in CDG1G;, features a modification of the amino acid from F to V at position 142.
+The protein's natural variant, known as in CDG1G;, features a modification of the amino acid from R to Q at position 146.
+The protein's natural variant, known as in CDG1G;, features a modification of the amino acid from L to P at position 158.
+The natural variant of this protein is characterized by an amino acid alteration from M to V at position 72.
+The natural variant of this protein is characterized by an amino acid alteration from E to G at position 286.
+The protein's natural variant, known as in 3KS; leads to defects in mitotic chromosome compaction and organization; increases the number of micronuclei; increases cell death;, features a modification of the amino acid from K to E at position 609.
+The protein's natural variant, known as in 3KS; leads to defects in mitotic chromosome compaction and organization; increases the number of micronuclei; increases cell death;, features a modification of the amino acid from T to M at position 693.
+The protein's natural variant, known as in 3KS;, features a modification of the amino acid from T to P at position 850.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation, features a modification of the amino acid from G to C at position 331.
+The protein's natural variant, known as in SPGF57, features a modification of the amino acid from P to S at position 84.
+The protein's natural variant, known as in SPGF57; unknown pathological significance;, features a modification of the amino acid from M to T at position 259.
+The protein's natural variant, known as in mutant dacA11191; inactive but still binds penicillin. Blocked in the release of the bound penicilloyl moiety; the mutant also fails to catalyze the D-alanine carboxypeptidase reaction as the hydrolysis of the acyl-enzyme formed with substrate is also blocked and the acyl-enzyme accumulates, features a modification of the amino acid from G to D at position 134.
+The protein's natural variant, known as in GM2G2;, features a modification of the amino acid from L to S at position 62.
+The protein's natural variant, known as in GM2G2;, features a modification of the amino acid from S to R at position 255.
+The protein's natural variant, known as in GM2G2; adult type; severe;, features a modification of the amino acid from C to Y at position 309.
+The protein's natural variant, known as in GM2G2;, features a modification of the amino acid from P to L at position 417.
+The protein's natural variant, known as in GM2G2;, features a modification of the amino acid from Y to S at position 456.
+The protein's natural variant, known as in GM2G2; decreases the isozyme A transport out of the endoplasmic reticulum. Lowers its heat stability. Affects the ability of isozyme A to hydrolyze GM2 ganglioside;, features a modification of the amino acid from P to S at position 504.
+The protein's natural variant, known as in GM2G2;, features a modification of the amino acid from R to Q at position 505.
+The protein's natural variant, known as in GM2G2; infantile type;, features a modification of the amino acid from C to Y at position 534.
+The protein's natural variant, known as in GM2G2;, features a modification of the amino acid from A to T at position 543.
+The protein's natural variant, known as in SPG88; decreased interaction with RCC1 and DDX21; no effect on interaction with NCBP1 and NCBP2, features a modification of the amino acid from T to I at position 315.
+The protein's natural variant, known as in SPG88; decreased interaction with RCC1 and DDX21; no effect on interaction with NCBP1 and NCBP2, features a modification of the amino acid from L to M at position 328.
+The protein's natural variant, known as in SPG88; loss of interaction with DDX21 and NCBP1; severely decreased interaction with RCC1 and NCBP2; compared to the wild type, the mutant shows increased cytoplasmic levels, features a modification of the amino acid from L to P at position 328.
+The protein's natural variant, known as in SPG88; decreased interaction with RCC1, DDX21, NCBP1 and NCBP2; compared to the wild type, the mutant shows increased cytoplasmic levels, features a modification of the amino acid from L to R at position 334.
+The protein's natural variant, known as in SPG88; loss of interaction with RCC1, DDX21, NCBP1 and NCBP2, features a modification of the amino acid from L to P at position 350.
+The protein's natural variant, known as in SPG88; loss of interaction with RCC1; severely decreased interaction with DDX21 and NCBP1; no effect on interaction with NCBP2, features a modification of the amino acid from P to L at position 415.
+The protein's natural variant, known as in RPSL4 (STRA1); confers streptomycin resistance and hyperaccurate translation, has no effect on natural antibiotic production, features a modification of the amino acid from K to I at position 56.
+The protein's natural variant, known as in RPSL1 (KO-267); confers streptomycin resistance but not hyperaccurate translation, increases natural antibiotic production 10-fold, features a modification of the amino acid from K to R at position 56.
+The protein's natural variant, known as in BBS5;, features a modification of the amino acid from G to S at position 72.
+The protein's natural variant, known as in BBS5; found in patient of Sri Lankan origin; not detected in patients of Northern European origin;, features a modification of the amino acid from T to A at position 183.
+The protein's natural variant, known as found in patients with Bardet-Biedl syndrome carrying homozygous mutations in other BBS genes; might have a modifying effect on disease phenotype;, features a modification of the amino acid from N to S at position 184.
+The protein's natural variant, known as found as heterozygous variant in patients with Bardet-Biedl syndrome; might have a modifying effect on disease phenotype;, features a modification of the amino acid from R to H at position 207.
+The protein's natural variant, known as in CONPM; loss of catalytic activity in patient fibroblasts;, features a modification of the amino acid from P to L at position 81.
+The protein's natural variant, known as in CONPM; unknown pathological significance;, features a modification of the amino acid from A to T at position 99.
+The protein's natural variant, known as in CONPM; loss of catalytic activity in patient fibroblasts;, features a modification of the amino acid from D to N at position 128.
+The protein's natural variant, known as in protamine-Z2, features a modification of the amino acid from S to A at position 7.
+The natural variant of this protein is characterized by an amino acid alteration from Q to P at position 280.
+The natural variant of this protein is characterized by an amino acid alteration from D to V at position 442.
+The natural variant of this protein is characterized by an amino acid alteration from A to V at position 444.
+The protein's natural variant, known as in PROTEUSS and breast cancer; also detected in colorectal and ovarian cancer; somatic mutation; results in increased phosphorylation at T-308 and higher basal ubiquitination; the mutant protein is more efficiently recruited to the plasma membrane; alters phosphatidylinositiol phosphates lipid specificity of the AKT1 PH domain;, features a modification of the amino acid from E to K at position 17.
+The protein's natural variant, known as in CWS6;, features a modification of the amino acid from R to C at position 25.
+The protein's natural variant, known as in CWS6;, features a modification of the amino acid from T to P at position 435.
+The protein's natural variant, known as in strain: Black German Shepherd, features a modification of the amino acid from R to C at position 96.
+The protein's natural variant, known as found in a renal cell carcinoma sample; somatic mutation, features a modification of the amino acid from V to I at position 149.
+The protein's natural variant, known as in CMH;, features a modification of the amino acid from A to V at position 87.
+The protein's natural variant, known as in CMH;, features a modification of the amino acid from A to E at position 95.
+The protein's natural variant, known as in a lung neuroendocrine carcinoma sample; somatic mutation;, features a modification of the amino acid from A to V at position 117.
+The protein's natural variant, known as in benomyl-resistant strain, features a modification of the amino acid from E to K at position 198.
+The protein's natural variant, known as in C1QD, features a modification of the amino acid from G to D at position 42.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from A to T at position 123.
+The protein's natural variant, known as in strain: TW-183, features a modification of the amino acid from K to N at position 87.
+The protein's natural variant, known as in strain: WA / Serotype O:8, features a modification of the amino acid from A to P at position 2.
+The protein's natural variant, known as in strain: WA / Serotype O:8, features a modification of the amino acid from E to D at position 355.
+The protein's natural variant, known as in allele AHRB1; no increase in specific ligand binding, features a modification of the amino acid from M to I at position 324.
+The protein's natural variant, known as in allele AHRB1 and allele AHRD; no reduction in specific ligand binding, features a modification of the amino acid from F to L at position 348.
+The protein's natural variant, known as in allele AHRD; reduced specific ligand binding, features a modification of the amino acid from A to V at position 375.
+The protein's natural variant, known as in allele AHRB1; no increase in specific ligand binding, features a modification of the amino acid from P to L at position 471.
+The protein's natural variant, known as in allele AHRB1; no increase in specific ligand binding, features a modification of the amino acid from N to S at position 533.
+The protein's natural variant, known as in allele AHRD, features a modification of the amino acid from M to I at position 589.
+The protein's natural variant, known as in allele AHRB1; no increase in specific ligand binding, features a modification of the amino acid from M to L at position 589.
+The protein's natural variant, known as in allele AHRB1 and allele AHRD, features a modification of the amino acid from T to A at position 758.
+The protein's natural variant, known as in allele AHRB3, features a modification of the amino acid from I to V at position 808.
+The protein's natural variant, known as in allele AHRB3, features a modification of the amino acid from G to D at position 821.
+The protein's natural variant, known as in allele AHRB3, features a modification of the amino acid from A to V at position 824.
+The protein's natural variant, known as in allele AHRB3, features a modification of the amino acid from TPGGFL to SHLVGSCSSHARMKFIQEQDTGTVRVGHQYYFSKTFDSCI at position 848.
+The protein's natural variant, known as in allele Alaska Silver (EA); darkly pigmented animals; constitutively activated, features a modification of the amino acid from C to R at position 125.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from R to T at position 62.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from Q to H at position 215.
+The protein's natural variant, known as in un, features a modification of the amino acid from G to S at position 103.
+The protein's natural variant, known as in strain: W, features a modification of the amino acid from G to C at position 121.
+The protein's natural variant, known as in breast cancer samples; infiltrating ductal carcinoma; somatic mutation, features a modification of the amino acid from P to T at position 371.
+The protein's natural variant, known as in a gastric adenocarcinoma sample; somatic mutation, features a modification of the amino acid from R to Q at position 407.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from S to G at position 523.
+The protein's natural variant, known as in POROK1; unknown pathological significance, features a modification of the amino acid from K to E at position 69.
+The protein's natural variant, known as increases resistance to terbutryn 300-fold, slightly increases resistance to atrazine and o-phenanthroline, features a modification of the amino acid from G to D at position 193.
+The protein's natural variant, known as decreases degradation of p53/TP53;, features a modification of the amino acid from Q to E at position 67.
+The protein's natural variant, known as decreases degradation of p53/TP53;, features a modification of the amino acid from G to D at position 111.
+The protein's natural variant, known as found in a patient with susceptibility to restless legs syndrome;, features a modification of the amino acid from R to H at position 272.
+The protein's natural variant, known as found in a family with retinitis pigmentosa;, features a modification of the amino acid from R to W at position 142.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from G to S at position 42.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from I to M at position 223.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from M to T at position 8.
+The protein's natural variant, known as may be associated with increased susceptibility to tuberculosis;, features a modification of the amino acid from L to S at position 425.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from G to S at position 683.
+The protein's natural variant, known as in MC1DN18;, features a modification of the amino acid from G to R at position 77.
+The protein's natural variant, known as in MC1DN18;, features a modification of the amino acid from R to P at position 122.
+The protein's natural variant, known as in MC1DN18;, features a modification of the amino acid from A to V at position 165.
+The protein's natural variant, known as in THPH11; HRGTokushima 1; results in increased intracellular degradation and reduced protein secretion;, features a modification of the amino acid from G to E at position 103.
+The protein's natural variant, known as in THPH11; HRGTokushima 2; results in increased intracellular degradation and reduced protein secretion;, features a modification of the amino acid from C to R at position 241.
+The protein's natural variant, known as in SPGFX4; unknown pathological significance;, features a modification of the amino acid from D to N at position 17.
+The protein's natural variant, known as in SPGFX4; unknown pathological significance;, features a modification of the amino acid from V to M at position 76.
+The protein's natural variant, known as in SPGFX4; unknown pathological significance, features a modification of the amino acid from S to R at position 102.
+The protein's natural variant, known as in SPGFX4; unknown pathological significance;, features a modification of the amino acid from N to K at position 182.
+The protein's natural variant, known as in SPGFX4; unknown pathological significance;, features a modification of the amino acid from P to S at position 189.
+The protein's natural variant, known as in SPGFX4; unknown pathological significance;, features a modification of the amino acid from K to N at position 218.
+The protein's natural variant, known as in SPGFX4; unknown pathological significance; requires 2 nucleotide substitutions, features a modification of the amino acid from K to S at position 218.
+The protein's natural variant, known as in SPGFX4; unknown pathological significance;, features a modification of the amino acid from S to P at position 285.
+The protein's natural variant, known as in SPGFX4; unknown pathological significance;, features a modification of the amino acid from S to P at position 295.
+The protein's natural variant, known as in SPGFX4; unknown pathological significance;, features a modification of the amino acid from R to S at position 441.
+The protein's natural variant, known as in SPGFX4; unknown pathological significance;, features a modification of the amino acid from T to I at position 465.
+The protein's natural variant, known as in SPGFX4; unknown pathological significance, features a modification of the amino acid from G to S at position 545.
+The protein's natural variant, known as in SPGFX4; unknown pathological significance;, features a modification of the amino acid from S to W at position 659.
+The protein's natural variant, known as in SPGFX4; unknown pathological significance;, features a modification of the amino acid from R to C at position 664.
+The protein's natural variant, known as in SPGFX4; unknown pathological significance;, features a modification of the amino acid from R to C at position 686.
+The protein's natural variant, known as in strain: ZJ-74, features a modification of the amino acid from T to K at position 181.
+The protein's natural variant, known as in strain: ZJ-74, features a modification of the amino acid from S to L at position 187.
+The protein's natural variant, known as in strain: ZJ-32 and ZJ-60, features a modification of the amino acid from A to T at position 286.
+The protein's natural variant, known as in PREMBL1; unknown pathological significance, features a modification of the amino acid from Q to H at position 74.
+The protein's natural variant, known as in PREMBL1; unknown pathological significance;, features a modification of the amino acid from D to N at position 130.
+The protein's natural variant, known as in PREMBL1; unknown pathological significance, features a modification of the amino acid from A to G at position 240.
+The protein's natural variant, known as in PREMBL1; unknown pathological significance, features a modification of the amino acid from T to R at position 298.
+The protein's natural variant, known as in PREMBL1; unknown pathological significance;, features a modification of the amino acid from R to H at position 338.
+The protein's natural variant, known as in PREMBL1; unknown pathological significance;, features a modification of the amino acid from R to Q at position 409.
+The protein's natural variant, known as in PREMBL1; unknown pathological significance;, features a modification of the amino acid from V to I at position 503.
+The protein's natural variant, known as in PREMBL1; almost complete loss of phosphorylation and reduced interaction with KHDC3L and OOEP;, features a modification of the amino acid from S to Y at position 510.
+The protein's natural variant, known as in PREMBL1; unknown pathological significance, features a modification of the amino acid from D to H at position 522.
+The protein's natural variant, known as in PREMBL1; unknown pathological significance;, features a modification of the amino acid from E to K at position 541.
+The natural variant of this protein is characterized by an amino acid alteration from V to A at position 427.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to H at position 246.
+The protein's natural variant, known as in strain: CA7, features a modification of the amino acid from H to Y at position 42.
+The protein's natural variant, known as in strain: 41552MA, features a modification of the amino acid from K to R at position 89.
+The protein's natural variant, known as in strain: CA8, features a modification of the amino acid from T to S at position 123.
+The protein's natural variant, known as in strain: 21343WI, 41552MA, 42373NY3, HB19 and HB19CT1, features a modification of the amino acid from A to T at position 126.
+The protein's natural variant, known as in strain: 21343WI, 41552MA, HB19 and HB19CT1, features a modification of the amino acid from D to N at position 128.
+The protein's natural variant, known as in strain: CA8, features a modification of the amino acid from Q to P at position 132.
+The protein's natural variant, known as in strain: CA8, features a modification of the amino acid from A to T at position 176.
+The protein's natural variant, known as in strain: CA8, features a modification of the amino acid from S to G at position 189.
+The protein's natural variant, known as in strain: CA8, features a modification of the amino acid from L to F at position 192.
+The protein's natural variant, known as in strain: 21343WI, CA3 and CA7, features a modification of the amino acid from G to V at position 198.
+The protein's natural variant, known as in strain: CA8, features a modification of the amino acid from K to Q at position 218.
+The protein's natural variant, known as in strain: 21343WI, 41552MA, 42373NY3, HB19 and HB19CT1, features a modification of the amino acid from K to T at position 253.
+The protein's natural variant, known as in strain: B5/EGFP, features a modification of the amino acid from K to R at position 77.
+The protein's natural variant, known as in strain: Czech II, features a modification of the amino acid from W to L at position 166.
+The protein's natural variant, known as in strain: Czech II, features a modification of the amino acid from D to E at position 499.
+The protein's natural variant, known as in strain: Czech II, features a modification of the amino acid from E to G at position 503.
+The protein's natural variant, known as in MQ19-97, features a modification of the amino acid from F to L at position 23.
+The protein's natural variant, known as in MQ19-97, features a modification of the amino acid from D to N at position 96.
+The protein's natural variant, known as in CMS25; unknown pathological significance;, features a modification of the amino acid from R to P at position 49.
+The protein's natural variant, known as in strain: CAM-2, CAM-3, CAM-8, CAM-12, CAM-41, CAM-44, CAM-48 and Berkeley, features a modification of the amino acid from E to D at position 170.
+The protein's natural variant, known as in strain: CAM-8, CAM-44, CAM-48 and Berkeley, features a modification of the amino acid from S to I at position 426.
+The protein's natural variant, known as in G- phenotype, features a modification of the amino acid from P to L at position 22.
+The protein's natural variant, known as in G- phenotype, features a modification of the amino acid from S to C at position 180.
+The protein's natural variant, known as in G- phenotype, features a modification of the amino acid from F to L at position 234.
+The protein's natural variant, known as in G- phenotype, features a modification of the amino acid from H to Y at position 237.
+The protein's natural variant, known as in G- phenotype, features a modification of the amino acid from L to V at position 240.
+The protein's natural variant, known as in G- phenotype, features a modification of the amino acid from C to S at position 338.
+The protein's natural variant, known as in G- phenotype, features a modification of the amino acid from E to D at position 369.
+The protein's natural variant, known as in allele 2, features a modification of the amino acid from T to A at position 21.
+The protein's natural variant, known as in allele 2, features a modification of the amino acid from R to C at position 67.
+The protein's natural variant, known as in allele 2, features a modification of the amino acid from R to S at position 301.
+The natural variant of this protein is characterized by an amino acid alteration from RR to QH at position 40.
+The protein's natural variant, known as found in a patient with sporadic periodic paralysis; unknown pathological significance; decreases potassium inward and outward currents density; reduces cell surface abundance; reduces conductance; dominant negative mutation;, features a modification of the amino acid from R to C at position 43.
+The protein's natural variant, known as in TTPP2;, features a modification of the amino acid from T to M at position 140.
+The protein's natural variant, known as in TTPP2; unknown pathological significance; decreases potassium inward and outward currents density; reduces cell surface abundance; reduces open propability; dominant negative mutation;, features a modification of the amino acid from V to M at position 168.
+The protein's natural variant, known as found in a patient with hypokalemic periodic paralysis without hyperthyroidism; reduces potassium inward and outward currents density;, features a modification of the amino acid from G to R at position 169.
+The protein's natural variant, known as found in a patient with sporadic periodic paralysis; unknown pathological significance; abolishes potassium inward and outward currents density; reduces cell surface abundance;, features a modification of the amino acid from A to P at position 200.
+The protein's natural variant, known as in TTPP2; hypermorphic; longer time required for half-maximal current degradation;, features a modification of the amino acid from R to H at position 205.
+The protein's natural variant, known as in TTPP2; small decrease in current density;, features a modification of the amino acid from T to M at position 354.
+The protein's natural variant, known as in TTPP2; abolishes potassium inward and outward currents density, features a modification of the amino acid from K to T at position 360.
+The protein's natural variant, known as in TTPP2; hypermorphic; longer time required for half-maximal current degradation;, features a modification of the amino acid from K to R at position 366.
+The protein's natural variant, known as in TTPP2; reduces potassium inward and outward currents density, features a modification of the amino acid from E to K at position 388.
+The protein's natural variant, known as in BBS11;, features a modification of the amino acid from P to S at position 130.
+The protein's natural variant, known as in a patient with Bardet-Biedl syndrome; unknown pathological significance;, features a modification of the amino acid from R to Q at position 299.
+The protein's natural variant, known as in LGMDR8;, features a modification of the amino acid from R to H at position 394.
+The protein's natural variant, known as in LGMDR8;, features a modification of the amino acid from D to N at position 487.
+The protein's natural variant, known as in strain: cv. Nd-0, cv. No-0, features a modification of the amino acid from VLVS to GLVA at position 36.
+The protein's natural variant, known as in strain: cv. Bay-0, cv. Landsberg erecta, features a modification of the amino acid from S to A at position 36.
+The protein's natural variant, known as in strain: cv. Bay-0, features a modification of the amino acid from S to F at position 194.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from P to S at position 257.
+The protein's natural variant, known as in strain: cv. Bay-0, cv. Cvi-0, cv. Landsberg erecta, cv. Nd-0, cv. No-0, features a modification of the amino acid from I to V at position 298.
+The protein's natural variant, known as in strain: cv. Cvi-0, features a modification of the amino acid from V to I at position 375.
+The protein's natural variant, known as in strain: Pasteur, features a modification of the amino acid from L to V at position 2.
+The protein's natural variant, known as loss-of-function mutation abolishing ligand binding, features a modification of the amino acid from A to E at position 207.
+The protein's natural variant, known as in W37 spotting; impaired protein stability and loss of kinase activity, features a modification of the amino acid from E to K at position 586.
+The protein's natural variant, known as in Wv spotting, features a modification of the amino acid from T to M at position 664.
+The protein's natural variant, known as in W42 spotting; loss of kinase activity and impaired internalization after exposure to KITLG/SCF, features a modification of the amino acid from D to N at position 794.
+The protein's natural variant, known as in W41 spotting; decreased kinase activity, features a modification of the amino acid from V to M at position 835.
+The protein's natural variant, known as in strain: Isolate Hya36, features a modification of the amino acid from P to L at position 22.
+The protein's natural variant, known as in strain: Isolate Hya36, features a modification of the amino acid from I to V at position 63.
+The protein's natural variant, known as in strain: Isolate Hya36, features a modification of the amino acid from R to Q at position 310.
+The protein's natural variant, known as in HSCR1; sporadic form, features a modification of the amino acid from P to L at position 20.
+The protein's natural variant, known as in HSCR1; familial form;, features a modification of the amino acid from S to L at position 32.
+The protein's natural variant, known as in HSCR1, features a modification of the amino acid from L to P at position 40.
+The protein's natural variant, known as in HSCR1; familial form;, features a modification of the amino acid from P to L at position 64.
+The protein's natural variant, known as in HSCR1, features a modification of the amino acid from R to C at position 77.
+The protein's natural variant, known as in HSCR1; unknown pathological significance;, features a modification of the amino acid from G to S at position 93.
+The protein's natural variant, known as in HSCR1; unknown pathological significance;, features a modification of the amino acid from R to C at position 114.
+The protein's natural variant, known as in HSCR1; sporadic form, features a modification of the amino acid from C to S at position 142.
+The protein's natural variant, known as in HSCR1; also in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from V to G at position 145.
+The protein's natural variant, known as in HSCR1, features a modification of the amino acid from P to L at position 155.
+The protein's natural variant, known as in HSCR1; unknown pathological significance, features a modification of the amino acid from C to Y at position 157.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from R to Q at position 163.
+The protein's natural variant, known as in HSCR1; sporadic form, features a modification of the amino acid from F to S at position 174.
+The protein's natural variant, known as in HSCR1, features a modification of the amino acid from R to P at position 175.
+The protein's natural variant, known as in HSCR1; sporadic form, features a modification of the amino acid from R to P at position 180.
+The protein's natural variant, known as in HSCR1; sporadic form, features a modification of the amino acid from C to Y at position 197.
+The protein's natural variant, known as in a patient with renal agenesis; unknown pathological significance; prevents phosphorylation in response to GDNF;, features a modification of the amino acid from P to T at position 198.
+The protein's natural variant, known as in HSCR1; familial form;, features a modification of the amino acid from R to H at position 231.
+The protein's natural variant, known as in HSCR1; familial form;, features a modification of the amino acid from E to K at position 251.
+The protein's natural variant, known as in HSCR1;, features a modification of the amino acid from T to A at position 278.
+The protein's natural variant, known as found in two patients with Hirschsprung disease;, features a modification of the amino acid from T to N at position 278.
+The protein's natural variant, known as in HSCR1, features a modification of the amino acid from T to P at position 278.
+The protein's natural variant, known as in HSCR1; sporadic form;, features a modification of the amino acid from R to Q at position 287.
+The protein's natural variant, known as found in patients with Hirschsprung disease; unknown pathological significance;, features a modification of the amino acid from V to M at position 292.
+The protein's natural variant, known as in HSCR1, features a modification of the amino acid from D to N at position 300.
+The protein's natural variant, known as in HSCR1;, features a modification of the amino acid from R to Q at position 313.
+The protein's natural variant, known as in HSCR1;, features a modification of the amino acid from S to I at position 316.
+The protein's natural variant, known as in HSCR1;, features a modification of the amino acid from R to Q at position 330.
+The protein's natural variant, known as in HSCR1;, features a modification of the amino acid from S to L at position 339.
+The protein's natural variant, known as in HSCR1;, features a modification of the amino acid from D to Y at position 353.
+The protein's natural variant, known as in HSCR1; unknown pathological significance, features a modification of the amino acid from N to K at position 359.
+The protein's natural variant, known as in HSCR1;, features a modification of the amino acid from R to Q at position 360.
+The protein's natural variant, known as in HSCR1, features a modification of the amino acid from R to W at position 360.
+The protein's natural variant, known as in a patient with renal agenesis; unknown pathological significance; constitutively phosphorylated; expressed only the immature intracellular form, features a modification of the amino acid from V to A at position 376.
+The protein's natural variant, known as in HSCR1; familial form;, features a modification of the amino acid from F to L at position 393.
+The protein's natural variant, known as in a patient with renal agenesis; unknown pathological significance; prevents phosphorylation in response to GDNF, features a modification of the amino acid from N to H at position 394.
+The protein's natural variant, known as in HSCR1, features a modification of the amino acid from N to K at position 394.
+The protein's natural variant, known as in HSCR1;, features a modification of the amino acid from V to M at position 397.
+The protein's natural variant, known as in HSCR1; sporadic form;, features a modification of the amino acid from P to L at position 399.
+The protein's natural variant, known as in HSCR1;, features a modification of the amino acid from V to M at position 412.
+The protein's natural variant, known as in HSCR1;, features a modification of the amino acid from G to R at position 423.
+The protein's natural variant, known as found in a patient with congenital central hypoventilation syndrome; unknown pathological significance;, features a modification of the amino acid from A to E at position 432.
+The protein's natural variant, known as in HSCR1; sporadic form;, features a modification of the amino acid from R to Q at position 475.
+The protein's natural variant, known as in HSCR1;, features a modification of the amino acid from E to K at position 480.
+The protein's natural variant, known as in MTC; familial form, features a modification of the amino acid from C to CEEC at position 531.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from G to E at position 593.
+The protein's natural variant, known as in HSCR1;, features a modification of the amino acid from E to Q at position 595.
+The protein's natural variant, known as in MEN2A;, features a modification of the amino acid from C to G at position 609.
+The protein's natural variant, known as in MEN2A;, features a modification of the amino acid from C to R at position 609.
+The protein's natural variant, known as in HSCR1; familial form;, features a modification of the amino acid from C to W at position 609.
+The protein's natural variant, known as in MTC, MEN2A and HSCR1; familial and sporadic forms;, features a modification of the amino acid from C to Y at position 609.
+The protein's natural variant, known as in MTC; familial form;, features a modification of the amino acid from C to G at position 611.
+The protein's natural variant, known as in MEN2A;, features a modification of the amino acid from C to R at position 611.
+The protein's natural variant, known as in MEN2A;, features a modification of the amino acid from C to S at position 611.
+The protein's natural variant, known as in MEN2A and MTC; familial form;, features a modification of the amino acid from C to W at position 611.
+The protein's natural variant, known as in MEN2A;, features a modification of the amino acid from C to Y at position 611.
+The protein's natural variant, known as in MEN2A and MTC; familial form;, features a modification of the amino acid from C to F at position 618.
+The protein's natural variant, known as in MEN2A;, features a modification of the amino acid from C to G at position 618.
+The protein's natural variant, known as in MEN2A, MTC and HSCR1;, features a modification of the amino acid from C to R at position 618.
+The protein's natural variant, known as in MEN2A, HSCR1 and MTC; familial and sporadic forms;, features a modification of the amino acid from C to S at position 618.
+The protein's natural variant, known as in MEN2A and MTC; familial form;, features a modification of the amino acid from C to Y at position 618.
+The protein's natural variant, known as in MEN2A and MTC; familial form;, features a modification of the amino acid from C to F at position 620.
+The protein's natural variant, known as in MEN2A and MTC; familial and sporadic forms;, features a modification of the amino acid from C to G at position 620.
+The protein's natural variant, known as in MEN2A, MTC and HSCR1; familial and sporadic forms;, features a modification of the amino acid from C to R at position 620.
+The protein's natural variant, known as in MEN2A and MTC; familial form;, features a modification of the amino acid from C to S at position 620.
+The protein's natural variant, known as in MEN2A and HSCR1;, features a modification of the amino acid from C to W at position 620.
+The protein's natural variant, known as in MEN2A;, features a modification of the amino acid from C to Y at position 620.
+The protein's natural variant, known as in HSCR1; sporadic form;, features a modification of the amino acid from Q to K at position 626.
+The protein's natural variant, known as in MEN2A and MTC; familial form;, features a modification of the amino acid from C to F at position 630.
+The protein's natural variant, known as in MTC; sporadic form;, features a modification of the amino acid from C to S at position 630.
+The protein's natural variant, known as in MTC; familial and sporadic forms;, features a modification of the amino acid from C to Y at position 630.
+The protein's natural variant, known as in thyroid carcinoma; somatic mutation;, features a modification of the amino acid from D to G at position 631.
+The protein's natural variant, known as in MEN2A;, features a modification of the amino acid from ELC to DVR at position 634.
+The protein's natural variant, known as in MEN2A, features a modification of the amino acid from CR to WG at position 635.
+The protein's natural variant, known as in MEN2A, features a modification of the amino acid from C to CHELC at position 634.
+The protein's natural variant, known as in MEN2A and pheochromocytoma;, features a modification of the amino acid from C to F at position 634.
+The protein's natural variant, known as in MEN2A and pheochromocytoma;, features a modification of the amino acid from C to G at position 634.
+The protein's natural variant, known as in MEN2A, pheochromocytoma and MTC; familial form; also found as somatic mutation in a sporadic thyroid carcinoma;, features a modification of the amino acid from C to R at position 634.
+The protein's natural variant, known as in MEN2A, pheochromocytoma and MTC; familial form;, features a modification of the amino acid from C to S at position 634.
+The protein's natural variant, known as in MEN2A, pheochromocytoma and MTC; familial form;, features a modification of the amino acid from C to W at position 634.
+The protein's natural variant, known as in MEN2A, pheochromocytoma and MTC; familial form;, features a modification of the amino acid from C to Y at position 634.
+The protein's natural variant, known as in MEN2A, features a modification of the amino acid from T to TCRT at position 636.
+The protein's natural variant, known as in MTC; sporadic form, features a modification of the amino acid from A to G at position 639.
+The protein's natural variant, known as in MEN2A;, features a modification of the amino acid from A to G at position 640.
+The protein's natural variant, known as in MTC; sporadic form, features a modification of the amino acid from A to G at position 641.
+The protein's natural variant, known as in HSCR1, features a modification of the amino acid from P to L at position 679.
+The protein's natural variant, known as in HSCR1; sporadic form, features a modification of the amino acid from S to P at position 690.
+The protein's natural variant, known as in HSCR1;, features a modification of the amino acid from R to Q at position 694.
+The protein's natural variant, known as in HSCR1; sporadic form, features a modification of the amino acid from E to Q at position 762.
+The protein's natural variant, known as in HSCR1;, features a modification of the amino acid from S to P at position 765.
+The protein's natural variant, known as in HSCR1; sporadic form, features a modification of the amino acid from S to R at position 767.
+The protein's natural variant, known as in MTC; familial and sporadic forms;, features a modification of the amino acid from E to D at position 768.
+The protein's natural variant, known as in a patient with renal agenesis; unknown pathological significance; constitutively phosphorylated;, features a modification of the amino acid from V to I at position 778.
+The protein's natural variant, known as in HSCR1;, features a modification of the amino acid from N to S at position 783.
+The protein's natural variant, known as in MEN2A and MTC; familial form;, features a modification of the amino acid from L to F at position 790.
+The protein's natural variant, known as in HSCR1, pheochromocytoma, MTC and MEN2A; familial form;, features a modification of the amino acid from Y to F at position 791.
+The protein's natural variant, known as in MTC; familial form;, features a modification of the amino acid from V to L at position 804.
+The protein's natural variant, known as in MTC; familial form;, features a modification of the amino acid from V to M at position 804.
+The protein's natural variant, known as in HSCR1; sporadic form;, features a modification of the amino acid from R to Q at position 813.
+The protein's natural variant, known as in HSCR1;, features a modification of the amino acid from G to R at position 830.
+The protein's natural variant, known as in MTC; familial form;, features a modification of the amino acid from R to L at position 844.
+The protein's natural variant, known as in HSCR1; sporadic form;, features a modification of the amino acid from R to Q at position 873.
+The protein's natural variant, known as in MEN2B; somatic mutation in sporadic medullary thyroid carcinoma; requires 2 nucleotide substitutions;, features a modification of the amino acid from A to F at position 883.
+The protein's natural variant, known as in MTC; familial form;, features a modification of the amino acid from S to A at position 891.
+The protein's natural variant, known as in HSCR1; sporadic form, features a modification of the amino acid from F to L at position 893.
+The protein's natural variant, known as in a patient with renal agenesis; unknown pathological significance; constitutively phosphorylated; expressed only the immature intracellular form, features a modification of the amino acid from G to S at position 894.
+The protein's natural variant, known as in HSCR1; sporadic form;, features a modification of the amino acid from R to Q at position 897.
+The protein's natural variant, known as in HSCR1; sporadic form;, features a modification of the amino acid from K to E at position 907.
+The protein's natural variant, known as in HSCR1, features a modification of the amino acid from K to T at position 907.
+The protein's natural variant, known as in MEN2B and MTC; sporadic form; somatic mutation; also found in a patient with renal agenesis;, features a modification of the amino acid from M to T at position 918.
+The protein's natural variant, known as in HSCR1; sporadic form, features a modification of the amino acid from E to K at position 921.
+The protein's natural variant, known as in MTC; sporadic form;, features a modification of the amino acid from S to F at position 922.
+The protein's natural variant, known as in MEN2B and MTC; familial form, features a modification of the amino acid from T to M at position 946.
+The protein's natural variant, known as in HSCR1, features a modification of the amino acid from F to L at position 961.
+The protein's natural variant, known as in HSCR1; familial form;, features a modification of the amino acid from R to G at position 972.
+The protein's natural variant, known as in HSCR1; familial form, features a modification of the amino acid from P to L at position 973.
+The protein's natural variant, known as in HSCR1; sporadic form, features a modification of the amino acid from M to T at position 980.
+The protein's natural variant, known as in HSCR1;, features a modification of the amino acid from P to L at position 1039.
+The protein's natural variant, known as in a patient with renal agenesis; unknown pathological significance; prevents phosphorylation in response to GDNF;, features a modification of the amino acid from P to L at position 1049.
+The protein's natural variant, known as in HSCR1;, features a modification of the amino acid from L to V at position 1052.
+The protein's natural variant, known as in HSCR1;, features a modification of the amino acid from L to P at position 1061.
+The protein's natural variant, known as in HSCR1;, features a modification of the amino acid from Y to C at position 1062.
+The protein's natural variant, known as in HSCR1; familial form;, features a modification of the amino acid from M to T at position 1064.
+The protein's natural variant, known as in a patient with renal agenesis; unknown pathological significance; prevents phosphorylation in response to GDNF;, features a modification of the amino acid from P to S at position 1067.
+The protein's natural variant, known as in a bladder transitional cell carcinoma sample; somatic mutation, features a modification of the amino acid from F to Y at position 1112.
+The protein's natural variant, known as in PSORS13; there is a reducing binding of this variant to TRAF6;, features a modification of the amino acid from D to N at position 19.
+The protein's natural variant, known as in CANDF8; abolishes homotypic interactions with the SEFIR domain of IL17RA, IL17RB and IL17RC; does not affect homodimerization; does not affect SEFIR-independent interactions with other proteins;, features a modification of the amino acid from T to I at position 536.
+The protein's natural variant, known as in strain: ECOR 52 and ECOR 60, features a modification of the amino acid from T to A at position 12.
+The protein's natural variant, known as in strain: ECOR 46 and ECOR 50, features a modification of the amino acid from F to Y at position 20.
+The protein's natural variant, known as in HND; no amino acid transport activity when expressed alone or coexpressed with CLTRN or ACE2; loss of surface expression when expressed alone or coexpressed with CLTRN or ACE2;, features a modification of the amino acid from R to C at position 57.
+The protein's natural variant, known as in HND; abolishes amino acid transport activity;, features a modification of the amino acid from G to R at position 66.
+The protein's natural variant, known as in HND; increases cell membrane localization in presence of ACE2 or CLTRN; does not affect interaction with ACE2; amino acid transport activity is not activated in presence of ACE2 or CLTRN, features a modification of the amino acid from A to T at position 69.
+The protein's natural variant, known as in HND; no amino acid transport activity when expressed alone or coexpressed with CLTRN or ACE2; increases surface cell expression when expressed alone or coexpressed with CLTRN or ACE2;, features a modification of the amino acid from G to R at position 93.
+The protein's natural variant, known as in HND; population allele frequency among Europeans is 0.007; reduced transport activity by 50% but does not completely inactivates the transporter; coexpression with ACE2 increased the transport rate whereas coexpression with CLTRN has the opposite effect; does not affect interaction with ACE2; decreased cell membrane localization in presence of CLTRN;, features a modification of the amino acid from D to N at position 173.
+The protein's natural variant, known as in HND; does not affect amino acid transport activity when expressed alone; decreases amino acid transport activity in presence of ACE2 or CLTRN; decreased surface cell expression when expressed with CLTRN or ACE2;, features a modification of the amino acid from R to Q at position 240.
+The protein's natural variant, known as in HND; no amino acid transport activity when expressed alone or coexpressed with CLTRN or ACE2; loss of surface expression when expressed coexpressed with CLTRN or ACE2;, features a modification of the amino acid from L to P at position 242.
+The protein's natural variant, known as does not affect cell membrane localization; does not affect amino acid transport activity;, features a modification of the amino acid from V to I at position 252.
+The protein's natural variant, known as in HND; does not affect interaction with ACE2; coexpression with ACE2 increased the transport rate whereas coexpression with CLTRN has the opposite effect;, features a modification of the amino acid from P to L at position 265.
+The protein's natural variant, known as in HND; abolishes amino acid transport activity;, features a modification of the amino acid from G to R at position 284.
+The protein's natural variant, known as in HND; abolishes amino acid transport activity;, features a modification of the amino acid from R to C at position 328.
+The protein's natural variant, known as in HND; abolishes amino acid transport activity;, features a modification of the amino acid from E to K at position 405.
+The protein's natural variant, known as in HND; no amino acid transport activity when expressed alone or coexpressed with CLTRN or ACE2; loss of surface expression when expressed alone or coexpressed with CLTRN or ACE2;, features a modification of the amino acid from E to K at position 501.
+The protein's natural variant, known as in HND; abolishes amino acid transport activity;, features a modification of the amino acid from D to G at position 517.
+The protein's natural variant, known as in HND; no amino acid transport activity when expressed alone or coexpressed with CLTRN or ACE2; loss of surface expression when expressed alone or coexpressed with CLTRN or ACE2;, features a modification of the amino acid from P to L at position 579.
+The protein's natural variant, known as in strain: A364A, features a modification of the amino acid from K to Q at position 41.
+The protein's natural variant, known as in strain: A364A, features a modification of the amino acid from Q to QQQQQQQQQQQQQQQQQQ at position 91.
+The protein's natural variant, known as in strain: A364A, features a modification of the amino acid from L to S at position 278.
+The natural variant of this protein is characterized by an amino acid alteration from K to M at position 412.
+The protein's natural variant, known as in AI1K; decreased binding to the AMBN promoter; requires 2 nucleotide substitutions, features a modification of the amino acid from A to K at position 273.
+The protein's natural variant, known as in AI1K; requires 2 nucleotide substitutions, features a modification of the amino acid from A to M at position 273.
+The protein's natural variant, known as in SE5221, temperature-sensitive, features a modification of the amino acid from D to N at position 249.
+The protein's natural variant, known as in PXE; acts as a modifier of disease severity; results in higher serum xylosyltransferase activity;, features a modification of the amino acid from A to S at position 115.
+The protein's natural variant, known as in DBQD2; causes retention in the endoplasmic reticulum; impairs dermatan sulfate proteoglycan synthesis;, features a modification of the amino acid from R to W at position 481.
+The protein's natural variant, known as in DBQD2; causes retention in the endoplasmic reticulum;, features a modification of the amino acid from R to C at position 598.
+The protein's natural variant, known as in strain: Isolate A-292, features a modification of the amino acid from P to S at position 94.
+The protein's natural variant, known as in strain: cv. Can-0, features a modification of the amino acid from GED to VEE at position 132.
+The protein's natural variant, known as in strain: cv. Aa-0, cv. An-1, cv. Bur-0, cv. Can-0, cv. Es-0, cv. Gr-1, cv. Hi-0, cv. Ita-0, cv. Kas-1, cv. Ms-0, cv. Mt-0, cv. Nd-0, cv. No-0, cv. Oy-0, cv. RLD, cv. Tsu-0, cv. Wassilewskija and cv. Yo-0, features a modification of the amino acid from C to R at position 149.
+The protein's natural variant, known as in strain: cv. Di-0 and cv. Landsberg erecta, features a modification of the amino acid from P to R at position 176.
+The protein's natural variant, known as in strain: cv. Aa-0, cv. An-1, cv. Bur-0, cv. Can-0, cv. Es-0, cv. Gr-1, cv. Hi-0, cv. Ita-0, cv. Kas-1, cv. Ms-0, cv. Mt-0, cv. Nd-0, cv. No-0, cv. Oy-0, cv. RLD, cv. Tsu-0, cv. Wassilewskija and cv. Yo-0, features a modification of the amino acid from GDV to SDI at position 224.
+The protein's natural variant, known as in LAD, features a modification of the amino acid from D to G at position 128.
+The protein's natural variant, known as in cell line MDTF, features a modification of the amino acid from L to V at position 31.
+The protein's natural variant, known as in cell line MDTF, features a modification of the amino acid from K to E at position 42.
+The protein's natural variant, known as in cell line MDTF, features a modification of the amino acid from GY to PF at position 46.
+The protein's natural variant, known as in cell lines L1.2 and 3T3, features a modification of the amino acid from G to R at position 45.
+The protein's natural variant, known as in cell lines L1.2 and 3T3, features a modification of the amino acid from KG to ID at position 49.
+The protein's natural variant, known as in cell line MDTF; requires 2 nucleotide substitutions, features a modification of the amino acid from G to K at position 49.
+The protein's natural variant, known as in cell line L1.2, features a modification of the amino acid from Q to R at position 122.
+The protein's natural variant, known as in cell lines L1.2 and 3T3, features a modification of the amino acid from IV to VL at position 124.
+The protein's natural variant, known as in cell line MDTF, features a modification of the amino acid from I to V at position 123.
+The protein's natural variant, known as in cell line MDTF, features a modification of the amino acid from S to F at position 139.
+The protein's natural variant, known as in cell line MDTF, features a modification of the amino acid from VQDPET to IRNPEN at position 150.
+The protein's natural variant, known as in cell lines L1.2 and 3T3, features a modification of the amino acid from VQ to IR at position 146.
+The protein's natural variant, known as in cell line 3T3, features a modification of the amino acid from TQ to NQL at position 151.
+The protein's natural variant, known as in cell line L1.2, features a modification of the amino acid from T to N at position 150.
+The protein's natural variant, known as in cell line MDTF, features a modification of the amino acid from Q to L at position 159.
+The protein's natural variant, known as in cell line MDTF, features a modification of the amino acid from KK to EE at position 174.
+The protein's natural variant, known as in cell lines L1.2 and 3T3, features a modification of the amino acid from R to K at position 192.
+The protein's natural variant, known as in cell line 3T3, features a modification of the amino acid from GRRMDP to RRRVHL at position 246.
+The natural variant of this protein is characterized by an amino acid alteration from MDP to VHL at position 246.
+The protein's natural variant, known as in cell line MDTF, features a modification of the amino acid from DP to SL at position 246.
+The protein's natural variant, known as in cell line MDTF, features a modification of the amino acid from Q to L at position 259.
+The protein's natural variant, known as in cell line 3T3, features a modification of the amino acid from RM to GV at position 270.
+The protein's natural variant, known as in cell line L1.2, features a modification of the amino acid from R to G at position 269.
+The protein's natural variant, known as in cell line MDTF, features a modification of the amino acid from C to F at position 275.
+The protein's natural variant, known as in cell line MDTF; requires 2 nucleotide substitutions, features a modification of the amino acid from Q to W at position 280.
+The protein's natural variant, known as in cell line MDTF, features a modification of the amino acid from A to E at position 285.
+The protein's natural variant, known as in cell lines L1.2 and 3T3, features a modification of the amino acid from T to I at position 317.
+The protein's natural variant, known as in cell line EL4, features a modification of the amino acid from S to G at position 325.
+The protein's natural variant, known as in cell line MDTF, features a modification of the amino acid from R to K at position 339.
+The protein's natural variant, known as in cell line MDTF, features a modification of the amino acid from N to S at position 392.
+The protein's natural variant, known as in splenocytes, features a modification of the amino acid from W to R at position 398.
+The protein's natural variant, known as in cell line MDTF, features a modification of the amino acid from II to KT at position 406.
+The protein's natural variant, known as in cell line L1.2, features a modification of the amino acid from T to A at position 410.
+The protein's natural variant, known as in cell lines MDTF and 3T3, features a modification of the amino acid from R to C at position 415.
+The protein's natural variant, known as in cell line L1.2, features a modification of the amino acid from R to H at position 415.
+The protein's natural variant, known as in COXPD20; decreased levels of the protein;, features a modification of the amino acid from T to I at position 337.
+The protein's natural variant, known as in COXPD20;, features a modification of the amino acid from A to T at position 349.
+The protein's natural variant, known as in COXPD20;, features a modification of the amino acid from A to D at position 596.
+The protein's natural variant, known as in MCPH6; reduced interaction with STIL;, features a modification of the amino acid from E to V at position 1235.
+The protein's natural variant, known as found in a patient with nephrotic syndrome; unknown pathological significance;, features a modification of the amino acid from V to I at position 552.
+The protein's natural variant, known as antagonist of the chemokine receptors CCR1 and CCR3;, features a modification of the amino acid from S to F at position 24.
+The protein's natural variant, known as in GSD-V, features a modification of the amino acid from R to W at position 490.
+The protein's natural variant, known as in RILDBC1;, features a modification of the amino acid from C to R at position 76.
+The protein's natural variant, known as in RILDBC1;, features a modification of the amino acid from F to S at position 252.
+The protein's natural variant, known as in RILDBC1;, features a modification of the amino acid from T to M at position 256.
+The protein's natural variant, known as in RILDBC1;, features a modification of the amino acid from K to E at position 262.
+The protein's natural variant, known as in RILDBC1;, features a modification of the amino acid from E to K at position 285.
+The protein's natural variant, known as in RILDBC1; has no defect in protein synthesis;, features a modification of the amino acid from R to Q at position 305.
+The protein's natural variant, known as in RILDBC1;, features a modification of the amino acid from R to Q at position 401.
+The protein's natural variant, known as in RILDBC1;, features a modification of the amino acid from T to P at position 461.
+The protein's natural variant, known as leu in snakes from Caribbean region, Phe in snakes from Pacific region, features a modification of the amino acid from L to F at position 130.
+The protein's natural variant, known as in strain: PLi, features a modification of the amino acid from G to D at position 22.
+The protein's natural variant, known as in strain: PLi, features a modification of the amino acid from S to N at position 26.
+The protein's natural variant, known as in strain: PLi, features a modification of the amino acid from P to S at position 107.
+The protein's natural variant, known as in strain: PLi, features a modification of the amino acid from T to A at position 125.
+The protein's natural variant, known as in strain: PLi, features a modification of the amino acid from N to D at position 194.
+The protein's natural variant, known as in strain: PLi, features a modification of the amino acid from S to G at position 219.
+The protein's natural variant, known as in strain: PLi, features a modification of the amino acid from I to V at position 253.
+The protein's natural variant, known as in strain: PLi, features a modification of the amino acid from A to S at position 257.
+The protein's natural variant, known as in strain: PLi, features a modification of the amino acid from S to A at position 264.
+The protein's natural variant, known as in strain: PLi, features a modification of the amino acid from N to S at position 271.
+The protein's natural variant, known as in a lung small cell carcinoma sample; somatic mutation, features a modification of the amino acid from D to G at position 635.
+The protein's natural variant, known as found in a patient with SCA11; unknown pathological significance;, features a modification of the amino acid from E to G at position 842.
+The protein's natural variant, known as found in a patient with SCA11; unknown pathological significance;, features a modification of the amino acid from R to H at position 1110.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from K to E at position 1090.
+The protein's natural variant, known as in strain: 2.2159, features a modification of the amino acid from D to G at position 9.
+The protein's natural variant, known as in strain: 2.2159 and NCYC 1513, features a modification of the amino acid from ET to GN at position 51.
+The protein's natural variant, known as in strain: 2.2159 and NCYC 1513, features a modification of the amino acid from E to V at position 53.
+The protein's natural variant, known as in strain: 2.2159 and NCYC 1513, features a modification of the amino acid from K to Q at position 56.
+The protein's natural variant, known as in strain: 2.2159 and NCYC 1513, features a modification of the amino acid from L to I at position 79.
+The protein's natural variant, known as in strain: 2.2159 and NCYC 1513, features a modification of the amino acid from N to K at position 84.
+The protein's natural variant, known as in strain: ATCC 56294 / CBS 8030 / CCRC 21757 / NRRLY-17325, features a modification of the amino acid from L to S at position 87.
+The protein's natural variant, known as in strain: 2.2159, features a modification of the amino acid from K to R at position 108.
+The protein's natural variant, known as in strain: 2.2159, features a modification of the amino acid from I to N at position 145.
+The protein's natural variant, known as in strain: 2.2159 and NCYC 1513, features a modification of the amino acid from L to V at position 184.
+The protein's natural variant, known as in strain: 2.2159 and NCYC 1513, features a modification of the amino acid from E to D at position 202.
+The protein's natural variant, known as in strain: 2.2159, features a modification of the amino acid from M to T at position 308.
+The protein's natural variant, known as in strain: 2.2159 and NCYC 1513, features a modification of the amino acid from E to Q at position 325.
+The natural variant of this protein is characterized by an amino acid alteration from A to V at position 1034.
+The natural variant of this protein is characterized by an amino acid alteration from H to Y at position 1213.
+The protein's natural variant, known as in strain: SG96/585 / Serotype III, features a modification of the amino acid from T to M at position 262.
+The protein's natural variant, known as in strain: COH1 / Serotype III, features a modification of the amino acid from V to A at position 370.
+The protein's natural variant, known as no effect on protein localization to midbody ring;, features a modification of the amino acid from H to Q at position 57.
+The protein's natural variant, known as no effect on protein localization to midbody ring; rescues craniofacial development when expressed in a zebrafish heterologous system;, features a modification of the amino acid from H to L at position 378.
+The protein's natural variant, known as in allele DQB1*05:01 and allele DQB1*05:02;, features a modification of the amino acid from A to S at position 6.
+The protein's natural variant, known as in allele DQB1*05:01, allele DQB1*05:02, allele DQB1*06:02 and allele DQB1*06:12;, features a modification of the amino acid from G to D at position 12.
+The protein's natural variant, known as in allele DQB1*03:02, allele DQB1*03:03, allele DQB1*04:01, allele DQB1*05:01, allele DQB1*05:02, allele DQB1*06:02 and allele DQB1*06:12;, features a modification of the amino acid from A to V at position 15.
+The protein's natural variant, known as in allele DQB1*02:01 and allele DQB1*02:02;, features a modification of the amino acid from A to S at position 23.
+The protein's natural variant, known as in allele DQB1*05:01 and allele DQB1*05:02;, features a modification of the amino acid from M to I at position 24.
+The protein's natural variant, known as in allele DQB1*04:01;, features a modification of the amino acid from T to A at position 27.
+The protein's natural variant, known as in allele DQB1*05:01, allele DQB1*05:02, allele DQB1*06:02 and allele DQB1*06:12;, features a modification of the amino acid from T to S at position 27.
+The protein's natural variant, known as in allele DQB1*06:02 and allele DQB1*06:12;, features a modification of the amino acid from P to L at position 28.
+The protein's natural variant, known as in allele DQB1*05:01 and allele DQB1*05:02;, features a modification of the amino acid from P to S at position 28.
+The protein's natural variant, known as in allele DQB1*05:01, allele DQB1*05:02, allele DQB1*06:02 and allele DQB1*06:12;, features a modification of the amino acid from V to L at position 29.
+The protein's natural variant, known as in allele DQB1*06:01;, features a modification of the amino acid from S to P at position 35.
+The protein's natural variant, known as in allele DQB1*04:01, allele DQB1*04:02, allele DQB1*04:03, allele DQB1*06:02, allele DQB1*06:10, allele DQB1*06:13, allele DQB1*06:14, allele DQB1*06:15, allele DQB1*06:16, allele DQB1*06:19, allele DQB1*06:20, allele DQB1*06:22, allele DQB1*06:23, allele DQB1*06:24, allele DQB1*06:29, allele DQB1*06:33 and allele DQB1*06:37;, features a modification of the amino acid from Y to F at position 41.
+The protein's natural variant, known as in allele DQB1*06:01 and allele DQB1*06:35; requires 2 nucleotide substitutions, features a modification of the amino acid from Y to L at position 41.
+The protein's natural variant, known as in allele DQB1*06:33;, features a modification of the amino acid from F to L at position 43.
+The protein's natural variant, known as in allele DQB1*02:01, allele DQB1*02:02, allele DQB1*02:03, allele DQB1*02:04, allele DQB1*02:05, allele DQB1*03:02, allele DQB1*03:03, allele DQB1*03:05, allele DQB1*03:06, allele DQB1*03:07, allele DQB1*03:08, allele DQB1*03:11, allele DQB1*03:15, allele DQB1*03:17, allele DQB1*03:18, allele DQB1*03:20, allele DQB1*03:23, allele DQB1*03:25, allele DQB1*03:26, allele DQB1*04:01, allele DQB1*04:02, allele DQB1*04:03, allele DQB1*05:01, allele DQB1*05:02, allele DQB1*05:03, allele DQB1*05:04, allele DQB1*05:05, allele DQB1*06:02, allele DQB1*06:03, allele DQB1*06:04, allele DQB1*06:05, allele DQB1*06:07, allele DQB1*06:08, allele DQB1*06:09, allele DQB1*06:10, allele DQB1*06:11, allele DQB1*06:12, allele DQB1*06:13, allele DQB1*06:14, allele DQB1*06:15, allele DQB1*06:16, allele DQB1*06:17, allele DQB1*06:18, allele DQB1*06:19, allele DQB1*06:20, allele DQB1*06:21, allele DQB1*06:22, allele DQB1*06:23, allele DQB1*06:24, allele DQB1*06:25, allele DQB1*06:27, allele DQB1*06:28, allele DQB1*06:29, allele DQB1*06:30, allele DQB1*06:31, allele DQB1*06:32, allele DQB1*06:33, allele DQB1*06:34, allele DQB1*06:36, allele DQB1*06:37, allele DQB1*06:38 and allele DQB1*06:39;, features a modification of the amino acid from A to G at position 45.
+The protein's natural variant, known as in allele DQB1*03:11, allele DQB1*03:26, allele DQB1*05:01, allele DQB1*05:02, allele DQB1*05:03, allele DQB1*05:04, allele DQB1*05:05, allele DQB1*06:05, allele DQB1*06:20 and allele DQB1*06:31;, features a modification of the amino acid from M to L at position 46.
+The protein's natural variant, known as in allele DQB1*04:01;, features a modification of the amino acid from R to L at position 55.
+The protein's natural variant, known as in allele DQB1*03:05, allele DQB1*03:17, allele DQB1*04:01, allele DQB1*04:02, allele DQB1*05:01, allele DQB1*05:02, allele DQB1*05:03, allele DQB1*05:04, allele DQB1*05:05 and allele DQB1*06:23; requires 2 nucleotide substitutions, features a modification of the amino acid from Y to G at position 58.
+The protein's natural variant, known as in allele DQB1*02:01, allele DQB1*02:02, allele DQB1*02:03, allele DQB1*02:04, allele DQB1*02:05, allele DQB1*03:02, allele DQB1*03:03, allele DQB1*03:06, allele DQB1*03:07, allele DQB1*03:08, allele DQB1*03:11, allele DQB1*03:12, allele DQB1*03:15, allele DQB1*03:18, allele DQB1*03:20, allele DQB1*03:23, allele DQB1*03:25, allele DQB1*03:26, allele DQB1*04:03, allele DQB1*06:02, allele DQB1*06:03, allele DQB1*06:04, allele DQB1*06:05, allele DQB1*06:06, allele DQB1*06:07, allele DQB1*06:08, allele DQB1*06:09, allele DQB1*06:10, allele DQB1*06:11, allele DQB1*06:12, allele DQB1*06:13, allele DQB1*06:14, allele DQB1*06:15, allele DQB1*06:16, allele DQB1*06:17, allele DQB1*06:18, allele DQB1*06:19, allele DQB1*06:20, allele DQB1*06:21, allele DQB1*06:22, allele DQB1*06:24, allele DQB1*06:25, allele DQB1*06:27, allele DQB1*06:28, allele DQB1*06:29, allele DQB1*06:30, allele DQB1*06:31, allele DQB1*06:32, allele DQB1*06:33, allele DQB1*06:34, allele DQB1*06:36, allele DQB1*06:37, allele DQB1*06:38 and allele DQB1*06:39; requires 2 nucleotide substitutions;, features a modification of the amino acid from Y to L at position 58.
+The protein's natural variant, known as in allele DQB1*03:18;, features a modification of the amino acid from V to L at position 59.
+The protein's natural variant, known as in allele DQB1*02:01, allele DQB1*02:02, allele DQB1*02:03, allele DQB1*02:04 and allele DQB1*02:05;, features a modification of the amino acid from T to S at position 60.
+The protein's natural variant, known as in allele DQB1*05:01, allele DQB1*05:02, allele DQB1*05:03, allele DQB1*05:05, allele DQB1*06:03, allele DQB1*06:04, allele DQB1*06:07, allele DQB1*06:08, allele DQB1*06:14, allele DQB1*06:17, allele DQB1*06:21, allele DQB1*06:25, allele DQB1*06:27, allele DQB1*06:28, allele DQB1*06:30, allele DQB1*06:31, allele DQB1*06:32, allele DQB1*06:34, allele DQB1*06:36, allele DQB1*06:38 and allele DQB1*06:39;, features a modification of the amino acid from Y to H at position 62.
+The protein's natural variant, known as in allele DQB1*02:01, allele DQB1*02:02, allele DQB1*02:03, allele DQB1*02:04 and allele DQB1*02:05, features a modification of the amino acid from Y to S at position 62.
+The protein's natural variant, known as in allele DQB1*06:01 and allele DQB1*06:35;, features a modification of the amino acid from Y to D at position 69.
+The protein's natural variant, known as in allele DQB1*02:01, allele DQB1*02:02, allele DQB1*02:03, allele DQB1*02:04 and allele DQB1*02:05; requires 2 nucleotide substitutions, features a modification of the amino acid from Y to I at position 69.
+The protein's natural variant, known as in allele DQB1*03:20;, features a modification of the amino acid from A to T at position 70.
+The protein's natural variant, known as in allele DQB1*02:01, allele DQB1*02:02, allele DQB1*02:03, allele DQB1*02:04, allele DQB1*02:05, allele DQB1*05:01, allele DQB1*05:02, allele DQB1*05:03, allele DQB1*05:04, allele DQB1*06:01, allele DQB1*06:28 and allele DQB1*06:35;, features a modification of the amino acid from A to V at position 70.
+The protein's natural variant, known as in allele DQB1*02:01, allele DQB1*02:02, allele DQB1*02:03, allele DQB1*02:04, allele DQB1*02:05, allele DQB1*03:02, allele DQB1*03:03, allele DQB1*03:05, allele DQB1*03:06, allele DQB1*03:07, allele DQB1*03:08, allele DQB1*03:10, allele DQB1*03:11, allele DQB1*03:12, allele DQB1*03:14, allele DQB1*03:15, allele DQB1*03:17, allele DQB1*03:18, allele DQB1*03:20, allele DQB1*03:23, allele DQB1*03:25, allele DQB1*03:26, allele DQB1*04:01, allele DQB1*04:02, allele DQB1*04:03, allele DQB1*05:01, allele DQB1*05:02, allele DQB1*05:03, allele DQB1*05:04, allele DQB1*05:05, allele DQB1*06:01, allele DQB1*06:02, allele DQB1*06:03, allele DQB1*06:04, allele DQB1*06:05, allele DQB1*06:06, allele DQB1*06:07, allele DQB1*06:08, allele DQB1*06:09, allele DQB1*06:10, allele DQB1*06:11, allele DQB1*06:12, allele DQB1*06:13, allele DQB1*06:14, allele DQB1*06:15, allele DQB1*06:16, allele DQB1*06:17, allele DQB1*06:18, allele DQB1*06:19, allele DQB1*06:20, allele DQB1*06:21, allele DQB1*06:22, allele DQB1*06:23, allele DQB1*06:24, allele DQB1*06:25, allele DQB1*06:27, allele DQB1*06:28, allele DQB1*06:29, allele DQB1*06:30, allele DQB1*06:31, allele DQB1*06:32, allele DQB1*06:33, allele DQB1*06:34, allele DQB1*06:36, allele DQB1*06:37, allele DQB1*06:38 and allele DQB1*06:39;, features a modification of the amino acid from E to G at position 77.
+The protein's natural variant, known as in allele DQB1*02:01, allele DQB1*02:02, allele DQB1*02:03, allele DQB1*02:04 and allele DQB1*02:05;, features a modification of the amino acid from V to E at position 78.
+The protein's natural variant, known as in allele DQB1*02:01, allele DQB1*02:02, allele DQB1*02:03, allele DQB1*02:04 and allele DQB1*02:05;, features a modification of the amino acid from Y to F at position 79.
+The protein's natural variant, known as in allele DQB1*03:07;, features a modification of the amino acid from A to V at position 81.
+The protein's natural variant, known as in allele DQB1*02:01, allele DQB1*02:02, allele DQB1*02:03, allele DQB1*02:04 and allele DQB1*02:05;, features a modification of the amino acid from P to L at position 84.
+The protein's natural variant, known as in allele DQB1*03:23, allele DQB1*05:01, allele DQB1*05:02, allele DQB1*05:03, allele DQB1*05:04, allele DQB1*05:05, allele DQB1*06:01, allele DQB1*06:02, allele DQB1*06:03, allele DQB1*06:04, allele DQB1*06:05, allele DQB1*06:06, allele DQB1*06:07, allele DQB1*06:08, allele DQB1*06:09, allele DQB1*06:10, allele DQB1*06:11, allele DQB1*06:12, allele DQB1*06:13, allele DQB1*06:14, allele DQB1*06:15, allele DQB1*06:16, allele DQB1*06:17, allele DQB1*06:18, allele DQB1*06:20, allele DQB1*06:22, allele DQB1*06:21, allele DQB1*06:23, allele DQB1*06:24, allele DQB1*06:25, allele DQB1*06:27, allele DQB1*06:28, allele DQB1*06:29, allele DQB1*06:30, allele DQB1*06:31, allele DQB1*06:32, allele DQB1*06:33, allele DQB1*06:34, allele DQB1*06:36, allele DQB1*06:37, allele DQB1*06:38 and allele DQB1*06:39;, features a modification of the amino acid from L to Q at position 85.
+The protein's natural variant, known as in allele DQB1*02:01, allele DQB1*02:02, allele DQB1*02:03, allele DQB1*02:04 and allele DQB1*02:05;, features a modification of the amino acid from P to L at position 87.
+The protein's natural variant, known as in allele DQB1*03:16;, features a modification of the amino acid from P to Q at position 87.
+The protein's natural variant, known as in allele DQB1*03:23, allele DQB1*03:25, allele DQB1*04:01, allele DQB1*04:02, allele DQB1*04:03, allele DQB1*05:01, allele DQB1*05:02, allele DQB1*05:03, allele DQB1*05:04, allele DQB1*05:05, allele DQB1*06:01, allele DQB1*06:02, allele DQB1*06:03, allele DQB1*06:04, allele DQB1*06:05, allele DQB1*06:06, allele DQB1*06:07, allele DQB1*06:08, allele DQB1*06:09, allele DQB1*06:10, allele DQB1*06:11, allele DQB1*06:12, allele DQB1*06:13, allele DQB1*06:14, allele DQB1*06:15, allele DQB1*06:16, allele DQB1*06:17, allele DQB1*06:18, allele DQB1*06:19, allele DQB1*06:20, allele DQB1*06:21, allele DQB1*06:22, allele DQB1*06:23, allele DQB1*06:24, allele DQB1*06:25, allele DQB1*06:27, allele DQB1*06:28, allele DQB1*06:30, allele DQB1*06:31, allele DQB1*06:32, allele DQB1*06:33, allele DQB1*06:34, allele DQB1*06:35, allele DQB1*06:36, allele DQB1*06:37, allele DQB1*06:38 and allele DQB1*06:39;, features a modification of the amino acid from P to R at position 87.
+The protein's natural variant, known as in allele DQB1*03:25, allele DQB1*04:01, allele DQB1*04:02 and allele DQB1*04:03;, features a modification of the amino acid from P to L at position 88.
+The protein's natural variant, known as in allele DQB1*02:01, allele DQB1*02:02, allele DQB1*02:04, allele DQB1*02:05, allele DQB1*03:02, allele DQB1*03:04, allele DQB1*03:05, allele DQB1*03:07, allele DQB1*03:08, allele DQB1*03:11, allele DQB1*03:14, allele DQB1*03:18 and allele DQB1*06:29;, features a modification of the amino acid from D to A at position 89.
+The protein's natural variant, known as in allele DQB1*05:02, allele DQB1*05:04, allele DQB1*05:05, allele DQB1*06:10 and allele DQB1*06:25; requires 2 nucleotide substitutions, features a modification of the amino acid from D to S at position 89.
+The protein's natural variant, known as in allele DQB1*05:01, allele DQB1*06:04, allele DQB1*06:05, allele DQB1*06:06, allele DQB1*06:08, allele DQB1*06:09, allele DQB1*06:12, allele DQB1*06:13, allele DQB1*06:17, allele DQB1*06:18, allele DQB1*06:21, allele DQB1*06:22, allele DQB1*06:27, allele DQB1*06:34, allele DQB1*06:36, allele DQB1*06:38 and allele DQB1*06:39;, features a modification of the amino acid from D to V at position 89.
+The protein's natural variant, known as in allele DQB1*06:16;, features a modification of the amino acid from Y to N at position 92.
+The protein's natural variant, known as in allele DQB1*06:37;, features a modification of the amino acid from N to K at position 94.
+The protein's natural variant, known as in allele DQB1*03:15;, features a modification of the amino acid from S to R at position 95.
+The protein's natural variant, known as in allele DQB1*02:01, allele DQB1*02:02, allele DQB1*02:03, allele DQB1*02:04, allele DQB1*02:05, allele DQB1*03:06, allele DQB1*03:25, allele DQB1*04:01, allele DQB1*04:02, allele DQB1*04:03, allele DQB1*05:04, allele DQB1*06:01 and allele DQB1*06:35;, features a modification of the amino acid from E to D at position 98.
+The protein's natural variant, known as in allele DQB1*03:13;, features a modification of the amino acid from V to D at position 99.
+The protein's natural variant, known as in allele DQB1*02:01, allele DQB1*02:02, allele DQB1*02:03, allele DQB1*02:04, allele DQB1*02:05, allele DQB1*03:06, allele DQB1*03:25, allele DQB1*04:01, allele DQB1*04:02, allele DQB1*04:03, allele DQB1*05:04, allele DQB1*06:01 and allele DQB1*06:35;, features a modification of the amino acid from V to I at position 99.
+The protein's natural variant, known as in allele DQB1*03:06, allele DQB1*03:25, allele DQB1*04:01, allele DQB1*04:02, allele DQB1*04:03 and allele DQB1*05:04; requires 2 nucleotide substitutions, features a modification of the amino acid from R to E at position 102.
+The protein's natural variant, known as in allele DQB1*03:08, allele DQB1*05:01, allele DQB1*05:02, allele DQB1*05:03, allele DQB1*05:05, allele DQB1*06:02, allele DQB1*06:03, allele DQB1*06:08, allele DQB1*06:10, allele DQB1*06:11, allele DQB1*06:12, allele DQB1*06:13, allele DQB1*06:14, allele DQB1*06:16, allele DQB1*06:17, allele DQB1*06:19, allele DQB1*06:20, allele DQB1*06:21, allele DQB1*06:23, allele DQB1*06:24, allele DQB1*06:28, allele DQB1*06:29, allele DQB1*06:30, allele DQB1*06:31 and allele DQB1*06:33;, features a modification of the amino acid from R to G at position 102.
+The protein's natural variant, known as in allele DQB1*05:01, allele DQB1*05:02, allele DQB1*05:03, allele DQB1*05:05, allele DQB1*06:17, allele DQB1*06:24 and allele DQB1*06:30;, features a modification of the amino acid from T to A at position 103.
+The protein's natural variant, known as in allele DQB1*03:06, allele DQB1*03:25, allele DQB1*04:01, allele DQB1*04:02, allele DQB1*04:03 and allele DQB1*05:04; requires 2 nucleotide substitutions, features a modification of the amino acid from T to D at position 103.
+The protein's natural variant, known as in allele DQB1*02:01, allele DQB1*02:02, allele DQB1*02:03, allele DQB1*02:04 and allele DQB1*02:05, features a modification of the amino acid from T to K at position 103.
+The protein's natural variant, known as in allele DQB1*02:01, allele DQB1*02:02, allele DQB1*02:03, allele DQB1*02:04, allele DQB1*02:05 and allele DQB1*06:06;, features a modification of the amino acid from E to A at position 106.
+The protein's natural variant, known as in allele DQB1*03:06, allele DQB1*03:25, allele DQB1*04:01, allele DQB1*04:02, allele DQB1*04:03, allele DQB1*05:01, allele DQB1*05:02, allele DQB1*05:03, allele DQB1*05:04 and allele DQB1*05:05; requires 2 nucleotide substitutions, features a modification of the amino acid from E to S at position 106.
+The protein's natural variant, known as in allele DQB1*02:01, allele DQB1*02:02, allele DQB1*02:03, allele DQB1*02:04, allele DQB1*02:05, allele DQB1*03:06, allele DQB1*03:25, allele DQB1*04:01, allele DQB1*04:02, allele DQB1*04:03, allele DQB1*05:01, allele DQB1*05:02, allele DQB1*05:03, allele DQB1*05:04, allele DQB1*05:05 and allele DQB1*06:06;, features a modification of the amino acid from L to V at position 107.
+The protein's natural variant, known as in allele DQB1*02:01, allele DQB1*02:02, allele DQB1*02:03, allele DQB1*02:04, allele DQB1*05:01, allele DQB1*05:02, allele DQB1*05:03, allele DQB1*05:04, allele DQB1*05:05 and allele DQB1*06:06;, features a modification of the amino acid from T to R at position 109.
+The protein's natural variant, known as in allele DQB1*05:01, allele DQB1*05:02, allele DQB1*05:03, allele DQB1*05:05, allele DQB1*06:01, allele DQB1*06:02, allele DQB1*06:03, allele DQB1*06:04, allele DQB1*06:05, allele DQB1*06:07, allele DQB1*06:08, allele DQB1*06:09, allele DQB1*06:10, allele DQB1*06:11, allele DQB1*06:12, allele DQB1*06:13, allele DQB1*06:14, allele DQB1*06:15, allele DQB1*06:16, allele DQB1*06:17, allele DQB1*06:18, allele DQB1*06:19, allele DQB1*06:20, allele DQB1*06:21, allele DQB1*06:22, allele DQB1*06:23, allele DQB1*06:24, allele DQB1*06:25, allele DQB1*06:27, allele DQB1*06:28, allele DQB1*06:29, allele DQB1*06:30, allele DQB1*06:31, allele DQB1*06:32, allele DQB1*06:33, allele DQB1*06:34, allele DQB1*06:35, allele DQB1*06:36, allele DQB1*06:37, allele DQB1*06:38, allele DQB1*06:39;, features a modification of the amino acid from Q to E at position 116.
+The protein's natural variant, known as in allele DQB1*05:01, allele DQB1*05:02, allele DQB1*05:03, allele DQB1*05:05, allele DQB1*06:01, allele DQB1*06:02, allele DQB1*06:03, allele DQB1*06:04, allele DQB1*06:05, allele DQB1*06:07, allele DQB1*06:08, allele DQB1*06:09, allele DQB1*06:10, allele DQB1*06:11, allele DQB1*06:12, allele DQB1*06:13, allele DQB1*06:14, allele DQB1*06:15, allele DQB1*06:16, allele DQB1*06:17, allele DQB1*06:18, allele DQB1*06:19, allele DQB1*06:20, allele DQB1*06:21, allele DQB1*06:22, allele DQB1*06:23, allele DQB1*06:24, allele DQB1*06:25, allele DQB1*06:27, allele DQB1*06:28, allele DQB1*06:29, allele DQB1*06:30, allele DQB1*06:31, allele DQB1*06:32, allele DQB1*06:33, allele DQB1*06:34, allele DQB1*06:35, allele DQB1*06:36, allele DQB1*06:37, allele DQB1*06:38 and allele DQB1*06:39;, features a modification of the amino acid from L to V at position 117.
+The protein's natural variant, known as in allele DQB1*05:01, allele DQB1*05:02, allele DQB1*05:03, allele DQB1*05:05, allele DQB1*06:01, allele DQB1*06:02, allele DQB1*06:03, allele DQB1*06:08, allele DQB1*06:10, allele DQB1*06:11, allele DQB1*06:13, allele DQB1*06:14, allele DQB1*06:16, allele DQB1*06:18, allele DQB1*06:19, allele DQB1*06:20, allele DQB1*06:23, allele DQB1*06:24, allele DQB1*06:27, allele DQB1*06:28, allele DQB1*06:29, allele DQB1*06:30, allele DQB1*06:31, allele DQB1*06:32, allele DQB1*06:33, allele DQB1*06:35 and allele DQB1*06:37;, features a modification of the amino acid from E to A at position 118.
+The protein's natural variant, known as in allele DQB1*06:04, allele DQB1*06:05, allele DQB1*06:07, allele DQB1*06:09, allele DQB1*06:12, allele DQB1*06:15, allele DQB1*06:17, allele DQB1*06:21, allele DQB1*06:22, allele DQB1*06:25, allele DQB1*06:34, allele DQB1*06:36, allele DQB1*06:38 and allele DQB1*06:39;, features a modification of the amino acid from E to G at position 118.
+The protein's natural variant, known as in allele DQB1*06:01, allele DQB1*06:02, allele DQB1*06:03, allele DQB1*06:08, allele DQB1*06:10, allele DQB1*06:11, allele DQB1*06:13, allele DQB1*06:14, allele DQB1*06:16, allele DQB1*06:18, allele DQB1*06:19, allele DQB1*06:20, allele DQB1*06:23, allele DQB1*06:24, allele DQB1*06:27, allele DQB1*06:28, allele DQB1*06:29, allele DQB1*06:30, allele DQB1*06:31, allele DQB1*06:32, allele DQB1*06:33, allele DQB1*06:35 and allele DQB1*06:37;, features a modification of the amino acid from L to F at position 119.
+The protein's natural variant, known as in allele DQB1*05:01, allele DQB1*05:02, allele DQB1*05:03, allele DQB1*05:05, allele DQB1*06:04, allele DQB1*06:05, allele DQB1*06:07, allele DQB1*06:09, allele DQB1*06:12, allele DQB1*06:15, allele DQB1*06:17, allele DQB1*06:21, allele DQB1*06:22, allele DQB1*06:25, allele DQB1*06:34, allele DQB1*06:36, allele DQB1*06:38 and allele DQB1*06:39; requires 2 nucleotide substitutions, features a modification of the amino acid from L to Y at position 119.
+The protein's natural variant, known as in allele DQB1*05:01, allele DQB1*05:02, allele DQB1*05:03, allele DQB1*05:05, allele DQB1*06:01, allele DQB1*06:02, allele DQB1*06:03, allele DQB1*06:04, allele DQB1*06:05, allele DQB1*06:07, allele DQB1*06:08, allele DQB1*06:09, allele DQB1*06:10, allele DQB1*06:11, allele DQB1*06:12, allele DQB1*06:13, allele DQB1*06:14, allele DQB1*06:15, allele DQB1*06:16, allele DQB1*06:17, allele DQB1*06:18, allele DQB1*06:19, allele DQB1*06:21, allele DQB1*06:22, allele DQB1*06:23, allele DQB1*06:24, allele DQB1*06:25, allele DQB1*06:27, allele DQB1*06:28, allele DQB1*06:29, allele DQB1*06:30, allele DQB1*06:31, allele DQB1*06:32, allele DQB1*06:33, allele DQB1*06:34, allele DQB1*06:35, allele DQB1*06:36, allele DQB1*06:37, allele DQB1*06:38 and allele DQB1*06:39; requires 2 nucleotide substitutions, features a modification of the amino acid from T to G at position 121.
+The protein's natural variant, known as in allele DQB1*05:01, allele DQB1*05:02, allele DQB1*05:03, allele DQB1*05:05, allele DQB1*06:01, allele DQB1*06:02, allele DQB1*06:03, allele DQB1*06:04, allele DQB1*06:05, allele DQB1*06:07, allele DQB1*06:08, allele DQB1*06:09, allele DQB1*06:10, allele DQB1*06:11, allele DQB1*06:12, allele DQB1*06:14, allele DQB1*06:15, allele DQB1*06:16, allele DQB1*06:17, allele DQB1*06:18, allele DQB1*06:19, allele DQB1*06:21, allele DQB1*06:22, allele DQB1*06:23, allele DQB1*06:24, allele DQB1*06:25, allele DQB1*06:27, allele DQB1*06:28, allele DQB1*06:29, allele DQB1*06:30, allele DQB1*06:31, allele DQB1*06:32, allele DQB1*06:33, allele DQB1*06:34, allele DQB1*06:35, allele DQB1*06:36, allele DQB1*06:37, allele DQB1*06:38 and allele DQB1*06:39;, features a modification of the amino acid from T to I at position 122.
+The protein's natural variant, known as in allele DQB1*05:01, allele DQB1*05:02 and allele DQB1*05:03;, features a modification of the amino acid from V to I at position 148.
+The protein's natural variant, known as in allele DQB1*06:01, allele DQB1*06:02, allele DQB1*06:03, allele DQB1*06:04, allele DQB1*06:09, allele DQB1*06:12, allele DQB1*06:34, allele DQB1*06:36, allele DQB1*06:38 and allele DQB1*06:39;, features a modification of the amino acid from A to G at position 157.
+The protein's natural variant, known as in allele DQB1*05:01, allele DQB1*05:02 and allele DQB1*05:03, features a modification of the amino acid from A to S at position 157.
+The protein's natural variant, known as in allele DQB1*05:02;, features a modification of the amino acid from Q to H at position 158.
+The protein's natural variant, known as in allele DQB1*03:22, allele DQB1*06:04, allele DQB1*06:09, allele DQB1*06:12, allele DQB1*06:34, allele DQB1*06:36 and allele DQB1*06:38;, features a modification of the amino acid from R to Q at position 162.
+The protein's natural variant, known as in allele DQB1*06:38;, features a modification of the amino acid from R to Q at position 165.
+The protein's natural variant, known as in allele DQB1*03:21;, features a modification of the amino acid from R to W at position 165.
+The protein's natural variant, known as in allele DQB1*02:02;, features a modification of the amino acid from D to G at position 167.
+The protein's natural variant, known as in allele DQB1*02:04;, features a modification of the amino acid from Q to E at position 168.
+The protein's natural variant, known as in allele DQB1*02:01, allele DQB1*02:02, allele DQB1*02:04, allele DQB1*05:01, allele DQB1*05:02, allele DQB1*05:03, allele DQB1*06:01, allele DQB1*06:02, allele DQB1*06:03, allele DQB1*06:04, allele DQB1*06:09, allele DQB1*06:12, allele DQB1*06:34, allele DQB1*06:36, allele DQB1*06:38 and allele DQB1*06:39;, features a modification of the amino acid from T to A at position 172.
+The protein's natural variant, known as in allele DQB1*02:01, allele DQB1*02:02, allele DQB1*02:04, allele DQB1*03:02, allele DQB1*03:03, allele DQB1*03:05, allele DQB1*03:23, allele DQB1*03:25, allele DQB1*04:01, allele DQB1*04:02, allele DQB1*05:01, allele DQB1*05:02, allele DQB1*05:03, allele DQB1*06:02, allele DQB1*06:03, allele DQB1*06:04, allele DQB1*06:09, allele DQB1*06:12, allele DQB1*06:34, allele DQB1*06:36, allele DQB1*06:38 and allele DQB1*06:39;, features a modification of the amino acid from H to R at position 199.
+The protein's natural variant, known as in allele DQB1*03:09, features a modification of the amino acid from GD to A at position 201.
+The protein's natural variant, known as in allele DQB1*03:24;, features a modification of the amino acid from V to I at position 202.
+The protein's natural variant, known as in allele DQB1*02:01, allele DQB1*02:02, allele DQB1*02:04, allele DQB1*05:01, allele DQB1*05:02, allele DQB1*05:03, allele DQB1*06:01, allele DQB1*06:02, allele DQB1*06:03, allele DQB1*06:04, allele DQB1*06:09, allele DQB1*06:12, allele DQB1*06:34, allele DQB1*06:36, allele DQB1*06:38 and allele DQB1*06:39;, features a modification of the amino acid from N to S at position 214.
+The protein's natural variant, known as in allele DQB1*03:02, allele DQB1*03:03, allele DQB1*03:05, allele DQB1*03:19, allele DQB1*03:25, allele DQB1*04:01 and allele DQB1*04:02;, features a modification of the amino acid from T to I at position 217.
+The protein's natural variant, known as in allele DQB1*06:36;, features a modification of the amino acid from V to A at position 218.
+The protein's natural variant, known as in allele DQB1*06:01;, features a modification of the amino acid from S to N at position 229.
+The protein's natural variant, known as in allele DQB1*05:01, allele DQB1*05:02, allele DQB1*05:03, allele DQB1*06:02, allele DQB1*06:03, allele DQB1*06:04, allele DQB1*06:09, allele DQB1*06:12 and allele DQB1*06:36;, features a modification of the amino acid from I to V at position 235.
+The protein's natural variant, known as in allele DQB1*05:01, allele DQB1*05:02, allele DQB1*05:03, allele DQB1*06:01, allele DQB1*06:02, allele DQB1*06:03, allele DQB1*06:04, allele DQB1*06:09, allele DQB1*06:12 and allele DQB1*06:36;, features a modification of the amino acid from H to R at position 252.
+The protein's natural variant, known as in allele DQB1*05:01, allele DQB1*05:02, allele DQB1*05:03, allele DQB1*06:01, allele DQB1*06:02, allele DQB1*06:03, allele DQB1*06:04, allele DQB1*06:09, allele DQB1*06:12 and allele DQB1*06:36;, features a modification of the amino acid from H to Q at position 253.
+The protein's natural variant, known as in allele DQB1*05:01, allele DQB1*05:02 and allele DQB1*05:03;, features a modification of the amino acid from Q to R at position 256.
+The protein's natural variant, known as in strain: CIP 103216, features a modification of the amino acid from A to T at position 17.
+The protein's natural variant, known as in strain: CIP 102922T, features a modification of the amino acid from I to T at position 32.
+The protein's natural variant, known as in strain: CIP 102922T, features a modification of the amino acid from E to D at position 44.
+The protein's natural variant, known as in strain: NEM1121, features a modification of the amino acid from A to V at position 113.
+The protein's natural variant, known as in strain: CIP 103216, features a modification of the amino acid from A to T at position 129.
+The protein's natural variant, known as in strain: NEM1121, features a modification of the amino acid from G to S at position 138.
+The protein's natural variant, known as rare variant found in a patient with Crohn disease; probably not involved in disease susceptibility; the mutant enzyme has normal activity and is normally secreted;, features a modification of the amino acid from A to G at position 3.
+The protein's natural variant, known as rare variant found in a patient with rheumatoid arthritis; probably not involved in disease susceptibility; the mutant enzyme has normal activity and is normally secreted;, features a modification of the amino acid from N to S at position 33.
+The protein's natural variant, known as the mutant enzyme has normal activity and is normally secreted;, features a modification of the amino acid from R to H at position 62.
+The protein's natural variant, known as the mutant enzyme has normal activity and is normally secreted;, features a modification of the amino acid from G to S at position 64.
+The protein's natural variant, known as at homozygosity may predispose to autoimmunity; normal enzyme activity;, features a modification of the amino acid from M to V at position 89.
+The protein's natural variant, known as the mutant enzyme has normal activity and is normally secreted;, features a modification of the amino acid from Q to K at position 161.
+The protein's natural variant, known as in AIS6; defective enzyme secretion and activity;, features a modification of the amino acid from C to F at position 196.
+The protein's natural variant, known as in AIS6; defective enzyme secretion and activity;, features a modification of the amino acid from G to R at position 212.
+The protein's natural variant, known as in AIS6; defective enzyme secretion and activity;, features a modification of the amino acid from R to W at position 230.
+The protein's natural variant, known as in AIS6; defective enzyme secretion and activity;, features a modification of the amino acid from C to G at position 266.
+The protein's natural variant, known as in AIS6; defective enzyme secretion and activity;, features a modification of the amino acid from Q to P at position 309.
+The protein's natural variant, known as may predispose to autoimmunity; defective enzyme secretion and activity;, features a modification of the amino acid from T to M at position 312.
+The protein's natural variant, known as defective enzyme secretion and activity;, features a modification of the amino acid from R to H at position 314.
+The protein's natural variant, known as in AIS6; defective enzyme secretion and activity;, features a modification of the amino acid from Y to C at position 349.
+The protein's natural variant, known as in AIS6; defective enzyme secretion and activity;, features a modification of the amino acid from R to H at position 393.
+The protein's natural variant, known as rare variant found in a patient with Crohn disease; probably not involved in disease susceptibility; the mutant protein has normal activity;, features a modification of the amino acid from K to N at position 400.
+The protein's natural variant, known as in AIS6; defective enzyme secretion and activity;, features a modification of the amino acid from F to S at position 404.
+The protein's natural variant, known as the mutant enzyme has normal activity and is normally secreted;, features a modification of the amino acid from H to R at position 447.
+The protein's natural variant, known as the mutant enzyme has normal activity and is normally secreted, features a modification of the amino acid from M to I at position 456.
+The protein's natural variant, known as the mutant enzyme has normal activity and is normally secreted;, features a modification of the amino acid from Q to R at position 462.
+The protein's natural variant, known as in AIS6; defective enzyme secretion and activity;, features a modification of the amino acid from R to C at position 479.
+The protein's natural variant, known as in strain: DBVPG1135, DBVPG1373, DBVPG1378, DBVPG1788, DBVPG1794, DBVPG1853, DBVPG3051, DBVPG6044, DBVPG6763, DBVPG6765, SK1, Y55 and YPS128, features a modification of the amino acid from V to I at position 17.
+The protein's natural variant, known as in strain: DBVPG1135, DBVPG1373, DBVPG1378, DBVPG1788, DBVPG1794, DBVPG1853, DBVPG3051, DBVPG6763, DBVPG6765 and SK1, features a modification of the amino acid from N to I at position 21.
+The protein's natural variant, known as in strain: YPS128, features a modification of the amino acid from Q to E at position 65.
+The protein's natural variant, known as in strain: YPS128, features a modification of the amino acid from V to A at position 105.
+The protein's natural variant, known as in strain: DBVPG1135, DBVPG1373, DBVPG1378, DBVPG1788, DBVPG1794, DBVPG1853, DBVPG3051, DBVPG6763, DBVPG6765 and SK1, features a modification of the amino acid from E to Q at position 161.
+The protein's natural variant, known as in strain: DBVPG6044 and Y55, features a modification of the amino acid from D to G at position 204.
+The protein's natural variant, known as in strain: DBVPG1135, DBVPG1373, DBVPG1378, DBVPG1788, DBVPG1794, DBVPG1853, DBVPG3051, DBVPG6763, DBVPG6765 and SK1, features a modification of the amino acid from L to F at position 231.
+The protein's natural variant, known as in strain: DBVPG1135, DBVPG1373, DBVPG1378, DBVPG1788, DBVPG1794, DBVPG1853, DBVPG3051, DBVPG6763, DBVPG6765 and SK1, features a modification of the amino acid from K to E at position 249.
+The protein's natural variant, known as in strain: DBVPG1135, DBVPG1373, DBVPG1378, DBVPG1788, DBVPG1794, DBVPG1853, DBVPG3051, DBVPG6763, DBVPG6765 and SK1, features a modification of the amino acid from A to V at position 270.
+The protein's natural variant, known as in strain: DBVPG1135, DBVPG1373, DBVPG1378, DBVPG1788, DBVPG1794, DBVPG1853, DBVPG3051, DBVPG6763, DBVPG6765 and SK1, features a modification of the amino acid from R to C at position 281.
+The protein's natural variant, known as in SPGF74; unknown pathological significance, features a modification of the amino acid from R to C at position 322.
+The protein's natural variant, known as in POF13; unknown pathological significance, features a modification of the amino acid from L to M at position 353.
+The protein's natural variant, known as in POF13; decreased function in DNA repair as suggested by the persistence of gamma-H2AX foci following cell treatment with etoposide;, features a modification of the amino acid from D to Y at position 487.
+The protein's natural variant, known as in POF13; unknown pathological significance;, features a modification of the amino acid from I to V at position 703.
+The protein's natural variant, known as in MDCMC; severely decreased choline kinase activity, features a modification of the amino acid from E to K at position 283.
+The protein's natural variant, known as in MDCMC; decreased choline kinase activity;, features a modification of the amino acid from R to L at position 377.
+The protein's natural variant, known as in GPHYSD1;, features a modification of the amino acid from W to C at position 50.
+The protein's natural variant, known as in GPHYSD1;, features a modification of the amino acid from R to Q at position 72.
+The protein's natural variant, known as in GPHYSD1; leads to the reduced secretion of the mutated protein;, features a modification of the amino acid from R to H at position 113.
+The protein's natural variant, known as in GPHYSD1;, features a modification of the amino acid from E to K at position 114.
+The protein's natural variant, known as in GPHYSD1; leads to the reduced secretion of the mutated protein;, features a modification of the amino acid from P to L at position 147.
+The protein's natural variant, known as in GPHYSD1;, features a modification of the amino acid from R to W at position 159.
+The protein's natural variant, known as in GPHYSD1;, features a modification of the amino acid from A to T at position 165.
+The protein's natural variant, known as in GPHYSD1, features a modification of the amino acid from C to R at position 171.
+The protein's natural variant, known as in GPHYSD1;, features a modification of the amino acid from R to C at position 221.
+The protein's natural variant, known as in GPHYSD1, features a modification of the amino acid from A to T at position 239.
+The protein's natural variant, known as in GPHYSD1, features a modification of the amino acid from R to C at position 593.
+The protein's natural variant, known as in GPHYSD1, features a modification of the amino acid from S to L at position 635.
+The protein's natural variant, known as in GPHYSD1; leads to the reduced secretion of the mutated protein;, features a modification of the amino acid from G to R at position 811.
+The protein's natural variant, known as in GPHYSD1;, features a modification of the amino acid from P to L at position 906.
+The protein's natural variant, known as in CSNB1H; sporadic case; unknown pathological significance;, features a modification of the amino acid from S to F at position 67.
+The protein's natural variant, known as in FASPS3; decreased stability; decreased protein abundance, features a modification of the amino acid from PVH to AVR at position 416.
+The protein's natural variant, known as associated with delayed sleep phase syndrome (DSPS);, features a modification of the amino acid from V to G at position 639.
+The protein's natural variant, known as only found in PER3.4 allele;, features a modification of the amino acid from M to T at position 1028.
+The protein's natural variant, known as in ADTKD5; decreases in protein stability; partly confers novel Golgi subcellular location;, features a modification of the amino acid from V to G at position 67.
+The protein's natural variant, known as probable disease-associated variant found in a family with hypogammaglobulinemia; decreased function in cotranslational protein targeting to endoplasmic reticulum;, features a modification of the amino acid from V to D at position 85.
+The protein's natural variant, known as in ADTKD5; decreases in protein stability; partly confers novel Golgi subcellular location;, features a modification of the amino acid from T to A at position 185.
+The protein's natural variant, known as in ATFB18;, features a modification of the amino acid from E to K at position 11.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from A to V at position 128.
+The protein's natural variant, known as in HMNDYT1; loss of localization to the plasma membrane; retained in the endoplasmic reticulum; increased proteasomal degradation; loss of function in intracellular manganese ion homeostasis;, features a modification of the amino acid from L to P at position 89.
+The protein's natural variant, known as in HMNDYT1;, features a modification of the amino acid from L to P at position 349.
+The natural variant of this protein is characterized by an amino acid alteration from H to Q at position 60.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 204.
+The natural variant of this protein is characterized by an amino acid alteration from A to T at position 215.
+The protein's natural variant, known as in Ly-24.2, features a modification of the amino acid from H to HPH at position 21.
+The protein's natural variant, known as in Ly-24.2, features a modification of the amino acid from G to S at position 194.
+The natural variant of this protein is characterized by an amino acid alteration from M to I at position 1003.
+The natural variant of this protein is characterized by an amino acid alteration from L to V at position 1093.
+The protein's natural variant, known as in DEE50; unknown pathological significance;, features a modification of the amino acid from M to R at position 33.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to Q at position 177.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from Y to C at position 735.
+The protein's natural variant, known as in DEE50;, features a modification of the amino acid from R to Q at position 2024.
+The natural variant of this protein is characterized by an amino acid alteration from N to S at position 65.
+The protein's natural variant, known as in a renal clear cell carcinoma sample; somatic mutation;, features a modification of the amino acid from I to T at position 216.
+The protein's natural variant, known as in strain; cv. Ag-0, features a modification of the amino acid from Y to F at position 439.
+The protein's natural variant, known as in strain: cv. Cvi-1, features a modification of the amino acid from M to T at position 526.
+The natural variant of this protein is characterized by an amino acid alteration from T to I at position 796.
+The protein's natural variant, known as in WFS1;, features a modification of the amino acid from A to V at position 58.
+The natural variant of this protein is characterized by an amino acid alteration from G to R at position 107.
+The protein's natural variant, known as in WFS1, features a modification of the amino acid from Y to N at position 110.
+The protein's natural variant, known as in WFS1;, features a modification of the amino acid from A to T at position 126.
+The protein's natural variant, known as in WFS1;, features a modification of the amino acid from A to T at position 133.
+The protein's natural variant, known as in WFS1;, features a modification of the amino acid from E to K at position 169.
+The protein's natural variant, known as in DFNA6;, features a modification of the amino acid from D to N at position 171.
+The protein's natural variant, known as in WFS1;, features a modification of the amino acid from P to S at position 292.
+The protein's natural variant, known as in WFS1, features a modification of the amino acid from I to S at position 296.
+The protein's natural variant, known as in WFS1;, features a modification of the amino acid from G to R at position 437.
+The protein's natural variant, known as in WFS1, features a modification of the amino acid from S to I at position 443.
+The protein's natural variant, known as in WFS1;, features a modification of the amino acid from R to S at position 457.
+The protein's natural variant, known as in CTRCT41;, features a modification of the amino acid from E to G at position 462.
+The protein's natural variant, known as in WFS1;, features a modification of the amino acid from P to L at position 504.
+The protein's natural variant, known as in WFS1;, features a modification of the amino acid from R to C at position 558.
+The protein's natural variant, known as in WFS1;, features a modification of the amino acid from R to W at position 629.
+The protein's natural variant, known as in DFNA6;, features a modification of the amino acid from K to T at position 634.
+The protein's natural variant, known as in DFNA6; also found in a patient with type 2 diabetes; unknown pathological significance;, features a modification of the amino acid from R to C at position 653.
+The protein's natural variant, known as in WFS1;, features a modification of the amino acid from Y to C at position 669.
+The protein's natural variant, known as in DFNA6, features a modification of the amino acid from Y to H at position 669.
+The protein's natural variant, known as in WFSL; greatly reduces protein expression compared to wild-type;, features a modification of the amino acid from A to V at position 684.
+The protein's natural variant, known as in DFNA6;, features a modification of the amino acid from R to P at position 685.
+The protein's natural variant, known as in WFS1;, features a modification of the amino acid from C to R at position 690.
+The protein's natural variant, known as in WFS1;, features a modification of the amino acid from G to V at position 695.
+The protein's natural variant, known as in DFNA6, features a modification of the amino acid from H to Y at position 696.
+The protein's natural variant, known as in DFNA6;, features a modification of the amino acid from T to M at position 699.
+The protein's natural variant, known as in WFS1, features a modification of the amino acid from W to C at position 700.
+The protein's natural variant, known as in DFNA6;, features a modification of the amino acid from R to H at position 703.
+The protein's natural variant, known as in DFNA6;, features a modification of the amino acid from A to T at position 716.
+The protein's natural variant, known as in WFS1;, features a modification of the amino acid from P to L at position 724.
+The protein's natural variant, known as in WFS1;, features a modification of the amino acid from G to S at position 736.
+The protein's natural variant, known as in DFNA6; benign variant;, features a modification of the amino acid from V to M at position 779.
+The protein's natural variant, known as in WFS1, features a modification of the amino acid from G to R at position 780.
+The protein's natural variant, known as in WFSL; mildly decreases protein expression compared to wild-type;, features a modification of the amino acid from G to S at position 780.
+The protein's natural variant, known as in WFSL, features a modification of the amino acid from D to Y at position 797.
+The protein's natural variant, known as in WFS1;, features a modification of the amino acid from R to C at position 818.
+The protein's natural variant, known as in DFNA6;, features a modification of the amino acid from L to P at position 829.
+The protein's natural variant, known as in DFNA6;, features a modification of the amino acid from G to D at position 831.
+The protein's natural variant, known as in WFSL;, features a modification of the amino acid from K to N at position 836.
+The protein's natural variant, known as in DFNA6;, features a modification of the amino acid from R to Q at position 859.
+The protein's natural variant, known as in WFSL;, features a modification of the amino acid from E to K at position 864.
+The protein's natural variant, known as in WFS1; mild form;, features a modification of the amino acid from P to L at position 885.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from E to K at position 1784.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from D to H at position 1955.
+The protein's natural variant, known as in strain: cv. W64A, features a modification of the amino acid from A to V at position 157.
+The protein's natural variant, known as in strain: cv. W64A, features a modification of the amino acid from S to T at position 211.
+The protein's natural variant, known as in strain: cv. W64A, features a modification of the amino acid from S to I at position 329.
+The protein's natural variant, known as in strain: cv. W64A, features a modification of the amino acid from P to A at position 483.
+The protein's natural variant, known as in CDG1B;, features a modification of the amino acid from M to T at position 51.
+The protein's natural variant, known as in CDG1B;, features a modification of the amino acid from S to L at position 102.
+The protein's natural variant, known as in CDG1B;, features a modification of the amino acid from Y to C at position 129.
+The protein's natural variant, known as in CDG1B;, features a modification of the amino acid from D to N at position 131.
+The protein's natural variant, known as in CDG1B;, features a modification of the amino acid from M to T at position 138.
+The protein's natural variant, known as in CDG1B;, features a modification of the amino acid from I to T at position 140.
+The protein's natural variant, known as in CDG1B;, features a modification of the amino acid from R to Q at position 152.
+The protein's natural variant, known as in CDG1B;, features a modification of the amino acid from R to Q at position 219.
+The protein's natural variant, known as in CDG1B;, features a modification of the amino acid from G to S at position 250.
+The protein's natural variant, known as in CDG1B, features a modification of the amino acid from Y to C at position 255.
+The protein's natural variant, known as in CDG1B;, features a modification of the amino acid from R to H at position 295.
+The protein's natural variant, known as in CDG1B;, features a modification of the amino acid from I to T at position 398.
+The protein's natural variant, known as in CDG1B;, features a modification of the amino acid from R to H at position 418.
+The protein's natural variant, known as in allele CYP6D3v4, features a modification of the amino acid from F to Y at position 4.
+The protein's natural variant, known as in allele CYP6D3v4, features a modification of the amino acid from L to V at position 10.
+The protein's natural variant, known as in allele CYP6D3v1, allele CYP6D3v3 and allele CYP6D3v4, features a modification of the amino acid from I to F at position 13.
+The protein's natural variant, known as in allele CYP6D3v4, features a modification of the amino acid from V to A at position 30.
+The protein's natural variant, known as in allele CYP6D3v4, features a modification of the amino acid from K to Q at position 74.
+The protein's natural variant, known as in allele CYP6D3v1, features a modification of the amino acid from E to D at position 190.
+The protein's natural variant, known as in allele CYP6D3v1, allele CYP6D3v3 and allele CYP6D3v4, features a modification of the amino acid from Q to R at position 221.
+The protein's natural variant, known as in allele CYP6D3v1, features a modification of the amino acid from E to D at position 339.
+The protein's natural variant, known as in allele CYP6D3v1, features a modification of the amino acid from A to V at position 344.
+The protein's natural variant, known as in allele CYP6D3v1, features a modification of the amino acid from I to L at position 363.
+The protein's natural variant, known as in strain: CS6, features a modification of the amino acid from GF to AY at position 12.
+The protein's natural variant, known as in strain: 5SI5K, features a modification of the amino acid from F to C at position 12.
+The protein's natural variant, known as in strain: NEM2021, features a modification of the amino acid from T to P at position 23.
+The protein's natural variant, known as in strain: 5SI5K, features a modification of the amino acid from E to V at position 25.
+The protein's natural variant, known as in strain: S087, features a modification of the amino acid from V to I at position 43.
+The protein's natural variant, known as in strain: S087, features a modification of the amino acid from D to G at position 61.
+The protein's natural variant, known as in strain: NEM2021, features a modification of the amino acid from G to D at position 96.
+The protein's natural variant, known as in strain: NEM2022, features a modification of the amino acid from Q to H at position 105.
+The protein's natural variant, known as in strain: 1K07, features a modification of the amino acid from A to T at position 111.
+The protein's natural variant, known as in strain: A4065G, features a modification of the amino acid from D to V at position 147.
+The protein's natural variant, known as in strain: A4065G, features a modification of the amino acid from IT to MN at position 151.
+The protein's natural variant, known as in strain: C4068G, features a modification of the amino acid from I to M at position 150.
+The protein's natural variant, known as in strain: 42M06, features a modification of the amino acid from A to S at position 181.
+The protein's natural variant, known as in strain: 41M06, features a modification of the amino acid from E to G at position 189.
+The protein's natural variant, known as in a gastric carcinoma sample;, features a modification of the amino acid from S to P at position 44.
+The protein's natural variant, known as in a pancreatic carcinoma sample;, features a modification of the amino acid from E to K at position 93.
+The protein's natural variant, known as in 20% of the molecules, features a modification of the amino acid from T to A at position 65.
+The protein's natural variant, known as in 20% of the molecules, features a modification of the amino acid from D to N at position 70.
+The protein's natural variant, known as in 20% of the molecules, features a modification of the amino acid from GPD to DES at position 78.
+The protein's natural variant, known as in 20% of the molecules, features a modification of the amino acid from GN to AA at position 82.
+The protein's natural variant, known as in 20% of the molecules, features a modification of the amino acid from F to Y at position 84.
+The protein's natural variant, known as in 20% of the molecules, features a modification of the amino acid from GT to SS at position 128.
+The protein's natural variant, known as in 20% of the molecules, features a modification of the amino acid from L to V at position 141.
+The protein's natural variant, known as in 20% of the molecules, features a modification of the amino acid from V to L at position 168.
+The protein's natural variant, known as in ARVD12; unknown pathological significance;, features a modification of the amino acid from T to I at position 19.
+The protein's natural variant, known as in ARVD12; affects the structure and distribution of mechanical and electrical cell junctions, features a modification of the amino acid from S to SS at position 39.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from T to I at position 4.
+The protein's natural variant, known as in HFTC2; only the C-terminal fragment is secreted, whereas the intact protein is retained in the Golgi complex;, features a modification of the amino acid from S to G at position 71.
+The protein's natural variant, known as in HFTC2;, features a modification of the amino acid from M to T at position 96.
+The protein's natural variant, known as in HFTC2; full-length and N-terminal fragments are barely detectable, whereas a C-terminal fragment with the same molecular weight as that from wild-type can be detected;, features a modification of the amino acid from S to F at position 129.
+The protein's natural variant, known as in HFTC2;, features a modification of the amino acid from F to L at position 157.
+The protein's natural variant, known as in ADHR; partially resistant to cleavage by furin;, features a modification of the amino acid from R to Q at position 176.
+The protein's natural variant, known as in ADHR; C-terminal processing is abolished; reduced proteolysis by PHEX; resistant to cleavage by furin;, features a modification of the amino acid from R to Q at position 179.
+The protein's natural variant, known as in ADHR; C-terminal processing is abolished;, features a modification of the amino acid from R to W at position 179.
+The protein's natural variant, known as in strain: MW56, NC335, NC336, NC362, NC740 and NC774, features a modification of the amino acid from A to T at position 28.
+The protein's natural variant, known as in strain: MW38, features a modification of the amino acid from P to H at position 109.
+The protein's natural variant, known as in strain: MW38, features a modification of the amino acid from M to L at position 132.
+The protein's natural variant, known as in strain: MW27, features a modification of the amino acid from E to V at position 141.
+The protein's natural variant, known as in strain: MW11, MW27, MW38, MW56, MW6, MW63, MW9, NC301, NC322, NC335, NC336, NC350, NC357, NC362, NC390, NC397, NC397, NC732, NC740 and NC774, features a modification of the amino acid from T to P at position 144.
+The protein's natural variant, known as in strain: NC358, features a modification of the amino acid from T to I at position 151.
+The protein's natural variant, known as in strain: MW9 and NC350, features a modification of the amino acid from Q to H at position 173.
+The protein's natural variant, known as in strain: NC350, features a modification of the amino acid from D to N at position 244.
+The protein's natural variant, known as in strain: MW11, MW27, MW6 and MW63, features a modification of the amino acid from M to I at position 284.
+The protein's natural variant, known as in NC319, NC335 and NC399, features a modification of the amino acid from TDN to I at position 322.
+The protein's natural variant, known as in strain: MW38, MW9, NC319, NC335, NC336, NC359, NC362 and NC399, features a modification of the amino acid from D to E at position 333.
+The protein's natural variant, known as in strain: MW38, MW9, NC319, NC335, NC336, NC359, NC362 and NC399, features a modification of the amino acid from H to N at position 341.
+The protein's natural variant, known as in strain: NC304, features a modification of the amino acid from Q to L at position 357.
+The protein's natural variant, known as in strain: MW56, features a modification of the amino acid from A to D at position 382.
+The protein's natural variant, known as in strain: NC359 and NC740, features a modification of the amino acid from V to A at position 408.
+The protein's natural variant, known as in strain: MW56, features a modification of the amino acid from H to Q at position 409.
+The protein's natural variant, known as in strain: MW63 and NC306, features a modification of the amino acid from L to I at position 499.
+The protein's natural variant, known as in strain: MW27, features a modification of the amino acid from P to H at position 549.
+The protein's natural variant, known as in strain: MW11, MW27, MW38, MW6, MW9, NC303, NC304, NC306, NC322, NC335, NC336, NC350, NC390, NC397, NC732, NC740 and NC774, features a modification of the amino acid from F to Y at position 647.
+The protein's natural variant, known as in strain: NC304, NC335, NC350, NC397, NC732 and MW9, features a modification of the amino acid from A to S at position 664.
+The protein's natural variant, known as in strain: MW9, features a modification of the amino acid from G to S at position 713.
+The protein's natural variant, known as in strain: NC303, NC319 and NC361, features a modification of the amino acid from L to S at position 773.
+The protein's natural variant, known as in strain: MW11, MW27, MW38, MW56, MW9, NC390 and NC740, features a modification of the amino acid from A to T at position 793.
+The protein's natural variant, known as in strain: MW11 and NC390, features a modification of the amino acid from L to F at position 802.
+The protein's natural variant, known as in strain: MW6, features a modification of the amino acid from S to T at position 803.
+The protein's natural variant, known as in strain: MW6, features a modification of the amino acid from S to P at position 820.
+The protein's natural variant, known as in strain: MW27, MW38, MW56, MW63, MW9, NC304, NC322, NC335, NC336, NC357, NC358, NC362, NC397, NC399, NC732 and NC774, features a modification of the amino acid from N to D at position 831.
+The protein's natural variant, known as in PKDYS2; strong decrease in serotonin transport;, features a modification of the amino acid from P to L at position 387.
+The protein's natural variant, known as in strain: L2/434/Bu, features a modification of the amino acid from QN to RG at position 56.
+The protein's natural variant, known as in strain: L2/434/Bu, features a modification of the amino acid from I to T at position 173.
+The protein's natural variant, known as in strain: L2/434/Bu, features a modification of the amino acid from M to I at position 245.
+The protein's natural variant, known as in strain: L2/434/Bu, features a modification of the amino acid from M to V at position 254.
+The protein's natural variant, known as in strain: L2/434/Bu, features a modification of the amino acid from I to V at position 401.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from L to P at position 43.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from L to P at position 44.
+The protein's natural variant, known as in NDI1;, features a modification of the amino acid from I to K at position 46.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from L to R at position 53.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from N to D at position 55.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from N to H at position 55.
+The protein's natural variant, known as in NDI1;, features a modification of the amino acid from L to P at position 59.
+The natural variant of this protein is characterized by an amino acid alteration from A to V at position 61.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from L to P at position 62.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from H to R at position 80.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from L to F at position 81.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from L to P at position 83.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from L to Q at position 83.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from A to D at position 84.
+The protein's natural variant, known as in NDI1;, features a modification of the amino acid from D to N at position 85.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from V to M at position 88.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from Q to R at position 92.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from L to Q at position 94.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from P to L at position 95.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from W to R at position 99.
+The protein's natural variant, known as in NDI1; binding capacity is 10% of wild-type, but binding affinity is stronger than wild-type;, features a modification of the amino acid from R to C at position 104.
+The protein's natural variant, known as in NDI1;, features a modification of the amino acid from F to V at position 105.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from R to C at position 106.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from G to E at position 107.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from C to R at position 112.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from C to Y at position 112.
+The protein's natural variant, known as in NDI1;, features a modification of the amino acid from R to W at position 113.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from G to D at position 122.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from G to R at position 122.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from M to K at position 123.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from S to F at position 126.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from S to F at position 127.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from Y to S at position 128.
+The protein's natural variant, known as in NDI1;, features a modification of the amino acid from I to F at position 130.
+The protein's natural variant, known as in NDI1;, features a modification of the amino acid from A to D at position 132.
+The protein's natural variant, known as in NDI1;, features a modification of the amino acid from L to P at position 135.
+The protein's natural variant, known as in NSIAD; constitutively active;, features a modification of the amino acid from R to C at position 137.
+The protein's natural variant, known as in NDI1; fails to activate the adenylyl cyclase system;, features a modification of the amino acid from R to H at position 137.
+The protein's natural variant, known as in NSIAD; constitutively active;, features a modification of the amino acid from R to L at position 137.
+The natural variant of this protein is characterized by an amino acid alteration from R to S at position 139.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from R to P at position 143.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from A to P at position 163.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from W to S at position 164.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from S to L at position 167.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from S to T at position 167.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from P to S at position 173.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from Q to L at position 174.
+The protein's natural variant, known as in NDI1;, features a modification of the amino acid from R to C at position 181.
+The protein's natural variant, known as in NDI1;, features a modification of the amino acid from G to C at position 185.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from D to G at position 191.
+The protein's natural variant, known as in NDI1;, features a modification of the amino acid from G to D at position 201.
+The protein's natural variant, known as in NDI1;, features a modification of the amino acid from R to C at position 202.
+The protein's natural variant, known as in NDI1;, features a modification of the amino acid from R to C at position 203.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from T to N at position 204.
+The protein's natural variant, known as in NDI1;, features a modification of the amino acid from Y to C at position 205.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from V to D at position 206.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from T to N at position 207.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from I to F at position 209.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from F to S at position 214.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from P to T at position 217.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from L to P at position 219.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from L to R at position 219.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from R to H at position 247.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from M to K at position 272.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from V to A at position 277.
+The protein's natural variant, known as in NDI1;, features a modification of the amino acid from Y to C at position 280.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from L to P at position 282.
+The protein's natural variant, known as in NDI1;, features a modification of the amino acid from A to P at position 285.
+The protein's natural variant, known as in NDI1;, features a modification of the amino acid from P to L at position 286.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from P to R at position 286.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from P to S at position 286.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from F to L at position 287.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from L to P at position 289.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from L to P at position 292.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from A to P at position 294.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from L to P at position 309.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from L to R at position 309.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from S to R at position 315.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from N to K at position 317.
+The natural variant of this protein is characterized by an amino acid alteration from S to T at position 318.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from C to R at position 319.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from N to D at position 321.
+The protein's natural variant, known as in NDI1;, features a modification of the amino acid from N to K at position 321.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from N to Y at position 321.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from P to H at position 322.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from P to S at position 322.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from W to R at position 323.
+The protein's natural variant, known as in NDI1, features a modification of the amino acid from W to S at position 323.
+The protein's natural variant, known as found in a patient with neuropathy; unknown pathological significance; loss of GalNAc-transferase activity; no effect on protein expression;, features a modification of the amino acid from H to R at position 234.
+The protein's natural variant, known as in SDJLABA; reduced GalNAc-transferase activity, features a modification of the amino acid from N to S at position 264.
+The protein's natural variant, known as in SDJLABA; loss of GalNAc-transferase activity;, features a modification of the amino acid from P to R at position 384.
+The protein's natural variant, known as in SDJLABA; severely reduced GalNAc transferase activity, features a modification of the amino acid from D to Y at position 432.
+The protein's natural variant, known as found in a patient with neuropathy; unknown pathological significance; loss of GalNAc-transferase activity; no effect on protein expression;, features a modification of the amino acid from M to R at position 509.
+The protein's natural variant, known as in VMD4; unknown pathological significance;, features a modification of the amino acid from L to P at position 154.
+The protein's natural variant, known as found in a patient with vitelliform macular dystrophy; unknown pathological significance, features a modification of the amino acid from L to P at position 238.
+The protein's natural variant, known as in VMD4;, features a modification of the amino acid from L to R at position 238.
+The protein's natural variant, known as in RP91, features a modification of the amino acid from L to P at position 579.
+The protein's natural variant, known as in RP91; unknown pathological significance, features a modification of the amino acid from L to P at position 613.
+The protein's natural variant, known as in RP91; unknown pathological significance, features a modification of the amino acid from L to F at position 626.
+The protein's natural variant, known as in EPM4; no renal failure;, features a modification of the amino acid from H to N at position 363.
+The protein's natural variant, known as may act as a modifier of Gaucher disease;, features a modification of the amino acid from E to G at position 471.
+The protein's natural variant, known as in CPHD1;, features a modification of the amino acid from P to L at position 24.
+The protein's natural variant, known as in CPHD1; reduces transactivation capacity on the GH1 gene; increases the functional binding on the GH1 promoter; increases the interaction with ELK1, LHX3 and PITX1, features a modification of the amino acid from P to L at position 76.
+The protein's natural variant, known as in CPHD1;, features a modification of the amino acid from F to C at position 135.
+The protein's natural variant, known as in CPHD1;, features a modification of the amino acid from R to Q at position 143.
+The protein's natural variant, known as in CPHD1;, features a modification of the amino acid from A to P at position 158.
+The protein's natural variant, known as in CPHD1; associated with severe impairment of transactivation; has a greatly reduced DNA-binding affinity as the wild-type protein;, features a modification of the amino acid from R to Q at position 172.
+The protein's natural variant, known as in CPHD1;, features a modification of the amino acid from E to G at position 174.
+The protein's natural variant, known as in CPHD1; transactivation capacity of this mutant is markedly decreased on the GH1; PRL, TSHB and POU1F1 genes; abolishes the functional interaction of POU1F1 on the PRL promoter with the coactivator CREBBP but not with the transcription factor LHX3; displays normal nuclear accumulation but a markedly decreased binding to a DNA response element;, features a modification of the amino acid from S to R at position 179.
+The protein's natural variant, known as in CPHD1;, features a modification of the amino acid from W to R at position 193.
+The protein's natural variant, known as in CPHD1; associated with less severe impairment of transactivation; has a similar DNA-binding affinity as the wild-type protein;, features a modification of the amino acid from E to K at position 230.
+The protein's natural variant, known as in CPHD1; loss of function;, features a modification of the amino acid from P to S at position 239.
+The protein's natural variant, known as in CPHD1; reduces transactivation capacity on the PRL gene; increases instability of the protein;, features a modification of the amino acid from R to W at position 265.
+The protein's natural variant, known as in CPHD1;, features a modification of the amino acid from R to W at position 271.
+The protein's natural variant, known as in MC1DN16;, features a modification of the amino acid from L to F at position 159.
+The protein's natural variant, known as in MC1DN16;, features a modification of the amino acid from L to P at position 229.
+The protein's natural variant, known as in MC1DN16;, features a modification of the amino acid from G to V at position 250.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from M to I at position 1213.
+The protein's natural variant, known as in DEE8; affects dendritic gephrin clustering and trafficking of GABA-A receptors to synapses;, features a modification of the amino acid from G to A at position 55.
+The protein's natural variant, known as in DEE8, features a modification of the amino acid from R to H at position 290.
+The protein's natural variant, known as probable disease-associated variant found in a patient with moderate intellectual disability, speech delay and sleep disturbances, features a modification of the amino acid from E to K at position 401.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from I to T at position 188.
+The protein's natural variant, known as in FSGS4;, features a modification of the amino acid from S to G at position 342.
+The protein's natural variant, known as in FSGS4;, features a modification of the amino acid from I to M at position 384.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to Q at position 336.
+The protein's natural variant, known as in SSASKS; decreased protein levels; decreased expression at the cell membrane;, features a modification of the amino acid from L to P at position 74.
+The protein's natural variant, known as in SSASKS;, features a modification of the amino acid from G to D at position 112.
+The protein's natural variant, known as in SSASKS; unknown pathological significance;, features a modification of the amino acid from G to R at position 130.
+The protein's natural variant, known as in SSASKS; mild skeletal features; results in altered regulation of calcium homeostasis and abnormal distribution of cellular calcium in patient fibroblasts, features a modification of the amino acid from P to L at position 303.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from V to M at position 43.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from M to V at position 655.
+The protein's natural variant, known as in HOMG5; perinuclear retention of the mutant protein;, features a modification of the amino acid from G to D at position 20.
+The protein's natural variant, known as in HOMG5; the mutant protein inserts correctly into the cell membrane although subsequent analyses suggested that dimer formation was disrupted;, features a modification of the amino acid from Q to E at position 57.
+The protein's natural variant, known as in HOMG5;, features a modification of the amino acid from L to P at position 90.
+The protein's natural variant, known as in strain: Isolate BEMA8, features a modification of the amino acid from A to V at position 12.
+The protein's natural variant, known as in BBS10;, features a modification of the amino acid from V to G at position 11.
+The protein's natural variant, known as in BBS10; has moderately reduced ability to interact with BBS7 and BBS9;, features a modification of the amino acid from R to P at position 34.
+The protein's natural variant, known as in BBS10; has moderately reduced ability to interact with BBS7 and BBS9;, features a modification of the amino acid from R to W at position 49.
+The protein's natural variant, known as in BBS10;, features a modification of the amino acid from L to P at position 55.
+The protein's natural variant, known as in BBS10; has moderately reduced ability to interact with BBS7 and BBS9;, features a modification of the amino acid from C to W at position 91.
+The protein's natural variant, known as in BBS10;, features a modification of the amino acid from L to S at position 170.
+The protein's natural variant, known as in BBS10; associated with V-636, features a modification of the amino acid from K to T at position 188.
+The protein's natural variant, known as in BBS10, features a modification of the amino acid from C to W at position 195.
+The protein's natural variant, known as in BBS10;, features a modification of the amino acid from Y to C at position 197.
+The protein's natural variant, known as in BBS10; has moderately reduced ability to interact with BBS7 and BBS9; severely reduces the interaction with BBS12; 8% of wild-type, features a modification of the amino acid from V to G at position 240.
+The protein's natural variant, known as found in a patient with Bardet-Biedl syndrome homozygous for a mutation in BBS2; unknown pathological significance;, features a modification of the amino acid from M to I at position 255.
+The protein's natural variant, known as found in a patient with Bardet-Biedl syndrome compound heterozygote for mutations in BBS1; rare variant; unknown pathological significance;, features a modification of the amino acid from A to T at position 296.
+The protein's natural variant, known as in BBS10; has moderately reduced ability to interact with BBS7 and BBS9, features a modification of the amino acid from L to F at position 308.
+The protein's natural variant, known as in BBS10; has moderately reduced ability to interact with BBS7 and BBS9; severely reduces the interaction with BBS12; 19% of wild-type;, features a modification of the amino acid from S to A at position 311.
+The protein's natural variant, known as in BBS10; has moderately reduced ability to interact with BBS7 and BBS9; severely reduces the interaction with BBS12; 15% of wild-type;, features a modification of the amino acid from S to L at position 329.
+The protein's natural variant, known as in BBS10; has moderately reduced ability to interact with BBS7 and BBS9;, features a modification of the amino acid from P to L at position 363.
+The protein's natural variant, known as in BBS10;, features a modification of the amino acid from H to Q at position 410.
+The protein's natural variant, known as in BBS10;, features a modification of the amino acid from L to S at position 414.
+The protein's natural variant, known as in BBS10;, features a modification of the amino acid from K to R at position 579.
+The protein's natural variant, known as in BBS10, features a modification of the amino acid from L to S at position 600.
+The protein's natural variant, known as in BBS10;, features a modification of the amino acid from Y to C at position 613.
+The protein's natural variant, known as in BBS10; has moderately reduced ability to interact with BBS7 and BBS9;, features a modification of the amino acid from Y to H at position 613.
+The protein's natural variant, known as in BBS10; associated with T-188;, features a modification of the amino acid from A to V at position 636.
+The protein's natural variant, known as in BBS10; has moderately reduced ability to interact with BBS7 and BBS9;, features a modification of the amino acid from G to V at position 677.
+The protein's natural variant, known as in BBS10, features a modification of the amino acid from L to P at position 687.
+The protein's natural variant, known as in BBS10; has moderately reduced ability to interact with BBS7 and BBS9;, features a modification of the amino acid from T to P at position 689.
+The protein's natural variant, known as in strain: QS4, QS8, QS9, QS11, QS15, QS18, QS21, QS23, QS32, QS34, QS36, QS38 and QS113, features a modification of the amino acid from T to I at position 27.
+The protein's natural variant, known as in strain: QS4, QS8, QS9, QS11, QS15, QS18, QS21, QS23, QS32, QS34, QS36, QS38 and QS113, features a modification of the amino acid from I to V at position 247.
+The protein's natural variant, known as in strain: QS113, features a modification of the amino acid from P to L at position 359.
+The protein's natural variant, known as in strain: QS23, features a modification of the amino acid from N to I at position 424.
+The protein's natural variant, known as in strain: QS8, QS9, QS11, QS15, QS21 and QS34, features a modification of the amino acid from V to I at position 455.
+The protein's natural variant, known as in strain: QS8, QS9, QS11, QS15, QS21 and QS34, features a modification of the amino acid from Y to N at position 591.
+The protein's natural variant, known as in strain: QS4, QS21, QS23, QS32, QS34 and QS113, features a modification of the amino acid from K to Q at position 892.
+The protein's natural variant, known as in strain: Rhodesiense WRATAT 1.1, features a modification of the amino acid from L to V at position 115.
+The protein's natural variant, known as in strain: Rhodesiense WRATAT 1.1, features a modification of the amino acid from V to D at position 143.
+The protein's natural variant, known as in strain: Rhodesiense WRATAT 1.1, features a modification of the amino acid from S to F at position 186.
+The protein's natural variant, known as in strain: Rhodesiense WRATAT 1.1, features a modification of the amino acid from N to G at position 189.
+The protein's natural variant, known as in strain: Rhodesiense WRATAT 1.1, features a modification of the amino acid from E to T at position 267.
+The protein's natural variant, known as in strain: Rhodesiense WRATAT 1.1, features a modification of the amino acid from K to E at position 283.
+The protein's natural variant, known as in DYT26; does not affect cytoplasmic subcellular location;, features a modification of the amino acid from R to H at position 145.
+The natural variant of this protein is characterized by an amino acid alteration from T to S at position 7.
+The protein's natural variant, known as in non-Hodgkin lymphoma; somatic mutation, features a modification of the amino acid from P to S at position 59.
+The protein's natural variant, known as in non-Hodgkin lymphoma; somatic mutation, features a modification of the amino acid from V to I at position 93.
+The protein's natural variant, known as in strain: Isolate BEMA8, features a modification of the amino acid from M to T at position 58.
+The protein's natural variant, known as in strain: KA31a, features a modification of the amino acid from G to V at position 3.
+The protein's natural variant, known as in strain: KA31a, features a modification of the amino acid from Y to C at position 55.
+The protein's natural variant, known as in strain: KA31a, features a modification of the amino acid from N to D at position 84.
+The protein's natural variant, known as in brown, features a modification of the amino acid from C to Y at position 110.
+The protein's natural variant, known as in brown, features a modification of the amino acid from R to H at position 326.
+The protein's natural variant, known as found in Wilms tumor from a patient with GLOW syndrome; somatic mutation; unknown pathological significance, features a modification of the amino acid from P to L at position 435.
+The protein's natural variant, known as in MNG1;, features a modification of the amino acid from S to F at position 839.
+The protein's natural variant, known as in PPB;, features a modification of the amino acid from L to R at position 1583.
+The protein's natural variant, known as in non-epithelial ovarian tumor; somatic mutation; results in reduced RNase IIIb activity but retention of RNase IIIa activity, features a modification of the amino acid from E to K at position 1705.
+The protein's natural variant, known as in non-epithelial ovarian tumor; somatic mutation; results in reduced RNase IIIb activity but retention of RNase IIIa activity, features a modification of the amino acid from D to E at position 1709.
+The protein's natural variant, known as in non-epithelial ovarian tumor; somatic mutation;, features a modification of the amino acid from D to G at position 1709.
+The protein's natural variant, known as in non-epithelial ovarian tumor; somatic mutation; results in reduced RNase IIIb activity but retention of RNase IIIa activity, features a modification of the amino acid from D to N at position 1709.
+The protein's natural variant, known as in GLOW; somatic mutation, features a modification of the amino acid from D to Y at position 1709.
+The protein's natural variant, known as in GLOW; somatic mutation, features a modification of the amino acid from D to V at position 1713.
+The protein's natural variant, known as in non-epithelial ovarian tumor; somatic mutation, features a modification of the amino acid from D to H at position 1810.
+The protein's natural variant, known as in non-epithelial ovarian tumor; somatic mutation;, features a modification of the amino acid from D to N at position 1810.
+The protein's natural variant, known as in non-epithelial ovarian tumor; somatic mutation, features a modification of the amino acid from D to Y at position 1810.
+The protein's natural variant, known as in non-epithelial ovarian tumor; somatic mutation, features a modification of the amino acid from E to G at position 1813.
+The protein's natural variant, known as in non-epithelial ovarian tumor; somatic mutation, features a modification of the amino acid from E to K at position 1813.
+The protein's natural variant, known as in non-epithelial ovarian tumor; somatic mutation, features a modification of the amino acid from E to Q at position 1813.
+The protein's natural variant, known as found in Wilms tumor from a patient with GLOW syndrome; somatic mutation; unknown pathological significance, features a modification of the amino acid from R to G at position 1898.
+The protein's natural variant, known as in strain: cv. Ag-0, cv. Bs-1, cv. Chi-1, cv. Cvi-0, cv. Kas-1, cv. Ita-0, cv. Landsberg erecta, cv. Lisse, cv. Me-0, cv. Mt-0, cv. Oy-0, features a modification of the amino acid from G to S at position 193.
+The protein's natural variant, known as in strain: cv. Ag-0, cv. Bs-1, cv. Chi-1, cv. Cvi-0, cv. Kas-1, cv. Ita-0, cv. Landsberg erecta, cv. Lisse, cv. Me-0, cv. Mt-0, cv. Oy-0, features a modification of the amino acid from S to N at position 204.
+The protein's natural variant, known as in strain: cv. Ag-0, cv. Bs-1, cv. Chi-1, cv. Cvi-0, cv. Kas-1, cv. Ita-0, cv. Landsberg erecta, cv. Lisse, cv. Me-0, cv. Mt-0, cv. Oy-0, features a modification of the amino acid from G to GS at position 213.
+The protein's natural variant, known as in strain: cv. Ag-0, cv. Bs-1, cv. Chi-1, cv. Cvi-0, cv. Kas-1, cv. Ita-0, cv. Landsberg erecta, cv. Lisse, cv. Me-0, cv. Mt-0, cv. Oy-0, features a modification of the amino acid from S to N at position 218.
+The protein's natural variant, known as in strain: cv. Ag-0, cv. Bs-1, cv. Chi-1, cv. Cvi-0, cv. Kas-1, cv. Ita-0, cv. Landsberg erecta, cv. Lisse, cv. Me-0, cv. Mt-0, cv. Oy-0, features a modification of the amino acid from E to D at position 233.
+The protein's natural variant, known as in strain: cv. Ag-0, cv. Bs-1, cv. Chi-1, cv. Cvi-0, cv. Kas-1, cv. Ita-0, cv. Landsberg erecta, cv. Lisse, cv. Me-0, cv. Mt-0, cv. Oy-0, features a modification of the amino acid from Q to H at position 236.
+The protein's natural variant, known as in strain: cv. Ag-0, cv. Lisse, features a modification of the amino acid from R to C at position 289.
+The protein's natural variant, known as in MKMS, features a modification of the amino acid from Y to C at position 159.
+The protein's natural variant, known as in MKMS; loss of interaction with RAD21; loss of interaction with cohesin complex, features a modification of the amino acid from S to N at position 327.
+The protein's natural variant, known as in MKMS; unknown pathological significance, features a modification of the amino acid from R to Q at position 604.
+The protein's natural variant, known as in MKMS, features a modification of the amino acid from K to N at position 1009.
+The protein's natural variant, known as 3-fold reduction in the uptake of sulfate by fibroblasts, features a modification of the amino acid from I to S at position 520.
+The protein's natural variant, known as in strain: NZW and C57BL/6, features a modification of the amino acid from AVP to TGS at position 24.
+The protein's natural variant, known as in strain: NZW and C57BL/6, features a modification of the amino acid from M to T at position 26.
+The protein's natural variant, known as in strain: NZW and C57BL/6, features a modification of the amino acid from G to S at position 40.
+The protein's natural variant, known as in strain: S2, features a modification of the amino acid from S to R at position 66.
+The protein's natural variant, known as in strain: S2, features a modification of the amino acid from K to T at position 68.
+The protein's natural variant, known as in strain: S2, features a modification of the amino acid from L to S at position 73.
+The protein's natural variant, known as in strain: FVB/N, features a modification of the amino acid from I to T at position 235.
+The protein's natural variant, known as in ILFS1;, features a modification of the amino acid from Y to C at position 373.
+The natural variant of this protein is characterized by an amino acid alteration from T to E at position 189.
+The natural variant of this protein is characterized by an amino acid alteration from T to L at position 192.
+The protein's natural variant, known as in strain: E/UW-5/Cx, features a modification of the amino acid from G to S at position 33.
+The protein's natural variant, known as in strain: E/UW-5/Cx, features a modification of the amino acid from K to E at position 213.
+The protein's natural variant, known as in strain: E/UW-5/Cx, features a modification of the amino acid from A to T at position 320.
+The protein's natural variant, known as in SCPV, features a modification of the amino acid from S to A at position 25.
+The protein's natural variant, known as in SCPV, VI and VII, features a modification of the amino acid from D to W at position 28.
+The protein's natural variant, known as in SCPVI, features a modification of the amino acid from N to E at position 29.
+The protein's natural variant, known as in CILD13;, features a modification of the amino acid from L to R at position 175.
+The protein's natural variant, known as in EPM2; atypical form; does not affect glycogen binding, features a modification of the amino acid from S to P at position 25.
+The protein's natural variant, known as in EPM2; does not affect glycogen binding;, features a modification of the amino acid from E to K at position 28.
+The protein's natural variant, known as in EPM2; impairs protein stability; affects phosphatase activity; abolishes glycogen binding; abolishes phosphatase activity with insoluble glucan; disrupts the interaction with PPP1R3C;, features a modification of the amino acid from W to G at position 32.
+The protein's natural variant, known as does not affect glycogen binding;, features a modification of the amino acid from A to P at position 46.
+The protein's natural variant, known as in EPM2; affects phosphatase activity and glycogen binding; disrupts the interaction with PPP1R3C;, features a modification of the amino acid from F to L at position 84.
+The protein's natural variant, known as in EPM2; does not affect glycogen binding;, features a modification of the amino acid from F to L at position 88.
+The protein's natural variant, known as in EPM2; atypical form; learning difficuties with childhood-onset, features a modification of the amino acid from R to P at position 91.
+The protein's natural variant, known as in EPM2; loss of phosphatase activity; reduced self-interaction capacity; disrupts the interaction with PPP1R3C;, features a modification of the amino acid from R to C at position 108.
+The natural variant of this protein is characterized by an amino acid alteration from E to D at position 114.
+The protein's natural variant, known as in EPM2, features a modification of the amino acid from K to N at position 140.
+The protein's natural variant, known as in EPM2, features a modification of the amino acid from N to Y at position 148.
+The protein's natural variant, known as in EPM2; results in ubiquitin-positive perinuclear aggregates; no effect on glycogen binding; abolishes phosphatase activity; may affect proper folding;, features a modification of the amino acid from R to H at position 171.
+The protein's natural variant, known as in EPM2; abolishes interaction with NHLRC1, features a modification of the amino acid from T to A at position 187.
+The protein's natural variant, known as in EPM2; results in ubiquitin-positive perinuclear aggregates; loss of phosphatase activity; affects glycogen binding; reduced self-interaction capacity; abolishes interaction with NHLRC1, PPP1R3C and PRKAA2; no effect on phosphorylation of protein;, features a modification of the amino acid from T to I at position 194.
+The protein's natural variant, known as in EPM2, features a modification of the amino acid from E to K at position 210.
+The protein's natural variant, known as in EPM2; impaired phosphatase activity; does not affect glycogen binding; disrupts the interaction with PPP1R3C, features a modification of the amino acid from G to S at position 240.
+The protein's natural variant, known as in EPM2; results in ubiquitin-positive perinuclear aggregates; loss of phosphatase activity; affects glycogen binding; disrupts the interaction with PPP1R3C;, features a modification of the amino acid from G to S at position 279.
+The protein's natural variant, known as in EPM2; results in ubiquitin-positive perinuclear aggregates; may affect proper folding; loss of phosphatase activity; affects glycogen binding; disrupts the interaction with PPP1R3C;, features a modification of the amino acid from Q to L at position 293.
+The protein's natural variant, known as in EPM2; results in ubiquitin-positive perinuclear aggregates; impairs phosphatase activity; affects glycogen binding; disrupts the interaction with PPP1R3C, features a modification of the amino acid from Y to N at position 294.
+The protein's natural variant, known as in EPM2; impairs protein stability; impairs phosphatase activity; affects glycogen binding; disrupts the interaction with PPP1R3C;, features a modification of the amino acid from P to L at position 301.
+The protein's natural variant, known as in EPM2; causes location of isoform 1 at cytoplasmic punctae; does not affect homodimerization of isoform 1 but prevents heterodimerization of isoform 1 and isoform 2, features a modification of the amino acid from L to W at position 310.
+The protein's natural variant, known as in strain: Usa13, features a modification of the amino acid from S to I at position 71.
+The protein's natural variant, known as in strain: Usa3, Usa16, Zim7, Zim10, Zim13, Zim16, Zim18, Zim22, Zim39, Zim41, Zim42, Z36 and Z50, features a modification of the amino acid from G to A at position 74.
+The protein's natural variant, known as in strain: Usa3, Zim7, Zim10, Zim13, Zim16, Zim18, Zim22, Zim39, Zim41, Zim42, Z36 and Z50, features a modification of the amino acid from V to A at position 75.
+The protein's natural variant, known as in strain: Usa3, Usa16, Zim7, Zim10, Zim13, Zim16, Zim18, Zim22, Zim39, Zim41, Zim42, Z36 and Z50, features a modification of the amino acid from S to T at position 77.
+The protein's natural variant, known as in strain: Zim39, features a modification of the amino acid from A to T at position 82.
+The protein's natural variant, known as in strain: Zim10, Zim13, Zim16, Zim18, Zim39, Z36 and Z50, features a modification of the amino acid from T to S at position 108.
+The protein's natural variant, known as in strain: Zim10, Zim13, Zim16, Zim18, Zim39, Z36 and Z50, features a modification of the amino acid from I to V at position 109.
+The protein's natural variant, known as in strain: Zim41, features a modification of the amino acid from I to T at position 125.
+The protein's natural variant, known as in strain: Zim15 and Z50, features a modification of the amino acid from M to I at position 135.
+The protein's natural variant, known as in strain: Zim41, features a modification of the amino acid from A to V at position 140.
+The protein's natural variant, known as in strain: Usa1, Zim15, Zim18, Zim22, Zim39 and Zim42, features a modification of the amino acid from L to P at position 143.
+The protein's natural variant, known as in strain: Zim13, features a modification of the amino acid from S to G at position 152.
+The protein's natural variant, known as in strain: Z50, features a modification of the amino acid from T to K at position 163.
+The protein's natural variant, known as in strain: Usa8, Usa12, Usa16, Zim7, Zim10, Zim13, Zim15, Zim16, Zim18, Zim22, Zim39, Zim42, Z36 and Z50, features a modification of the amino acid from A to T at position 164.
+The protein's natural variant, known as in strain: Usa8 and Usa12, features a modification of the amino acid from P to H at position 167.
+The protein's natural variant, known as in strain: Usa8, Usa12, Usa16, Zim18, Zim39 and Zim41, features a modification of the amino acid from V to A at position 168.
+The natural variant of this protein is characterized by an amino acid alteration from D to G at position 47.
+The natural variant of this protein is characterized by an amino acid alteration from M to V at position 136.
+The natural variant of this protein is characterized by an amino acid alteration from S to G at position 782.
+The natural variant of this protein is characterized by an amino acid alteration from G to R at position 844.
+The protein's natural variant, known as in CDG1L; impairs activity;, features a modification of the amino acid from Y to C at position 287.
+The protein's natural variant, known as in CDG1L; impairs activity;, features a modification of the amino acid from E to K at position 523.
+The protein's natural variant, known as associated with increased basal heart rate and decreased heart rate variability;, features a modification of the amino acid from I to V at position 646.
+The protein's natural variant, known as in IDDMSSD; gain of function; enhanced PAK1 kinase activity and significantly reduced homodimerization;, features a modification of the amino acid from Y to C at position 131.
+The protein's natural variant, known as in IDDMSSD; gain-of-function; enhanced PAK1 kinase activity and significantly reduced homodimerization;, features a modification of the amino acid from Y to C at position 429.
+The protein's natural variant, known as in NPHS18; decreased function in nephrogenesis; unable to fully rescue morpholino-induced nephrogenesis defects in Xenopus;, features a modification of the amino acid from R to G at position 231.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from G to V at position 326.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from G to R at position 448.
+The protein's natural variant, known as in NPHS18; loss of function in nephrogenesis; unable to rescue morpholino-induced nephrogenesis defects in Xenopus; decreased interaction with NUP107;, features a modification of the amino acid from S to R at position 974.
+The protein's natural variant, known as in NPHS18; loss of function in nephrogenesis; unable to rescue morpholino-induced nephrogenesis defects in Xenopus;, features a modification of the amino acid from L to S at position 1055.
+The natural variant of this protein is characterized by an amino acid alteration from A to S at position 26.
+The protein's natural variant, known as in strain: 0811.4, features a modification of the amino acid from V to I at position 57.
+The protein's natural variant, known as in strain: 0811.0 and Lima, features a modification of the amino acid from T to A at position 77.
+The protein's natural variant, known as in strain: Manaus I, features a modification of the amino acid from S to P at position 138.
+The protein's natural variant, known as in strain: Manaus III, features a modification of the amino acid from S to P at position 194.
+The protein's natural variant, known as in strain: Cano Mora and Atlixco, features a modification of the amino acid from T to A at position 213.
+The protein's natural variant, known as in strain: A57, features a modification of the amino acid from I to T at position 225.
+The natural variant of this protein is characterized by an amino acid alteration from G to R at position 38.
+The protein's natural variant, known as in SCDO3; not localized to the correct compartment of the cell; unable to modulate Notch signaling in a cell-based assay; enzymatically inactive;, features a modification of the amino acid from F to L at position 188.
+The protein's natural variant, known as in SRXY8; partially impaired activity;, features a modification of the amino acid from I to V at position 79.
+The protein's natural variant, known as in SRXY8; partially impaired activity;, features a modification of the amino acid from H to Q at position 90.
+The protein's natural variant, known as in SRXY8; partially impaired activity;, features a modification of the amino acid from H to Q at position 222.
+The protein's natural variant, known as in SRXY8; partially impaired activity;, features a modification of the amino acid from N to T at position 300.
+The protein's natural variant, known as in HYPT13; dominant negative; decreased keratin intermediate filament formation;, features a modification of the amino acid from F to C at position 141.
+The protein's natural variant, known as in DFNB32;, features a modification of the amino acid from R to G at position 312.
+The protein's natural variant, known as in DFNB32;, features a modification of the amino acid from R to Q at position 312.
+The protein's natural variant, known as in DFNB32;, features a modification of the amino acid from Q to P at position 320.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from D to Y at position 493.
+The protein's natural variant, known as in strain: Hp921023, features a modification of the amino acid from H to R at position 67.
+The protein's natural variant, known as in strain: Hp921023, features a modification of the amino acid from E to D at position 256.
+The protein's natural variant, known as in strain: Hp921023, features a modification of the amino acid from K to R at position 272.
+The protein's natural variant, known as in strain: Hp921023, features a modification of the amino acid from T to A at position 274.
+The natural variant of this protein is characterized by an amino acid alteration from A to D at position 1.
+The natural variant of this protein is characterized by an amino acid alteration from A to P at position 32.
+The protein's natural variant, known as in strain: OK17, OK94, Z42, Z55, Z64 and Z74, features a modification of the amino acid from T to A at position 44.
+The protein's natural variant, known as in strain: OK94, features a modification of the amino acid from P to S at position 315.
+The protein's natural variant, known as in strain: Z27, OK13, OK5 and Z16, features a modification of the amino acid from A to S at position 469.
+The protein's natural variant, known as in strain: Eagan, features a modification of the amino acid from V to F at position 16.
+The protein's natural variant, known as in strain: 33, features a modification of the amino acid from T to A at position 59.
+The protein's natural variant, known as in strain: Eagan, features a modification of the amino acid from R to H at position 81.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from D to V at position 429.
+The natural variant of this protein is characterized by an amino acid alteration from L to S at position 81.
+The natural variant of this protein is characterized by an amino acid alteration from S to G at position 632.
+The protein's natural variant, known as in allele SNF1621; sterile, features a modification of the amino acid from R to H at position 49.
+The protein's natural variant, known as in CDG1K; decreased function in protein glycosylation as shown by rescue assays in an ALG1-deficient yeast strain;, features a modification of the amino acid from Q to R at position 50.
+The protein's natural variant, known as in CDG1K; decreased function in protein glycosylation as shown by rescue assays in an ALG1-deficient yeast strain;, features a modification of the amino acid from S to F at position 71.
+The protein's natural variant, known as in CDG1K; decreased function in protein glycosylation as shown by rescue assays in an ALG1-deficient yeast strain;, features a modification of the amino acid from H to L at position 74.
+The protein's natural variant, known as in CDG1K; decreased function in protein glycosylation as shown by rescue assays in an ALG1-deficient yeast strain;, features a modification of the amino acid from L to V at position 88.
+The protein's natural variant, known as in CDG1K; decreased function in protein glycosylation as shown by rescue assays in an ALG1-deficient yeast strain;, features a modification of the amino acid from P to L at position 98.
+The protein's natural variant, known as in CDG1K; decreased function in protein glycosylation as shown by rescue assays in an ALG1-deficient yeast strain;, features a modification of the amino acid from L to F at position 114.
+The protein's natural variant, known as in CDG1K; decreased function in protein glycosylation as shown by rescue assays in an ALG1-deficient yeast strain;, features a modification of the amino acid from S to R at position 150.
+The protein's natural variant, known as in CDG1K; decreased function in protein glycosylation as shown by rescue assays in an ALG1-deficient yeast strain;, features a modification of the amino acid from I to S at position 209.
+The protein's natural variant, known as in CDG1K; decreased function in protein glycosylation as shown by rescue assays in an ALG1-deficient yeast strain;, features a modification of the amino acid from S to L at position 258.
+The protein's natural variant, known as no effect on function in protein glycosylation;, features a modification of the amino acid from S to N at position 267.
+The protein's natural variant, known as in CDG1K; decreased function in protein glycosylation as shown by rescue assays in an ALG1-deficient yeast strain;, features a modification of the amino acid from R to W at position 276.
+The protein's natural variant, known as in CDG1K; decreased function in protein glycosylation as shown by rescue assays in an ALG1-deficient yeast strain;, features a modification of the amino acid from V to F at position 281.
+The protein's natural variant, known as in CDG1K; decreased function in protein glycosylation as shown by rescue assays in an ALG1-deficient yeast strain;, features a modification of the amino acid from D to G at position 289.
+The protein's natural variant, known as in CDG1K; decreased function in protein glycosylation as shown by rescue assays in an ALG1-deficient yeast strain;, features a modification of the amino acid from D to V at position 291.
+The protein's natural variant, known as in CDG1K; decreased function in protein glycosylation as shown by rescue assays in an ALG1-deficient yeast strain;, features a modification of the amino acid from Q to P at position 342.
+The protein's natural variant, known as in CDG1K; decreased function in protein glycosylation as shown by rescue assays in an ALG1-deficient yeast strain;, features a modification of the amino acid from Y to D at position 353.
+The protein's natural variant, known as in CDG1K; decreased function in protein glycosylation as shown by rescue assays in an ALG1-deficient yeast strain;, features a modification of the amino acid from G to R at position 358.
+The protein's natural variant, known as in CDG1K; decreased function in protein glycosylation as shown by rescue assays in an ALG1-deficient yeast strain;, features a modification of the amino acid from S to L at position 359.
+The protein's natural variant, known as in CDG1K; decreased function in protein glycosylation as shown by rescue assays in an ALG1-deficient yeast strain;, features a modification of the amino acid from A to V at position 360.
+The protein's natural variant, known as in CDG1K; decreased function in protein glycosylation as shown by rescue assays in an ALG1-deficient yeast strain;, features a modification of the amino acid from G to A at position 363.
+The protein's natural variant, known as in CDG1K; decreased function in protein glycosylation as shown by rescue assays in an ALG1-deficient yeast strain;, features a modification of the amino acid from L to Q at position 366.
+The protein's natural variant, known as in CDG1K; decreased function in protein glycosylation as shown by rescue assays in an ALG1-deficient yeast strain;, features a modification of the amino acid from H to Q at position 367.
+The protein's natural variant, known as in CDG1K; decreased function in protein glycosylation as shown by rescue assays in an ALG1-deficient yeast strain;, features a modification of the amino acid from M to K at position 382.
+The protein's natural variant, known as in CDG1K; decreased function in protein glycosylation as shown by rescue assays in an ALG1-deficient yeast strain;, features a modification of the amino acid from G to R at position 384.
+The protein's natural variant, known as in CDG1K; decreased function in protein glycosylation as shown by rescue assays in an ALG1-deficient yeast strain;, features a modification of the amino acid from P to S at position 388.
+The protein's natural variant, known as no effect on function in protein glycosylation as shown by rescue assays in an ALG1-deficient yeast strain;, features a modification of the amino acid from D to E at position 429.
+The protein's natural variant, known as in CDG1K; decreased function in protein glycosylation as shown by rescue assays in an ALG1-deficient yeast strain;, features a modification of the amino acid from R to W at position 438.
+The protein's natural variant, known as in ACLS; atypical phenotype; unknown pathological significance;, features a modification of the amino acid from R to Q at position 154.
+The protein's natural variant, known as in BBS; the patient also carries homozygous mutation R-390 in BBS1; may affect splicing; hypomorphic variant in vitro;, features a modification of the amino acid from R to G at position 641.
+The protein's natural variant, known as in ACLS; may affect splicing; hypomorphic mutation in vitro;, features a modification of the amino acid from R to Q at position 702.
+The protein's natural variant, known as found as heterozygous variant in a patient with Bardet-Biedl syndrome; hypomorphic variant in vitro, features a modification of the amino acid from L to P at position 759.
+The protein's natural variant, known as in ACLS; atypical phenotype; unknown pathological significance;, features a modification of the amino acid from V to M at position 828.
+The protein's natural variant, known as rare variant found in a patient with Bardet-Biedl syndrome also carrying a frameshift mutation in BBS10 and variant P-293 in BBS7;, features a modification of the amino acid from Q to R at position 834.
+The protein's natural variant, known as in ACLS; atypical phenotype; unknown pathological significance;, features a modification of the amino acid from E to K at position 987.
+The protein's natural variant, known as in BBS; the patient is a compound heterozygote for a truncating mutation and mutation R-390 in BBS1; hypomorphic variant in vitro;, features a modification of the amino acid from Q to R at position 994.
+The protein's natural variant, known as in AGBK;, features a modification of the amino acid from N to S at position 1060.
+The protein's natural variant, known as in BBS; the patient is a compound heterozygote for two frameshift mutations in BBS9; hypomorphic variant in vitro;, features a modification of the amino acid from R to W at position 1068.
+The protein's natural variant, known as in ACLS; atypical phenotype; unknown pathological significance;, features a modification of the amino acid from S to W at position 1122.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from I to L at position 361.
+The protein's natural variant, known as in salt-sensitive hypertension, features a modification of the amino acid from N to S at position 518.
+The protein's natural variant, known as in salt-sensitive hypertension, features a modification of the amino acid from C to R at position 562.
+The protein's natural variant, known as in IDDHISD, features a modification of the amino acid from Q to R at position 28.
+The protein's natural variant, known as in IDDHISD, features a modification of the amino acid from Q to R at position 32.
+The protein's natural variant, known as in IDDHISD, features a modification of the amino acid from P to R at position 61.
+The protein's natural variant, known as in IDDHISD, features a modification of the amino acid from K to N at position 118.
+The protein's natural variant, known as in IDDHISD, features a modification of the amino acid from D to N at position 156.
+The protein's natural variant, known as in IDDHISD, features a modification of the amino acid from W to C at position 370.
+The protein's natural variant, known as in IDDHISD, features a modification of the amino acid from W to R at position 370.
+The protein's natural variant, known as in IDDHISD, features a modification of the amino acid from KR to QW at position 492.
+The protein's natural variant, known as in IDDHISD, features a modification of the amino acid from P to L at position 514.
+The protein's natural variant, known as in IDDHISD, features a modification of the amino acid from A to V at position 546.
+The protein's natural variant, known as in IDDHISD, features a modification of the amino acid from S to F at position 548.
+The protein's natural variant, known as in IDDHISD, features a modification of the amino acid from W to C at position 727.
+The protein's natural variant, known as in SHRF;, features a modification of the amino acid from G to V at position 30.
+The protein's natural variant, known as in SHRF;, features a modification of the amino acid from G to D at position 198.
+The protein's natural variant, known as no effect on thiamine pyrophosphate transporter activity;, features a modification of the amino acid from R to L at position 6.
+The protein's natural variant, known as no effect on thiamine pyrophosphate transporter activity;, features a modification of the amino acid from D to V at position 123.
+The protein's natural variant, known as in DFNA72; decreases choline transmembrane transporter activity;, features a modification of the amino acid from M to V at position 156.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from A to T at position 347.
+The protein's natural variant, known as no effect on thiamine pyrophosphate transporter activity;, features a modification of the amino acid from P to S at position 397.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from T to M at position 411.
+The protein's natural variant, known as in strain: MD-8, features a modification of the amino acid from V to I at position 381.
+The protein's natural variant, known as associated with higher bone mineral density and lower frequency of vertebral fractures in Japanese post-menopausal women;, features a modification of the amino acid from L to P at position 10.
+The protein's natural variant, known as in IBDIMDE; decreased TGFB1-mediated activation of SMAD signaling; reduced levels of secreted TGFB1, features a modification of the amino acid from R to C at position 45.
+The protein's natural variant, known as in CAEND; leads to TGF-beta-1 intracellular accumulation, features a modification of the amino acid from Y to H at position 81.
+The protein's natural variant, known as in IBDIMDE; decreased TGFB1-mediated activation of SMAD signaling; reduced levels of secreted TGFB1, features a modification of the amino acid from R to C at position 110.
+The protein's natural variant, known as in CAEND; higher levels of active TGF-beta-1 in the culture medium; enhances osteoclast formation in vitro, features a modification of the amino acid from R to C at position 218.
+The protein's natural variant, known as in CAEND, features a modification of the amino acid from R to H at position 218.
+The protein's natural variant, known as in CAEND; sporadic case; higher levels of active TGF-beta-1 in the culture medium, features a modification of the amino acid from H to D at position 222.
+The protein's natural variant, known as in CAEND, features a modification of the amino acid from C to G at position 223.
+The protein's natural variant, known as in CAEND, features a modification of the amino acid from C to R at position 223.
+The protein's natural variant, known as in CAEND; higher levels of active TGF-beta-1 in the culture medium, features a modification of the amino acid from C to R at position 225.
+The protein's natural variant, known as in IBDIMDE; loss of TGFB1-mediated activation of SMAD signaling; mutant TGFB1 is not secreted, features a modification of the amino acid from C to R at position 387.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from T to S at position 40.
+The protein's natural variant, known as in DEE67;, features a modification of the amino acid from E to K at position 590.
+The protein's natural variant, known as in strain: 2CPA-7, features a modification of the amino acid from A to D at position 108.
+The protein's natural variant, known as in strain: 2CPA-122, features a modification of the amino acid from Q to P at position 138.
+The protein's natural variant, known as in EE;, features a modification of the amino acid from Y to C at position 38.
+The protein's natural variant, known as in EE; reduces protein stability;, features a modification of the amino acid from L to P at position 55.
+The protein's natural variant, known as in EE;, features a modification of the amino acid from T to A at position 136.
+The protein's natural variant, known as in EE; reduces protein stability, iron content and enzyme activity;, features a modification of the amino acid from T to I at position 152.
+The protein's natural variant, known as in EE;, features a modification of the amino acid from R to Q at position 163.
+The protein's natural variant, known as in EE;, features a modification of the amino acid from R to W at position 163.
+The protein's natural variant, known as in EE; reduces protein stability;, features a modification of the amino acid from T to K at position 164.
+The protein's natural variant, known as in EE;, features a modification of the amino acid from L to R at position 185.
+The protein's natural variant, known as in EE; reduces protein stability and affinity for substrate;, features a modification of the amino acid from D to N at position 196.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from E to K at position 706.
+The protein's natural variant, known as in allele APOH*4, features a modification of the amino acid from K to E at position 229.
+The protein's natural variant, known as in MC3DN4;, features a modification of the amino acid from S to F at position 45.
+The protein's natural variant, known as in allele alpha-D, features a modification of the amino acid from G to D at position 16.
+The protein's natural variant, known as in alpha-2, features a modification of the amino acid from G to S at position 20.
+The protein's natural variant, known as in alpha-1-B, features a modification of the amino acid from D to Y at position 76.
+The protein's natural variant, known as in alpha-2, features a modification of the amino acid from L to H at position 114.
+The protein's natural variant, known as in alpha-2, features a modification of the amino acid from N to S at position 116.
+The protein's natural variant, known as in strain: cv. Se-0, features a modification of the amino acid from E to D at position 131.
+The protein's natural variant, known as in strain: cv. Cvi-1, features a modification of the amino acid from L to I at position 229.
+The protein's natural variant, known as in strain: cv. Ct-1, cv. Edi-0 and cv. Ga-0, features a modification of the amino acid from L to V at position 238.
+The protein's natural variant, known as in plasmid R1033, features a modification of the amino acid from H to N at position 39.
+The protein's natural variant, known as in plasmid R1033, features a modification of the amino acid from S to T at position 187.
+The protein's natural variant, known as in strain: Isolate HG18; streptomycin resistant, features a modification of the amino acid from P to S at position 42.
+The protein's natural variant, known as in strain: Isolate HG3; streptomycin resistant, features a modification of the amino acid from K to R at position 43.
+The protein's natural variant, known as in strain: Isolate HG14; streptomycin pseudo-dependent, features a modification of the amino acid from R to C at position 86.
+The protein's natural variant, known as in strain: Isolate HG31; streptomycin pseudo-dependent, features a modification of the amino acid from R to H at position 86.
+The protein's natural variant, known as in strain: Isolate HG19; streptomycin resistant, features a modification of the amino acid from K to E at position 88.
+The protein's natural variant, known as in strain: Isolate HG1; streptomycin resistant, features a modification of the amino acid from K to R at position 88.
+The protein's natural variant, known as in strain: Isolate HG11; streptomycin dependent, features a modification of the amino acid from P to L at position 91.
+The protein's natural variant, known as in DFNA36;, features a modification of the amino acid from D to N at position 572.
+The protein's natural variant, known as in DFNB7;, features a modification of the amino acid from M to V at position 654.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from G to S at position 15.
+The protein's natural variant, known as in UVR-induced corneal tumor, features a modification of the amino acid from Q to L at position 61.
+The protein's natural variant, known as in RP77;, features a modification of the amino acid from E to K at position 75.
+The protein's natural variant, known as in RP77; decreased protein levels; does not affect localization to endoplasmic reticulum;, features a modification of the amino acid from P to L at position 128.
+The protein's natural variant, known as in RP77; decreased protein levels; does not affect localization to endoplasmic reticulum; loss of rod photoreceptor function shown by a mouse knockin model of the mutation;, features a modification of the amino acid from L to P at position 135.
+The protein's natural variant, known as in CsEv2B and CsEv2D, features a modification of the amino acid from I to M at position 6.
+The protein's natural variant, known as in CsEv2A*, features a modification of the amino acid from LFLI to FALV at position 14.
+The protein's natural variant, known as in CsEv2B, features a modification of the amino acid from K to R at position 20.
+The protein's natural variant, known as in CsEv2D, features a modification of the amino acid from G to A at position 30.
+The protein's natural variant, known as in CsEv2C, features a modification of the amino acid from K to E at position 51.
+The protein's natural variant, known as in AVED;, features a modification of the amino acid from R to W at position 59.
+The protein's natural variant, known as in AVED;, features a modification of the amino acid from H to Q at position 101.
+The protein's natural variant, known as in AVED;, features a modification of the amino acid from A to T at position 120.
+The protein's natural variant, known as in AVED;, features a modification of the amino acid from E to K at position 141.
+The protein's natural variant, known as in AVED;, features a modification of the amino acid from R to H at position 192.
+The protein's natural variant, known as in AVED;, features a modification of the amino acid from R to W at position 221.
+The protein's natural variant, known as in AVED; mild and slowly progressive form of the disease;, features a modification of the amino acid from G to R at position 246.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from P to S at position 380.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from P to S at position 659.
+The protein's natural variant, known as induces white cream or cream coat color, caused by dilution of pheomelanin, features a modification of the amino acid from R to C at position 51.
+The protein's natural variant, known as found in a clear cell renal carcinoma case; somatic mutation, features a modification of the amino acid from T to A at position 790.
+The protein's natural variant, known as in strain: ZBMEL377, features a modification of the amino acid from G to D at position 25.
+The protein's natural variant, known as in strain: ZBMEL131, features a modification of the amino acid from A to T at position 90.
+The protein's natural variant, known as in strain: MEL16 and ZBMEL84, features a modification of the amino acid from E to K at position 95.
+The protein's natural variant, known as in MYP26; unknown pathological significance;, features a modification of the amino acid from L to P at position 80.
+The protein's natural variant, known as in MYP26; unknown pathological significance;, features a modification of the amino acid from A to D at position 298.
+The protein's natural variant, known as in strain: cv. Coerula W2, features a modification of the amino acid from K to R at position 87.
+The protein's natural variant, known as in strain: cv. Coerula W2, features a modification of the amino acid from A to S at position 107.
+The protein's natural variant, known as in LCA9; does not affect nuclear localization; results in significantly reduced enzymatic activity;, features a modification of the amino acid from V to M at position 9.
+The protein's natural variant, known as in LCA9;, features a modification of the amino acid from A to T at position 13.
+The protein's natural variant, known as in LCA9;, features a modification of the amino acid from I to N at position 20.
+The protein's natural variant, known as in LCA9, features a modification of the amino acid from D to G at position 33.
+The protein's natural variant, known as in LCA9, features a modification of the amino acid from M to T at position 35.
+The protein's natural variant, known as in LCA9;, features a modification of the amino acid from A to V at position 54.
+The protein's natural variant, known as in LCA9; does not affect nuclear localization; results in significantly reduced enzymatic activity;, features a modification of the amino acid from R to W at position 66.
+The protein's natural variant, known as in LCA9;, features a modification of the amino acid from V to F at position 67.
+The protein's natural variant, known as in LCA9;, features a modification of the amino acid from M to V at position 69.
+The protein's natural variant, known as in LCA9, features a modification of the amino acid from L to H at position 72.
+The protein's natural variant, known as in LCA9;, features a modification of the amino acid from V to G at position 98.
+The protein's natural variant, known as in LCA9, features a modification of the amino acid from A to P at position 147.
+The protein's natural variant, known as in LCA9;, features a modification of the amino acid from V to F at position 151.
+The protein's natural variant, known as in LCA9, features a modification of the amino acid from L to P at position 153.
+The protein's natural variant, known as in LCA9;, features a modification of the amino acid from L to V at position 153.
+The protein's natural variant, known as in LCA9;, features a modification of the amino acid from G to R at position 156.
+The protein's natural variant, known as in LCA9, features a modification of the amino acid from D to G at position 173.
+The protein's natural variant, known as in LCA9;, features a modification of the amino acid from V to M at position 178.
+The protein's natural variant, known as in LCA9;, features a modification of the amino acid from Y to C at position 181.
+The protein's natural variant, known as in LCA9, features a modification of the amino acid from I to M at position 184.
+The protein's natural variant, known as in LCA9; results in significantly reduced enzymatic activity;, features a modification of the amino acid from R to W at position 207.
+The protein's natural variant, known as in LCA9, features a modification of the amino acid from I to N at position 217.
+The protein's natural variant, known as in LCA9; does not affect nuclear localization;, features a modification of the amino acid from R to C at position 237.
+The protein's natural variant, known as in LCA9;, features a modification of the amino acid from R to L at position 237.
+The protein's natural variant, known as in LCA9;, features a modification of the amino acid from L to S at position 239.
+The protein's natural variant, known as in LCA9;, features a modification of the amino acid from H to P at position 251.
+The protein's natural variant, known as in LCA9; results in significantly reduced enzymatic activity; the mutant localizes to the cytoplasm;, features a modification of the amino acid from E to K at position 257.
+The protein's natural variant, known as in LCA9; results in significantly reduced enzymatic activity;, features a modification of the amino acid from N to D at position 273.
+The protein's natural variant, known as may be associated with a reduced risk for hypertension especially in men; reduces activity 4.7 fold; no effect on plasmin-mediated proteolytic processing; increase in ability to inhibit nicotine-evoked catecholamine secretion in vitro; displays alterations in baroreceptor function;, features a modification of the amino acid from G to S at position 382.
+The protein's natural variant, known as increases activity 2.3 fold; decrease in plasmin-mediated proteolytic processing; decrease in ability to inhibit nicotine-evoked catecholamine secretion in vitro;, features a modification of the amino acid from P to L at position 388.
+The protein's natural variant, known as no effect on plasmin-mediated proteolytic processing; decrease in ability to inhibit nicotine-evoked catecholamine secretion in vitro;, features a modification of the amino acid from R to Q at position 392.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from S to P at position 227.
+The protein's natural variant, known as in strain: Xinghua, features a modification of the amino acid from R to G at position 2.
+The protein's natural variant, known as increased tendency to form aggregates;, features a modification of the amino acid from D to V at position 86.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from S to C at position 779.
+The protein's natural variant, known as in ACNINV1, features a modification of the amino acid from P to R at position 211.
+The protein's natural variant, known as in allele P, features a modification of the amino acid from EV to AI at position 24.
+The protein's natural variant, known as found in a patient with cornea guttata with anterior polar cataracts; unknown pathological significance;, features a modification of the amino acid from P to L at position 14.
+The protein's natural variant, known as in strain: Sr41 / 8000, Sr41 / HNr21; loss of feedback inhibition, features a modification of the amino acid from G to D at position 330.
+The protein's natural variant, known as in strain: Sr41 / TLr156; loss of feedback inhibition, features a modification of the amino acid from S to F at position 352.
+The protein's natural variant, known as in strain: Sr41 / HNr59; Thr-resistant HDI, features a modification of the amino acid from A to T at position 479.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from G to A at position 554.
+The protein's natural variant, known as can be associated with insulin resistance;, features a modification of the amino acid from D to Y at position 905.
+The protein's natural variant, known as in T2D;, features a modification of the amino acid from A to E at position 931.
+The protein's natural variant, known as in MRD67; unknown pathological significance; no effect on localization to the cell membrane; does not affect AMPA glutamate receptor activity;, features a modification of the amino acid from R to Q at position 345.
+The protein's natural variant, known as in MRD67; decreased AMPA glutamate receptor activity; no effect on localization to the cell membrane, features a modification of the amino acid from I to T at position 627.
+The protein's natural variant, known as in MRD67; increased AMPA glutamate receptor activity; increased sensitivity towards glutamate; no effect on localization to the cell membrane;, features a modification of the amino acid from A to T at position 636.
+The protein's natural variant, known as in MRD67; decreased AMPA glutamate receptor activity; no effect on localization to the cell membrane;, features a modification of the amino acid from G to D at position 745.
+The protein's natural variant, known as in benomyl-resistant strain, features a modification of the amino acid from Y to N at position 50.
+The protein's natural variant, known as in NEM9, features a modification of the amino acid from S to SL at position 153.
+The protein's natural variant, known as in NEM9;, features a modification of the amino acid from S to L at position 413.
+The protein's natural variant, known as in MTCHRS; abolishes DNA-binding;, features a modification of the amino acid from R to Q at position 181.
+The protein's natural variant, known as in MTCHRS; induces a slight reduction in DNA-binding; in a patient still alive at age 4.5 years;, features a modification of the amino acid from S to P at position 217.
+The protein's natural variant, known as in MTCHRS; inhibits the transactivation of the insulin and beta-cell L-type calcium channel genes, features a modification of the amino acid from V to G at position 506.
+The protein's natural variant, known as may influence susceptibility to SLE;, features a modification of the amino acid from R to H at position 61.
+The protein's natural variant, known as may influence susceptibility to SLE;, features a modification of the amino acid from A to T at position 383.
+The natural variant of this protein is characterized by an amino acid alteration from E to G at position 6.
+The protein's natural variant, known as in strain: dpf95_94.1 and zim_26H, features a modification of the amino acid from A to T at position 9.
+The natural variant of this protein is characterized by an amino acid alteration from K to Q at position 17.
+The natural variant of this protein is characterized by an amino acid alteration from K to N at position 28.
+The natural variant of this protein is characterized by an amino acid alteration from T to M at position 36.
+The protein's natural variant, known as in strain: zim_38H, features a modification of the amino acid from A to V at position 50.
+The protein's natural variant, known as in strain: zim_36H, features a modification of the amino acid from A to I at position 52.
+The protein's natural variant, known as in strain: dpf95_48.2, dpf95_100.3 and hfl97_93.0, features a modification of the amino acid from A to V at position 52.
+The protein's natural variant, known as in strain: zim_36H, features a modification of the amino acid from F to Y at position 64.
+The protein's natural variant, known as in strain: B4039, features a modification of the amino acid from G to A at position 109.
+The protein's natural variant, known as in strain: dpf95_56.1, features a modification of the amino acid from E to K at position 197.
+The protein's natural variant, known as in strain: dpf95_13.0, features a modification of the amino acid from E to K at position 235.
+The protein's natural variant, known as in strain: dpf95_38.3 and dpf95_4.2, features a modification of the amino acid from R to L at position 240.
+The protein's natural variant, known as in strain: dpf95_38.3 and dpf95_4.2, features a modification of the amino acid from E to D at position 245.
+The protein's natural variant, known as in strain: dpf95_36.4, features a modification of the amino acid from A to S at position 338.
+The protein's natural variant, known as in strain: B4039, dpf95_77.4 and dpf95_90.2, features a modification of the amino acid from V to M at position 341.
+The protein's natural variant, known as in strain: dpf95_90.2, hfl97_1.0, hfl97_13.0, hfl97_15.0, hfl97_50.0, md90_709.1, zim_36H and zim_39H, features a modification of the amino acid from R to K at position 346.
+The natural variant of this protein is characterized by an amino acid alteration from E to K at position 351.
+The protein's natural variant, known as in strain: dpf95_29.3, features a modification of the amino acid from T to S at position 465.
+The protein's natural variant, known as in strain: dpf95_38.3, dpf95_4.2, dpf95_44.3, dpf95_48.2, dpf95_53.1, dpf95_56.1, dpf95_85.1, hfl97_1.0, hfl97_13.0, hfl97_15.0, hfl97_50.0, hfl97_93.0, md90_709.1, zim_11S, zim_23H, zim_35S, zim_36H, zim_38H, zim_39H, zim_44H, zim_48S and zim_49S, features a modification of the amino acid from V to L at position 484.
+The protein's natural variant, known as in strain: dpf95_44.3, dpf95_53.1 and dpf95_85.1, features a modification of the amino acid from A to T at position 530.
+The protein's natural variant, known as in strain: zim_48S, features a modification of the amino acid from I to F at position 540.
+The protein's natural variant, known as in TCS1, features a modification of the amino acid from W to R at position 53.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to K at position 1030.
+The protein's natural variant, known as in PFIC11, features a modification of the amino acid from R to W at position 148.
+The protein's natural variant, known as results in JMH-variant phenotype;, features a modification of the amino acid from R to Q at position 207.
+The protein's natural variant, known as results in JMH-variant phenotype;, features a modification of the amino acid from R to W at position 207.
+The protein's natural variant, known as results in JMH-variant phenotype;, features a modification of the amino acid from R to L at position 347.
+The protein's natural variant, known as results in JMH-variant phenotype;, features a modification of the amino acid from R to H at position 460.
+The protein's natural variant, known as results in JMH-variant phenotype;, features a modification of the amino acid from R to C at position 461.
+The natural variant of this protein is characterized by an amino acid alteration from S to D at position 29.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 106.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from VS to AG at position 9.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from A to S at position 389.
+The protein's natural variant, known as in allele CYP3A43*2, features a modification of the amino acid from YGTHSHKLFKKLGIPGPTPLPFLGTILFYLRGLWNFDRECNEKYGEMWGLYEGQQPMLVIMDPD to LGPIHINFLRSWEFLGQPLCLFWELFCSTLGVFGILTENVMKNTEKCGGCMRGNSPCWSSWIPT at position 88.
+The protein's natural variant, known as in allele CYP3A43*3;, features a modification of the amino acid from P to A at position 340.
+The natural variant of this protein is characterized by an amino acid alteration from H to L at position 114.
+The protein's natural variant, known as found in patients with Barrett esophagus;, features a modification of the amino acid from N to S at position 318.
+The protein's natural variant, known as in SPAX8; unknown pathological significance;, features a modification of the amino acid from L to V at position 163.
+The protein's natural variant, known as in strain: 304A, 319A, 375A, 773A, 774A, 813A, 852A and 859A, features a modification of the amino acid from T to A at position 15.
+The protein's natural variant, known as in strain: 301A, 306A, 313A, 315A, 318A, 322A, 324A, 332A, 357A, 390A, 399A, 732A, 735A, 736A, 737A, 797A, 799A, 808A, 820A, 822A, 838A and 868A, features a modification of the amino acid from V to M at position 88.
+The protein's natural variant, known as in strain: 907A, features a modification of the amino acid from T to S at position 120.
+The protein's natural variant, known as in plasmid pYVa127/90, features a modification of the amino acid from D to E at position 29.
+The protein's natural variant, known as in PFBMFT1; impaired telomerase activity;, features a modification of the amino acid from L to Q at position 55.
+The protein's natural variant, known as associated with acute myeloid leukemia;, features a modification of the amino acid from P to A at position 65.
+The protein's natural variant, known as in PFBMFT1; the mutant protein is demonstrated to cause decreased telomerase activity;, features a modification of the amino acid from V to M at position 170.
+The protein's natural variant, known as in PFBMFT1 and AA; severe and moderate; associated with disease susceptibility; shorter telomeres;, features a modification of the amino acid from A to T at position 202.
+The protein's natural variant, known as associated with acute myeloid leukemia;, features a modification of the amino acid from V to M at position 299.
+The protein's natural variant, known as in PFBMFT1, AA and DKCB4; severe and moderate; associated with susceptibility to acute myelogenous leukemia; the mutant protein has 36% residual activity;, features a modification of the amino acid from H to Y at position 412.
+The protein's natural variant, known as associated with acute myeloid leukemia;, features a modification of the amino acid from R to K at position 522.
+The protein's natural variant, known as in AA; abolishes telomerase catalytic activity but no effect on binding to TERC, features a modification of the amino acid from K to N at position 570.
+The protein's natural variant, known as in AA;, features a modification of the amino acid from R to Q at position 631.
+The protein's natural variant, known as in AA; non-severe; abolishes telomerase catalytic activity but little effect on binding to TERC;, features a modification of the amino acid from G to D at position 682.
+The protein's natural variant, known as in PFBMFT1 and AA; moderate;, features a modification of the amino acid from V to M at position 694.
+The protein's natural variant, known as in DKCB4; the mutant protein has 13% residual activity;, features a modification of the amino acid from P to S at position 704.
+The protein's natural variant, known as in PFBMFT1; the mutant protein is demonstrated to cause severely compromised telomerase activity;, features a modification of the amino acid from A to T at position 716.
+The protein's natural variant, known as in DKCB4; no effect on telomerase catalytic activity and little effect on binding to TERC;, features a modification of the amino acid from P to R at position 721.
+The protein's natural variant, known as in AA; very severe; no effect on telomerase catalytic activity but shortened telomeres;, features a modification of the amino acid from T to M at position 726.
+The protein's natural variant, known as in PFBMFT1; moderate;, features a modification of the amino acid from Y to C at position 772.
+The protein's natural variant, known as in AA;, features a modification of the amino acid from P to L at position 785.
+The protein's natural variant, known as in PFBMFT1; associated with Met-867 in cis on the same allele; the double mutant shows severe defects in telomere repeat addition processivity;, features a modification of the amino acid from V to I at position 791.
+The protein's natural variant, known as in DKCB4; 50% reduction in telomerase activity;, features a modification of the amino acid from R to C at position 811.
+The protein's natural variant, known as in PFBMFT1, features a modification of the amino acid from L to F at position 841.
+The protein's natural variant, known as in PFBMFT1;, features a modification of the amino acid from R to H at position 865.
+The protein's natural variant, known as in PFBMFT1; associated with Ile-791 in cis on the same allele; the double mutant shows severe defects in telomere repeat addition processivity; this mutation causes most if not all of the functional defects;, features a modification of the amino acid from V to M at position 867.
+The protein's natural variant, known as in DKCB4; severe phenotype overlapping with Hoyeraal-Hreidarsson syndrome; very short telomeres and greatly reduced telomerase activity;, features a modification of the amino acid from R to W at position 901.
+The protein's natural variant, known as in DKCA2; abolishes telomerase catalytic activity but no effect on binding to TERC;, features a modification of the amino acid from K to N at position 902.
+The protein's natural variant, known as in PFBMFT1;, features a modification of the amino acid from K to R at position 902.
+The protein's natural variant, known as in PFBMFT1;, features a modification of the amino acid from P to L at position 923.
+The protein's natural variant, known as in DKCA2; shortened telomeres but no effect on telomerase catalytic activity nor on binding to TERC;, features a modification of the amino acid from R to W at position 979.
+The protein's natural variant, known as in PFBMFT1, features a modification of the amino acid from V to F at position 1025.
+The protein's natural variant, known as increased incidence in sporadic acute myeloid leukemia;, features a modification of the amino acid from A to T at position 1062.
+The protein's natural variant, known as in PFBMFT1; severe;, features a modification of the amino acid from V to M at position 1090.
+The protein's natural variant, known as in PFBMFT1; unknown pathological significance; impaired telomerase activity;, features a modification of the amino acid from T to M at position 1110.
+The protein's natural variant, known as in DKCA2; severe; shortened telomeres but no effect on telomerase catalytic activity nor on binding to TERC;, features a modification of the amino acid from F to L at position 1127.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from P to R at position 209.
+The protein's natural variant, known as in strain: Ar5-H12, features a modification of the amino acid from P to T at position 46.
+The protein's natural variant, known as in a plasmacytoma cell line;, features a modification of the amino acid from G to E at position 11.
+The protein's natural variant, known as in a T-cell acute lymphoblastic leukemia cell line; loss of heterodimerization with Bcl-2 or Bcl-X(L);, features a modification of the amino acid from G to R at position 67.
+The protein's natural variant, known as in a Burkitt lymphoma; loss of homodimerization, features a modification of the amino acid from G to V at position 108.
+The protein's natural variant, known as in MPS9;, features a modification of the amino acid from E to K at position 268.
+The protein's natural variant, known as in strain: Isolate TK 22845, features a modification of the amino acid from M to V at position 129.
+The protein's natural variant, known as may represent an allelic variant or a cloning artifact, features a modification of the amino acid from I to N at position 191.
+The protein's natural variant, known as in strain: s2, features a modification of the amino acid from M to L at position 17.
+The protein's natural variant, known as in XLP1; reduced protein stability and reduced affinity for SLAMF1, decreases interaction with FYN;, features a modification of the amino acid from Y to C at position 7.
+The protein's natural variant, known as in XLP1, features a modification of the amino acid from H to D at position 8.
+The protein's natural variant, known as in XLP1; abolishes interaction with SLAMF1, features a modification of the amino acid from G to D at position 16.
+The protein's natural variant, known as in XLP1; unknown pathological significance, features a modification of the amino acid from A to P at position 22.
+The protein's natural variant, known as in XLP1, features a modification of the amino acid from G to S at position 27.
+The protein's natural variant, known as in XLP1; reduced protein stability, features a modification of the amino acid from S to R at position 28.
+The protein's natural variant, known as in XLP1; reduced protein stability and reduced affinity for SLAMF1 and FYN, features a modification of the amino acid from L to P at position 31.
+The protein's natural variant, known as in XLP1;, features a modification of the amino acid from R to T at position 32.
+The protein's natural variant, known as in XLP1, features a modification of the amino acid from D to Y at position 33.
+The protein's natural variant, known as in XLP1; loss of interaction with CD84 and reduced affinity for SLAMF1, features a modification of the amino acid from C to W at position 42.
+The protein's natural variant, known as in XLP1; unknown pathological significance, features a modification of the amino acid from C to Y at position 42.
+The protein's natural variant, known as in XLP1, features a modification of the amino acid from G to V at position 49.
+The protein's natural variant, known as in XLP1; loss of interaction with CD84; loss of interaction with non-phosphorylated SLAMF1, features a modification of the amino acid from T to I at position 53.
+The protein's natural variant, known as in XLP1; reduced protein stability and reduced affinity for SLAMF1 and FYN, features a modification of the amino acid from Y to C at position 54.
+The protein's natural variant, known as in XLP1; reduced affinity for SLAMF1 and FYN;, features a modification of the amino acid from R to L at position 55.
+The protein's natural variant, known as in XLP1; unknown pathological significance, features a modification of the amino acid from R to Q at position 55.
+The protein's natural variant, known as in one XLP1 patient; unknown pathological significance, features a modification of the amino acid from S to P at position 57.
+The protein's natural variant, known as in XLP1; unknown pathological significance, features a modification of the amino acid from E to G at position 67.
+The protein's natural variant, known as in XLP1; loss of interaction with CD84; strongly reduced affinity for SLAMF1;, features a modification of the amino acid from T to I at position 68.
+The protein's natural variant, known as in XLP1; reduced protein stability, features a modification of the amino acid from I to T at position 84.
+The protein's natural variant, known as in XLP1; reduced protein stability and reduced affinity for SLAMF1 and FYN, features a modification of the amino acid from F to S at position 87.
+The protein's natural variant, known as in XLP1; reduced protein stability and strongly reduced affinity for SLAMF1, disrupts interaction with FYN, features a modification of the amino acid from Q to P at position 99.
+The protein's natural variant, known as in XLP1; reduced protein stability and reduced affinity for SLAMF1, decreases interaction with FYN;, features a modification of the amino acid from P to L at position 101.
+The protein's natural variant, known as in XLP1; reduced protein stability and strongly reduced affinity for SLAMF1, decreases interaction with FYN, features a modification of the amino acid from V to G at position 102.
+The protein's natural variant, known as in MCR; profound effect on the voltage-dependence of activation such that mutant channels have a greatly reduced open probability at voltages near the resting membrane potential of skeletal muscle, features a modification of the amino acid from T to M at position 268.
+The protein's natural variant, known as in COFS4; does not alter interaction with ERCC4/XPF;, features a modification of the amino acid from F to L at position 231.
+The natural variant of this protein is characterized by an amino acid alteration from V to A at position 452.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 463.
+The natural variant of this protein is characterized by an amino acid alteration from G to S at position 506.
+The protein's natural variant, known as in PEOB2; has partial residual endonuclease activity;, features a modification of the amino acid from V to I at position 142.
+The protein's natural variant, known as in PEOB2; has partial residual endonuclease activity;, features a modification of the amino acid from A to V at position 185.
+The protein's natural variant, known as in strain: A28, features a modification of the amino acid from G to D at position 107.
+The protein's natural variant, known as in strain: O11, ABM, A28 and C2, features a modification of the amino acid from I to S at position 201.
+The protein's natural variant, known as in strain: C2, features a modification of the amino acid from G to V at position 207.
+The protein's natural variant, known as in strain: O11, ABM and A28, features a modification of the amino acid from V to G at position 209.
+The protein's natural variant, known as in strain: A28, features a modification of the amino acid from G to GGGGGGG at position 212.
+The protein's natural variant, known as in strain: O11 and ABM, features a modification of the amino acid from G to GGVVGG at position 212.
+The protein's natural variant, known as in strain: A28, features a modification of the amino acid from G to GVG at position 237.
+The protein's natural variant, known as in strain: O11 and ABM, features a modification of the amino acid from G to S at position 251.
+The protein's natural variant, known as in strain: I1, features a modification of the amino acid from T to I at position 270.
+The protein's natural variant, known as in strain: A28, features a modification of the amino acid from S to P at position 328.
+The protein's natural variant, known as in strain: O11, features a modification of the amino acid from N to K at position 338.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from P to L at position 80.
+The protein's natural variant, known as in allele CYP2A6*13;, features a modification of the amino acid from G to R at position 5.
+The protein's natural variant, known as in allele CYP2A6*14;, features a modification of the amino acid from S to N at position 29.
+The protein's natural variant, known as in allele CYP2A6*24; increases phenacetin O-deethylation activity 4 fold;, features a modification of the amino acid from V to L at position 110.
+The protein's natural variant, known as in allele CYP2A6*25 and allele CYP2A6*26;, features a modification of the amino acid from F to L at position 118.
+The protein's natural variant, known as in allele CYP2A6*26;, features a modification of the amino acid from R to L at position 128.
+The protein's natural variant, known as in allele CYP2A6*6; loss of activity;, features a modification of the amino acid from R to Q at position 128.
+The protein's natural variant, known as in allele CYP2A6*26;, features a modification of the amino acid from S to A at position 131.
+The protein's natural variant, known as in allele CYP2A6*2; unable to catalyze 7-hydroxylation of coumarin; causes switching from coumarin 7-hydroxylation to 3-hydroxylation;, features a modification of the amino acid from L to H at position 160.
+The protein's natural variant, known as in allele CYP2A6*15;, features a modification of the amino acid from K to E at position 194.
+The protein's natural variant, known as in allele CYP2A6*23; greatly reduced activity toward nicotine C-oxidation as well as reduced coumarin 7-hydroxylation;, features a modification of the amino acid from R to C at position 203.
+The protein's natural variant, known as in allele CYP2A6*16;, features a modification of the amino acid from R to S at position 203.
+The protein's natural variant, known as in allele CYP2A6*17; increases phenacetin O-deethylation activity 2 fold;, features a modification of the amino acid from V to M at position 365.
+The protein's natural variant, known as in allele CYP2A6*28;, features a modification of the amino acid from N to D at position 418.
+The protein's natural variant, known as in allele CYP2A6*28;, features a modification of the amino acid from E to D at position 419.
+The protein's natural variant, known as in allele CYP2A6*24;, features a modification of the amino acid from N to Y at position 438.
+The protein's natural variant, known as in allele CYP2A6*7;, features a modification of the amino acid from I to T at position 471.
+The protein's natural variant, known as in allele CYP2A6*5; loss of activity;, features a modification of the amino acid from G to V at position 479.
+The protein's natural variant, known as in allele CYP2A6*8;, features a modification of the amino acid from R to L at position 485.
+The protein's natural variant, known as in trypanosome isolates, features a modification of the amino acid from V to M at position 131.
+The protein's natural variant, known as in trypanosome isolates, features a modification of the amino acid from S to N at position 472.
+The protein's natural variant, known as in D2HGA2;, features a modification of the amino acid from R to G at position 140.
+The protein's natural variant, known as in D2HGA2;, features a modification of the amino acid from R to Q at position 140.
+The protein's natural variant, known as in GLM; somatic mutation, features a modification of the amino acid from P to L at position 158.
+The protein's natural variant, known as in GLM; somatic mutation, features a modification of the amino acid from P to S at position 162.
+The protein's natural variant, known as in GLM; somatic mutation; reduces enzymatic activity;, features a modification of the amino acid from R to G at position 172.
+The protein's natural variant, known as in GLM; somatic mutation; reduces enzymatic activity;, features a modification of the amino acid from R to K at position 172.
+The protein's natural variant, known as in GLM; somatic mutation; reduces enzymatic activity;, features a modification of the amino acid from R to M at position 172.
+The protein's natural variant, known as found in patients with cartilagenous tumors;, features a modification of the amino acid from R to S at position 172.
+The protein's natural variant, known as found in patients with cartilagenous tumors, features a modification of the amino acid from R to T at position 172.
+The protein's natural variant, known as found in patients with cartilagenous tumors;, features a modification of the amino acid from R to W at position 172.
+The protein's natural variant, known as in CILD20; expressed at very low levels in patients' nasal epithelial cells; the genetic variation producing this missense variant predominantly affects splicing;, features a modification of the amino acid from A to T at position 248.
+The protein's natural variant, known as in PG4D; type I; degradation in the cytoplasm due to defects in maturation;, features a modification of the amino acid from P to S at position 90.
+The protein's natural variant, known as in individuals from a malaria endemic area in West Africa;, features a modification of the amino acid from E to K at position 123.
+The protein's natural variant, known as in individuals from a malaria endemic area in West Africa;, features a modification of the amino acid from T to A at position 174.
+The protein's natural variant, known as in individuals from a malaria endemic area in West Africa, features a modification of the amino acid from G to GN at position 232.
+The protein's natural variant, known as in PG4D; type I;, features a modification of the amino acid from F to L at position 254.
+The protein's natural variant, known as in individuals from a malaria endemic area in West Africa;, features a modification of the amino acid from I to T at position 271.
+The protein's natural variant, known as in PG4D; type I;, features a modification of the amino acid from I to L at position 413.
+The natural variant of this protein is characterized by an amino acid alteration from K to E at position 303.
+The protein's natural variant, known as in allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, allele DQA1*04:01 and allele DQA1*06:01;, features a modification of the amino acid from M to L at position 8.
+The protein's natural variant, known as in allele DQA1*05:05, allele DQA1*05:08 and allele DQA1*05:09;, features a modification of the amino acid from A to T at position 11.
+The protein's natural variant, known as in allele DQA1*01:04 and allele DQA1*01:05;, features a modification of the amino acid from V to M at position 17.
+The protein's natural variant, known as in allele DQA1*03:03;, features a modification of the amino acid from M to T at position 18.
+The protein's natural variant, known as in allele DQA1*05:09;, features a modification of the amino acid from E to K at position 24.
+The protein's natural variant, known as in allele DQA1*01:04 and allele DQA1*01:05;, features a modification of the amino acid from D to G at position 25.
+The protein's natural variant, known as in allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, allele DQA1*01:06 and allele DQA1*01:07;, features a modification of the amino acid from Y to C at position 34.
+The protein's natural variant, known as in allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, allele DQA1*01:06 and allele DQA1*01:07;, features a modification of the amino acid from S to F at position 41.
+The protein's natural variant, known as in allele DQA1*05:04;, features a modification of the amino acid from P to L at position 44.
+The protein's natural variant, known as in allele DQA1*02:01, allele DQA1*01:03, allele DQA1*06:01 and allele DQA1*06:02;, features a modification of the amino acid from Y to F at position 48.
+The protein's natural variant, known as in allele DQA1*03:01, allele DQA1*03:02 and allele DQA1*03:03;, features a modification of the amino acid from T to S at position 49.
+The protein's natural variant, known as in allele DQA1*01:01, allele DQA1*01:04, allele DQA1*01:05, allele DQA1*01:07, allele DQA1*02:01, allele DQA1*03:01, allele DQA1*03:02 and allele DQA1*03:03;, features a modification of the amino acid from Q to E at position 57.
+The protein's natural variant, known as in allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, allele DQA1*01:06, allele DQA1*01:07, allele DQA1*02:01, allele DQA1*03:01, allele DQA1*03:02 and allele DQA1*03:03;, features a modification of the amino acid from G to E at position 63.
+The protein's natural variant, known as in allele DQA1*01:03;, features a modification of the amino acid from R to K at position 64.
+The protein's natural variant, known as in allele DQA1*01:06;, features a modification of the amino acid from T to A at position 67.
+The protein's natural variant, known as in allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, allele DQA1*01:06 and allele DQA1*01:07;, features a modification of the amino acid from V to A at position 68.
+The protein's natural variant, known as in allele DQA1*02:01; requires 2 nucleotide substitutions, features a modification of the amino acid from C to K at position 70.
+The protein's natural variant, known as in allele DQA1*03:01, allele DQA1*03:02 and allele DQA1*03:03; requires 2 nucleotide substitutions, features a modification of the amino acid from C to Q at position 70.
+The protein's natural variant, known as in allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, allele DQA1*01:06 and allele DQA1*01:07;, features a modification of the amino acid from C to R at position 70.
+The protein's natural variant, known as in allele DQA1*01:01, allele DQA1*01:02,allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, allele DQA1*01:06 and allele DQA1*01:07;, features a modification of the amino acid from L to W at position 71.
+The protein's natural variant, known as in allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, allele DQA1*01:06 and allele DQA1*01:07;, features a modification of the amino acid from V to E at position 73.
+The protein's natural variant, known as in allele DQA1*02:01, allele DQA1*03:01, allele DQA1*03:02 and allele DQA1*03:03;, features a modification of the amino acid from V to L at position 73.
+The protein's natural variant, known as in allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, allele DQA1*01:06, allele DQA1*01:07, allele DQA1*02:01, allele DQA1*03:01, allele DQA1*03:02 and allele DQA1*03:03;, features a modification of the amino acid from L to F at position 74.
+The protein's natural variant, known as in allele DQA1*02:01;, features a modification of the amino acid from R to H at position 75.
+The protein's natural variant, known as in allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, allele DQA1*01:06 and allele DQA1*01:07;, features a modification of the amino acid from R to S at position 75.
+The protein's natural variant, known as in allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, allele DQA1*01:06 and allele DQA1*01:07;, features a modification of the amino acid from Q to K at position 76.
+The protein's natural variant, known as in allele DQA1*02:01, allele DQA1*03:01, allele DQA1*03:02 and allele DQA1*03:03;, features a modification of the amino acid from Q to R at position 76.
+The protein's natural variant, known as in allele DQA1*02:01;, features a modification of the amino acid from F to L at position 77.
+The protein's natural variant, known as in allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05,allele DQA1*01:06 and allele DQA1*01:07;, features a modification of the amino acid from R to GG at position 78.
+The protein's natural variant, known as in allele DQA1*03:01, allele DQA1*03:02 and allele DQA1*03:03, features a modification of the amino acid from R to RR at position 78.
+The protein's natural variant, known as in allele DQA1*05:02;, features a modification of the amino acid from P to R at position 81.
+The protein's natural variant, known as in allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, allele DQA1*01:06 and allele DQA1*01:07; requires 2 nucleotide substitutions, features a modification of the amino acid from F to G at position 83.
+The protein's natural variant, known as in allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, allele DQA1*01:06 and allele DQA1*01:07;, features a modification of the amino acid from T to R at position 86.
+The protein's natural variant, known as in allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, allele DQA1*01:06 and allele DQA1*01:07;, features a modification of the amino acid from I to M at position 88.
+The protein's natural variant, known as in allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, allele DQA1*01:06 and allele DQA1*01:07; requires 2 nucleotide substitutions, features a modification of the amino acid from L to A at position 91.
+The protein's natural variant, known as in allele DQA1*04:01, allele DQA1*04:02, allele DQA1*04:04, allele DQA1*06:01 and allele DQA1*06:02; requires 2 nucleotide substitutions, features a modification of the amino acid from L to T at position 91.
+The protein's natural variant, known as in allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, allele DQA1*01:06, allele DQA1*01:07, allele DQA1*02:01, allele DQA1*03:01, allele DQA1*03:02, allele DQA1*03:03, allele DQA1*04:01, allele DQA1*04:02, allele DQA1*04:04, allele DQA1*06:01 and allele DQA1*06:02;, features a modification of the amino acid from S to I at position 97.
+The protein's natural variant, known as in allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, allele DQA1*01:06 and allele DQA1*01:07;, features a modification of the amino acid from L to M at position 98.
+The protein's natural variant, known as in allele DQA1*03:01, allele DQA1*03:02 and allele DQA1*03:03;, features a modification of the amino acid from L to V at position 98.
+The protein's natural variant, known as in allele DQA1*01:07;, features a modification of the amino acid from R to C at position 101.
+The protein's natural variant, known as in allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, allele DQA1*01:06 and allele DQA1*01:07;, features a modification of the amino acid from S to Y at position 102.
+The protein's natural variant, known as in allele DQA1*05:06;, features a modification of the amino acid from L to V at position 124.
+The protein's natural variant, known as in allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, allele DQA1*01:07, allele DQA1*02:01, allele DQA1*03:01, allele DQA1*03:02, allele DQA1*03:03, allele DQA1*04:01, allele DQA1*04:02, allele DQA1*04:04, allele DQA1*06:01 and allele DQA1*06:02;, features a modification of the amino acid from I to T at position 129.
+The protein's natural variant, known as in allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:04, allele DQA1*01:05 and allele DQA1*01:07;, features a modification of the amino acid from H to Q at position 151.
+The protein's natural variant, known as in allele DQA1*01:03;, features a modification of the amino acid from S to A at position 152.
+The protein's natural variant, known as in allele DQA1*04:02;, features a modification of the amino acid from T to I at position 160.
+The protein's natural variant, known as in allele DQA1*05:08;, features a modification of the amino acid from S to I at position 161.
+The protein's natural variant, known as in allele DQA1*06:02;, features a modification of the amino acid from S to R at position 161.
+The protein's natural variant, known as in allele DQA1*04:04;, features a modification of the amino acid from Y to H at position 175.
+The protein's natural variant, known as in allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, allele DQA1*01:07, allele DQA1*02:01, allele DQA1*03:01, allele DQA1*03:02, allele DQA1*03:03, allele DQA1*04:01, allele DQA1*04:02, allele DQA1*04:04, allele DQA1*06:01 and allele DQA1*06:02;, features a modification of the amino acid from L to F at position 178.
+The protein's natural variant, known as in allele DQA1*03:02 and allele DQA1*03:03;, features a modification of the amino acid from A to D at position 182.
+The protein's natural variant, known as in allele DQA1*05:03, allele DQA1*05:06 and allele DQA1*05:07;, features a modification of the amino acid from A to S at position 182.
+The protein's natural variant, known as in allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, allele DQA1*01:07, allele DQA1*02:01, allele DQA1*03:01, allele DQA1*03:02, allele DQA1*03:03, allele DQA1*04:01, allele DQA1*04:02, allele DQA1*04:04, allele DQA1*06:01 and allele DQA1*06:02;, features a modification of the amino acid from E to D at position 183.
+The protein's natural variant, known as in allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, allele DQA1*01:07, allele DQA1*02:01, allele DQA1*03:01, allele DQA1*03:02, allele DQA1*03:03, allele DQA1*04:01, allele DQA1*04:02, allele DQA1*04:04, allele DQA1*06:01 and allele DQA1*06:02;, features a modification of the amino acid from S to I at position 185.
+The protein's natural variant, known as in allele DQA1*02:01, allele DQA1*03:01, allele DQA1*03:02, allele DQA1*03:03, allele DQA1*04:01, allele DQA1*04:02, allele DQA1*04:04, allele DQA1*06:01 and allele DQA1*06:02;, features a modification of the amino acid from K to E at position 197.
+The protein's natural variant, known as in allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05 and allele DQA1*01:07;, features a modification of the amino acid from K to Q at position 197.
+The protein's natural variant, known as in allele DQA1*03:01, allele DQA1*03:02 and allele DQA1*03:03;, features a modification of the amino acid from A to T at position 209.
+The protein's natural variant, known as in allele DQA1*01:04;, features a modification of the amino acid from A to T at position 221.
+The protein's natural variant, known as in allele DQA1*01:02;, features a modification of the amino acid from V to M at position 229.
+The protein's natural variant, known as in allele DQA1*05:07;, features a modification of the amino acid from G to C at position 230.
+The protein's natural variant, known as in allele DQA1*02:01, allele DQA1*03:01, allele DQA1*03:02 and allele DQA1*03:03;, features a modification of the amino acid from F to L at position 237.
+The protein's natural variant, known as in allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04 and allele DQA1*01:05;, features a modification of the amino acid from R to Q at position 240.
+The protein's natural variant, known as in WMS3;, features a modification of the amino acid from V to M at position 1177.
+The protein's natural variant, known as in RDGCA;, features a modification of the amino acid from E to A at position 261.
+The protein's natural variant, known as in CAA-ITM2B2; amyloid ADan; colocalizes with APP amyloid-beta protein 42 in parenchymal and vascular lesions; interacts with APP amyloid-beta protein 42; oligomerizes and is subjected to disulfide bond formation; undergoes cyclic pyroglutamate formation on the N-terminus Gln residues and is further proteolytically cleaved in the cerebral cortex, features a modification of the amino acid from S to FNLFLNSQEKHY at position 266.
+The protein's natural variant, known as in CAA-ITM2B1; amyloid ABri, features a modification of the amino acid from S to SRTVKKNIIEEN at position 266.
+The protein's natural variant, known as in strain: Isolate AF 21115, features a modification of the amino acid from A to T at position 23.
+The protein's natural variant, known as in strain: Isolate AF 21116, features a modification of the amino acid from N to D at position 214.
+The protein's natural variant, known as in PCH1B;, features a modification of the amino acid from G to A at position 31.
+The protein's natural variant, known as in PCH1B;, features a modification of the amino acid from D to A at position 132.
+The protein's natural variant, known as in PCH1B;, features a modification of the amino acid from A to P at position 139.
+The protein's natural variant, known as in PCH1B;, features a modification of the amino acid from W to R at position 238.
+The protein's natural variant, known as associated with lower sodium concentrations in serum; shows diminished response to hypotonic stress relative to wild-type;, features a modification of the amino acid from P to S at position 19.
+The protein's natural variant, known as in MTD; lethal form;, features a modification of the amino acid from T to I at position 89.
+The protein's natural variant, known as in HMN8; loss of function mutation;, features a modification of the amino acid from P to R at position 97.
+The protein's natural variant, known as found in a patient with spondyloepiphyseal dysplasia Maroteaux type; decreased protein stability; increased ATP-binding;, features a modification of the amino acid from E to K at position 183.
+The protein's natural variant, known as in MTD; lethal form; decreased protein stability; reduced ATP-binding;, features a modification of the amino acid from K to R at position 197.
+The protein's natural variant, known as in MTD; decreased protein stability;, features a modification of the amino acid from L to F at position 199.
+The protein's natural variant, known as in HMN8 and CMT2C; does not affect channel localization to plasma membrane; results in increased agonist-induced channel activity and increased basal intracellular calcium concentration; decreases ATP-binding; no effect on protein stability; decreases binding to membranes enriched in phosphatidylinositol-2,4-bisphosphate; causes increased cell death;, features a modification of the amino acid from R to C at position 232.
+The protein's natural variant, known as in CMT2C; increased agonist-induced channel activity; causes increased cell death; no effect on protein stability and ATP-binding;, features a modification of the amino acid from R to C at position 269.
+The protein's natural variant, known as in HMN8 and CMT2C; increased agonist-induced channel activity and increased basal intracellular calcium concentration; slightly decreased protein stability and ATP-binding; decreases binding to membranes enriched in phosphatidylinositol-2,4-bisphosphate; causes increased cell death;, features a modification of the amino acid from R to H at position 269.
+The protein's natural variant, known as in FDAB; poorly expressed on the cell surface; mutant channels show a significantly reduced response to agonists;, features a modification of the amino acid from G to V at position 270.
+The protein's natural variant, known as in FDAB; poorly expressed on the cell surface; mutant channels show a significantly reduced response to agonists;, features a modification of the amino acid from R to P at position 271.
+The protein's natural variant, known as in FDAB; poorly expressed on the cell surface; mutant channels show a significantly reduced response to agonists;, features a modification of the amino acid from F to L at position 273.
+The protein's natural variant, known as in SMDK; slightly increased ATP-binding; slightly decreased protein stability;, features a modification of the amino acid from E to K at position 278.
+The protein's natural variant, known as in MTD; impairs protein folding or stability;, features a modification of the amino acid from T to A at position 295.
+The protein's natural variant, known as in CMT2C; increased basal and agonist-induced channel activity, decreased protein stability; decreased ATP-binding; decreases binding to membranes enriched in phosphatidylinositol-2,4-bisphosphate; causes increased cell death;, features a modification of the amino acid from R to W at position 315.
+The protein's natural variant, known as in CMT2C and SPSMA; decreased protein stability; decreased ATP-binding;, features a modification of the amino acid from R to C at position 316.
+The protein's natural variant, known as in CMT2C; does not affect channel localization to plasma membrane; results in increased agonist-induced channel activity and increased basal intracellular calcium concentration; decreases protein stability; causes increased cell death;, features a modification of the amino acid from R to H at position 316.
+The protein's natural variant, known as in MTD; decreased protein stability; no effect on ATP-binding;, features a modification of the amino acid from I to F at position 331.
+The protein's natural variant, known as in MTD; no effect on protein stability; no effect on ATP-binding;, features a modification of the amino acid from I to T at position 331.
+The protein's natural variant, known as in SMDK; decreased protein stability; no effect on ATP-binding;, features a modification of the amino acid from D to G at position 333.
+The protein's natural variant, known as in MTD; decreased protein stability; decreased ATP-binding;, features a modification of the amino acid from V to F at position 342.
+The protein's natural variant, known as in CMT2C;, features a modification of the amino acid from S to Y at position 542.
+The protein's natural variant, known as in MTD;, features a modification of the amino acid from F to L at position 592.
+The protein's natural variant, known as in SMDK and PSTD;, features a modification of the amino acid from R to H at position 594.
+The protein's natural variant, known as in SMDK;, features a modification of the amino acid from L to P at position 596.
+The protein's natural variant, known as in SMDK;, features a modification of the amino acid from G to W at position 600.
+The protein's natural variant, known as found in a patient with spondyloepiphyseal dysplasia Maroteaux type;, features a modification of the amino acid from Y to C at position 602.
+The protein's natural variant, known as in MTD; lethal form;, features a modification of the amino acid from I to M at position 604.
+The protein's natural variant, known as in BCYM3; results in a gain of function and a constitutive activation of the channel;, features a modification of the amino acid from R to Q at position 616.
+The protein's natural variant, known as in MTD;, features a modification of the amino acid from F to L at position 617.
+The protein's natural variant, known as in MTD;, features a modification of the amino acid from L to P at position 618.
+The protein's natural variant, known as in BCYM3; results in a gain of function and a constitutive activation of the channel;, features a modification of the amino acid from V to I at position 620.
+The protein's natural variant, known as in SMDK;, features a modification of the amino acid from M to I at position 625.
+The protein's natural variant, known as in SMDK;, features a modification of the amino acid from L to M at position 709.
+The protein's natural variant, known as in SMDK;, features a modification of the amino acid from A to S at position 716.
+The protein's natural variant, known as in MTD, features a modification of the amino acid from R to K at position 775.
+The protein's natural variant, known as in SMDK;, features a modification of the amino acid from C to Y at position 777.
+The protein's natural variant, known as in MTD and SMDK; also found in a patient with spondyloepiphyseal dysplasia Maroteaux type;, features a modification of the amino acid from E to K at position 797.
+The protein's natural variant, known as in MTD;, features a modification of the amino acid from P to A at position 799.
+The protein's natural variant, known as in MTD; also found in a patient with spondyloepiphyseal dysplasia Maroteaux type;, features a modification of the amino acid from P to L at position 799.
+The protein's natural variant, known as in MTD;, features a modification of the amino acid from P to R at position 799.
+The protein's natural variant, known as in MTD;, features a modification of the amino acid from P to S at position 799.
+The protein's natural variant, known as in susceptible haplotype, features a modification of the amino acid from Q to L at position 88.
+The protein's natural variant, known as in susceptible haplotype, features a modification of the amino acid from P to S at position 149.
+The protein's natural variant, known as in susceptible haplotype, features a modification of the amino acid from I to T at position 166.
+The protein's natural variant, known as in susceptible haplotype, features a modification of the amino acid from F to V at position 559.
+The protein's natural variant, known as in susceptible haplotype, features a modification of the amino acid from N to S at position 563.
+The protein's natural variant, known as in susceptible haplotype, features a modification of the amino acid from K to R at position 566.
+The protein's natural variant, known as in susceptible haplotype, features a modification of the amino acid from SKLGSLRNLLLDGCSLTSTPPRIGLLTCLKSLSCFVIGKRKGH to ISKLLCYWQEKGY at position 635.
+The protein's natural variant, known as in susceptible haplotype, features a modification of the amino acid from R to L at position 715.
+The protein's natural variant, known as in susceptible haplotype, features a modification of the amino acid from D to E at position 762.
+The protein's natural variant, known as in susceptible haplotype, features a modification of the amino acid from A to S at position 970.
+The protein's natural variant, known as in common allele, features a modification of the amino acid from N to D at position 80.
+The protein's natural variant, known as in common and uncommon allele, features a modification of the amino acid from Q to K at position 87.
+The protein's natural variant, known as in allele CYP2E1*2; reduced activity;, features a modification of the amino acid from R to H at position 76.
+The protein's natural variant, known as in allele CYP2E1*4;, features a modification of the amino acid from V to I at position 179.
+The protein's natural variant, known as in allele CYP2E1*3;, features a modification of the amino acid from V to I at position 389.
+The protein's natural variant, known as in strain: FVB/N, features a modification of the amino acid from P to S at position 288.
+The protein's natural variant, known as in CTRCT16; unknown pathological significance;, features a modification of the amino acid from R to C at position 69.
+The protein's natural variant, known as probable disease-associated variant found in patients with restrictive cardiomyopathy; reduces CRYAB and DES localization at the Z-bands and the intercalated disk in the myocardium; cytoplasmic aggregations of CRYAB and DES;, features a modification of the amino acid from D to G at position 109.
+The protein's natural variant, known as in MFM2;, features a modification of the amino acid from D to H at position 109.
+The protein's natural variant, known as in MFM2; decreased interactions with wild-type CRYAA and CRYAB but increased interactions with wild-type CRYBB2 and CRYGC; cytoplasmic aggregation;, features a modification of the amino acid from R to G at position 120.
+The protein's natural variant, known as in CMD1II;, features a modification of the amino acid from G to S at position 154.
+The protein's natural variant, known as in CMD1II;, features a modification of the amino acid from R to H at position 157.
+The protein's natural variant, known as in CTRCT16; unknown pathological significance;, features a modification of the amino acid from A to T at position 171.
+The natural variant of this protein is characterized by an amino acid alteration from R to P at position 125.
+The protein's natural variant, known as in beta-2, features a modification of the amino acid from E to Q at position 125.
+The protein's natural variant, known as in AMACRD and CBAS4; inactive enzyme;, features a modification of the amino acid from S to P at position 52.
+The protein's natural variant, known as in CBAS4; inactive enzyme;, features a modification of the amino acid from L to P at position 107.
+The protein's natural variant, known as in NS9;, features a modification of the amino acid from M to K at position 267.
+The protein's natural variant, known as in NS9; unknown pathological significance, features a modification of the amino acid from N to K at position 310.
+The protein's natural variant, known as in NS9; unknown pathological significance;, features a modification of the amino acid from R to H at position 334.
+The protein's natural variant, known as in NS9;, features a modification of the amino acid from T to S at position 376.
+The protein's natural variant, known as in NS9; unknown pathological significance;, features a modification of the amino acid from P to L at position 1092.
+The protein's natural variant, known as in GM2GAB;, features a modification of the amino acid from C to R at position 138.
+The protein's natural variant, known as in GM2GAB;, features a modification of the amino acid from R to P at position 169.
+The protein's natural variant, known as sumoylated and increases total protein sumoylation levels;, features a modification of the amino acid from N to K at position 103.
+The protein's natural variant, known as in BEFAHRS; unknown pathological significance; no effect on methylcytosine dioxygenase activity;, features a modification of the amino acid from R to C at position 752.
+The protein's natural variant, known as in BEFAHRS;, features a modification of the amino acid from T to M at position 851.
+The protein's natural variant, known as in BEFAHRS; decreases methylcytosine dioxygenase activity;, features a modification of the amino acid from V to L at position 908.
+The protein's natural variant, known as in BEFAHRS; decreases methylcytosine dioxygenase activity;, features a modification of the amino acid from F to C at position 1072.
+The protein's natural variant, known as in BEFAHRS; decreases methylcytosine dioxygenase activity;, features a modification of the amino acid from A to T at position 1076.
+The protein's natural variant, known as in BEFAHRS; decreases methylcytosine dioxygenase activity;, features a modification of the amino acid from V to M at position 1089.
+The protein's natural variant, known as in BEFAHRS;, features a modification of the amino acid from P to L at position 1677.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from R to H at position 396.
+The protein's natural variant, known as in strain: BALB/c, C3H/He, CBA/Ca and DBA/2J, features a modification of the amino acid from T to I at position 44.
+The protein's natural variant, known as in strain: BALB/c, C3H/He, CBA/Ca and DBA/2J, features a modification of the amino acid from G to D at position 155.
+The protein's natural variant, known as in strain: BALB/c, C3H/He, CBA/Ca and DBA/2J, features a modification of the amino acid from L to R at position 294.
+The protein's natural variant, known as in isoform TX11P, features a modification of the amino acid from MVII to LVFF at position 7.
+The protein's natural variant, known as in isoform TX11P, features a modification of the amino acid from V to L at position 13.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation, features a modification of the amino acid from R to K at position 19.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation, features a modification of the amino acid from P to L at position 23.
+The protein's natural variant, known as in LPFS1; shows nearly undetectable mutant ITK protein consistent with severe protein instability;, features a modification of the amino acid from R to W at position 335.
+The protein's natural variant, known as in a gastric adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from R to Q at position 451.
+The protein's natural variant, known as in strain: Tulahuen, features a modification of the amino acid from A to P at position 186.
+The protein's natural variant, known as in strain: cv. Pinot noir, features a modification of the amino acid from Q to Z at position 47.
+The protein's natural variant, known as in strain: cv. Italia, cv. Pinot noir and cv. Ruby Okuyama, features a modification of the amino acid from I to V at position 69.
+The protein's natural variant, known as in strain: cv. Pinot noir / PN40024, features a modification of the amino acid from P to A at position 74.
+The protein's natural variant, known as in strain: cv. Flame Muscat, cv. Italia, cv. Muscat of Alexandria, cv. Pinot noir, cv. Pinot noir /PN40024, cv. Red Globe and cv. Ruby Okuyama, features a modification of the amino acid from T to M at position 91.
+The protein's natural variant, known as in strain: cv. Flame Muscat, cv. Italia, cv. Muscat of Alexandria, cv. Pinot noir, cv. Pinot noir /PN40024, cv. Red Globe and cv. Ruby Okuyama, features a modification of the amino acid from L to V at position 134.
+The protein's natural variant, known as in strain: cv. Flame Muscat, cv. Italia, cv. Muscat of Alexandria, cv. Pinot noir / PN40024, cv. Red Globe and cv. Ruby Okuyama, features a modification of the amino acid from I to T at position 153.
+The protein's natural variant, known as in cv. Red Globe, features a modification of the amino acid from G to A at position 161.
+The protein's natural variant, known as in strain: cv. Pinot noir / PN40024, features a modification of the amino acid from S to SG at position 163.
+The protein's natural variant, known as in strain: cv. Italia, cv. Pinot noir /PN40024 and cv. Ruby Okuyama, features a modification of the amino acid from V to I at position 255.
+The protein's natural variant, known as in strain: cv. Flame Muscat, cv. Italia, cv. Muscat of Alexandria, cv. Pinot noir, cv. Pinot noir /PN40024, cv. Red Globe and cv. Ruby Okuyama, features a modification of the amino acid from V to L at position 289.
+The protein's natural variant, known as in strain: cv. Flame Muscat, cv. Italia, cv. Muscat of Alexandria, cv. Pinot noir, cv. Pinot noir /PN40024, cv. Red Globe and cv. Ruby Okuyama, features a modification of the amino acid from S to A at position 293.
+The protein's natural variant, known as in strain: cv. Flame Muscat, cv. Lambrusco Foglia Frastagliata and cv. Muscat of Alexandria, features a modification of the amino acid from R to S at position 312.
+The protein's natural variant, known as in cv. Red Globe, features a modification of the amino acid from Y to H at position 326.
+The protein's natural variant, known as in strain: cv. Pinot noir / PN40024, features a modification of the amino acid from F to Y at position 372.
+The protein's natural variant, known as in strain: cv. Flame Muscat, cv. Italia, cv. Muscat of Alexandria, cv. Pinot noir, cv. Pinot noir /PN40024, cv. Red Globe and cv. Ruby Okuyama, features a modification of the amino acid from V to A at position 385.
+The protein's natural variant, known as in strain: cv. Flame Muscat and cv. Muscat of Alexandria, features a modification of the amino acid from KS to EN at position 400.
+The protein's natural variant, known as in strain: cv. Flame Muscat, cv. Italia, cv. Muscat of Alexandria, cv. Pinot noir, cv. Pinot noir /PN40024 and cv. Ruby Okuyama, features a modification of the amino acid from K to E at position 399.
+The protein's natural variant, known as in strain: cv. Pinot noir / PN40024, features a modification of the amino acid from R to G at position 423.
+The protein's natural variant, known as in strain: cv. Flame Muscat, cv. Italia, cv. Lambrusco Foglia Frastagliata, cv. Muscat of Alexandria, cv. Pinot noir, cv. Pinot noir / PN40024, cv. Red Globe and cv. Ruby Okuyama, features a modification of the amino acid from I to K at position 444.
+The protein's natural variant, known as in strain: PBOL, features a modification of the amino acid from S to N at position 142.
+The protein's natural variant, known as in strain: PBOL, features a modification of the amino acid from R to G at position 249.
+The protein's natural variant, known as in strain: PBOL, features a modification of the amino acid from R to P at position 457.
+The protein's natural variant, known as in strain: PBOL, features a modification of the amino acid from A to P at position 521.
+The protein's natural variant, known as in strain: PBOL, features a modification of the amino acid from A to T at position 531.
+The protein's natural variant, known as in strain: PBOL, features a modification of the amino acid from A to S at position 534.
+The protein's natural variant, known as in strain: PBOL, features a modification of the amino acid from L to F at position 538.
+The protein's natural variant, known as in strain: NVIII-m11, features a modification of the amino acid from V to F at position 83.
+The protein's natural variant, known as in strain: NVIII-m11, features a modification of the amino acid from H to Q at position 151.
+The protein's natural variant, known as in RP89; increase in primary cilia length; does not affect protein stability; significant increase of rhodopsin in the rod inner segment when expressed in zebrafish; coinjection with wild-type rescued the rhodopsin mislocalization defects, features a modification of the amino acid from E to Q at position 250.
+The protein's natural variant, known as in RP89; increase in primary cilia length; does not affect protein stability; significant increase of rhodopsin in the rod inner segment when expressed in zebrafish; coinjection with wild-type rescued the rhodopsin mislocalization defects, features a modification of the amino acid from L to P at position 523.
+The protein's natural variant, known as in factor XI deficiency, features a modification of the amino acid from F to LYVQNI at position 290.
+The protein's natural variant, known as found in a patient with very early onset inflammatory bowel disease; unknown pathological significance; no effect on subcellular location; significantly reduced basal and phorbol ester-stimulated ROS generation, which may decrease resistance to infection by enteric pathogens, such as Campylobacter jejuni, features a modification of the amino acid from P to S at position 330.
+The protein's natural variant, known as found in a patient with very early onset inflammatory bowel disease; unknown pathological significance; no effect on subcellular location; significantly reduced basal and phorbol ester-stimulated ROS generation, which may decrease resistance to infection by enteric pathogens, such as Campylobacter jejuni;, features a modification of the amino acid from D to N at position 360.
+The natural variant of this protein is characterized by an amino acid alteration from K to E at position 276.
+The natural variant of this protein is characterized by an amino acid alteration from C to R at position 354.
+The natural variant of this protein is characterized by an amino acid alteration from T to A at position 415.
+The protein's natural variant, known as in CHM; may affect splicing, features a modification of the amino acid from Q to L at position 471.
+The protein's natural variant, known as in CHM; impairs the interaction with RABGGTA;, features a modification of the amino acid from H to R at position 507.
+The protein's natural variant, known as in CHM, features a modification of the amino acid from L to P at position 550.
+The protein's natural variant, known as in cht, features a modification of the amino acid from G to V at position 19.
+The protein's natural variant, known as in HFS; infantile form;, features a modification of the amino acid from L to P at position 45.
+The protein's natural variant, known as in HFS;, features a modification of the amino acid from G to D at position 105.
+The protein's natural variant, known as in HFS; infantile form;, features a modification of the amino acid from I to T at position 189.
+The protein's natural variant, known as in HFS; infantile form;, features a modification of the amino acid from C to R at position 218.
+The protein's natural variant, known as in HFS, features a modification of the amino acid from V to VQ at position 293.
+The protein's natural variant, known as in HFS;, features a modification of the amino acid from L to R at position 329.
+The protein's natural variant, known as in HFS;, features a modification of the amino acid from Y to C at position 381.
+The protein's natural variant, known as in IMD72; loss of function; decreased protein levels in T-cells; T-cells display excessive degranulation and granule release;, features a modification of the amino acid from R to L at position 258.
+The protein's natural variant, known as in IMD72; loss of function; decreased protein levels in T-cells; decreased interaction with WASF2 and poor formation of WAVE2 complex; T-cells display excessive degranulation and granule release; cells exhibit reduced cortical F-actin and aberrant membrane spikes and WAS-mediated puncta, defective cell spreading and lamellipodia and reduced migratory velocity, as well as abnormal activation, blunted proliferation, decreased IL2 and TNF production and defective TCR-induced phosphorylation of mTORC2 complex substrate AKT; homozygous patient neutrophils migrating in chemokine gradients exhibit reduced velocity and directional persistence, unusual elongation and misdirected competing leading edges; no effect on interaction with RICTOR;, features a modification of the amino acid from P to L at position 359.
+The protein's natural variant, known as in IMD72; loss of function; T-cells display excessive degranulation and granule release; no effect on protein levels in T-cells, nor on interaction with WASF2; when tested in a heterologous system, formed WAVE complexes that poorly interact with ARF1 and could not promote F-actin polymerization upon stimulation with an ARF1-RAC1 dimer; no effect on interaction with RICTOR;, features a modification of the amino acid from M to V at position 371.
+The protein's natural variant, known as in IMD72; loss of function; decreased protein levels in T-cells; decreased interaction with WASF2 and poor formation of WAVE2 complex;, features a modification of the amino acid from V to L at position 519.
+The protein's natural variant, known as in HH11; unequivocal evidence of impaired receptor signaling;, features a modification of the amino acid from G to D at position 93.
+The protein's natural variant, known as in HH11, features a modification of the amino acid from F to V at position 137.
+The protein's natural variant, known as may contribute to hypogonadotropic hypogonadism in patients carrying disease-causing mutations in FGFR1;, features a modification of the amino acid from K to R at position 286.
+The protein's natural variant, known as in HH11;, features a modification of the amino acid from M to V at position 346.
+The protein's natural variant, known as in HH11; unequivocal evidence of impaired receptor signaling;, features a modification of the amino acid from P to S at position 353.
+The protein's natural variant, known as in HH11; the patient also carries a mutation in FGFR1;, features a modification of the amino acid from R to Q at position 364.
+The protein's natural variant, known as may contribute to hypogonadotropic hypogonadism in patients carrying disease-causing mutations in SPRY4 or KAL1;, features a modification of the amino acid from A to T at position 449.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from E to G at position 420.
+The protein's natural variant, known as in PHPVAR; unknown pathological significance, features a modification of the amino acid from R to P at position 42.
+The protein's natural variant, known as in PHPVAR; loss of function; polypeptide is stable, but does not bind DNA or activate transcription; does not restore retinal ganglion cell development in retinal explants from a mouse Atoh7 null mutant; abolishes heterodimerization with TCF3 E47 isoform; reduces DNA-binding ability and abolishes transcriptional activation; no effect on nuclear localization;, features a modification of the amino acid from N to H at position 46.
+The protein's natural variant, known as found in a sporadic case of optic nerve hypoplasia; unknown pathological significance; does not affect DNA-binding activity but reduces transcription activation, features a modification of the amino acid from A to T at position 47.
+The protein's natural variant, known as in PHPVAR;, features a modification of the amino acid from E to V at position 49.
+The protein's natural variant, known as found in patients with bilateral optic nerve hypoplasia; unknown pathological significance; abolishes heterodimerization with TCF3 E47 isoform; reduces DNA-binding ability and abolishes transcriptional activation; no effect on nuclear localization;, features a modification of the amino acid from A to T at position 59.
+The protein's natural variant, known as found in patients with bilateral optic nerve hypoplasia; unknown pathological significance; abolishes heterodimerization with TCF3 E47 isoform; reduces DNA-binding ability and abolishes transcriptional activation; no effect on nuclear localization;, features a modification of the amino acid from A to V at position 59.
+The protein's natural variant, known as does not affect DNA-binding activity or transcription activation;, features a modification of the amino acid from R to G at position 65.
+The protein's natural variant, known as in strain: CCUG 37603, features a modification of the amino acid from N to S at position 5.
+The protein's natural variant, known as in CDLSMD; unknown pathological significance; no effect on enzymatic activity; does not localize to plasma membrane; accumulates in the endoplasmic reticulum, features a modification of the amino acid from I to S at position 62.
+The protein's natural variant, known as in CDLSMD; unknown pathological significance; no effect on enzymatic activity; does not localize to plasma membrane; accumulates in the endoplasmic reticulum, features a modification of the amino acid from M to R at position 64.
+The protein's natural variant, known as in strain: 178.7, 709.6, A-26, DPF-13, DPF-2, DPF-30, DPF-46, DPF-53, DPF-62, DPF-77, DPF-81, DPF-82.1, EM-10, Mali-10.2, Mali-4.2, Mali-4.4, Oregon-R, R-60, VC-805, VC-815, Z-1, Z-35, Z-44, Z-48 and Z-5, features a modification of the amino acid from Q to K at position 173.
+The protein's natural variant, known as in strain: 709.6, features a modification of the amino acid from V to F at position 230.
+The natural variant of this protein is characterized by an amino acid alteration from D to L at position 40.
+The natural variant of this protein is characterized by an amino acid alteration from NDI to Q at position 120.
+The protein's natural variant, known as in strain: CNRZ 1269, features a modification of the amino acid from Q to P at position 242.
+The protein's natural variant, known as in MRT46;, features a modification of the amino acid from G to S at position 611.
+The protein's natural variant, known as in MRT46;, features a modification of the amino acid from F to L at position 640.
+The protein's natural variant, known as in MRT46;, features a modification of the amino acid from E to D at position 642.
+The protein's natural variant, known as in MRT46;, features a modification of the amino acid from R to Q at position 709.
+The protein's natural variant, known as in TLIND; unknown pathological significance, features a modification of the amino acid from E to K at position 169.
+The protein's natural variant, known as does not affect transcriptional activity as shown by a transcriptional reporter assay;, features a modification of the amino acid from P to S at position 242.
+The natural variant of this protein is characterized by an amino acid alteration from A to V at position 283.
+The protein's natural variant, known as in TIDAND and TLIND; severely reduced transcriptional activity as shown by a transcriptional reporter assay;, features a modification of the amino acid from R to W at position 320.
+The protein's natural variant, known as in TLIND; unknown pathological significance, features a modification of the amino acid from H to N at position 321.
+The protein's natural variant, known as in TLIND; unknown pathological significance, features a modification of the amino acid from L to P at position 325.
+The protein's natural variant, known as in TIDTA; decreased transcriptional activity as shown by a transcriptional reporter assay, features a modification of the amino acid from WKRKDP to C at position 368.
+The protein's natural variant, known as does not affect transcriptional activity as shown by a transcriptional reporter assay;, features a modification of the amino acid from P to S at position 430.
+The natural variant of this protein is characterized by an amino acid alteration from N to S at position 105.
+The natural variant of this protein is characterized by an amino acid alteration from T to A at position 211.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from E to G at position 250.
+The protein's natural variant, known as found in a patient with gout; does not affect isoform 2 localization at the cell membrane; results in reduced urate efflux;, features a modification of the amino acid from N to H at position 68.
+The protein's natural variant, known as found in a patient with hyperuricemia; decreased expression of isoform 2 at the cell membrane; results in highly reduced urate efflux;, features a modification of the amino acid from F to S at position 226.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation, features a modification of the amino acid from G to E at position 848.
+The protein's natural variant, known as in a gastric adenocarcinoma sample; somatic mutation, features a modification of the amino acid from G to E at position 870.
+The protein's natural variant, known as in strain: K1. DS21; results in a greatly reduced affinity for the herbicide glyphosate, features a modification of the amino acid from G to A at position 96.
+The natural variant of this protein is characterized by an amino acid alteration from S to T at position 566.
+The natural variant of this protein is characterized by an amino acid alteration from L to V at position 579.
+The protein's natural variant, known as in TPFS, features a modification of the amino acid from P to L at position 65.
+The protein's natural variant, known as in TPFS, features a modification of the amino acid from P to S at position 65.
+The protein's natural variant, known as in murF2; temperature-sensitive mutant with low activity, features a modification of the amino acid from A to T at position 288.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from A to T at position 137.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from N to S at position 53.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from M to V at position 105.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from P to S at position 659.
+The protein's natural variant, known as in NDHSAL;, features a modification of the amino acid from R to Q at position 1191.
+The protein's natural variant, known as in NDHSAL;, features a modification of the amino acid from F to V at position 1193.
+The protein's natural variant, known as in NDHSAL;, features a modification of the amino acid from R to W at position 1330.
+The protein's natural variant, known as in NDHSAL;, features a modification of the amino acid from E to G at position 1445.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from D to H at position 383.
+The protein's natural variant, known as in ATORS;, features a modification of the amino acid from S to R at position 81.
+The protein's natural variant, known as in ATORS;, features a modification of the amino acid from R to W at position 132.
+The protein's natural variant, known as in ATORS;, features a modification of the amino acid from G to V at position 142.
+The protein's natural variant, known as associated with lower insulin level;, features a modification of the amino acid from A to T at position 206.
+The protein's natural variant, known as in ATORS;, features a modification of the amino acid from R to Q at position 231.
+The protein's natural variant, known as in ATORS;, features a modification of the amino acid from G to E at position 246.
+The protein's natural variant, known as in ATORS;, features a modification of the amino acid from G to W at position 426.
+The protein's natural variant, known as in ATORS;, features a modification of the amino acid from E to K at position 437.
+The protein's natural variant, known as in ATORS;, features a modification of the amino acid from G to E at position 445.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from D to H at position 1245.
+The protein's natural variant, known as impaired ability to bind substrate proteins, features a modification of the amino acid from C to R at position 627.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from K to N at position 33.
+The protein's natural variant, known as in CDG2C; does not rescue defective fucosylation in cells lacking GDP-fucose transport;, features a modification of the amino acid from R to C at position 147.
+The protein's natural variant, known as in CDG2C;, features a modification of the amino acid from T to R at position 308.
+The protein's natural variant, known as in PPRD;, features a modification of the amino acid from C to R at position 78.
+The protein's natural variant, known as in PPRD, features a modification of the amino acid from C to Y at position 78.
+The protein's natural variant, known as in PPRD; unknown pathological significance, features a modification of the amino acid from Y to F at position 99.
+The protein's natural variant, known as in PPRD; unknown pathological significance, features a modification of the amino acid from C to S at position 100.
+The protein's natural variant, known as in PPRD, features a modification of the amino acid from C to R at position 114.
+The protein's natural variant, known as in PPRD, features a modification of the amino acid from C to W at position 114.
+The protein's natural variant, known as in PPRD, features a modification of the amino acid from C to Y at position 114.
+The protein's natural variant, known as in PPRD; unknown pathological significance, features a modification of the amino acid from C to R at position 145.
+The protein's natural variant, known as in PPRD; unknown pathological significance;, features a modification of the amino acid from C to Y at position 145.
+The protein's natural variant, known as in PPRD;, features a modification of the amino acid from C to G at position 223.
+The protein's natural variant, known as in PPRD, features a modification of the amino acid from G to V at position 226.
+The protein's natural variant, known as in PPRD; unknown pathological significance, features a modification of the amino acid from S to P at position 228.
+The protein's natural variant, known as in PPRD; unknown pathological significance, features a modification of the amino acid from C to G at position 268.
+The protein's natural variant, known as in PPRD;, features a modification of the amino acid from S to P at position 334.
+The protein's natural variant, known as in PPRD, features a modification of the amino acid from C to Y at position 337.
+The protein's natural variant, known as in PKD2;, features a modification of the amino acid from R to Q at position 306.
+The protein's natural variant, known as in PKD2;, features a modification of the amino acid from R to Q at position 322.
+The protein's natural variant, known as in PKD2;, features a modification of the amino acid from R to W at position 322.
+The protein's natural variant, known as in PKD2, features a modification of the amino acid from A to P at position 356.
+The protein's natural variant, known as in PKD2, features a modification of the amino acid from A to P at position 384.
+The protein's natural variant, known as in PKD2; affects channel activity as it is able to abolish channel currents induced by the gain-of-function artificial mutant P-604, features a modification of the amino acid from W to G at position 414.
+The protein's natural variant, known as in PKD2; affects channel activity as it is able to abolish channel currents induced by the gain-of-function artificial mutant P-604, features a modification of the amino acid from R to G at position 420.
+The protein's natural variant, known as in PKD2; loss of function in the release of Ca(2+) stores from the endoplasmic reticulum; no effect on location at the endoplasmic reticulum; affects channel activity as it is able to abolish channel currents induced by the gain-of-function artificial mutant P-604;, features a modification of the amino acid from D to V at position 511.
+The protein's natural variant, known as in PKD2, features a modification of the amino acid from C to R at position 632.
+The protein's natural variant, known as in PKD2;, features a modification of the amino acid from R to Q at position 807.
+The protein's natural variant, known as in 01F09, features a modification of the amino acid from N to D at position 85.
+The protein's natural variant, known as in 01F09, features a modification of the amino acid from N to D at position 107.
+The protein's natural variant, known as in 01F09, features a modification of the amino acid from N to D at position 129.
+The protein's natural variant, known as in 01F09, features a modification of the amino acid from N to D at position 140.
+The protein's natural variant, known as in PNPOD;, features a modification of the amino acid from R to H at position 225.
+The protein's natural variant, known as in PNPOD;, features a modification of the amino acid from R to Q at position 229.
+The protein's natural variant, known as in PNPOD; strong activity decrease;, features a modification of the amino acid from R to W at position 229.
+The protein's natural variant, known as in bm; activity abolished, features a modification of the amino acid from G to R at position 79.
+The natural variant of this protein is characterized by an amino acid alteration from R to K at position 109.
+The natural variant of this protein is characterized by an amino acid alteration from L to D at position 195.
+The natural variant of this protein is characterized by an amino acid alteration from D to L at position 207.
+The protein's natural variant, known as in an ovarian mucinous carcinoma sample; somatic mutation, features a modification of the amino acid from A to T at position 354.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from R to Q at position 503.
+The protein's natural variant, known as in plasmid pCP301, features a modification of the amino acid from K to R at position 110.
+The protein's natural variant, known as decreases arachidonate 5-lipoxygenase activity. Increases leukotriene A4 synthase activity;, features a modification of the amino acid from E to K at position 254.
+The protein's natural variant, known as decreases arachidonate 5-lipoxygenase activity, features a modification of the amino acid from P to S at position 337.
+The protein's natural variant, known as increases arachidonate 5-lipoxygenase activity, features a modification of the amino acid from A to S at position 447.
+The protein's natural variant, known as decreases arachidonate 5-lipoxygenase activity, features a modification of the amino acid from A to V at position 549.
+The protein's natural variant, known as does not affect arachidonate 5-lipoxygenase activity, features a modification of the amino acid from P to L at position 577.
+The protein's natural variant, known as increases arachidonate 5-lipoxygenase activity. Does not affect leukotriene A4 synthase activity, features a modification of the amino acid from T to M at position 591.
+The protein's natural variant, known as increases arachidonate 5-lipoxygenase activity, features a modification of the amino acid from K to Q at position 656.
+The natural variant of this protein is characterized by an amino acid alteration from T to R at position 41.
+The protein's natural variant, known as in ALYUS; decreased interaction with TAF1 and TBP shown by functional expression studies in a Drosophila cell line;, features a modification of the amino acid from R to C at position 46.
+The protein's natural variant, known as in ALYUS; decreased interaction with TAF1, TAF9 and TBP shown by functional expression studies in a Drosophila cell line;, features a modification of the amino acid from I to T at position 71.
+The protein's natural variant, known as in manganese-resistant mutant 2, features a modification of the amino acid from S to A at position 204.
+The protein's natural variant, known as in manganese-resistant mutant 1, features a modification of the amino acid from L to P at position 208.
+The protein's natural variant, known as in VCX1-D1, features a modification of the amino acid from M to I at position 383.
+The protein's natural variant, known as in strain: CCUG 17915L, features a modification of the amino acid from A to V at position 6.
+The protein's natural variant, known as in strain: CCUG 17915L, features a modification of the amino acid from YDA to FDG at position 35.
+The protein's natural variant, known as in strain: CCUG 17915L, features a modification of the amino acid from EII to DVV at position 46.
+The protein's natural variant, known as in strain: CCUG 17915L, features a modification of the amino acid from S to N at position 82.
+The protein's natural variant, known as in strain: CCUG 17915L, features a modification of the amino acid from T to I at position 88.
+The protein's natural variant, known as in strain: CCUG 17915L, features a modification of the amino acid from G to A at position 101.
+The protein's natural variant, known as in strain: CCUG 17915L, features a modification of the amino acid from ILG to VLA at position 108.
+The protein's natural variant, known as in strain: CCUG 17915L, features a modification of the amino acid from E to K at position 121.
+The protein's natural variant, known as in strain: CCUG 17915L, features a modification of the amino acid from GIIAAAH to NIIETVQ at position 134.
+The protein's natural variant, known as in strain: CCUG 17915L, features a modification of the amino acid from AKIT to GRIL at position 145.
+The protein's natural variant, known as in strain: CCUG 17915L, features a modification of the amino acid from AH to VK at position 151.
+The protein's natural variant, known as in strain: CCUG 17915L, features a modification of the amino acid from N to K at position 155.
+The protein's natural variant, known as in strain: CCUG 17915L, features a modification of the amino acid from G to D at position 158.
+The protein's natural variant, known as in strain: CCUG 17915L, features a modification of the amino acid from V to A at position 174.
+The protein's natural variant, known as in strain: CCUG 17915L, features a modification of the amino acid from SG to AE at position 196.
+The protein's natural variant, known as in strain: ATCC 7962 and NCDO 2054, features a modification of the amino acid from Q to H at position 95.
+The protein's natural variant, known as in strain: ATCC 7962 and NCDO 2054, features a modification of the amino acid from T to A at position 128.
+The protein's natural variant, known as in strain: ATCC 7962 and NCDO 2054, features a modification of the amino acid from K to R at position 435.
+The protein's natural variant, known as in FHCA1; affects the interaction with claudins;, features a modification of the amino acid from V to A at position 48.
+The protein's natural variant, known as in MPSVII, features a modification of the amino acid from E to K at position 351.
+The protein's natural variant, known as in strain: Qingyuan Ma, features a modification of the amino acid from T to P at position 5.
+The protein's natural variant, known as in strain: Xinghua, features a modification of the amino acid from A to G at position 17.
+The protein's natural variant, known as in strain: Taihe silkies, features a modification of the amino acid from L to F at position 23.
+The protein's natural variant, known as in strain: Taihe silkies, features a modification of the amino acid from K to R at position 41.
+The protein's natural variant, known as in IMD101; unknown pathological significance, features a modification of the amino acid from R to W at position 50.
+The protein's natural variant, known as in chylomicronemia syndrome, features a modification of the amino acid from R to G at position 435.
+The natural variant of this protein is characterized by an amino acid alteration from E to V at position 11.
+The protein's natural variant, known as frequency in African-Americans 0.008; not detected in Caucasian-Americans; enzyme activity is 31% of wild-type;, features a modification of the amino acid from R to W at position 173.
+The protein's natural variant, known as frequency in African-Americans 0.108 and Caucasian-Americans 0.100; enzyme activity is 350% of wild-type;, features a modification of the amino acid from M to T at position 287.
+The protein's natural variant, known as frequency in Caucasian-Americans 0.008; not detected in African-Americans;, features a modification of the amino acid from T to I at position 306.
+The protein's natural variant, known as in IMD46; increases protein expression; increases cell surface expression on T and B cells; increases soluble form level; impairs receptor internalization; impairs transferrin transport; impairs T and B cell proliferation as well as B cell class-switching; interacts with STEAP3; doesn't affect receptor internalization in erythroid precursor cells;, features a modification of the amino acid from Y to H at position 20.
+The protein's natural variant, known as found in a patient with congenital hydrocephalus; unknown pathological significance;, features a modification of the amino acid from R to Q at position 473.
+The protein's natural variant, known as in BRKS2;, features a modification of the amino acid from R to H at position 598.
+The protein's natural variant, known as in BRKS2; phenotype characterized by mild to severe osteogenesis imperfecta with or without postnatal contractures;, features a modification of the amino acid from G to C at position 601.
+The protein's natural variant, known as in BRKS2;, features a modification of the amino acid from G to V at position 601.
+The protein's natural variant, known as in BRKS2;, features a modification of the amino acid from T to I at position 608.
+The protein's natural variant, known as found in a patient with congenital hydrocephalus; unknown pathological significance;, features a modification of the amino acid from T to M at position 643.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from A to P at position 59.
+The protein's natural variant, known as in a lung large cell carcinoma sample; somatic mutation, features a modification of the amino acid from A to S at position 8.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation, features a modification of the amino acid from M to T at position 135.
+The protein's natural variant, known as in FCORD2; somatic mutation; unknown pathological significance;, features a modification of the amino acid from R to H at position 624.
+The protein's natural variant, known as found in a patient with focal epilepsy; unknown pathological significance;, features a modification of the amino acid from D to E at position 1376.
+The protein's natural variant, known as in FCORD2; somatic mutation, features a modification of the amino acid from Y to D at position 1450.
+The protein's natural variant, known as in FCORD2; somatic mutation;, features a modification of the amino acid from W to G at position 1456.
+The protein's natural variant, known as in FCORD2; somatic mutation; increased TOR signaling, features a modification of the amino acid from A to D at position 1459.
+The protein's natural variant, known as in FCORD2; somatic mutation, features a modification of the amino acid from A to S at position 1459.
+The protein's natural variant, known as in FCORD2; somatic mutation; increased TOR signaling;, features a modification of the amino acid from L to P at position 1460.
+The protein's natural variant, known as in FCORD2; somatic mutation; increased TOR signaling; increased kinase activity;, features a modification of the amino acid from C to R at position 1483.
+The protein's natural variant, known as in SKS, features a modification of the amino acid from W to R at position 1490.
+The protein's natural variant, known as in SKS;, features a modification of the amino acid from M to I at position 1595.
+The protein's natural variant, known as in FCORD2; somatic mutation; unknown pathological significance;, features a modification of the amino acid from R to H at position 1709.
+The protein's natural variant, known as in SKS; results in increased mTOR signaling;, features a modification of the amino acid from E to K at position 1799.
+The protein's natural variant, known as in SKS;, features a modification of the amino acid from A to T at position 1832.
+The protein's natural variant, known as in SKS;, features a modification of the amino acid from F to C at position 1888.
+The protein's natural variant, known as in FCORD2; somatic mutation;, features a modification of the amino acid from T to K at position 1977.
+The protein's natural variant, known as in an ovarian mucinous carcinoma sample; somatic mutation, features a modification of the amino acid from M to V at position 2011.
+The protein's natural variant, known as in FCORD2; somatic mutation, features a modification of the amino acid from R to C at position 2193.
+The protein's natural variant, known as in FCORD2; somatic mutation; increased TOR signaling;, features a modification of the amino acid from S to F at position 2215.
+The protein's natural variant, known as in FCORD2; also found in a colorectal adenocarcinoma sample; somatic mutation; increased TOR signaling;, features a modification of the amino acid from S to Y at position 2215.
+The protein's natural variant, known as found in a renal cell carcinoma sample; somatic mutation, features a modification of the amino acid from L to F at position 2220.
+The protein's natural variant, known as in SKS;, features a modification of the amino acid from M to I at position 2327.
+The protein's natural variant, known as found in a renal cell carcinoma sample; somatic mutation, features a modification of the amino acid from V to A at position 2406.
+The protein's natural variant, known as in FCORD2; somatic mutation; increased TOR signaling; increased kinase activity;, features a modification of the amino acid from L to P at position 2427.
+The protein's natural variant, known as in FCORD2; somatic mutation; increased TOR signaling; increased kinase activity;, features a modification of the amino acid from L to Q at position 2427.
+The protein's natural variant, known as in a glioblastoma multiforme sample; somatic mutation, features a modification of the amino acid from P to L at position 2476.
+The protein's natural variant, known as found in a patient with non-lesional nocturnal frontal epilepsy; unknown pathological significance;, features a modification of the amino acid from I to V at position 2501.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from C to Y at position 217.
+The protein's natural variant, known as in MCPH14; impairs the centriole-forming function of the protein;, features a modification of the amino acid from I to T at position 62.
+The protein's natural variant, known as in CMD1LL; unknown pathological significance;, features a modification of the amino acid from E to K at position 271.
+The protein's natural variant, known as in CMD1LL; unknown pathological significance;, features a modification of the amino acid from P to L at position 291.
+The protein's natural variant, known as in LVNC8;, features a modification of the amino acid from N to S at position 816.
+The protein's natural variant, known as in CMD1LL; unknown pathological significance;, features a modification of the amino acid from L to P at position 887.
+The protein's natural variant, known as in strain: Isolate MN 48041, features a modification of the amino acid from Y to D at position 104.
+The protein's natural variant, known as in strain: Isolate MN 48041, features a modification of the amino acid from K to E at position 217.
+The protein's natural variant, known as in HMSN6B; unknown pathological significance;, features a modification of the amino acid from L to R at position 138.
+The protein's natural variant, known as in PCH1E; loss of protein expression;, features a modification of the amino acid from T to I at position 142.
+The protein's natural variant, known as in HMSN6B; unknown pathological significance; no effect on protein abundance;, features a modification of the amino acid from G to D at position 249.
+The protein's natural variant, known as in HMSN6B; decreased protein abundance;, features a modification of the amino acid from P to L at position 333.
+The protein's natural variant, known as in HMSN6B; unknown pathological significance; slightly decreased protein abundance;, features a modification of the amino acid from E to D at position 335.
+The protein's natural variant, known as in HMSN6B; slightly decreased protein abundance;, features a modification of the amino acid from R to C at position 340.
+The protein's natural variant, known as in PCH1E; decreased protein abundance; loss of function in mitochondrial fission; no effect on localization to the mitochondrial outer membrane;, features a modification of the amino acid from L to P at position 341.
+The protein's natural variant, known as in SPG6;, features a modification of the amino acid from T to R at position 45.
+The protein's natural variant, known as in SPG6;, features a modification of the amino acid from G to R at position 106.
+The protein's natural variant, known as in strain: ATCC 200060 / W303, features a modification of the amino acid from P to R at position 614.
+The protein's natural variant, known as in strain: BALB/c, DBA/1 and DBA/2; enhances cytotoxicity, features a modification of the amino acid from T to A at position 184.
+The protein's natural variant, known as in strain: BALB/c, DBA/1 and DBA/2; enhances cytotoxicity, features a modification of the amino acid from E to G at position 218.
+The protein's natural variant, known as in gld; abolishes binding of FASL to its receptor, features a modification of the amino acid from F to L at position 273.
+The natural variant of this protein is characterized by an amino acid alteration from R to K at position 207.
+The protein's natural variant, known as in strain: Oregon-R, NVIII-1, NVIII-18, NVIII-2, NVIII-22, NVIII-24, NVIII-28, NVIII-41, NVIII-42, NVIII-46, NVIII-5, NVIII-9, NVIII-m11, NVIII-m12, NVIII-m13, NVIII-m15 and NVIII-m19, features a modification of the amino acid from D to G at position 170.
+The natural variant of this protein is characterized by an amino acid alteration from T to S at position 2.
+The protein's natural variant, known as in SPG30, features a modification of the amino acid from R to Q at position 11.
+The protein's natural variant, known as in SPG30, features a modification of the amino acid from R to W at position 11.
+The protein's natural variant, known as in KAND, features a modification of the amino acid from R to C at position 13.
+The protein's natural variant, known as in KAND; complete loss of motility, when tested in vitro;, features a modification of the amino acid from R to H at position 13.
+The protein's natural variant, known as in SPG30; unknown pathological significance, features a modification of the amino acid from M to T at position 30.
+The protein's natural variant, known as in KAND; unknown pathological significance, features a modification of the amino acid from Y to D at position 54.
+The protein's natural variant, known as in SPG30; unknown pathological significance, features a modification of the amino acid from Y to C at position 56.
+The protein's natural variant, known as in NESCAVS;, features a modification of the amino acid from S to L at position 58.
+The protein's natural variant, known as in SPG30;, features a modification of the amino acid from S to L at position 69.
+The protein's natural variant, known as in SPG30; unknown pathological significance, features a modification of the amino acid from Y to C at position 74.
+The protein's natural variant, known as in SPG30, features a modification of the amino acid from G to S at position 78.
+The protein's natural variant, known as in KAND; affects subcellular location; strong decrease in localization at the distal tip of neurites and accumulation in the neuronal cell body, when assayed in differentiated SH-SY5Y cells;, features a modification of the amino acid from Y to D at position 89.
+The protein's natural variant, known as in KAND; affects subcellular location, binding to microtubules and motility; contrary to wild-type, does not accumulate in the distal tips of differentiated SH-SY5Y cells, but localizes closer to the cell body in transfected cells; retains its ability to move processively along microtubules, but shows reduced velocity; may decrease interaction with microtubules, features a modification of the amino acid from C to R at position 92.
+The protein's natural variant, known as in NESCAVS; affects subcellular location; reduced distal localization and increased accumulation throughout the cell body and proximal neurites; disrupts microtubule motility;, features a modification of the amino acid from T to M at position 99.
+The protein's natural variant, known as in NESCAVS;, features a modification of the amino acid from G to D at position 102.
+The protein's natural variant, known as in SPG30; affects subcellular location; contrary to wild-type, does not accumulate in the distal tips of differentiated SH-SY5Y cells, but localizes closer to the cell body in transfected cells;, features a modification of the amino acid from G to S at position 102.
+The protein's natural variant, known as in KAND, features a modification of the amino acid from K to T at position 103.
+The protein's natural variant, known as in SPG30, features a modification of the amino acid from T to N at position 106.
+The protein's natural variant, known as in KAND; affects subcellular location; contrary to wild-type, does not accumulate in the distal tips of differentiated SH-SY5Y cells, but localizes closer to the cell body in transfected cells;, features a modification of the amino acid from G to V at position 117.
+The protein's natural variant, known as in NESCAVS;, features a modification of the amino acid from V to F at position 144.
+The protein's natural variant, known as in NESCAVS, features a modification of the amino acid from E to D at position 148.
+The protein's natural variant, known as in KAND, features a modification of the amino acid from E to K at position 148.
+The protein's natural variant, known as in KAND; unknown pathological significance, features a modification of the amino acid from C to Y at position 151.
+The protein's natural variant, known as in KAND; unknown pathological significance, features a modification of the amino acid from R to C at position 155.
+The protein's natural variant, known as in KAND, features a modification of the amino acid from D to V at position 156.
+The protein's natural variant, known as in KAND; unknown pathological significance, features a modification of the amino acid from L to H at position 157.
+The protein's natural variant, known as in NESCAVS and SPG30;, features a modification of the amino acid from R to C at position 167.
+The protein's natural variant, known as in SPG30, features a modification of the amino acid from R to H at position 167.
+The protein's natural variant, known as in KAND;, features a modification of the amino acid from H to P at position 171.
+The protein's natural variant, known as in SPG30, features a modification of the amino acid from L to P at position 173.
+The protein's natural variant, known as in KAND; unknown pathological significance;, features a modification of the amino acid from E to G at position 179.
+The protein's natural variant, known as in NESCAVS, features a modification of the amino acid from V to F at position 186.
+The protein's natural variant, known as in KAND, features a modification of the amino acid from G to E at position 199.
+The protein's natural variant, known as in NESCAVS, features a modification of the amino acid from G to R at position 199.
+The protein's natural variant, known as in NESCAVS; affects subcellular location; reduces accumulation in distal regions of the neurites;, features a modification of the amino acid from A to P at position 202.
+The protein's natural variant, known as in KAND, features a modification of the amino acid from R to S at position 203.
+The protein's natural variant, known as in KAND; unknown pathological significance;, features a modification of the amino acid from A to V at position 206.
+The protein's natural variant, known as in KAND; unknown pathological significance, features a modification of the amino acid from M to T at position 210.
+The protein's natural variant, known as in KAND; unknown pathological significance, features a modification of the amino acid from N to H at position 211.
+The protein's natural variant, known as in KAND, features a modification of the amino acid from S to N at position 214.
+The protein's natural variant, known as in NESCAVS; affects subcellular location; reduces accumulation in distal regions of the neurites;, features a modification of the amino acid from S to R at position 215.
+The protein's natural variant, known as in NESCAVS; disrupts microtubule motility;, features a modification of the amino acid from R to C at position 216.
+The protein's natural variant, known as in NESCAVS;, features a modification of the amino acid from R to H at position 216.
+The protein's natural variant, known as in NESCAVS; reduces accumulation in distal regions of the neurites;, features a modification of the amino acid from R to P at position 216.
+The protein's natural variant, known as in KAND; affects subcellular location; contrary to wild-type, does not accumulate in the distal tips of differentiated SH-SY5Y cells, but localizes closer to the cell body in transfected cells, features a modification of the amino acid from S to Y at position 217.
+The protein's natural variant, known as no effect on microtubule motility;, features a modification of the amino acid from V to I at position 220.
+The protein's natural variant, known as in KAND; unknown pathological significance;, features a modification of the amino acid from R to C at position 229.
+The protein's natural variant, known as in KAND, features a modification of the amino acid from V to M at position 247.
+The protein's natural variant, known as in KAND; affects subcellular location and motility; contrary to wild-type, does not accumulate in the distal tips of differentiated SH-SY5Y cells, but localizes closer to the cell body in transfected cells; retains its ability to move processively along microtubules, but shows a strongly reduced velocity, features a modification of the amino acid from D to E at position 248.
+The protein's natural variant, known as in KAND; affects subcellular location; contrary to wild-type, does not accumulate in the distal tips of differentiated SH-SY5Y cells, but localizes closer to the cell body in transfected cells, features a modification of the amino acid from D to G at position 248.
+The protein's natural variant, known as in NESCAVS;, features a modification of the amino acid from L to Q at position 249.
+The protein's natural variant, known as in KAND; affects subcellular location; contrary to wild-type, does not accumulate in the distal tips of differentiated SH-SY5Y cells, but localizes closer to the cell body in transfected cells; complete loss of motility, when tested in vitro, features a modification of the amino acid from G to R at position 251.
+The protein's natural variant, known as in SPG30, features a modification of the amino acid from S to R at position 252.
+The protein's natural variant, known as in NESCAVS; reduces accumulation in distal regions of the neurites; disrupts microtubule motility;, features a modification of the amino acid from E to K at position 253.
+The protein's natural variant, known as in KAND; affects subcellular location; contrary to wild-type, does not accumulate in the distal tips of differentiated SH-SY5Y cells, but localizes closer to the cell body in transfected cells, features a modification of the amino acid from R to P at position 254.
+The protein's natural variant, known as in NESCAVS; affects subcellular location; contrary to wild-type, does not accumulate in the distal tips of differentiated SH-SY5Y cells, but localizes closer to the cell body in transfected cells, features a modification of the amino acid from R to Q at position 254.
+The protein's natural variant, known as in NESCAVS; affects subcellular location, binding to microtubules and motility; contrary to wild-type, does not accumulate in the distal tips of differentiated SH-SY5Y cells, but localizes closer to the cell body in transfected cells; retains its ability to move processively along microtubules, but shows reduced velocity and processivity; increased interaction with microtubules, features a modification of the amino acid from R to W at position 254.
+The protein's natural variant, known as in SPG30; reduces accumulation in distal regions of the neurites; no effect on microtubule motility;, features a modification of the amino acid from A to V at position 255.
+The protein's natural variant, known as in SPG30, features a modification of the amino acid from T to M at position 258.
+The protein's natural variant, known as in KAND, features a modification of the amino acid from E to Q at position 267.
+The protein's natural variant, known as in KAND; unknown pathological significance;, features a modification of the amino acid from N to S at position 272.
+The protein's natural variant, known as in KAND; retains its ability to move processively along microtubules, but shows reduced velocity and processivity; decreased interaction with microtubules;, features a modification of the amino acid from S to L at position 274.
+The protein's natural variant, known as in KAND, features a modification of the amino acid from L to P at position 275.
+The protein's natural variant, known as in KAND; strong decrease in localization at the distal tip of neurites and accumulation in the neuronal cell body, when assayed in differentiated SH-SY5Y cells, features a modification of the amino acid from L to P at position 278.
+The protein's natural variant, known as in KAND, features a modification of the amino acid from G to D at position 279.
+The protein's natural variant, known as in KAND, features a modification of the amino acid from G to R at position 279.
+The protein's natural variant, known as in KAND, features a modification of the amino acid from K to R at position 280.
+The protein's natural variant, known as in SPG30; affects subcellular location, binding to microtubules and motility; contrary to wild-type, does not accumulate in the distal tips of differentiated SH-SY5Y cells, but localizes closer to the cell body in transfected cells; retains its ability to move processively along microtubules, but shows reduced velocity; small decrease of interaction with microtubules, features a modification of the amino acid from P to L at position 305.
+The protein's natural variant, known as in KAND, features a modification of the amino acid from Y to C at position 306.
+The protein's natural variant, known as in KAND, features a modification of the amino acid from R to G at position 307.
+The protein's natural variant, known as in NESCAVS; affects subcellular location; contrary to wild-type, does not accumulate in the distal tips of differentiated SH-SY5Y cells, but localizes closer to the cell body in transfected cells, features a modification of the amino acid from R to P at position 307.
+The protein's natural variant, known as in NESCAVS, features a modification of the amino acid from R to Q at position 307.
+The protein's natural variant, known as in KAND, features a modification of the amino acid from L to P at position 314.
+The protein's natural variant, known as in KAND;, features a modification of the amino acid from R to Q at position 316.
+The protein's natural variant, known as in NESCAVS; affects subcellular location, binding to microtubules and motility; contrary to wild-type, does not accumulate in the distal tips of differentiated SH-SY5Y cells, but localizes closer to the cell body in transfected cells; retains its ability to move processively along microtubules, but shows reduced velocity; small decrease of interaction with microtubules;, features a modification of the amino acid from R to W at position 316.
+The protein's natural variant, known as in NESCAVS, features a modification of the amino acid from S to P at position 323.
+The protein's natural variant, known as in KAND; affects subcellular location; contrary to wild-type, does not accumulate in the distal tips of differentiated SH-SY5Y cells, but localizes closer to the cell body in transfected cells, features a modification of the amino acid from T to M at position 344.
+The protein's natural variant, known as in SPG30; reduces accumulation in distal regions of the neurites;, features a modification of the amino acid from R to G at position 350.
+The protein's natural variant, known as in SPG30, features a modification of the amino acid from R to W at position 350.
+The protein's natural variant, known as in NESCAVS; unknown pathological significance, features a modification of the amino acid from R to W at position 380.
+The protein's natural variant, known as in SPG30; unknown pathological significance, features a modification of the amino acid from A to G at position 460.
+The protein's natural variant, known as in KAND, features a modification of the amino acid from A to D at position 475.
+The protein's natural variant, known as in SPG30; unknown pathological significance, features a modification of the amino acid from R to C at position 843.
+The protein's natural variant, known as in SPG30; unknown pathological significance, features a modification of the amino acid from N to K at position 859.
+The protein's natural variant, known as in SPG30; unknown pathological significance, features a modification of the amino acid from I to T at position 1026.
+The protein's natural variant, known as in strain: BG1, features a modification of the amino acid from M to I at position 103.
+The protein's natural variant, known as in strain: BG1, features a modification of the amino acid from V to M at position 235.
+The protein's natural variant, known as in CILD49; unknown pathological significance, features a modification of the amino acid from R to W at position 218.
+The protein's natural variant, known as in CILD49; unknown pathological significance, features a modification of the amino acid from G to D at position 328.
+The protein's natural variant, known as in CILD49; unknown pathological significance, features a modification of the amino acid from D to N at position 1178.
+The protein's natural variant, known as in CILD49; unknown pathological significance, features a modification of the amino acid from S to T at position 1444.
+The protein's natural variant, known as in strain: cv. Kas-1, cv. Kon and cv. Sorbo; confers sensitivity to the pathogenic biotrophic bacteria Xanthomonas campestris pv. campestris (Xcc), features a modification of the amino acid from S to F at position 211.
+The natural variant of this protein is characterized by an amino acid alteration from P to T at position 104.
+The natural variant of this protein is characterized by an amino acid alteration from I to N at position 106.
+The protein's natural variant, known as reduces serum myo-inositol concentration;, features a modification of the amino acid from V to A at position 182.
+The natural variant of this protein is characterized by an amino acid alteration from M to I at position 526.
+The protein's natural variant, known as in CORTRD1; no effect on protein abundance; decreased glucose-6-phosphate dehydrogenase activity, features a modification of the amino acid from P to L at position 146.
+The protein's natural variant, known as in CORTRD1; loss of glucose-6-phosphate dehydrogenase activity;, features a modification of the amino acid from G to D at position 359.
+The protein's natural variant, known as in CORTRD1; unknown pathological significance; no effect on glucose-6-phosphate dehydrogenase activity; however an effect was originally observed;, features a modification of the amino acid from R to Q at position 453.
+The protein's natural variant, known as in HFG, features a modification of the amino acid from A to AAAAAAA at position 125.
+The protein's natural variant, known as in HFG, features a modification of the amino acid from A to AAAAAAAAA at position 129.
+The protein's natural variant, known as in HFG; severe phenotype overlapping with Guttmacher syndrome, features a modification of the amino acid from I to F at position 368.
+The protein's natural variant, known as in GUTTS, features a modification of the amino acid from Q to L at position 371.
+The protein's natural variant, known as in HFG; severe;, features a modification of the amino acid from N to H at position 372.
+The protein's natural variant, known as in HFG, features a modification of the amino acid from V to F at position 375.
+The protein's natural variant, known as in GSD5;, features a modification of the amino acid from L to P at position 116.
+The protein's natural variant, known as in GSD5;, features a modification of the amino acid from R to W at position 194.
+The protein's natural variant, known as in GSD5;, features a modification of the amino acid from G to S at position 205.
+The protein's natural variant, known as in GSD5; rare mutation;, features a modification of the amino acid from L to P at position 292.
+The protein's natural variant, known as in GSD5, features a modification of the amino acid from E to K at position 349.
+The protein's natural variant, known as in GSD5;, features a modification of the amino acid from L to P at position 397.
+The protein's natural variant, known as in GSD5;, features a modification of the amino acid from T to N at position 488.
+The protein's natural variant, known as in GSD5;, features a modification of the amino acid from K to T at position 543.
+The protein's natural variant, known as in GSD5;, features a modification of the amino acid from R to W at position 602.
+The protein's natural variant, known as in GSD5;, features a modification of the amino acid from E to K at position 655.
+The protein's natural variant, known as in GSD5, features a modification of the amino acid from A to D at position 660.
+The protein's natural variant, known as in GSD5;, features a modification of the amino acid from Q to E at position 666.
+The protein's natural variant, known as in GSD5, features a modification of the amino acid from N to Y at position 685.
+The protein's natural variant, known as in GSD5;, features a modification of the amino acid from G to R at position 686.
+The protein's natural variant, known as in GSD5, features a modification of the amino acid from A to P at position 687.
+The protein's natural variant, known as in GSD5;, features a modification of the amino acid from A to V at position 704.
+The protein's natural variant, known as in GSD5;, features a modification of the amino acid from W to R at position 798.
+The protein's natural variant, known as in strain: Arzag, features a modification of the amino acid from S to N at position 221.
+The protein's natural variant, known as in NKH; loss of glycine catabolic process; loss of expression;, features a modification of the amino acid from T to K at position 146.
+The protein's natural variant, known as in NKH; loss of glycine catabolic process; decreased abundance, features a modification of the amino acid from L to P at position 173.
+The protein's natural variant, known as in NKH; decreased glycine catabolic process; changed localization to the mitochondria; also expressed diffusely throughout the cytosol; decreased abundance;, features a modification of the amino acid from P to A at position 267.
+The protein's natural variant, known as in NKH;, features a modification of the amino acid from A to P at position 283.
+The protein's natural variant, known as in one non-ketotic hyperglycinemia patient;, features a modification of the amino acid from P to T at position 329.
+The protein's natural variant, known as in NKH; decreased glycine catabolic process; decreased abundance;, features a modification of the amino acid from R to C at position 362.
+The protein's natural variant, known as in NKH; decreased glycine catabolic process; decreased abundance;, features a modification of the amino acid from R to W at position 373.
+The protein's natural variant, known as in NKH; decreased glycine catabolic process; decreased abundance;, features a modification of the amino acid from K to E at position 376.
+The protein's natural variant, known as in NKH; decreased glycine catabolic process; changed localization to the mitochondria; also expressed diffusely throughout the cytosol; decreased abundance;, features a modification of the amino acid from R to W at position 461.
+The protein's natural variant, known as in NKH;, features a modification of the amino acid from R to S at position 515.
+The protein's natural variant, known as in NKH; decreased GCSP-protein glycine exchange activity; no effect on abundance, features a modification of the amino acid from L to P at position 548.
+The protein's natural variant, known as in NKH; common mutation in Finland;, features a modification of the amino acid from S to I at position 564.
+The protein's natural variant, known as in NKH; loss of glycine catabolic process; loss of expression, features a modification of the amino acid from H to Y at position 580.
+The protein's natural variant, known as in NKH; loss of glycine catabolic process; decreased abundance;, features a modification of the amino acid from P to R at position 581.
+The protein's natural variant, known as in NKH; loss of GCSP-protein glycine exchange activity; no effect on abundance, features a modification of the amino acid from A to D at position 624.
+The protein's natural variant, known as in NKH; loss of GCSP-protein glycine exchange activity; no effect on abundance;, features a modification of the amino acid from G to D at position 763.
+The protein's natural variant, known as in NKH; loss of GCSP-protein glycine exchange activity; no effect on abundance, features a modification of the amino acid from G to E at position 768.
+The protein's natural variant, known as in NKH; decreased glycine catabolic process; decreased abundance;, features a modification of the amino acid from R to W at position 790.
+The protein's natural variant, known as in NKH, features a modification of the amino acid from Y to C at position 839.
+The protein's natural variant, known as in NKH; decreased glycine catabolic process; decreased abundance, features a modification of the amino acid from D to H at position 866.
+The protein's natural variant, known as in NKH; decreased GCSP-protein glycine exchange activity; no effect on abundance;, features a modification of the amino acid from V to G at position 905.
+The protein's natural variant, known as in NKH; decreased glycine catabolic process; decreased abundance;, features a modification of the amino acid from I to T at position 933.
+The protein's natural variant, known as in NKH; loss of glycine catabolic process; loss of expression;, features a modification of the amino acid from G to R at position 994.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from D to V at position 605.
+The protein's natural variant, known as probable disease-associated variant found in patients with atypical form of axonal peripheral neuropathy, characterized by acute or subacute onset and episodes of recurrent mononeuropathy;, features a modification of the amino acid from I to T at position 184.
+The protein's natural variant, known as in NPHS14; probable disease-associated variant also found in a patient with isolated primary adrenal insufficiency; decreased protein abundance; increased aggregation; decreased sphinganine-1-phosphate aldolase activity;, features a modification of the amino acid from R to Q at position 222.
+The protein's natural variant, known as in NPHS14;, features a modification of the amino acid from R to W at position 222.
+The protein's natural variant, known as in NPHS14; unknown pathological significance;, features a modification of the amino acid from R to W at position 340.
+The protein's natural variant, known as in NPHS1; decreased protein abundance in cells of patients homozygous for the mutation; increased aggregation; decreased sphinganine-1-phosphate aldolase activity;, features a modification of the amino acid from S to I at position 346.
+The protein's natural variant, known as in NPHS14; unknown pathological significance;, features a modification of the amino acid from Y to C at position 416.
+The protein's natural variant, known as in RP86; unknown pathological significance;, features a modification of the amino acid from H to Q at position 1562.
+The natural variant of this protein is characterized by an amino acid alteration from Y to H at position 148.
+The natural variant of this protein is characterized by an amino acid alteration from E to K at position 179.
+The natural variant of this protein is characterized by an amino acid alteration from V to A at position 222.
+The natural variant of this protein is characterized by an amino acid alteration from S to T at position 234.
+The natural variant of this protein is characterized by an amino acid alteration from E to Q at position 313.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from I to V at position 318.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from H to Y at position 110.
+The protein's natural variant, known as in strain: H4, features a modification of the amino acid from K to R at position 3.
+The protein's natural variant, known as in strain: H4, features a modification of the amino acid from F to L at position 19.
+The protein's natural variant, known as in strain: EGD-SmR / Serovar 1/2a, features a modification of the amino acid from T to A at position 51.
+The protein's natural variant, known as in strain: EGD-SmR / Serovar 1/2a, F4233 /Serotype 1/2b, F6789 / Serotype 1/2b, F5782 / Serotype 4b and H4, features a modification of the amino acid from V to L at position 94.
+The protein's natural variant, known as in strain: EGD-SmR / Serovar 1/2a, F4233 /Serotype 1/2b, F6789 / Serotype 1/2b, F5782 / Serotype 4b and H4, features a modification of the amino acid from N to D at position 118.
+The protein's natural variant, known as in strain: F5782 / Serotype 4b and H4, features a modification of the amino acid from T to S at position 142.
+The protein's natural variant, known as in strain: EGD-SmR / Serovar 1/2a, F4233 /Serotype 1/2b, F6789 / Serotype 1/2b and H4, features a modification of the amino acid from S to N at position 187.
+The protein's natural variant, known as in strain: F5782 / Serotype 4b, F4233 /Serotype 1/2b and F6789 / Serotype 1/2b, features a modification of the amino acid from F to L at position 193.
+The protein's natural variant, known as in strain: F4233 / Serotype 1/2b and F6789 /Serotype 1/2b, features a modification of the amino acid from L to W at position 253.
+The protein's natural variant, known as in strain: F4233 / Serotype 1/2b and F5782 /Serotype 4b, features a modification of the amino acid from S to P at position 292.
+The protein's natural variant, known as in strain: F6789 / Serotype 1/2b, features a modification of the amino acid from S to R at position 292.
+The protein's natural variant, known as in strain: H4, features a modification of the amino acid from N to S at position 321.
+The protein's natural variant, known as in strain: H4, features a modification of the amino acid from N to S at position 381.
+The protein's natural variant, known as in strain: F4233 / Serotype 1/2b, F6789 /Serotype 1/2b and F5782 / Serotype 4b, features a modification of the amino acid from A to E at position 416.
+The protein's natural variant, known as in strain: EGD-SmR / Serovar 1/2a and H4, features a modification of the amino acid from T to A at position 454.
+The protein's natural variant, known as in strain: H4, features a modification of the amino acid from S to N at position 474.
+The protein's natural variant, known as in strain: H4, features a modification of the amino acid from P to S at position 476.
+The protein's natural variant, known as in strain: EGD-SmR / Serovar 1/2a and H4, features a modification of the amino acid from V to A at position 500.
+The protein's natural variant, known as in strain: H4, features a modification of the amino acid from H to Y at position 530.
+The protein's natural variant, known as in strain: H4, features a modification of the amino acid from N to D at position 558.
+The protein's natural variant, known as in strain: EGD-SmR / Serovar 1/2a, features a modification of the amino acid from D to E at position 573.
+The protein's natural variant, known as in strain: EGD-SmR / Serovar 1/2a, features a modification of the amino acid from A to P at position 594.
+The protein's natural variant, known as in strain: H4, features a modification of the amino acid from S to T at position 648.
+The protein's natural variant, known as in strain: H4, features a modification of the amino acid from A to T at position 664.
+The protein's natural variant, known as in strain: H4, features a modification of the amino acid from P to S at position 729.
+The protein's natural variant, known as in strain: H4, features a modification of the amino acid from D to N at position 738.
+The protein's natural variant, known as in strain: H4, features a modification of the amino acid from L to I at position 781.
+The protein's natural variant, known as in strain: H4, features a modification of the amino acid from M to V at position 790.
+The protein's natural variant, known as in HYPP; found in a Quarter Horse lineage segregating the disease, features a modification of the amino acid from F to L at position 1416.
+The protein's natural variant, known as in strain: Isolate gulf of Mexico and Isolate Pacific ocean, features a modification of the amino acid from I to T at position 238.
+The protein's natural variant, known as in strain: Isolate gulf of Mexico, features a modification of the amino acid from T to A at position 246.
+The protein's natural variant, known as in strain: Isolate gulf of Mexico, features a modification of the amino acid from L to F at position 323.
+The protein's natural variant, known as in strain: Isolate Pacific ocean, features a modification of the amino acid from I to L at position 356.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from H to L at position 424.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from S to F at position 455.
+The protein's natural variant, known as in LESKRES; impairs shRNA-mediated silencing. Does not affect targeting to P-bodies. Increases binding to mRNA targets. Does not affect interaction with DICER1. Decreased phosphorylation of the C-terminal serine cluster. Does not affect phosphorylation of Ser-387, features a modification of the amino acid from L to P at position 192.
+The protein's natural variant, known as in LESKRES; impairs shRNA-mediated silencing. Does not affect targeting to P-bodies. Increases binding to mRNA targets. Does not affect interaction with DICER1. Decreased phosphorylation of the C-terminal serine cluster. Does not affect phosphorylation of Ser-387, features a modification of the amino acid from G to C at position 201.
+The protein's natural variant, known as in LESKRES, features a modification of the amino acid from G to V at position 201.
+The protein's natural variant, known as in LESKRES; impairs shRNA-mediated silencing. Does not affect targeting to P-bodies. Increases binding to mRNA targets. Does not affect interaction with DICER1. Does not affect phosphorylation of the C-terminal serine cluster. Does not affect phosphorylation of Ser-387, features a modification of the amino acid from H to Q at position 203.
+The protein's natural variant, known as in LESKRES, features a modification of the amino acid from T to M at position 357.
+The protein's natural variant, known as in LESKRES; impairs shRNA-mediated silencing. Does not affect targeting to P-bodies. Increases binding to mRNA targets. Does not affect interaction with DICER1. Decreased phosphorylation of the C-terminal serine cluster. Does not affect phosphorylation of Ser-387, features a modification of the amino acid from M to T at position 364.
+The protein's natural variant, known as in LESKRES; impairs shRNA-mediated silencing. Decreased phosphorylation of the C-terminal serine cluster. Increased binding to mRNA targets, features a modification of the amino acid from A to P at position 367.
+The protein's natural variant, known as in LESKRES, features a modification of the amino acid from G to S at position 573.
+The protein's natural variant, known as in LESKRES; complete loss of function. Changes in the subcellular location pattern. Diffuse location into the cytoplasm. Does not bind mRNA. Abolishes interaction with DICER1. Abolishes phosphorylation of the C-terminal serine cluster. Does not affect phosphorylation of Ser-387, features a modification of the amino acid from G to R at position 733.
+The protein's natural variant, known as in LESKRES, features a modification of the amino acid from C to Y at position 751.
+The protein's natural variant, known as in LESKRES; impairs shRNA-mediated silencing. Does not affect targeting to P-bodies. Increases binding to mRNA targets. Does not affect interaction with DICER1. Decreased phosphorylation of a C-terminal serine cluster. Does not affect phosphorylation of Ser-387, features a modification of the amino acid from S to R at position 760.
+The protein's natural variant, known as in strain: K1 / RS218, features a modification of the amino acid from L to I at position 6.
+The protein's natural variant, known as in strain: K1 / RS218, features a modification of the amino acid from L to M at position 20.
+The protein's natural variant, known as in strain: K1 / RS218, features a modification of the amino acid from P to S at position 27.
+The protein's natural variant, known as in strain: K1 / RS218, features a modification of the amino acid from Q to H at position 33.
+The protein's natural variant, known as in strain: K1 / RS218, features a modification of the amino acid from QN to RS at position 51.
+The protein's natural variant, known as in strain: K1 / RS218, features a modification of the amino acid from T to A at position 81.
+The protein's natural variant, known as in strain: K1 / RS218, features a modification of the amino acid from L to F at position 102.
+The protein's natural variant, known as in strain: K1 / RS218, features a modification of the amino acid from G to D at position 106.
+The protein's natural variant, known as in strain: K1 / RS218, features a modification of the amino acid from NT to DS at position 118.
+The protein's natural variant, known as in strain: K1 / RS218, features a modification of the amino acid from S to F at position 167.
+The protein's natural variant, known as in strain: K1 / RS218, features a modification of the amino acid from R to G at position 191.
+The protein's natural variant, known as in strain: K1 / RS218, features a modification of the amino acid from Q to R at position 232.
+The protein's natural variant, known as in strain: K1 / RS218, features a modification of the amino acid from S to P at position 273.
+The protein's natural variant, known as in strain: K1 / RS218, features a modification of the amino acid from G to GWQQ at position 457.
+The protein's natural variant, known as in strain: 71, features a modification of the amino acid from A to T at position 37.
+The protein's natural variant, known as in strain: 71, features a modification of the amino acid from I to V at position 297.
+The protein's natural variant, known as in strain: 71, features a modification of the amino acid from T to N at position 399.
+The protein's natural variant, known as associated with change in bone mineral density;, features a modification of the amino acid from L to P at position 447.
+The natural variant of this protein is characterized by an amino acid alteration from I to T at position 51.
+The protein's natural variant, known as in CPSQ3; decreased actin capping activity; increased fibroblast proliferation and migration; decreased colocalization with alpha subunit ADD1;, features a modification of the amino acid from G to D at position 367.
+The protein's natural variant, known as in MD, features a modification of the amino acid from H to R at position 674.
+The protein's natural variant, known as in MD, features a modification of the amino acid from S to P at position 1381.
+The natural variant of this protein is characterized by an amino acid alteration from F to L at position 109.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from A to T at position 457.
+The protein's natural variant, known as in ETL5; affects protein secretion presumably by altering protein folding or stability;, features a modification of the amino acid from G to R at position 267.
+The protein's natural variant, known as in FEB11; affects protein secretion presumably by altering protein folding or stability;, features a modification of the amino acid from A to V at position 270.
+The protein's natural variant, known as in MTHFRD; reduces methylenetetrahydrofolate reductase activity; no effect on affinity for NADPH;, features a modification of the amino acid from R to Q at position 46.
+The protein's natural variant, known as in MTHFRD; reduced methylenetetrahydrofolate reductase activity; no effect on affinity for NADPH;, features a modification of the amino acid from R to W at position 46.
+The protein's natural variant, known as in MTHFRD;, features a modification of the amino acid from R to P at position 51.
+The protein's natural variant, known as in MTHFRD; reduced methylenetetrahydrofolate reductase activity; reduced affinity for NADPH;, features a modification of the amino acid from R to Q at position 52.
+The protein's natural variant, known as in MTHFRD; loss of methylenetetrahydrofolate reductase activity;, features a modification of the amino acid from W to S at position 59.
+The protein's natural variant, known as in MTHFRD; reduced methylenetetrahydrofolate reductase activity; reduced affinity for NADPH;, features a modification of the amino acid from R to G at position 68.
+The protein's natural variant, known as in MTHFRD; reduced methylenetetrahydrofolate reductase activity; no effect on affinity for NADPH;, features a modification of the amino acid from R to W at position 82.
+The protein's natural variant, known as in MTHFRD; reduced methylenetetrahydrofolate reductase activity; no effect on affinity for NADPH;, features a modification of the amino acid from A to T at position 113.
+The protein's natural variant, known as in MTHFRD; loss of methylenetetrahydrofolate reductase activity;, features a modification of the amino acid from H to Y at position 127.
+The protein's natural variant, known as in MTHFRD; reduced methylenetetrahydrofolate reductase activity; reduced affinity for NADPH, features a modification of the amino acid from T to N at position 129.
+The protein's natural variant, known as in MTHFRD; reduced methylenetetrahydrofolate reductase activity; no effect on affinity for NADPH;, features a modification of the amino acid from C to R at position 130.
+The protein's natural variant, known as in MTHFRD; loss of methylenetetrahydrofolate reductase activity;, features a modification of the amino acid from Q to P at position 147.
+The protein's natural variant, known as in MTHFRD; loss of methylenetetrahydrofolate reductase activity, features a modification of the amino acid from G to V at position 149.
+The protein's natural variant, known as in MTHFRD; reduced methylenetetrahydrofolate reductase activity; no effect on affinity for NADPH;, features a modification of the amino acid from I to M at position 153.
+The protein's natural variant, known as in MTHFRD; reduced methylenetetrahydrofolate reductase activity; reduced affinity for NADPH;, features a modification of the amino acid from R to Q at position 157.
+The protein's natural variant, known as in MTHFRD; reduced methylenetetrahydrofolate reductase activity; reduced affinity for NADPH;, features a modification of the amino acid from A to T at position 175.
+The protein's natural variant, known as in MTHFRD; reduced methylenetetrahydrofolate reductase activity; no effect on affinity for NADPH;, features a modification of the amino acid from R to Q at position 183.
+The protein's natural variant, known as in MTHFRD; reduced methylenetetrahydrofolate reductase activity; reduced affinity for NADPH;, features a modification of the amino acid from A to V at position 195.
+The protein's natural variant, known as in MTHFRD; reduced methylenetetrahydrofolate reductase activity; reduced affinity for NADPH;, features a modification of the amino acid from G to D at position 196.
+The protein's natural variant, known as in MTHFRD; decreased affinity for FAD cofactor, features a modification of the amino acid from V to L at position 218.
+The protein's natural variant, known as at homozygosity reduces the risk for colorectal cancer in individuals with adequate folate status; decreased risk for adult acute leukemia; increased risk for NTDFS; increased risk for schizophrenia; thermolabile; decreased affinity for FAD cofactor; 50% reduced activity;, features a modification of the amino acid from A to V at position 222.
+The protein's natural variant, known as in MTHFRD; reduced methylenetetrahydrofolate reductase activity; no effect on affinity for NADPH;, features a modification of the amino acid from I to L at position 225.
+The protein's natural variant, known as in MTHFRD;, features a modification of the amino acid from T to M at position 227.
+The protein's natural variant, known as in MTHFRD, features a modification of the amino acid from P to L at position 251.
+The protein's natural variant, known as in MTHFRD; reduced methylenetetrahydrofolate reductase activity; reduced affinity for NADPH, features a modification of the amino acid from V to F at position 253.
+The protein's natural variant, known as in MTHFRD; reduced methylenetetrahydrofolate reductase activity; no effect on affinity for NADPH;, features a modification of the amino acid from P to S at position 254.
+The protein's natural variant, known as in MTHFRD; loss of methylenetetrahydrofolate reductase activity;, features a modification of the amino acid from G to V at position 255.
+The protein's natural variant, known as in MTHFRD; loss of methylenetetrahydrofolate reductase activity;, features a modification of the amino acid from I to N at position 256.
+The protein's natural variant, known as in MTHFRD; loss of methylenetetrahydrofolate reductase activity;, features a modification of the amino acid from F to V at position 257.
+The protein's natural variant, known as in MTHFRD;, features a modification of the amino acid from L to P at position 323.
+The protein's natural variant, known as in MTHFRD;, features a modification of the amino acid from N to S at position 324.
+The protein's natural variant, known as in MTHFRD;, features a modification of the amino acid from R to C at position 325.
+The protein's natural variant, known as in MTHFRD;, features a modification of the amino acid from R to C at position 335.
+The protein's natural variant, known as in MTHFRD; reduced methylenetetrahydrofolate reductase activity; no effect on affinity for NADPH;, features a modification of the amino acid from R to H at position 335.
+The protein's natural variant, known as in MTHFRD; loss of methylenetetrahydrofolate reductase activity;, features a modification of the amino acid from M to T at position 338.
+The protein's natural variant, known as in MTHFRD; loss of methylenetetrahydrofolate reductase activity;, features a modification of the amino acid from W to G at position 339.
+The protein's natural variant, known as in MTHFRD; reduced methylenetetrahydrofolate reductase activity; reduced affinity for NADPH;, features a modification of the amino acid from P to S at position 348.
+The protein's natural variant, known as in MTHFRD; reduced methylenetetrahydrofolate reductase activity; reduced affinity for NADPH;, features a modification of the amino acid from H to Y at position 354.
+The protein's natural variant, known as in MTHFRD;, features a modification of the amino acid from R to C at position 357.
+The protein's natural variant, known as in MTHFRD; reduced methylenetetrahydrofolate reductase activity; reduced affinity for NADPH;, features a modification of the amino acid from R to H at position 363.
+The protein's natural variant, known as in MTHFRD; reduced methylenetetrahydrofolate reductase activity; reduced affinity for NADPH;, features a modification of the amino acid from K to E at position 372.
+The protein's natural variant, known as in MTHFRD; reduced methylenetetrahydrofolate reductase activity; reduced affinity for NADPH;, features a modification of the amino acid from R to C at position 377.
+The protein's natural variant, known as in MTHFRD; reduced methylenetetrahydrofolate reductase activity; reduced affinity for NADPH;, features a modification of the amino acid from R to H at position 377.
+The protein's natural variant, known as in MTHFRD; reduced methylenetetrahydrofolate reductase activity; reduced affinity for NADPH;, features a modification of the amino acid from G to D at position 387.
+The protein's natural variant, known as in MTHFRD; reduced methylenetetrahydrofolate reductase activity; reduced affinity for NADPH;, features a modification of the amino acid from W to S at position 421.
+The protein's natural variant, known as decreased risk for adult acute leukemia; thermolabile; decreased activity;, features a modification of the amino acid from E to A at position 429.
+The protein's natural variant, known as in MTHFRD;, features a modification of the amino acid from F to S at position 435.
+The natural variant of this protein is characterized by an amino acid alteration from E to A at position 470.
+The protein's natural variant, known as in MTHFRD; reduced methylenetetrahydrofolate reductase activity; reduced affinity for NADPH;, features a modification of the amino acid from Y to D at position 506.
+The protein's natural variant, known as in MTHFRD; reduced methylenetetrahydrofolate reductase activity; reduced affinity for NADPH;, features a modification of the amino acid from V to F at position 536.
+The protein's natural variant, known as in MTHFRD; reduced methylenetetrahydrofolate reductase activity; reduced affinity for NADPH;, features a modification of the amino acid from P to L at position 572.
+The protein's natural variant, known as in MTHFRD; reduced methylenetetrahydrofolate reductase activity; reduced affinity for NADPH, features a modification of the amino acid from V to G at position 574.
+The protein's natural variant, known as in MTHFRD; reduced methylenetetrahydrofolate reductase activity; reduced affinity for NADPH;, features a modification of the amino acid from V to G at position 575.
+The protein's natural variant, known as in MTHFRD;, features a modification of the amino acid from E to K at position 586.
+The protein's natural variant, known as in MTHFRD; reduced methylenetetrahydrofolate reductase activity; reduced affinity for NADPH;, features a modification of the amino acid from L to P at position 598.
+The protein's natural variant, known as in MTHFRD; reduced methylenetetrahydrofolate reductase activity; reduced affinity for NADPH;, features a modification of the amino acid from L to P at position 628.
+The protein's natural variant, known as in strain: 85/2082, features a modification of the amino acid from A to T at position 135.
+The protein's natural variant, known as found in a patient with global developmental delay; unknown pathological significance, features a modification of the amino acid from R to Q at position 400.
+The protein's natural variant, known as in strain: 3153A, features a modification of the amino acid from K to N at position 687.
+The protein's natural variant, known as found in a patient with global developmental delay, spasticity and epilepsy; unknown pathological significance, features a modification of the amino acid from N to I at position 472.
+The protein's natural variant, known as in POF8 and SPGF61, features a modification of the amino acid from R to H at position 321.
+The protein's natural variant, known as in SPGF61, features a modification of the amino acid from L to R at position 421.
+The natural variant of this protein is characterized by an amino acid alteration from M to L at position 56.
+The natural variant of this protein is characterized by an amino acid alteration from R to K at position 59.
+The natural variant of this protein is characterized by an amino acid alteration from G to R at position 74.
+The protein's natural variant, known as in strain: CWL029 and TW-183, features a modification of the amino acid from V to A at position 354.
+The protein's natural variant, known as in Nv3-2, features a modification of the amino acid from K to N at position 5.
+The protein's natural variant, known as in Nv1-10, features a modification of the amino acid from V to A at position 9.
+The protein's natural variant, known as in Nv1-10 and Nv3-2, features a modification of the amino acid from F to Y at position 33.
+The protein's natural variant, known as in Nv3-2, features a modification of the amino acid from IP to FA at position 41.
+The protein's natural variant, known as in Nv3-2, features a modification of the amino acid from DGPDIR to PGIG at position 52.
+The protein's natural variant, known as in Nv1-10, features a modification of the amino acid from M to V at position 62.
+The protein's natural variant, known as in strain: cv. Onward, features a modification of the amino acid from L to I at position 59.
+The protein's natural variant, known as in strain: cv. Onward, features a modification of the amino acid from I to L at position 85.
+The protein's natural variant, known as in strain: CWL029 and TW-183, features a modification of the amino acid from I to T at position 372.
+The protein's natural variant, known as in SPG10; complicated form, features a modification of the amino acid from Y to C at position 63.
+The protein's natural variant, known as in SPG10; complicated form, features a modification of the amino acid from M to T at position 198.
+The protein's natural variant, known as in SPG10, features a modification of the amino acid from S to C at position 203.
+The protein's natural variant, known as in SPG10; complicated form;, features a modification of the amino acid from R to Q at position 204.
+The protein's natural variant, known as in SPG10; complicated form;, features a modification of the amino acid from E to K at position 251.
+The protein's natural variant, known as in SPG10; decreases microtubule affinity; reduces gliding velocity; reduces microtubule-dependent ATP turnover, features a modification of the amino acid from K to N at position 253.
+The protein's natural variant, known as in SPG10; slightly decreases microtubule affinity; reduces gliding velocity; reduces microtubule-dependent ATP turnover;, features a modification of the amino acid from N to S at position 256.
+The protein's natural variant, known as in SPG10; complicated form, features a modification of the amino acid from K to N at position 257.
+The protein's natural variant, known as in SPG10;, features a modification of the amino acid from Y to C at position 276.
+The protein's natural variant, known as in SPG10;, features a modification of the amino acid from R to C at position 280.
+The protein's natural variant, known as in SPG10; complicated form;, features a modification of the amino acid from R to H at position 280.
+The protein's natural variant, known as in SPG10; pure form, features a modification of the amino acid from R to L at position 280.
+The protein's natural variant, known as in SPG10; does not affect microtubule affinity; does not affect gliding velocity; does not affect microtubule-dependent ATP turnover;, features a modification of the amino acid from A to V at position 361.
+The protein's natural variant, known as in ALS25; unknown pathological significance;, features a modification of the amino acid from E to G at position 413.
+The protein's natural variant, known as in ALS25; unknown pathological significance;, features a modification of the amino acid from Q to H at position 474.
+The protein's natural variant, known as in ALS25; unknown pathological significance;, features a modification of the amino acid from S to G at position 577.
+The protein's natural variant, known as in ALS25; unknown pathological significance;, features a modification of the amino acid from P to L at position 986.
+The protein's natural variant, known as in ALS25;, features a modification of the amino acid from R to G at position 1007.
+The protein's natural variant, known as in allele HP*1F;, features a modification of the amino acid from N to D at position 129.
+The protein's natural variant, known as in allele HP*1F;, features a modification of the amino acid from E to K at position 130.
+The protein's natural variant, known as in AHP; causes reduced expression of the protein;, features a modification of the amino acid from I to T at position 247.
+The protein's natural variant, known as in strain: RC101, features a modification of the amino acid from S to R at position 68.
+The protein's natural variant, known as in strain: RC101, features a modification of the amino acid from T to A at position 154.
+The natural variant of this protein is characterized by an amino acid alteration from N to T at position 7.
+The natural variant of this protein is characterized by an amino acid alteration from D to N at position 63.
+The natural variant of this protein is characterized by an amino acid alteration from L to V at position 179.
+The natural variant of this protein is characterized by an amino acid alteration from N to D at position 234.
+The natural variant of this protein is characterized by an amino acid alteration from NN to KS at position 311.
+The natural variant of this protein is characterized by an amino acid alteration from A to D at position 333.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from K to I at position 275.
+The protein's natural variant, known as in CMS15; results in a severe reduction in protein expression; loss of function mutation;, features a modification of the amino acid from P to L at position 65.
+The protein's natural variant, known as in MEPCA;, features a modification of the amino acid from D to N at position 74.
+The protein's natural variant, known as in MEPCA; unknown pathological significance;, features a modification of the amino acid from R to Q at position 109.
+The protein's natural variant, known as in MEPCA; unknown pathological significance;, features a modification of the amino acid from V to G at position 141.
+The protein's natural variant, known as higher fasting circulating triglyceride levels;, features a modification of the amino acid from T to A at position 532.
+The protein's natural variant, known as higher fasting circulating triglyceride levels;, features a modification of the amino acid from I to V at position 606.
+The natural variant of this protein is characterized by an amino acid alteration from D to N at position 106.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from A to V at position 220.
+The natural variant of this protein is characterized by an amino acid alteration from V to A at position 318.
+The protein's natural variant, known as in strain: Isolate JEW38, features a modification of the amino acid from W to G at position 184.
+The protein's natural variant, known as in an ovarian undifferentiated carcinoma sample; somatic mutation, features a modification of the amino acid from E to K at position 942.
+The protein's natural variant, known as in a melanoma metastatic sample; somatic mutation, features a modification of the amino acid from K to T at position 1476.
+The protein's natural variant, known as rare variant found in East Asian patients; decreases luminal apoptosis, cell aggregation and basolateral membrane localization in colorectal cancer cells;, features a modification of the amino acid from Q to E at position 1853.
+The protein's natural variant, known as resistance to EMB, features a modification of the amino acid from N to D at position 394.
+The protein's natural variant, known as resistance to EMB, features a modification of the amino acid from R to Q at position 738.
+The protein's natural variant, known as in a cutaneous metastatic melanoma sample; somatic mutation;, features a modification of the amino acid from P to S at position 14.
+The protein's natural variant, known as in a cutaneous metastatic melanoma sample; somatic mutation;, features a modification of the amino acid from R to C at position 31.
+The protein's natural variant, known as in a cutaneous metastatic melanoma sample; somatic mutation;, features a modification of the amino acid from P to S at position 36.
+The protein's natural variant, known as in a cutaneous metastatic melanoma sample; somatic mutation;, features a modification of the amino acid from H to Y at position 106.
+The protein's natural variant, known as detected in a melanoma cell line, features a modification of the amino acid from L to P at position 173.
+The protein's natural variant, known as in a cutaneous metastatic melanoma sample; somatic mutation, features a modification of the amino acid from V to A at position 180.
+The protein's natural variant, known as in a cutaneous metastatic melanoma sample; somatic mutation; does not affect cell growth but conferes reduced cell adhesion to laminin-1, features a modification of the amino acid from H to Y at position 243.
+The protein's natural variant, known as in a cutaneous metastatic melanoma sample; somatic mutation, features a modification of the amino acid from G to E at position 302.
+The protein's natural variant, known as in a cutaneous metastatic melanoma sample; somatic mutation; does not affect cell growth but conferes reduced cell adhesion to collagen IV;, features a modification of the amino acid from M to I at position 359.
+The protein's natural variant, known as in a cutaneous metastatic melanoma sample; somatic mutation;, features a modification of the amino acid from G to E at position 533.
+The protein's natural variant, known as detected in a melanoma cell line, features a modification of the amino acid from F to L at position 593.
+The protein's natural variant, known as in a cutaneous metastatic melanoma sample; somatic mutation; does not affect cell growth but conferes reduced cell adhesion to collagen IV and laminin-1; increases cell migration capabilities compared to wild-type;, features a modification of the amino acid from E to K at position 639.
+The protein's natural variant, known as in a cutaneous metastatic melanoma sample; somatic mutation; does not affect cell growth but conferes reduced cell adhesion to collagen IV and laminin-1; increases cell migration capabilities compared to wild-type, features a modification of the amino acid from S to N at position 703.
+The protein's natural variant, known as found in a patient with Rett syndrome-like phenotype; unknown pathological significance;, features a modification of the amino acid from R to W at position 146.
+The protein's natural variant, known as found in a family with Stocco dos Santos-type X-linked syndromic intellectual developmental disorder; unknown pathological significance;, features a modification of the amino acid from S to L at position 1089.
+The protein's natural variant, known as in RP76; no effect on protein abundance; reduced acetylglucosaminyltransferase activity;, features a modification of the amino acid from L to R at position 120.
+The protein's natural variant, known as in RP76; reduced acetylglucosaminyltransferase activity;, features a modification of the amino acid from E to K at position 156.
+The protein's natural variant, known as in MDDGA3;, features a modification of the amino acid from T to P at position 176.
+The protein's natural variant, known as in MDDGA3;, features a modification of the amino acid from S to R at position 198.
+The protein's natural variant, known as in MDDGA3; specific activity abolished in the membrane bound form but not the soluble form;, features a modification of the amino acid from E to K at position 223.
+The protein's natural variant, known as in MDDGA3; found on the same allele as Q-311; unknown pathological significance;, features a modification of the amino acid from R to H at position 265.
+The protein's natural variant, known as in MDDGA3; specific activity abolished of the membrane bound form but not the soluble form;, features a modification of the amino acid from C to Y at position 269.
+The protein's natural variant, known as in RP76; reduced acetylglucosaminyltransferase activity;, features a modification of the amino acid from I to S at position 287.
+The protein's natural variant, known as in MDDGA3 and MDDGB3;, features a modification of the amino acid from R to Q at position 311.
+The protein's natural variant, known as in MDDGA3;, features a modification of the amino acid from R to H at position 367.
+The protein's natural variant, known as in MDDGA3;, features a modification of the amino acid from W to S at position 425.
+The protein's natural variant, known as in MDDGA3, features a modification of the amino acid from D to H at position 427.
+The protein's natural variant, known as in MDDGA3;, features a modification of the amino acid from R to C at position 442.
+The protein's natural variant, known as in MDDGA3 and MDDGB3;, features a modification of the amino acid from C to Y at position 490.
+The protein's natural variant, known as in MDDGA3; specific activity abolished;, features a modification of the amino acid from P to R at position 493.
+The protein's natural variant, known as in RP76;, features a modification of the amino acid from G to A at position 502.
+The protein's natural variant, known as in MDDGA3;, features a modification of the amino acid from S to N at position 550.
+The protein's natural variant, known as in MDDGC3; normal enzyme activity but altered kinetic properties;, features a modification of the amino acid from D to N at position 556.
+The protein's natural variant, known as in MDDGB3;, features a modification of the amino acid from R to P at position 605.
+The protein's natural variant, known as in NEDMAS; impaired serine-activation of enzyme resulting in a significant decrease in the first step of the aminoacylation reaction; reduced protein stability; reduced protein expression;, features a modification of the amino acid from D to N at position 172.
+The protein's natural variant, known as in NEDMAS; reduced protein stability resulting in a significant decrease in cellular enzyme activity, features a modification of the amino acid from R to L at position 213.
+The protein's natural variant, known as in strain: Mae/Stm, features a modification of the amino acid from S to W at position 14.
+The protein's natural variant, known as in strain: MSM/Ms, features a modification of the amino acid from A to T at position 19.
+The protein's natural variant, known as in strain: Mae/Stm, features a modification of the amino acid from A to E at position 60.
+The protein's natural variant, known as in strain: MSM/Ms, features a modification of the amino acid from Q to R at position 118.
+The protein's natural variant, known as in strain: Mae/Stm, features a modification of the amino acid from N to K at position 160.
+The protein's natural variant, known as in strain: Mae/Stm and MSM/Ms, features a modification of the amino acid from E to K at position 449.
+The protein's natural variant, known as in strain: Mae/Stm and MSM/Ms, features a modification of the amino acid from S to R at position 497.
+The protein's natural variant, known as in strain: Mae/Stm and MSM/Ms, features a modification of the amino acid from R to H at position 503.
+The protein's natural variant, known as in strain: Mae/Stm, features a modification of the amino acid from H to Q at position 564.
+The protein's natural variant, known as in strain: MSM/Ms, features a modification of the amino acid from N to S at position 569.
+The protein's natural variant, known as in strain: Mae/Stm and MSM/Ms, features a modification of the amino acid from S to N at position 577.
+The natural variant of this protein is characterized by an amino acid alteration from P to S at position 42.
+The natural variant of this protein is characterized by an amino acid alteration from H to R at position 119.
+The natural variant of this protein is characterized by an amino acid alteration from R to S at position 246.
+The natural variant of this protein is characterized by an amino acid alteration from P to L at position 256.
+The natural variant of this protein is characterized by an amino acid alteration from P to A at position 261.
+The natural variant of this protein is characterized by an amino acid alteration from L to P at position 1105.
+The natural variant of this protein is characterized by an amino acid alteration from K to M at position 2180.
+The protein's natural variant, known as in CDSP; unknown pathological significance; reduces carnitine transport but the mutant retains 50% of wild-type activity;, features a modification of the amino acid from G to S at position 12.
+The protein's natural variant, known as in CDSP; carnitine transport reduced to less than 20% of wild-type;, features a modification of the amino acid from G to W at position 15.
+The protein's natural variant, known as in CDSP; loss of carnitine transport, features a modification of the amino acid from P to L at position 16.
+The protein's natural variant, known as in CDSP; carnitine transport reduced to less than 20% of wild-type;, features a modification of the amino acid from F to L at position 17.
+The protein's natural variant, known as in CDSP; carnitine transport is reduced to less than 5% of normal;, features a modification of the amino acid from R to P at position 19.
+The protein's natural variant, known as in CDSP; unknown pathological significance; reduces carnitine transport but the mutant retains 50% of wild-type activity;, features a modification of the amino acid from L to H at position 20.
+The protein's natural variant, known as in CDSP; carnitine transport reduced to less than 6% of wild-type;, features a modification of the amino acid from S to N at position 26.
+The protein's natural variant, known as in CDSP; carnitine transport reduced to 1% of wild-type;, features a modification of the amino acid from S to I at position 28.
+The protein's natural variant, known as in CDSP; carnitine transport reduced to less than 1% of wild-type;, features a modification of the amino acid from N to S at position 32.
+The protein's natural variant, known as in CDSP; carnitine transport reduced to less than 10% of wild-type;, features a modification of the amino acid from A to V at position 44.
+The protein's natural variant, known as in CDSP; carnitine transport reduced to less than 5% of wild-type;, features a modification of the amino acid from P to L at position 46.
+The protein's natural variant, known as in CDSP; carnitine transport is reduced to less than 5% of normal;, features a modification of the amino acid from P to S at position 46.
+The protein's natural variant, known as in CDSP; loss of carnitine transport, features a modification of the amino acid from C to Y at position 50.
+The protein's natural variant, known as in CDSP; carnitine transport reduced to 2% of wild-type, features a modification of the amino acid from T to P at position 66.
+The protein's natural variant, known as in CDSP; carnitine transport reduced to 2% of wild-type;, features a modification of the amino acid from R to P at position 75.
+The protein's natural variant, known as in CDSP; loss of carnitine transport;, features a modification of the amino acid from R to L at position 83.
+The protein's natural variant, known as in CDSP; loss of carnitine transport;, features a modification of the amino acid from S to W at position 93.
+The protein's natural variant, known as in CDSP; unknown pathological significance; reduces carnitine transport but the mutant retains 30% of wild-type activity;, features a modification of the amino acid from L to V at position 95.
+The protein's natural variant, known as in CDSP; carnitine transport reduced to 20% of wild-type;, features a modification of the amino acid from G to A at position 96.
+The protein's natural variant, known as in CDSP; carnitine transport reduced to less than 5% of wild-type;, features a modification of the amino acid from D to G at position 115.
+The protein's natural variant, known as in CDSP;, features a modification of the amino acid from D to Y at position 122.
+The protein's natural variant, known as in CDSP; carnitine transport reduced to less than 20% of wild-type;, features a modification of the amino acid from V to G at position 123.
+The protein's natural variant, known as in CDSP; may affect splicing; unknown pathological significance; reduces carnitine transport but the mutant retains 30% of wild-type activity, features a modification of the amino acid from E to D at position 131.
+The protein's natural variant, known as in CDSP; unknown pathological significance; reduces carnitine transport but the mutant retains more than 25% of wild-type activity;, features a modification of the amino acid from A to S at position 142.
+The protein's natural variant, known as in CDSP; carnitine transport reduced to less than 2% of wild-type;, features a modification of the amino acid from P to L at position 143.
+The protein's natural variant, known as in CDSP; unknown pathological significance; reduces carnitine transport but the mutant retains more than 60% of wild-type activity;, features a modification of the amino acid from V to M at position 151.
+The protein's natural variant, known as in CDSP; loss of carnitine transport, features a modification of the amino acid from R to P at position 169.
+The protein's natural variant, known as in CDSP; loss of carnitine transport;, features a modification of the amino acid from R to Q at position 169.
+The protein's natural variant, known as in CDSP; loss of carnitine transport;, features a modification of the amino acid from R to W at position 169.
+The protein's natural variant, known as in CDSP; carnitine transport reduced to less than 10% of wild-type;, features a modification of the amino acid from V to M at position 175.
+The protein's natural variant, known as in CDSP; carnitine transport reduced to less than 20% of wild-type;, features a modification of the amino acid from M to V at position 177.
+The protein's natural variant, known as in CDSP; unknown pathological significance; reduces carnitine transport but the mutant retains more than 40% of wild-type activity;, features a modification of the amino acid from M to L at position 179.
+The protein's natural variant, known as in CDSP; loss of carnitine transport;, features a modification of the amino acid from L to P at position 186.
+The protein's natural variant, known as in CDSP; loss of carnitine transport;, features a modification of the amino acid from M to R at position 205.
+The protein's natural variant, known as in CDSP; loss of carnitine transport;, features a modification of the amino acid from N to S at position 210.
+The protein's natural variant, known as in CDSP; loss of carnitine transport;, features a modification of the amino acid from Y to C at position 211.
+The protein's natural variant, known as in CDSP; unknown pathological significance; reduces carnitine transport but the mutant retains 30% of wild-type activity;, features a modification of the amino acid from A to V at position 214.
+The protein's natural variant, known as in CDSP; unknown pathological significance; reduces carnitine transport but the mutant retains 30% of wild-type activity, features a modification of the amino acid from T to K at position 219.
+The protein's natural variant, known as in CDSP; reduces carnitine transport to less than 20% of wild-type activity;, features a modification of the amino acid from S to L at position 225.
+The protein's natural variant, known as in CDSP; reduces carnitine transport to less than 10% of wild-type activity;, features a modification of the amino acid from R to H at position 227.
+The protein's natural variant, known as in CDSP; reduces carnitine transport to less than 1% of wild-type activity;, features a modification of the amino acid from F to L at position 230.
+The protein's natural variant, known as in CDSP; loss of carnitine transport;, features a modification of the amino acid from S to F at position 231.
+The protein's natural variant, known as in CDSP; reduces carnitine transport to less than 20% of wild-type activity;, features a modification of the amino acid from T to M at position 232.
+The protein's natural variant, known as in CDSP;, features a modification of the amino acid from G to R at position 234.
+The protein's natural variant, known as in CDSP; reduces carnitine transport to less than 2% of wild-type activity, features a modification of the amino acid from A to T at position 240.
+The protein's natural variant, known as in CDSP; loss of carnitine transport;, features a modification of the amino acid from G to V at position 242.
+The protein's natural variant, known as in CDSP; loss of carnitine transport, features a modification of the amino acid from P to R at position 247.
+The protein's natural variant, known as in CDSP; unknown pathological significance; reduces carnitine transport but the mutant retains more than 30% of wild-type activity;, features a modification of the amino acid from R to Q at position 254.
+The protein's natural variant, known as in CDSP; reduces carnitine transport to less than 10% of wild-type activity;, features a modification of the amino acid from R to W at position 257.
+The protein's natural variant, known as in CDSP; unknown pathological significance; reduces carnitine transport but the mutant retains more than 40% of wild-type activity;, features a modification of the amino acid from T to M at position 264.
+The protein's natural variant, known as in CDSP; reduces carnitine transport to less than 5% of wild-type activity;, features a modification of the amino acid from T to R at position 264.
+The protein's natural variant, known as in CDSP; unknown pathological significance; reduces carnitine transport but the mutant retains more than 40% of wild-type activity, features a modification of the amino acid from L to P at position 269.
+The protein's natural variant, known as in CDSP; reduces carnitine transport to less than 1% of wild-type activity;, features a modification of the amino acid from S to F at position 280.
+The protein's natural variant, known as in CDSP; reduces carnitine transport to 5% of wild-type activity;, features a modification of the amino acid from R to Q at position 282.
+The protein's natural variant, known as in CDSP; loss of carnitine transport;, features a modification of the amino acid from W to C at position 283.
+The protein's natural variant, known as in CDSP; reduces carnitine transport to less than 1% of wild-type activity;, features a modification of the amino acid from W to R at position 283.
+The protein's natural variant, known as in CDSP; reduces carnitine transport to less-than-1% to 3% of wild-type activity;, features a modification of the amino acid from A to D at position 301.
+The protein's natural variant, known as in CDSP; unknown pathological significance; reduces carnitine transport but the mutant retains 70% of wild-type activity;, features a modification of the amino acid from I to V at position 312.
+The protein's natural variant, known as in CDSP; unknown pathological significance; no effect on carnitine transport;, features a modification of the amino acid from E to K at position 317.
+The protein's natural variant, known as in CDSP; unknown pathological significance; reduces carnitine transport but the mutant retains 60% of wild-type activity;, features a modification of the amino acid from I to T at position 348.
+The protein's natural variant, known as in CDSP; loss of carnitine transport;, features a modification of the amino acid from W to R at position 351.
+The protein's natural variant, known as in CDSP; reduces carnitine transport to less than 2% of wild-type activity;, features a modification of the amino acid from S to L at position 355.
+The protein's natural variant, known as in CDSP; loss of carnitine transport;, features a modification of the amino acid from Y to N at position 358.
+The protein's natural variant, known as in CDSP;, features a modification of the amino acid from S to L at position 362.
+The protein's natural variant, known as in CDSP; loss of carnitine transport;, features a modification of the amino acid from L to P at position 363.
+The protein's natural variant, known as in CDSP; reduces carnitine transport to less than 1% of wild-type activity;, features a modification of the amino acid from P to L at position 398.
+The protein's natural variant, known as in CDSP; carnitine transport is reduced to less than 1% of normal;, features a modification of the amino acid from R to Q at position 399.
+The protein's natural variant, known as in CDSP; reduces carnitine transport to less than 5% of wild-type activity;, features a modification of the amino acid from R to W at position 399.
+The protein's natural variant, known as in CDSP; unknown pathological significance; no effect on carnitine transport, features a modification of the amino acid from S to G at position 412.
+The protein's natural variant, known as in CDSP; reduces carnitine transport to less than 1% of wild-type activity, features a modification of the amino acid from V to G at position 439.
+The protein's natural variant, known as in CDSP; loss of carnitine transport;, features a modification of the amino acid from T to M at position 440.
+The protein's natural variant, known as in CDSP; requires 2 nucleotide substitutions; reduces carnitine transport to less than 20% of wild-type activity;, features a modification of the amino acid from A to I at position 442.
+The protein's natural variant, known as in CDSP; reduces carnitine transport to less than 1% of wild-type, features a modification of the amino acid from F to V at position 443.
+The protein's natural variant, known as in CDSP; reduces carnitine transport to less than 1% of wild-type;, features a modification of the amino acid from V to F at position 446.
+The protein's natural variant, known as in CDSP; loss of carnitine transport;, features a modification of the amino acid from Y to C at position 447.
+The protein's natural variant, known as in CDSP; reduces carnitine transport to less than 20% of wild-type;, features a modification of the amino acid from V to L at position 448.
+The protein's natural variant, known as in CDSP; unknown pathological significance; reduces carnitine transport to less than 20% of wild-type;, features a modification of the amino acid from Y to D at position 449.
+The protein's natural variant, known as in CDSP; reduces carnitine transport to less than 5% of wild-type;, features a modification of the amino acid from E to K at position 452.
+The protein's natural variant, known as in CDSP; loss of carnitine transport;, features a modification of the amino acid from P to R at position 455.
+The protein's natural variant, known as in CDSP; reduces carnitine transport to less than 5% of wild-type, features a modification of the amino acid from G to V at position 462.
+The protein's natural variant, known as in CDSP; reduces carnitine transport to less than 20% of wild-type activity;, features a modification of the amino acid from S to C at position 467.
+The protein's natural variant, known as in CDSP; markedly reduced carnitine transport compared to the wild-type protein; less than 1% of wild-type activity;, features a modification of the amino acid from T to R at position 468.
+The protein's natural variant, known as in CDSP; loss of carnitine transport;, features a modification of the amino acid from S to F at position 470.
+The protein's natural variant, known as in CDSP;, features a modification of the amino acid from R to C at position 471.
+The protein's natural variant, known as in CDSP; reduces carnitine transport to less than 2% of wild-type;, features a modification of the amino acid from R to H at position 471.
+The protein's natural variant, known as in CDSP; loss of carnitine transport, features a modification of the amino acid from R to P at position 471.
+The protein's natural variant, known as in CDSP; loss of carnitine transport, features a modification of the amino acid from L to R at position 476.
+The protein's natural variant, known as in CDSP; loss of carnitine transport but stimulated organic cation transport; no effect on protein expression;, features a modification of the amino acid from P to L at position 478.
+The protein's natural variant, known as reduces carnitine transport but the mutant retains more than 60% of wild-type activity;, features a modification of the amino acid from V to F at position 481.
+The protein's natural variant, known as in CDSP; reduces carnitine transport to less than 10% of wild-type;, features a modification of the amino acid from R to C at position 488.
+The protein's natural variant, known as in CDSP; unknown pathological significance; reduces carnitine transport to 40% of wild-type;, features a modification of the amino acid from R to H at position 488.
+The protein's natural variant, known as in CDSP; reduces carnitine transport to 5% of wild-type;, features a modification of the amino acid from L to S at position 507.
+The protein's natural variant, known as reduces carnitine transport but the mutant retains more than 20% of wild-type activity;, features a modification of the amino acid from P to S at position 549.
+The protein's natural variant, known as impaired phosphoenolpyruvate carboxykinase activity, leading to reduced intramuscular fat content, enhanced backfat thickness and lower meat quality, features a modification of the amino acid from M to L at position 139.
+The protein's natural variant, known as in OPA13; may impair dimerization and tetramerization, features a modification of the amino acid from R to Q at position 38.
+The protein's natural variant, known as in OPA13; reduced ability to stimulate POLG-dependent DNA synthesis in vitro, features a modification of the amino acid from G to V at position 40.
+The protein's natural variant, known as in OPA13; reduced ability to stimulate POLG-dependent DNA synthesis in vitro, features a modification of the amino acid from N to D at position 62.
+The protein's natural variant, known as in OPA13; reduced ability to stimulate POLG-dependent DNA synthesis in vitro, features a modification of the amino acid from R to Q at position 107.
+The protein's natural variant, known as in OPA13; reduced ability to stimulate POLG-dependent DNA synthesis in vitro, features a modification of the amino acid from E to Q at position 111.
+The protein's natural variant, known as found in a patient with a systemic mitochondrial disorder; unknown pathological significance; impaired multimerization; reduced ability to stimulate POLG-dependent DNA synthesis in vitro; mtDNA depletion without any detectable energetic defects;, features a modification of the amino acid from I to V at position 132.
+The protein's natural variant, known as in OPA13, features a modification of the amino acid from S to N at position 141.
+The protein's natural variant, known as in GHISID2; exhibits strong growth hormone-induced phosphorylation, but no subsequent nuclear localization; when forming homodimers with the wild-type protein, may also prevent its nuclear localization following growth hormone-stimulation;, features a modification of the amino acid from Q to P at position 177.
+The protein's natural variant, known as in GHISID2; loss of DNA-binding ability; when forming homodimers with the wild-type protein, may prevent wild-type binding to DNA; consequently, disruption of transcriptional activity;, features a modification of the amino acid from Q to R at position 474.
+The protein's natural variant, known as in GHISID2; loss of DNA-binding ability; when forming homodimers with the wild-type protein, may prevent wild-type binding to DNA; consequently, disruption of transcriptional activity;, features a modification of the amino acid from A to V at position 478.
+The protein's natural variant, known as in GHISID1; affects activation by growth hormone or interferon-gamma;, features a modification of the amino acid from A to P at position 630.
+The protein's natural variant, known as in GHISID1; transcriptionally inactive, features a modification of the amino acid from F to S at position 646.
+The protein's natural variant, known as in LPHAS;, features a modification of the amino acid from E to K at position 72.
+The protein's natural variant, known as in LPHAS; unknown pathological significance;, features a modification of the amino acid from R to W at position 102.
+The protein's natural variant, known as in FUHRS; retains activity that is significant but not comparable to wild-type activity;, features a modification of the amino acid from A to T at position 109.
+The protein's natural variant, known as in LPHAS;, features a modification of the amino acid from R to W at position 222.
+The protein's natural variant, known as in LPHAS; results in a loss of function mutation with some residual activity;, features a modification of the amino acid from R to C at position 292.
+The protein's natural variant, known as in strain: Serogroup D isolate 340, features a modification of the amino acid from GE to DK at position 66.
+The protein's natural variant, known as in strain: Serogroup D isolate 340, features a modification of the amino acid from D to E at position 80.
+The protein's natural variant, known as in strain: Serogroup D isolate 340, features a modification of the amino acid from A to T at position 95.
+The protein's natural variant, known as in Td, features a modification of the amino acid from G to R at position 107.
+The protein's natural variant, known as in strain: PB306, features a modification of the amino acid from G to W at position 185.
+The protein's natural variant, known as in strain: PB306, features a modification of the amino acid from F to L at position 187.
+The protein's natural variant, known as in strain: CB4854, features a modification of the amino acid from N to S at position 222.
+The protein's natural variant, known as in strain: CB4856, features a modification of the amino acid from Y to N at position 235.
+The protein's natural variant, known as in SHMS;, features a modification of the amino acid from R to W at position 203.
+The protein's natural variant, known as in strain: cv. Ehimehadaka No.1, features a modification of the amino acid from H to P at position 11.
+The protein's natural variant, known as in strain: cv. Igri, features a modification of the amino acid from K to R at position 117.
+The protein's natural variant, known as in strain: cv. Ehimehadaka No.1 and cv. Igri, features a modification of the amino acid from Q to R at position 174.
+The protein's natural variant, known as in strain: cv. Igri, features a modification of the amino acid from K to R at position 261.
+The protein's natural variant, known as in strain: cv. Igri, features a modification of the amino acid from A to V at position 272.
+The protein's natural variant, known as in strain: cv. Igri, features a modification of the amino acid from K to E at position 299.
+The protein's natural variant, known as in strain: cv. Igri, features a modification of the amino acid from T to I at position 308.
+The protein's natural variant, known as in COXPD32; significant decrease in protein levels; destabilizes the small ribosomal subunit resulting in impaired mitochondrial translation;, features a modification of the amino acid from E to K at position 13.
+The protein's natural variant, known as in 50% of the molecules, features a modification of the amino acid from A to T at position 13.
+The protein's natural variant, known as in PEOB5; results in decreased DNA decatenation;, features a modification of the amino acid from M to V at position 100.
+The protein's natural variant, known as in MGRISCE2, features a modification of the amino acid from A to V at position 176.
+The natural variant of this protein is characterized by an amino acid alteration from C to Y at position 596.
+The natural variant of this protein is characterized by an amino acid alteration from L to H at position 262.
+The natural variant of this protein is characterized by an amino acid alteration from F to L at position 276.
+The natural variant of this protein is characterized by an amino acid alteration from L to M at position 292.
+The natural variant of this protein is characterized by an amino acid alteration from L to M at position 353.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from P to Q at position 75.
+The natural variant of this protein is characterized by an amino acid alteration from E to K at position 184.
+The protein's natural variant, known as in a lung large cell carcinoma sample; somatic mutation;, features a modification of the amino acid from D to H at position 484.
+The protein's natural variant, known as in P2 form, features a modification of the amino acid from H to N at position 788.
+The protein's natural variant, known as in strain: CC-503, features a modification of the amino acid from T to S at position 49.
+The protein's natural variant, known as in strain: CC-503, features a modification of the amino acid from N to G at position 231.
+The protein's natural variant, known as in HAGRD; decreased glutathione reductase activity; decreased enzyme stability;, features a modification of the amino acid from G to A at position 374.
+The protein's natural variant, known as in RP45;, features a modification of the amino acid from G to V at position 993.
+The protein's natural variant, known as in PCTT; benign variant;, features a modification of the amino acid from L to F at position 12.
+The protein's natural variant, known as in PCTT;, features a modification of the amino acid from L to P at position 14.
+The protein's natural variant, known as in PCTT and TCP; associated with disease susceptibility; risk factor also for acute pancreatitis; may confer susceptibility to fibrocalculous pancreatic diabetes;, features a modification of the amino acid from N to S at position 34.
+The protein's natural variant, known as in POF2B; disrupts binding to nonmuscle actin filaments; abolishes tight junction localization; altered ciliogenesis and cystogenesis;, features a modification of the amino acid from R to Q at position 329.
+The protein's natural variant, known as in SPG39;, features a modification of the amino acid from V to I at position 263.
+The protein's natural variant, known as in BNHS;, features a modification of the amino acid from G to W at position 578.
+The protein's natural variant, known as in LNMS, features a modification of the amino acid from G to R at position 726.
+The protein's natural variant, known as in SPG39;, features a modification of the amino acid from G to E at position 840.
+The protein's natural variant, known as in SPG39;, features a modification of the amino acid from R to H at position 938.
+The protein's natural variant, known as in BNHS;, features a modification of the amino acid from S to L at position 1045.
+The protein's natural variant, known as in BNHS;, features a modification of the amino acid from T to I at position 1058.
+The protein's natural variant, known as in SPG39;, features a modification of the amino acid from M to V at position 1060.
+The protein's natural variant, known as in BNHS;, features a modification of the amino acid from F to S at position 1066.
+The protein's natural variant, known as in OMCS;, features a modification of the amino acid from R to Q at position 1099.
+The protein's natural variant, known as found in a patient with sporadic ataxia and BNHS; unknown pathological significance;, features a modification of the amino acid from V to G at position 1100.
+The protein's natural variant, known as in BNHS;, features a modification of the amino acid from V to M at position 1110.
+The protein's natural variant, known as in BNHS;, features a modification of the amino acid from P to L at position 1122.
+The protein's natural variant, known as in OMCS;, features a modification of the amino acid from G to R at position 1129.
+The protein's natural variant, known as in BNHS;, features a modification of the amino acid from R to C at position 1147.
+The protein's natural variant, known as in BNHS;, features a modification of the amino acid from S to C at position 1175.
+The protein's natural variant, known as in OMCS;, features a modification of the amino acid from G to S at position 1176.
+The protein's natural variant, known as in OMCS;, features a modification of the amino acid from V to A at position 1215.
+The protein's natural variant, known as in BNHS;, features a modification of the amino acid from R to W at position 1359.
+The protein's natural variant, known as found in a patient with Gordon-Holmes syndrome; unknown pathological significance;, features a modification of the amino acid from R to G at position 1362.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from T to N at position 464.
+The protein's natural variant, known as in strain: ZW141, features a modification of the amino acid from Q to L at position 511.
+The protein's natural variant, known as in strain: ZW122, features a modification of the amino acid from Q to QQ at position 514.
+The protein's natural variant, known as in strain: FGSC 430, features a modification of the amino acid from W to R at position 221.
+The protein's natural variant, known as in strain: FGSC 430, features a modification of the amino acid from F to L at position 362.
+The protein's natural variant, known as in strain: GEO, features a modification of the amino acid from A to D at position 95.
+The protein's natural variant, known as in strain: GEO, features a modification of the amino acid from K to M at position 115.
+The protein's natural variant, known as in strain: GEO, features a modification of the amino acid from A to T at position 178.
+The protein's natural variant, known as in strain: GEO, features a modification of the amino acid from F to H at position 230.
+The protein's natural variant, known as in strain: GEO, features a modification of the amino acid from N to D at position 265.
+The protein's natural variant, known as in strain: GEO, features a modification of the amino acid from L to M at position 486.
+The protein's natural variant, known as in CILD45; reduced protein abundance; changed axonemal dynein complex assembly; loss of sperm axoneme assembly;, features a modification of the amino acid from M to R at position 567.
+The protein's natural variant, known as in SSDA; loss of catalytic activity toward IGFBP3 and IGFBP5, features a modification of the amino acid from A to V at position 1033.
+The protein's natural variant, known as in allele HA-8P and allele HA-8PL;, features a modification of the amino acid from R to P at position 289.
+The protein's natural variant, known as in allele HA-8PL;, features a modification of the amino acid from V to L at position 297.
+The protein's natural variant, known as in ITPAD; complete loss of enzymatic activity at homozygosity; partial loss of activity without ITP accumulation in heterozygous individuals;, features a modification of the amino acid from P to T at position 32.
+The protein's natural variant, known as in DEE35; unknown pathological significance;, features a modification of the amino acid from R to C at position 178.
+The protein's natural variant, known as in MTDPS5;, features a modification of the amino acid from G to R at position 118.
+The protein's natural variant, known as in MTDPS5;, features a modification of the amino acid from D to N at position 251.
+The protein's natural variant, known as in MTDPS5;, features a modification of the amino acid from R to C at position 284.
+The protein's natural variant, known as in PG14, features a modification of the amino acid from A to V at position 359.
+The protein's natural variant, known as associated with a decreased susceptibility to diabetic nephropathy in Japanese and Chinese patients with type 2 diabetes;, features a modification of the amino acid from V to A at position 16.
+The protein's natural variant, known as in SPGF63; reduced protein expression;, features a modification of the amino acid from H to P at position 86.
+The protein's natural variant, known as in ASMB2/3; reduced activity, features a modification of the amino acid from F to S at position 50.
+The protein's natural variant, known as in ASMB1; reduced activity, features a modification of the amino acid from G to S at position 210.
+The protein's natural variant, known as in AMPDDE, features a modification of the amino acid from N to K at position 310.
+The protein's natural variant, known as in AMPDDE;, features a modification of the amino acid from V to L at position 311.
+The protein's natural variant, known as in AMPDDE;, features a modification of the amino acid from A to V at position 320.
+The protein's natural variant, known as in AMPDDE;, features a modification of the amino acid from M to T at position 324.
+The protein's natural variant, known as in AMPDDE;, features a modification of the amino acid from R to C at position 331.
+The protein's natural variant, known as in AMPDDE;, features a modification of the amino acid from R to C at position 402.
+The protein's natural variant, known as in AMPDDE;, features a modification of the amino acid from W to R at position 450.
+The protein's natural variant, known as in AMPDDE; enzyme inactive;, features a modification of the amino acid from R to C at position 573.
+The protein's natural variant, known as in AMPDDE;, features a modification of the amino acid from P to L at position 585.
+The protein's natural variant, known as in AMPDDE, features a modification of the amino acid from Q to P at position 712.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from G to E at position 139.
+The protein's natural variant, known as in SCHIND; type III;, features a modification of the amino acid from S to C at position 160.
+The protein's natural variant, known as in SCHIND; type I and type III;, features a modification of the amino acid from E to K at position 325.
+The protein's natural variant, known as in KANZD;, features a modification of the amino acid from R to Q at position 329.
+The protein's natural variant, known as in KANZD; loss of activity;, features a modification of the amino acid from R to W at position 329.
+The protein's natural variant, known as in strain: R5-R/c, features a modification of the amino acid from S to N at position 23.
+The protein's natural variant, known as in allele b', features a modification of the amino acid from K to R at position 25.
+The protein's natural variant, known as in allele b', features a modification of the amino acid from A to V at position 117.
+The protein's natural variant, known as in allele b', features a modification of the amino acid from H to Q at position 120.
+The protein's natural variant, known as in strain: Z362, features a modification of the amino acid from Q to H at position 284.
+The protein's natural variant, known as in strain: Z229, features a modification of the amino acid from E to K at position 317.
+The protein's natural variant, known as in strain: Z95, Z197 and Z229, features a modification of the amino acid from A to S at position 337.
+The protein's natural variant, known as in strain: Z184, Z210 and Z216, features a modification of the amino acid from A to P at position 438.
+The protein's natural variant, known as in strain: Z157, features a modification of the amino acid from V to L at position 458.
+The protein's natural variant, known as in strain: Oregon-R, Z145, Z266, Z346 and Z398, features a modification of the amino acid from M to L at position 460.
+The protein's natural variant, known as in LARS, features a modification of the amino acid from C to S at position 56.
+The protein's natural variant, known as in LARS, features a modification of the amino acid from S to L at position 58.
+The protein's natural variant, known as in GHIP;, features a modification of the amino acid from E to K at position 62.
+The protein's natural variant, known as in LARS, features a modification of the amino acid from W to R at position 68.
+The protein's natural variant, known as in LARS, features a modification of the amino acid from R to K at position 89.
+The protein's natural variant, known as in LARS; loss of ability to bind ligand;, features a modification of the amino acid from F to S at position 114.
+The protein's natural variant, known as in LARS, features a modification of the amino acid from V to A at position 143.
+The protein's natural variant, known as in LARS; disrupts GH binding;, features a modification of the amino acid from P to Q at position 149.
+The protein's natural variant, known as in LARS, features a modification of the amino acid from V to D at position 162.
+The protein's natural variant, known as found in a patient with idiopathic short stature; unknown pathological significance;, features a modification of the amino acid from V to I at position 162.
+The protein's natural variant, known as in LARS; abolishes receptor homodimerization;, features a modification of the amino acid from D to H at position 170.
+The protein's natural variant, known as in LARS; almost completely abolishes GH-binding at cell surface: 53% binding to membrane fractions;, features a modification of the amino acid from I to T at position 171.
+The protein's natural variant, known as in LARS; almost completely abolishes GH-binding at cell surface and in membrane fractions;, features a modification of the amino acid from Q to P at position 172.
+The protein's natural variant, known as in LARS; almost completely abolishes GH-binding at cell surface: 26% binding to membrane fractions;, features a modification of the amino acid from V to G at position 173.
+The protein's natural variant, known as in LARS and GHIP;, features a modification of the amino acid from R to C at position 179.
+The protein's natural variant, known as in LARS, features a modification of the amino acid from Y to C at position 226.
+The protein's natural variant, known as in LARS, features a modification of the amino acid from R to G at position 229.
+The protein's natural variant, known as found in a patient with idiopathic short stature; unknown pathological significance;, features a modification of the amino acid from R to H at position 229.
+The protein's natural variant, known as found in a patient with idiopathic short stature; unknown pathological significance;, features a modification of the amino acid from E to D at position 242.
+The protein's natural variant, known as in LARS;, features a modification of the amino acid from S to I at position 244.
+The protein's natural variant, known as in LARS, features a modification of the amino acid from D to N at position 262.
+The protein's natural variant, known as benign variant; associated with lower plasma HDL cholesterol levels in hypercholesterolemia patients that carry a pathogenic variant in LDLR;, features a modification of the amino acid from I to L at position 544.
+The protein's natural variant, known as in IP; shows the same luciferase activity as the control;, features a modification of the amino acid from E to K at position 57.
+The protein's natural variant, known as in IP; shows the same luciferase activity as the control;, features a modification of the amino acid from R to W at position 123.
+The protein's natural variant, known as in EDAID1;, features a modification of the amino acid from L to R at position 153.
+The protein's natural variant, known as in IP, features a modification of the amino acid from L to P at position 170.
+The protein's natural variant, known as in IMD33;, features a modification of the amino acid from R to G at position 173.
+The protein's natural variant, known as in IP;, features a modification of the amino acid from R to Q at position 173.
+The protein's natural variant, known as in EDAID1;, features a modification of the amino acid from R to P at position 175.
+The protein's natural variant, known as in IP;, features a modification of the amino acid from Q to H at position 183.
+The protein's natural variant, known as in EDAID1;, features a modification of the amino acid from L to P at position 227.
+The protein's natural variant, known as in EDAID1;, features a modification of the amino acid from A to G at position 288.
+The protein's natural variant, known as in EDAID1; abolishes binding to polyubiquitin ('K63'-linked and linear) and greatly impairs tandem ubiquitin binding;, features a modification of the amino acid from D to N at position 311.
+The protein's natural variant, known as in IP, features a modification of the amino acid from A to P at position 314.
+The protein's natural variant, known as in IMD33; greatly impairs tandem ubiquitin binding. Impairs oligomerization, impairs binding of 'Lys-63'-linked ubiuitin and linear tetra-ubiquitin, impairs TNF-induced NF-kappa-B activation;, features a modification of the amino acid from E to A at position 315.
+The protein's natural variant, known as in IMD33; impairs tandem ubiquitin binding;, features a modification of the amino acid from R to Q at position 319.
+The protein's natural variant, known as in IP, features a modification of the amino acid from L to P at position 322.
+The protein's natural variant, known as in IP; diminishes interaction with TRAF6 and polyubiquitination, greatly impairs tandem ubiquitin binding. Impairs oligomerization, greatly impairs binding of 'Lys-63'-linked ubiuitin and linear tetra-ubiquitin, impairs TNF-induced NF-kappa-B activation;, features a modification of the amino acid from A to P at position 323.
+The protein's natural variant, known as in EDAID1;, features a modification of the amino acid from D to V at position 406.
+The protein's natural variant, known as in IP; impairs binding to ubiquitin;, features a modification of the amino acid from M to V at position 407.
+The protein's natural variant, known as in IP, features a modification of the amino acid from H to Y at position 413.
+The protein's natural variant, known as in EDAID1;, features a modification of the amino acid from C to F at position 417.
+The protein's natural variant, known as in EDAID1; loss of sumoylation;, features a modification of the amino acid from C to R at position 417.
+The protein's natural variant, known as in IMD33;, features a modification of the amino acid from C to Y at position 417.
+The protein's natural variant, known as in NTD; uncertain pathological significance; does not affect interaction with DVL2; does not affect subcellular location; increases RHOA activation but decreases the ability to activate JNK;, features a modification of the amino acid from R to W at position 45.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from G to C at position 124.
+The protein's natural variant, known as found in a patient with craniorachischisis; sporadic case; unknown pathological significance, features a modification of the amino acid from D to G at position 142.
+The protein's natural variant, known as in NTD; does not affect interaction with DVL2; does not affect subcellular location; results in reduced RHOA and JNK activation, features a modification of the amino acid from N to K at position 356.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from S to L at position 682.
+The protein's natural variant, known as found in a patient with closed spina bifida; sporadic case; unknown pathological significance;, features a modification of the amino acid from V to G at position 702.
+The protein's natural variant, known as found in a patient with encephalocele; sporadic case; unknown pathological significance, features a modification of the amino acid from T to K at position 808.
+The protein's natural variant, known as in NTD;, features a modification of the amino acid from S to F at position 84.
+The protein's natural variant, known as in NTD; the mutant protein has diminished interaction with DVL1 compared to wild-type;, features a modification of the amino acid from R to C at position 353.
+The protein's natural variant, known as in NTD; the mutation protein completely abrogates interaction with DVL1 compared to wild-type;, features a modification of the amino acid from F to S at position 437.
+The protein's natural variant, known as in tryptic peptides, features a modification of the amino acid from SD to PN at position 167.
+The protein's natural variant, known as in strain: SW18, SW4, SW24 and SW1, features a modification of the amino acid from D to T at position 2.
+The protein's natural variant, known as in strain: SW18, features a modification of the amino acid from GKEILGEGWN to AKQILAKDWD at position 33.
+The protein's natural variant, known as in strain: SW24 and SW1, features a modification of the amino acid from GKEILGEG to AKQILADD at position 31.
+The protein's natural variant, known as in strain: SW4, features a modification of the amino acid from GKEILGEG to AKQILAED at position 31.
+The protein's natural variant, known as in strain: SW18, SW4, SW24 and SW1, features a modification of the amino acid from D to G at position 56.
+The protein's natural variant, known as in strain: SW24 and SW1, features a modification of the amino acid from D to N at position 65.
+The protein's natural variant, known as in strain: SW18, SW4, SW24 and SW1, features a modification of the amino acid from DILKQSD to NIIKNSN at position 76.
+The protein's natural variant, known as in strain: SW18, SW4, SW24 and SW1, features a modification of the amino acid from N to V at position 87.
+The protein's natural variant, known as in strain: SW4, SW24 and SW1, features a modification of the amino acid from I to S at position 91.
+The protein's natural variant, known as in strain: SW18, features a modification of the amino acid from I to T at position 91.
+The protein's natural variant, known as in strain: SW18, SW4, SW24 and SW1, features a modification of the amino acid from P to T at position 94.
+The protein's natural variant, known as in strain: SW18, SW4, SW24 and SW1, features a modification of the amino acid from E to P at position 110.
+The protein's natural variant, known as in strain: SW4, SW24 and SW1, features a modification of the amino acid from L to I at position 123.
+The protein's natural variant, known as in strain: SW18, features a modification of the amino acid from L to V at position 123.
+The protein's natural variant, known as in strain: SW18, SW4, SW24 and SW1, features a modification of the amino acid from K to N at position 127.
+The protein's natural variant, known as in strain: SW18, SW4, SW24 and SW1, features a modification of the amino acid from L to S at position 130.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from N to K at position 181.
+The protein's natural variant, known as in ALS10;, features a modification of the amino acid from D to G at position 169.
+The protein's natural variant, known as in ALS10; also in a patient with frontotemporal dementia;, features a modification of the amino acid from N to S at position 267.
+The protein's natural variant, known as in ALS10; loss of ability to negatively regulate the expression of CDK6;, features a modification of the amino acid from G to S at position 287.
+The protein's natural variant, known as in ALS10;, features a modification of the amino acid from G to A at position 290.
+The protein's natural variant, known as in ALS10;, features a modification of the amino acid from G to A at position 294.
+The protein's natural variant, known as in ALS10; a patient with bulbar signs and dementia;, features a modification of the amino acid from G to V at position 294.
+The protein's natural variant, known as in ALS10;, features a modification of the amino acid from G to R at position 295.
+The protein's natural variant, known as in ALS10; also in patients with frontotemporal lobar degeneration with motor neuron disease;, features a modification of the amino acid from G to S at position 295.
+The protein's natural variant, known as in ALS10;, features a modification of the amino acid from G to S at position 298.
+The protein's natural variant, known as in ALS10; triggers mitochondrial DNA release into the cytosol, which is then detected by CGAS, leading to activation of the cGAS-STING pathway and autoinflammation; slight reduction in interaction with PPIA/CYPA;, features a modification of the amino acid from A to T at position 315.
+The protein's natural variant, known as in ALS10; loss of ability to negatively regulate the expression of CDK6, features a modification of the amino acid from A to V at position 321.
+The protein's natural variant, known as in ALS10; triggers mitochondrial DNA release into the cytosol, which is then detected by CGAS, leading to activation of the cGAS-STING pathway and autoinflammation; impedes the development of normal limb and tail buds and increases the number of apoptotic nuclei when expressed in chick embryos; does not affect the interaction with ATXN2;, features a modification of the amino acid from Q to K at position 331.
+The protein's natural variant, known as in ALS10;, features a modification of the amino acid from S to N at position 332.
+The protein's natural variant, known as in ALS10;, features a modification of the amino acid from G to D at position 335.
+The protein's natural variant, known as in ALS10; impedes the development of normal limb and tail buds and increases the number of apoptotic nuclei when expressed in chick embryos; loss of ability to negatively regulate the expression of CDK6;, features a modification of the amino acid from M to V at position 337.
+The protein's natural variant, known as in ALS10;, features a modification of the amino acid from Q to R at position 343.
+The protein's natural variant, known as in ALS10;, features a modification of the amino acid from G to C at position 348.
+The protein's natural variant, known as in ALS10; loss of interaction with PPIA/CYPA, features a modification of the amino acid from G to V at position 348.
+The protein's natural variant, known as in ALS10, features a modification of the amino acid from G to R at position 357.
+The protein's natural variant, known as in ALS10; significant reduction in interaction with PPIA/CYPA;, features a modification of the amino acid from R to S at position 361.
+The protein's natural variant, known as in ALS10, features a modification of the amino acid from R to T at position 361.
+The protein's natural variant, known as in ALS10;, features a modification of the amino acid from S to C at position 379.
+The protein's natural variant, known as in ALS10;, features a modification of the amino acid from S to P at position 379.
+The protein's natural variant, known as in ALS10;, features a modification of the amino acid from A to T at position 382.
+The protein's natural variant, known as in ALS10;, features a modification of the amino acid from N to D at position 390.
+The protein's natural variant, known as in ALS10;, features a modification of the amino acid from N to S at position 390.
+The protein's natural variant, known as in ALS10;, features a modification of the amino acid from S to L at position 393.
+The protein's natural variant, known as defines the Lu(a) antigen;, features a modification of the amino acid from R to H at position 77.
+The protein's natural variant, known as in STR41 mutation, high level of resistance to streptomycin, features a modification of the amino acid from K to T at position 56.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from A to D at position 155.
+The protein's natural variant, known as in CFDS;, features a modification of the amino acid from R to W at position 223.
+The protein's natural variant, known as in CFDS;, features a modification of the amino acid from S to L at position 226.
+The protein's natural variant, known as in CFDS;, features a modification of the amino acid from T to M at position 259.
+The protein's natural variant, known as in CFDS;, features a modification of the amino acid from P to H at position 292.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from V to M at position 542.
+The protein's natural variant, known as in strain: cv. Cvi-0, features a modification of the amino acid from T to S at position 29.
+The natural variant of this protein is characterized by an amino acid alteration from R to Q at position 16.
+The protein's natural variant, known as in MTPD; mild phenotype with slowly progressive myopathy and sensorimotor polyneuropathy;, features a modification of the amino acid from V to D at position 282.
+The protein's natural variant, known as in MTPD; mild phenotype with slowly progressive myopathy and sensorimotor polyneuropathy;, features a modification of the amino acid from I to N at position 305.
+The protein's natural variant, known as in LCHAD deficiency;, features a modification of the amino acid from L to P at position 342.
+The protein's natural variant, known as in AFLP and LCHAD deficiency; loss of long-chain-3-hydroxyacyl-CoA dehydrogenase activity;, features a modification of the amino acid from E to Q at position 510.
+The protein's natural variant, known as in ATFB15; fails to accumulate at various foci of the nuclear envelope and is diffusely distributed in the cytoplasm; shows significantly reduced permeability of the nuclear envelope compared to wild-type;, features a modification of the amino acid from R to H at position 391.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from RT to SL at position 114.
+The protein's natural variant, known as in strain: CAM-44, CAM-48 and Berkeley, features a modification of the amino acid from K to M at position 163.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to Q at position 1160.
+The protein's natural variant, known as in MNLIX;, features a modification of the amino acid from E to K at position 407.
+The protein's natural variant, known as in MNLIX;, features a modification of the amino acid from E to K at position 418.
+The protein's natural variant, known as in strain: NEM1278, features a modification of the amino acid from A to V at position 42.
+The protein's natural variant, known as in strain: NEM667 and D39, features a modification of the amino acid from ESIPA to DLSQH at position 65.
+The protein's natural variant, known as in strain: 1510, features a modification of the amino acid from A to T at position 100.
+The protein's natural variant, known as in strain: NEM1122, features a modification of the amino acid from F to L at position 110.
+The protein's natural variant, known as in strain: 1510, features a modification of the amino acid from T to I at position 143.
+The protein's natural variant, known as in strain: 872, features a modification of the amino acid from Q to L at position 148.
+The protein's natural variant, known as in strain: 1293, 1454, 1565, 1639, 3051 and 3203, features a modification of the amino acid from Q to P at position 148.
+The protein's natural variant, known as in strain: 661, features a modification of the amino acid from I to F at position 152.
+The protein's natural variant, known as in allele MICA*010, allele MICA*025 and allele MICA*054; abolishes cell surface expression, probably by interfering with protein folding;, features a modification of the amino acid from R to P at position 29.
+The protein's natural variant, known as in allele MICA*002, allele MICA*011, allele MICA*013, allele MICA*014, allele MICA*015, allele MICA*017, allele MICA*020, allele MICA*022, allele MICA*023, allele MICA*030, allele MICA*034, allele MICA*035, allele MICA*036, allele MICA*041, allele MICA*044, allele MICA*046, allele MICA*047, allele MICA*052, allele MICA*053 and allele MICA*055;, features a modification of the amino acid from W to G at position 37.
+The protein's natural variant, known as in allele MICA*002, allele MICA*004, allele MICA*005, allele MICA*006, allele MICA*007, allele MICA*008, allele MICA*009, allele MICA*010, allele MICA*011, allele MICA*013, allele MICA*014, allele MICA*015, allele MICA*016, allele MICA*017, allele MICA*019, allele MICA*020, allele MICA*022, allele MICA*023, allele MICA*024, allele MICA*025, allele MICA*026, allele MICA*027, allele MICA*028, allele MICA*029, allele MICA*030, allele MICA*031, allele MICA*032, allele MICA*033, allele MICA*034, allele MICA*035, allele MICA*036, allele MICA*037, allele MICA*038, allele MICA*039, allele MICA*040, allele MICA*041, allele MICA*042, allele MICA*043, allele MICA*044, allele MICA*045, allele MICA*046, allele MICA*047, allele MICA*048, allele MICA*049, allele MICA*051, allele MICA*052, allele MICA*053, allele MICA*054, allele MICA*055 and allele MICA*056;, features a modification of the amino acid from T to A at position 47.
+The protein's natural variant, known as in allele MICA*041;, features a modification of the amino acid from V to G at position 49.
+The protein's natural variant, known as in allele MICA*004, allele MICA*005, allele MICA*006, allele MICA*008, allele MICA*009, allele MICA*010, allele MICA*016, allele MICA*019, allele MICA*024, allele MICA*025, allele MICA*027, allele MICA*028, allele MICA*031, allele MICA*032, allele MICA*033, allele MICA*042, allele MICA*044, allele MICA*048, allele MICA*049, allele MICA*051, allele MICA*054 and allele MICA*056;, features a modification of the amino acid from C to Y at position 59.
+The protein's natural variant, known as in allele MICA*017;, features a modification of the amino acid from Q to R at position 114.
+The protein's natural variant, known as in allele MICA*036;, features a modification of the amino acid from R to K at position 128.
+The protein's natural variant, known as in allele MICA*014 and allele MICA*015;, features a modification of the amino acid from G to R at position 137.
+The protein's natural variant, known as in allele MICA*004, allele MICA*006, allele MICA*009, allele MICA*044 and allele MICA*049;, features a modification of the amino acid from L to V at position 145.
+The protein's natural variant, known as in allele MICA*033;, features a modification of the amino acid from T to S at position 147.
+The protein's natural variant, known as in allele MICA*002, allele MICA*004, allele MICA*005, allele MICA*006, allele MICA*007, allele MICA*008, allele MICA*009, allele MICA*010, allele MICA*011, allele MICA*012, allele MICA*013, allele MICA*014, allele MICA*015, allele MICA*016, allele MICA*017, allele MICA*018, allele MICA*019, allele MICA*020, allele MICA*022, allele MICA*023, allele MICA*024, allele MICA*025, allele MICA*026, allele MICA*027, allele MICA*028, allele MICA*029, allele MICA*030, allele MICA*032, allele MICA*033, allele MICA*034, allele MICA*035, allele MICA*036, allele MICA*037, allele MICA*038, allele MICA*039, allele MICA*041, allele MICA*042, allele MICA*043, allele MICA*044, allele MICA*045, allele MICA*046, allele MICA*047, allele MICA*048, allele MICA*049, allele MICA*051, allele MICA*052, allele MICA*053, allele MICA*054, allele MICA*055 and allele MICA*056;, features a modification of the amino acid from K to E at position 148.
+The protein's natural variant, known as in allele MICA*004, allele MICA*005, allele MICA*006, allele MICA*008, allele MICA*009, allele MICA*010, allele MICA*013, allele MICA*016, allele MICA*019, allele MICA*022, allele MICA*024, allele MICA*027, allele MICA*028, allele MICA*033, allele MICA*044, allele MICA*048, allele MICA*049, allele MICA*053, allele MICA*054 and allele MICA*056; reduces binding affinity for KLRK1;, features a modification of the amino acid from M to V at position 152.
+The protein's natural variant, known as in allele MICA*029;, features a modification of the amino acid from V to I at position 165.
+The protein's natural variant, known as in allele MICA*011 and allele MICA*034;, features a modification of the amino acid from M to V at position 174.
+The protein's natural variant, known as in allele MICA*012, allele MICA*032 and allele MICA*043;, features a modification of the amino acid from H to L at position 179.
+The protein's natural variant, known as in allele MICA*004, allele MICA*006, allele MICA*008, allele MICA*009, allele MICA*010, allele MICA*013, allele MICA*014, allele MICA*016, allele MICA*019, allele MICA*022, allele MICA*024, allele MICA*027, allele MICA*028, allele MICA*033, allele MICA*036, allele MICA*044, allele MICA*048, allele MICA*049, allele MICA*053, allele MICA*054 and allele MICA*056;, features a modification of the amino acid from K to E at position 196.
+The protein's natural variant, known as in allele MICA*004, allele MICA*006, allele MICA*009, allele MICA*010, allele MICA*016, allele MICA*019, allele MICA*031, allele MICA*033, allele MICA*036, allele MICA*044, allele MICA*049, allele MICA*054 and allele MICA*056;, features a modification of the amino acid from G to S at position 198.
+The protein's natural variant, known as in allele MICA*006;, features a modification of the amino acid from V to I at position 199.
+The protein's natural variant, known as in allele MICA*004, allele MICA*014, allele MICA*032 and allele MICA*044;, features a modification of the amino acid from T to R at position 204.
+The protein's natural variant, known as in allele MICA*004, allele MICA*005, allele MICA*006, allele MICA*008, allele MICA*009, allele MICA*010, allele MICA*016, allele MICA*019, allele MICA*022, allele MICA*024, allele MICA*027, allele MICA*033, allele MICA*034, allele MICA*035, allele MICA*037, allele MICA*038, allele MICA*039, allele MICA*042, allele MICA*044, allele MICA*048, allele MICA*049, allele MICA*053, allele MICA*054 and allele MICA*056;, features a modification of the amino acid from G to S at position 229.
+The protein's natural variant, known as in allele MICA*046;, features a modification of the amino acid from Y to C at position 231.
+The protein's natural variant, known as in allele MICA*004, allele MICA*005, allele MICA*006, allele MICA*008, allele MICA*009, allele MICA*010, allele MICA*016, allele MICA*019, allele MICA*022, allele MICA*024, allele MICA*027, allele MICA*033, allele MICA*034, allele MICA*035, allele MICA*037, allele MICA*038, allele MICA*039, allele MICA*042, allele MICA*044, allele MICA*048, allele MICA*049, allele MICA*053, allele MICA*054 and allele MICA*056;, features a modification of the amino acid from W to R at position 233.
+The protein's natural variant, known as in allele MICA*008, allele MICA*010, allele MICA*016, allele MICA*019, allele MICA*022, allele MICA*027, allele MICA*033, allele MICA*035, allele MICA*037, allele MICA*039, allele MICA*042, allele MICA*048, allele MICA*053, allele MICA*054 and allele MICA*056;, features a modification of the amino acid from T to I at position 236.
+The protein's natural variant, known as in allele MICA*004, allele MICA*006, allele MICA*008, allele MICA*009, allele MICA*010, allele MICA*016, allele MICA*019, allele MICA*022, allele MICA*024, allele MICA*027, allele MICA*033, allele MICA*034, allele MICA*035, allele MICA*037, allele MICA*038, allele MICA*039, allele MICA*042, allele MICA*044, allele MICA*048, allele MICA*049, allele MICA*053, allele MICA*054 and allele MICA*056;, features a modification of the amino acid from S to T at position 238.
+The protein's natural variant, known as in allele MICA*016 and allele MICA*039;, features a modification of the amino acid from V to L at position 244.
+The protein's natural variant, known as in allele MICA*056;, features a modification of the amino acid from W to S at position 253.
+The protein's natural variant, known as in allele MICA*005, allele MICA*008, allele MICA*010, allele MICA*013, allele MICA*016, allele MICA*019, allele MICA*022, allele MICA*027, allele MICA*033, allele MICA*035, allele MICA*037, allele MICA*039, allele MICA*042, allele MICA*045, allele MICA*048, allele MICA*053, allele MICA*054 and allele MICA*056;, features a modification of the amino acid from Q to R at position 274.
+The protein's natural variant, known as in allele MICA*043;, features a modification of the amino acid from R to S at position 279.
+The protein's natural variant, known as in allele MICA*054;, features a modification of the amino acid from S to G at position 291.
+The protein's natural variant, known as in allele MICA*011, allele MICA*030 and allele MICA*047;, features a modification of the amino acid from P to A at position 294.
+The protein's natural variant, known as in allele MICA*015 and allele MICA*017, features a modification of the amino acid from VLVLQSHWQTFHVSAVAAAAIFVIIIFYVRCCKKKTSAAEGPELVSLQVLDQHPVGTSDHRDATQLGFQPLMSDLGSTGSTEGA to CWCFRVIGRHSMFLLLLLLLLLLLLFLLLLFSTSVVVRRKHQLQRVQSS at position 383.
+The protein's natural variant, known as in allele MICA*008, allele MICA*023, allele MICA*028 and allele MICA*053, features a modification of the amino acid from AAIFVIIIFYVRCCKKKTSAAEGPELVSLQVLDQHPVGTSDHRDATQLGFQPLMSDLGSTGSTEGA to GCCYFCYYYFLCPLL at position 383.
+The protein's natural variant, known as in allele MICA*010, allele MICA*016, allele MICA*019, allele MICA*027, allele MICA*033, allele MICA*048, allele MICA*054 and allele MICA*056, features a modification of the amino acid from A to AA at position 319.
+The protein's natural variant, known as in allele MICA*004, allele MICA*006, allele MICA*009, allele MICA*011, allele MICA*026, allele MICA*047 and allele MICA*049, features a modification of the amino acid from A to AAA at position 319.
+The protein's natural variant, known as in allele MICA*050, features a modification of the amino acid from A to AAAA at position 319.
+The protein's natural variant, known as in allele MICA*055, features a modification of the amino acid from A to AAAAA at position 319.
+The protein's natural variant, known as in allele MICA*002, allele MICA*041, allele MICA*046 and allele MICA*052, features a modification of the amino acid from A to AAAAAA at position 319.
+The protein's natural variant, known as in allele MICA*020, features a modification of the amino acid from A to AAAAAAA at position 319.
+The protein's natural variant, known as in allele MICA*052;, features a modification of the amino acid from V to I at position 328.
+The protein's natural variant, known as in allele MICA*002, allele MICA*011, allele MICA*020, allele MICA*041, allele MICA*043, allele MICA*046, allele MICA*047, allele MICA*050 and allele MICA*052;, features a modification of the amino acid from R to C at position 329.
+The protein's natural variant, known as in allele MICA*049;, features a modification of the amino acid from T to M at position 356.
+The protein's natural variant, known as in allele MICA*004, allele MICA*006, allele MICA*010, allele MICA*011, allele MICA*016, allele MICA*019, allele MICA*048 and allele MICA*049;, features a modification of the amino acid from D to A at position 373.
+The protein's natural variant, known as in allele MICA*011;, features a modification of the amino acid from T to A at position 377.
+The protein's natural variant, known as in allele MICA*018;, features a modification of the amino acid from A to T at position 383.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to Q at position 299.
+The protein's natural variant, known as in a gastric adenocarcinoma sample; somatic mutation, features a modification of the amino acid from K to E at position 321.
+The natural variant of this protein is characterized by an amino acid alteration from S to C at position 443.
+The natural variant of this protein is characterized by an amino acid alteration from I to M at position 559.
+The protein's natural variant, known as in AOMS4; strongly decreased elastase activity; abolishes interaction with SERPINA1; impaired insulin degradation; increased platelet aggregation;, features a modification of the amino acid from T to M at position 70.
+The protein's natural variant, known as in AOMS4; unknown pathological significance; strongly decreased elastase activity; no effect on interaction with SERPINA1; no effect on insulin degradation; increased platelet aggregation;, features a modification of the amino acid from L to M at position 85.
+The protein's natural variant, known as in AOMS4; strongly decreased elastase activity; abolishes interaction with SERPINA1; increased levels in plasma; impaired insulin degradation; increased platelet aggregation;, features a modification of the amino acid from D to N at position 121.
+The protein's natural variant, known as in SENEBAC; unknown pathological significance;, features a modification of the amino acid from L to P at position 10.
+The protein's natural variant, known as in RP7; in combination with a null mutation of ROM1;, features a modification of the amino acid from R to W at position 13.
+The protein's natural variant, known as in some patients with macular dystrophy;, features a modification of the amino acid from I to V at position 32.
+The protein's natural variant, known as in RP7 and VMD3; results in retinitis pigmentosa in combination with a null mutation of ROM1;, features a modification of the amino acid from L to F at position 45.
+The protein's natural variant, known as in MDPT1; also in cone-rod dystrophy;, features a modification of the amino acid from G to R at position 68.
+The protein's natural variant, known as in CACD2;, features a modification of the amino acid from R to W at position 123.
+The protein's natural variant, known as in RP7, features a modification of the amino acid from L to P at position 126.
+The protein's natural variant, known as in RP7, features a modification of the amino acid from L to R at position 126.
+The protein's natural variant, known as in RP7 and VMD3;, features a modification of the amino acid from Y to C at position 141.
+The protein's natural variant, known as in RP7; also found in a patient with central areolar choroidal dystrophy;, features a modification of the amino acid from R to W at position 142.
+The protein's natural variant, known as in RP7;, features a modification of the amino acid from K to R at position 153.
+The protein's natural variant, known as in MDPT1;, features a modification of the amino acid from D to N at position 157.
+The protein's natural variant, known as in RP7;, features a modification of the amino acid from C to Y at position 165.
+The protein's natural variant, known as in MDPT1; butterfly-shaped;, features a modification of the amino acid from G to D at position 167.
+The protein's natural variant, known as in MDPT1; butterfly-shaped;, features a modification of the amino acid from G to S at position 167.
+The protein's natural variant, known as in MDPT1; butterfly-shaped;, features a modification of the amino acid from R to G at position 172.
+The protein's natural variant, known as in some patients with macular dystrophy;, features a modification of the amino acid from R to Q at position 172.
+The protein's natural variant, known as in some patients with macular dystrophy; also in a family affected by central areolar choroidal dystrophy;, features a modification of the amino acid from R to W at position 172.
+The protein's natural variant, known as in RP7;, features a modification of the amino acid from D to V at position 173.
+The protein's natural variant, known as in cone-rod dystrophy;, features a modification of the amino acid from Y to S at position 184.
+The protein's natural variant, known as in RP7; digenic inheritance; results in disease in combination with a null mutation of ROM1;, features a modification of the amino acid from L to P at position 185.
+The protein's natural variant, known as in CACD2; increased protein expression;, features a modification of the amino acid from R to L at position 195.
+The protein's natural variant, known as in RP7; decreased protein expression;, features a modification of the amino acid from S to R at position 198.
+The protein's natural variant, known as in RP7;, features a modification of the amino acid from G to D at position 208.
+The protein's natural variant, known as in VMD3; increased protein expression;, features a modification of the amino acid from V to I at position 209.
+The protein's natural variant, known as in RP7; decreased protein expression;, features a modification of the amino acid from P to L at position 210.
+The protein's natural variant, known as in MDPT1 and RP7; also in adult-onset foveomacular dystrophy with choroidal neovascularization;, features a modification of the amino acid from P to R at position 210.
+The protein's natural variant, known as in RP7;, features a modification of the amino acid from P to S at position 210.
+The protein's natural variant, known as in RP7;, features a modification of the amino acid from F to L at position 211.
+The protein's natural variant, known as in RP7;, features a modification of the amino acid from S to G at position 212.
+The protein's natural variant, known as in VMD3;, features a modification of the amino acid from S to T at position 212.
+The protein's natural variant, known as in VMD3, features a modification of the amino acid from C to F at position 213.
+The protein's natural variant, known as in MDPT1;, features a modification of the amino acid from C to R at position 213.
+The protein's natural variant, known as in RP7; decreased protein expression;, features a modification of the amino acid from C to S at position 214.
+The protein's natural variant, known as in RP7, features a modification of the amino acid from P to A at position 216.
+The protein's natural variant, known as in RP7;, features a modification of the amino acid from P to L at position 216.
+The protein's natural variant, known as in RP7, features a modification of the amino acid from P to R at position 216.
+The protein's natural variant, known as in RP7;, features a modification of the amino acid from P to S at position 216.
+The protein's natural variant, known as in some patients with macular dystrophy;, features a modification of the amino acid from P to R at position 219.
+The protein's natural variant, known as in MDPT1; increased protein expression;, features a modification of the amino acid from R to Q at position 220.
+The protein's natural variant, known as in MDPT1;, features a modification of the amino acid from R to W at position 220.
+The protein's natural variant, known as in CACD2, features a modification of the amino acid from P to L at position 221.
+The protein's natural variant, known as in cone-rod dystrophy;, features a modification of the amino acid from N to H at position 244.
+The protein's natural variant, known as in RP7; with bulls-eye maculopathy;, features a modification of the amino acid from N to K at position 244.
+The protein's natural variant, known as in RP7; decreased protein expression, features a modification of the amino acid from G to S at position 249.
+The protein's natural variant, known as in RP7;, features a modification of the amino acid from G to D at position 266.
+The protein's natural variant, known as in VMD3;, features a modification of the amino acid from V to I at position 268.
+The protein's natural variant, known as in VMD3;, features a modification of the amino acid from G to D at position 305.
+The protein's natural variant, known as in strain: AB1, AB2, CB4852, CB4853, CB4855, CB4857, CB4858, KR314 and PB306, features a modification of the amino acid from I to V at position 288.
+The protein's natural variant, known as in HHC1; demonstrates reduced intracellular and plasma membrane expression and signaling to the MAPK pathway in response to extracellular calcium relative to wild-type; fails to be inserted in the microsomes and does not undergo proper glycosylation;, features a modification of the amino acid from L to S at position 11.
+The protein's natural variant, known as in HHC1; has a dose-response curve shifted to the right relative to that of wild-type; demonstrates reduced intracellular and plasma membrane expression and signaling to the MAPK pathway in response to extracellular calcium relative to wild-type; fails to be inserted in the microsomes and does not undergo proper glycosylation;, features a modification of the amino acid from L to P at position 13.
+The protein's natural variant, known as does not demonstrate reduced intracellular and plasma membrane expression and signaling to the MAPK pathway in response to extracellular calcium relative to wild-type; does not fail to be inserted in the microsomes and does undergo proper glycosylation;, features a modification of the amino acid from T to A at position 14.
+The protein's natural variant, known as in HHC1;, features a modification of the amino acid from G to R at position 21.
+The protein's natural variant, known as found in a patient with primary hyperparathyroidism detected at adulthood; mutant CASR is activated by a higher calcium concentrations than the wild-type, features a modification of the amino acid from Q to R at position 27.
+The protein's natural variant, known as in HHC1;, features a modification of the amino acid from P to A at position 39.
+The protein's natural variant, known as in HHC1;, features a modification of the amino acid from F to S at position 42.
+The protein's natural variant, known as in HYPOC1; the EC(50) of the mutant is significantly lower than that of wild-type;, features a modification of the amino acid from K to N at position 47.
+The protein's natural variant, known as in HHC1; decreased G-protein coupled receptor signaling pathway, features a modification of the amino acid from S to P at position 53.
+The protein's natural variant, known as in HHC1; decreased G-protein coupled receptor signaling pathway;, features a modification of the amino acid from P to L at position 55.
+The protein's natural variant, known as in HHC1; mild; decreased G-protein coupled receptor signaling pathway;, features a modification of the amino acid from R to M at position 62.
+The protein's natural variant, known as in HHC1; does not affect homodimerization; impaired N-glycosylation; impaired cell membrane localization; decreased G-protein coupled receptor signaling pathway;, features a modification of the amino acid from R to C at position 66.
+The protein's natural variant, known as in HHC1; does not affect homodimerization; impaired N-glycosylation; impaired cell membrane localization; decreased G-protein coupled receptor signaling pathway;, features a modification of the amino acid from R to H at position 66.
+The protein's natural variant, known as in HHC1; decreased G-protein coupled receptor signaling pathway, features a modification of the amino acid from I to M at position 81.
+The protein's natural variant, known as in NSHPT; Abolished G-protein coupled receptor activity, features a modification of the amino acid from T to I at position 100.
+The protein's natural variant, known as in HHC1; decreased G-protein coupled receptor signaling pathway, features a modification of the amino acid from A to T at position 110.
+The protein's natural variant, known as in HYPOC1;, features a modification of the amino acid from A to T at position 116.
+The protein's natural variant, known as in HYPOC1; the mutation shifts the concentration-response curve to the left and increases maximal activity;, features a modification of the amino acid from N to K at position 118.
+The protein's natural variant, known as in HYPOC1; increased G-protein coupled receptor signaling pathway, features a modification of the amino acid from S to C at position 122.
+The protein's natural variant, known as in HYPOC1, features a modification of the amino acid from L to F at position 125.
+The protein's natural variant, known as in HYPOC1; shifts the concentration-response curve of calcium ions to the left;, features a modification of the amino acid from L to P at position 125.
+The protein's natural variant, known as in HYPOC1; increased G-protein coupled receptor signaling pathway;, features a modification of the amino acid from E to A at position 127.
+The protein's natural variant, known as in HYPOC1; increased G-protein coupled receptor signaling pathway;, features a modification of the amino acid from F to L at position 128.
+The protein's natural variant, known as in HYPOC1, features a modification of the amino acid from C to R at position 129.
+The protein's natural variant, known as in HYPOC1; associated with clinical features of Bartter syndrome;, features a modification of the amino acid from C to W at position 131.
+The protein's natural variant, known as in HYPOC1; increased G-protein coupled receptor signaling pathway; does not affect cell membrane localization, features a modification of the amino acid from P to L at position 136.
+The protein's natural variant, known as in HHC1; decreased G-protein coupled receptor signaling pathway;, features a modification of the amino acid from T to M at position 138.
+The protein's natural variant, known as in HHC1; decreased G-protein coupled receptor signaling pathway;, features a modification of the amino acid from G to E at position 143.
+The protein's natural variant, known as in HHC1;, features a modification of the amino acid from G to R at position 143.
+The protein's natural variant, known as in HYPOC1; increased G-protein coupled receptor signaling pathway;, features a modification of the amino acid from T to M at position 151.
+The protein's natural variant, known as in HHC1, features a modification of the amino acid from G to R at position 158.
+The protein's natural variant, known as in HHC1; decreased G-protein coupled receptor signaling pathway, features a modification of the amino acid from L to P at position 159.
+The protein's natural variant, known as in HHC1;, features a modification of the amino acid from S to G at position 166.
+The protein's natural variant, known as in HHC1, features a modification of the amino acid from S to N at position 171.
+The protein's natural variant, known as in HHC1; decreased G-protein coupled receptor signaling pathway;, features a modification of the amino acid from R to G at position 172.
+The protein's natural variant, known as in HHC1, features a modification of the amino acid from L to R at position 174.
+The protein's natural variant, known as in HHC1; decreased G-protein coupled receptor signaling pathway;, features a modification of the amino acid from N to D at position 178.
+The protein's natural variant, known as in HHC1; although the mutant receptor is expressed normally at the cell surface it is unresponsive with respect to intracellular signaling (MAPK activation) to increases in extracellular calcium concentrations;, features a modification of the amino acid from F to C at position 180.
+The protein's natural variant, known as in HHC1; decreased G-protein coupled receptor signaling pathway;, features a modification of the amino acid from R to Q at position 185.
+The protein's natural variant, known as in HYPOC1; increased G-protein coupled receptor signaling pathway;, features a modification of the amino acid from E to K at position 191.
+The protein's natural variant, known as in HHC1; decreased G-protein coupled receptor signaling pathway, features a modification of the amino acid from D to G at position 215.
+The protein's natural variant, known as in HHC1;, features a modification of the amino acid from R to W at position 220.
+The protein's natural variant, known as in HYPOC1;, features a modification of the amino acid from P to L at position 221.
+The protein's natural variant, known as in HHC1;, features a modification of the amino acid from P to Q at position 221.
+The protein's natural variant, known as in HHC1; decreased G-protein coupled receptor signaling pathway, features a modification of the amino acid from P to S at position 221.
+The protein's natural variant, known as in HHC1, features a modification of the amino acid from K to T at position 225.
+The protein's natural variant, known as in NSHPT; decreased G-protein coupled receptor signaling pathway; does not affect cell membrane localization;, features a modification of the amino acid from R to L at position 227.
+The protein's natural variant, known as in HHC1; G-protein coupled receptor signaling pathway; less markedly impaired relative to wild-type than L-227; does not affect cell membrane localization;, features a modification of the amino acid from R to Q at position 227.
+The protein's natural variant, known as in HYPOC1, features a modification of the amino acid from E to K at position 228.
+The protein's natural variant, known as in HHC1, features a modification of the amino acid from S to F at position 271.
+The protein's natural variant, known as in HHC1; decreased G-protein coupled receptor signaling pathway;, features a modification of the amino acid from E to K at position 297.
+The protein's natural variant, known as mutation found in a patient with primary hyperparathyroidism detected at adulthood; inactivating mutation; mutant CASR is activated by a higher calcium concentrations than the wild-type, features a modification of the amino acid from P to T at position 339.
+The protein's natural variant, known as in EIG8; patients present juvenile myoclonus epilepsy, features a modification of the amino acid from E to A at position 354.
+The protein's natural variant, known as in HHC1;, features a modification of the amino acid from G to R at position 397.
+The protein's natural variant, known as in HHC1; decreased G-protein coupled receptor signaling pathway; does not affect cell membrane localization, features a modification of the amino acid from Q to R at position 459.
+The protein's natural variant, known as in HHC1; loss-of-function mutation; the quantity of the mutant receptor is higher than that of the wild-type receptor; dose-response curves show that the mutation significantly reduces the sensitivity of the receptor to extracellular calcium concentrations;, features a modification of the amino acid from R to Q at position 465.
+The protein's natural variant, known as in HHC1;, features a modification of the amino acid from G to R at position 509.
+The protein's natural variant, known as in HHC1, features a modification of the amino acid from G to R at position 549.
+The protein's natural variant, known as in HHC1; decreased G-protein coupled receptor signaling pathway, features a modification of the amino acid from T to I at position 550.
+The protein's natural variant, known as in NSHPT; decreased G-protein coupled receptor signaling pathway; does not affect cell membrane localization;, features a modification of the amino acid from R to K at position 551.
+The protein's natural variant, known as in HHC1;, features a modification of the amino acid from G to R at position 553.
+The protein's natural variant, known as in HHC1;, features a modification of the amino acid from I to V at position 555.
+The protein's natural variant, known as in HHC1; Abolished G-protein coupled receptor activity, features a modification of the amino acid from G to E at position 557.
+The protein's natural variant, known as in HHC1, features a modification of the amino acid from C to Y at position 562.
+The protein's natural variant, known as in HHC1, features a modification of the amino acid from C to G at position 565.
+The protein's natural variant, known as in HYPOC1; increased G-protein coupled receptor signaling pathway, features a modification of the amino acid from P to H at position 569.
+The protein's natural variant, known as in HHC1; decreased G-protein coupled receptor signaling pathway; does not affect cell membrane localization, features a modification of the amino acid from G to W at position 571.
+The protein's natural variant, known as in HHC1;, features a modification of the amino acid from C to F at position 582.
+The protein's natural variant, known as in NSHPT and HHC1;, features a modification of the amino acid from C to Y at position 582.
+The protein's natural variant, known as in HYPOC1; there is a significant leftward shift in the concentration response curves for the effects of extracellular calcium on both intracellular calcium mobilization and MAPK activity;, features a modification of the amino acid from E to K at position 604.
+The protein's natural variant, known as in HYPOC1;, features a modification of the amino acid from F to S at position 612.
+The protein's natural variant, known as in HYPOC1; does not affect the total accumulation of inositol phosphates as a function of extracellular calcium concentrations in transfected cells;, features a modification of the amino acid from L to V at position 616.
+The protein's natural variant, known as in HHC1, features a modification of the amino acid from G to D at position 623.
+The protein's natural variant, known as in NSHPT, features a modification of the amino acid from L to P at position 650.
+The protein's natural variant, known as in HHC1, features a modification of the amino acid from S to Y at position 657.
+The protein's natural variant, known as in HHC1, features a modification of the amino acid from C to Y at position 661.
+The protein's natural variant, known as in NSHPT;, features a modification of the amino acid from G to E at position 670.
+The protein's natural variant, known as in HHC1, features a modification of the amino acid from G to R at position 670.
+The protein's natural variant, known as in HHC1;, features a modification of the amino acid from R to H at position 680.
+The protein's natural variant, known as in HYPOC1;, features a modification of the amino acid from Q to H at position 681.
+The protein's natural variant, known as in HYPOC1; increased G-protein coupled receptor signaling pathway; does not affect cell membrane localization, features a modification of the amino acid from Q to R at position 681.
+The protein's natural variant, known as in EIG8; patients present juvenile myoclonus epilepsy;, features a modification of the amino acid from I to V at position 686.
+The protein's natural variant, known as in NSHPT, features a modification of the amino acid from V to M at position 689.
+The protein's natural variant, known as in HHC1, features a modification of the amino acid from V to M at position 697.
+The protein's natural variant, known as in HHC1; decreased protein level, features a modification of the amino acid from E to V at position 707.
+The protein's natural variant, known as in HYPOC1; increased G-protein coupled receptor signaling pathway; does not affect cell membrane localization;, features a modification of the amino acid from L to Q at position 727.
+The protein's natural variant, known as in HHC1, features a modification of the amino acid from V to F at position 728.
+The protein's natural variant, known as in HHC1, features a modification of the amino acid from W to R at position 742.
+The protein's natural variant, known as in HHC1, features a modification of the amino acid from P to R at position 748.
+The protein's natural variant, known as in HYPOC1, features a modification of the amino acid from E to K at position 767.
+The protein's natural variant, known as in HYPOC1; the mutation shifts the concentration-response curve to the left and increases maximal activity;, features a modification of the amino acid from L to R at position 773.
+The protein's natural variant, known as in HHC1; decreased G-protein coupled receptor signaling pathway; does not affect cell membrane localization, features a modification of the amino acid from G to S at position 774.
+The protein's natural variant, known as in HYPOC1; leftward shift in the concentration-response curve for the mutant receptor; cells cotransfected with both the wild-type and the mutant receptor show an EC(50) similar to the mutant; a gain-of-function mutation rendering the receptor more sensitive than normal to activation;, features a modification of the amino acid from F to C at position 788.
+The protein's natural variant, known as in HYPOC1; induces a significant shift to the left relative to the wild-type protein in the MAPK response to increasing extracellular calcium concentrations;, features a modification of the amino acid from F to L at position 788.
+The protein's natural variant, known as in HHC1; decreased G-protein coupled receptor signaling pathway;, features a modification of the amino acid from R to W at position 795.
+The protein's natural variant, known as in HYPOC1; increased G-protein coupled receptor signaling pathway, features a modification of the amino acid from N to I at position 802.
+The protein's natural variant, known as in HHC1; decreased G-protein coupled receptor signaling pathway;, features a modification of the amino acid from N to S at position 802.
+The protein's natural variant, known as in HYPOC1; does not produce a significant activating effect; decreased cell surface receptor expression;, features a modification of the amino acid from F to S at position 806.
+The protein's natural variant, known as in HHC1; decreased G-protein coupled receptor signaling pathway;, features a modification of the amino acid from V to I at position 817.
+The protein's natural variant, known as in HYPOC1; the concentration-response curve of the mutant receptor is left-shifted and its EC(50) is significantly lower than that of the wild-type;, features a modification of the amino acid from S to F at position 820.
+The protein's natural variant, known as in HYPOC1, features a modification of the amino acid from G to S at position 830.
+The protein's natural variant, known as in HYPOC1, features a modification of the amino acid from F to L at position 832.
+The protein's natural variant, known as in HYPOC1, features a modification of the amino acid from F to S at position 832.
+The protein's natural variant, known as in HYPOC1; increased G-protein coupled receptor signaling pathway, features a modification of the amino acid from I to T at position 839.
+The protein's natural variant, known as in HYPOC1; also in HYPOC1 associated with clinical features of Bartter syndrome; shifts the concentration-response curve of calcium ions to the left;, features a modification of the amino acid from A to E at position 843.
+The protein's natural variant, known as probable disease-associated variant found in a patient with hypercalciuric hypercalcemia; mutant CASR has a right-shifted dose-response to extracellular calcium concentrations; activated by a higher calcium concentrations than the wild-type;, features a modification of the amino acid from F to L at position 881.
+The protein's natural variant, known as in HHC1, features a modification of the amino acid from R to W at position 886.
+The protein's natural variant, known as in EIG8;, features a modification of the amino acid from R to Q at position 898.
+The protein's natural variant, known as in HHC1; decreased G-protein coupled receptor signaling pathway;, features a modification of the amino acid from T to M at position 972.
+The protein's natural variant, known as associated with high serum level of calcium; is also a potential predisposing factor in disorders of bone and mineral metabolism;, features a modification of the amino acid from A to S at position 986.
+The protein's natural variant, known as in EIG8; patients present juvenile myoclonus epilepsy, features a modification of the amino acid from A to G at position 988.
+The protein's natural variant, known as in EIG8; patients present juvenile myoclonus epilepsy;, features a modification of the amino acid from A to V at position 988.
+The protein's natural variant, known as associated with low serum level of calcium;, features a modification of the amino acid from R to G at position 990.
+The protein's natural variant, known as found in a patient with primordial dwarfism; unknown pathological significance;, features a modification of the amino acid from R to W at position 98.
+The protein's natural variant, known as in TNDM1;, features a modification of the amino acid from R to H at position 166.
+The protein's natural variant, known as in TNDM1;, features a modification of the amino acid from H to N at position 193.
+The protein's natural variant, known as in TNDM1;, features a modification of the amino acid from H to D at position 374.
+The protein's natural variant, known as in tx mice, features a modification of the amino acid from M to V at position 1356.
+The protein's natural variant, known as in OI7; severe form;, features a modification of the amino acid from A to E at position 13.
+The protein's natural variant, known as in OI7;, features a modification of the amino acid from L to P at position 67.
+The protein's natural variant, known as in OI7; severe form;, features a modification of the amino acid from K to E at position 157.
+The protein's natural variant, known as in DHS1;, features a modification of the amino acid from G to S at position 718.
+The protein's natural variant, known as in DHS1;, features a modification of the amino acid from G to S at position 782.
+The protein's natural variant, known as in DHS1;, features a modification of the amino acid from R to Q at position 808.
+The protein's natural variant, known as in LMPHM6; unknown pathological significance;, features a modification of the amino acid from L to M at position 939.
+The protein's natural variant, known as in DHS1;, features a modification of the amino acid from S to L at position 1117.
+The protein's natural variant, known as in DHS1; gives rise to mechanically activated currents that inactivate more slowly than wild-type currents;, features a modification of the amino acid from R to P at position 1358.
+The protein's natural variant, known as in DHS1, features a modification of the amino acid from A to D at position 2003.
+The protein's natural variant, known as in DHS1; gives rise to mechanically activated currents that inactivate more slowly than wild-type currents;, features a modification of the amino acid from A to T at position 2020.
+The protein's natural variant, known as in DHS1;, features a modification of the amino acid from A to V at position 2020.
+The protein's natural variant, known as in DHS1; gives rise to mechanically activated currents that inactivate more slowly than wild-type currents;, features a modification of the amino acid from T to M at position 2127.
+The protein's natural variant, known as in DHS1; gives rise to mechanically activated currents that inactivate more slowly than wild-type currents;, features a modification of the amino acid from M to R at position 2225.
+The protein's natural variant, known as found in Er(5-) blood group phenotype that is associated with hemolytic disease of the fetus and newborn;, features a modification of the amino acid from R to Q at position 2245.
+The protein's natural variant, known as found in Er(a-b+) and Er(a-b-) blood group phenotypes;, features a modification of the amino acid from E to K at position 2392.
+The protein's natural variant, known as found in Er(a-b+) blood group phenotype;, features a modification of the amino acid from G to S at position 2394.
+The protein's natural variant, known as found in Er(4-) blood group phenotype that is associated with hemolytic disease of the fetus and newborn;, features a modification of the amino acid from E to K at position 2407.
+The protein's natural variant, known as found in Er(4-) blood group phenotype that is associated with hemolytic disease of the fetus and newborn;, features a modification of the amino acid from E to Q at position 2407.
+The protein's natural variant, known as in LMPHM6; unknown pathological significance;, features a modification of the amino acid from P to L at position 2430.
+The protein's natural variant, known as in LMPHM6; unknown pathological significance, features a modification of the amino acid from R to C at position 2456.
+The protein's natural variant, known as in DHS1; gives rise to mechanically activated currents that inactivate more slowly than wild-type currents;, features a modification of the amino acid from R to H at position 2456.
+The protein's natural variant, known as in LMPHM6; unknown pathological significance;, features a modification of the amino acid from F to L at position 2458.
+The protein's natural variant, known as in DHS1; increased cation transport in erythroid cells;, features a modification of the amino acid from R to Q at position 2488.
+The protein's natural variant, known as in DHS1; gives rise to mechanically activated currents that inactivate more slowly than wild-type currents, features a modification of the amino acid from E to ELE at position 2496.
+The protein's natural variant, known as in clone SE-P4, features a modification of the amino acid from L to M at position 85.
+The natural variant of this protein is characterized by an amino acid alteration from P to S at position 572.
+The protein's natural variant, known as in kidney, features a modification of the amino acid from S to P at position 2.
+The protein's natural variant, known as in kidney, features a modification of the amino acid from F to S at position 61.
+The protein's natural variant, known as in kidney, features a modification of the amino acid from D to H at position 71.
+The protein's natural variant, known as in kidney, features a modification of the amino acid from N to S at position 95.
+The protein's natural variant, known as in kidney, features a modification of the amino acid from Q to K at position 183.
+The protein's natural variant, known as in kidney, features a modification of the amino acid from P to T at position 346.
+The protein's natural variant, known as in kidney, features a modification of the amino acid from A to G at position 398.
+The protein's natural variant, known as in kidney, features a modification of the amino acid from VE to AT at position 415.
+The protein's natural variant, known as in kidney, features a modification of the amino acid from V to D at position 433.
+The protein's natural variant, known as in kidney, features a modification of the amino acid from K to L at position 475.
+The protein's natural variant, known as in kidney, features a modification of the amino acid from Q to L at position 488.
+The protein's natural variant, known as in strain: Arzag, features a modification of the amino acid from V to I at position 5.
+The protein's natural variant, known as in strain: Arzag, features a modification of the amino acid from M to T at position 32.
+The protein's natural variant, known as in haplotype 19, features a modification of the amino acid from G to S at position 188.
+The protein's natural variant, known as in haplotype 10, features a modification of the amino acid from D to N at position 239.
+The protein's natural variant, known as in haplotype 15, features a modification of the amino acid from V to I at position 253.
+The protein's natural variant, known as in haplotype 26, features a modification of the amino acid from VN to MK at position 378.
+The protein's natural variant, known as in ODCD1; due to a nucleotide substitution that causes in-frame exon 9 skipping or results in missense variant Y-410; patient cells contain both type of transcripts; the transcript lacking exon 9 is the most abundant;, features a modification of the amino acid from D to Y at position 410.
+The natural variant of this protein is characterized by an amino acid alteration from V to A at position 559.
+The protein's natural variant, known as in ODCD1; due to a nucleotide substitution that causes missplicing of exon 18 or results in missense variant V-1806; patient cells contain both type of transcripts; the transcript with the missense variant is the most abundant;, features a modification of the amino acid from M to V at position 1806.
+The protein's natural variant, known as in MC1DN11;, features a modification of the amino acid from T to P at position 207.
+The protein's natural variant, known as in MC1DN11;, features a modification of the amino acid from R to C at position 211.
+The protein's natural variant, known as in MC1DN11;, features a modification of the amino acid from G to R at position 245.
+The protein's natural variant, known as in MC1DN11; due to a nucleotide substitution located in the splice site consensus sequence at the end of exon 3; patient cells contain normally spliced transcripts corresponding to protein variant R-253 but also transcripts lacking the final 6 base pairs of exon 3 and corresponding to protein variant 252-VK-253 del;, features a modification of the amino acid from K to R at position 253.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to C at position 170.
+The protein's natural variant, known as in WTS; unknown pathological significance, features a modification of the amino acid from A to G at position 269.
+The protein's natural variant, known as in WTS; unknown pathological significance;, features a modification of the amino acid from R to W at position 415.
+The protein's natural variant, known as in EVMPS and LMPS;, features a modification of the amino acid from V to G at position 107.
+The protein's natural variant, known as in EVMPS and LMPS;, features a modification of the amino acid from R to C at position 239.
+The natural variant of this protein is characterized by an amino acid alteration from C to G at position 28.
+The protein's natural variant, known as in NRCLP7;, features a modification of the amino acid from S to C at position 133.
+The natural variant of this protein is characterized by an amino acid alteration from T to P at position 103.
+The protein's natural variant, known as in CTT-IA, features a modification of the amino acid from A to T at position 113.
+The natural variant of this protein is characterized by an amino acid alteration from L to F at position 322.
+The protein's natural variant, known as in COA; inactive;, features a modification of the amino acid from A to P at position 140.
+The protein's natural variant, known as in DIGC;, features a modification of the amino acid from S to P at position 193.
+The protein's natural variant, known as in SMDP3; unknown pathological significance, features a modification of the amino acid from R to L at position 43.
+The protein's natural variant, known as in SMDP3; loss of intracellular vesicle membrane location; loss of proteolytic cleavage; does not affect N-glycosylation; loss of ATP hydrolysis activity; decreases ATP binding in vitro;, features a modification of the amino acid from L to P at position 101.
+The protein's natural variant, known as in SMDP3; loss of lamellar bodies membrane location; loss of proteolytic cleavage; increases cellular free cholesterol and phosphatidylcholine transport; loss of vesicles formation; increases free cholesterol induced cell death; loss of protein oligomerization;, features a modification of the amino acid from Q to K at position 215.
+The protein's natural variant, known as in SMDP3; unknown pathological significance; does not affect protein oligomerization;, features a modification of the amino acid from R to C at position 280.
+The protein's natural variant, known as in SMDP3; unknown pathological significance; does not affect protein oligomerization;, features a modification of the amino acid from R to K at position 288.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from L to M at position 290.
+The protein's natural variant, known as in SMDP3; unknown pathological significance; does not affect lamellar bodies membrane location; does not affect proteolytic cleavage; affects lamellar bodies formation; does not affect cholesterol and phosphatidylcholine transport; decreases vesicles formation; does not affect free cholesterol induced cell death;, features a modification of the amino acid from E to V at position 292.
+The protein's natural variant, known as in SMDP3; does not affect location in intracellular vesicle membrane; does not affect proteolytic cleavage; does not affect N-glycosylation; loss of ATP hydrolysis activity; decreases ATP binding in vitro; does not affect protein expression; does not affect multivesicular bodies and lamellar bodies location; affects multivesicular bodies and lamellar bodies development; loss of phosphatidylcholine transport; does not affect cholesterol transport;, features a modification of the amino acid from N to D at position 568.
+The protein's natural variant, known as in SMDP3; unknown pathological significance, features a modification of the amino acid from L to P at position 579.
+The protein's natural variant, known as in SMDP3; unknown pathological significance;, features a modification of the amino acid from R to Q at position 605.
+The protein's natural variant, known as in SMDP3, features a modification of the amino acid from E to K at position 690.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from E to D at position 801.
+The protein's natural variant, known as in SMDP3; loss of intracellular vesicle membrane location; loss of proteolytic cleavage; does not affect N-glycosylation;, features a modification of the amino acid from L to P at position 982.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from H to Q at position 1069.
+The protein's natural variant, known as in SMDP3; unknown pathological significance, features a modification of the amino acid from N to K at position 1076.
+The protein's natural variant, known as in SMDP3;, features a modification of the amino acid from T to M at position 1114.
+The protein's natural variant, known as in SMDP3; does not affect intracellular vesicle membrane location; does not affect proteolytic cleavage; does not affect N-glycosylation; loss of ATP hydrolysis activity, features a modification of the amino acid from G to S at position 1221.
+The protein's natural variant, known as in SMDP3;, features a modification of the amino acid from P to L at position 1301.
+The protein's natural variant, known as in SMDP3; unknown pathological significance, features a modification of the amino acid from G to E at position 1302.
+The protein's natural variant, known as in SMDP3; decreases phosphatidylcholine transport; increases protein abundance; does not affect folding in the endoplasmic reticulum; decreases proteolytic processing; affects lamellar bodies development; reduces free cholesterol transport, features a modification of the amino acid from K to N at position 1388.
+The protein's natural variant, known as in SMDP3;, features a modification of the amino acid from V to M at position 1399.
+The protein's natural variant, known as in SMDP3; loss of intracellular vesicle membrane location; loss of proteolytic cleavage; does not affect N-glycosylation;, features a modification of the amino acid from L to P at position 1553.
+The protein's natural variant, known as in SMDP3; does not affect location in intracellular vesicle membrane; does not affect proteolytic cleavage; does not affect N-glycosylation; loss of ATP hydrolysis activity; decreases ATP binding in vitro; affects the intracellular vesicles development; decreases phosphatidylcholine transport, features a modification of the amino acid from L to P at position 1580.
+The protein's natural variant, known as in SMDP3; loss of intracellular vesicle membrane location; loss of proteolytic cleavage; does not affect N-glycosylation;, features a modification of the amino acid from Q to P at position 1591.
+The natural variant of this protein is characterized by an amino acid alteration from K to Q at position 850.
+The protein's natural variant, known as in RUS; unknown pathological significance;, features a modification of the amino acid from S to L at position 187.
+The protein's natural variant, known as in AOVD2; unknown pathological significance;, features a modification of the amino acid from G to A at position 204.
+The protein's natural variant, known as in RUS; unknown pathological significance;, features a modification of the amino acid from C to S at position 205.
+The protein's natural variant, known as in AOVD2; unknown pathological significance;, features a modification of the amino acid from R to G at position 231.
+The protein's natural variant, known as in AOVD2; unknown pathological significance;, features a modification of the amino acid from R to P at position 231.
+The protein's natural variant, known as in RUS; unknown pathological significance;, features a modification of the amino acid from S to N at position 267.
+The protein's natural variant, known as in CRS7; unknown pathological significance;, features a modification of the amino acid from E to K at position 287.
+The protein's natural variant, known as in CRS7; associated with disease susceptibility, features a modification of the amino acid from T to A at position 306.
+The protein's natural variant, known as in CRS7; associated with disease susceptibility;, features a modification of the amino acid from P to L at position 323.
+The protein's natural variant, known as found in a patient with congenital mitral valve prolapse;, features a modification of the amino acid from A to T at position 325.
+The protein's natural variant, known as in AOVD2; unknown pathological significance;, features a modification of the amino acid from A to E at position 335.
+The protein's natural variant, known as in RUS; unknown pathological significance;, features a modification of the amino acid from H to P at position 339.
+The protein's natural variant, known as in RUS; unknown pathological significance;, features a modification of the amino acid from Q to R at position 370.
+The protein's natural variant, known as in CRS7; associated with disease susceptibility; de novo mutation, features a modification of the amino acid from G to C at position 390.
+The protein's natural variant, known as in AOVD2; decreased inhibition of BMP signaling pathway, features a modification of the amino acid from I to IGI at position 391.
+The protein's natural variant, known as in AOVD2; decreased inhibition of BMP signaling pathway;, features a modification of the amino acid from P to L at position 415.
+The protein's natural variant, known as in CRS7; associated with disease susceptibility;, features a modification of the amino acid from R to C at position 465.
+The protein's natural variant, known as in RUS; unknown pathological significance;, features a modification of the amino acid from G to D at position 471.
+The protein's natural variant, known as in AOVD2; decreased inhibition of BMP signaling pathway;, features a modification of the amino acid from C to F at position 484.
+The protein's natural variant, known as in CRS7; associated with disease susceptibility;, features a modification of the amino acid from I to T at position 490.
+The protein's natural variant, known as in BARTS4B; a patient also carrying a mutation in CLCNKB;, features a modification of the amino acid from W to C at position 80.
+The protein's natural variant, known as in allele CYP2K1v2, features a modification of the amino acid from DI to GL at position 7.
+The protein's natural variant, known as in allele CYP2K1v2, features a modification of the amino acid from E to G at position 37.
+The protein's natural variant, known as in allele CYP2K1v2, features a modification of the amino acid from V to F at position 79.
+The protein's natural variant, known as in allele CYP2K1v2, features a modification of the amino acid from I to T at position 256.
+The protein's natural variant, known as in allele CYP2K1v2, features a modification of the amino acid from G to S at position 261.
+The protein's natural variant, known as in allele CYP2K1v2, features a modification of the amino acid from N to D at position 372.
+The protein's natural variant, known as in strain: Sigma 1278B, features a modification of the amino acid from Y to H at position 215.
+The protein's natural variant, known as in strain: Sigma 1278B, features a modification of the amino acid from L to P at position 221.
+The protein's natural variant, known as in strain: Sigma 1278B, features a modification of the amino acid from S to R at position 552.
+The protein's natural variant, known as in strain: Sigma 1278B, features a modification of the amino acid from A to T at position 674.
+The protein's natural variant, known as in strain: Sigma 1278B, features a modification of the amino acid from P to S at position 777.
+The protein's natural variant, known as in MFHIEN; creates a novel nonuniform expression pattern in the nucleus;, features a modification of the amino acid from G to D at position 177.
+The protein's natural variant, known as found in a patient with dilated cardiomyopathy and septo-optic dysplasia; unknown pathological significance;, features a modification of the amino acid from I to T at position 33.
+The protein's natural variant, known as in THPH5; reduced mutant protein levels and secretion, features a modification of the amino acid from L to H at position 15.
+The protein's natural variant, known as in THPH5; expresses very low/undetectable PROS1 levels compared to wild-type; has impaired secretion; intracellular degradation of unsecreted material is found, features a modification of the amino acid from V to E at position 18.
+The protein's natural variant, known as in THPH5;, features a modification of the amino acid from R to L at position 40.
+The protein's natural variant, known as in THPH5;, features a modification of the amino acid from R to H at position 41.
+The protein's natural variant, known as in THPH5;, features a modification of the amino acid from K to E at position 50.
+The protein's natural variant, known as in THPH5; does not affect PROS1 production but results in 15.2-fold reduced PROS1 activity; has 5.4 fold reduced affinity for anionic phospholipid vesicles (P < 0.0001) and decreased affinity for an antibody specific for the Ca(2+)-dependent conformation of the PROS1 Gla domain, features a modification of the amino acid from G to D at position 52.
+The protein's natural variant, known as in THPH5;, features a modification of the amino acid from E to A at position 67.
+The protein's natural variant, known as in THPH5, features a modification of the amino acid from A to D at position 68.
+The protein's natural variant, known as in THPH5, features a modification of the amino acid from F to C at position 72.
+The protein's natural variant, known as in THPH5; reduces expression of PROS1 by 33.2% (P < 0.001) and activity by 3.6-fold; has only a modest 1.5-fold (P < 0.001) reduced affinity for phospholipid and an antibody specific for the Ca(2+)-dependent conformation of the PROS1 Gla domain;, features a modification of the amino acid from T to M at position 78.
+The protein's natural variant, known as in THPH5;, features a modification of the amino acid from V to L at position 87.
+The protein's natural variant, known as in THPH5, features a modification of the amino acid from C to Y at position 88.
+The protein's natural variant, known as in THPH5; produces around 50% of PROS1 levels compared to wild-type; has impaired secretion; intracellular degradation of unsecreted material is found;, features a modification of the amino acid from R to C at position 90.
+The protein's natural variant, known as in THPH5;, features a modification of the amino acid from R to H at position 90.
+The protein's natural variant, known as in THPH5;, features a modification of the amino acid from G to E at position 95.
+The protein's natural variant, known as in THPH5; the activated protein cofactor activity is inhibited by C4BPB with a dose dependency similar to that of wild-type PROS1, features a modification of the amino acid from G to R at position 95.
+The protein's natural variant, known as in THPH5;, features a modification of the amino acid from R to C at position 101.
+The protein's natural variant, known as in THPH5, features a modification of the amino acid from R to S at position 111.
+The protein's natural variant, known as in THPH5, features a modification of the amino acid from C to Y at position 121.
+The protein's natural variant, known as in THPH5;, features a modification of the amino acid from D to G at position 129.
+The protein's natural variant, known as in THPH5;, features a modification of the amino acid from T to N at position 144.
+The protein's natural variant, known as in THPH5, features a modification of the amino acid from W to C at position 149.
+The protein's natural variant, known as in THPH5;, features a modification of the amino acid from D to G at position 157.
+The protein's natural variant, known as in THPH5, features a modification of the amino acid from C to G at position 161.
+The protein's natural variant, known as in THPH5, features a modification of the amino acid from N to Y at position 166.
+The protein's natural variant, known as in THPH5, features a modification of the amino acid from C to F at position 175.
+The protein's natural variant, known as in THPH5;, features a modification of the amino acid from C to Y at position 186.
+The protein's natural variant, known as in THPH5; Tokushima; the specific activity decreases to 58% of that of the wild-type PROS1; the activated protein cofactor activity is inhibited by C4BPB with a dose dependency similar to that of wild-type PROS1;, features a modification of the amino acid from K to E at position 196.
+The protein's natural variant, known as in THPH5, features a modification of the amino acid from E to G at position 204.
+The protein's natural variant, known as does not affect protein levels; the mutant is normally secreted;, features a modification of the amino acid from R to K at position 233.
+The protein's natural variant, known as in THPH6;, features a modification of the amino acid from Y to C at position 234.
+The protein's natural variant, known as in THPH5, features a modification of the amino acid from C to S at position 241.
+The protein's natural variant, known as in THPH5, features a modification of the amino acid from D to N at position 243.
+The protein's natural variant, known as in THPH5;, features a modification of the amino acid from D to G at position 245.
+The protein's natural variant, known as in THPH5, features a modification of the amino acid from C to G at position 247.
+The protein's natural variant, known as in THPH5;, features a modification of the amino acid from E to K at position 249.
+The protein's natural variant, known as in THPH5; produces around 30% of PROS1 levels compared to wild-type; has impaired secretion; intracellular degradation of unsecreted material is found;, features a modification of the amino acid from N to S at position 258.
+The protein's natural variant, known as in THPH5, features a modification of the amino acid from C to R at position 265.
+The protein's natural variant, known as in THPH5, features a modification of the amino acid from C to W at position 265.
+The protein's natural variant, known as in THPH5;, features a modification of the amino acid from Y to C at position 266.
+The protein's natural variant, known as in THPH5, features a modification of the amino acid from C to S at position 267.
+The protein's natural variant, known as in THPH5, features a modification of the amino acid from L to P at position 300.
+The protein's natural variant, known as in THPH5, features a modification of the amino acid from S to P at position 324.
+The protein's natural variant, known as in THPH5, features a modification of the amino acid from G to D at position 336.
+The protein's natural variant, known as in THPH5, features a modification of the amino acid from G to S at position 336.
+The protein's natural variant, known as in THPH5; expresses very low/undetectable PROS1 levels compared to wild-type; has impaired secretion; intracellular degradation of unsecreted material is found, features a modification of the amino acid from G to V at position 336.
+The protein's natural variant, known as in THPH5, features a modification of the amino acid from L to P at position 339.
+The protein's natural variant, known as in THPH5, features a modification of the amino acid from L to P at position 351.
+The protein's natural variant, known as in THPH5;, features a modification of the amino acid from R to H at position 355.
+The protein's natural variant, known as in THPH5;, features a modification of the amino acid from G to R at position 357.
+The protein's natural variant, known as in THPH5, features a modification of the amino acid from K to E at position 364.
+The protein's natural variant, known as in THPH5, features a modification of the amino acid from D to N at position 376.
+The protein's natural variant, known as in THPH5;, features a modification of the amino acid from G to D at position 381.
+The protein's natural variant, known as in THPH5, features a modification of the amino acid from G to V at position 381.
+The protein's natural variant, known as in THPH5, features a modification of the amino acid from W to R at position 383.
+The protein's natural variant, known as in THPH5, features a modification of the amino acid from E to K at position 390.
+The protein's natural variant, known as in THPH5, features a modification of the amino acid from L to P at position 446.
+The protein's natural variant, known as in THPH5, features a modification of the amino acid from C to S at position 449.
+The protein's natural variant, known as in THPH5, features a modification of the amino acid from C to R at position 475.
+The protein's natural variant, known as in THPH5, features a modification of the amino acid from G to C at position 482.
+The protein's natural variant, known as in THPH5;, features a modification of the amino acid from Y to C at position 485.
+The protein's natural variant, known as in THPH5;, features a modification of the amino acid from S to A at position 501.
+The protein's natural variant, known as variant Heerlen; could be associated with THPH5;, features a modification of the amino acid from S to P at position 501.
+The protein's natural variant, known as in THPH5, features a modification of the amino acid from V to G at position 508.
+The protein's natural variant, known as in THPH5, features a modification of the amino acid from V to M at position 508.
+The protein's natural variant, known as in THPH5; secretion of the mutant markedly decreased compared with that of the wild-type; intracellular degradation and impaired secretion of the mutant;, features a modification of the amino acid from R to C at position 515.
+The protein's natural variant, known as in THPH5, features a modification of the amino acid from R to P at position 515.
+The protein's natural variant, known as in THPH5, features a modification of the amino acid from G to D at position 521.
+The protein's natural variant, known as in THPH5, features a modification of the amino acid from A to P at position 525.
+The protein's natural variant, known as in THPH5, features a modification of the amino acid from L to S at position 526.
+The protein's natural variant, known as in THPH5;, features a modification of the amino acid from T to A at position 532.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from E to G at position 545.
+The protein's natural variant, known as in THPH5, features a modification of the amino acid from L to S at position 552.
+The protein's natural variant, known as in THPH5;, features a modification of the amino acid from R to G at position 561.
+The protein's natural variant, known as in THPH5; unknown pathological significance;, features a modification of the amino acid from I to L at position 562.
+The protein's natural variant, known as in THPH5, features a modification of the amino acid from C to Y at position 568.
+The protein's natural variant, known as in THPH5, features a modification of the amino acid from L to R at position 575.
+The protein's natural variant, known as in THPH5, features a modification of the amino acid from L to Q at position 584.
+The protein's natural variant, known as in THPH5, features a modification of the amino acid from M to K at position 611.
+The protein's natural variant, known as in THPH5;, features a modification of the amino acid from M to T at position 611.
+The protein's natural variant, known as in THPH5, features a modification of the amino acid from A to P at position 616.
+The protein's natural variant, known as in THPH5, features a modification of the amino acid from L to R at position 622.
+The protein's natural variant, known as in THPH5; the activated protein cofactor activity is inhibited by C4BPB with a dose dependency similar to that of wild-type PROS1;, features a modification of the amino acid from T to I at position 630.
+The protein's natural variant, known as in THPH5; shows intracellular degradation and decreased secretion;, features a modification of the amino acid from Y to C at position 636.
+The protein's natural variant, known as in THPH5, features a modification of the amino acid from G to D at position 638.
+The protein's natural variant, known as in THPH5, features a modification of the amino acid from C to F at position 639.
+The protein's natural variant, known as in THPH5, features a modification of the amino acid from C to Y at position 639.
+The protein's natural variant, known as in THPH5; does not affect protein levels; the mutant is secreted at lower levels compared to wild-type, features a modification of the amino acid from M to T at position 640.
+The protein's natural variant, known as in THPH5, features a modification of the amino acid from I to S at position 644.
+The protein's natural variant, known as in THPH5; expresses very low/undetectable PROS1 levels compared to wild-type; has impaired secretion; intracellular degradation of unsecreted material is found, features a modification of the amino acid from H to P at position 664.
+The protein's natural variant, known as in THPH5;, features a modification of the amino acid from S to L at position 665.
+The protein's natural variant, known as in THPH5;, features a modification of the amino acid from C to R at position 666.
+The protein's natural variant, known as in THPH5;, features a modification of the amino acid from P to L at position 667.
+The protein's natural variant, known as in OPTB2;, features a modification of the amino acid from M to K at position 199.
+The natural variant of this protein is characterized by an amino acid alteration from C to Y at position 21.
+The natural variant of this protein is characterized by an amino acid alteration from S to H at position 74.
+The natural variant of this protein is characterized by an amino acid alteration from F to Y at position 76.
+The natural variant of this protein is characterized by an amino acid alteration from C to S at position 109.
+The protein's natural variant, known as in strain: Persimi42 and Persimi50, features a modification of the amino acid from A to E at position 200.
+The protein's natural variant, known as in strain: Persimi42 and Persimi50, features a modification of the amino acid from T to S at position 204.
+The protein's natural variant, known as in strain: Persimi40 and Persimi42, features a modification of the amino acid from Q to K at position 222.
+The protein's natural variant, known as in 6B4-2, features a modification of the amino acid from F to L at position 17.
+The protein's natural variant, known as in 6B4-2, features a modification of the amino acid from F to I at position 160.
+The protein's natural variant, known as in 6B4-2, features a modification of the amino acid from I to L at position 229.
+The protein's natural variant, known as in 6B4-2, features a modification of the amino acid from L to F at position 286.
+The protein's natural variant, known as in 6B4-2, features a modification of the amino acid from N to S at position 477.
+The protein's natural variant, known as in 6B4-2, features a modification of the amino acid from K to T at position 481.
+The protein's natural variant, known as in 6B4-2, features a modification of the amino acid from I to L at position 496.
+The protein's natural variant, known as in an extended family with high risk of late-onset Alzheimer Disease;, features a modification of the amino acid from S to C at position 1038.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from K to M at position 1289.
+The protein's natural variant, known as in SDLT;, features a modification of the amino acid from K to E at position 204.
+The protein's natural variant, known as in MCT1D;, features a modification of the amino acid from R to Q at position 313.
+The protein's natural variant, known as in SDLT;, features a modification of the amino acid from G to R at position 472.
+The natural variant of this protein is characterized by an amino acid alteration from E to K at position 574.
+The protein's natural variant, known as in A1, B(C) and AMY-2.2Y, features a modification of the amino acid from V to I at position 64.
+The protein's natural variant, known as in AMY-2.2Y, features a modification of the amino acid from V to I at position 66.
+The protein's natural variant, known as in A1, B(A) and B(C), features a modification of the amino acid from A to S at position 120.
+The protein's natural variant, known as in A1, B(A) and B(C); requires 2 nucleotide substitutions, features a modification of the amino acid from D to S at position 161.
+The protein's natural variant, known as in A1 and B(C), features a modification of the amino acid from L to V at position 174.
+The protein's natural variant, known as in B(A), features a modification of the amino acid from T to S at position 175.
+The protein's natural variant, known as in A1 and B(C), features a modification of the amino acid from I to V at position 254.
+The protein's natural variant, known as in A1 and B(C), features a modification of the amino acid from YGA to FGV at position 272.
+The protein's natural variant, known as in A1, B(A) and B(C), features a modification of the amino acid from L to M at position 298.
+The protein's natural variant, known as in B(A), features a modification of the amino acid from S to A at position 322.
+The protein's natural variant, known as in B1, features a modification of the amino acid from S to A at position 419.
+The protein's natural variant, known as in B(C), features a modification of the amino acid from A to E at position 450.
+The protein's natural variant, known as in C and C', features a modification of the amino acid from L to F at position 3.
+The protein's natural variant, known as in strain: CLIB 219, features a modification of the amino acid from V to I at position 8.
+The protein's natural variant, known as in strain: CLIB 219, CLIB 410, CLIB 413 and YIIc17 haplotype Ha2, features a modification of the amino acid from I to L at position 30.
+The protein's natural variant, known as in strain: YIIc12 and YIIc17 haplotype Ha1, features a modification of the amino acid from T to A at position 92.
+The protein's natural variant, known as in strain: YIIc17 haplotype Ha2, features a modification of the amino acid from K to N at position 216.
+The natural variant of this protein is characterized by an amino acid alteration from T to A at position 243.
+The protein's natural variant, known as in HSAN5; uncertain pathological significance, features a modification of the amino acid from E to EGE at position 162.
+The protein's natural variant, known as found in a patient with congenital insensitivity to pain; uncertain pathological significance, features a modification of the amino acid from S to N at position 187.
+The protein's natural variant, known as in HSAN5; impaired processing of the precursor to mature NGF; nearly abolishes secretion; loss of function in stimulating cell differentiation; loss of the ability to activate the NTRK1 receptor;, features a modification of the amino acid from R to W at position 221.
+The protein's natural variant, known as in PEBEL1;, features a modification of the amino acid from A to D at position 94.
+The protein's natural variant, known as in PEBEL1;, features a modification of the amino acid from D to V at position 218.
+The protein's natural variant, known as in CILD17; unknown pathological significance; hypomorphic variant; reduced cilia beat amplitude in homozygous nasal respiratory cells; does not fully rescue abnormal phenotype in a zebrafish animal model;, features a modification of the amino acid from H to P at position 154.
+The protein's natural variant, known as in clone PH-2D-1, features a modification of the amino acid from Q to L at position 212.
+The protein's natural variant, known as in clone PH-2D-1, features a modification of the amino acid from V to G at position 285.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from R to C at position 620.
+The protein's natural variant, known as in allele E*01:01;, features a modification of the amino acid from G to R at position 128.
+The protein's natural variant, known as in allele E*01:04;, features a modification of the amino acid from R to G at position 178.
+The protein's natural variant, known as in MDDGA12; loss of kinase activity;, features a modification of the amino acid from L to R at position 137.
+The protein's natural variant, known as in MDDGA12;, features a modification of the amino acid from Q to R at position 258.
+The protein's natural variant, known as in MDDGA12;, features a modification of the amino acid from V to D at position 302.
+The protein's natural variant, known as in a lung small cell carcinoma sample; somatic mutation, features a modification of the amino acid from M to I at position 342.
+The protein's natural variant, known as in NEDLBA; unknown pathological significance;, features a modification of the amino acid from G to V at position 60.
+The protein's natural variant, known as in NEDLBA; loss of phosphatase activity in an in vitro assay; strong decrease in C-terminal methylation; decreased interaction with PP2A subunit APPP2R1A/PPP2R1B; loss of interaction with PP2A subunit B component PPP2R2A; decreased interaction with PP2A subunit B components PPP2R5A, PPP2R5B, PPP2R5E, PPP2R3A and STRN3;, features a modification of the amino acid from D to G at position 88.
+The protein's natural variant, known as in NEDLBA; decreased phosphatase activity in an in vitro assay; no effect on the interaction with PP2A subunit APPP2R1A/PPP2R1B; increased interaction with PP2A subunit B component STRN3; no effect on interaction with other PP2A subunit B components;, features a modification of the amino acid from Q to H at position 122.
+The protein's natural variant, known as in NEDLBA; almost complete loss of phosphatase activity in an in vitro assay; strong decrease in C-terminal methylation; no effect on the interaction with PP2A subunit APPP2R1A/PPP2R1B; decreased interaction with PP2A subunit B components PPP2R5A, PPP2R5B, PPP2R5C, PPP2R5D, PPP2R5E and PPP2R3A; no effect on interaction with PP2A subunit B component PPP2R2A;, features a modification of the amino acid from Y to C at position 127.
+The protein's natural variant, known as in NEDLBA; increased phosphatase activity in an in vitro assay; no effect on C-terminal methylation; decreased interaction with PP2A subunit APPP2R1A/PPP2R1B; loss of interaction with PP2A subunit B components PPP2R5A, PPP2R5B, PPP2R5C, PPP2R5D and PPP2R5E; no effect on interaction with PP2A subunit B components PPP2R2A and PPP2R3A;, features a modification of the amino acid from D to H at position 131.
+The protein's natural variant, known as in NEDLBA; decreased phosphatase activity in an in vitro assay; no effect on the interaction with PP2A subunit APPP2R1A/PPP2R1B; decreased interaction with PP2A subunit B component PPP2R5D; increased interaction with PP2A subunit B component STRN3; no effect on interaction with other PP2A subunit B components;, features a modification of the amino acid from H to R at position 191.
+The protein's natural variant, known as in NEDLBA; decreased phosphatase activity in an in vitro assay; no effect on C-terminal methylation; no effect on the interaction with PP2A subunit APPP2R1A/PPP2R1B; no effect on interaction with PP2A subunit B components;, features a modification of the amino acid from D to H at position 223.
+The protein's natural variant, known as in NEDLBA; no effect on phosphatase activity in an in vitro assay; no effect on the interaction with PP2A subunit APPP2R1A/PPP2R1B; no effect on interaction with PP2A subunit B components;, features a modification of the amino acid from D to V at position 223.
+The protein's natural variant, known as in NEDLBA; severe decrease in phosphatase activity in an in vitro assay; strong decrease in C-terminal methylation; decreased interaction with PP2A subunit APPP2R1A/PPP2R1B; loss of interaction with PP2A subunit B components PPP2R2A, PPP2R5A, PPP2R5B, PPP2R5E, PPP2R3A and STRN3; decreased interaction with PP2A subunit B components PPP2R5C and PPP2R5D;, features a modification of the amino acid from Y to C at position 265.
+The protein's natural variant, known as in NEDLBA; almost complete loss of phosphatase activity in an in vitro assay; decreased interaction with PP2A subunit APPP2R1A/PPP2R1B; strongly decreased interaction with PP2A subunit B components PPP2R2A and PPP2R3A; increased interaction with PP2A subunit B component STRN3; no effect on interaction with PP2A subunit B components PPP2R5A, PPP2R5B, PPP2R5C, PPP2R5D and PPP2R5E, features a modification of the amino acid from F to FF at position 308.
+The protein's natural variant, known as in allele ALS3-2, features a modification of the amino acid from Y to F at position 628.
+The protein's natural variant, known as in allele ALS3-2, features a modification of the amino acid from I to V at position 634.
+The protein's natural variant, known as in allele ALS3-2, features a modification of the amino acid from E to G at position 640.
+The protein's natural variant, known as in allele ALS3-2, features a modification of the amino acid from L to I at position 645.
+The protein's natural variant, known as in allele ALS3-1, features a modification of the amino acid from G to E at position 676.
+The protein's natural variant, known as in allele ALS3-1, features a modification of the amino acid from II to VT at position 815.
+The protein's natural variant, known as in allele ALS3-1, features a modification of the amino acid from E to G at position 820.
+The protein's natural variant, known as in allele ALS3-1, features a modification of the amino acid from S to P at position 843.
+The protein's natural variant, known as in allele ALS3-1, features a modification of the amino acid from A to T at position 847.
+The protein's natural variant, known as in allele ALS3-1, features a modification of the amino acid from T to I at position 851.
+The protein's natural variant, known as in allele ALS3-1, features a modification of the amino acid from T to S at position 935.
+The protein's natural variant, known as in allele ALS3-1, features a modification of the amino acid from F to V at position 963.
+The protein's natural variant, known as in allele ALS3-1, features a modification of the amino acid from Q to P at position 1062.
+The protein's natural variant, known as in a medulloblastoma sample; somatic mutation; loss of ability to induce apoptosis;, features a modification of the amino acid from S to L at position 34.
+The protein's natural variant, known as in CMT2A1;, features a modification of the amino acid from Q to L at position 98.
+The protein's natural variant, known as confers susceptibility to neuroblastoma; found as germline mutation in a neuroblastoma patient; loss of ability to induce apoptosis;, features a modification of the amino acid from E to V at position 692.
+The protein's natural variant, known as confers susceptibility to neuroblastoma; found as germline mutation in a neuroblastoma patient; loss of ability to induce apoptosis;, features a modification of the amino acid from T to I at position 873.
+The protein's natural variant, known as confers susceptibility to neuroblastoma; found as germline mutation in a neuroblastoma patient; loss of ability to induce apoptosis;, features a modification of the amino acid from P to S at position 1263.
+The protein's natural variant, known as confers susceptibility to pheochromocytoma; found as germline mutation in a pheochromocytoma family; loss of ability to induce apoptosis;, features a modification of the amino acid from S to N at position 1527.
+The protein's natural variant, known as in a pheochromocytoma sample; loss of ability to induce apoptosis;, features a modification of the amino acid from E to K at position 1674.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to H at position 3.
+The protein's natural variant, known as in a lung small cell carcinoma sample; somatic mutation, features a modification of the amino acid from L to R at position 514.
+The protein's natural variant, known as in variant 1A, features a modification of the amino acid from S to E at position 91.
+The protein's natural variant, known as in strain: WSII16, features a modification of the amino acid from N to S at position 148.
+The protein's natural variant, known as in strain: WSII16, features a modification of the amino acid from A to V at position 190.
+The protein's natural variant, known as in strain: SENGWA2, SENGWA22, SENGWA29, SENGWA32, SENGWA37, SENGWA51, WSII19 and WSII49, features a modification of the amino acid from T to S at position 198.
+The protein's natural variant, known as in strain: WSII6, features a modification of the amino acid from E to G at position 231.
+The protein's natural variant, known as in strain: SENGWA2, SENGWA29, SENGWA32, SENGWA51, WSII19 and WSII49, features a modification of the amino acid from Q to QSQ at position 253.
+The protein's natural variant, known as in strain: WSII6, features a modification of the amino acid from E to G at position 307.
+The protein's natural variant, known as in strain: WSII16, features a modification of the amino acid from I to F at position 316.
+The protein's natural variant, known as in strain: SENGWA37, features a modification of the amino acid from K to T at position 325.
+The protein's natural variant, known as in strain: SENGWA30, features a modification of the amino acid from S to P at position 335.
+The protein's natural variant, known as in strain: SENGWA2, SENGWA22, SENGWA29, SENGWA30, SENGWA32, SENGWA37, SENGWA51, WSII16, WSII19 and WSII49, features a modification of the amino acid from Q to QLLREAQQK at position 352.
+The protein's natural variant, known as in strain: WSII1, features a modification of the amino acid from F to HQN at position 385.
+The protein's natural variant, known as in strain: WSII16, features a modification of the amino acid from V to I at position 430.
+The protein's natural variant, known as in strain: Canton-S, SENGWA2, SENGWA22, SENGWA29, SENGWA32 and SENGWA51, features a modification of the amino acid from L to F at position 464.
+The protein's natural variant, known as in strain: WSII6, features a modification of the amino acid from E to G at position 496.
+The protein's natural variant, known as in strain: SENGWA22, SENGWA29, SENGWA37 and SENGWA51, features a modification of the amino acid from L to V at position 507.
+The protein's natural variant, known as in strain: WSII16, features a modification of the amino acid from L to Q at position 575.
+The protein's natural variant, known as in strain: WSII26 and WSII49, features a modification of the amino acid from S to I at position 601.
+The protein's natural variant, known as in strain: SENGWA30, features a modification of the amino acid from E to K at position 613.
+The protein's natural variant, known as in strain: SENGWA22, SENGWA30 and WSII16, features a modification of the amino acid from P to A at position 650.
+The protein's natural variant, known as in strain: SENGWA29, SENGWA30, SENGWA37 and SENGWA51, features a modification of the amino acid from L to V at position 666.
+The protein's natural variant, known as in strain: SENGWA29, SENGWA30, SENGWA37 and SENGWA51, features a modification of the amino acid from G to E at position 670.
+The protein's natural variant, known as in strain: SENGWA37 and SENGWA51, features a modification of the amino acid from T to A at position 758.
+The protein's natural variant, known as in strain: WSII26, features a modification of the amino acid from Q to E at position 830.
+The protein's natural variant, known as in strain: WSII16, features a modification of the amino acid from Q to R at position 844.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from V to M at position 48.
+The protein's natural variant, known as decreased bis(monoacylglycero)phosphate (BMP) hydrolase activity;, features a modification of the amino acid from R to H at position 113.
+The protein's natural variant, known as loss of bis(monoacylglycero)phosphate (BMP) hydrolase activity;, features a modification of the amino acid from S to C at position 148.
+The protein's natural variant, known as loss of bis(monoacylglycero)phosphate (BMP) hydrolase activity;, features a modification of the amino acid from P to L at position 204.
+The protein's natural variant, known as loss of lipase activity;, features a modification of the amino acid from T to P at position 206.
+The protein's natural variant, known as decreased bis(monoacylglycero)phosphate (BMP) hydrolase activity;, features a modification of the amino acid from G to V at position 231.
+The natural variant of this protein is characterized by an amino acid alteration from I to K at position 63.
+The natural variant of this protein is characterized by an amino acid alteration from L to K at position 70.
+The protein's natural variant, known as confers ciprofloxacin resistance, in clinical isolate, features a modification of the amino acid from A to V at position 90.
+The protein's natural variant, known as confers ciprofloxacin resistance, in clinical isolate, features a modification of the amino acid from S to P at position 91.
+The protein's natural variant, known as confers ciprofloxacin resistance, in clinical isolate, features a modification of the amino acid from D to A at position 94.
+The protein's natural variant, known as confers ciprofloxacin resistance, in clinical isolate, features a modification of the amino acid from D to G at position 94.
+The protein's natural variant, known as confers ciprofloxacin resistance, in clinical isolate, features a modification of the amino acid from D to H at position 94.
+The protein's natural variant, known as confers ciprofloxacin resistance, in clinical isolate, features a modification of the amino acid from D to N at position 94.
+The protein's natural variant, known as confers ciprofloxacin resistance, in clinical isolate, features a modification of the amino acid from D to Y at position 94.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from S to T at position 407.
+The natural variant of this protein is characterized by an amino acid alteration from E to T at position 15.
+The natural variant of this protein is characterized by an amino acid alteration from K to V at position 16.
+The natural variant of this protein is characterized by an amino acid alteration from T to L at position 19.
+The natural variant of this protein is characterized by an amino acid alteration from K to R at position 33.
+The protein's natural variant, known as in strain: Czech II, features a modification of the amino acid from T to R at position 61.
+The protein's natural variant, known as in strain: Czech II, features a modification of the amino acid from G to S at position 280.
+The protein's natural variant, known as in strain: Czech II, features a modification of the amino acid from G to E at position 293.
+The protein's natural variant, known as in strain: Czech II, features a modification of the amino acid from G to S at position 638.
+The protein's natural variant, known as in strain: Czech II, features a modification of the amino acid from K to T at position 819.
+The protein's natural variant, known as in strain: Czech II, features a modification of the amino acid from A to T at position 829.
+The protein's natural variant, known as in strain: Czech II, features a modification of the amino acid from T to A at position 859.
+The protein's natural variant, known as in strain: C57BL/6, features a modification of the amino acid from R to S at position 2065.
+The protein's natural variant, known as in HH6; phenotype consistent with normosmic idiopathic hypogonadotropic hypogonadism;, features a modification of the amino acid from H to N at position 14.
+The protein's natural variant, known as in HH6; phenotype consistent with Kallmann syndrome;, features a modification of the amino acid from P to L at position 26.
+The protein's natural variant, known as in HH6; phenotype consistent with normosmic idiopathic hypogonadotropic hypogonadism; some patients also carry mutations in FGFR1;, features a modification of the amino acid from F to L at position 40.
+The protein's natural variant, known as in HH6; phenotype consistent with normosmic idiopathic hypogonadotropic hypogonadism; some patients also carry mutations in FGFR1;, features a modification of the amino acid from K to E at position 89.
+The protein's natural variant, known as in HH6; phenotype consistent with Kallmann syndrome;, features a modification of the amino acid from R to G at position 116.
+The protein's natural variant, known as in HH6; phenotype consistent with normosmic idiopathic hypogonadotropic hypogonadism;, features a modification of the amino acid from T to M at position 218.
+The protein's natural variant, known as in SEMDK; decreased protein expression; decreased kinase activity; no effect on the interaction with DEPTOR, MLST8/GbetaL, RICTOR and RPTOR;, features a modification of the amino acid from R to C at position 187.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from H to L at position 389.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from A to V at position 1161.
+The natural variant of this protein is characterized by an amino acid alteration from M to T at position 198.
+The natural variant of this protein is characterized by an amino acid alteration from I to L at position 219.
+The protein's natural variant, known as in strain: cv. Be-0, cv. Kl-0, cv. Tac-0 and cv. Wassilewskija, features a modification of the amino acid from G to A at position 21.
+The protein's natural variant, known as in strain: CWL029 and TW-183, features a modification of the amino acid from R to Q at position 132.
+The protein's natural variant, known as in FBP1D; unknown pathological significance;, features a modification of the amino acid from R to W at position 158.
+The protein's natural variant, known as in FBP1D;, features a modification of the amino acid from G to S at position 164.
+The protein's natural variant, known as in FBP1D;, features a modification of the amino acid from A to D at position 177.
+The protein's natural variant, known as in FBP1D;, features a modification of the amino acid from F to S at position 194.
+The protein's natural variant, known as in FBP1D;, features a modification of the amino acid from P to R at position 284.
+The natural variant of this protein is characterized by an amino acid alteration from V to A at position 325.
+The protein's natural variant, known as in a glioblastoma multiforme sample; somatic mutation, features a modification of the amino acid from S to N at position 106.
+The protein's natural variant, known as in PXE; acts as a modifier of disease severity; more frequent in patients with a severe disease course;, features a modification of the amino acid from T to R at position 801.
+The protein's natural variant, known as in HYCHL; severe decrease of activity in the presence of physiological NaCl concentrations; no effect on localization to cell membrane;, features a modification of the amino acid from H to Q at position 121.
+The protein's natural variant, known as in HYCHL; severe decrease of activity in the presence of physiological NaCl concentrations; mutant enzyme is highly inhibited by acetazolamide and shows higher sensitivity to inhibition by anions compared to wild-type; the mutation affects the chloride-mediated negative feedback regulation of the enzyme leading to excessive chloride secretion in sweat; no effect on localization to cell membrane;, features a modification of the amino acid from E to K at position 143.
+The protein's natural variant, known as in strain: 789, features a modification of the amino acid from V to I at position 8.
+The protein's natural variant, known as in strain: A-20, features a modification of the amino acid from V to L at position 193.
+The protein's natural variant, known as in strain: 789, features a modification of the amino acid from G to S at position 308.
+The protein's natural variant, known as in cy; loss of ability to self-associate, does not affect interaction with Bicc1; loss of interaction with ANKS3, features a modification of the amino acid from R to W at position 823.
+The protein's natural variant, known as in a breast infiltrating ductal carcinoma sample; somatic mutation;, features a modification of the amino acid from G to A at position 11.
+The protein's natural variant, known as in OCRL;, features a modification of the amino acid from F to S at position 242.
+The protein's natural variant, known as in OCRL;, features a modification of the amino acid from I to T at position 274.
+The protein's natural variant, known as in OCRL;, features a modification of the amino acid from Q to R at position 277.
+The protein's natural variant, known as in DENT2 and OCRL;, features a modification of the amino acid from R to C at position 318.
+The protein's natural variant, known as in OCRL; associated with I-361;, features a modification of the amino acid from R to C at position 337.
+The protein's natural variant, known as in OCRL, features a modification of the amino acid from R to P at position 337.
+The protein's natural variant, known as in DENT2;, features a modification of the amino acid from N to H at position 354.
+The protein's natural variant, known as in OCRL; uncertain pathological significance;, features a modification of the amino acid from G to E at position 357.
+The protein's natural variant, known as in OCRL; associated with C-337;, features a modification of the amino acid from R to I at position 361.
+The protein's natural variant, known as in OCRL;, features a modification of the amino acid from V to G at position 372.
+The protein's natural variant, known as in OCRL;, features a modification of the amino acid from N to Y at position 373.
+The protein's natural variant, known as in OCRL;, features a modification of the amino acid from S to F at position 374.
+The protein's natural variant, known as in OCRL;, features a modification of the amino acid from H to Y at position 375.
+The protein's natural variant, known as in OCRL;, features a modification of the amino acid from H to R at position 414.
+The protein's natural variant, known as in OCRL;, features a modification of the amino acid from G to E at position 421.
+The protein's natural variant, known as in OCRL;, features a modification of the amino acid from N to D at position 424.
+The protein's natural variant, known as in OCRL;, features a modification of the amino acid from D to G at position 451.
+The protein's natural variant, known as in OCRL;, features a modification of the amino acid from D to N at position 451.
+The protein's natural variant, known as in OCRL;, features a modification of the amino acid from R to G at position 457.
+The protein's natural variant, known as in OCRL;, features a modification of the amino acid from F to S at position 463.
+The protein's natural variant, known as in OCRL;, features a modification of the amino acid from E to G at position 468.
+The protein's natural variant, known as in OCRL;, features a modification of the amino acid from E to K at position 468.
+The protein's natural variant, known as in DENT2;, features a modification of the amino acid from Y to C at position 479.
+The protein's natural variant, known as in DENT2;, features a modification of the amino acid from R to W at position 493.
+The protein's natural variant, known as in OCRL, features a modification of the amino acid from P to L at position 495.
+The protein's natural variant, known as in OCRL;, features a modification of the amino acid from C to Y at position 498.
+The protein's natural variant, known as in OCRL;, features a modification of the amino acid from D to H at position 499.
+The protein's natural variant, known as in OCRL;, features a modification of the amino acid from R to G at position 500.
+The protein's natural variant, known as in OCRL;, features a modification of the amino acid from R to Q at position 500.
+The protein's natural variant, known as in OCRL;, features a modification of the amino acid from W to R at position 503.
+The protein's natural variant, known as in OCRL;, features a modification of the amino acid from V to D at position 508.
+The protein's natural variant, known as in OCRL;, features a modification of the amino acid from Y to C at position 513.
+The protein's natural variant, known as in OCRL;, features a modification of the amino acid from S to R at position 522.
+The protein's natural variant, known as in OCRL;, features a modification of the amino acid from H to Q at position 524.
+The protein's natural variant, known as in OCRL;, features a modification of the amino acid from H to R at position 524.
+The protein's natural variant, known as in OCRL;, features a modification of the amino acid from P to L at position 526.
+The protein's natural variant, known as in OCRL, features a modification of the amino acid from I to S at position 533.
+The protein's natural variant, known as in OCRL;, features a modification of the amino acid from N to K at position 591.
+The protein's natural variant, known as in OCRL; uncertain pathological significance; abolishes FAM109A-, FAM109B- and APPL1-binding, features a modification of the amino acid from I to N at position 768.
+The protein's natural variant, known as in OCRL; uncertain pathological significance;, features a modification of the amino acid from A to P at position 797.
+The protein's natural variant, known as in DENT2, features a modification of the amino acid from P to L at position 799.
+The protein's natural variant, known as in OCRL, features a modification of the amino acid from P to L at position 801.
+The protein's natural variant, known as in OCRL;, features a modification of the amino acid from L to R at position 891.
+The protein's natural variant, known as in strain: New Caledonia, features a modification of the amino acid from G to N at position 45.
+The protein's natural variant, known as in strain: New Caledonia, features a modification of the amino acid from L to S at position 58.
+The protein's natural variant, known as in BSD, features a modification of the amino acid from R to Q at position 560.
+The protein's natural variant, known as may be associated with an increased risk for prostate cancer; associated with decreased activity;, features a modification of the amino acid from I to V at position 102.
+The protein's natural variant, known as in allozyme B; increased arylesterase activity;, features a modification of the amino acid from Q to R at position 192.
+The protein's natural variant, known as in SAVI;, features a modification of the amino acid from V to L at position 147.
+The protein's natural variant, known as in SAVI;, features a modification of the amino acid from N to S at position 154.
+The protein's natural variant, known as in SAVI; constitutively active mutant that promotes the production of type I interferon in absence of cGAMP ligand;, features a modification of the amino acid from V to M at position 155.
+The protein's natural variant, known as activated by both 2'-3' linked cGAMP and 3'-3' linked cGAMP;, features a modification of the amino acid from H to R at position 232.
+The protein's natural variant, known as probable disease-associated variant found in a 9-month-old patient who died following a fever and severe neck abscess without indication of any severe bacterial infection; may affect splicing; constitutively active mutant that promotes the production of type I interferon in absence of cyclic dinucleotide ligand; localizes to the perinuclear region in absence of cyclic dinucleotide ligand, features a modification of the amino acid from R to S at position 284.
+The protein's natural variant, known as can cooperate with an activated Ras to transform fibroblasts, features a modification of the amino acid from A to V at position 135.
+The protein's natural variant, known as in clone P53-M11, features a modification of the amino acid from E to G at position 168.
+The natural variant of this protein is characterized by an amino acid alteration from L to R at position 191.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from E to D at position 193.
+The protein's natural variant, known as in GALAC2; founder Romani mutation;, features a modification of the amino acid from P to T at position 28.
+The protein's natural variant, known as in GALAC2;, features a modification of the amino acid from V to M at position 32.
+The protein's natural variant, known as in GALAC2, features a modification of the amino acid from G to R at position 36.
+The protein's natural variant, known as in GALAC2;, features a modification of the amino acid from H to Y at position 44.
+The protein's natural variant, known as in GALAC2;, features a modification of the amino acid from R to C at position 68.
+The protein's natural variant, known as in GALAC2; mild deficiency; Osaka;, features a modification of the amino acid from A to V at position 198.
+The protein's natural variant, known as in GALAC2;, features a modification of the amino acid from R to Q at position 239.
+The protein's natural variant, known as in GALAC2;, features a modification of the amino acid from T to M at position 288.
+The natural variant of this protein is characterized by an amino acid alteration from V to A at position 338.
+The protein's natural variant, known as in GALAC2;, features a modification of the amino acid from G to S at position 346.
+The protein's natural variant, known as in GALAC2;, features a modification of the amino acid from G to S at position 349.
+The protein's natural variant, known as in GALAC2;, features a modification of the amino acid from A to P at position 384.
+The protein's natural variant, known as found in a patient with HSAN2B; uncertain pathological significance; dramatically enhances homooligomerization which results in aberrant endoplasmic reticulum scission and excessive reticulophagy; induces sensory neuron death in vitro;, features a modification of the amino acid from G to R at position 216.
+The protein's natural variant, known as in MPD5; decreased protein abundance; decreased stability; decreased adenylosuccinate synthase activity;, features a modification of the amino acid from D to N at position 261.
+The protein's natural variant, known as found in a child with sporadic epilepsy; unknown pathological significance;, features a modification of the amino acid from N to S at position 62.
+The protein's natural variant, known as found in a consanguineous family with intellectual disability; unknown pathological significance, features a modification of the amino acid from H to L at position 363.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to H at position 1116.
+The protein's natural variant, known as in TufB, features a modification of the amino acid from A to S at position 37.
+The natural variant of this protein is characterized by an amino acid alteration from L to P at position 522.
+The natural variant of this protein is characterized by an amino acid alteration from L to S at position 634.
+The protein's natural variant, known as in CMD2D; unknown pathological significance;, features a modification of the amino acid from G to D at position 27.
+The protein's natural variant, known as in CMD2D; unknown pathological significance, features a modification of the amino acid from A to T at position 51.
+The protein's natural variant, known as in CMD2D; unknown pathological significance;, features a modification of the amino acid from R to H at position 116.
+The protein's natural variant, known as in CMD2D; unknown pathological significance;, features a modification of the amino acid from R to W at position 161.
+The protein's natural variant, known as in CMD2D; unknown pathological significance;, features a modification of the amino acid from T to M at position 189.
+The protein's natural variant, known as in CMD2D; unknown pathological significance, features a modification of the amino acid from V to F at position 231.
+The protein's natural variant, known as in CMD2D; unknown pathological significance;, features a modification of the amino acid from D to N at position 308.
+The protein's natural variant, known as in CMD2D; unknown pathological significance, features a modification of the amino acid from D to V at position 308.
+The protein's natural variant, known as in CMD2D; unknown pathological significance;, features a modification of the amino acid from R to W at position 343.
+The protein's natural variant, known as in FALBI; decreased stability;, features a modification of the amino acid from G to S at position 35.
+The protein's natural variant, known as in FALBI; decreased stability; loss of 11-cis retinol dehydrogenase activity; accumulates in the perinuclear region;, features a modification of the amino acid from S to F at position 73.
+The protein's natural variant, known as in FALBI; decreased stability;, features a modification of the amino acid from L to I at position 105.
+The protein's natural variant, known as in FALBI; associated with macular dystrophy, features a modification of the amino acid from G to R at position 107.
+The protein's natural variant, known as in FALBI; decreased stability;, features a modification of the amino acid from D to N at position 128.
+The protein's natural variant, known as in FALBI;, features a modification of the amino acid from V to M at position 132.
+The protein's natural variant, known as in FALBI; decreased stability;, features a modification of the amino acid from R to W at position 157.
+The protein's natural variant, known as in FALBI;, features a modification of the amino acid from V to F at position 164.
+The protein's natural variant, known as in FALBI;, features a modification of the amino acid from Y to F at position 175.
+The protein's natural variant, known as in FALBI;, features a modification of the amino acid from V to G at position 177.
+The protein's natural variant, known as in FALBI;, features a modification of the amino acid from K to R at position 179.
+The protein's natural variant, known as in FALBI; decreased stability; loss of 11-cis retinol dehydrogenase activity; accumulates in the perinuclear region;, features a modification of the amino acid from G to W at position 238.
+The protein's natural variant, known as in FALBI;, features a modification of the amino acid from M to R at position 253.
+The protein's natural variant, known as in FALBI; decreased stability, features a modification of the amino acid from V to G at position 264.
+The protein's natural variant, known as in FALBI, features a modification of the amino acid from C to W at position 267.
+The protein's natural variant, known as in FALBI; decreased stability; loss of 11-cis retinol dehydrogenase activity;, features a modification of the amino acid from R to H at position 280.
+The protein's natural variant, known as in FALBI;, features a modification of the amino acid from Y to H at position 281.
+The protein's natural variant, known as in FALBI; no effect on 11-cis retinol dehydrogenase activity; accumulates in the perinuclear region;, features a modification of the amino acid from A to P at position 294.
+The protein's natural variant, known as in FALBI; loss of 11-cis retinol dehydrogenase activity; accumulates in the perinuclear region, features a modification of the amino acid from L to EV at position 310.
+The protein's natural variant, known as in SOTOS, features a modification of the amino acid from H to L at position 1616.
+The protein's natural variant, known as in SOTOS, features a modification of the amino acid from L to P at position 1637.
+The protein's natural variant, known as in SOTOS, features a modification of the amino acid from C to W at position 1674.
+The protein's natural variant, known as in SOTOS, features a modification of the amino acid from I to N at position 1687.
+The protein's natural variant, known as in SOTOS, features a modification of the amino acid from G to V at position 1792.
+The protein's natural variant, known as in SOTOS, features a modification of the amino acid from C to R at position 1925.
+The protein's natural variant, known as in SOTOS, features a modification of the amino acid from G to D at position 1955.
+The protein's natural variant, known as in SOTOS; loss of enzyme activity;, features a modification of the amino acid from R to Q at position 1984.
+The protein's natural variant, known as in SOTOS;, features a modification of the amino acid from Y to C at position 1997.
+The protein's natural variant, known as in SOTOS; strongly reduced enzyme activity;, features a modification of the amino acid from R to Q at position 2005.
+The protein's natural variant, known as in SOTOS; loss of enzyme activity;, features a modification of the amino acid from R to Q at position 2017.
+The protein's natural variant, known as in SOTOS;, features a modification of the amino acid from R to W at position 2017.
+The protein's natural variant, known as in SOTOS;, features a modification of the amino acid from H to Q at position 2143.
+The protein's natural variant, known as in SOTOS;, features a modification of the amino acid from C to S at position 2183.
+The natural variant of this protein is characterized by an amino acid alteration from I to S at position 114.
+The protein's natural variant, known as in FSGS8; results in decreased interaction with CD2AP;, features a modification of the amino acid from R to C at position 431.
+The protein's natural variant, known as in FSGS8;, features a modification of the amino acid from G to C at position 618.
+The protein's natural variant, known as in clone 86T1, features a modification of the amino acid from Y to H at position 70.
+The protein's natural variant, known as in melittin-S, features a modification of the amino acid from T to S at position 53.
+The protein's natural variant, known as in melittin-2; possibly an artifact, features a modification of the amino acid from K to S at position 64.
+The protein's natural variant, known as in melittin-2; possibly an artifact, features a modification of the amino acid from K to KK at position 66.
+The protein's natural variant, known as in OORS; defective GPI anchor biosynthesis in homozygous patient cells, features a modification of the amino acid from P to R at position 172.
+The protein's natural variant, known as in PLDECO; impaired protein stability; strongly decreased enzyme activity; decreased ceramide catabolic process; in fibroblasts of patients homozygous for the mutation;, features a modification of the amino acid from E to G at position 33.
+The protein's natural variant, known as in HPS2;, features a modification of the amino acid from L to R at position 580.
+The protein's natural variant, known as in strain: Isolate AFTC 25274 and Isolate MZI-CH6, features a modification of the amino acid from W to L at position 21.
+The protein's natural variant, known as in strain: Isolate MZI-CH6, features a modification of the amino acid from L to V at position 150.
+The protein's natural variant, known as in strain: Isolate AFTC 25274, features a modification of the amino acid from S to T at position 159.
+The protein's natural variant, known as in strain: Goe 2, G25, PWudll and TN, features a modification of the amino acid from D to E at position 55.
+The protein's natural variant, known as in strain: Goe 2, G25, PWudll and TN, features a modification of the amino acid from N to K at position 216.
+The protein's natural variant, known as in strain: Goe 2, G25, PWudll and TN, features a modification of the amino acid from S to T at position 221.
+The protein's natural variant, known as in strain: Goe 2, G25, PWudll and TN, features a modification of the amino acid from A to D at position 271.
+The natural variant of this protein is characterized by an amino acid alteration from T to S at position 70.
+The protein's natural variant, known as in ATFB14; the mutant results in reduced sodium currents and altered channel gating when coexpressed with SCN5A in a heterologous expression system;, features a modification of the amino acid from R to Q at position 28.
+The protein's natural variant, known as in ATFB14; the mutant results in reduced sodium currents and altered channel gating when coexpressed with SCN5A in a heterologous expression system;, features a modification of the amino acid from R to W at position 28.
+The protein's natural variant, known as found in a patient with Brugada syndrome; unknown pathological significance; induces a reduction in sodium current density most likely by decreasing SCN5A protein cell surface expression;, features a modification of the amino acid from D to G at position 211.
+The protein's natural variant, known as in strain: L2, features a modification of the amino acid from T to I at position 89.
+The protein's natural variant, known as in strain: L2, features a modification of the amino acid from S to A at position 314.
+The protein's natural variant, known as in strain: L2, features a modification of the amino acid from R to Q at position 372.
+The protein's natural variant, known as in strain: L2, features a modification of the amino acid from I to M at position 405.
+The protein's natural variant, known as in strain: FRD2, features a modification of the amino acid from C to A at position 46.
+The protein's natural variant, known as in allele F, features a modification of the amino acid from V to I at position 22.
+The protein's natural variant, known as in allele B, features a modification of the amino acid from E to K at position 79.
+The protein's natural variant, known as in allele 0, features a modification of the amino acid from E to K at position 161.
+The protein's natural variant, known as in allele C and allele E, features a modification of the amino acid from K to I at position 182.
+The protein's natural variant, known as in allele E, features a modification of the amino acid from P to R at position 208.
+The protein's natural variant, known as in COQ10D4;, features a modification of the amino acid from R to W at position 213.
+The protein's natural variant, known as in COQ10D4;, features a modification of the amino acid from R to C at position 271.
+The protein's natural variant, known as in COQ10D4;, features a modification of the amino acid from G to D at position 272.
+The protein's natural variant, known as in COQ10D4;, features a modification of the amino acid from G to V at position 272.
+The protein's natural variant, known as in COQ10D4; decreased stability;, features a modification of the amino acid from R to W at position 299.
+The protein's natural variant, known as in COQ10D4;, features a modification of the amino acid from A to T at position 304.
+The protein's natural variant, known as in COQ10D4;, features a modification of the amino acid from A to V at position 304.
+The protein's natural variant, known as in COQ10D4; decreased stability;, features a modification of the amino acid from Y to C at position 429.
+The protein's natural variant, known as in COQ10D4;, features a modification of the amino acid from Y to C at position 514.
+The protein's natural variant, known as in COQ10D4; decreased stability;, features a modification of the amino acid from G to S at position 549.
+The protein's natural variant, known as in COQ10D4; decreased stability;, features a modification of the amino acid from E to K at position 551.
+The protein's natural variant, known as in COQ10D4; unknown pathological significance, features a modification of the amino acid from F to V at position 578.
+The protein's natural variant, known as in COQ10D4;, features a modification of the amino acid from P to R at position 602.
+The protein's natural variant, known as in LDS4;, features a modification of the amino acid from R to W at position 299.
+The protein's natural variant, known as in LDS4;, features a modification of the amino acid from R to C at position 302.
+The protein's natural variant, known as probable disease-associated variant found in a family with non-syndromic aortic disease;, features a modification of the amino acid from R to C at position 320.
+The protein's natural variant, known as in LDS4;, features a modification of the amino acid from P to H at position 338.
+The protein's natural variant, known as in strain: TB12.O3+4+8, TB131.O3+4+8, TB132.O3+4+8, TB144.O3+4+8, TB150.O3+4+8, TB153.O3+4+8, TB173.O3+4+8, TB189.O3+4+8, TB19.O3+4+8, TB192.O3+4+8, TB198.O3+4+8, TB202.O3+4+8, TB27.O3+4+8, TB35.O3+4+8, TB358a.O3+4+8, TB64.O3+4+8, TB80.O3+4+8 and TB98pp.O3+4+8, features a modification of the amino acid from I to V at position 93.
+The protein's natural variant, known as in COXPD46, features a modification of the amino acid from P to R at position 40.
+The protein's natural variant, known as in SCAR10;, features a modification of the amino acid from L to R at position 510.
+The protein's natural variant, known as no effect on activation of STAT1 upon IFNA2 or IFNG binding;, features a modification of the amino acid from A to V at position 24.
+The protein's natural variant, known as no effect on activation of STAT1 upon IFNA2 or IFNG binding;, features a modification of the amino acid from G to R at position 57.
+The protein's natural variant, known as abolished STAT1 activation upon IFNA2 binding but no effect upon IFNG binding;, features a modification of the amino acid from W to C at position 73.
+The protein's natural variant, known as no effect on activation of STAT1 upon IFNA2 or IFNG binding IFNG binding;, features a modification of the amino acid from Q to H at position 80.
+The protein's natural variant, known as no effect on activation of STAT1 upon IFNA2 or IFNG binding, features a modification of the amino acid from T to A at position 83.
+The protein's natural variant, known as no effect on activation of STAT1 upon IFNA2 or IFNG binding;, features a modification of the amino acid from N to S at position 88.
+The protein's natural variant, known as no effect on activation of STAT1 upon IFNA2 or IFNG binding;, features a modification of the amino acid from I to M at position 169.
+The protein's natural variant, known as no effect on activation of STAT1 upon IFNA2 or IFNG binding;, features a modification of the amino acid from I to V at position 183.
+The protein's natural variant, known as no effect on activation of STAT1 upon IFNA2 or IFNG binding;, features a modification of the amino acid from R to C at position 306.
+The protein's natural variant, known as no effect on activation of STAT1 upon IFNA2 or IFNG binding;, features a modification of the amino acid from V to I at position 307.
+The protein's natural variant, known as requires 2 nucleotide substitutions; no effect on activation of STAT1 upon IFNA2 or IFNG binding, features a modification of the amino acid from E to L at position 386.
+The protein's natural variant, known as abolished STAT1 activation upon IFNA2 binding but no effect upon IFNG binding;, features a modification of the amino acid from S to R at position 422.
+The protein's natural variant, known as no effect on activation of STAT1 upon IFNA2 or IFNG binding;, features a modification of the amino acid from A to T at position 424.
+The protein's natural variant, known as no effect on activation of STAT1 upon IFNA2 or IFNG binding;, features a modification of the amino acid from E to K at position 515.
+The protein's natural variant, known as probable disease-associated variant found in patients with adult onset primary cervical dystonia, features a modification of the amino acid from P to S at position 47.
+The protein's natural variant, known as probable disease-associated variant found in a family with adult onset primary cervical dystonia; exonic splicing enhancer mutation resulting in altered CIZ1 splicing pattern;, features a modification of the amino acid from S to G at position 264.
+The protein's natural variant, known as probable disease-associated variant found in patients with adult onset primary cervical dystonia, features a modification of the amino acid from R to M at position 672.
+The protein's natural variant, known as in ALS8; it forms insoluble cytosolic aggregates; cannot activate the UPR pathway through ERN1/IRE1 induction; results in ubiquitinated aggregates accumulation and cell death;, features a modification of the amino acid from T to I at position 46.
+The protein's natural variant, known as in ALS8 and SMAPAD; it forms insoluble cytosolic aggregates; cannot activate the UPR pathway; affects interaction with RMDN3; affects cellular calcium homeostasis; induces mislocalization to the non-ER compartments; enhances homodimerization;, features a modification of the amino acid from P to S at position 56.
+The protein's natural variant, known as in PC4;, features a modification of the amino acid from E to K at position 472.
+The protein's natural variant, known as in IMD84; no effect on homodimerization activity; no effect on heterodimerization activity; changed localization; changed DNA-binding transcription activator activity; changed sequence-specific DNA binding; binds novel and non-specific DNA motifs and acts as a dominant negative through its homodimerization and heterodimerization activities, features a modification of the amino acid from G to R at position 159.
+The protein's natural variant, known as found in a renal cell carcinoma sample; somatic mutation, features a modification of the amino acid from E to Q at position 277.
+The protein's natural variant, known as in an ovarian serous carcinoma sample; somatic mutation, features a modification of the amino acid from K to Q at position 191.
+The protein's natural variant, known as in myeloproliferative disorder with erythrocytosis, features a modification of the amino acid from FHK to L at position 539.
+The protein's natural variant, known as in myeloproliferative disorder with erythrocytosis, features a modification of the amino acid from HK to QL at position 539.
+The protein's natural variant, known as in myeloproliferative disorder with erythrocytosis; requires 2 nucleotide substitutions;, features a modification of the amino acid from K to L at position 539.
+The protein's natural variant, known as in AML;, features a modification of the amino acid from K to N at position 607.
+The protein's natural variant, known as in PV, THCYT3 and AML; associated with susceptibility to Budd-Chiari syndrome; somatic mutation in a high percentage of patients with essential thrombocythemia or myelofibrosis; leads to constitutive tyrosine phosphorylation activity that promotes cytokine hypersensitivity;, features a modification of the amino acid from V to F at position 617.
+The protein's natural variant, known as in THCYT3;, features a modification of the amino acid from V to I at position 617.
+The protein's natural variant, known as in PCH2F; Almost complete loss of tRNA-intron endonuclease activity in vitro; may affect protein levels;, features a modification of the amino acid from W to G at position 76.
+The protein's natural variant, known as in PCH2F; Almost complete loss of tRNA-intron endonuclease activity in vitro;, features a modification of the amino acid from H to Y at position 116.
+The protein's natural variant, known as in PCH2F; Almost complete loss of tRNA-intron endonuclease activity in vitro; may affect protein levels;, features a modification of the amino acid from Y to C at position 152.
+The protein's natural variant, known as in HPMRS1;, features a modification of the amino acid from Q to K at position 256.
+The protein's natural variant, known as in HPMRS1;, features a modification of the amino acid from A to E at position 341.
+The protein's natural variant, known as in HPMRS1;, features a modification of the amino acid from A to V at position 341.
+The protein's natural variant, known as in HPMRS1;, features a modification of the amino acid from H to P at position 385.
+The protein's natural variant, known as in strain: Isolate Anna, features a modification of the amino acid from D to N at position 4.
+The protein's natural variant, known as in strain: Isolate Anna, features a modification of the amino acid from T to A at position 178.
+The protein's natural variant, known as in CORD19;, features a modification of the amino acid from E to K at position 543.
+The protein's natural variant, known as in LS; unknown pathological significance; decrease in enzyme activity;, features a modification of the amino acid from Q to K at position 26.
+The protein's natural variant, known as in MC1DM1;, features a modification of the amino acid from S to P at position 34.
+The protein's natural variant, known as in MC1DM1;, features a modification of the amino acid from S to P at position 45.
+The protein's natural variant, known as in LS and MC1DM1;, features a modification of the amino acid from A to T at position 47.
+The natural variant of this protein is characterized by an amino acid alteration from M to V at position 53.
+The protein's natural variant, known as in strain: A.BY, B10.H7 and C3H.SW; correlated with B6dom1-negative phenotype, features a modification of the amino acid from E to D at position 776.
+The protein's natural variant, known as in SPGF70; unknown pathological significance;, features a modification of the amino acid from M to V at position 227.
+The protein's natural variant, known as in IMF1;, features a modification of the amino acid from R to C at position 561.
+The protein's natural variant, known as in KOGS;, features a modification of the amino acid from P to R at position 584.
+The protein's natural variant, known as in a gastric adenocarcinoma sample; somatic mutation, features a modification of the amino acid from Y to H at position 589.
+The protein's natural variant, known as in IBGC4; no effect on protein abundance; loss of PDGF beta receptor activity;, features a modification of the amino acid from L to P at position 658.
+The protein's natural variant, known as in IMF1;, features a modification of the amino acid from P to T at position 660.
+The protein's natural variant, known as in PENTT; gain of function in protein tyrosine kinase activity; shows ligand-independent constitutive signaling;, features a modification of the amino acid from V to A at position 665.
+The protein's natural variant, known as in a breast infiltrating ductal carcinoma sample; somatic mutation, features a modification of the amino acid from T to I at position 882.
+The protein's natural variant, known as in IBGC4; decreased protein abundance; no effect on receptor activity; decreased PDGF signaling pathway;, features a modification of the amino acid from R to W at position 987.
+The protein's natural variant, known as in IBGC4; no effect on protein abundance; no effect on receptor activity; decreased PDGF signaling pathway, features a modification of the amino acid from E to V at position 1071.
+The protein's natural variant, known as in MC3DN9; decreases protein abundance; reduces complex III formation; reduces complex III activity;, features a modification of the amino acid from V to E at position 20.
+The protein's natural variant, known as in SCRA; loss of interaction with YAP1 and also activation by YAP1;, features a modification of the amino acid from Y to H at position 421.
+The protein's natural variant, known as observed with a marginally higher frequency in patients with systemic lupus erythematosus;, features a modification of the amino acid from Q to E at position 152.
+The protein's natural variant, known as in DFNA3B; unknown pathological significance;, features a modification of the amino acid from T to M at position 5.
+The protein's natural variant, known as in ECTD2;, features a modification of the amino acid from G to R at position 11.
+The protein's natural variant, known as in ECTD2;, features a modification of the amino acid from V to E at position 37.
+The protein's natural variant, known as found in one patient with a syndrome resembling Vohwinkel and Bart-Pumphrey syndromes, features a modification of the amino acid from G to R at position 59.
+The protein's natural variant, known as in ECTD2;, features a modification of the amino acid from A to V at position 88.
+The natural variant of this protein is characterized by an amino acid alteration from S to G at position 139.
+The protein's natural variant, known as in strain: Isolate MVZ 174229 and Isolate MVZ 174230, features a modification of the amino acid from M to T at position 39.
+The protein's natural variant, known as in a hepatocellular carcinoma sample, features a modification of the amino acid from R to S at position 106.
+The protein's natural variant, known as in a hepatocellular carcinoma sample, features a modification of the amino acid from D to Y at position 108.
+The protein's natural variant, known as in a hepatocellular carcinoma sample;, features a modification of the amino acid from A to T at position 116.
+The protein's natural variant, known as in a hepatocellular carcinoma sample; reduces protein stability, features a modification of the amino acid from G to V at position 134.
+The protein's natural variant, known as in a hepatocellular carcinoma sample, features a modification of the amino acid from L to I at position 144.
+The protein's natural variant, known as highly associated with hepatocellular carcinoma (HCC) progression;, features a modification of the amino acid from S to R at position 197.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from Q to K at position 340.
+The natural variant of this protein is characterized by an amino acid alteration from H to Y at position 522.
+The natural variant of this protein is characterized by an amino acid alteration from E to D at position 50.
+The natural variant of this protein is characterized by an amino acid alteration from L to W at position 51.
+The protein's natural variant, known as in CTS2; reduced secretion in tendon cells; no effect on secretion in chondrocytes; disrupted pentamerization; induced ER stress;, features a modification of the amino acid from V to E at position 66.
+The natural variant of this protein is characterized by an amino acid alteration from A to G at position 109.
+The protein's natural variant, known as in EDM1;, features a modification of the amino acid from G to E at position 167.
+The natural variant of this protein is characterized by an amino acid alteration from R to G at position 224.
+The protein's natural variant, known as in PSACH;, features a modification of the amino acid from P to S at position 234.
+The protein's natural variant, known as in EDM1;, features a modification of the amino acid from P to R at position 276.
+The natural variant of this protein is characterized by an amino acid alteration from R to P at position 285.
+The protein's natural variant, known as in PSACH;, features a modification of the amino acid from D to G at position 290.
+The protein's natural variant, known as in PSACH; mild form, features a modification of the amino acid from D to N at position 290.
+The protein's natural variant, known as in EDM1; phenotypic features overlapping with mild PSACH, features a modification of the amino acid from S to L at position 298.
+The protein's natural variant, known as in PSACH, features a modification of the amino acid from G to R at position 299.
+The protein's natural variant, known as in EDM1, features a modification of the amino acid from A to D at position 311.
+The protein's natural variant, known as in EDM1; atypical form, features a modification of the amino acid from D to G at position 317.
+The protein's natural variant, known as in EDM1, features a modification of the amino acid from D to G at position 326.
+The protein's natural variant, known as in PSACH, features a modification of the amino acid from D to Y at position 326.
+The protein's natural variant, known as in PSACH; mild form;, features a modification of the amino acid from C to R at position 328.
+The protein's natural variant, known as in EDM1; Fairbank type;, features a modification of the amino acid from D to Y at position 342.
+The protein's natural variant, known as in EDM1, features a modification of the amino acid from C to F at position 348.
+The protein's natural variant, known as in PSACH;, features a modification of the amino acid from C to R at position 348.
+The protein's natural variant, known as in PSACH; mild form, features a modification of the amino acid from D to V at position 349.
+The protein's natural variant, known as in EDM1; Fairbank type, features a modification of the amino acid from D to V at position 361.
+The protein's natural variant, known as in EDM1; binds less calcium, features a modification of the amino acid from D to Y at position 361.
+The protein's natural variant, known as in EDM1; Fairbank type, features a modification of the amino acid from C to S at position 371.
+The protein's natural variant, known as in EDM1;, features a modification of the amino acid from C to Y at position 371.
+The protein's natural variant, known as in EDM1, features a modification of the amino acid from D to N at position 374.
+The protein's natural variant, known as in EDM1, features a modification of the amino acid from D to N at position 376.
+The protein's natural variant, known as in PSACH, features a modification of the amino acid from D to V at position 378.
+The protein's natural variant, known as in EDM1; atypical form, features a modification of the amino acid from D to N at position 385.
+The protein's natural variant, known as in EDM1; atypical form;, features a modification of the amino acid from D to Y at position 385.
+The protein's natural variant, known as in PSACH; mild form, features a modification of the amino acid from C to G at position 387.
+The protein's natural variant, known as in PSACH, features a modification of the amino acid from C to R at position 387.
+The protein's natural variant, known as in PSACH, features a modification of the amino acid from PNSD to V at position 394.
+The protein's natural variant, known as in EDM1, features a modification of the amino acid from D to H at position 397.
+The protein's natural variant, known as in PSACH, features a modification of the amino acid from GIG to VC at position 404.
+The protein's natural variant, known as in EDM1;, features a modification of the amino acid from G to R at position 404.
+The protein's natural variant, known as in EDM1, features a modification of the amino acid from D to Y at position 408.
+The protein's natural variant, known as in EDM1; phenotype overlapping with mild PSACH, features a modification of the amino acid from C to Y at position 410.
+The protein's natural variant, known as in EDM1, features a modification of the amino acid from N to K at position 415.
+The protein's natural variant, known as in EDM1, features a modification of the amino acid from D to A at position 420.
+The protein's natural variant, known as in EDM1, features a modification of the amino acid from G to E at position 427.
+The protein's natural variant, known as in EDM1, features a modification of the amino acid from CDS to LWC at position 432.
+The protein's natural variant, known as in PSACH; mild form, features a modification of the amino acid from G to E at position 440.
+The protein's natural variant, known as in PSACH;, features a modification of the amino acid from G to R at position 440.
+The protein's natural variant, known as in PSACH, features a modification of the amino acid from D to N at position 446.
+The protein's natural variant, known as in PSACH, features a modification of the amino acid from C to S at position 448.
+The protein's natural variant, known as in EDM1; Fairbank type;, features a modification of the amino acid from N to S at position 453.
+The protein's natural variant, known as in PSACH; severe form;, features a modification of the amino acid from C to Y at position 468.
+The protein's natural variant, known as in PSACH; severe form;, features a modification of the amino acid from D to Y at position 472.
+The protein's natural variant, known as in EDM1, features a modification of the amino acid from D to DD at position 473.
+The protein's natural variant, known as in PSACH; severe form;, features a modification of the amino acid from D to G at position 473.
+The protein's natural variant, known as in PSACH, features a modification of the amino acid from D to H at position 473.
+The protein's natural variant, known as in PSACH, features a modification of the amino acid from D to N at position 475.
+The protein's natural variant, known as in PSACH, features a modification of the amino acid from D to G at position 482.
+The protein's natural variant, known as in EDM1;, features a modification of the amino acid from G to D at position 501.
+The protein's natural variant, known as in PSACH, features a modification of the amino acid from D to G at position 507.
+The protein's natural variant, known as in PSACH, features a modification of the amino acid from D to G at position 511.
+The protein's natural variant, known as in PSACH, features a modification of the amino acid from D to G at position 515.
+The protein's natural variant, known as in PSACH; mild form;, features a modification of the amino acid from D to N at position 518.
+The protein's natural variant, known as in EDM1; Ribbing type;, features a modification of the amino acid from N to K at position 523.
+The protein's natural variant, known as in PSACH;, features a modification of the amino acid from T to I at position 529.
+The protein's natural variant, known as in PSACH; mild form and EDM1;, features a modification of the amino acid from T to M at position 585.
+The protein's natural variant, known as in EDM1 and PSACH;, features a modification of the amino acid from T to R at position 585.
+The protein's natural variant, known as in EDM1;, features a modification of the amino acid from R to P at position 718.
+The protein's natural variant, known as in EDM1 and CTS2; reduced secretion in tendon cells and chondrocytes;, features a modification of the amino acid from R to W at position 718.
+The protein's natural variant, known as in PSACH; severe;, features a modification of the amino acid from G to D at position 719.
+The protein's natural variant, known as in PSACH;, features a modification of the amino acid from G to S at position 719.
+The protein's natural variant, known as in a patient with multiple epiphyseal dysplasia;, features a modification of the amino acid from Q to R at position 756.
+The protein's natural variant, known as in strain: HBA, features a modification of the amino acid from A to T at position 18.
+The protein's natural variant, known as in strain: HBA, features a modification of the amino acid from T to R at position 137.
+The protein's natural variant, known as in strain: HBA, features a modification of the amino acid from I to T at position 164.
+The protein's natural variant, known as in Pla l 1.0102 and 1.0103, features a modification of the amino acid from D to G at position 58.
+The protein's natural variant, known as in Pla l 1.0103, features a modification of the amino acid from S to G at position 82.
+The protein's natural variant, known as in IBDD;, features a modification of the amino acid from M to I at position 128.
+The protein's natural variant, known as in IBDD;, features a modification of the amino acid from D to Y at position 134.
+The protein's natural variant, known as in IBDD; loss of protein solubility; complete loss of isobutyryl-CoA dehydrogenase activity;, features a modification of the amino acid from G to R at position 137.
+The protein's natural variant, known as in IBDD;, features a modification of the amino acid from M to T at position 152.
+The protein's natural variant, known as in IBDD;, features a modification of the amino acid from V to I at position 203.
+The protein's natural variant, known as in IBDD; no effect on localization to the mitochondrion; complete loss of isobutyryl-CoA dehydrogenase activity; loss of protein expression in patient cells;, features a modification of the amino acid from R to Q at position 302.
+The protein's natural variant, known as in IBDD; decreased isobutyryl-CoA dehydrogenase activity; less than 20% of wild-type;, features a modification of the amino acid from A to T at position 320.
+The protein's natural variant, known as in IBDD;, features a modification of the amino acid from R to C at position 334.
+The protein's natural variant, known as in IBDD;, features a modification of the amino acid from Q to R at position 385.
+The protein's natural variant, known as in strain: OMZ409, features a modification of the amino acid from EMKLA to AMELV at position 104.
+The protein's natural variant, known as in strain: OMZ409, features a modification of the amino acid from A to T at position 126.
+The protein's natural variant, known as in strain: OMZ409, features a modification of the amino acid from E to D at position 136.
+The natural variant of this protein is characterized by an amino acid alteration from C to F at position 17.
+The natural variant of this protein is characterized by an amino acid alteration from N to S at position 26.
+The natural variant of this protein is characterized by an amino acid alteration from S to T at position 93.
+The natural variant of this protein is characterized by an amino acid alteration from K to M at position 141.
+The natural variant of this protein is characterized by an amino acid alteration from Y to F at position 148.
+The protein's natural variant, known as in ECTD13;, features a modification of the amino acid from F to S at position 207.
+The protein's natural variant, known as in strain: AF1, AF2, AF3, AF5, AF6, AF7, AF8, AF9, AF10, Au4, Au7, Au8, La3, La10, La13, La14, La15, La28, La31, La32, La36, La37, La54, La58, La60, La62, La105, La106, La116, La118, La120, La125, Ma3, Ma6, Ma11, Ma18, Ma20, Ma21, Ma23, Ma24, Ma31, Ma35, Ma37, Ma43, Ma50, Ma53, Ma56, Ma57, Ma60, Ma74, Mo29b, Mo40b, Mo52b, NC-003, NC-004, NC-006, NC-008, NC-009, Ny2, Ny3, Ny4, Ny5, TW1, TW2, TW5, TW6, TW7, TW8, TW10 and TW11, features a modification of the amino acid from Q to H at position 64.
+The protein's natural variant, known as in strain: TW9, features a modification of the amino acid from P to R at position 77.
+The protein's natural variant, known as in strain: La3, La10, La13, La15, La27, La28, La31, La62, La105, La106, La116, La118, La120, Ma3, Ma6, Ma18, Ma23, Ma31, Ma37, Ma43, Ma56, Ma57, Ma60, Ma74, Mo13a, Mo29b, Mo34a, Mo40b, Mo52b, NC-002, NC-003, NC-004, NC-006, NC-008, Ny2, Ny4, TW2, TW4, TW5, TW8, TW10 and TW11, features a modification of the amino acid from I to V at position 80.
+The protein's natural variant, known as in strain: Au4 and Ma60, features a modification of the amino acid from M to I at position 89.
+The protein's natural variant, known as in strain: AF1, AF2, AF3, AF5, AF6, AF7, AF8, AF9, AF10, La14, La31, La32, La60, La106, La118, La125, Ma6, Ma21, Ma24, Ma31, Ma37, Ma50, Ma56, Ma57, Ma74, TW1 and TW6, features a modification of the amino acid from A to E at position 90.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from Q to R at position 245.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from L to V at position 505.
+The protein's natural variant, known as increased chitinase activity; when associated with N-47 and M-61;, features a modification of the amino acid from N to D at position 45.
+The protein's natural variant, known as increased chitinase activity; when associated with D-45 and M-61;, features a modification of the amino acid from D to N at position 47.
+The protein's natural variant, known as increased chitinase activity; when associated with D-45 and N-47;, features a modification of the amino acid from R to M at position 61.
+The protein's natural variant, known as found in a non-responder to ezetimibe treatment;, features a modification of the amino acid from V to L at position 55.
+The protein's natural variant, known as found in a non-responder to ezetimibe treatment;, features a modification of the amino acid from I to N at position 1233.
+The protein's natural variant, known as no effect on IFNB induction upon Sendai virus infection, features a modification of the amino acid from R to H at position 37.
+The protein's natural variant, known as abolished IFNB induction upon Sendai virus infection, features a modification of the amino acid from F to S at position 95.
+The protein's natural variant, known as abolished IFNB induction upon Sendai virus infection, features a modification of the amino acid from D to N at position 117.
+The protein's natural variant, known as no effect on IFNB induction upon Sendai virus infection, features a modification of the amino acid from G to R at position 133.
+The protein's natural variant, known as requires 2 nucleotide substitutions; no effect on IFNB induction upon Sendai virus infection, features a modification of the amino acid from G to L at position 214.
+The protein's natural variant, known as no effect IFNB induction upon Sendai virus infection, features a modification of the amino acid from T to A at position 254.
+The protein's natural variant, known as no effect on IFNB induction upon Sendai virus infection, features a modification of the amino acid from R to Q at position 369.
+The protein's natural variant, known as decreased IFNB induction upon Sendai virus infection, features a modification of the amino acid from M to V at position 371.
+The protein's natural variant, known as in IMD39; loss of function mutation; shows abnormal localization to the cytoplasm rather than the nucleus; abolished IFNB induction upon Sendai virus infection;, features a modification of the amino acid from F to V at position 410.
+The protein's natural variant, known as no effect on IFNB induction upon Sendai virus infection, features a modification of the amino acid from A to T at position 419.
+The natural variant of this protein is characterized by an amino acid alteration from I to N at position 22.
+The protein's natural variant, known as in strain: A68 and UA802, features a modification of the amino acid from A to T at position 84.
+The protein's natural variant, known as in strain: NCTC 11638, features a modification of the amino acid from V to M at position 138.
+The protein's natural variant, known as in strain: NCTC 11638, features a modification of the amino acid from R to H at position 202.
+The protein's natural variant, known as in strain: NCTC 11638, features a modification of the amino acid from A to T at position 237.
+The protein's natural variant, known as in strain: Ty2 and Ty21a, features a modification of the amino acid from RLREILQTQGLNIEALFRE to PSARNSADAGAEYRSAVPRVSTLVKKRPVDRLAFFLPFVFCQQRRDTRHHWRVINIFLRHAKRLWIVFAAGTA at position 330.
+The protein's natural variant, known as in allele NKG2-F*02;, features a modification of the amino acid from I to S at position 29.
+The protein's natural variant, known as in allele NKG2-F*02;, features a modification of the amino acid from N to S at position 104.
+The protein's natural variant, known as in CMT2A2A;, features a modification of the amino acid from V to F at position 69.
+The protein's natural variant, known as in CMT2A2A;, features a modification of the amino acid from L to P at position 76.
+The protein's natural variant, known as in CMT2A2A, CMT2A2B and HMSN6A;, features a modification of the amino acid from R to Q at position 94.
+The protein's natural variant, known as in HMSN6A; severely reduced homo-oligomerization; no effect on hetero-oligomerization with MFN1;, features a modification of the amino acid from R to W at position 94.
+The protein's natural variant, known as in CMT2A2B; unknown pathological significance, features a modification of the amino acid from V to M at position 112.
+The protein's natural variant, known as in CMT2A2A; unknown pathological significance, features a modification of the amino acid from G to V at position 127.
+The protein's natural variant, known as in CMT2A2B; unknown pathological significance;, features a modification of the amino acid from A to V at position 164.
+The protein's natural variant, known as in HMSN6A;, features a modification of the amino acid from T to I at position 206.
+The protein's natural variant, known as in CMT2A2B; unknown pathological significance, features a modification of the amino acid from D to N at position 214.
+The protein's natural variant, known as in CMT2A2B;, features a modification of the amino acid from F to S at position 216.
+The protein's natural variant, known as in CMT2A2A, features a modification of the amino acid from L to V at position 233.
+The protein's natural variant, known as in CMT2A2A;, features a modification of the amino acid from P to A at position 251.
+The protein's natural variant, known as found in a patient with hereditary motor and sensory neuropathy; unknown pathological significance;, features a modification of the amino acid from R to H at position 259.
+The protein's natural variant, known as in HMSN6A;, features a modification of the amino acid from Q to R at position 276.
+The protein's natural variant, known as in CMT2A2A;, features a modification of the amino acid from R to H at position 280.
+The protein's natural variant, known as in CMT2A2A; unknown pathological significance, features a modification of the amino acid from E to V at position 347.
+The protein's natural variant, known as in CMT2A2A;, features a modification of the amino acid from K to N at position 357.
+The protein's natural variant, known as in HMSN6A, features a modification of the amino acid from H to Y at position 361.
+The protein's natural variant, known as in CMT2A2B; unknown pathological significance;, features a modification of the amino acid from T to M at position 362.
+The protein's natural variant, known as in HMSN6A and CMT2A2A;, features a modification of the amino acid from R to W at position 364.
+The protein's natural variant, known as in CMT2A2A; unknown pathological significance;, features a modification of the amino acid from M to I at position 376.
+The protein's natural variant, known as in CMT2A2B; unknown pathological significance, features a modification of the amino acid from C to R at position 390.
+The protein's natural variant, known as in CMT2A2A; also found in patients with an unclassified form of Charcot-Marie-Tooth disease; unknown pathological significance;, features a modification of the amino acid from R to H at position 468.
+The protein's natural variant, known as found in a patient with hereditary motor neuropathy; unknown pathological significance;, features a modification of the amino acid from N to S at position 570.
+The protein's natural variant, known as in CMT2A2A and CMT2A2B; decreased function in mitochondrial fusion; reduced homo-oligomerization; no effect on hetero-oligomerization with MFN1;, features a modification of the amino acid from R to W at position 707.
+The protein's natural variant, known as found in a patient with intermediate Charcot-Marie-Tooth disease; unknown pathological significance;, features a modification of the amino acid from A to T at position 716.
+The protein's natural variant, known as in CMT2A2A;, features a modification of the amino acid from W to S at position 740.
+The protein's natural variant, known as in CMT2A2A; requires 2 nucleotide substitutions, features a modification of the amino acid from E to M at position 744.
+The protein's natural variant, known as in strain: M551, features a modification of the amino acid from P to T at position 63.
+The protein's natural variant, known as in strain: M553, M535, CO391, CO407 and 653/36, features a modification of the amino acid from V to L at position 171.
+The protein's natural variant, known as in strain: M548, features a modification of the amino acid from K to N at position 204.
+The protein's natural variant, known as in strain: 569B, features a modification of the amino acid from A to T at position 223.
+The protein's natural variant, known as in strain: M550, M551, M554, M557, M558 and GD98200, features a modification of the amino acid from A to E at position 277.
+The protein's natural variant, known as in strain: Isolate 4183, features a modification of the amino acid from T to A at position 122.
+The protein's natural variant, known as in CMS12;, features a modification of the amino acid from T to A at position 15.
+The protein's natural variant, known as in CMS12;, features a modification of the amino acid from T to M at position 15.
+The protein's natural variant, known as in CMS12, features a modification of the amino acid from D to V at position 43.
+The protein's natural variant, known as in CMS12;, features a modification of the amino acid from R to C at position 111.
+The protein's natural variant, known as in CMS12;, features a modification of the amino acid from I to T at position 121.
+The protein's natural variant, known as in CMS12;, features a modification of the amino acid from V to F at position 199.
+The protein's natural variant, known as in CMS12;, features a modification of the amino acid from D to Y at position 366.
+The protein's natural variant, known as in CMS12;, features a modification of the amino acid from R to H at position 403.
+The protein's natural variant, known as in CMS12, features a modification of the amino acid from R to H at position 452.
+The protein's natural variant, known as in CMS12;, features a modification of the amino acid from M to T at position 509.
+The protein's natural variant, known as in CMS12, features a modification of the amino acid from M to T at position 510.
+The protein's natural variant, known as in CMS12, features a modification of the amino acid from R to W at position 514.
+The protein's natural variant, known as in CMS12;, features a modification of the amino acid from R to W at position 530.
+The protein's natural variant, known as in strain: Isolate C-201, features a modification of the amino acid from T to I at position 371.
+The protein's natural variant, known as in DKCB1;, features a modification of the amino acid from R to W at position 34.
+The protein's natural variant, known as in LQT7; there is loss of function when the mutant is expressed alone and a dominant-negative effect when expressed with wild-type channels; channel trafficking and assembly are not affected;, features a modification of the amino acid from C to F at position 54.
+The protein's natural variant, known as in LQT7;, features a modification of the amino acid from R to W at position 67.
+The protein's natural variant, known as in LQT7; loss of function mutation acting in a dominant-negative manner;, features a modification of the amino acid from D to V at position 71.
+The protein's natural variant, known as in LQT7; loss of function mutation acting in a dominant-negative manner;, features a modification of the amino acid from T to R at position 75.
+The protein's natural variant, known as in ATFB9; has a gain-of-function effect on the channels;, features a modification of the amino acid from V to I at position 93.
+The protein's natural variant, known as in SQT3; gain of function;, features a modification of the amino acid from D to N at position 172.
+The protein's natural variant, known as in LQT7;, features a modification of the amino acid from P to L at position 186.
+The protein's natural variant, known as in LQT7;, features a modification of the amino acid from N to H at position 216.
+The protein's natural variant, known as in LQT7; loss of function and dominant-negative effect in current;, features a modification of the amino acid from R to W at position 218.
+The protein's natural variant, known as in LQT7;, features a modification of the amino acid from G to V at position 300.
+The protein's natural variant, known as in LQT7;, features a modification of the amino acid from V to M at position 302.
+The protein's natural variant, known as in LQT7; there is loss of function when the mutant is expressed alone and a dominant-negative effect when expressed with wild-type channels; channel trafficking and assembly are not affected;, features a modification of the amino acid from T to P at position 305.
+The natural variant of this protein is characterized by an amino acid alteration from LI to YF at position 49.
+The natural variant of this protein is characterized by an amino acid alteration from R to Q at position 79.
+The natural variant of this protein is characterized by an amino acid alteration from M to L at position 84.
+The natural variant of this protein is characterized by an amino acid alteration from V to L at position 90.
+The natural variant of this protein is characterized by an amino acid alteration from T to S at position 97.
+The natural variant of this protein is characterized by an amino acid alteration from K to W at position 104.
+The natural variant of this protein is characterized by an amino acid alteration from M to I at position 233.
+The natural variant of this protein is characterized by an amino acid alteration from V to A at position 75.
+The natural variant of this protein is characterized by an amino acid alteration from E to K at position 89.
+The natural variant of this protein is characterized by an amino acid alteration from E to K at position 196.
+The natural variant of this protein is characterized by an amino acid alteration from R to H at position 201.
+The protein's natural variant, known as in IBD29; decreases protein stability;, features a modification of the amino acid from Y to F at position 333.
+The protein's natural variant, known as in NEM10, features a modification of the amino acid from G to R at position 326.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from P to L at position 31.
+The protein's natural variant, known as in a melanoma cell line, features a modification of the amino acid from L to F at position 72.
+The protein's natural variant, known as in a cutaneous metastatic melanoma sample; somatic mutation, features a modification of the amino acid from I to M at position 89.
+The protein's natural variant, known as in a cutaneous metastatic melanoma sample; somatic mutation; increases the adhesion of melanoma cells to collagens I and IV;, features a modification of the amino acid from E to K at position 111.
+The protein's natural variant, known as in a cutaneous metastatic melanoma sample; somatic mutation; increases the adhesion of melanoma cells to collagens I and IV, features a modification of the amino acid from S to F at position 112.
+The protein's natural variant, known as in a cutaneous metastatic melanoma sample; somatic mutation; increases the adhesion of melanoma cells to collagens I and IV, features a modification of the amino acid from S to F at position 115.
+The protein's natural variant, known as in a cutaneous metastatic melanoma sample; somatic mutation, features a modification of the amino acid from D to N at position 131.
+The protein's natural variant, known as in a cutaneous metastatic melanoma sample; somatic mutation;, features a modification of the amino acid from E to K at position 176.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from V to I at position 205.
+The protein's natural variant, known as in a cutaneous metastatic melanoma sample; somatic mutation;, features a modification of the amino acid from S to F at position 234.
+The protein's natural variant, known as in a cutaneous metastatic melanoma sample; somatic mutation; increases the adhesion of melanoma cells to collagens I and IV;, features a modification of the amino acid from I to F at position 257.
+The protein's natural variant, known as in a cutaneous metastatic melanoma sample; somatic mutation;, features a modification of the amino acid from G to E at position 305.
+The protein's natural variant, known as in a cutaneous metastatic melanoma sample; somatic mutation;, features a modification of the amino acid from D to N at position 345.
+The protein's natural variant, known as in a cutaneous metastatic melanoma sample; somatic mutation;, features a modification of the amino acid from G to D at position 403.
+The protein's natural variant, known as in a cutaneous metastatic melanoma sample; somatic mutation; increases the adhesion of melanoma cells to collagens I and IV;, features a modification of the amino acid from G to D at position 434.
+The protein's natural variant, known as in a cutaneous metastatic melanoma sample; somatic mutation; increases the adhesion of melanoma cells to collagens I and IV, features a modification of the amino acid from E to K at position 503.
+The protein's natural variant, known as in a cutaneous metastatic melanoma sample; somatic mutation;, features a modification of the amino acid from H to Y at position 533.
+The protein's natural variant, known as in HLD15; slightly decreased protein level; does not affect multisynthetase complex assembly;, features a modification of the amino acid from P to R at position 1115.
+The protein's natural variant, known as in HLD15; unknown pathological significance; small decrease in aminoacylation activity;, features a modification of the amino acid from M to T at position 1126.
+The protein's natural variant, known as in HLD15; unknown pathological significance;, features a modification of the amino acid from P to S at position 1160.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from L to S at position 176.
+The protein's natural variant, known as in MKS10; unknown pathological significance, features a modification of the amino acid from H to Q at position 5.
+The protein's natural variant, known as in JBTS34; unknown pathological significance;, features a modification of the amino acid from L to P at position 36.
+The protein's natural variant, known as in JBTS34; unknown pathological significance;, features a modification of the amino acid from P to S at position 74.
+The protein's natural variant, known as in MKS10; loss-of-function; could not rescue in vitro dosage-dependent ciliary defects; fails to interact with MKS1 although it retains its ability to interact with B9D1;, features a modification of the amino acid from S to R at position 101.
+The protein's natural variant, known as in JBTS34; unknown pathological significance;, features a modification of the amino acid from G to S at position 155.
+The protein's natural variant, known as in Chinese, features a modification of the amino acid from T to A at position 24.
+The protein's natural variant, known as in 0.05% of European and African populations;, features a modification of the amino acid from R to C at position 52.
+The protein's natural variant, known as associated with low serum mannose-binding protein (MBP) concentrations and recurrent infections;, features a modification of the amino acid from G to D at position 54.
+The protein's natural variant, known as associated with low serum mannose-binding protein (MBP) concentrations; associated with protection against tuberculosis caused by Mycobacterium africanum;, features a modification of the amino acid from G to E at position 57.
+The protein's natural variant, known as in Lt5.4.1, features a modification of the amino acid from A to S at position 55.
+The protein's natural variant, known as in Lt5.4.2, features a modification of the amino acid from K to N at position 56.
+The protein's natural variant, known as in hepatocellular carcinoma; no effect;, features a modification of the amino acid from S to R at position 23.
+The protein's natural variant, known as in hepatocellular carcinoma;, features a modification of the amino acid from D to A at position 32.
+The protein's natural variant, known as in PTR and hepatocellular carcinoma;, features a modification of the amino acid from D to G at position 32.
+The protein's natural variant, known as in PTR, hepatoblastoma and hepatocellular carcinoma;, features a modification of the amino acid from D to Y at position 32.
+The protein's natural variant, known as in PTR, MDB and hepatocellular carcinoma;, features a modification of the amino acid from S to F at position 33.
+The protein's natural variant, known as in hepatocellular carcinoma, features a modification of the amino acid from S to L at position 33.
+The protein's natural variant, known as in colorectal cancer and PTR; constitutively active Wnt signaling pathway; enhances transactivation of target genes;, features a modification of the amino acid from S to Y at position 33.
+The protein's natural variant, known as in PTR;, features a modification of the amino acid from G to E at position 34.
+The protein's natural variant, known as in hepatocellular carcinoma;, features a modification of the amino acid from G to R at position 34.
+The protein's natural variant, known as in hepatoblastoma;, features a modification of the amino acid from G to V at position 34.
+The protein's natural variant, known as in hepatocellular carcinoma, features a modification of the amino acid from I to S at position 35.
+The protein's natural variant, known as in hepatocellular carcinoma, features a modification of the amino acid from SG to W at position 38.
+The protein's natural variant, known as in MDB and hepatocellular carcinoma; enhances transactivation of target genes;, features a modification of the amino acid from S to A at position 37.
+The protein's natural variant, known as in PTR, hepatoblastoma and ovarian cancer;, features a modification of the amino acid from S to C at position 37.
+The protein's natural variant, known as in PTR;, features a modification of the amino acid from S to F at position 37.
+The protein's natural variant, known as in hepatocellular carcinoma;, features a modification of the amino acid from S to Y at position 37.
+The protein's natural variant, known as in hepatoblastoma and hepatocellular carcinoma; also in a desmoid tumor; strongly reduces phosphorylation and degradation; abolishes phosphorylation on Ser-33 and Ser-37 and enhances transactivation of target genes;, features a modification of the amino acid from T to A at position 41.
+The protein's natural variant, known as in PTR, hepatocellular carcinoma and ovarian cancer;, features a modification of the amino acid from T to I at position 41.
+The protein's natural variant, known as in hepatocellular carcinoma;, features a modification of the amino acid from S to F at position 45.
+The protein's natural variant, known as in hepatocellular carcinoma;, features a modification of the amino acid from S to P at position 45.
+The protein's natural variant, known as in NEDSDV, features a modification of the amino acid from L to P at position 388.
+The protein's natural variant, known as in EVR7; unknown pathological significance;, features a modification of the amino acid from R to C at position 710.
+The protein's natural variant, known as in COXPD52; decreased protein expression in homozygous patient cells;, features a modification of the amino acid from R to Q at position 72.
+The protein's natural variant, known as in allele HOXB1*B, features a modification of the amino acid from A to AHSA at position 27.
+The protein's natural variant, known as in HCFP3; decreased transactivation activity at low DNA concentrations; increased transactivation activity at high DNA concentrations compared to wild-type;, features a modification of the amino acid from R to C at position 207.
+The natural variant of this protein is characterized by an amino acid alteration from M to K at position 129.
+The natural variant of this protein is characterized by an amino acid alteration from F to S at position 140.
+The natural variant of this protein is characterized by an amino acid alteration from H to L at position 196.
+The natural variant of this protein is characterized by an amino acid alteration from L to P at position 200.
+The natural variant of this protein is characterized by an amino acid alteration from I to F at position 229.
+The natural variant of this protein is characterized by an amino acid alteration from W to R at position 282.
+The protein's natural variant, known as in strain: Qingyuan Ma, features a modification of the amino acid from S to F at position 9.
+The protein's natural variant, known as in strain: Guangxi Huang, features a modification of the amino acid from L to F at position 33.
+The protein's natural variant, known as in HHHS; abolishes ornithine/ornithine exchange;, features a modification of the amino acid from A to V at position 15.
+The protein's natural variant, known as in HHHS;, features a modification of the amino acid from G to E at position 27.
+The protein's natural variant, known as in HHHS; incapable of catalyzing homo-exchanges of ornithine, arginine, lysine and citrulline;, features a modification of the amino acid from G to R at position 27.
+The protein's natural variant, known as in HHHS; exhibits very low transport activity despite normal insertion in the liposomal membrane;, features a modification of the amino acid from M to R at position 37.
+The protein's natural variant, known as in HHHS; requires 2 nucleotide substitutions; unknown pathological significance;, features a modification of the amino acid from A to L at position 70.
+The protein's natural variant, known as in HHHS; exhibits very low transport activity despite normal insertion in the liposomal membrane;, features a modification of the amino acid from L to Q at position 71.
+The protein's natural variant, known as in HHHS; exhibits very low transport activity despite normal insertion in the liposomal membrane;, features a modification of the amino acid from G to C at position 113.
+The protein's natural variant, known as in HHHS, features a modification of the amino acid from P to R at position 126.
+The protein's natural variant, known as in HHHS; does not affect mitochondrial localization;, features a modification of the amino acid from E to K at position 180.
+The protein's natural variant, known as in HHHS;, features a modification of the amino acid from F to L at position 188.
+The protein's natural variant, known as in HHHS; maintains a residual transport activity of 35%;, features a modification of the amino acid from G to D at position 190.
+The protein's natural variant, known as in HHHS;, features a modification of the amino acid from G to S at position 216.
+The protein's natural variant, known as in HHHS; exhibits very low transport activity despite normal insertion in the liposomal membrane;, features a modification of the amino acid from T to I at position 272.
+The protein's natural variant, known as in HHHS; exhibits very low transport activity despite normal insertion in the liposomal membrane;, features a modification of the amino acid from M to K at position 273.
+The protein's natural variant, known as in HHHS; incapable of catalyzing homo-exchanges of ornithine, arginine, lysine and citrulline;, features a modification of the amino acid from R to Q at position 275.
+The protein's natural variant, known as in HHHS; exhibits very low transport activity despite normal insertion in the liposomal membrane;, features a modification of the amino acid from L to F at position 283.
+The protein's natural variant, known as in allele UGT1A7*2 and allele UGT1A7*3;, features a modification of the amino acid from N to K at position 129.
+The protein's natural variant, known as in allele UGT1A7*2 and allele UGT1A7*3;, features a modification of the amino acid from R to K at position 131.
+The protein's natural variant, known as in allele UGT1A7*3 and allele UGT1A7*4;, features a modification of the amino acid from W to R at position 208.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from A to V at position 2.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from P to S at position 7.
+The protein's natural variant, known as in LQT1; unknown pathological significance; hardly any effect on channel activity, shows fast activation;, features a modification of the amino acid from A to T at position 46.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from S to F at position 66.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from P to T at position 73.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from Y to C at position 111.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from E to G at position 115.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from P to L at position 117.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from C to Y at position 122.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from F to L at position 127.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from V to I at position 133.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from L to P at position 134.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from C to F at position 136.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from L to F at position 137.
+The protein's natural variant, known as in ATFB3; gain of function;, features a modification of the amino acid from S to G at position 140.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from T to A at position 144.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from E to K at position 146.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from T to M at position 153.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from F to C at position 157.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from E to K at position 160.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from V to M at position 162.
+The protein's natural variant, known as in LQT1, features a modification of the amino acid from FG to W at position 168.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from G to R at position 168.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from V to M at position 172.
+The protein's natural variant, known as in LQT1; affects channel activity; when expressed in heterologous system the mutant significantly reduces total IKs steady-state and tail currents with a positive shift of the voltage dependence of activation;, features a modification of the amino acid from V to D at position 173.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from R to C at position 174.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from R to H at position 174.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from R to P at position 174.
+The protein's natural variant, known as in LQT1; loss of channel activity;, features a modification of the amino acid from A to P at position 178.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from A to T at position 178.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from G to S at position 179.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from Y to H at position 184.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from Y to S at position 184.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from G to R at position 186.
+The protein's natural variant, known as in LQT1; familial sudden death;, features a modification of the amino acid from G to R at position 189.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from R to L at position 190.
+The protein's natural variant, known as in LQT1; loss of channel activity;, features a modification of the amino acid from R to Q at position 190.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from R to W at position 190.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from L to P at position 191.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from R to P at position 192.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from A to P at position 194.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from R to W at position 195.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from I to V at position 198.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from S to A at position 199.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from D to H at position 202.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from I to F at position 204.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from I to M at position 204.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from S to F at position 209.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from V to M at position 215.
+The protein's natural variant, known as in LQT1, features a modification of the amino acid from G to R at position 216.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from T to M at position 224.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from S to L at position 225.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from R to C at position 231.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from R to H at position 231.
+The protein's natural variant, known as in LQT1; decreases delayed rectifier potassium current Iks; prevents the up-regulation of Iks through PKA activation;, features a modification of the amino acid from I to N at position 235.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from L to P at position 239.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from V to G at position 241.
+The protein's natural variant, known as in LQT1; decreases outward potassium current; decreases plasma membrane localization;, features a modification of the amino acid from D to N at position 242.
+The protein's natural variant, known as in LQT1; slower rate of activation and voltage dependence of activation-inactivation shifted to more positive potentials (homomultimers); channels non-functional (heteromultimers);, features a modification of the amino acid from R to C at position 243.
+The protein's natural variant, known as in JLNS1; minor changes of wt current (homomultimers); positive voltage shift of the channel activation (heteromultimers);, features a modification of the amino acid from R to H at position 243.
+The protein's natural variant, known as in LQT1; complete loss of outward potassium current; enhances outward potassium current when co-transfected with wild type; decreases plasma membrane localization;, features a modification of the amino acid from R to P at position 243.
+The protein's natural variant, known as in JLNS1; requires 2 nucleotide substitutions; does not affect plasma membrane localization; complete loss of outward currents; enhances outward currents when coexpressed with wild type at equimolar ratio;, features a modification of the amino acid from W to F at position 248.
+The protein's natural variant, known as in LQT1; slower rate of activation and voltage dependence of activation-inactivation shifted to more positive potentials (homomultimers); channels non-functional (heteromultimers);, features a modification of the amino acid from W to R at position 248.
+The protein's natural variant, known as in LQT1; complete loss of outward potassium current; enhances outward potassium current when co-transfected with wild type; decreases plasma membrane localization;, features a modification of the amino acid from L to H at position 250.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from L to P at position 250.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from V to L at position 254.
+The protein's natural variant, known as in LQT1; associated with M-417 in a patient;, features a modification of the amino acid from V to M at position 254.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from H to N at position 258.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from H to R at position 258.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from R to C at position 259.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from R to H at position 259.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from R to L at position 259.
+The protein's natural variant, known as in JLNS1;, features a modification of the amino acid from E to D at position 261.
+The protein's natural variant, known as in LQT1; loss of channel activity and no interaction with wt KVLQT1 or MINK subunits;, features a modification of the amino acid from E to K at position 261.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from L to V at position 262.
+The protein's natural variant, known as in LQT1; unknown pathological significance; no effect on channel activity;, features a modification of the amino acid from T to I at position 265.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from L to P at position 266.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from I to S at position 268.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from G to D at position 269.
+The protein's natural variant, known as in LQT1; decreases IKs amplitude; accelerates the IKs deactivation; effect on plasma membrane localization; reduces up-regulation of Iks through PKA activation;, features a modification of the amino acid from G to S at position 269.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from G to D at position 272.
+The protein's natural variant, known as in LQT1; functional channel with reduced macroscopic conductance (homomultimers); alteration of normal KVLQT1 function (mut/wt homomultimers);, features a modification of the amino acid from L to F at position 273.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from L to R at position 273.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from I to V at position 274.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from F to S at position 275.
+The protein's natural variant, known as in LQT1; loss of function mutation acting in a dominant-negative manner;, features a modification of the amino acid from S to L at position 277.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from S to P at position 277.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from S to W at position 277.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from Y to H at position 278.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from V to E at position 280.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from Y to C at position 281.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from L to P at position 282.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from A to G at position 283.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from A to E at position 287.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from E to K at position 290.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from G to D at position 292.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from R to C at position 293.
+The protein's natural variant, known as in LQT1; loss of channel activity;, features a modification of the amino acid from F to S at position 296.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from A to T at position 300.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from A to E at position 302.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from A to T at position 302.
+The protein's natural variant, known as in LQT1; loss of channel activity;, features a modification of the amino acid from A to V at position 302.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from L to P at position 303.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from W to R at position 304.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from W to R at position 305.
+The protein's natural variant, known as in JLNS1;, features a modification of the amino acid from W to S at position 305.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from G to R at position 306.
+The protein's natural variant, known as in LQT1; complete loss of outward potassium current; enhances outward potassium current when co-transfected with wild type; decreases plasma membrane localization;, features a modification of the amino acid from G to V at position 306.
+The protein's natural variant, known as in SQT2; gain of function;, features a modification of the amino acid from V to L at position 307.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from V to D at position 308.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from T to R at position 309.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from V to I at position 310.
+The protein's natural variant, known as in LQT1 and JLNS1; impairs outward potassium current; affects plasma membrane localization;, features a modification of the amino acid from T to I at position 311.
+The protein's natural variant, known as in LQT1; loss of channel activity;, features a modification of the amino acid from T to I at position 312.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from I to M at position 313.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from G to C at position 314.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from G to D at position 314.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from G to R at position 314.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from G to S at position 314.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from Y to C at position 315.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from Y to S at position 315.
+The protein's natural variant, known as in LQT1; loss of channel activity;, features a modification of the amino acid from G to E at position 316.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from G to R at position 316.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from G to V at position 316.
+The protein's natural variant, known as in LQT1; complete loss of outward potassium current when expressed alone and even in the presence of the wild type at variable ratios; decreases plasma membrane localization;, features a modification of the amino acid from D to N at position 317.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from K to N at position 318.
+The protein's natural variant, known as in LQT1; loss of function mutation acting in a dominant-negative manner;, features a modification of the amino acid from P to A at position 320.
+The protein's natural variant, known as in LQT1; loss of function mutation acting in a dominant-negative manner;, features a modification of the amino acid from P to H at position 320.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from P to S at position 320.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from T to A at position 322.
+The protein's natural variant, known as in JLNS1 and LQT1; impairs outward potassium current; affects plasma membrane localization;, features a modification of the amino acid from T to M at position 322.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from G to R at position 325.
+The protein's natural variant, known as in LQT1; loss of channel activity;, features a modification of the amino acid from F to S at position 339.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from F to Y at position 339.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from A to E at position 341.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from A to G at position 341.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from A to V at position 341.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from L to F at position 342.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from P to L at position 343.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from P to R at position 343.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from P to S at position 343.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from A to E at position 344.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from A to V at position 344.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from G to E at position 345.
+The protein's natural variant, known as in LQT1; familial sudden death;, features a modification of the amino acid from G to R at position 345.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from S to P at position 349.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from S to W at position 349.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from G to R at position 350.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from F to S at position 351.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from L to P at position 353.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from K to R at position 354.
+The protein's natural variant, known as in LQT1; loss of channel activity;, features a modification of the amino acid from R to G at position 360.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from R to M at position 360.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from R to T at position 360.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from K to R at position 362.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from N to H at position 365.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from R to P at position 366.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from R to Q at position 366.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from R to W at position 366.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from A to T at position 371.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from A to D at position 372.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from S to P at position 373.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from L to H at position 374.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from W to G at position 379.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from R to S at position 380.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from E to K at position 385.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from S to P at position 389.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from S to Y at position 389.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from T to I at position 391.
+The protein's natural variant, known as in LQT1; unknown pathological significance, features a modification of the amino acid from T to TT at position 391.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from W to R at position 392.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from K to M at position 393.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from R to W at position 397.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from K to R at position 398.
+The protein's natural variant, known as in LQT1; associated with M-254 in a patient;, features a modification of the amino acid from V to M at position 417.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from D to E at position 446.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from P to L at position 448.
+The protein's natural variant, known as in LQT1; benign variant;, features a modification of the amino acid from P to R at position 448.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from R to W at position 451.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from R to W at position 452.
+The protein's natural variant, known as in LQT1; loss of channel activity;, features a modification of the amino acid from H to Y at position 455.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from G to S at position 460.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from P to L at position 477.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from R to W at position 511.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from R to G at position 518.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from R to P at position 518.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from R to Q at position 518.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from M to R at position 520.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from Y to S at position 522.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from V to G at position 524.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from A to T at position 525.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from A to V at position 525.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from K to E at position 526.
+The protein's natural variant, known as in LQT1; minor changes of wt current (homomultimers); positive voltage shift of the channel activation (heteromultimers);, features a modification of the amino acid from R to W at position 533.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from R to Q at position 539.
+The protein's natural variant, known as in LQT1; minor changes of wt current (homomultimers); positive voltage shift of the channel activation (heteromultimers);, features a modification of the amino acid from R to W at position 539.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from V to I at position 541.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from E to K at position 543.
+The protein's natural variant, known as in LQT1; decreases interaction with KCNE1 C-terminus; does not affect plasma membrane localization; reduces IKS current density; impairs binding with phosphatidylinositol 4,5-bisphosphate; loss of channel activity;, features a modification of the amino acid from S to L at position 546.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from Q to R at position 547.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from G to D at position 548.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from V to A at position 554.
+The protein's natural variant, known as in LQT1; associated with a fruste phenotype; decreases interaction with KCNE1 C-terminus; does not affect plasma membrane localization; reduces IKS current density; shifts activation of the voltage dependence; deactivates more rapidly; impairs binding with phosphatidylinositol 4,5-bisphosphate;, features a modification of the amino acid from R to C at position 555.
+The protein's natural variant, known as in LQT1; decreases interaction with KCNE1 C-terminus; does not affect plasma membrane localization; reduces IKS current density; impairs binding with Phosphatidylinositol 4,5-bisphosphate;, features a modification of the amino acid from R to H at position 555.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from R to S at position 555.
+The protein's natural variant, known as in LQT1; no effect on cell membrane localization; slows activation kinetics; accelerates deactivation kinetics; rightshifts the voltage-dependent activation; does not affect cAMP-dependent up-regulation; decreases interaction with KCNE1 C-terminus; does not affect plasma membrane localization; does not affect phosphorylation at S-27 during cAMP-dependent stimulation; reduces IKS current density; impairs binding with Phosphatidylinositol 4,5-bisphosphate;, features a modification of the amino acid from K to E at position 557.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from S to F at position 566.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from S to P at position 566.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from S to Y at position 566.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from I to S at position 567.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from I to T at position 567.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from G to R at position 568.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from K to E at position 569.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from S to L at position 571.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from F to L at position 573.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from R to C at position 583.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from R to H at position 583.
+The protein's natural variant, known as in LQT1; decreases outward potassium current; decreases plasma membrane localization;, features a modification of the amino acid from N to D at position 586.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from T to M at position 587.
+The protein's natural variant, known as in LQT1 and JLNS1; affects plasma membrane localization; strongly reduces potassium current; impairs binding to AKAP9 and the targeting protein kinase A (PKA) catalytic subunit and protein phosphatase 1 (PP1);, features a modification of the amino acid from G to D at position 589.
+The protein's natural variant, known as in LQT1; reduces IKs density and causes a right-shift of the current?voltage relation of channel activation; reduces cell surface expression; no effect on interaction with AKAP9; does not affect the cAMP-dependent IKs up-regulation;, features a modification of the amino acid from A to T at position 590.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from R to C at position 591.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from R to H at position 591.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from R to P at position 594.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from R to Q at position 594.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from E to K at position 596.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from T to M at position 600.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from D to N at position 611.
+The protein's natural variant, known as in LQT1; decreases outward potassium current; decreases plasma membrane localization;, features a modification of the amino acid from L to M at position 619.
+The protein's natural variant, known as in LQT1;, features a modification of the amino acid from G to S at position 626.
+The protein's natural variant, known as in LQT1; unknown pathological significance;, features a modification of the amino acid from G to R at position 635.
+The protein's natural variant, known as in strain: Isolate 1, features a modification of the amino acid from T to A at position 176.
+The protein's natural variant, known as in strain: Isolate 3, features a modification of the amino acid from F to L at position 303.
+The protein's natural variant, known as in allele CLEC18A-1;, features a modification of the amino acid from V to A at position 118.
+The protein's natural variant, known as in allele CLEC18A-1;, features a modification of the amino acid from T to M at position 151.
+The protein's natural variant, known as in allele CLEC18A-1; abolishes binding to polysaccharides, features a modification of the amino acid from S to R at position 339.
+The protein's natural variant, known as in INCCR5-71A; results in absent sulfation and greatly decreased binding CCL4 and CCL5 when associated with D-3, D-10 and D-15; restored most CCL4 binding when associated with D-3 and D-15, features a modification of the amino acid from Y to D at position 10.
+The natural variant of this protein is characterized by an amino acid alteration from I to L at position 12.
+The protein's natural variant, known as in INCCR5-72A;, features a modification of the amino acid from R to H at position 31.
+The protein's natural variant, known as in TZCCR5-179, features a modification of the amino acid from P to L at position 34.
+The protein's natural variant, known as associated with susceptibility to HIV-1; reduced cell surface expression; may be associated with reduced susceptibility to infection by microbes that depend on these molecules as their receptors;, features a modification of the amino acid from R to S at position 60.
+The protein's natural variant, known as in UGCCR5-145B, features a modification of the amino acid from K to R at position 62.
+The protein's natural variant, known as in ZWCCR5-7;, features a modification of the amino acid from Y to H at position 68.
+The protein's natural variant, known as in MWCCR5-107;, features a modification of the amino acid from D to N at position 95.
+The protein's natural variant, known as in INCCR5-467, features a modification of the amino acid from G to E at position 97.
+The protein's natural variant, known as protects against HIV-1 infection; CD4+ T-cells from R-106 carriers are less susceptible to infection by HIV-1 R5; results in reduced CCR5 surface expression;, features a modification of the amino acid from G to R at position 106.
+The protein's natural variant, known as in ZWCCR5-7, features a modification of the amino acid from L to P at position 122.
+The protein's natural variant, known as in UGCCR5-145A, features a modification of the amino acid from F to S at position 158.
+The protein's natural variant, known as in KECCR5-116, features a modification of the amino acid from Y to C at position 176.
+The protein's natural variant, known as in INCCR5-45C, features a modification of the amino acid from T to A at position 177.
+The protein's natural variant, known as protects against HIV-1 infection; CD4+ T-cells from R-178 carriers are less susceptible to infection by HIV-1 R5; results in reduced CCR5 surface expression;, features a modification of the amino acid from C to R at position 178.
+The protein's natural variant, known as in UGCCR5-145A, features a modification of the amino acid from S to N at position 185.
+The protein's natural variant, known as in ZWCCR5-7, features a modification of the amino acid from M to V at position 210.
+The protein's natural variant, known as in KECCR5-3B, features a modification of the amino acid from Y to C at position 214.
+The protein's natural variant, known as in INCCR5-71A, features a modification of the amino acid from T to S at position 239.
+The protein's natural variant, known as in UGCCR5-145A;, features a modification of the amino acid from L to P at position 246.
+The protein's natural variant, known as in INCCR5-72A;, features a modification of the amino acid from T to M at position 288.
+The protein's natural variant, known as in TZCCR5-179, features a modification of the amino acid from E to G at position 302.
+The protein's natural variant, known as in THCCR5-5, features a modification of the amino acid from K to E at position 303.
+The protein's natural variant, known as in MWCCR5-1567, features a modification of the amino acid from N to S at position 306.
+The protein's natural variant, known as in THCCR5-5, features a modification of the amino acid from K to R at position 322.
+The protein's natural variant, known as in THCCR5-2, features a modification of the amino acid from E to G at position 333.
+The protein's natural variant, known as in MWCCR5-1567, MWCCR5-1568, ZWCCR5-14 and ZWCCR5-112;, features a modification of the amino acid from A to V at position 335.
+The protein's natural variant, known as in TZCCR5-181A and MWCCR5-107;, features a modification of the amino acid from Y to F at position 339.
+The protein's natural variant, known as in UGCCR5-145C, features a modification of the amino acid from E to G at position 345.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 468.
+The natural variant of this protein is characterized by an amino acid alteration from N to D at position 720.
+The protein's natural variant, known as in strain: cv. Mr-0, features a modification of the amino acid from R to Q at position 170.
+The protein's natural variant, known as in strain: C57BL/6J, features a modification of the amino acid from Q to R at position 481.
+The protein's natural variant, known as in CN2; mutant protein rapidly degraded by the proteasome owing to its mislocalization in the cell;, features a modification of the amino acid from L to R at position 15.
+The protein's natural variant, known as in CN2, features a modification of the amino acid from P to Q at position 34.
+The protein's natural variant, known as in CN1, features a modification of the amino acid from D to N at position 36.
+The protein's natural variant, known as in CN1;, features a modification of the amino acid from H to D at position 39.
+The protein's natural variant, known as in CN2, GILBS and HBLRTFN; has significant residual bilirubin glucuronidation activity of about 25% to 50% of that of the wild-type protein; displays no change in biluribin affinity;, features a modification of the amino acid from G to R at position 71.
+The protein's natural variant, known as in GILBS; displays less than 10% of wild-type bilirubin glucuronidation activity;, features a modification of the amino acid from F to L at position 83.
+The protein's natural variant, known as in CN2; has low residual bilirubin glucuronidation activity of about 4.6% of that of the wild-type protein;, features a modification of the amino acid from L to Q at position 175.
+The protein's natural variant, known as in CN1;, features a modification of the amino acid from C to R at position 177.
+The protein's natural variant, known as in CN2; has low residual bilirubin glucuronidation activity of about 5.3% of that of the wild-type protein, features a modification of the amino acid from S to F at position 191.
+The protein's natural variant, known as in CN2; has low residual bilirubin glucuronidation activity of about 2.9% of that of the wild-type protein;, features a modification of the amino acid from R to W at position 209.
+The protein's natural variant, known as in CN2;, features a modification of the amino acid from V to G at position 225.
+The protein's natural variant, known as in CN2 and GILBS; displays 2-fold decrease in biluribin affinity and 61% of wild-type bilirubin glucuronidation activity;, features a modification of the amino acid from P to Q at position 229.
+The protein's natural variant, known as in CN2;, features a modification of the amino acid from Y to C at position 230.
+The protein's natural variant, known as in CN1;, features a modification of the amino acid from G to R at position 276.
+The protein's natural variant, known as in CN2;, features a modification of the amino acid from N to Y at position 279.
+The protein's natural variant, known as in CN1, features a modification of the amino acid from E to V at position 291.
+The protein's natural variant, known as in CN1;, features a modification of the amino acid from A to V at position 292.
+The protein's natural variant, known as in GILBS and CN2; 40-55% normal bilirubin glucuronidation activity; normal Km for bilirubin; when homozygous far less repressive and generates the mild Gilbert phenotype;, features a modification of the amino acid from I to T at position 294.
+The protein's natural variant, known as in CN1; no bilirubin glucuronidation activity;, features a modification of the amino acid from G to E at position 308.
+The protein's natural variant, known as in CN2; has no residual bilirubin glucuronidation activity;, features a modification of the amino acid from Q to R at position 331.
+The protein's natural variant, known as in CN1 and CN2, features a modification of the amino acid from R to L at position 336.
+The protein's natural variant, known as in CN1;, features a modification of the amino acid from R to Q at position 336.
+The protein's natural variant, known as in CN2; has very low residual bilirubin glucuronidation activity of about 0.4% of that of the wild-type protein;, features a modification of the amino acid from R to W at position 336.
+The protein's natural variant, known as in CN2;, features a modification of the amino acid from W to R at position 354.
+The protein's natural variant, known as in CN1;, features a modification of the amino acid from Q to R at position 357.
+The protein's natural variant, known as in CN2;, features a modification of the amino acid from R to C at position 367.
+The protein's natural variant, known as in GILBS;, features a modification of the amino acid from R to G at position 367.
+The protein's natural variant, known as in CN1;, features a modification of the amino acid from A to T at position 368.
+The protein's natural variant, known as in CN2;, features a modification of the amino acid from I to V at position 370.
+The protein's natural variant, known as in CN1; no bilirubin glucuronidation activity;, features a modification of the amino acid from S to F at position 375.
+The protein's natural variant, known as in CN1 and CN2;, features a modification of the amino acid from H to R at position 376.
+The protein's natural variant, known as in CN1 and CN2;, features a modification of the amino acid from G to V at position 377.
+The protein's natural variant, known as in CN1;, features a modification of the amino acid from S to R at position 381.
+The protein's natural variant, known as in CN2; has no residual bilirubin glucuronidation activity, features a modification of the amino acid from P to H at position 387.
+The protein's natural variant, known as in CN1;, features a modification of the amino acid from P to S at position 387.
+The protein's natural variant, known as in CN1; has no residual bilirubin glucuronidation activity;, features a modification of the amino acid from G to V at position 395.
+The protein's natural variant, known as in CN2;, features a modification of the amino acid from N to D at position 400.
+The protein's natural variant, known as in CN1;, features a modification of the amino acid from A to P at position 401.
+The protein's natural variant, known as in CN1; has no residual bilirubin glucuronidation activity; N-glycosylation does take place at this new additional site, features a modification of the amino acid from K to T at position 402.
+The protein's natural variant, known as in CN2;, features a modification of the amino acid from R to C at position 403.
+The protein's natural variant, known as in CN1;, features a modification of the amino acid from K to E at position 428.
+The protein's natural variant, known as in CN2; has no residual bilirubin glucuronidation activity;, features a modification of the amino acid from L to P at position 443.
+The protein's natural variant, known as in CN1 and CN2;, features a modification of the amino acid from W to R at position 461.
+The protein's natural variant, known as in CN2, features a modification of the amino acid from A to D at position 478.
+The protein's natural variant, known as in CN2, GILBS and HBLRTFN; displays less than 10% of wild-type bilirubin glucuronidation activity;, features a modification of the amino acid from Y to D at position 486.
+The protein's natural variant, known as in MCPH1; mild phenotype;, features a modification of the amino acid from T to R at position 27.
+The natural variant of this protein is characterized by an amino acid alteration from V to M at position 111.
+The natural variant of this protein is characterized by an amino acid alteration from L to H at position 116.
+The protein's natural variant, known as in MRXSB;, features a modification of the amino acid from R to Q at position 206.
+The protein's natural variant, known as in MRXSB;, features a modification of the amino acid from R to W at position 206.
+The protein's natural variant, known as in MRXSB;, features a modification of the amino acid from P to L at position 209.
+The protein's natural variant, known as in SEDKF; due to a nucleotide substitution that creates a dominant splice donor site in exon 9; two different type of transcripts are produced, a major non-functional alternatively spliced transcript with a 41-bp deletion of exon 9, loss of S-414 in the catalytic triad and premature truncation and a normally spliced transcript with variant G-365; the transcript with G-365 produces a catalytically active protein but is the less abundant;, features a modification of the amino acid from D to G at position 365.
+The protein's natural variant, known as in SEDKF; unknown pathological significance, features a modification of the amino acid from S to R at position 878.
+The protein's natural variant, known as in strain: ATCC 14028 / SGSG 2980 / CDC 6516-60 / NCTC 12023, features a modification of the amino acid from N to D at position 22.
+The protein's natural variant, known as in strain: ATCC 14028 / SGSG 2980 / CDC 6516-60 / NCTC 12023, features a modification of the amino acid from P to L at position 271.
+The protein's natural variant, known as in JBTS31; unknown pathological significance;, features a modification of the amino acid from V to A at position 194.
+The protein's natural variant, known as in SRTD13; also found in a patient with more complex ciliopathy;, features a modification of the amino acid from A to P at position 199.
+The protein's natural variant, known as in JBTS31; unknown pathological significance;, features a modification of the amino acid from A to V at position 549.
+The protein's natural variant, known as in JBTS31; unknown pathological significance;, features a modification of the amino acid from L to F at position 712.
+The protein's natural variant, known as in JBTS31; unknown pathological significance;, features a modification of the amino acid from L to P at position 726.
+The protein's natural variant, known as found in a patient with Meckel syndrome; unknown pathological significance;, features a modification of the amino acid from I to S at position 975.
+The protein's natural variant, known as confirmed at protein level;, features a modification of the amino acid from S to C at position 489.
+The protein's natural variant, known as found in a patient with spastic paraplegia; unknown pathological significance;, features a modification of the amino acid from L to P at position 319.
+The protein's natural variant, known as in CMM5; moderate decrease in coupling to the cAMP pathway; reduced cell surface expression as a consequence of retention in the endoplasmic reticulum;, features a modification of the amino acid from V to M at position 38.
+The protein's natural variant, known as associated with fair hair and light skin; partial loss-of-function;, features a modification of the amino acid from I to T at position 40.
+The protein's natural variant, known as in CMM5; complete absence of functional coupling to the cAMP pathway; reduced cell surface expression as a consequence of retention in the endoplasmic reticulum, features a modification of the amino acid from S to F at position 41.
+The protein's natural variant, known as in CMM5; moderate decrease in coupling to the cAMP pathway; reduced cell surface expression as a consequence of retention in the endoplasmic reticulum;, features a modification of the amino acid from V to A at position 51.
+The protein's natural variant, known as associated with a risk for developing melanoma; unable to stimulate cAMP production as strongly as the wild type receptor in response to alpha-melanocyte-stimulating hormone stimulation;, features a modification of the amino acid from V to L at position 60.
+The protein's natural variant, known as shows a moderate and not significant decrease of cAMP production to NDP-MSH stimulation; shows a decreased responses to low concentrations of NDP-MSH stimulation;, features a modification of the amino acid from R to Q at position 67.
+The protein's natural variant, known as may be associated with a risk for developing melanoma; reduced expression at the cell surface;, features a modification of the amino acid from D to E at position 84.
+The protein's natural variant, known as associated with a risk for developing melanoma; predominantly found in type I skin; shows a moderate and not significant decreased of cAMP production to NDP-MSH stimulation;, features a modification of the amino acid from V to M at position 92.
+The protein's natural variant, known as loss-of-function mutation abolishing agonist binding, features a modification of the amino acid from L to R at position 93.
+The protein's natural variant, known as shows a moderate and not significant decrease of cAMP production to NDP-MSH stimulation; shows decreased responses to low concentrations of NDP-MSH stimulation;, features a modification of the amino acid from I to T at position 120.
+The protein's natural variant, known as associated with fair hair and light skin; partial loss-of-function;, features a modification of the amino acid from V to M at position 122.
+The protein's natural variant, known as in CMM5; complete absence of functional coupling to the cAMP pathway; trafficked to the cell surface but unable to bind agonist efficiently;, features a modification of the amino acid from M to T at position 128.
+The protein's natural variant, known as associated with red hair and light skin of type I; binds to alpha-MSH but cannot be stimulated to produce cAMP; reduced expression at the cell surface;, features a modification of the amino acid from R to C at position 151.
+The protein's natural variant, known as associated with a risk for developing melanoma; reduced expression at the cell surface;, features a modification of the amino acid from I to T at position 155.
+The protein's natural variant, known as associated with UV induced susceptibility to skin damage; shows a dramatically decreased cAMP production to NDP-MSH stimulation;, features a modification of the amino acid from T to I at position 157.
+The protein's natural variant, known as associated with UV induced susceptibility to skin damage; shows a strong decreased cAMP production to NDP-MSH stimulation;, features a modification of the amino acid from P to T at position 159.
+The protein's natural variant, known as associated with a risk for developing melanoma; unable to stimulate cAMP production as strongly as the wild type receptor in response to alpha-melanocyte-stimulating hormone stimulation; reduced expression at the cell surface.;, features a modification of the amino acid from R to W at position 160.
+The natural variant of this protein is characterized by an amino acid alteration from R to P at position 162.
+The protein's natural variant, known as associated with a risk for developing melanoma; shows a moderate and not significant decrease of cAMP production to NDP-MSH stimulation; shows a not significant decrease in cAMP production at any concentrations of NDP-MSH stimulation;, features a modification of the amino acid from R to Q at position 163.
+The protein's natural variant, known as shows a moderate and not significant decrease of cAMP production to NDP-MSH stimulation; shows a not significant decrease in cAMP production at any concentrations of NDP-MSH stimulation;, features a modification of the amino acid from A to G at position 166.
+The protein's natural variant, known as does not affect receptor surface expression, agonist binding and agonist-induced signaling;, features a modification of the amino acid from N to S at position 281.
+The protein's natural variant, known as in CMM5; complete absence of functional coupling to the cAMP pathway; trafficked to the cell surface but unable to bind agonist efficiently;, features a modification of the amino acid from C to R at position 289.
+The protein's natural variant, known as associated with a risk for developing melanoma; unable to stimulate cAMP production as strongly as the wild type receptor in response to alpha-melanocyte-stimulating hormone stimulation;, features a modification of the amino acid from D to H at position 294.
+The protein's natural variant, known as in strain: NZ; INH-resistant, features a modification of the amino acid from S to A at position 94.
+The protein's natural variant, known as in FSGS5;, features a modification of the amino acid from A to T at position 13.
+The protein's natural variant, known as in FSGS5;, features a modification of the amino acid from L to P at position 42.
+The protein's natural variant, known as in CMTDIE; unknown pathological significance;, features a modification of the amino acid from L to R at position 57.
+The protein's natural variant, known as in CMTDIE; unknown pathological significance;, features a modification of the amino acid from F to S at position 68.
+The protein's natural variant, known as in FSGS5; unknown pathological significance;, features a modification of the amino acid from G to S at position 73.
+The protein's natural variant, known as in FSGS5, features a modification of the amino acid from L to P at position 76.
+The protein's natural variant, known as in CMTDIE; de novo mutation; unknown pathological significance;, features a modification of the amino acid from L to R at position 77.
+The protein's natural variant, known as in FSGS5, features a modification of the amino acid from L to P at position 81.
+The protein's natural variant, known as in CMTDIE;, features a modification of the amino acid from C to F at position 104.
+The protein's natural variant, known as in CMTDIE;, features a modification of the amino acid from C to R at position 104.
+The protein's natural variant, known as in CMTDIE;, features a modification of the amino acid from C to W at position 104.
+The protein's natural variant, known as in CMTDIE;, features a modification of the amino acid from V to G at position 105.
+The protein's natural variant, known as in CMTDIE;, features a modification of the amino acid from L to P at position 128.
+The protein's natural variant, known as in CMTDIE;, features a modification of the amino acid from L to P at position 132.
+The protein's natural variant, known as in CMTDIE;, features a modification of the amino acid from L to R at position 132.
+The protein's natural variant, known as in FSGS5, features a modification of the amino acid from C to R at position 151.
+The protein's natural variant, known as in FSGS5, features a modification of the amino acid from H to D at position 158.
+The protein's natural variant, known as in FSGS5, features a modification of the amino acid from L to R at position 162.
+The protein's natural variant, known as in FSGS5;, features a modification of the amino acid from R to C at position 177.
+The protein's natural variant, known as in FSGS5;, features a modification of the amino acid from R to H at position 177.
+The protein's natural variant, known as in FSGS5; unknown pathological significance, features a modification of the amino acid from V to G at position 181.
+The natural variant of this protein is characterized by an amino acid alteration from N to K at position 183.
+The protein's natural variant, known as in CMTDIE and FSGS5;, features a modification of the amino acid from E to K at position 184.
+The protein's natural variant, known as in FSGS5, features a modification of the amino acid from E to Q at position 184.
+The protein's natural variant, known as in FSGS5;, features a modification of the amino acid from S to P at position 186.
+The protein's natural variant, known as in FSGS5, features a modification of the amino acid from Y to H at position 193.
+The protein's natural variant, known as in FSGS5, features a modification of the amino acid from L to R at position 198.
+The protein's natural variant, known as in FSGS5, features a modification of the amino acid from N to D at position 202.
+The protein's natural variant, known as in FSGS5;, features a modification of the amino acid from A to D at position 203.
+The protein's natural variant, known as in FSGS5;, features a modification of the amino acid from R to C at position 214.
+The protein's natural variant, known as in FSGS5;, features a modification of the amino acid from R to H at position 214.
+The protein's natural variant, known as in FSGS5;, features a modification of the amino acid from R to Q at position 218.
+The protein's natural variant, known as in FSGS5;, features a modification of the amino acid from R to W at position 218.
+The protein's natural variant, known as in FSGS5;, features a modification of the amino acid from E to K at position 220.
+The protein's natural variant, known as in FSGS5, features a modification of the amino acid from L to P at position 245.
+The protein's natural variant, known as in a glioblastoma multiforme sample; somatic mutation, features a modification of the amino acid from V to I at position 395.
+The protein's natural variant, known as in FGS4; does not reveal significant alterations induced by the mutation substitution; causes a partial skipping of exon 2 of the protein;, features a modification of the amino acid from R to L at position 28.
+The protein's natural variant, known as in a lung large cell carcinoma sample; somatic mutation, features a modification of the amino acid from G to V at position 96.
+The protein's natural variant, known as in MICPCH;, features a modification of the amino acid from Y to H at position 268.
+The protein's natural variant, known as in MICPCH;, features a modification of the amino acid from P to S at position 396.
+The protein's natural variant, known as in MICPCH;, features a modification of the amino acid from D to G at position 710.
+The protein's natural variant, known as in MPLPF; unknown pathological significance; no effect on localization;, features a modification of the amino acid from R to W at position 164.
+The protein's natural variant, known as in MPLPF; unknown pathological significance;, features a modification of the amino acid from I to T at position 396.
+The protein's natural variant, known as in MPLPF; no effect on localization; changed interaction with spliceosomal complexes;, features a modification of the amino acid from R to H at position 525.
+The protein's natural variant, known as found in a patient with age-related cataract; unknown pathological significance; decreases creatine transport;, features a modification of the amino acid from G to S at position 437.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to Q at position 21.
+The protein's natural variant, known as identified in a patient with mtDNA maintenance disorders;, features a modification of the amino acid from H to Y at position 269.
+The protein's natural variant, known as identified in a patient with mtDNA maintenance disorders;, features a modification of the amino acid from N to H at position 392.
+The protein's natural variant, known as in CDG2Y; unknown pathological significance, features a modification of the amino acid from R to H at position 122.
+The protein's natural variant, known as in CDG2Y; unknown pathological significance, features a modification of the amino acid from I to M at position 279.
+The protein's natural variant, known as in NMIHBA; loss of function in regulation of cell proliferation and migration; loss of function in neurogenesis; impaired regulation of microtubule polymerization; increased phosphatase activity; no effect on interaction with tubulin beta;, features a modification of the amino acid from D to N at position 30.
+The protein's natural variant, known as in NMIHBA; unknown pathological significance;, features a modification of the amino acid from P to T at position 54.
+The protein's natural variant, known as in NMIHBA;, features a modification of the amino acid from D to N at position 106.
+The protein's natural variant, known as in NMIHBA;, features a modification of the amino acid from R to Q at position 128.
+The protein's natural variant, known as in NMIHBA; loss of function in regulation of cell proliferation and migration; loss of function in neurogenesis; impaired regulation of microtubule polymerization; increased phosphatase activity; decreased interaction with tubulin beta;, features a modification of the amino acid from R to W at position 297.
+The protein's natural variant, known as identified in warfarin-resistant animals, features a modification of the amino acid from L to S at position 128.
+The protein's natural variant, known as identified in warfarin-resistant animals, features a modification of the amino acid from Y to C at position 139.
+The protein's natural variant, known as in strain: cv. No-0, features a modification of the amino acid from L to V at position 13.
+The protein's natural variant, known as in strain: cv. Cvi-1 and cv. No-0, features a modification of the amino acid from K to N at position 112.
+The protein's natural variant, known as in strain: cv. Cvi-1, cv. Landsberg erecta, cv. No-0 and cv. Wassilewskija, features a modification of the amino acid from Y to C at position 141.
+The protein's natural variant, known as in strain: cv. Cvi-1 and cv. No-0, features a modification of the amino acid from E to D at position 161.
+The protein's natural variant, known as inhibition of IFNB induction;, features a modification of the amino acid from T to I at position 4.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from M to I at position 46.
+The protein's natural variant, known as inhibition of IFNB induction;, features a modification of the amino acid from S to C at position 60.
+The protein's natural variant, known as no effect on IFNB induction;, features a modification of the amino acid from R to Q at position 71.
+The protein's natural variant, known as no effect on IFNB induction;, features a modification of the amino acid from V to M at position 80.
+The protein's natural variant, known as no effect on IFNB induction;, features a modification of the amino acid from A to T at position 111.
+The protein's natural variant, known as no effect on IFNB induction;, features a modification of the amino acid from T to M at position 157.
+The protein's natural variant, known as in IIAE6; no effect on IFNB induction;, features a modification of the amino acid from S to L at position 186.
+The protein's natural variant, known as no effect on IFNB induction, features a modification of the amino acid from V to L at position 302.
+The protein's natural variant, known as no effect on IFNB induction;, features a modification of the amino acid from T to I at position 377.
+The protein's natural variant, known as no effect on IFNB induction, features a modification of the amino acid from L to P at position 386.
+The protein's natural variant, known as inhibition of IFNB induction, features a modification of the amino acid from Q to K at position 392.
+The protein's natural variant, known as no effect on IFNB induction, features a modification of the amino acid from S to N at position 465.
+The protein's natural variant, known as no effect on IFNB induction;, features a modification of the amino acid from D to N at position 557.
+The protein's natural variant, known as no effect on IFNB induction;, features a modification of the amino acid from M to L at position 595.
+The protein's natural variant, known as no effect on IFNB induction;, features a modification of the amino acid from G to W at position 598.
+The protein's natural variant, known as no effect on IFNB induction, features a modification of the amino acid from Q to R at position 702.
+The protein's natural variant, known as in strain: ECOR 70, features a modification of the amino acid from S to L at position 2.
+The protein's natural variant, known as in strain: ECOR 70, features a modification of the amino acid from F to Y at position 32.
+The protein's natural variant, known as in strain: O7:K1 / VW187, features a modification of the amino acid from T to Q at position 39.
+The protein's natural variant, known as in strain: ECOR 10, features a modification of the amino acid from V to D at position 52.
+The protein's natural variant, known as in strain: ECOR 10, features a modification of the amino acid from Y to F at position 55.
+The protein's natural variant, known as in strain: ECOR 65, features a modification of the amino acid from N to K at position 102.
+The protein's natural variant, known as in strain: ECOR 70, features a modification of the amino acid from A to S at position 117.
+The protein's natural variant, known as in strain: O7:K1 / VW187, features a modification of the amino acid from IGT to YRY at position 125.
+The protein's natural variant, known as in strain: ECOR 10, features a modification of the amino acid from V to F at position 170.
+The protein's natural variant, known as in strain: ECOR 45, features a modification of the amino acid from A to S at position 175.
+The protein's natural variant, known as in strain: ECOR 68, features a modification of the amino acid from N to S at position 209.
+The protein's natural variant, known as in strain: ECOR 10 and ECOR 69, features a modification of the amino acid from T to S at position 211.
+The protein's natural variant, known as in strain: ECOR 67, features a modification of the amino acid from A to T at position 216.
+The protein's natural variant, known as in strain: ECOR 70, features a modification of the amino acid from D to E at position 294.
+The protein's natural variant, known as in strain: ECOR 68, features a modification of the amino acid from A to G at position 308.
+The protein's natural variant, known as in strain: ECOR 67, features a modification of the amino acid from D to N at position 313.
+The protein's natural variant, known as in strain: ECOR 70, features a modification of the amino acid from A to G at position 315.
+The protein's natural variant, known as in strain: ECOR 69, features a modification of the amino acid from L to Q at position 325.
+The protein's natural variant, known as in strain: ECOR 10, features a modification of the amino acid from I to S at position 330.
+The protein's natural variant, known as in strain: ECOR 10 and ECOR 69, features a modification of the amino acid from D to A at position 350.
+The protein's natural variant, known as in strain: ECOR 10, features a modification of the amino acid from Q to R at position 369.
+The protein's natural variant, known as in strain: ECOR 10, ECOR 65, ECOR 68, ECOR 69 and ECOR 70, features a modification of the amino acid from S to A at position 422.
+The protein's natural variant, known as in strain: PA48, features a modification of the amino acid from T to A at position 69.
+The protein's natural variant, known as in strain: OCR1; leads to increased expression of mexAB-oprM, features a modification of the amino acid from R to W at position 70.
+The protein's natural variant, known as in strain: PA41, features a modification of the amino acid from L to F at position 95.
+The protein's natural variant, known as in strain: 58823, 65629, 55699 and GRR, features a modification of the amino acid from V to E at position 126.
+The protein's natural variant, known as in strain: PA36, features a modification of the amino acid from T to S at position 130.
+The protein's natural variant, known as in a glioblastoma multiforme sample; somatic mutation;, features a modification of the amino acid from P to L at position 198.
+The protein's natural variant, known as in strain: CLIB 95, CLIB 219, CLIB 382, CLIB 388, CLIB 410, CLIB 413, CLIB 556, CLIB 630, K1, R12, R13, YIIc12 and YIIc17, features a modification of the amino acid from N to D at position 9.
+The protein's natural variant, known as in strain: CLIB 219, CLIB 388, CLIB 410, CLIB 413, CLIB 556, CLIB 630, YIIc12 haplotype Ha2 and YIIc17 haplotype Ha2, features a modification of the amino acid from F to L at position 47.
+The protein's natural variant, known as in strain: CLIB 95, CLIB 382, CLIB 556 haplotype Ha1, K1, R12, R13, YIIc12 haplotype Ha1 and YIIc17 haplotype Ha1, features a modification of the amino acid from I to V at position 75.
+The protein's natural variant, known as in strain: CLIB 388, features a modification of the amino acid from L to F at position 77.
+The protein's natural variant, known as in strain: CLIB 388, features a modification of the amino acid from L to P at position 86.
+The protein's natural variant, known as in strain: CLIB 95, CLIB 219, CLIB 382, CLIB 388, CLIB 410, CLIB 413, CLIB 556, CLIB 630, K1, R12, R13, YIIc12 and YIIc17, features a modification of the amino acid from S to N at position 96.
+The protein's natural variant, known as in strain: CLIB 388, CLIB 410, CLIB 556 haplotype Ha2, CLIB 630, YIIc12 haplotype Ha2 and YIIc17 haplotype Ha2, features a modification of the amino acid from R to T at position 103.
+The protein's natural variant, known as in strain: CLIB 95, CLIB 219, CLIB 382, CLIB 388, CLIB 410, CLIB 413, CLIB 556, CLIB 630, K1, R12, R13, YIIc12 and YIIc17, features a modification of the amino acid from M to V at position 124.
+The protein's natural variant, known as in strain: R12 haplotype Ha2, features a modification of the amino acid from I to M at position 145.
+The protein's natural variant, known as in strain: CLIB 95, CLIB 219, CLIB 382, CLIB 388, CLIB 410, CLIB 413, CLIB 556, CLIB 630, K1, R12, R13, YIIc12 and YIIc17, features a modification of the amino acid from Y to S at position 157.
+The protein's natural variant, known as in strain: CLIB 556 haplotype Ha1, features a modification of the amino acid from Q to R at position 160.
+The protein's natural variant, known as in strain: CLIB 95, CLIB 382, K1, R12, R13, YIIc12 haplotype Ha1 and YIIc17 haplotype Ha1, features a modification of the amino acid from Y to D at position 180.
+The protein's natural variant, known as in strain: CLIB 95, CLIB 219, CLIB 382, CLIB 388, CLIB 410, CLIB 413, CLIB 556, CLIB 630, K1, R12, R13, YIIc12 and YIIc17, features a modification of the amino acid from G to A at position 189.
+The protein's natural variant, known as in strain: CLIB 630, features a modification of the amino acid from EDKYPEMGVTV to RISIQRWGTQF at position 235.
+The protein's natural variant, known as in strain: CLIB 219, CLIB 388, CLIB 410, CLIB 413, CLIB 556, CLIB 630, YIIc12 haplotype Ha2 and YIIc17 haplotype Ha2, features a modification of the amino acid from V to D at position 233.
+The protein's natural variant, known as in strain: CLIB 413 haplotype Ha1, features a modification of the amino acid from T to I at position 234.
+The protein's natural variant, known as found in an endometrial carcinoma sample; no effect on its nuclear localization; loss of its ability to inhibit cell proliferation; unknown pathological significance;, features a modification of the amino acid from R to C at position 278.
+The protein's natural variant, known as in a Wilms' tumor;, features a modification of the amino acid from R to W at position 339.
+The protein's natural variant, known as found in an endometrial carcinoma sample; no effect on its nuclear localization; loss of its ability to inhibit cell proliferation; unknown pathological significance, features a modification of the amino acid from R to H at position 342.
+The protein's natural variant, known as in a breast tumor;, features a modification of the amino acid from K to E at position 344.
+The protein's natural variant, known as in a prostate tumor, features a modification of the amino acid from H to R at position 345.
+The protein's natural variant, known as found in an endometrial carcinoma sample; no effect on its nuclear localization; no loss of its ability to inhibit cell proliferation; unknown pathological significance, features a modification of the amino acid from K to T at position 365.
+The protein's natural variant, known as in a Wilms' tumor, features a modification of the amino acid from R to Q at position 448.
+The protein's natural variant, known as in MRD21;, features a modification of the amino acid from R to W at position 567.
+The protein's natural variant, known as in NEDCHS; occurs in a splice site resulting in altered splicing and probable nonsense-mediated mRNA decay;, features a modification of the amino acid from D to G at position 298.
+The protein's natural variant, known as in ICF1;, features a modification of the amino acid from S to P at position 270.
+The protein's natural variant, known as in FSHD4, features a modification of the amino acid from C to R at position 527.
+The protein's natural variant, known as in ICF1;, features a modification of the amino acid from A to T at position 585.
+The protein's natural variant, known as in ICF1, features a modification of the amino acid from A to V at position 585.
+The protein's natural variant, known as in ICF1;, features a modification of the amino acid from A to T at position 603.
+The protein's natural variant, known as in ICF1;, features a modification of the amino acid from V to A at position 606.
+The protein's natural variant, known as in ICF1;, features a modification of the amino acid from G to S at position 663.
+The protein's natural variant, known as in ICF1, features a modification of the amino acid from L to P at position 664.
+The protein's natural variant, known as in FSHD4;, features a modification of the amino acid from P to L at position 691.
+The protein's natural variant, known as in ICF1, features a modification of the amino acid from V to G at position 699.
+The protein's natural variant, known as in ICF1;, features a modification of the amino acid from V to G at position 726.
+The protein's natural variant, known as in ICF1;, features a modification of the amino acid from A to P at position 766.
+The protein's natural variant, known as in ICF1, features a modification of the amino acid from E to ESTP at position 806.
+The protein's natural variant, known as in ICF1;, features a modification of the amino acid from H to R at position 814.
+The protein's natural variant, known as in ICF1;, features a modification of the amino acid from D to G at position 817.
+The protein's natural variant, known as in ICF1;, features a modification of the amino acid from V to M at position 818.
+The protein's natural variant, known as in ICF1; unknown pathological significance;, features a modification of the amino acid from V to M at position 836.
+The protein's natural variant, known as in ICF1;, features a modification of the amino acid from R to Q at position 840.
+The protein's natural variant, known as in strain: 63915, features a modification of the amino acid from V to I at position 386.
+The protein's natural variant, known as in strain: 63915, features a modification of the amino acid from E to K at position 397.
+The protein's natural variant, known as in strain: 63915, features a modification of the amino acid from M to I at position 523.
+The protein's natural variant, known as in strain: 45607, features a modification of the amino acid from D to E at position 533.
+The protein's natural variant, known as in strain: 63915, features a modification of the amino acid from T to S at position 540.
+The protein's natural variant, known as in strain: 45607, features a modification of the amino acid from N to S at position 657.
+The protein's natural variant, known as in TBRS; somatic mutation;, features a modification of the amino acid from I to N at position 310.
+The protein's natural variant, known as in HESJAS; no effect on protein expression; changed DNA methylation; results in aberrant expression of genes involved in developmental processes, features a modification of the amino acid from W to R at position 330.
+The protein's natural variant, known as in HESJAS; changed DNA methylation; results in aberrant expression of genes involved in developmental processes, features a modification of the amino acid from D to N at position 333.
+The protein's natural variant, known as in TBRS; unknown pathological significance;, features a modification of the amino acid from Y to C at position 365.
+The protein's natural variant, known as in TBRS; unknown pathological significance;, features a modification of the amino acid from D to N at position 529.
+The protein's natural variant, known as in TBRS; somatic mutation;, features a modification of the amino acid from G to S at position 532.
+The protein's natural variant, known as in TBRS; somatic mutation;, features a modification of the amino acid from M to K at position 548.
+The protein's natural variant, known as in TBRS; somatic mutation, features a modification of the amino acid from C to R at position 549.
+The protein's natural variant, known as in TBRS; somatic mutation;, features a modification of the amino acid from L to P at position 648.
+The protein's natural variant, known as in a patient with chronic myelomonocytic leukemia;, features a modification of the amino acid from G to D at position 699.
+The protein's natural variant, known as in TBRS; somatic mutation;, features a modification of the amino acid from P to L at position 700.
+The protein's natural variant, known as in TBRS; somatic mutation;, features a modification of the amino acid from R to C at position 749.
+The protein's natural variant, known as in TBRS; unknown pathological significance;, features a modification of the amino acid from R to Q at position 771.
+The protein's natural variant, known as in TBRS; unknown pathological significance;, features a modification of the amino acid from V to G at position 778.
+The protein's natural variant, known as in TBRS; somatic mutation;, features a modification of the amino acid from N to D at position 838.
+The protein's natural variant, known as in TBRS and AML; somatic variant in AML;, features a modification of the amino acid from R to C at position 882.
+The protein's natural variant, known as in TBRS and AML; somatic variant in AML;, features a modification of the amino acid from R to H at position 882.
+The protein's natural variant, known as in a patient with chronic myelomonocytic leukemia; somatic mutation;, features a modification of the amino acid from R to P at position 882.
+The protein's natural variant, known as in TBRS; somatic mutation;, features a modification of the amino acid from F to S at position 902.
+The protein's natural variant, known as in TBRS; somatic mutation;, features a modification of the amino acid from P to L at position 904.
+The protein's natural variant, known as in ICAS; reduced protein levels;, features a modification of the amino acid from T to N at position 54.
+The protein's natural variant, known as in ICAS; reduced protein levels;, features a modification of the amino acid from L to F at position 58.
+The protein's natural variant, known as in ICAS; reduced protein levels;, features a modification of the amino acid from R to G at position 180.
+The protein's natural variant, known as in ICAS; reduced protein levels;, features a modification of the amino acid from R to W at position 180.
+The protein's natural variant, known as in ICAS; reduced protein levels;, features a modification of the amino acid from R to C at position 186.
+The protein's natural variant, known as in DEE64; reduced RHOBTB2 proteasomal degradation; does not affect interaction with CUL3;, features a modification of the amino acid from A to G at position 452.
+The protein's natural variant, known as in DEE64; reduced RHOBTB2 proteasomal degradation; does not affect interaction with CUL3;, features a modification of the amino acid from R to H at position 461.
+The protein's natural variant, known as in DEE64; decreased proteasomal degradation; does not affect interaction with CUL3;, features a modification of the amino acid from R to C at position 485.
+The protein's natural variant, known as in DEE64; also found in a patient with Rett syndrome-like phenotype;, features a modification of the amino acid from N to D at position 488.
+The protein's natural variant, known as in DEE64; reduced RHOBTB2 proteasomal degradation; does not affect interaction with CUL3;, features a modification of the amino acid from R to Q at position 489.
+The protein's natural variant, known as in DEE64;, features a modification of the amino acid from R to W at position 489.
+The protein's natural variant, known as affects water and glycerol transport;, features a modification of the amino acid from G to V at position 264.
+The natural variant of this protein is characterized by an amino acid alteration from A to T at position 214.
+The protein's natural variant, known as in strain: JiuLong, features a modification of the amino acid from Q to L at position 86.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from L to R at position 123.
+The protein's natural variant, known as in strain: AL585, features a modification of the amino acid from R to M at position 430.
+The protein's natural variant, known as in strain: AL585, features a modification of the amino acid from K to R at position 467.
+The protein's natural variant, known as in strain: AL585, features a modification of the amino acid from G to E at position 754.
+The protein's natural variant, known as in MEND; patients have mildly increased concentrations of plasma 8(9)-cholestenol and 8-dehydrocholesterol; probable hypomorphic mutation;, features a modification of the amino acid from L to P at position 18.
+The protein's natural variant, known as in MEND; patients have increased concentrations of plasma 8(9)-cholestenol, 8-dehydrocholesterol and 7-dehydrocholesterol; probable hypomorphic mutation;, features a modification of the amino acid from W to C at position 47.
+The protein's natural variant, known as in MEND; patients have increased concentrations of plasma 8-dehydrocholesterol and 8(9)-cholestenol; probable hypomorphic mutation;, features a modification of the amino acid from W to R at position 47.
+The protein's natural variant, known as in MEND; patients have increased plasma levels of 8(9)-cholestenol; probable hypomorphic mutation;, features a modification of the amino acid from I to N at position 75.
+The protein's natural variant, known as in CDPX2;, features a modification of the amino acid from E to K at position 80.
+The protein's natural variant, known as in CDPX2, features a modification of the amino acid from E to K at position 103.
+The protein's natural variant, known as in CDPX2;, features a modification of the amino acid from R to Q at position 110.
+The protein's natural variant, known as in CDPX2, features a modification of the amino acid from R to G at position 147.
+The protein's natural variant, known as in CDPX2;, features a modification of the amino acid from R to H at position 147.
+The natural variant of this protein is characterized by an amino acid alteration from K to Q at position 199.
+The natural variant of this protein is characterized by an amino acid alteration from A to T at position 246.
+The natural variant of this protein is characterized by an amino acid alteration from G to R at position 352.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from A to S at position 5.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from A to T at position 5.
+The protein's natural variant, known as in ALS1; severe form; reduces structural stability and enzyme activity; increases tendency to form fibrillar aggregates;, features a modification of the amino acid from A to V at position 5.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from C to F at position 7.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from V to E at position 8.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from L to Q at position 9.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from L to V at position 9.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from G to R at position 13.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from V to G at position 15.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from V to M at position 15.
+The protein's natural variant, known as in ALS1; sporadic young onset;, features a modification of the amino acid from G to S at position 17.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from F to C at position 21.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from E to G at position 22.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from E to K at position 22.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from Q to L at position 23.
+The protein's natural variant, known as in ALS1; mild form; ubiquitinated by RNF19A. Ubiquitinated by MARCH5; leading to the degradation of mitochondrial SOD1;, features a modification of the amino acid from G to R at position 38.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from L to R at position 39.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from L to V at position 39.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from G to D at position 42.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from G to S at position 42.
+The protein's natural variant, known as in ALS1; reduces structural stability and enzyme activity; increases tendency to form fibrillar aggregates;, features a modification of the amino acid from H to R at position 44.
+The protein's natural variant, known as in ALS1; slow progression;, features a modification of the amino acid from F to C at position 46.
+The protein's natural variant, known as in ALS1; 'benign' form; 80% of wild-type activity; ubiquitinated by RNF19A;, features a modification of the amino acid from H to R at position 47.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from H to Q at position 49.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from H to R at position 49.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from E to K at position 50.
+The protein's natural variant, known as in ALS1; reduces tendency to form fibrillar aggregates;, features a modification of the amino acid from T to R at position 55.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from N to S at position 66.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from L to P at position 68.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from L to R at position 68.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from G to S at position 73.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from D to Y at position 77.
+The protein's natural variant, known as in ALS1; sporadic form; interferes with zinc binding; requires 2 nucleotide substitutions, features a modification of the amino acid from H to A at position 81.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from L to F at position 85.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from L to V at position 85.
+The protein's natural variant, known as in ALS1; ubiquitinated by RNF19A; interferes with zinc-binding; ubiquitinated by MARCH5; leading to the degradation of mitochondrial SOD1;, features a modification of the amino acid from G to R at position 86.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from N to S at position 87.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from V to A at position 88.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from A to T at position 90.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from A to V at position 90.
+The protein's natural variant, known as in ALS1; does not seem to be linked with a decrease in activity;, features a modification of the amino acid from D to A at position 91.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from D to V at position 91.
+The protein's natural variant, known as in ALS1; increases tendency to form fibrillar aggregates; ubiquitinated by RNF19A;, features a modification of the amino acid from G to A at position 94.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from G to C at position 94.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from G to D at position 94.
+The protein's natural variant, known as in ALS1; 30% of wild-type activity;, features a modification of the amino acid from G to R at position 94.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from G to V at position 94.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from A to G at position 96.
+The protein's natural variant, known as in ALS1; increases tendency to form fibrillar aggregates;, features a modification of the amino acid from V to M at position 98.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from E to G at position 101.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from E to K at position 101.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from D to G at position 102.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from D to N at position 102.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from I to F at position 105.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from S to L at position 106.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from L to V at position 107.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from G to V at position 109.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from C to Y at position 112.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from I to M at position 113.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from I to T at position 113.
+The protein's natural variant, known as in ALS1; destabilizes dimeric protein structure and increases tendency to form fibrillar aggregates;, features a modification of the amino acid from I to T at position 114.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from G to A at position 115.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from R to G at position 116.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from V to L at position 119.
+The protein's natural variant, known as in ALS1, features a modification of the amino acid from V to VFLQ at position 119.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from D to G at position 125.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from D to V at position 125.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from D to H at position 126.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from L to S at position 127.
+The protein's natural variant, known as in ALS1; reduced metal binding; increases tendency to form fibrillar aggregates;, features a modification of the amino acid from S to N at position 135.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from N to K at position 140.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from L to F at position 145.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from L to S at position 145.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from A to T at position 146.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from C to R at position 147.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from G to R at position 148.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from V to G at position 149.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from V to I at position 149.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from I to T at position 150.
+The protein's natural variant, known as in ALS1;, features a modification of the amino acid from I to T at position 152.
+The protein's natural variant, known as in NEDFLPH; decreased stability, features a modification of the amino acid from G to R at position 7.
+The protein's natural variant, known as in NEDFLPH; decreased stability, features a modification of the amino acid from I to N at position 133.
+The protein's natural variant, known as in NEDFLPH; slightly decreased stability; impaired endoplasmic reticulum organization, features a modification of the amino acid from R to W at position 166.
+The protein's natural variant, known as in 50% of the molecules, features a modification of the amino acid from M to L at position 64.
+The protein's natural variant, known as in 30% of the molecules, features a modification of the amino acid from E to K at position 98.
+The natural variant of this protein is characterized by an amino acid alteration from S to F at position 121.
+The protein's natural variant, known as m-MIITX-Mp1b, features a modification of the amino acid from V to I at position 61.
+The protein's natural variant, known as in HYPT4; unknown pathological significance; increases HR protein expression; abolishes the inhibitory effect on HR translation, features a modification of the amino acid from I to N at position 24.
+The protein's natural variant, known as in HYPT4; unknown pathological significance; increases HR protein expression; abolishes the inhibitory effect on HR translation;, features a modification of the amino acid from P to A at position 25.
+The protein's natural variant, known as in HYPT4; unknown pathological significance; increases HR protein expression; abolishes the inhibitory effect on HR translation, features a modification of the amino acid from E to K at position 26.
+The protein's natural variant, known as in HYPT4; unknown pathological significance; increases HR protein expression; abolishes the inhibitory effect on HR translation, features a modification of the amino acid from D to H at position 28.
+The protein's natural variant, known as in PARK; sporadic case; unknown pathological significance; results in decreased synaptic vesicle trafficking;, features a modification of the amino acid from Y to C at position 29.
+The protein's natural variant, known as in PARK; unknown pathological significance; results in decreased synaptic vesicle trafficking;, features a modification of the amino acid from R to L at position 78.
+The natural variant of this protein is characterized by an amino acid alteration from P to RA at position 152.
+The protein's natural variant, known as in EPXD;, features a modification of the amino acid from R to H at position 286.
+The natural variant of this protein is characterized by an amino acid alteration from R to L at position 326.
+The protein's natural variant, known as associated with Japanese cedar pollinosis;, features a modification of the amino acid from P to L at position 358.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from C to F at position 267.
+The natural variant of this protein is characterized by an amino acid alteration from D to E at position 253.
+The protein's natural variant, known as in GLUT1DS2;, features a modification of the amino acid from N to I at position 34.
+The protein's natural variant, known as in GLUT1DS1; 55% of wild-type glucose uptake activity;, features a modification of the amino acid from N to S at position 34.
+The protein's natural variant, known as in GLUT1DS1, features a modification of the amino acid from N to Y at position 34.
+The protein's natural variant, known as in EIG12; unknown pathological significance;, features a modification of the amino acid from R to H at position 51.
+The protein's natural variant, known as in EIG12; unknown pathological significance; decreased glucose transport;, features a modification of the amino acid from T to M at position 60.
+The protein's natural variant, known as in GLUT1DS1;, features a modification of the amino acid from S to F at position 66.
+The protein's natural variant, known as in EIG12; decreased glucose transport;, features a modification of the amino acid from M to T at position 77.
+The protein's natural variant, known as in GLUT1DS1; significantly decreases the transport of 3-O-methyl-D-glucose;, features a modification of the amino acid from G to D at position 91.
+The protein's natural variant, known as in GLUT1DS2;, features a modification of the amino acid from R to W at position 92.
+The protein's natural variant, known as in GLUT1DS2;, features a modification of the amino acid from R to W at position 93.
+The protein's natural variant, known as in GLUT1DS2;, features a modification of the amino acid from S to I at position 95.
+The protein's natural variant, known as in GLUT1DS1;, features a modification of the amino acid from M to V at position 96.
+The protein's natural variant, known as in GLUT1DS1, GLUT1DS2 and DYT9; reduced transporter activity;, features a modification of the amino acid from R to C at position 126.
+The protein's natural variant, known as in GLUT1DS1; significantly decreases the transport of 3-O-methyl-D-glucose and dehydroascorbic acid; 57% of wild-type glucose uptake activity;, features a modification of the amino acid from R to H at position 126.
+The protein's natural variant, known as in GLUT1DS1;, features a modification of the amino acid from R to L at position 126.
+The protein's natural variant, known as in GLUT1DS1; 75% of wild-type glucose uptake activity;, features a modification of the amino acid from G to S at position 130.
+The protein's natural variant, known as in GLUT1DS1;, features a modification of the amino acid from E to K at position 146.
+The protein's natural variant, known as in EIG12; unknown pathological significance, features a modification of the amino acid from P to A at position 149.
+The protein's natural variant, known as in GLUT1DS1; 44% of wild-type glucose uptake activity, features a modification of the amino acid from R to C at position 153.
+The protein's natural variant, known as in GLUT1DS2;, features a modification of the amino acid from R to H at position 153.
+The protein's natural variant, known as in GLUT1DS1, features a modification of the amino acid from A to V at position 155.
+The protein's natural variant, known as in GLUT1DS2;, features a modification of the amino acid from V to I at position 165.
+The protein's natural variant, known as in GLUT1DS1 and DYT9;, features a modification of the amino acid from R to C at position 212.
+The protein's natural variant, known as in GLUT1DS1;, features a modification of the amino acid from R to H at position 212.
+The protein's natural variant, known as in EIG12; decreased glucose transport, features a modification of the amino acid from R to S at position 218.
+The protein's natural variant, known as in EIG12; mild phenotype; reduced transporter activity; impaired phosphorylation by PKC;, features a modification of the amino acid from R to P at position 223.
+The protein's natural variant, known as in EIG12; unknown pathological significance; no effect on glucose transport; impaired phosphorylation by PKC;, features a modification of the amino acid from R to Q at position 223.
+The protein's natural variant, known as in GLUT1DS1; impaired phosphorylation by PKC;, features a modification of the amino acid from R to W at position 223.
+The protein's natural variant, known as in EIG12; the mutant protein is expressed at the cell surface but has mildly decreased glucose uptake (70%) compared to wild-type;, features a modification of the amino acid from R to C at position 232.
+The protein's natural variant, known as in EIG12; decreased glucose transport, features a modification of the amino acid from E to V at position 243.
+The protein's natural variant, known as in GLUT1DS1;, features a modification of the amino acid from K to E at position 256.
+The protein's natural variant, known as in GLUT1DS2; the mutation decreases glucose transport but does not affect cation permeability;, features a modification of the amino acid from A to T at position 275.
+The protein's natural variant, known as in SDCHCN; no effect on protein abundance; no effect on localization to the plasma membrane; loss of D-glucose transporter activity; increased cation leakage;, features a modification of the amino acid from G to D at position 286.
+The protein's natural variant, known as in GLUT1DS1, features a modification of the amino acid from Y to YY at position 292.
+The protein's natural variant, known as in GLUT1DS2, features a modification of the amino acid from S to P at position 294.
+The protein's natural variant, known as in GLUT1DS1; 75% of wild-type glucose uptake activity;, features a modification of the amino acid from T to M at position 295.
+The protein's natural variant, known as found in a patient with GLUT1 deficiency syndrome;, features a modification of the amino acid from V to L at position 303.
+The protein's natural variant, known as in GLUT1DS1;, features a modification of the amino acid from T to I at position 310.
+The protein's natural variant, known as in GLUT1DS2; the mutation decreases glucose transport but does not affect cation permeability;, features a modification of the amino acid from G to S at position 314.
+The protein's natural variant, known as in GLUT1DS2, features a modification of the amino acid from N to T at position 317.
+The protein's natural variant, known as in GLUT1DS2; mild phenotype; reduced transporter activity;, features a modification of the amino acid from S to L at position 324.
+The protein's natural variant, known as in GLUT1DS1; stabilizes the inward-open conformation, features a modification of the amino acid from E to Q at position 329.
+The protein's natural variant, known as in GLUT1DS1 and GLUT1DS2;, features a modification of the amino acid from R to Q at position 333.
+The protein's natural variant, known as in GLUT1DS1; 43% of wild-type glucose uptake activity;, features a modification of the amino acid from R to W at position 333.
+The protein's natural variant, known as in GLUT1DS1, features a modification of the amino acid from G to D at position 382.
+The protein's natural variant, known as in GLUT1DS1, features a modification of the amino acid from A to D at position 405.
+The protein's natural variant, known as in EIG12; decreased glucose transport;, features a modification of the amino acid from N to S at position 411.
+The protein's natural variant, known as in EIG12; decreased glucose transport;, features a modification of the amino acid from R to W at position 458.
+The protein's natural variant, known as in GLUT1DS1;, features a modification of the amino acid from R to W at position 468.
+The protein's natural variant, known as in GLUT1DS1; creates a dileucine internalization motif that promotes recruitment of clathrin and mislocalization of the protein to endocytic compartments, features a modification of the amino acid from P to L at position 485.
+The protein's natural variant, known as decreased transcription factor activity due to impaired interaction with ARNT2;, features a modification of the amino acid from F to S at position 147.
+The protein's natural variant, known as does not affect the transcription factor activity;, features a modification of the amino acid from G to C at position 208.
+The protein's natural variant, known as decreased transcription factor activity;, features a modification of the amino acid from E to K at position 257.
+The protein's natural variant, known as does not affect the transcription factor activity;, features a modification of the amino acid from W to R at position 293.
+The protein's natural variant, known as likely benign variant; does not affect the transcription factor activity, features a modification of the amino acid from C to R at position 296.
+The protein's natural variant, known as does not affect the transcription factor activity;, features a modification of the amino acid from M to L at position 317.
+The protein's natural variant, known as does not affect the transcription factor activity;, features a modification of the amino acid from P to A at position 344.
+The protein's natural variant, known as does not affect the transcription factor activity;, features a modification of the amino acid from T to I at position 359.
+The protein's natural variant, known as does not affect the transcription factor activity;, features a modification of the amino acid from P to S at position 472.
+The protein's natural variant, known as does not affect the transcription factor activity;, features a modification of the amino acid from Q to K at position 500.
+The protein's natural variant, known as does not affect the transcription factor activity;, features a modification of the amino acid from T to M at position 587.
+The protein's natural variant, known as does not affect the transcription factor activity;, features a modification of the amino acid from N to D at position 702.
+The protein's natural variant, known as does not affect the transcription factor activity;, features a modification of the amino acid from D to Y at position 750.
+The protein's natural variant, known as does not affect the transcription factor activity;, features a modification of the amino acid from T to I at position 777.
+The natural variant of this protein is characterized by an amino acid alteration from R to H at position 23.
+The natural variant of this protein is characterized by an amino acid alteration from K to Q at position 48.
+The natural variant of this protein is characterized by an amino acid alteration from E to G at position 150.
+The natural variant of this protein is characterized by an amino acid alteration from N to D at position 170.
+The natural variant of this protein is characterized by an amino acid alteration from V to A at position 241.
+The natural variant of this protein is characterized by an amino acid alteration from S to F at position 379.
+The protein's natural variant, known as in OCA8;, features a modification of the amino acid from C to S at position 40.
+The protein's natural variant, known as in OCA8;, features a modification of the amino acid from C to W at position 61.
+The protein's natural variant, known as in MC1DN9;, features a modification of the amino acid from C to Y at position 115.
+The natural variant of this protein is characterized by an amino acid alteration from R to A at position 4.
+The natural variant of this protein is characterized by an amino acid alteration from R to V at position 4.
+The protein's natural variant, known as does not affect cystine transport;, features a modification of the amino acid from V to I at position 42.
+The protein's natural variant, known as in CTNS; atypical; does not affect cystine transport;, features a modification of the amino acid from G to V at position 110.
+The protein's natural variant, known as in CTNS; does not affect cystine transport;, features a modification of the amino acid from I to F at position 133.
+The protein's natural variant, known as in CTNS; atypical; abolished cystine transport;, features a modification of the amino acid from S to F at position 139.
+The protein's natural variant, known as in CTNS; abolished cystine transport, features a modification of the amino acid from S to F at position 141.
+The protein's natural variant, known as in CTNS;, features a modification of the amino acid from R to G at position 151.
+The protein's natural variant, known as in CTNSJAN; decreased cystine transport, features a modification of the amino acid from S to SPCS at position 154.
+The protein's natural variant, known as in CTNS, features a modification of the amino acid from G to D at position 157.
+The protein's natural variant, known as in CTNS; abolished cystine transport;, features a modification of the amino acid from L to P at position 158.
+The protein's natural variant, known as in CTNS; abolished cystine transport;, features a modification of the amino acid from G to D at position 169.
+The protein's natural variant, known as in CTNS;, features a modification of the amino acid from Y to C at position 173.
+The protein's natural variant, known as in CTNS; abolished cystine transport, features a modification of the amino acid from N to S at position 177.
+The protein's natural variant, known as in CTNSJAN, features a modification of the amino acid from N to T at position 177.
+The protein's natural variant, known as in CTNS; does not affect cystine transport;, features a modification of the amino acid from W to R at position 182.
+The protein's natural variant, known as in CTNSANN; decreased cystine transport;, features a modification of the amino acid from G to R at position 197.
+The protein's natural variant, known as in CTNSJAN; decreased cystine transport, features a modification of the amino acid from P to L at position 200.
+The protein's natural variant, known as in CTNS; abolished cystine transport;, features a modification of the amino acid from D to N at position 205.
+The protein's natural variant, known as in CTNS; partial relocation to the cell membrane; abolished cystine transport;, features a modification of the amino acid from Q to R at position 222.
+The protein's natural variant, known as slightly decreased cystine transport;, features a modification of the amino acid from T to I at position 260.
+The protein's natural variant, known as in CTNSJAN; abolished cystine transport, features a modification of the amino acid from K to R at position 280.
+The protein's natural variant, known as in CTNS;, features a modification of the amino acid from M to I at position 287.
+The protein's natural variant, known as in CTNS; abolished cystine transport, features a modification of the amino acid from N to K at position 288.
+The protein's natural variant, known as found in patients with cystinosis; uncertain pathological significance;, features a modification of the amino acid from K to R at position 292.
+The protein's natural variant, known as in CTNS; does not affect cystine transport;, features a modification of the amino acid from S to N at position 298.
+The protein's natural variant, known as in CTNS;, features a modification of the amino acid from D to G at position 305.
+The protein's natural variant, known as in CTNS; abolished cystine transport, features a modification of the amino acid from D to Y at position 305.
+The protein's natural variant, known as in CTNS; abolished cystine transport;, features a modification of the amino acid from G to R at position 308.
+The protein's natural variant, known as in CTNS;, features a modification of the amino acid from G to V at position 308.
+The protein's natural variant, known as in CTNS, features a modification of the amino acid from G to D at position 309.
+The protein's natural variant, known as in CTNSJAN; abolished cystine transport;, features a modification of the amino acid from N to K at position 323.
+The protein's natural variant, known as in CTNS, features a modification of the amino acid from G to R at position 337.
+The protein's natural variant, known as in CTNS; abolished cystine transport, features a modification of the amino acid from L to P at position 338.
+The protein's natural variant, known as in CTNS, features a modification of the amino acid from L to R at position 338.
+The protein's natural variant, known as in CTNS; abolished cystine transport;, features a modification of the amino acid from G to R at position 339.
+The protein's natural variant, known as in CTNS; atypical; slightly decreased cystine transport;, features a modification of the amino acid from D to N at position 346.
+The protein's natural variant, known as in CTNS; abolished cystine transport, features a modification of the amino acid from F to FDVEF at position 349.
+The natural variant of this protein is characterized by an amino acid alteration from N to L at position 434.
+The protein's natural variant, known as in SMC2;, features a modification of the amino acid from K to Q at position 46.
+The protein's natural variant, known as in SMC2; strongly inhibits protein expression and may disrupt the Golgi apparatus structure;, features a modification of the amino acid from N to K at position 148.
+The protein's natural variant, known as in a gastric adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from R to H at position 150.
+The natural variant of this protein is characterized by an amino acid alteration from L to P at position 630.
+The protein's natural variant, known as in a breast infiltrating ductal carcinoma sample; somatic mutation, features a modification of the amino acid from H to R at position 775.
+The natural variant of this protein is characterized by an amino acid alteration from A to T at position 956.
+The natural variant of this protein is characterized by an amino acid alteration from H to R at position 201.
+The protein's natural variant, known as in P5ND;, features a modification of the amino acid from R to G at position 95.
+The protein's natural variant, known as in P5ND; reduced catalytic activity especially towards UMP, features a modification of the amino acid from C to R at position 113.
+The protein's natural variant, known as in P5ND; reduced catalytic activity;, features a modification of the amino acid from D to V at position 137.
+The protein's natural variant, known as in P5ND; reduced catalytic activity in vitro; reduced protein stability in vivo, probably through increased proteasomal degradation, features a modification of the amino acid from L to P at position 181.
+The protein's natural variant, known as in P5ND; reduced catalytic activity especially towards UMP, features a modification of the amino acid from G to R at position 207.
+The protein's natural variant, known as in P5ND; almost complete loss of catalytic activity;, features a modification of the amino acid from N to S at position 229.
+The protein's natural variant, known as in P5ND; greatly reduced catalytic activity;, features a modification of the amino acid from G to R at position 280.
+The protein's natural variant, known as in P5ND, features a modification of the amino acid from I to T at position 297.
+The natural variant of this protein is characterized by an amino acid alteration from S to A at position 88.
+The protein's natural variant, known as in HG and IG; no effect on localization to the plasma membrane; decreased amino acid:proton symporter activity; no effect on protein reaction kinetics; decreased affinity for proline; 3-fold increase of Km value for proline; decreased affinity for glycine; 5-fold increase of Km for glycine;, features a modification of the amino acid from G to V at position 87.
+The protein's natural variant, known as in strain: IL1403, features a modification of the amino acid from S to C at position 23.
+The protein's natural variant, known as in strain: IL1403, features a modification of the amino acid from R to G at position 38.
+The protein's natural variant, known as in strain: IL1403, features a modification of the amino acid from R to K at position 126.
+The protein's natural variant, known as in strain: IL1403, features a modification of the amino acid from D to E at position 193.
+The protein's natural variant, known as in strain: IL1403, features a modification of the amino acid from G to V at position 297.
+The protein's natural variant, known as in strain: IL1403, features a modification of the amino acid from EIYVSQGEGSGSV to GAGSL at position 423.
+The protein's natural variant, known as in PERYTHM; causes a hyperpolarizing shift of -5.3 mV for the midpoint of activation which is smaller than that seen in other mutations causing early-onset erythromelalgia mutations; also causes a faster rate of activation and slower deactivation compared to wild-type; expression of the mutant protein induced hyperexcitability in dorsal root ganglion neurons but the increase is smaller than that produced by Thr-859;, features a modification of the amino acid from Q to R at position 10.
+The protein's natural variant, known as found in a patient with febrile seizures; unknown pathological significance;, features a modification of the amino acid from I to V at position 62.
+The protein's natural variant, known as found in a patient with febrile seizures; unknown pathological significance;, features a modification of the amino acid from P to Q at position 149.
+The protein's natural variant, known as in PERYTHM; hyperpolarizes the voltage dependence of activation by 11 mV, accelerates activation, slows deactivation and enhances the response to slow, small depolarizations;, features a modification of the amino acid from F to S at position 216.
+The protein's natural variant, known as in PERYTHM;, features a modification of the amino acid from S to T at position 241.
+The protein's natural variant, known as in PERYTHM;, features a modification of the amino acid from N to K at position 395.
+The protein's natural variant, known as found in patients with febrile seizures plus; unknown pathological significance;, features a modification of the amino acid from N to Y at position 641.
+The protein's natural variant, known as found in a patient with severe myoclonic epilepsy in infancy; unknown pathological significance;, features a modification of the amino acid from C to Y at position 710.
+The protein's natural variant, known as in PERYTHM; sporadic; activated at more negative potentials; slower inactivation kinetics than wild-type channels;, features a modification of the amino acid from I to T at position 859.
+The protein's natural variant, known as in PERYTHM; causes a hyperpolarizing shift in channel activation, a depolarizing shift of inactivation and an 18-fold increase in deactivation time compared to wild-type; the mean ramp current amplitude in response to slow depolarization is higher in the mutant channels;, features a modification of the amino acid from L to F at position 869.
+The protein's natural variant, known as in PERYTHM; activated at more negative potentials; slower inactivation kinetics than wild-type channels;, features a modification of the amino acid from L to H at position 869.
+The protein's natural variant, known as in CIP; significant reduction in membrane localization of the mutant protein compared to the wild-type; complete loss of function of the sodium channel;, features a modification of the amino acid from R to Q at position 907.
+The protein's natural variant, known as in PEXPD;, features a modification of the amino acid from R to C at position 1007.
+The protein's natural variant, known as found in a patient with severe myoclonic epilepsy in infancy; unknown pathological significance, features a modification of the amino acid from E to Q at position 1171.
+The protein's natural variant, known as in PEXPD;, features a modification of the amino acid from V to D at position 1309.
+The protein's natural variant, known as in PEXPD;, features a modification of the amino acid from V to F at position 1309.
+The protein's natural variant, known as in PEXPD;, features a modification of the amino acid from V to F at position 1310.
+The protein's natural variant, known as in PERYTHM; produces a hyperpolarizing shift in channel activation and a depolarizing shift in steady-state activation;, features a modification of the amino acid from F to V at position 1460.
+The protein's natural variant, known as in PEXPD; reduction in fast inactivation leading to persistent sodium current;, features a modification of the amino acid from I to T at position 1472.
+The protein's natural variant, known as in PEXPD;, features a modification of the amino acid from F to V at position 1473.
+The protein's natural variant, known as in PEXPD; reduction in fast inactivation leading to persistent sodium current;, features a modification of the amino acid from T to I at position 1475.
+The protein's natural variant, known as in PEXPD; depolarizes the voltage-dependence of channel activation and steady-state fast inactivation; increases ramp current;, features a modification of the amino acid from L to P at position 1623.
+The protein's natural variant, known as in PEXPD; reduction in fast inactivation leading to persistent sodium current, features a modification of the amino acid from M to K at position 1638.
+The protein's natural variant, known as in PERYTHM and PEXPD; hyperpolarizes voltage-dependence of channel activation; depolarizes the voltage-dependence of steady-state fast inactivation; slows channel deactivation; enhances persistent and resurgent current; enhances neuronal hyperexcitability in dorsal root ganglion neurons;, features a modification of the amino acid from A to E at position 1643.
+The protein's natural variant, known as in PERYTHM; no effect on voltage-dependence of channel activation; depolarizes the voltage dependence of steady-state fast inactivation; accelerates channel deactivation; no increase in persistent and resurgent currents; enhances neuronal hyperexcitability in dorsal root ganglion neurons, features a modification of the amino acid from A to T at position 1643.
+The natural variant of this protein is characterized by an amino acid alteration from I to T at position 197.
+The natural variant of this protein is characterized by an amino acid alteration from S to G at position 142.
+The protein's natural variant, known as in PEBAT;, features a modification of the amino acid from L to R at position 229.
+The protein's natural variant, known as in PEBAT; severely decreased interaction with beta tubulin; does not affect localization to centrosome;, features a modification of the amino acid from T to M at position 374.
+The protein's natural variant, known as in PEBAT; decreased protein abundance; severely decreased interaction with beta tubulin; does not affect localization to centrosome;, features a modification of the amino acid from R to Q at position 377.
+The protein's natural variant, known as in PEBAT; decreased function in neuron morphogenesis; severely decreased interaction with ARL2; decreased interaction with TBCE; decreased interaction with beta tubulin;, features a modification of the amino acid from M to R at position 387.
+The protein's natural variant, known as in PEBAT; decreased function in tubulin complex assembly; increased protein degradation;, features a modification of the amino acid from A to T at position 475.
+The protein's natural variant, known as in PEBAT; decreased function in tubulin complex assembly;, features a modification of the amino acid from A to V at position 586.
+The protein's natural variant, known as in PEBAT; decreased protein abundance; does not affect localization to centrosome;, features a modification of the amino acid from A to T at position 626.
+The protein's natural variant, known as in PEBAT; decreased function in neuron morphogenesis; decreased interaction with ARL2; decreased interaction with TBCE; decreased interaction with beta tubulin;, features a modification of the amino acid from R to C at position 772.
+The protein's natural variant, known as in PEBAT; decreased interaction with ARL2; decreased interaction with TBCE; decreased interaction with beta tubulin;, features a modification of the amino acid from A to T at position 921.
+The protein's natural variant, known as in PEBAT; decreased interaction with TBCE; decreased interaction with beta tubulin; does not affect interaction with ARL2;, features a modification of the amino acid from P to R at position 937.
+The protein's natural variant, known as in PEBAT; unknown pathological significance;, features a modification of the amino acid from T to M at position 994.
+The protein's natural variant, known as in PEBAT; unknown pathological significance;, features a modification of the amino acid from V to M at position 1105.
+The protein's natural variant, known as in PEBAT; severely decreased protein abundance; does not affect localization to centrosome; decreased interaction with ARL2; decreased interaction with TBCE; decreased interaction with beta tubulin;, features a modification of the amino acid from P to L at position 1122.
+The protein's natural variant, known as in TROFAS, features a modification of the amino acid from H to LN at position 59.
+The protein's natural variant, known as in AAT10; unknown pathological significance;, features a modification of the amino acid from A to T at position 79.
+The protein's natural variant, known as in AAT10; unknown pathological significance;, features a modification of the amino acid from L to F at position 154.
+The protein's natural variant, known as in AAT10; unknown pathological significance; 8% decrease of lysyl oxidase activity;, features a modification of the amino acid from T to I at position 248.
+The protein's natural variant, known as in AAT10;, features a modification of the amino acid from Q to P at position 267.
+The protein's natural variant, known as in AAT10; 50% decrease of lysyl oxidase activity;, features a modification of the amino acid from S to I at position 280.
+The protein's natural variant, known as in AAT10;, features a modification of the amino acid from M to R at position 298.
+The protein's natural variant, known as in AAT10; 21% decrease of lysyl oxidase activity;, features a modification of the amino acid from S to R at position 348.
+The protein's natural variant, known as in strain: Isolate 22 AP 01, features a modification of the amino acid from E to G at position 188.
+The protein's natural variant, known as in CSCSC2; enhances binding to microtubules;, features a modification of the amino acid from N to S at position 68.
+The protein's natural variant, known as in CSCSC2; enhances binding to microtubules;, features a modification of the amino acid from Y to C at position 87.
+The protein's natural variant, known as in CSCSC2; enhances binding to microtubules;, features a modification of the amino acid from R to C at position 143.
+The protein's natural variant, known as in strain: 001, features a modification of the amino acid from I to L at position 63.
+The protein's natural variant, known as in a Charcot-Marie-Tooth disease patient;, features a modification of the amino acid from E to K at position 7.
+The protein's natural variant, known as in CMT1F;, features a modification of the amino acid from P to L at position 8.
+The protein's natural variant, known as in CMT1F;, features a modification of the amino acid from P to Q at position 8.
+The protein's natural variant, known as in CMT2E and CMT1F;, features a modification of the amino acid from P to R at position 8.
+The protein's natural variant, known as in CMT2E;, features a modification of the amino acid from P to S at position 22.
+The protein's natural variant, known as in CMT1F;, features a modification of the amino acid from E to K at position 90.
+The protein's natural variant, known as in CMT1F and CMTDIG;, features a modification of the amino acid from N to S at position 98.
+The protein's natural variant, known as in CMT2E; unknown pathological significance;, features a modification of the amino acid from Y to C at position 265.
+The protein's natural variant, known as in CMT2E;, features a modification of the amino acid from L to P at position 268.
+The protein's natural variant, known as in CMT2E;, features a modification of the amino acid from Q to P at position 332.
+The protein's natural variant, known as in CMT2E; unknown pathological significance;, features a modification of the amino acid from L to P at position 336.
+The protein's natural variant, known as in CMTDIG and CMT2E;, features a modification of the amino acid from E to K at position 396.
+The protein's natural variant, known as in CMT2E; unknown pathological significance;, features a modification of the amino acid from P to L at position 440.
+The natural variant of this protein is characterized by an amino acid alteration from P to S at position 239.
+The protein's natural variant, known as in strain: cv. CMS89, features a modification of the amino acid from A to L at position 228.
+The protein's natural variant, known as in DFNA64; does not increase apoptotic activity compared to wild-type; enhances the degradation of mutant and wild-type protein via heterodimerization; cells expressing the mutant protein show increased susceptibility to calcium-induced loss of mitochondrial potential compared to wild-type, indicating increased sensitivity to mitochondrial stress and suggestive of mitochondrial dysfunction;, features a modification of the amino acid from S to L at position 126.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from P to T at position 77.
+The protein's natural variant, known as in OFD5; markedly reduced expression in fibroblasts compared to wild-type protein; impaired SHH signaling in SAG-treated fibroblasts;, features a modification of the amino acid from V to G at position 367.
+The protein's natural variant, known as in OFD5;, features a modification of the amino acid from G to R at position 534.
+The protein's natural variant, known as in strain: S288c / GRF88, features a modification of the amino acid from PI to SY at position 46.
+The protein's natural variant, known as in strain: C3H/He, features a modification of the amino acid from Q to R at position 232.
+The protein's natural variant, known as in CFNS, features a modification of the amino acid from P to R at position 27.
+The protein's natural variant, known as in CFNS;, features a modification of the amino acid from P to L at position 54.
+The protein's natural variant, known as in CFNS, features a modification of the amino acid from I to T at position 62.
+The protein's natural variant, known as in CFNS, features a modification of the amino acid from L to S at position 98.
+The protein's natural variant, known as in CFNS;, features a modification of the amino acid from T to I at position 111.
+The protein's natural variant, known as in CFNS, features a modification of the amino acid from Q to P at position 115.
+The protein's natural variant, known as in CFNS, features a modification of the amino acid from P to H at position 119.
+The protein's natural variant, known as in CFNS, features a modification of the amino acid from P to S at position 119.
+The protein's natural variant, known as in CFNS, features a modification of the amino acid from P to T at position 119.
+The protein's natural variant, known as in CFNS;, features a modification of the amino acid from T to A at position 137.
+The protein's natural variant, known as in CFNS, features a modification of the amino acid from S to F at position 138.
+The protein's natural variant, known as in CFNS;, features a modification of the amino acid from G to S at position 151.
+The protein's natural variant, known as in CFNS;, features a modification of the amino acid from G to V at position 151.
+The protein's natural variant, known as in CFNS, features a modification of the amino acid from C to S at position 153.
+The protein's natural variant, known as in CFNS, features a modification of the amino acid from C to Y at position 153.
+The protein's natural variant, known as in CFNS, features a modification of the amino acid from T to P at position 155.
+The protein's natural variant, known as in CFNS;, features a modification of the amino acid from M to I at position 158.
+The protein's natural variant, known as in CFNS;, features a modification of the amino acid from M to V at position 158.
+The protein's natural variant, known as in CFNS, features a modification of the amino acid from S to R at position 182.
+The protein's natural variant, known as in strain: BIO-HTT, features a modification of the amino acid from VHW to FM at position 153.
+The protein's natural variant, known as in BPS;, features a modification of the amino acid from I to N at position 81.
+The protein's natural variant, known as in BPS; loss of function;, features a modification of the amino acid from I to N at position 121.
+The protein's natural variant, known as in CHANDS; unknown pathological significance;, features a modification of the amino acid from G to D at position 163.
+The protein's natural variant, known as in BPS; loss of function, features a modification of the amino acid from T to I at position 184.
+The protein's natural variant, known as in BPS; unknown pathological significance, features a modification of the amino acid from P to L at position 189.
+The protein's natural variant, known as in CHANDS; unknown pathological significance, features a modification of the amino acid from E to K at position 284.
+The protein's natural variant, known as in BPS; unknown pathological significance, features a modification of the amino acid from A to P at position 496.
+The protein's natural variant, known as in BPS; unknown pathological significance;, features a modification of the amino acid from R to H at position 666.
+The natural variant of this protein is characterized by an amino acid alteration from D to A at position 173.
+The protein's natural variant, known as in strain: JM43, features a modification of the amino acid from D to E at position 153.
+The protein's natural variant, known as in strain: JM43, features a modification of the amino acid from N to D at position 345.
+The protein's natural variant, known as in strain: JM43, features a modification of the amino acid from L to V at position 365.
+The protein's natural variant, known as in allele Red, features a modification of the amino acid from N to D at position 75.
+The natural variant of this protein is characterized by an amino acid alteration from Y to C at position 98.
+The natural variant of this protein is characterized by an amino acid alteration from K to R at position 175.
+The protein's natural variant, known as found in a patient with a Cowden-like phenotype; unknown pathological significance; associated with increased manganese superoxide dismutase expression and normal levels of reactive oxygen species; associated with a 1.2-fold increase in AKT expression and 1.3-fold change in MAPK expression;, features a modification of the amino acid from A to G at position 3.
+The protein's natural variant, known as in PCC, features a modification of the amino acid from A to AQ at position 29.
+The natural variant of this protein is characterized by an amino acid alteration from K to E at position 40.
+The protein's natural variant, known as in PCC, features a modification of the amino acid from A to P at position 43.
+The protein's natural variant, known as in PCC;, features a modification of the amino acid from R to G at position 46.
+The protein's natural variant, known as in PCC and PGL4;, features a modification of the amino acid from R to Q at position 46.
+The protein's natural variant, known as in MC2DN4; decreased succinate dehydrogenase (ubiquinone) activity in homozygous patient cells; decreased protein levels in homozygous patient cells;, features a modification of the amino acid from D to V at position 48.
+The protein's natural variant, known as in PCC;, features a modification of the amino acid from G to R at position 53.
+The protein's natural variant, known as in PCC;, features a modification of the amino acid from L to H at position 65.
+The protein's natural variant, known as in PCC;, features a modification of the amino acid from L to P at position 65.
+The protein's natural variant, known as in PCC;, features a modification of the amino acid from L to S at position 87.
+The protein's natural variant, known as in PCC; absence of expression in tumor cells indicating complete loss of SDHB function;, features a modification of the amino acid from S to F at position 100.
+The protein's natural variant, known as in PCC;, features a modification of the amino acid from C to Y at position 101.
+The protein's natural variant, known as in MC2DN4; unknown pathological significance;, features a modification of the amino acid from A to T at position 102.
+The protein's natural variant, known as in MC2DN4;, features a modification of the amino acid from M to T at position 103.
+The protein's natural variant, known as in PCC, features a modification of the amino acid from I to N at position 127.
+The protein's natural variant, known as in PGL4, features a modification of the amino acid from P to R at position 131.
+The protein's natural variant, known as in PGL4;, features a modification of the amino acid from H to P at position 132.
+The protein's natural variant, known as found in a patient with a Cowden-like phenotype; unknown pathological significance; associated with increased manganese superoxide dismutase function and increased levels of reactive oxygen species; associated with a 2.7-fold change in AKT expression and a 1.7-fold increase in MAPK expression;, features a modification of the amino acid from S to P at position 163.
+The protein's natural variant, known as in PCC;, features a modification of the amino acid from C to R at position 192.
+The protein's natural variant, known as in PCC;, features a modification of the amino acid from C to Y at position 196.
+The protein's natural variant, known as in PGL4;, features a modification of the amino acid from P to R at position 197.
+The protein's natural variant, known as in PCC;, features a modification of the amino acid from R to C at position 230.
+The protein's natural variant, known as in MC2DN4;, features a modification of the amino acid from R to H at position 230.
+The protein's natural variant, known as in PGL4 and PCC;, features a modification of the amino acid from R to H at position 242.
+The protein's natural variant, known as in MC2DN4; decreased succinate dehydrogenase (ubiquinone) activity; decreased protein levels in homozygous patient cells;, features a modification of the amino acid from L to V at position 257.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from F to L at position 157.
+The protein's natural variant, known as in HMN2C;, features a modification of the amino acid from R to S at position 7.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from E to G at position 290.
+The natural variant of this protein is characterized by an amino acid alteration from A to I at position 303.
+The natural variant of this protein is characterized by an amino acid alteration from F to I at position 382.
+The protein's natural variant, known as in strain: CDC 137-85 and CDC 179-87, features a modification of the amino acid from Y to S at position 139.
+The protein's natural variant, known as in strain: CDC 137-85, features a modification of the amino acid from K to N at position 197.
+The protein's natural variant, known as in strain: CDC 179-87, features a modification of the amino acid from V to G at position 388.
+The protein's natural variant, known as in strain: CDC 179-87, features a modification of the amino acid from Q to H at position 393.
+The protein's natural variant, known as in strain: CDC 179-87, features a modification of the amino acid from E to D at position 414.
+The protein's natural variant, known as in strain: CDC 179-87, CDC 331-86 and CDC 655-84, features a modification of the amino acid from A to R at position 449.
+The protein's natural variant, known as in strain: CDC 137-85, features a modification of the amino acid from L to F at position 463.
+The protein's natural variant, known as in strain: CDC 137-85, features a modification of the amino acid from A to T at position 538.
+The protein's natural variant, known as in strain: CDC 137-85, features a modification of the amino acid from N to K at position 544.
+The protein's natural variant, known as in strain: cv. Bomi, features a modification of the amino acid from Y to H at position 118.
+The protein's natural variant, known as in strain: cv. Bomi, features a modification of the amino acid from G to V at position 210.
+The protein's natural variant, known as in MANSB; nearly complete loss of enzyme activity;, features a modification of the amino acid from R to W at position 182.
+The protein's natural variant, known as decreased enzyme activity;, features a modification of the amino acid from V to I at position 253.
+The protein's natural variant, known as in MANSB; nearly complete loss of enzyme activity, features a modification of the amino acid from G to E at position 392.
+The protein's natural variant, known as in MANSB; nearly complete loss of enzyme activity;, features a modification of the amino acid from S to P at position 505.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from D to N at position 42.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from A to T at position 131.
+The protein's natural variant, known as in MUL; decreased ubiquitination and abolishes the formation of perinuclear aggregates;, features a modification of the amino acid from L to P at position 76.
+The protein's natural variant, known as in MUL; no effect on E3 ubiquitin-protein ligase activity;, features a modification of the amino acid from C to S at position 109.
+The protein's natural variant, known as in MUL; no effect on ubiquitination but affects subcellular localization;, features a modification of the amino acid from G to V at position 322.
+The natural variant of this protein is characterized by an amino acid alteration from S to N at position 687.
+The protein's natural variant, known as loss of mitochondrial location, features a modification of the amino acid from R to Q at position 4.
+The protein's natural variant, known as in B1, features a modification of the amino acid from V to I at position 39.
+The protein's natural variant, known as in B1, features a modification of the amino acid from I to V at position 174.
+The protein's natural variant, known as in B1, features a modification of the amino acid from L to I at position 290.
+The protein's natural variant, known as in B1, features a modification of the amino acid from M to L at position 314.
+The protein's natural variant, known as in B1, features a modification of the amino acid from L to M at position 420.
+The natural variant of this protein is characterized by an amino acid alteration from E to V at position 609.
+The natural variant of this protein is characterized by an amino acid alteration from S to P at position 820.
+The protein's natural variant, known as associated with susceptibility to obesity; induces a 10.4% reduction of activity (P = 0.03) when compared to the wild-type enzyme;, features a modification of the amino acid from N to D at position 221.
+The protein's natural variant, known as in PC1 deficiency; in vitro the mutation markedly impairs the catalytic activity of the enzyme; however intracellular trafficking of this mutant enzyme appears normal; retains some autocatalytic activity even though it is completely inactive on other substrates;, features a modification of the amino acid from S to L at position 307.
+The protein's natural variant, known as in PC1 deficiency; prevents processing of pro-PCSK1 and leads to its retention in the endoplasmic reticulum;, features a modification of the amino acid from G to R at position 483.
+The protein's natural variant, known as in MCPH28; increased proteolytic degradation; decreased recruitment to the nucleolus; decreased interaction with NOL6; decreased function in localization of NOL6 to the nucleolus; loss of function in rRNA processing; changed function in cilia resorption;, features a modification of the amino acid from W to C at position 155.
+The protein's natural variant, known as in SIDBA1; significantly reduced activity, features a modification of the amino acid from K to E at position 156.
+The protein's natural variant, known as in SIDBA1;, features a modification of the amino acid from D to Y at position 159.
+The protein's natural variant, known as in SIDBA1;, features a modification of the amino acid from F to L at position 165.
+The protein's natural variant, known as in SIDBA1, features a modification of the amino acid from R to C at position 170.
+The protein's natural variant, known as in SIDBA1; significantly increased thermosensitivity, features a modification of the amino acid from R to H at position 170.
+The protein's natural variant, known as in SIDBA1;, features a modification of the amino acid from Y to H at position 199.
+The protein's natural variant, known as in SIDBA1; 15% to 35% activity of wild-type;, features a modification of the amino acid from R to Q at position 204.
+The protein's natural variant, known as in SIDBA1; significantly increased thermosensitivity;, features a modification of the amino acid from R to H at position 218.
+The protein's natural variant, known as in SIDBA1; significantly reduced activity, features a modification of the amino acid from E to K at position 242.
+The protein's natural variant, known as in SIDBA1; significantly reduced activity, features a modification of the amino acid from D to N at position 263.
+The protein's natural variant, known as in SIDBA1, features a modification of the amino acid from V to A at position 301.
+The protein's natural variant, known as in SIDBA1; significantly reduced activity, features a modification of the amino acid from P to L at position 339.
+The protein's natural variant, known as in SIDBA1; significantly reduced activity, features a modification of the amino acid from R to C at position 375.
+The protein's natural variant, known as in SIDBA1;, features a modification of the amino acid from T to S at position 388.
+The protein's natural variant, known as in SIDBA1; 12% to 25% activity of wild-type;, features a modification of the amino acid from R to C at position 411.
+The protein's natural variant, known as in SIDBA1; significantly reduced activity, features a modification of the amino acid from R to H at position 411.
+The protein's natural variant, known as in SIDBA1, features a modification of the amino acid from R to Q at position 448.
+The protein's natural variant, known as in SIDBA1;, features a modification of the amino acid from R to C at position 452.
+The protein's natural variant, known as in SIDBA1; does not affect activity, features a modification of the amino acid from R to G at position 452.
+The protein's natural variant, known as in SIDBA1;, features a modification of the amino acid from R to H at position 452.
+The protein's natural variant, known as in SIDBA1;, features a modification of the amino acid from I to N at position 476.
+The protein's natural variant, known as in SIDBA1, features a modification of the amino acid from R to G at position 517.
+The protein's natural variant, known as in SIDBA1; likely benign variant; associated in cis with H-560 in a patient;, features a modification of the amino acid from P to L at position 520.
+The protein's natural variant, known as in SIDBA1; associated in cis with L-520 in a patient;, features a modification of the amino acid from R to H at position 560.
+The protein's natural variant, known as in SIDBA1; does not affect activity, features a modification of the amino acid from R to H at position 572.
+The protein's natural variant, known as rare variant found in a congenital erythropoietic porphyria patient that also carries UROS mutations R-73 and Q-248; increased enzyme activity;, features a modification of the amino acid from Y to F at position 586.
+The protein's natural variant, known as in RP58; cannot bind to promoters of retinal-specific genes;, features a modification of the amino acid from C to R at position 339.
+The natural variant of this protein is characterized by an amino acid alteration from E to D at position 92.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from T to A at position 27.
+The protein's natural variant, known as in 50% of the molecules, features a modification of the amino acid from S to N at position 493.
+The protein's natural variant, known as in PITA1; unknown pathological significance;, features a modification of the amino acid from K to E at position 241.
+The protein's natural variant, known as in PITA1; unknown pathological significance;, features a modification of the amino acid from R to W at position 271.
+The protein's natural variant, known as in PITA1; ACTH-secreting pituitary adenoma;, features a modification of the amino acid from R to Q at position 304.
+The protein's natural variant, known as in strain: IL1403, features a modification of the amino acid from N to T at position 31.
+The protein's natural variant, known as in strain: IL1403, features a modification of the amino acid from GAK to DAN at position 56.
+The protein's natural variant, known as in strain: IL1403, features a modification of the amino acid from L to I at position 65.
+The protein's natural variant, known as in strain: IL1403, features a modification of the amino acid from D to E at position 71.
+The protein's natural variant, known as in strain: IL1403, features a modification of the amino acid from RIV to KII at position 127.
+The protein's natural variant, known as in strain: IL1403, features a modification of the amino acid from G to K at position 227.
+The protein's natural variant, known as in SOFT;, features a modification of the amino acid from L to P at position 171.
+The protein's natural variant, known as in strain: Bf-H09, features a modification of the amino acid from P to S at position 6.
+The protein's natural variant, known as in strain: Bf-M01 and Bf-H10, features a modification of the amino acid from V to I at position 52.
+The protein's natural variant, known as in strain: Bf-H07, features a modification of the amino acid from A to V at position 160.
+The protein's natural variant, known as in strain: Bf-H03 and Bf-H04, features a modification of the amino acid from I to V at position 210.
+The protein's natural variant, known as found in a patient with azoospermia; unknown pathological significance, features a modification of the amino acid from H to R at position 22.
+The protein's natural variant, known as found in a patient with azoospermia; unknown pathological significance;, features a modification of the amino acid from R to W at position 53.
+The protein's natural variant, known as found in a patient with azoospermia; unknown pathological significance;, features a modification of the amino acid from A to S at position 88.
+The protein's natural variant, known as found in a patient with azoospermia; unknown pathological significance;, features a modification of the amino acid from A to T at position 156.
+The protein's natural variant, known as found in patients with azoospermia; unknown pathological significance;, features a modification of the amino acid from G to R at position 212.
+The protein's natural variant, known as found in a patient with azoospermia; unknown pathological significance;, features a modification of the amino acid from R to C at position 332.
+The protein's natural variant, known as in SMA2 and SMA3;, features a modification of the amino acid from A to G at position 2.
+The protein's natural variant, known as in SMA2;, features a modification of the amino acid from D to N at position 30.
+The protein's natural variant, known as in SMA3; impairs GEMIN2 binding;, features a modification of the amino acid from D to V at position 44.
+The protein's natural variant, known as in SMA3; reduces SMN binding to Sm proteins;, features a modification of the amino acid from G to R at position 95.
+The protein's natural variant, known as in SMA2; reduces SMN binding to Sm proteins; abolishes the interaction with ELAVL4;, features a modification of the amino acid from A to G at position 111.
+The protein's natural variant, known as in SMA1; abolishes the interaction with ELAVL4;, features a modification of the amino acid from I to F at position 116.
+The protein's natural variant, known as in SMA1; abolishes the interaction with ELAVL4;, features a modification of the amino acid from Q to E at position 136.
+The protein's natural variant, known as in SMA3;, features a modification of the amino acid from P to L at position 245.
+The protein's natural variant, known as in SMA3;, features a modification of the amino acid from S to G at position 262.
+The protein's natural variant, known as in SMA3; slightly reduces SMN binding to RPP20/POP7;, features a modification of the amino acid from S to I at position 262.
+The protein's natural variant, known as in SMA1; abolishes SMN1 binding to RPP20/POP7 and severely impairs binding to SNRPB, GEMIN8 and homooligomerization;, features a modification of the amino acid from Y to C at position 272.
+The protein's natural variant, known as in SMA2 and SMA3; Impairs SMN1 binding to RPP20/POP7, GEMIN8 and homooligomerization;, features a modification of the amino acid from T to I at position 274.
+The protein's natural variant, known as in SMA3; impairs homooligomerization.;, features a modification of the amino acid from G to S at position 275.
+The protein's natural variant, known as in SMA2 and SMA3;, features a modification of the amino acid from G to C at position 279.
+The protein's natural variant, known as in SMA1; slightly reduces SMN binding to RPP20/POP7. Impairs homooligomerization and axon localization;, features a modification of the amino acid from G to V at position 279.
+The protein's natural variant, known as in PCKDC; decreased stability; no effect on phosphoenolpyruvate carboxykinase activity;, features a modification of the amino acid from I to T at position 45.
+The protein's natural variant, known as in PCKDC; unknown pathological significance; decreased phosphoenolpyruvate carboxykinase activity;, features a modification of the amino acid from G to R at position 309.
+The natural variant of this protein is characterized by an amino acid alteration from G to E at position 55.
+The natural variant of this protein is characterized by an amino acid alteration from F to Y at position 295.
+The protein's natural variant, known as in strain: cv. Provar, features a modification of the amino acid from H to D at position 25.
+The protein's natural variant, known as in strain: cv. Provar, features a modification of the amino acid from P to S at position 57.
+The protein's natural variant, known as in strain: cv. Provar, features a modification of the amino acid from L to P at position 112.
+The protein's natural variant, known as in strain: cv. Provar, features a modification of the amino acid from V to I at position 201.
+The protein's natural variant, known as in strain: cv. Provar, features a modification of the amino acid from E to D at position 382.
+The protein's natural variant, known as in strain: cv. Provar, features a modification of the amino acid from G to D at position 428.
+The protein's natural variant, known as in strain: cv. Provar, features a modification of the amino acid from A to T at position 630.
+The protein's natural variant, known as in spastic 1, features a modification of the amino acid from NFKGIPVDVV to TTMLDIQPMI at position 83.
+The protein's natural variant, known as in spastic 2, features a modification of the amino acid from LFFANEKSA to VSMSWIYNR at position 151.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from I to V at position 282.
+The protein's natural variant, known as in GVIIB, features a modification of the amino acid from L to S at position 21.
+The protein's natural variant, known as in pRTA-OA; decreased localization to the basolateral membrane; mistargeting to the apical membrane probably explains the loss of the cotransporter activity;, features a modification of the amino acid from R to S at position 342.
+The protein's natural variant, known as in pRTA-OA; mistargeting to the apical membrane and altered function, features a modification of the amino acid from S to L at position 471.
+The protein's natural variant, known as in pRTA-OA; decreased cotransporter activity; mediates electroneutral sodium/bicarbonate cotransport rather than electrogenic sodium/bicarbonate cotransport; no effect on cell membrane localization; significant loss of cotransporter activity when associated with S-530, features a modification of the amino acid from T to S at position 529.
+The protein's natural variant, known as in pRTA-OA; decreased cotransporter activity; no effect on localization to the basolateral membrane; significant loss of cotransporter activity when associated with S-529, features a modification of the amino acid from G to R at position 530.
+The protein's natural variant, known as in pRTA-OA; mistargeting and altered function;, features a modification of the amino acid from R to H at position 554.
+The protein's natural variant, known as in pRTA-OA; loss of localization to the plasma membrane; the retention in the cytoplasm probably explains the loss of the cotransporter activity, features a modification of the amino acid from L to P at position 566.
+The protein's natural variant, known as in pRTA-OA; altered function, features a modification of the amino acid from A to V at position 843.
+The protein's natural variant, known as in pRTA-OA; altered function;, features a modification of the amino acid from R to C at position 925.
+The protein's natural variant, known as in strain: JCM 7638, features a modification of the amino acid from N to H at position 50.
+The protein's natural variant, known as no effect on U-44069 and 9,11-diazo-prostadienoic acid (U-51605) hydroxylation; loss of 20:4n-6 or 22:5n-6 oxidation;, features a modification of the amino acid from Y to F at position 125.
+The protein's natural variant, known as in strain: 91001 / Biovar Mediaevalis, features a modification of the amino acid from A to APAPA at position 39.
+The protein's natural variant, known as in strain: KIM5 / Biovar Mediaevalis, features a modification of the amino acid from A to APAPAPAPA at position 39.
+The protein's natural variant, known as in BOS3; crucial for interaction with EYA1 and EYA2 and transcription factor activity;, features a modification of the amino acid from V to E at position 17.
+The protein's natural variant, known as in BOS3, features a modification of the amino acid from H to P at position 73.
+The protein's natural variant, known as in BOS3; crucial for protein stability, DNA binding and transcription factor activity;, features a modification of the amino acid from V to G at position 106.
+The protein's natural variant, known as in BOS3;, features a modification of the amino acid from R to Q at position 110.
+The protein's natural variant, known as in BOS3; crucial for interaction with EYA1, DNA binding and transcription factor activity;, features a modification of the amino acid from R to W at position 110.
+The protein's natural variant, known as in BOS3; crucial for DNA binding and transcription factor activity;, features a modification of the amino acid from R to C at position 112.
+The protein's natural variant, known as in BOS3;, features a modification of the amino acid from W to R at position 122.
+The protein's natural variant, known as in BOS3; crucial for interaction with EYA1, DNA binding and transcription factor activity;, features a modification of the amino acid from Y to C at position 129.
+The protein's natural variant, known as in BOR; uncertain pathological significance;, features a modification of the amino acid from P to L at position 249.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from V to M at position 138.
+The protein's natural variant, known as in strain: 9106, 9181, An03, F12, F18 and TCVGH21; resistant to streptomycin, features a modification of the amino acid from K to R at position 43.
+The protein's natural variant, known as in strain: TCVGH25; probably resistant to streptomycin, features a modification of the amino acid from K to T at position 43.
+The protein's natural variant, known as in strain: F05; resistant to streptomycin, features a modification of the amino acid from K to Q at position 88.
+The protein's natural variant, known as in strain: C37; probably resistant to streptomycin, features a modification of the amino acid from K to R at position 88.
+The protein's natural variant, known as in strain: F18; resistant to streptomycin, features a modification of the amino acid from K to T at position 88.
+The protein's natural variant, known as in alpha-1, features a modification of the amino acid from D to G at position 15.
+The protein's natural variant, known as in alpha-1, features a modification of the amino acid from T to A at position 57.
+The protein's natural variant, known as in HH24;, features a modification of the amino acid from C to G at position 69.
+The protein's natural variant, known as in HH2; unknown pathological significance;, features a modification of the amino acid from W to C at position 4.
+The protein's natural variant, known as in HH2; phenotype consistent with normosmic idiopathic hypogonadotropic hypogonadism;, features a modification of the amino acid from G to S at position 48.
+The protein's natural variant, known as in HH2;, features a modification of the amino acid from G to R at position 70.
+The protein's natural variant, known as in HH2;, features a modification of the amino acid from R to C at position 78.
+The protein's natural variant, known as in HH2; unknown pathological significance, features a modification of the amino acid from S to C at position 96.
+The protein's natural variant, known as in HH2, features a modification of the amino acid from G to D at position 97.
+The protein's natural variant, known as in HH2; impairs the tertiary folding resulting in incomplete glycosylation and reduced cell surface expression;, features a modification of the amino acid from Y to C at position 99.
+The protein's natural variant, known as in HH2, features a modification of the amino acid from C to F at position 101.
+The protein's natural variant, known as in HH2;, features a modification of the amino acid from V to I at position 102.
+The protein's natural variant, known as in HH2;, features a modification of the amino acid from V to I at position 116.
+The protein's natural variant, known as in HH2; some patients also carry GNRHR mutations;, features a modification of the amino acid from N to S at position 117.
+The protein's natural variant, known as in a breast infiltrating ductal carcinoma sample; somatic mutation;, features a modification of the amino acid from S to L at position 125.
+The protein's natural variant, known as in HH2;, features a modification of the amino acid from D to A at position 129.
+The protein's natural variant, known as in HRTFDS;, features a modification of the amino acid from L to S at position 165.
+The protein's natural variant, known as in HH2; with cleft palate, corpus callosum agenesis, unilateral deafness and fusion of fourth and fifth metacarpal bones;, features a modification of the amino acid from A to S at position 167.
+The protein's natural variant, known as in HH2, features a modification of the amino acid from V to A at position 174.
+The protein's natural variant, known as in HH2; with severe ear anomalies, features a modification of the amino acid from C to S at position 178.
+The protein's natural variant, known as in HRTFDS;, features a modification of the amino acid from L to S at position 191.
+The protein's natural variant, known as in HH2, features a modification of the amino acid from D to H at position 224.
+The protein's natural variant, known as in HH2; some patients also carry KISS1R mutations; impairs the tertiary folding resulting in incomplete glycosylation and reduced cell surface expression, features a modification of the amino acid from Y to D at position 228.
+The protein's natural variant, known as in HH2, features a modification of the amino acid from G to D at position 237.
+The protein's natural variant, known as in HH2; with or without anosmia; also found in a family member with isolated anosmia; may impair proper folding;, features a modification of the amino acid from G to S at position 237.
+The protein's natural variant, known as in HH2; some patients also carry PROKR2 and GNRH1 mutations; impairs the tertiary folding resulting in incomplete glycosylation and reduced cell surface expression, features a modification of the amino acid from I to T at position 239.
+The protein's natural variant, known as in HH2, features a modification of the amino acid from L to P at position 245.
+The protein's natural variant, known as in HH2; with or without anosmia; results in Kallmann syndrome in the presence of HS6ST1 mutation TRP-306; reduces receptor affinity for fibroblast growth factor;, features a modification of the amino acid from R to Q at position 250.
+The protein's natural variant, known as in HH2, features a modification of the amino acid from R to W at position 250.
+The protein's natural variant, known as in PS and JWS;, features a modification of the amino acid from P to R at position 252.
+The protein's natural variant, known as in a lung bronchoalveolar carcinoma sample; somatic mutation;, features a modification of the amino acid from P to T at position 252.
+The protein's natural variant, known as in HH2, features a modification of the amino acid from R to Q at position 254.
+The protein's natural variant, known as in HH2, features a modification of the amino acid from G to D at position 270.
+The protein's natural variant, known as in HH2;, features a modification of the amino acid from V to M at position 273.
+The protein's natural variant, known as in HH2; also found in a family member with isolated anosmia;, features a modification of the amino acid from E to G at position 274.
+The protein's natural variant, known as in HH2, features a modification of the amino acid from C to Y at position 277.
+The protein's natural variant, known as in HH2, features a modification of the amino acid from P to R at position 283.
+The protein's natural variant, known as in TRIGNO1;, features a modification of the amino acid from I to T at position 300.
+The protein's natural variant, known as in OGD;, features a modification of the amino acid from N to I at position 330.
+The protein's natural variant, known as in HH2, features a modification of the amino acid from S to C at position 332.
+The protein's natural variant, known as in HH2, features a modification of the amino acid from Y to C at position 339.
+The protein's natural variant, known as in HH2; phenotype consistent with Kallmann syndrome; the patient also carries a splice site mutation in NSMF;, features a modification of the amino acid from L to S at position 342.
+The protein's natural variant, known as in HH2, features a modification of the amino acid from A to V at position 343.
+The protein's natural variant, known as in HH2; also found in a family member with isolated anosmia, features a modification of the amino acid from S to C at position 346.
+The protein's natural variant, known as in HH2; phenotype consistent with Kallmann syndrome; the patient also carries a mutation in IL17RD;, features a modification of the amino acid from G to R at position 348.
+The protein's natural variant, known as in HH2; with or without anosmia;, features a modification of the amino acid from P to L at position 366.
+The protein's natural variant, known as in OGD; elevated basal activity and increased FGF2-mediated activity;, features a modification of the amino acid from Y to C at position 374.
+The protein's natural variant, known as in OGD;, features a modification of the amino acid from C to R at position 381.
+The protein's natural variant, known as in HH2; some patients also carry GNRHR mutations;, features a modification of the amino acid from R to L at position 470.
+The protein's natural variant, known as in HH2; phenotype consistent with Kallmann syndrome; the patient also carries a rare variant in SPRY4;, features a modification of the amino acid from P to T at position 483.
+The protein's natural variant, known as in HRTFDS;, features a modification of the amino acid from G to R at position 490.
+The protein's natural variant, known as in HH2;, features a modification of the amino acid from A to T at position 520.
+The protein's natural variant, known as in HH2, features a modification of the amino acid from I to V at position 538.
+The protein's natural variant, known as in ECCL; somatic mutation; activating mutation; strongly increased speed of the first autophosphorylation and loss of the normal sequential order of autophosphorylation;, features a modification of the amino acid from N to K at position 546.
+The natural variant of this protein is characterized by an amino acid alteration from V to M at position 561.
+The protein's natural variant, known as in HH2; with bimanual synkinesis;, features a modification of the amino acid from V to M at position 607.
+The protein's natural variant, known as in HH2; some patients also carry GNRHR mutations; impairs tyrosine kinase activity, features a modification of the amino acid from K to N at position 618.
+The protein's natural variant, known as in HH2, features a modification of the amino acid from H to R at position 621.
+The protein's natural variant, known as in HH2; with severe ear anomalies;, features a modification of the amino acid from R to G at position 622.
+The protein's natural variant, known as in HH2, features a modification of the amino acid from R to Q at position 622.
+The protein's natural variant, known as in HRTFDS;, features a modification of the amino acid from D to Y at position 623.
+The protein's natural variant, known as in HRTFDS;, features a modification of the amino acid from R to T at position 627.
+The protein's natural variant, known as in HRTFDS;, features a modification of the amino acid from N to K at position 628.
+The protein's natural variant, known as in ECCL; somatic mutation;, features a modification of the amino acid from K to E at position 656.
+The protein's natural variant, known as in a lung large cell carcinoma sample; somatic mutation, features a modification of the amino acid from V to L at position 664.
+The protein's natural variant, known as in HH2; with cleft palate;, features a modification of the amino acid from W to R at position 666.
+The protein's natural variant, known as in HH2; phenotype consistent with Kallmann syndrome; the patient also carries a rare variant in FLRT3;, features a modification of the amino acid from E to K at position 670.
+The protein's natural variant, known as in HH2, features a modification of the amino acid from A to P at position 671.
+The protein's natural variant, known as in HH2, features a modification of the amino acid from S to F at position 685.
+The protein's natural variant, known as in HH2;, features a modification of the amino acid from G to R at position 687.
+The protein's natural variant, known as in HH2; phenotype consistent with Kallmann syndrome; the patient also carries a rare variant in DUSP6;, features a modification of the amino acid from E to G at position 692.
+The protein's natural variant, known as in HH2, features a modification of the amino acid from I to F at position 693.
+The protein's natural variant, known as in HH2, features a modification of the amino acid from G to R at position 703.
+The protein's natural variant, known as in HH2;, features a modification of the amino acid from G to S at position 703.
+The protein's natural variant, known as in HH2, features a modification of the amino acid from M to R at position 719.
+The protein's natural variant, known as in HH2; unknown pathological significance;, features a modification of the amino acid from M to V at position 719.
+The protein's natural variant, known as in HH2; associated with K-724; also found in a family member with isolated anosmia; reduced tyrosine kinase activity;, features a modification of the amino acid from P to H at position 722.
+The protein's natural variant, known as in HH2;, features a modification of the amino acid from P to S at position 722.
+The protein's natural variant, known as in HH2; associated with H-722; also found in a family member with isolated anosmia; reduced tyrosine kinase activity;, features a modification of the amino acid from N to K at position 724.
+The protein's natural variant, known as in HRTFDS;, features a modification of the amino acid from C to Y at position 725.
+The protein's natural variant, known as in HH2, features a modification of the amino acid from P to S at position 745.
+The protein's natural variant, known as in HH2; the patient also carries a rare variant in FGF8;, features a modification of the amino acid from D to Y at position 768.
+The protein's natural variant, known as in HH2; also found in a family member with isolated anosmia;, features a modification of the amino acid from V to I at position 795.
+The protein's natural variant, known as in CHILD;, features a modification of the amino acid from A to V at position 105.
+The protein's natural variant, known as in CHILD;, features a modification of the amino acid from A to P at position 182.
+The protein's natural variant, known as in CHILD;, features a modification of the amino acid from G to S at position 205.
+The protein's natural variant, known as in EDFAOB; somatic mosaic variant; decreased Rho protein signal transduction; decreased substrate adhesion-dependent cell spreading; decreased number of stress fibers assembly; decreased cytoplasmic microtubule organization, features a modification of the amino acid from E to K at position 47.
+The protein's natural variant, known as in EDFAOB; somatic mosaic variant; decreased Rho protein signal transduction; decreased substrate adhesion-dependent cell spreading; decreased stress fibers assembly; decreased cytoplasmic microtubule organization, features a modification of the amino acid from P to S at position 71.
+The natural variant of this protein is characterized by an amino acid alteration from P to E at position 3.
+The natural variant of this protein is characterized by an amino acid alteration from W to D at position 10.
+The natural variant of this protein is characterized by an amino acid alteration from A to G at position 60.
+The natural variant of this protein is characterized by an amino acid alteration from K to N at position 66.
+The natural variant of this protein is characterized by an amino acid alteration from K to Q at position 83.
+The protein's natural variant, known as in HMAKD; the mutant shows some residual adenosine kinase activity;, features a modification of the amino acid from G to E at position 30.
+The protein's natural variant, known as in HMAKD; the mutant shows some residual adenosine kinase activity;, features a modification of the amino acid from D to A at position 235.
+The protein's natural variant, known as in HMAKD; complete loss of adenosine kinase activity;, features a modification of the amino acid from A to E at position 318.
+The natural variant of this protein is characterized by an amino acid alteration from G to S at position 146.
+The natural variant of this protein is characterized by an amino acid alteration from R to Q at position 298.
+The protein's natural variant, known as in cell line LoVo; does not undergo autocatalytic activation and is not transported to the Golgi apparatus, features a modification of the amino acid from W to R at position 547.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 636.
+The protein's natural variant, known as in strain: NOD/LtJ, features a modification of the amino acid from C to R at position 211.
+The protein's natural variant, known as in strain: SJL/J, features a modification of the amino acid from P to L at position 967.
+The protein's natural variant, known as in strain: BALB/CBYJ, features a modification of the amino acid from S to F at position 968.
+The protein's natural variant, known as in strain: CN13X, features a modification of the amino acid from L to F at position 399.
+The protein's natural variant, known as in strain: CN11X, features a modification of the amino acid from A to T at position 560.
+The protein's natural variant, known as in strain: NVIII-42 and NVIII-18, features a modification of the amino acid from H to R at position 121.
+The protein's natural variant, known as in strain: NVIII-m11, features a modification of the amino acid from D to V at position 162.
+The protein's natural variant, known as in strain: UO1, features a modification of the amino acid from S to A at position 19.
+The protein's natural variant, known as in strain: UO1, features a modification of the amino acid from R to K at position 23.
+The protein's natural variant, known as in strain: UO1, features a modification of the amino acid from H to N at position 89.
+The protein's natural variant, known as in ORAC1; reduced OPRT activity; no effect on ODC activity; reduced OPRT and ODC activities when associated with R-429;, features a modification of the amino acid from R to G at position 96.
+The protein's natural variant, known as in ORAC1; reduced OPRT activity; reduced ODC activity;, features a modification of the amino acid from V to G at position 109.
+The protein's natural variant, known as in ORAC1; increased OPRT activity; reduced ODC activity; reduced OPRT and ODC activities when associated with G-96;, features a modification of the amino acid from G to R at position 429.
+The protein's natural variant, known as probable disease-associated variant found in a patient with congenital heart defect; severe decrease of positive regulation of transcription from TH promoter, features a modification of the amino acid from L to P at position 38.
+The protein's natural variant, known as in MK1, features a modification of the amino acid from RPAPVAA to LAGAGRR at position 147.
+The protein's natural variant, known as in MK1, features a modification of the amino acid from VA to LR at position 194.
+The protein's natural variant, known as in allele A*34:01, features a modification of the amino acid from V to I at position 3.
+The protein's natural variant, known as in allele A*80:01, features a modification of the amino acid from A to P at position 5.
+The protein's natural variant, known as in allele A*02:01, allele A*02:05, allele A*23:01, allele A*24:02, allele A*25:01, allele A*26:01, allele A*34:01, allele A*43:01, allele A*66:01, allele A*68:01 and allele A*69:01, features a modification of the amino acid from L to V at position 10.
+The protein's natural variant, known as in allele A*29:02, allele A*31:01, allele A*32:01, allele A*33:01 and allele A*74:01, features a modification of the amino acid from S to L at position 14.
+The protein's natural variant, known as in allele A*74:01, features a modification of the amino acid from W to R at position 23.
+The protein's natural variant, known as in allele A*23:01, allele A*24:02 and allele A*30:01;, features a modification of the amino acid from F to S at position 33.
+The protein's natural variant, known as in allele A*29:02, allele A*31:01 and allele A*33:01; requires 2 nucleotide substitutions, features a modification of the amino acid from F to T at position 33.
+The protein's natural variant, known as in allele A*02:05, allele A*11:01, allele A*25:01, allele A*26:01, allele A*34:01, allele A*43:01, allele A*66:01, allele A*68:01 and allele A*69:01;, features a modification of the amino acid from F to Y at position 33.
+The protein's natural variant, known as in allele A*30:01;, features a modification of the amino acid from R to S at position 41.
+The protein's natural variant, known as in allele A*80:01, features a modification of the amino acid from T to S at position 55.
+The protein's natural variant, known as in allele A*80:01, features a modification of the amino acid from R to Q at position 59.
+The protein's natural variant, known as in allele A*02:05;, features a modification of the amino acid from Q to R at position 67.
+The protein's natural variant, known as in alleles A*01:01 and allele A*36:01, features a modification of the amino acid from R to K at position 68.
+The protein's natural variant, known as in allele A*80:01, features a modification of the amino acid from G to E at position 80.
+The protein's natural variant, known as in allele A*30:01 and allele A*31:01;, features a modification of the amino acid from G to R at position 80.
+The protein's natural variant, known as in allele A*23:01, allele 24:02 and allele A*80:01, features a modification of the amino acid from Q to E at position 86.
+The protein's natural variant, known as in allele A*02:01 and allele A*02:05; requires 2 nucleotide substitutions, features a modification of the amino acid from Q to G at position 86.
+The protein's natural variant, known as in alleles A*29:02 and allele A*43:01, features a modification of the amino acid from Q to L at position 86.
+The protein's natural variant, known as in allele A*25:01, allele A*26:01, allele A*33:01, allele A*34:01, allele A*66:01, allele A*68:01 and allele A*69:01, features a modification of the amino acid from Q to R at position 86.
+The protein's natural variant, known as in alleles A*25:01, allele A*26:01, allele A*33:01, allele A*34:01, allele A*66:01, allele A*68:01 and allele A*69:01; requires 2 nucleotide substitutions, features a modification of the amino acid from E to N at position 87.
+The protein's natural variant, known as in allele A*29:02 and allele A*43:01, features a modification of the amino acid from E to Q at position 87.
+The protein's natural variant, known as in allele A*23:01 and allele 24:02;, features a modification of the amino acid from R to G at position 89.
+The protein's natural variant, known as in allele A*02:01, allele A*02:05, allele A*23:01, allele 24:02 and allele A*34:01;, features a modification of the amino acid from N to K at position 90.
+The protein's natural variant, known as in allele A*01:01 and allele A*36:01, features a modification of the amino acid from V to M at position 91.
+The protein's natural variant, known as in allele A*01:01, allele A*02:01, allele A*02:05, allele A*23:01, allele 24:02, allele A*25:01, allele A*26:01, allele A*31:01, allele A*32:01, allele A*33:01, allele A*36:01, allele A*43:01, allele A*74:01 and allele A*80:01;, features a modification of the amino acid from Q to H at position 94.
+The protein's natural variant, known as in allele A*31:01 and allele A*33:01;, features a modification of the amino acid from T to I at position 97.
+The protein's natural variant, known as in allele A*02:01 and allele A*02:05, features a modification of the amino acid from D to H at position 98.
+The protein's natural variant, known as in allele A*80:01, features a modification of the amino acid from D to N at position 98.
+The protein's natural variant, known as in allele A*01:01, allele A*26:01, allele A*29:02, allele A*36:01, allele A*43:01 and allele A*80:01, features a modification of the amino acid from V to A at position 100.
+The protein's natural variant, known as in allele A*23:01, allele A*24:02, allele A*25:01 and allele A*32:01;, features a modification of the amino acid from V to E at position 100.
+The protein's natural variant, known as allele A*01:01, allele A*23:01, allele A*24:02, allele A*26:01, allele A*29:02, allele A*36:01, allele A*43:01 and allele A*80:01;, features a modification of the amino acid from D to N at position 101.
+The protein's natural variant, known as in allele A*25:01 and allele A*32:01; requires 2 nucleotide substitutions, features a modification of the amino acid from D to S at position 101.
+The protein's natural variant, known as in allele A*23:01, allele A*24:02, allele A*25:01 and allele A*32:01; Bw4 motif RIALR is involved in the recognition of NK cell inhibitory receptor KIR3DL1, features a modification of the amino acid from GTLRG to RIALR at position 107.
+The protein's natural variant, known as in allele A*01:01, allele A*11:01, allele A*25:01, allele A*26:01, allele A*34:01, allele A*36:01, allele A*43:01, allele A*66:01 and allele A*80:01;, features a modification of the amino acid from A to D at position 114.
+The protein's natural variant, known as in allele A*02:05, allele A*23:01 and allele 24:02;, features a modification of the amino acid from I to L at position 119.
+The protein's natural variant, known as in allele A*02:01 and allele A*69:01, features a modification of the amino acid from I to V at position 119.
+The protein's natural variant, known as in allele A*23:01, allele 24:02, allele A*29:02, allele A*31:01, allele A*32:01, allele A*33:01, allele A*68:01 and allele A*74:01;, features a modification of the amino acid from I to M at position 121.
+The protein's natural variant, known as in allele A*02:01, allele A*02:05, allele A*25:01, allele A*26:01, allele A*34:01, allele A*43:01, allele A*66:01 and allele A*69:01, features a modification of the amino acid from I to R at position 121.
+The protein's natural variant, known as in allele A*23:01, allele 24:02;, features a modification of the amino acid from Y to F at position 123.
+The protein's natural variant, known as in allele A*01:01, allele A*11:01, allele A*25:01, allele A*26:01, allele A*32:01, allele A*34:01, allele A*36:01, allele A*43:01, allele A*66:01 and allele A*74:01;, features a modification of the amino acid from S to P at position 129.
+The protein's natural variant, known as in allele A*02:01, allele A*02:05 and allele A*69:01;, features a modification of the amino acid from G to W at position 131.
+The protein's natural variant, known as in allele A*32:01 and allele A*74:01;, features a modification of the amino acid from F to L at position 133.
+The protein's natural variant, known as in allele A*30:01; requires 2 nucleotide substitutions, features a modification of the amino acid from R to E at position 138.
+The protein's natural variant, known as in allele A*02:01, allele A*02:05, allele A*23:01, allele A*24:02, allele A*69:01, features a modification of the amino acid from R to H at position 138.
+The protein's natural variant, known as in allele A*25:01, allele A*26:01, allele A*31:01, allele A*32:01, allele A*33:01, allele A*34:01, allele A*43:01, allele A*66:01, allele A*74:01, features a modification of the amino acid from R to Q at position 138.
+The protein's natural variant, known as in allele A*30:01, features a modification of the amino acid from D to H at position 140.
+The protein's natural variant, known as in allele A*02:01, allele A*02:05, allele A*23:01, allele A*24:02 and allele A*69:01, features a modification of the amino acid from D to Y at position 140.
+The protein's natural variant, known as in allele A*02:01, allele A*02:05, allele A*23:01, allele A*24:02, allele A*68:01 and allele A*69:01;, features a modification of the amino acid from N to K at position 151.
+The protein's natural variant, known as in allele A*02:01, allele A*02:05, allele A*68:01 and allele A*69:01;, features a modification of the amino acid from I to T at position 166.
+The protein's natural variant, known as in allele A*23:01, allele A*25:01, allele A*26:01, allele A*29:02, allele A*30:01, allele A*31:01, allele A*32:01, allele A*33:01, allele A*34:01, allele A*43:01, allele A*66:01 and allele A*74:01, features a modification of the amino acid from K to Q at position 168.
+The protein's natural variant, known as in allele A*02:01, allele A*02:05, allele A*68:01 and allele A*69:01;, features a modification of the amino acid from R to H at position 169.
+The protein's natural variant, known as in allele A*25:01, allele A*26:01, allele A*34:01, allele A*43:01 and allele A*66:01;, features a modification of the amino acid from A to T at position 173.
+The protein's natural variant, known as in allele A*01:01 and allele A*36:01, features a modification of the amino acid from A to V at position 174.
+The protein's natural variant, known as in allele A*23:01, allele A*29:02, allele A*30:01, allele A*31:01, allele A*32:01, allele A*33:01, allele A*74:01 and allele A*80:01, features a modification of the amino acid from H to R at position 175.
+The protein's natural variant, known as in allele A*01:01, allele A*11:01 and allele A*36:01, features a modification of the amino acid from E to A at position 176.
+The protein's natural variant, known as in allele A*80:01; requires 2 nucleotide substitutions, features a modification of the amino acid from E to R at position 176.
+The protein's natural variant, known as in allele A*02:01, allele A*02:05, allele A*23:01, allele A*24:02, allele A*29:02, allele A*31:01, allele A*32:01, allele A*33:01, allele A*68:01, allele A*69:01 and allele A*74:01; results in inefficient T cell recognition of epitopes derived from influenza A virus.;, features a modification of the amino acid from E to V at position 176.
+The protein's natural variant, known as in allele A*30:01; requires 2 nucleotide substitutions, features a modification of the amino acid from E to W at position 176.
+The protein's natural variant, known as in allele A*11:01 and allele A*24:02, features a modification of the amino acid from L to Q at position 180.
+The protein's natural variant, known as in allele A*01:01 and allele A*36:01, features a modification of the amino acid from L to R at position 180.
+The protein's natural variant, known as in allele A*02:05, allele A*25:01, allele A*26:01, allele A*34:01, allele A*43:01, allele A*66:01, allele A*68:01;, features a modification of the amino acid from L to W at position 180.
+The protein's natural variant, known as in allele A*01:01 and allele A*36:01, features a modification of the amino acid from A to V at position 182.
+The protein's natural variant, known as in allele A*01:01, allele A*02:01, allele A*02:05, allele A*11:01, allele A*23:01, allele A*24:02, allele A*25:01, allele A*26:01, allele A*29:02, allele A*30:01, allele A*31:01, allele A*32:01, allele A*33:01, allele A*34:01, allele A*36:01, allele A*43:01, allele A*66:01, allele A*68:01, allele A*69:01, allele A*74:01 and allele A*80:01;, features a modification of the amino acid from D to E at position 185.
+The protein's natural variant, known as in allele A*80:01; requires 2 nucleotide substitutions, features a modification of the amino acid from T to E at position 187.
+The protein's natural variant, known as in allele A*01:01, allele A*11:01, allele A*25:01, allele A*26:01, allele A*43:01 and allele A*66:01, features a modification of the amino acid from T to R at position 187.
+The protein's natural variant, known as in allele A*01:01, allele A*23:01, allele A*24:02 and allele A*80:01;, features a modification of the amino acid from E to D at position 190.
+The protein's natural variant, known as in allele A*01:01, allele A*23:01, allele A*24:02 and allele A*80:01;, features a modification of the amino acid from W to G at position 191.
+The protein's natural variant, known as in allele A*33:01, features a modification of the amino acid from Y to H at position 195.
+The protein's natural variant, known as in allele A*02:01, allele A*02:05, allele A*25:01, allele A*26:01, allele A*29:02, allele A*32:01, allele A*34:01, allele A*43:01, allele A*66:01, allele A*68:01, allele A*69:01 and allele A*74:01, features a modification of the amino acid from P to A at position 208.
+The protein's natural variant, known as in allele A*33:01, features a modification of the amino acid from K to R at position 210.
+The protein's natural variant, known as in allele A*02:01, allele A*02:05, allele A*25:01, allele A*26:01, allele A*29:02, allele A*31:01, allele A*32:01, allele A*33:01, allele A*34:01, allele A*43:01, allele A*66:01, allele A*68:01, allele A*69:01, allele A*74:01, features a modification of the amino acid from P to A at position 217.
+The protein's natural variant, known as in allele A*02:01, allele A*02:05, allele A*25:01, allele A*26:01, allele A*29:02, allele A*31:01, allele A*32:01, allele A*33:01, allele A*34:01, allele A*43:01, allele A*66:01, allele A*68:01, allele A*69:01 and allele A*74:01, features a modification of the amino acid from I to V at position 218.
+The protein's natural variant, known as in allele A*02:01, allele A*02:05, allele A*25:01, allele A*26:01, allele A*29:02, allele A*31:01, allele A*32:01, allele A*33:01, allele A*34:01, allele A*43:01, allele A*66:01, allele A*68:01, allele A*69:01, allele A*74:01 and allele A*80:01, features a modification of the amino acid from G to S at position 231.
+The protein's natural variant, known as in allele A*68:01; impairs binding to CD8A and reduces recognition by antigen-specific CD8-positive T cells, features a modification of the amino acid from A to V at position 269.
+The protein's natural variant, known as in allele A*25:01, allele A*26:01, allele A*29:02, allele A*31:01, allele A*32:01, allele A*33:01, allele A*34:01, allele A*43:01, allele A*66:01 and allele A*74:01, features a modification of the amino acid from A to S at position 270.
+The protein's natural variant, known as in allele A*80:01, features a modification of the amino acid from E to K at position 277.
+The protein's natural variant, known as in allele A*02:01, allele A*02:05, allele A*25:01, allele A*26:01, allele A*29:02, allele A*31:01, allele A*32:01, allele A*33:01, allele A*34:01, allele A*43:01, allele A*66:01, allele A*68:01, allele A*69:01 and allele A*74:01, features a modification of the amino acid from E to Q at position 277.
+The protein's natural variant, known as in allele A*80:01, features a modification of the amino acid from Q to K at position 279.
+The protein's natural variant, known as in allele A*80:01, features a modification of the amino acid from K to E at position 292.
+The protein's natural variant, known as in allele A*02:01, allele A*02:05, allele A*23:01, allele A*24:02, allele A*25:01, allele A*26:01, allele A*29:02, allele A*31:01, allele A*32:01, allele A*33:01, allele A*34:01, allele A*43:01, allele A*66:01, allele A*68:01, allele A*69:01, allele A*74:01 and allele A*80:01, features a modification of the amino acid from L to P at position 300.
+The protein's natural variant, known as in allele A*23:01 and allele A*24:02, features a modification of the amino acid from I to V at position 306.
+The protein's natural variant, known as in allele A*23:01, features a modification of the amino acid from P to H at position 307.
+The protein's natural variant, known as in allele A*34:01, features a modification of the amino acid from I to L at position 312.
+The protein's natural variant, known as in allele A*02:01, allele A*02:05, allele A*25:01, allele A*26:01, allele A*29:02, allele A*31:01, allele A*32:01, allele A*33:01, allele A*34:01, allele A*43:01, allele A*66:01, allele A*68:01, allele A*69:01 and allele A*74:01, features a modification of the amino acid from L to F at position 318.
+The protein's natural variant, known as in allele A*32:01 and allele A*74:01, features a modification of the amino acid from V to M at position 321.
+The protein's natural variant, known as in allele A*29:02, allele A*31:01, allele A*32:01, allele A*33:01 and allele A*74:01, features a modification of the amino acid from I to F at position 322.
+The protein's natural variant, known as in allele A*25:01, allele A*26:01, allele A*29:02, allele A*31:01, allele A*32:01, allele A*33:01, allele A*34:01, allele A*43:01, allele A*66:01, allele A*74:01 and allele A*80:01, features a modification of the amino acid from T to A at position 323.
+The protein's natural variant, known as in allele A*29:02, allele A*31:01, allele A*32:01, allele A*33:01 and allele A*74:01, features a modification of the amino acid from M to R at position 331.
+The protein's natural variant, known as allele A*80:01, features a modification of the amino acid from R to K at position 334.
+The protein's natural variant, known as in allele A*23:01 and allele A*24:02, features a modification of the amino acid from K to N at position 335.
+The protein's natural variant, known as allele A*80:01, features a modification of the amino acid from D to V at position 338.
+The protein's natural variant, known as in allele A*02:01, allele A*02:05, allele A*23:01, allele A*24:02, allele A*25:01, allele A*26:01, allele A*29:02, allele A*31:01, allele A*32:01, allele A*33:01, allele A*34:01, allele A*43:01, allele A*66:01, allele A*68:01 allele A*69:01, allele A*74:01 and allele A*80:01, features a modification of the amino acid from T to S at position 345.
+The protein's natural variant, known as in allele A*25:01, allele A*26:01, allele A*29:02, allele A*31:01, allele A*32:01, allele A*33:01, allele A*34:01, allele A*43:01, allele A*66:01 and allele A*74:01, features a modification of the amino acid from V to M at position 358.
+The protein's natural variant, known as in allele TNFB*2;, features a modification of the amino acid from T to N at position 60.
+The protein's natural variant, known as in allele 8.1, features a modification of the amino acid from T to P at position 125.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from G to E at position 215.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from G to R at position 557.
+The natural variant of this protein is characterized by an amino acid alteration from C to S at position 272.
+The natural variant of this protein is characterized by an amino acid alteration from H to Q at position 65.
+The natural variant of this protein is characterized by an amino acid alteration from S to T at position 82.
+The natural variant of this protein is characterized by an amino acid alteration from L to I at position 92.
+The natural variant of this protein is characterized by an amino acid alteration from ARN to GRT at position 104.
+The natural variant of this protein is characterized by an amino acid alteration from N to D at position 129.
+The natural variant of this protein is characterized by an amino acid alteration from T to K at position 132.
+The protein's natural variant, known as in PFRD, features a modification of the amino acid from DV to EL at position 146.
+The protein's natural variant, known as does not affect transcriptional activation in response to type I interferon stimulation; does not affect anti-viral immunity;, features a modification of the amino acid from Q to H at position 127.
+The protein's natural variant, known as decreased transcriptional activation in response to type I interferon stimulation;, features a modification of the amino acid from R to C at position 292.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from H to D at position 168.
+The natural variant of this protein is characterized by an amino acid alteration from V to A at position 429.
+The protein's natural variant, known as in VIPB;, features a modification of the amino acid from R to G at position 570.
+The natural variant of this protein is characterized by an amino acid alteration from F to L at position 309.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation, features a modification of the amino acid from S to L at position 430.
+The protein's natural variant, known as in CCDD; the mutation results in decreased protein solubility; causes abnormal aggregation; markedly reduced protein expression is observed in the sarcoplasm and nuclei of patient cardiomyocytes;, features a modification of the amino acid from G to D at position 526.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from R to G at position 629.
+The protein's natural variant, known as in a head & Neck squamous cell carcinoma sample; somatic mutation;, features a modification of the amino acid from M to I at position 798.
+The protein's natural variant, known as in EDAID2;, features a modification of the amino acid from S to I at position 32.
+The protein's natural variant, known as in NEDHIB; mild; unknown pathological significance, features a modification of the amino acid from P to L at position 371.
+The protein's natural variant, known as in NEDHIB; severe; unknown pathological significance; no effect on cell viability, features a modification of the amino acid from I to T at position 457.
+The protein's natural variant, known as in NEDHIB; unknown pathological significance; no effect on cell viability, features a modification of the amino acid from N to S at position 531.
+The protein's natural variant, known as in NEDHIB; profound; decreased cell viability, features a modification of the amino acid from T to M at position 736.
+The protein's natural variant, known as in NEDHIB; severe; unknown pathological significance, features a modification of the amino acid from M to T at position 769.
+The protein's natural variant, known as in NEDHIB; moderate; unknown pathological significance, features a modification of the amino acid from I to T at position 848.
+The protein's natural variant, known as in NEDHIB; moderate; unknown pathological significance, features a modification of the amino acid from Y to H at position 1109.
+The protein's natural variant, known as in NEDHIB; mild; decreased cell viability, features a modification of the amino acid from L to P at position 1124.
+The protein's natural variant, known as in NEDHIB; severe; unknown pathological significance; no effect on cell viability, features a modification of the amino acid from N to S at position 1251.
+The protein's natural variant, known as in NEDHIB; moderate; unknown pathological significance; no effect on cell viability, features a modification of the amino acid from R to H at position 1603.
+The natural variant of this protein is characterized by an amino acid alteration from S to T at position 55.
+The natural variant of this protein is characterized by an amino acid alteration from R to K at position 91.
+The natural variant of this protein is characterized by an amino acid alteration from M to I at position 95.
+The natural variant of this protein is characterized by an amino acid alteration from M to V at position 95.
+The protein's natural variant, known as in strain: Hp921023, features a modification of the amino acid from S to T at position 155.
+The protein's natural variant, known as in NEDGS; unknown pathological significance, features a modification of the amino acid from D to E at position 483.
+The protein's natural variant, known as in NEDGS; unknown pathological significance, features a modification of the amino acid from A to V at position 488.
+The protein's natural variant, known as in NEDGS; unknown pathological significance, features a modification of the amino acid from V to G at position 606.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from S to T at position 381.
+The protein's natural variant, known as in HHF6; diminished sensitivity to GTP, features a modification of the amino acid from S to C at position 270.
+The protein's natural variant, known as in HHF6; diminished sensitivity to GTP;, features a modification of the amino acid from R to C at position 274.
+The protein's natural variant, known as in HHF6;, features a modification of the amino acid from R to K at position 318.
+The protein's natural variant, known as in HHF6; diminished sensitivity to GTP, features a modification of the amino acid from R to T at position 318.
+The protein's natural variant, known as in HHF6;, features a modification of the amino acid from Y to C at position 319.
+The protein's natural variant, known as in HHF6; diminished sensitivity to GTP, features a modification of the amino acid from R to C at position 322.
+The protein's natural variant, known as in HHF6; diminished sensitivity to GTP;, features a modification of the amino acid from R to H at position 322.
+The protein's natural variant, known as in HHF6;, features a modification of the amino acid from E to A at position 349.
+The protein's natural variant, known as in HHF6;, features a modification of the amino acid from S to L at position 498.
+The protein's natural variant, known as in HHF6;, features a modification of the amino acid from G to D at position 499.
+The protein's natural variant, known as in HHF6;, features a modification of the amino acid from G to S at position 499.
+The protein's natural variant, known as in HHF6;, features a modification of the amino acid from S to P at position 501.
+The protein's natural variant, known as in HHF6; abolishes inhibition by ATP; no effect on activation by ADP; Strongly reduces inhibition by GTP;, features a modification of the amino acid from H to Y at position 507.
+The protein's natural variant, known as in strain: YFS, features a modification of the amino acid from Y to N at position 29.
+The protein's natural variant, known as in strain: YFS, features a modification of the amino acid from A to T at position 276.
+The natural variant of this protein is characterized by an amino acid alteration from G to S at position 282.
+The protein's natural variant, known as in strain: KYT, features a modification of the amino acid from S to N at position 291.
+The protein's natural variant, known as in strain: KYT, features a modification of the amino acid from A to G at position 294.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to C at position 481.
+The natural variant of this protein is characterized by an amino acid alteration from C to CCCRPS at position 80.
+The protein's natural variant, known as in HYC3; unknown pathological significance;, features a modification of the amino acid from G to E at position 282.
+The protein's natural variant, known as in CAMRQ2;, features a modification of the amino acid from P to L at position 856.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from L to F at position 81.
+The natural variant of this protein is characterized by an amino acid alteration from T to I at position 81.
+The natural variant of this protein is characterized by an amino acid alteration from S to F at position 114.
+The protein's natural variant, known as in FPCT; insoluble protein;, features a modification of the amino acid from G to E at position 25.
+The protein's natural variant, known as in HEP; mild phenotype; strong decrease of activity;, features a modification of the amino acid from F to L at position 46.
+The protein's natural variant, known as in HEP;, features a modification of the amino acid from P to L at position 62.
+The protein's natural variant, known as in HEP;, features a modification of the amino acid from A to G at position 80.
+The protein's natural variant, known as in FPCT; decrease of activity;, features a modification of the amino acid from A to S at position 80.
+The protein's natural variant, known as in FPCT and HEP; requires 2 nucleotide substitutions; nearly normal activity, features a modification of the amino acid from V to Q at position 134.
+The protein's natural variant, known as in FPCT;, features a modification of the amino acid from R to Q at position 142.
+The protein's natural variant, known as in FPCT; decrease of activity, features a modification of the amino acid from R to P at position 144.
+The protein's natural variant, known as in FPCT; decrease of activity;, features a modification of the amino acid from G to D at position 156.
+The protein's natural variant, known as in FPCT, features a modification of the amino acid from L to Q at position 161.
+The protein's natural variant, known as in FPCT; activity < 2%;, features a modification of the amino acid from M to R at position 165.
+The protein's natural variant, known as in HEP and FPCT; nearly normal activity;, features a modification of the amino acid from E to K at position 167.
+The protein's natural variant, known as in HEP; relative activity of 65% of wild-type towards uroporphyrinogen III, features a modification of the amino acid from G to R at position 168.
+The protein's natural variant, known as in HEP; relative activity of 17% and 60% of wild-type towards uroporphyrinogen I and III respectively, features a modification of the amino acid from G to D at position 170.
+The protein's natural variant, known as in FPCT; insoluble protein;, features a modification of the amino acid from R to P at position 193.
+The protein's natural variant, known as in FPCT;, features a modification of the amino acid from L to F at position 195.
+The protein's natural variant, known as in FPCT, features a modification of the amino acid from L to Q at position 216.
+The protein's natural variant, known as in FPCT; significant decrease of activity, features a modification of the amino acid from E to K at position 218.
+The protein's natural variant, known as in FPCT;, features a modification of the amino acid from S to F at position 219.
+The protein's natural variant, known as in HEP; mild form, features a modification of the amino acid from H to P at position 220.
+The protein's natural variant, known as in FPCT, features a modification of the amino acid from F to L at position 229.
+The protein's natural variant, known as in FPCT; decrease of activity, features a modification of the amino acid from F to L at position 232.
+The protein's natural variant, known as in FPCT;, features a modification of the amino acid from P to S at position 235.
+The protein's natural variant, known as in FPCT; decrease of activity;, features a modification of the amino acid from L to Q at position 253.
+The protein's natural variant, known as in FPCT; decrease of activity;, features a modification of the amino acid from I to T at position 260.
+The protein's natural variant, known as in FPCT and HEP;, features a modification of the amino acid from G to E at position 281.
+The protein's natural variant, known as in FPCT;, features a modification of the amino acid from G to V at position 281.
+The protein's natural variant, known as in FPCT, features a modification of the amino acid from L to R at position 282.
+The protein's natural variant, known as in HEP;, features a modification of the amino acid from R to G at position 292.
+The protein's natural variant, known as in FPCT;, features a modification of the amino acid from G to S at position 303.
+The protein's natural variant, known as in FPCT;, features a modification of the amino acid from N to K at position 304.
+The protein's natural variant, known as in HEP;, features a modification of the amino acid from Y to C at position 311.
+The protein's natural variant, known as in FPCT;, features a modification of the amino acid from G to R at position 318.
+The protein's natural variant, known as in FPCT;, features a modification of the amino acid from M to T at position 324.
+The protein's natural variant, known as in FPCT;, features a modification of the amino acid from R to H at position 332.
+The protein's natural variant, known as in FPCT, features a modification of the amino acid from I to T at position 334.
+The protein's natural variant, known as in DEE72;, features a modification of the amino acid from E to Q at position 130.
+The protein's natural variant, known as in DEE72;, features a modification of the amino acid from M to T at position 134.
+The protein's natural variant, known as in GKAF; unknown pathological significance; homozygous patient fibroblasts have impaired ability to progress through the cell cycle; decreased protein abundance in patient fibroblasts, features a modification of the amino acid from I to T at position 196.
+The protein's natural variant, known as in allele CYP5A1*2;, features a modification of the amino acid from R to H at position 60.
+The protein's natural variant, known as in GHDD;, features a modification of the amino acid from L to P at position 82.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from R to W at position 85.
+The protein's natural variant, known as in allele CYP5A1*3;, features a modification of the amino acid from D to E at position 160.
+The protein's natural variant, known as in allele CYP5A1*4;, features a modification of the amino acid from N to S at position 245.
+The protein's natural variant, known as the KM value is about 1.5 higher for PEG2; in allele CYP5A1*5; KM value about 1.5 higher for PEG2; Vmax/KM approximately 50% of that of the wild-type;, features a modification of the amino acid from K to E at position 257.
+The protein's natural variant, known as in allele CYP5A1*5; KM value about 1.5 higher for PEG2; Vmax/KM approximately 27% of that of the wild-type;, features a modification of the amino acid from L to V at position 356.
+The protein's natural variant, known as in GHDD;, features a modification of the amino acid from R to Q at position 412.
+The protein's natural variant, known as in allele CYP5A1*6; does not affect KM value for PEG2; does not affect Vmax/KM value;, features a modification of the amino acid from Q to E at position 416.
+The protein's natural variant, known as in allele CYP5A1*7; does not affect KM value for PEG2; does not affect Vmax/KM value;, features a modification of the amino acid from E to K at position 449.
+The protein's natural variant, known as in allele CYP5A1*8; KM value about 1.5 higher for PEG2; Vmax/KM approximately 56 % of that of the wild-type;, features a modification of the amino acid from T to N at position 450.
+The protein's natural variant, known as in allele CYP5A1*9;, features a modification of the amino acid from R to Q at position 465.
+The protein's natural variant, known as in GHDD;, features a modification of the amino acid from G to W at position 481.
+The protein's natural variant, known as in GHDD;, features a modification of the amino acid from L to P at position 487.
+The protein's natural variant, known as in a breast cancer sample;, features a modification of the amino acid from S to N at position 1055.
+The protein's natural variant, known as in a breast cancer sample;, features a modification of the amino acid from E to D at position 1533.
+The protein's natural variant, known as in SCKL9; abolished localization to the nucleolus;, features a modification of the amino acid from R to C at position 18.
+The protein's natural variant, known as in allele CYP2C8*3; reduces enzymatic activity with paclitaxel as substrate; decreases intrinsic clearance of paclitaxel; reduces enzymatic activity with amodiaquine as substrate;, features a modification of the amino acid from R to K at position 139.
+The natural variant of this protein is characterized by an amino acid alteration from E to D at position 154.
+The protein's natural variant, known as in allele CYP2C8*6; no effect on affinity or enzymatic activity with paclitaxel as substrate; decreases affinity for amodiaquine; reduces enzymatic activity with amodiaquine as substrate; decreases intrinsic clearance of amodiaquine;, features a modification of the amino acid from G to S at position 171.
+The protein's natural variant, known as in allele CYP2C8*8; increases affinity for paclitaxel; reduces enzymatic activity with paclitaxel as substrate; decreases intrinsic clearance of paclitaxel; reduces enzymatic activity with amodiaquine as substrate; decreases intrinsic clearance of amodiaquine;, features a modification of the amino acid from R to G at position 186.
+The natural variant of this protein is characterized by an amino acid alteration from N to K at position 193.
+The protein's natural variant, known as in allele CYP2C8*13; reduces enzymatic activity with paclitaxel as substrate; decreases intrinsic clearance of paclitaxel; reduces enzymatic activity with amodiaquine as substrate; decreases intrinsic clearance of amodiaquine, features a modification of the amino acid from I to M at position 223.
+The protein's natural variant, known as in allele CYP2C8*14; reduces enzymatic activity with paclitaxel as substrate; decreases intrinsic clearance of paclitaxel;, features a modification of the amino acid from A to P at position 238.
+The protein's natural variant, known as in allele CYP2C8*9; increases enzymatic activity with paclitaxel as substrate; reduces enzymatic activity with amodiaquine as substrate; decreases intrinsic clearance of amodiaquine;, features a modification of the amino acid from K to R at position 247.
+The natural variant of this protein is characterized by an amino acid alteration from K to R at position 249.
+The protein's natural variant, known as in allele CYP2C8*4; reduces enzymatic activity with paclitaxel as substrate; decreases affinity for amodiaquine;, features a modification of the amino acid from I to M at position 264.
+The protein's natural variant, known as in allele CYP2C8*2; only found in African-Americans; increases intrinsic clearance of paclitaxel; decreases affinity for amodiaquine; increases enzymatic activity with amodiaquine as substrate;, features a modification of the amino acid from I to F at position 269.
+The protein's natural variant, known as in allele CYP2C8*10; reduces enzymatic activity with paclitaxel as substrate; reduces enzymatic activity with amodiaquine as substrate; decreases intrinsic clearance of amodiaquine, features a modification of the amino acid from K to N at position 383.
+The protein's natural variant, known as in allele CYP2C8*3; reduces enzymatic activity with paclitaxel as substrate; decreases intrinsic clearance of paclitaxel; reduces enzymatic activity with amodiaquine as substrate;, features a modification of the amino acid from K to R at position 399.
+The natural variant of this protein is characterized by an amino acid alteration from H to L at position 411.
+The protein's natural variant, known as in ECTD4;, features a modification of the amino acid from R to H at position 78.
+The protein's natural variant, known as found in a patient with intellectual disability; unknown pathological significance;, features a modification of the amino acid from P to H at position 28.
+The protein's natural variant, known as in 50% of the molecules, features a modification of the amino acid from M to A at position 24.
+The protein's natural variant, known as in 25% of the molecules, features a modification of the amino acid from E to K at position 50.
+The protein's natural variant, known as in Hol l 1.0102, features a modification of the amino acid from T to S at position 103.
+The natural variant of this protein is characterized by an amino acid alteration from Y to H at position 118.
+The natural variant of this protein is characterized by an amino acid alteration from V to A at position 422.
+The natural variant of this protein is characterized by an amino acid alteration from S to F at position 242.
+The protein's natural variant, known as in MRD48; decreased substrate adhesion-dependent cell spreading; dominant-negative effect; reduced neuronal proliferation;, features a modification of the amino acid from C to Y at position 18.
+The protein's natural variant, known as in MRD48; decreased substrate adhesion-dependent cell spreading; dominant-negative effect; reduced neuronal proliferation;, features a modification of the amino acid from N to S at position 39.
+The protein's natural variant, known as in MRD48; unknown pathological significance;, features a modification of the amino acid from V to L at position 51.
+The protein's natural variant, known as in MRD48; decreased substrate adhesion-dependent cell spreading; weak dominant-negative effect;, features a modification of the amino acid from V to M at position 51.
+The protein's natural variant, known as in MRD48; increased substrate adhesion-dependent cell spreading; constitutively active;, features a modification of the amino acid from Y to D at position 64.
+The protein's natural variant, known as in MRD48; decreased substrate adhesion-dependent cell spreading; weak dominant-negative effect, features a modification of the amino acid from P to L at position 73.
+The protein's natural variant, known as in MRD48; decreased substrate adhesion-dependent cell spreading; weak dominant-negative effect;, features a modification of the amino acid from C to Y at position 157.
+The protein's natural variant, known as in ARCL2B;, features a modification of the amino acid from R to G at position 119.
+The protein's natural variant, known as in ARCL2B;, features a modification of the amino acid from R to H at position 119.
+The protein's natural variant, known as in ARCL2B;, features a modification of the amino acid from A to T at position 179.
+The natural variant of this protein is characterized by an amino acid alteration from A to V at position 189.
+The protein's natural variant, known as in ARCL2B;, features a modification of the amino acid from G to R at position 206.
+The protein's natural variant, known as in ARCL2B;, features a modification of the amino acid from G to W at position 206.
+The protein's natural variant, known as in ARCL3B; results in a reduction of protein expression in skin fibroblasts from the patient;, features a modification of the amino acid from G to E at position 248.
+The protein's natural variant, known as in ARCL3B;, features a modification of the amino acid from R to H at position 251.
+The protein's natural variant, known as in ARCL3B;, features a modification of the amino acid from A to T at position 257.
+The protein's natural variant, known as in ARCL2B; may cause skipping of exon 6;, features a modification of the amino acid from R to Q at position 266.
+The natural variant of this protein is characterized by an amino acid alteration from G to R at position 297.
+The protein's natural variant, known as in strain: ZBMEL377, features a modification of the amino acid from A to P at position 16.
+The protein's natural variant, known as in strain: ZBMEL84, ZBMEL95, ZBMEL131 and ZBMEL157, features a modification of the amino acid from T to K at position 298.
+The protein's natural variant, known as in HH8; absence of inositol phosphate accumulation under kisspeptin challenge; normal affinity for kisspeptin;, features a modification of the amino acid from L to P at position 102.
+The protein's natural variant, known as in HH8; 65% reduction of inositol phosphate production;, features a modification of the amino acid from L to S at position 148.
+The protein's natural variant, known as in HH8; phenotype consistent with normosmic idiopathic hypogonadotropic hypogonadism; benign variant; the patient also carries a mutation in FGFR1;, features a modification of the amino acid from A to T at position 189.
+The protein's natural variant, known as in HH8; phenotype consistent with Kallmann syndrome; the patient also carries a mutation in IL17RD;, features a modification of the amino acid from A to D at position 194.
+The protein's natural variant, known as in HH8; exhibit profoundly impaired signaling, features a modification of the amino acid from C to R at position 223.
+The protein's natural variant, known as in HH8;, features a modification of the amino acid from S to L at position 262.
+The protein's natural variant, known as in HH8; mild reduction in ligand-stimulated activity across the ligand dose range;, features a modification of the amino acid from R to L at position 297.
+The protein's natural variant, known as in CPPB1; reduced rate of decline in inositol phosphate accumulation after kisspeptin stimulation; prolonged phosphorylation of ERK;, features a modification of the amino acid from R to P at position 386.
+The protein's natural variant, known as in strain: Isolate Macedonia, features a modification of the amino acid from T to A at position 23.
+The protein's natural variant, known as in strain: Isolate Macedonia, features a modification of the amino acid from V to I at position 156.
+The protein's natural variant, known as in strain: Isolate Macedonia, features a modification of the amino acid from M to A at position 215.
+The protein's natural variant, known as in strain: Isolate Macedonia, features a modification of the amino acid from T to M at position 234.
+The protein's natural variant, known as in strain: Isolate Macedonia, features a modification of the amino acid from V to M at position 372.
+The protein's natural variant, known as in strain: AF1, AF2, AF3, AF4, K11, K14, K16, K2, K21, K3, K5, K7, ZH1, ZH13, ZH16, ZH19, ZH2, ZH20, ZH21, ZH23, ZH25, ZH29, ZH31 and ZH33, features a modification of the amino acid from T to S at position 67.
+The protein's natural variant, known as in strain: ZH20, features a modification of the amino acid from D to V at position 71.
+The protein's natural variant, known as in strain: wi3, features a modification of the amino acid from Q to L at position 97.
+The protein's natural variant, known as in strain: AF1, AF2, AF3, AF4, K11, K14, K16, K2, K21, K3, K5, K7, ZH1, ZH13, ZH16, ZH19, ZH2, ZH20, ZH21, ZH23, ZH25, ZH29, ZH31 and ZH33, features a modification of the amino acid from T to A at position 107.
+The protein's natural variant, known as in DEE17 and NEDIM;, features a modification of the amino acid from G to R at position 40.
+The protein's natural variant, known as probable disease-associated variant found in a patient with intractable early-onset epilepsy, features a modification of the amino acid from G to W at position 40.
+The protein's natural variant, known as in NEDIM, features a modification of the amino acid from S to G at position 47.
+The protein's natural variant, known as probable disease-associated variant found in a patient with intractable early-onset epilepsy; loss of GTP binding; decreased interaction with RGS19; decreased interaction with heterodimers formed by GNB1 and GNG3; strongly decreased localization to cell membrane, features a modification of the amino acid from Q to P at position 52.
+The protein's natural variant, known as in DEE17; loss of GTP binding; decreased interaction with RGS19; decreased interaction with heterodimers formed by GNB1 and GNG3; strongly decreased localization to cell membrane, features a modification of the amino acid from Q to R at position 52.
+The protein's natural variant, known as in NEDIM, features a modification of the amino acid from I to T at position 56.
+The protein's natural variant, known as in DEE17; somatic mosaic mutation; the mutant protein has some abnormal cytoplasmic localization;, features a modification of the amino acid from D to G at position 174.
+The protein's natural variant, known as in DEE17; the mutant protein localizes normally to the cell periphery;, features a modification of the amino acid from G to R at position 203.
+The protein's natural variant, known as in DEE17 and NEDIM;, features a modification of the amino acid from R to C at position 209.
+The protein's natural variant, known as in NEDIM;, features a modification of the amino acid from R to G at position 209.
+The protein's natural variant, known as in NEDIM;, features a modification of the amino acid from R to H at position 209.
+The protein's natural variant, known as in NEDIM, features a modification of the amino acid from R to L at position 209.
+The protein's natural variant, known as in NEDIM;, features a modification of the amino acid from A to V at position 227.
+The protein's natural variant, known as in NEDIM;, features a modification of the amino acid from E to G at position 246.
+The protein's natural variant, known as in NEDIM;, features a modification of the amino acid from E to K at position 246.
+The protein's natural variant, known as in DEE17; the mutant protein has some abnormal cytoplasmic localization;, features a modification of the amino acid from I to N at position 279.
+The protein's natural variant, known as in OI17; decreased secretion of the protein; altered secretion of procollagen type I;, features a modification of the amino acid from R to H at position 166.
+The protein's natural variant, known as in OI17; no effect on expression and secretion of the protein; altered secretion of procollagen type I;, features a modification of the amino acid from E to K at position 263.
+The protein's natural variant, known as in CTRCT46;, features a modification of the amino acid from L to R at position 13.
+The protein's natural variant, known as in MARUPS, features a modification of the amino acid from S to F at position 479.
+The protein's natural variant, known as in strain: LO4, features a modification of the amino acid from NS to DP at position 180.
+The protein's natural variant, known as in strain: LO4, features a modification of the amino acid from D to N at position 195.
+The protein's natural variant, known as in strain: LO4, features a modification of the amino acid from A to V at position 330.
+The protein's natural variant, known as in strain: LO4, features a modification of the amino acid from V to A at position 381.
+The protein's natural variant, known as in strain: LO4, features a modification of the amino acid from Q to P at position 405.
+The protein's natural variant, known as in strain: LO4, features a modification of the amino acid from F to Y at position 427.
+The protein's natural variant, known as may be a predisposing factor for congenital dwarfism, features a modification of the amino acid from F to L at position 81.
+The protein's natural variant, known as in XLID105;, features a modification of the amino acid from Y to H at position 381.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from C to Y at position 23.
+The protein's natural variant, known as in a lung adenocarcinoma patient, features a modification of the amino acid from V to F at position 167.
+The protein's natural variant, known as in a NSCLC cell line, features a modification of the amino acid from D to H at position 236.
+The protein's natural variant, known as in a lung adenocarcinoma patient, features a modification of the amino acid from Q to L at position 284.
+The protein's natural variant, known as in a NSCLC cell line; strongly reduces interaction with NFE2L2/NRF2 and reduces repression of NFE2L2/NRF2-dependent gene expression, features a modification of the amino acid from G to C at position 333.
+The protein's natural variant, known as in a NSCLC cell line;, features a modification of the amino acid from G to S at position 350.
+The protein's natural variant, known as in a lung adenocarcinoma cell line; also in NSCLC cell lines; strongly reduces interaction with NFE2L2/NRF2 and reduces repression of NFE2L2/NRF2-dependent gene expression;, features a modification of the amino acid from G to C at position 364.
+The protein's natural variant, known as in a lung adenocarcinoma patient; somatic mutation; strongly reduces interaction with NFE2L2/NRF2 and reduces repression of NFE2L2/NRF2-dependent gene expression, features a modification of the amino acid from G to C at position 430.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from A to V at position 522.
+The protein's natural variant, known as in Eur m 2 0102, features a modification of the amino acid from I to V at position 21.
+The protein's natural variant, known as in SPGF37;, features a modification of the amino acid from Y to C at position 114.
+The protein's natural variant, known as in CRS2; gain of function;, features a modification of the amino acid from P to H at position 148.
+The protein's natural variant, known as in CRS2;, features a modification of the amino acid from P to L at position 148.
+The protein's natural variant, known as in PFM1, features a modification of the amino acid from L to P at position 154.
+The protein's natural variant, known as in PFM1; loss of function;, features a modification of the amino acid from R to H at position 172.
+The protein's natural variant, known as in CMT2D; shows a reduction in aminoacylation activity;, features a modification of the amino acid from A to V at position 111.
+The protein's natural variant, known as in CMT2D; phenotype overlapping with HMN5A; complements the defect of the wild-type gene in yeast; contrary to the wild-type protein, strongly binds to NRP1 and competes with VEGFA for NRP1-binding; displays slightly elevated aminoacylation activity over wild-type;, features a modification of the amino acid from E to G at position 125.
+The protein's natural variant, known as in HMN5A; does not complement the defect of the wild-type gene in yeast; contrary to the wild-type protein, strongly interacts with NRP1;, features a modification of the amino acid from L to P at position 183.
+The protein's natural variant, known as in CMT2D and HMN5A; shows a large reduction in aminoacylation activity;, features a modification of the amino acid from D to N at position 200.
+The protein's natural variant, known as in CMT2D, features a modification of the amino acid from D to Y at position 200.
+The protein's natural variant, known as in CMT2D and HMN5A; shows a large reduction in aminoacylation activity; demonstrates a change in the subcellular location pattern; does not associate with granules;, features a modification of the amino acid from S to F at position 265.
+The protein's natural variant, known as in CMT2D; unknown pathological significance, features a modification of the amino acid from S to Y at position 265.
+The protein's natural variant, known as found in a patient with mild left ventricular posterior wall hypertrophy, exercise intolerance and lactic acidosis; unknown pathological significance;, features a modification of the amino acid from T to I at position 268.
+The protein's natural variant, known as in CMT2D;, features a modification of the amino acid from M to R at position 292.
+The protein's natural variant, known as in CMT2D; shows a large reduction in aminoacylation activity; does not impair transcription or translation or protein stability; contrary to the wild-type protein, strongly interacts with NRP1;, features a modification of the amino acid from G to R at position 294.
+The protein's natural variant, known as in CMT2D; shows a large reduction in aminoacylation activity; demonstrates a change in subcellular location pattern; does not associate with granules;, features a modification of the amino acid from P to L at position 298.
+The protein's natural variant, known as probable disease-associated variant found in a patient with growth retardation, microcephaly, thinning of the corpus callosum, decreased white matter and brain stem involvement, as well as large calvaria, cerebellar vermis atrophy, dysmorphic features, prominent epicanthal folds, hypotelorism, high-arched palate, delayed motor milestones, apnea and sparse thin scalp hair; reduces to less than 1% aminoacylation activity;, features a modification of the amino acid from R to Q at position 310.
+The protein's natural variant, known as in CMT2D; shows a large reduction in aminoacylation activity; demonstrates a change in subcellular location pattern; does not associate with granules; unknown pathological significance;, features a modification of the amino acid from I to F at position 334.
+The protein's natural variant, known as in SMAJI; loss of function; based on yeast complementation assay;, features a modification of the amino acid from I to N at position 334.
+The protein's natural variant, known as found in a patient with mild left ventricular posterior wall hypertrophy, exercise intolerance and lactic acidosis; unknown pathological significance;, features a modification of the amino acid from R to C at position 412.
+The protein's natural variant, known as in HMN5A; shows a large reduction in aminoacylation activity; does not complement the defect of the wild-type gene in yeast;, features a modification of the amino acid from H to R at position 472.
+The protein's natural variant, known as in CMT2D; demonstrates no change in subcellular location pattern;, features a modification of the amino acid from D to N at position 554.
+The protein's natural variant, known as in HMN5A; higher dimerization stability; loss of activity; shows a large reduction in aminoacylation activity;, features a modification of the amino acid from G to R at position 580.
+The protein's natural variant, known as in HMN5A; unknown pathological significance;, features a modification of the amino acid from G to A at position 598.
+The protein's natural variant, known as has no effect on subcellular localization; results in decreased affinity for glycine;, features a modification of the amino acid from S to L at position 635.
+The protein's natural variant, known as in CMT2D; shows a large reduction in aminoacylation activity; demonstrates a change in subcellular location pattern; does not associate with granules;, features a modification of the amino acid from G to A at position 652.
+The protein's natural variant, known as in SMAJI;, features a modification of the amino acid from G to R at position 652.
+The protein's natural variant, known as in strain: NA-1508/92, features a modification of the amino acid from L to F at position 8.
+The protein's natural variant, known as in strain: NA-1064/97, features a modification of the amino acid from V to I at position 9.
+The protein's natural variant, known as in strain: NA-1064/97, NA-1383/97 and NA-1508/92, features a modification of the amino acid from A to V at position 14.
+The protein's natural variant, known as in strain: NA-1064/97 and NA-1383/97, features a modification of the amino acid from I to A at position 16.
+The protein's natural variant, known as in strain: NA-1508/92, features a modification of the amino acid from I to V at position 16.
+The protein's natural variant, known as in strain: NA-1064/97, NA-1383/97 and NA-1508/92, features a modification of the amino acid from TT to AA at position 28.
+The protein's natural variant, known as in strain: NA-1064/97, features a modification of the amino acid from G to S at position 30.
+The protein's natural variant, known as in strain: NA-1383/97, features a modification of the amino acid from I to V at position 62.
+The protein's natural variant, known as in strain: NA-1383/97, features a modification of the amino acid from E to Q at position 81.
+The protein's natural variant, known as in strain: TIGR4, features a modification of the amino acid from D to N at position 83.
+The protein's natural variant, known as in strain: NA-1064/97, NA-1383/97 and NA-1508/92, features a modification of the amino acid from D to E at position 120.
+The protein's natural variant, known as in strain: NA-1064/97 and NA-1508/92, features a modification of the amino acid from Q to K at position 130.
+The protein's natural variant, known as in strain: NA-1383/97, features a modification of the amino acid from I to M at position 148.
+The protein's natural variant, known as in strain: NA-1383/97, features a modification of the amino acid from N to S at position 164.
+The protein's natural variant, known as in strain: NA-1383/97, features a modification of the amino acid from SKD to AKE at position 189.
+The protein's natural variant, known as in strain: NA-1064/97, NA-1383/97 and NA-1508/92, features a modification of the amino acid from K to N at position 193.
+The protein's natural variant, known as in strain: NA-1383/97, features a modification of the amino acid from A to C at position 207.
+The protein's natural variant, known as in strain: NA-1383/97, features a modification of the amino acid from E to D at position 234.
+The protein's natural variant, known as in strain: NA-1383/97, features a modification of the amino acid from V to T at position 248.
+The protein's natural variant, known as in strain: NA-1508/92, features a modification of the amino acid from Q to E at position 285.
+The protein's natural variant, known as in strain: NA-1383/97, features a modification of the amino acid from S to N at position 294.
+The protein's natural variant, known as in non-small cell lung cancer cell lines, features a modification of the amino acid from R to S at position 145.
+The protein's natural variant, known as in non-small cell lung cancer cell lines;, features a modification of the amino acid from T to S at position 207.
+The protein's natural variant, known as in allele D4.7, features a modification of the amino acid from S to GLPPDPCGPDCAPPAPGLPQDPCGPDCAPPAPGLPRGPCGPDCAPPAPG at position 284.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 20.
+The protein's natural variant, known as in strain: Isolate Bba1, features a modification of the amino acid from L to V at position 328.
+The protein's natural variant, known as in strain: Isolate Australia, features a modification of the amino acid from D to N at position 16.
+The protein's natural variant, known as in strain: Isolate Australia, features a modification of the amino acid from N to S at position 26.
+The protein's natural variant, known as in strain: Isolate Australia, features a modification of the amino acid from T to M at position 43.
+The protein's natural variant, known as in strain: Isolate Australia, features a modification of the amino acid from I to T at position 194.
+The protein's natural variant, known as in strain: Isolate Australia, features a modification of the amino acid from S to G at position 340.
+The natural variant of this protein is characterized by an amino acid alteration from S to F at position 327.
+The protein's natural variant, known as associated with susceptibility to lumbar disk disease in Japanese; increases binding and inhibition of TGFB1;, features a modification of the amino acid from I to T at position 395.
+The natural variant of this protein is characterized by an amino acid alteration from M to K at position 22.
+The natural variant of this protein is characterized by an amino acid alteration from D to G at position 33.
+The protein's natural variant, known as in strain: cv. Chi-1, cv. Wassilewskija, features a modification of the amino acid from L to S at position 80.
+The protein's natural variant, known as in strain: cv. An-2, cv. Bla-1, cv. Bs-1, cv. Bu-0, cv. Chi-1, cv. Co-1, cv. Cvi-0, cv. El-0, cv. Gr-3, cv. Ita-0, cv. Jl-3, cv. Kas-1, cv. Landsberg erecta, cv. Lisse-2, cv. Lu-1, cv. Pi-0, cv. Sf-1, cv. Wassilewskija, features a modification of the amino acid from S to G at position 87.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from S to C at position 110.
+The protein's natural variant, known as in strain: cv. An-2, cv. Bla-1, cv. Bs-1, cv. Chi-1, cv. Cvi-0, cv. Lisse-2, cv. Sf-1, cv. Wassilewskija, features a modification of the amino acid from T to I at position 125.
+The protein's natural variant, known as in strain: cv. Bu-0, cv. Co-1, cv. El-0, cv. Gr-3, cv. Jl-3, cv. Kas-1, cv. Landsberg erecta, cv. Lu-1, cv. Pi-0, features a modification of the amino acid from V to I at position 134.
+The protein's natural variant, known as in strain: cv. Bu-0, cv. Co-1, cv. El-0, cv. Gr-3, cv. Jl-3, cv. Kas-1, cv. Landsberg erecta, cv. Lu-1, cv. Pi-0, features a modification of the amino acid from ATFV to PTFM at position 142.
+The protein's natural variant, known as in strain: cv. An-2, features a modification of the amino acid from A to T at position 139.
+The protein's natural variant, known as in strain: cv. Bu-0, cv. Co-1, cv. El-0, cv. Gr-3, cv. Jl-3, cv. Kas-1, cv. Landsberg erecta, cv. Lu-1, cv. Pi-0, features a modification of the amino acid from R to G at position 148.
+The protein's natural variant, known as in strain: cv. Bu-0, cv. Co-1, cv. El-0, cv. Gr-3, cv. Jl-3, cv. Kas-1, cv. Landsberg erecta, cv. Lu-1, cv. Pi-0, features a modification of the amino acid from D to N at position 157.
+The protein's natural variant, known as in strain: cv. An-2, cv. Bla-1, cv. Bs-1, cv. Chi-1, cv. Cvi-0, cv. Lisse-2, cv. Sf-1, cv. Wassilewskija, features a modification of the amino acid from V to I at position 162.
+The protein's natural variant, known as in strain: cv. An-2, cv. Bla-1, cv. Bs-1, cv. Bu-0, cv. Chi-1, cv. Co-1, cv. Cvi-0, cv. El-0, cv. Gr-3, cv. Ita-0, cv. Jl-3, cv. Kas-1, cv. Landsberg erecta, cv. Lisse-2, cv. Lu-1, cv. Pi-0, cv. Sf-1, cv. Wassilewskija, features a modification of the amino acid from N to D at position 168.
+The protein's natural variant, known as in strain: cv. An-2, cv. Bla-1, cv. Bs-1, cv. Chi-1, cv. Cvi-0, cv. Lisse-2, cv. Sf-1, cv. Wassilewskija, features a modification of the amino acid from F to I at position 178.
+The protein's natural variant, known as in strain: cv. Bu-0, cv. Co-1, cv. El-0, cv. Gr-3, cv. Ita-0, cv. Jl-3, cv. Kas-1, cv. Landsberg erecta, cv. Lu-1, cv. Pi-0, features a modification of the amino acid from F to L at position 178.
+The protein's natural variant, known as in strain: cv. Ita-0, features a modification of the amino acid from M to I at position 207.
+The protein's natural variant, known as in strain: cv. Bu-0, cv. Co-1, cv. El-0, cv. Gr-3, cv. Ita-0, cv. Jl-3, cv. Kas-1, cv. Landsberg erecta, cv. Lu-1, cv. Pi-0, features a modification of the amino acid from Q to R at position 227.
+The protein's natural variant, known as in strain: cv. Bu-0, cv. Co-1, cv. El-0, cv. Gr-3, cv. Ita-0, cv. Jl-3, cv. Kas-1, cv. Landsberg erecta, cv. Lu-1, cv. Pi-0, features a modification of the amino acid from ILNI to VLNL at position 247.
+The protein's natural variant, known as in strain: cv. Ita-0, features a modification of the amino acid from K to T at position 264.
+The protein's natural variant, known as in strain: cv. Bu-0, cv. Co-1, cv. El-0, cv. Gr-3, cv. Jl-3, cv. Kas-1, cv. Landsberg erecta, cv. Lu-1, cv. Pi-0, features a modification of the amino acid from M to V at position 285.
+The protein's natural variant, known as in strain: cv. Ita-0, features a modification of the amino acid from R to C at position 303.
+The protein's natural variant, known as in strain: cv. Bu-0, cv. Co-1, cv. El-0, cv. Gr-3, cv. Jl-3, cv. Kas-1, cv. Landsberg erecta, cv. Lu-1, cv. Pi-0, features a modification of the amino acid from A to S at position 374.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from K to R at position 572.
+The protein's natural variant, known as in strain: cv. Wassilewskija, features a modification of the amino acid from A to T at position 649.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to Q at position 137.
+The protein's natural variant, known as found in a sporadic case of total anomalous pulmonary venous return; unknown pathological significance;, features a modification of the amino acid from T to M at position 116.
+The protein's natural variant, known as in strain: Ba194, CECT 10233, M5-7A, M5-7B, M7-8D, MMR2-1, MMR2-3, MMW1-12, ORM1-1, Sgu52E, Y-9, YPS396, YPS400, YPS598, YPS600, YPS602, YPS604, YPS606, YPS608 and YPS610, features a modification of the amino acid from M to V at position 19.
+The protein's natural variant, known as in strain: ATCC 76625 / YPH499, Ba194, Bb32, M1-2A, M2-8, M5-7A, M5-7B, M7-8D, MMR2-1, MMR2-3, MMR2-5, MMW1-15, MMW1-15h2, MMW1-2, MMW1-2h2, MMW1-12, ORM1-1, S288c/ YPH1, Sgu52E, Sgu52F, Y-9, YPS396, YPS400, YPS598, YPS600, YPS602, YPS604, YPS606, YPS608 and YPS610, features a modification of the amino acid from A to T at position 52.
+The protein's natural variant, known as in strain: Ba194, Bb32, M1-2A, M2-8, M5-7A, M5-7B, M7-8D, MMR2-5, MMW1-15h2, MMW1-2h2, Sgu52E, Sgu52F and Y-9, features a modification of the amino acid from N to S at position 90.
+The protein's natural variant, known as in strain: Bb32, M1-2A, M2-8, MMR2-5, MMW1-15h2, MMW1-2h2 and Sgu52F, features a modification of the amino acid from A to S at position 122.
+The protein's natural variant, known as in strain: Ba194, Bb32, M1-2A, M2-8, M5-7A, M5-7B, M7-8D, MMR2-1, MMR2-3, MMR2-5, MMW1-12, MMW1-15h2, MMW1-2h2, ORM1-1, Sgu52E, Sgu52F, Y-9, YPS396, YPS400, YPS598, YPS600, YPS602, YPS604, YPS606, YPS608 and YPS610, features a modification of the amino acid from P to S at position 157.
+The protein's natural variant, known as in strain: Bb32, M1-2A, M2-8, MMR2-5, MMW1-15h2, MMW1-2h2 and Sgu52F, features a modification of the amino acid from Y to H at position 164.
+The protein's natural variant, known as in strain: ATCC 76625 / YPH499,MMW1-15, MMW1-2 and S288c / YPH1, features a modification of the amino acid from A to T at position 191.
+The protein's natural variant, known as in strain: Sgu52F, features a modification of the amino acid from G to E at position 344.
+The protein's natural variant, known as in strain: ATCC 76625 / YPH499, MMW1-15 and MMW1-2, features a modification of the amino acid from K to R at position 345.
+The protein's natural variant, known as in strain: NMB, HF130 and P63, features a modification of the amino acid from I to V at position 302.
+The protein's natural variant, known as in BARTS3;, features a modification of the amino acid from P to L at position 124.
+The protein's natural variant, known as in BARTS3;, features a modification of the amino acid from A to T at position 204.
+The protein's natural variant, known as in BARTS3;, features a modification of the amino acid from A to D at position 349.
+The protein's natural variant, known as in BARTS3;, features a modification of the amino acid from Y to H at position 432.
+The protein's natural variant, known as in BARTS3;, features a modification of the amino acid from R to C at position 438.
+The protein's natural variant, known as in strain: cv. Hiroshima, features a modification of the amino acid from F to Y at position 43.
+The protein's natural variant, known as in strain: cv. Bla-10, cv. Ci-0, cv. Cvi-0, cv. Hiroshima, cv. Kas-1 and cv. Ita-0, features a modification of the amino acid from V to L at position 51.
+The protein's natural variant, known as in strain: cv. Aa-0, cv. Al-0, cv. Bl-1, cv. Bs-0, cv. Gr-1, cv. Mt-0, cv. Shokei and cv. Yo-0, features a modification of the amino acid from E to D at position 101.
+The protein's natural variant, known as in strain: cv. Bl-1 and cv. Gr-1, features a modification of the amino acid from H to K at position 106.
+The protein's natural variant, known as in strain: cv. Aa-0, cv. Al-0, cv. Bs-0, cv. Mt-0, cv. Shokei and cv. Yo-0, features a modification of the amino acid from H to Q at position 106.
+The protein's natural variant, known as in strain: cv. Es-0, features a modification of the amino acid from T to P at position 120.
+The protein's natural variant, known as in strain: cv. Bla-10, features a modification of the amino acid from S to A at position 180.
+The protein's natural variant, known as in strain: cv. Cvi-0, features a modification of the amino acid from S to T at position 197.
+The protein's natural variant, known as in strain: cv. Kas-1, features a modification of the amino acid from A to V at position 217.
+The protein's natural variant, known as in CFZ-R1; leads to increased expression of mmpL5 and partial resistance to both clofazimine and bedaquiline, features a modification of the amino acid from S to R at position 63.
+The protein's natural variant, known as in minor component, features a modification of the amino acid from R to T at position 55.
+The protein's natural variant, known as in strain: M982B / NRCC 4725, features a modification of the amino acid from G to S at position 2.
+The protein's natural variant, known as in strain: 406Y / NRCC 4030 and NRCC 4725, features a modification of the amino acid from Q to H at position 29.
+The protein's natural variant, known as in strain: 406Y / NRCC 4030, M982B / NRCC 4725 and 126E / NRCC 4010, features a modification of the amino acid from E to D at position 40.
+The protein's natural variant, known as in strain: 406Y / NRCC 4030 and M982B / NRCC 4725, features a modification of the amino acid from N to K at position 94.
+The protein's natural variant, known as in strain: 126E / NRCC 4010, features a modification of the amino acid from R to W at position 102.
+The protein's natural variant, known as in strain: 126E / NRCC 4010, features a modification of the amino acid from S to A at position 129.
+The protein's natural variant, known as in strain: 126E / NRCC 4010, features a modification of the amino acid from G to I at position 168.
+The protein's natural variant, known as in strain: 406Y / NRCC 4030 and 126E / NRCC 4010, features a modification of the amino acid from T to A at position 242.
+The protein's natural variant, known as in strain: 406Y / NRCC 4030 and 126E / NRCC 4010, features a modification of the amino acid from K to N at position 273.
+The natural variant of this protein is characterized by an amino acid alteration from M to R at position 144.
+The protein's natural variant, known as in GBD1; reduces efflux activity for PC in a phosphorylation-dependent manner;, features a modification of the amino acid from T to M at position 34.
+The protein's natural variant, known as in GBD1; partly retained intracellularly; reduces efflux activity for PC in a phosphorylation-dependent manner, features a modification of the amino acid from R to G at position 47.
+The protein's natural variant, known as found in patients with cholangitis; unknown pathological significance;, features a modification of the amino acid from R to Q at position 47.
+The protein's natural variant, known as in PFIC3; retained in the reticulum endoplasmic; greatly reduced expression;, features a modification of the amino acid from G to R at position 68.
+The protein's natural variant, known as in PFIC3, features a modification of the amino acid from G to R at position 70.
+The protein's natural variant, known as in GBD1;, features a modification of the amino acid from L to H at position 71.
+The protein's natural variant, known as in PFIC3 and GBD1;, features a modification of the amino acid from L to V at position 73.
+The protein's natural variant, known as in GBD1;, features a modification of the amino acid from F to C at position 78.
+The protein's natural variant, known as in GBD1;, features a modification of the amino acid from S to F at position 99.
+The protein's natural variant, known as in GBD1, features a modification of the amino acid from G to S at position 124.
+The protein's natural variant, known as in PFIC3;, features a modification of the amino acid from G to E at position 126.
+The protein's natural variant, known as in PFIC3;, features a modification of the amino acid from W to R at position 138.
+The protein's natural variant, known as in ICP3;, features a modification of the amino acid from R to K at position 150.
+The protein's natural variant, known as in GBD1, features a modification of the amino acid from F to S at position 154.
+The protein's natural variant, known as in GBD1, features a modification of the amino acid from F to I at position 165.
+The protein's natural variant, known as found in patients with gallbladder and cholestasis; unknown pathological significance;, features a modification of the amino acid from T to A at position 175.
+The protein's natural variant, known as in PFIC3; greatly reduced expression; alters efflux activity for PC;, features a modification of the amino acid from T to M at position 201.
+The protein's natural variant, known as in PFIC3, features a modification of the amino acid from A to P at position 250.
+The protein's natural variant, known as in PFIC3 and GBD1; does not alter plasma membrane location; inhibits efflux activity for PC;, features a modification of the amino acid from A to V at position 286.
+The protein's natural variant, known as in GBD1;, features a modification of the amino acid from M to T at position 301.
+The protein's natural variant, known as in ICP3, GBD1 and PFIC3; unknown pathological significance; does not alter plasma membrane location; does not inhibit efflux activity for PC;, features a modification of the amino acid from S to F at position 320.
+The protein's natural variant, known as in PFIC3;, features a modification of the amino acid from S to I at position 346.
+The protein's natural variant, known as in PFIC3, features a modification of the amino acid from F to L at position 357.
+The protein's natural variant, known as in PFIC3, features a modification of the amino acid from A to V at position 364.
+The protein's natural variant, known as in PFIC3;, features a modification of the amino acid from E to G at position 395.
+The protein's natural variant, known as in PFIC3; does not alter cytoplasmic and cell membrane location; inhibits efflux activity for PC and cholesterol;, features a modification of the amino acid from Y to H at position 403.
+The protein's natural variant, known as in GBD1, features a modification of the amino acid from R to G at position 406.
+The protein's natural variant, known as found in patients with cholangitis; unknown pathological significance;, features a modification of the amino acid from R to Q at position 406.
+The protein's natural variant, known as in PFIC3;, features a modification of the amino acid from T to A at position 424.
+The protein's natural variant, known as in PFIC3, features a modification of the amino acid from V to M at position 425.
+The protein's natural variant, known as in PFIC3; retained in the reticulum endoplasmic; greatly reduced expression, features a modification of the amino acid from D to H at position 459.
+The protein's natural variant, known as in PFIC3, features a modification of the amino acid from V to A at position 475.
+The protein's natural variant, known as in PFIC3; greatly reduced expression; alters efflux activity for PC;, features a modification of the amino acid from P to L at position 479.
+The protein's natural variant, known as in PFIC3; does not alter cytoplasmic and cell membrane location; inhibits efflux activity for PC and cholesterol, features a modification of the amino acid from L to R at position 481.
+The protein's natural variant, known as in GBD1;, features a modification of the amino acid from N to S at position 510.
+The protein's natural variant, known as in PFIC3 and GBD1;, features a modification of the amino acid from A to T at position 511.
+The protein's natural variant, known as in GBD1, features a modification of the amino acid from E to K at position 513.
+The protein's natural variant, known as in GBD1; unknown pathological significance; moderate decrease of phosphatidylcholine transporter activity; does not alter plasma membrane location;, features a modification of the amino acid from E to D at position 528.
+The protein's natural variant, known as in PFIC3; reduced phosphatidylcholine transporter activity; does not alter plasma membrane location, features a modification of the amino acid from G to D at position 535.
+The protein's natural variant, known as in GBD1; loss of phosphatidylcholine transporter activity; does not alter plasma membrane location, features a modification of the amino acid from G to R at position 536.
+The protein's natural variant, known as in PFIC3 and GBD1;, features a modification of the amino acid from I to F at position 541.
+The protein's natural variant, known as in GBD1, features a modification of the amino acid from R to H at position 545.
+The protein's natural variant, known as in ICP3; disruption of protein trafficking with subsequent lack of functional protein at the cell surface;, features a modification of the amino acid from A to D at position 546.
+The protein's natural variant, known as in GBD1;, features a modification of the amino acid from R to H at position 549.
+The protein's natural variant, known as in PFIC3, features a modification of the amino acid from L to R at position 556.
+The protein's natural variant, known as in PFIC3;, features a modification of the amino acid from E to K at position 558.
+The protein's natural variant, known as in PFIC3, features a modification of the amino acid from D to G at position 564.
+The protein's natural variant, known as in GBD1; requires 2 nucleotide substitutions, features a modification of the amino acid from H to T at position 589.
+The protein's natural variant, known as found in patients with gallbladder and cholestasis; unknown pathological significance;, features a modification of the amino acid from R to Q at position 590.
+The protein's natural variant, known as in GBD1;, features a modification of the amino acid from L to Q at position 591.
+The protein's natural variant, known as in PFIC3, features a modification of the amino acid from T to A at position 593.
+The protein's natural variant, known as in GBD1;, features a modification of the amino acid from T to M at position 593.
+The protein's natural variant, known as in PFIC3;, features a modification of the amino acid from M to V at position 630.
+The protein's natural variant, known as in GBD1;, features a modification of the amino acid from E to K at position 647.
+The protein's natural variant, known as in PFIC3;, features a modification of the amino acid from L to P at position 701.
+The protein's natural variant, known as in PFIC3;, features a modification of the amino acid from F to S at position 711.
+The protein's natural variant, known as in PFIC3;, features a modification of the amino acid from T to I at position 715.
+The protein's natural variant, known as in PFIC3, features a modification of the amino acid from G to E at position 723.
+The protein's natural variant, known as in GBD1; loss of phosphatidylcholine transporter activity; does not alter plasma membrane location;, features a modification of the amino acid from P to L at position 726.
+The protein's natural variant, known as in PFIC3, features a modification of the amino acid from P to T at position 726.
+The protein's natural variant, known as in GBD1;, features a modification of the amino acid from S to L at position 729.
+The protein's natural variant, known as in PFIC3;, features a modification of the amino acid from A to V at position 737.
+The natural variant of this protein is characterized by an amino acid alteration from G to S at position 742.
+The protein's natural variant, known as in ICP3, features a modification of the amino acid from G to E at position 762.
+The protein's natural variant, known as in a heterozygous patient with risperidone-induced cholestasis, features a modification of the amino acid from I to L at position 764.
+The protein's natural variant, known as found in patients with cholangitis; unknown pathological significance;, features a modification of the amino acid from T to M at position 775.
+The protein's natural variant, known as in GBD1; benign variant;, features a modification of the amino acid from R to Q at position 788.
+The protein's natural variant, known as in PFIC3, features a modification of the amino acid from A to D at position 840.
+The protein's natural variant, known as found in patients with gallbladder and cholestasis; unknown pathological significance;, features a modification of the amino acid from A to T at position 934.
+The protein's natural variant, known as in PFIC3;, features a modification of the amino acid from G to S at position 954.
+The protein's natural variant, known as requires 2 nucleotide substitutions; found in patients with cholangitis; unknown pathological significance, features a modification of the amino acid from V to T at position 964.
+The protein's natural variant, known as in GBD1;, features a modification of the amino acid from L to V at position 975.
+The protein's natural variant, known as in PFIC3; alters efflux activity for PC;, features a modification of the amino acid from S to P at position 978.
+The protein's natural variant, known as in PFIC3;, features a modification of the amino acid from G to S at position 983.
+The protein's natural variant, known as in a heterozygous patient with amoxicillin/clavulanic acid-induced cholestasis;, features a modification of the amino acid from L to Q at position 1082.
+The protein's natural variant, known as in GBD1;, features a modification of the amino acid from R to W at position 1084.
+The protein's natural variant, known as in PFIC3; alters efflux activity for PC, features a modification of the amino acid from E to K at position 1125.
+The protein's natural variant, known as in GBD1; reduced phosphatidylcholine transporter activity; does not alter plasma membrane location;, features a modification of the amino acid from P to S at position 1168.
+The protein's natural variant, known as in GBD1; severely reduced phosphatidylcholine transporter activity; does not alter plasma membrane location, features a modification of the amino acid from S to L at position 1183.
+The protein's natural variant, known as in GBD1; loss of phosphatidylcholine transporter activity; does not alter plasma membrane location, features a modification of the amino acid from G to S at position 1185.
+The protein's natural variant, known as in PFIC3, features a modification of the amino acid from A to T at position 1193.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation, features a modification of the amino acid from L to F at position 138.
+The natural variant of this protein is characterized by an amino acid alteration from G to R at position 309.
+The protein's natural variant, known as in DEE58; unknown pathological significance;, features a modification of the amino acid from Y to C at position 434.
+The protein's natural variant, known as in a lung carcinoma sample; somatic mutation, features a modification of the amino acid from M to I at position 697.
+The protein's natural variant, known as in a lung carcinoma sample; somatic mutation, features a modification of the amino acid from R to G at position 699.
+The protein's natural variant, known as in OBHD; unknown pathological significance;, features a modification of the amino acid from T to I at position 704.
+The protein's natural variant, known as in OBHD; expressed normally on the cell surface; results in markedly impaired ligand-induced phosphorylation as well as impaired downstream MAPK1 phosphorylation;, features a modification of the amino acid from Y to C at position 706.
+The protein's natural variant, known as in a lung carcinoma sample; somatic mutation;, features a modification of the amino acid from R to C at position 718.
+The natural variant of this protein is characterized by an amino acid alteration from D to E at position 41.
+The protein's natural variant, known as found in a patient with Rett syndrome-like phenotype; unknown pathological significance, features a modification of the amino acid from G to V at position 978.
+The protein's natural variant, known as in strain: Isolate AF 3221, features a modification of the amino acid from I to M at position 11.
+The protein's natural variant, known as in strain: Isolate AF 2664, features a modification of the amino acid from S to A at position 17.
+The protein's natural variant, known as in strain: Isolate AF 3221, features a modification of the amino acid from A to T at position 23.
+The protein's natural variant, known as in strain: Isolate AF 2664, features a modification of the amino acid from C to W at position 40.
+The protein's natural variant, known as in strain: Isolate AF 3221, features a modification of the amino acid from I to A at position 42.
+The protein's natural variant, known as in strain: Isolate AF 2664, features a modification of the amino acid from I to T at position 42.
+The protein's natural variant, known as in strain: Isolate AF 3221, features a modification of the amino acid from M to T at position 237.
+The protein's natural variant, known as in strain: Isolate AF 4995, features a modification of the amino acid from N to S at position 286.
+The protein's natural variant, known as in strain: Isolate AF 2664 and Isolate AF 3221, features a modification of the amino acid from V to I at position 300.
+The protein's natural variant, known as in strain: Isolate AF 3221, features a modification of the amino acid from I to V at position 349.
+The protein's natural variant, known as in strain: Isolate AF 2664 and Isolate AF 3221, features a modification of the amino acid from T to A at position 360.
+The protein's natural variant, known as in strain: Isolate AF 2664 and Isolate AF 3221, features a modification of the amino acid from I to V at position 363.
+The protein's natural variant, known as in strain: Isolate AF 2664, features a modification of the amino acid from L to F at position 365.
+The protein's natural variant, known as in strain: Isolate AF 3221, features a modification of the amino acid from N to S at position 375.
+The protein's natural variant, known as in strain: Isolate AF 3221, features a modification of the amino acid from D to G at position 378.
+The protein's natural variant, known as in strain: Beverley, MAS and Me49, features a modification of the amino acid from H to Y at position 7.
+The protein's natural variant, known as in strain: Castells, FOU, MAS, NED, RUB and TONT, features a modification of the amino acid from V to L at position 17.
+The protein's natural variant, known as in strain: Castells, NED and TONT, features a modification of the amino acid from G to D at position 47.
+The protein's natural variant, known as in strain: FOU, features a modification of the amino acid from K to Q at position 50.
+The protein's natural variant, known as in strain: Beverley and Me49, features a modification of the amino acid from K to R at position 50.
+The protein's natural variant, known as in strain: RUB, features a modification of the amino acid from S to L at position 58.
+The protein's natural variant, known as in strain: Beverley, Castells, FOU, MAS, Me49, NED, RUB and TONT, features a modification of the amino acid from E to D at position 94.
+The protein's natural variant, known as in strain: Beverley, MAS and Me49, features a modification of the amino acid from V to A at position 105.
+The protein's natural variant, known as in strain: Castells, FOU, NED, RUB and TONT, features a modification of the amino acid from Q to P at position 180.
+The protein's natural variant, known as in strain: Beverley, MAS and Me49, features a modification of the amino acid from D to G at position 185.
+The protein's natural variant, known as in strain: RUB, features a modification of the amino acid from D to H at position 185.
+The protein's natural variant, known as in strain: M7741, NED and TONT, features a modification of the amino acid from G to R at position 198.
+The protein's natural variant, known as in strain: Castells and FOU, features a modification of the amino acid from G to R at position 206.
+The protein's natural variant, known as in strain: Castells, FOU, M7741, NED, RUB and TONT, features a modification of the amino acid from A to G at position 213.
+The protein's natural variant, known as in strain: MAS, features a modification of the amino acid from D to G at position 216.
+The protein's natural variant, known as in strain: FOU, features a modification of the amino acid from R to G at position 217.
+The protein's natural variant, known as in strain: MAS, features a modification of the amino acid from R to G at position 218.
+The protein's natural variant, known as in strain: Castells, FOU, M7741, NED, RUB and TONT, features a modification of the amino acid from P to A at position 219.
+The protein's natural variant, known as in strain: RUB, features a modification of the amino acid from P to L at position 222.
+The protein's natural variant, known as in strain: Beverley, Castells, MAS and Me49, features a modification of the amino acid from E to G at position 223.
+The protein's natural variant, known as in strain: Beverley, Castells, MAS and Me49, features a modification of the amino acid from R to S at position 224.
+The protein's natural variant, known as in strain: RUB, features a modification of the amino acid from V to A at position 227.
+The protein's natural variant, known as in strain: Beverley, MAS and Me49, features a modification of the amino acid from V to E at position 227.
+The protein's natural variant, known as in strain: Beverley, MAS and Me49, features a modification of the amino acid from Y to F at position 230.
+The protein's natural variant, known as in strain: cv. NK 1558, features a modification of the amino acid from T to N at position 120.
+The protein's natural variant, known as in strain: cv. IRBB5; confers resistance to X.oryzae, features a modification of the amino acid from V to E at position 39.
+The protein's natural variant, known as in PARK6;, features a modification of the amino acid from C to F at position 92.
+The protein's natural variant, known as in PARK6, features a modification of the amino acid from C to G at position 125.
+The protein's natural variant, known as in PARK6; strongly reduces interaction with PRKN;, features a modification of the amino acid from Q to P at position 126.
+The protein's natural variant, known as in PARK6; unknown pathological significance;, features a modification of the amino acid from R to H at position 147.
+The protein's natural variant, known as in PARK6; no effect on autophosphorylation; localizes to the mitochondria and immunogold experiments reveal that both wild-type and mutant proteins face the mitochondrial intermembrane space;, features a modification of the amino acid from A to P at position 168.
+The protein's natural variant, known as in PARK6;, features a modification of the amino acid from V to G at position 170.
+The protein's natural variant, known as in PARK6;, features a modification of the amino acid from P to L at position 196.
+The protein's natural variant, known as in a glioblastoma multiforme sample; somatic mutation;, features a modification of the amino acid from P to L at position 215.
+The protein's natural variant, known as in PARK6;, features a modification of the amino acid from A to D at position 217.
+The protein's natural variant, known as in PARK6;, features a modification of the amino acid from E to K at position 240.
+The protein's natural variant, known as in PARK6;, features a modification of the amino acid from L to V at position 268.
+The protein's natural variant, known as in PARK6;, features a modification of the amino acid from H to Q at position 271.
+The protein's natural variant, known as in PARK6;, features a modification of the amino acid from R to H at position 279.
+The protein's natural variant, known as in PARK6; early-onset;, features a modification of the amino acid from A to T at position 280.
+The protein's natural variant, known as in PARK6; fails to maintain mitochondrial membrane potential; full-length mutant has no effect on autophosphorylation; strongly reduces interaction with PRKN; decreases PRKN and SNCAIP ubiquitination and degradation; decreases Drp1 phosphorylation;, features a modification of the amino acid from G to D at position 309.
+The protein's natural variant, known as in PARK6; decreases PRKN and SNCAIP ubiquitination and degradation; slightly decreases Drp1 phosphorylation;, features a modification of the amino acid from T to M at position 313.
+The protein's natural variant, known as in PARK6; strongly reduces interaction with PRKN; reduced ubiquitination of MIRO1;, features a modification of the amino acid from L to P at position 347.
+The natural variant of this protein is characterized by an amino acid alteration from D to H at position 362.
+The protein's natural variant, known as in PARK6;, features a modification of the amino acid from L to P at position 369.
+The protein's natural variant, known as in PARK6; abolishes kinase activity, features a modification of the amino acid from G to A at position 386.
+The protein's natural variant, known as in PARK6;, features a modification of the amino acid from C to R at position 388.
+The protein's natural variant, known as probable disease-associated variant found in early-onset Parkinson disease with digenic inheritance; found in a patient also carrying mutation S-39 in PARK7; decreases PRKN and SNCAIP ubiquitination and degradation;, features a modification of the amino acid from P to L at position 399.
+The protein's natural variant, known as in PARK6; early-onset;, features a modification of the amino acid from R to Q at position 407.
+The protein's natural variant, known as in PARK6;, features a modification of the amino acid from G to V at position 409.
+The protein's natural variant, known as in PARK6;, features a modification of the amino acid from E to G at position 417.
+The protein's natural variant, known as may predispose to Parkinson disease development; shows decreased mitochondrial membrane potential under stress conditions;, features a modification of the amino acid from Y to H at position 431.
+The protein's natural variant, known as may predispose to Parkinson disease development; shows decreased mitochondrial membrane potential under stress conditions;, features a modification of the amino acid from N to S at position 451.
+The natural variant of this protein is characterized by an amino acid alteration from L to S at position 461.
+The protein's natural variant, known as in PARK6;, features a modification of the amino acid from R to H at position 464.
+The protein's natural variant, known as may predispose to Parkinson disease development; shows decreased mitochondrial membrane potential under stress conditions;, features a modification of the amino acid from E to K at position 476.
+The protein's natural variant, known as in PARK6;, features a modification of the amino acid from L to P at position 489.
+The protein's natural variant, known as may predispose to Parkinson disease development; shows decreased mitochondrial membrane potential under stress conditions;, features a modification of the amino acid from R to P at position 501.
+The protein's natural variant, known as in PARK6, features a modification of the amino acid from Q to QQ at position 534.
+The protein's natural variant, known as may predispose to Parkinson disease development; shows decreased mitochondrial membrane potential under stress conditions;, features a modification of the amino acid from C to R at position 575.
+The protein's natural variant, known as in OI21; unknown pathological significance;, features a modification of the amino acid from R to W at position 5.
+The protein's natural variant, known as in OI21; changed maintenance of protein localization in endoplasmic reticulum; SERPINH1 is not retained in the endoplasmic reticulum and secreted; leads to a loss of fiber formation of the bones connective tissue; no effect on protein abundance;, features a modification of the amino acid from H to D at position 12.
+The protein's natural variant, known as in OI21; unknown pathological significance;, features a modification of the amino acid from P to L at position 133.
+The protein's natural variant, known as in OI21; unknown pathological significance, features a modification of the amino acid from Y to C at position 162.
+The natural variant of this protein is characterized by an amino acid alteration from Y to I at position 73.
+The natural variant of this protein is characterized by an amino acid alteration from T to K at position 86.
+The protein's natural variant, known as in KIDAR;, features a modification of the amino acid from C to R at position 144.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to C at position 262.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from K to Q at position 19.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from P to R at position 126.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from E to V at position 375.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from Q to L at position 1045.
+The protein's natural variant, known as in COQ10D2;, features a modification of the amino acid from D to E at position 308.
+The protein's natural variant, known as in DDIB, features a modification of the amino acid from E to G at position 17.
+The protein's natural variant, known as in DDIB;, features a modification of the amino acid from S to F at position 111.
+The protein's natural variant, known as in DDIB, features a modification of the amino acid from R to I at position 150.
+The protein's natural variant, known as in DDIB; affects neuron maturation and migration, features a modification of the amino acid from L to R at position 167.
+The protein's natural variant, known as in DDIB; unknown pathological significance, features a modification of the amino acid from M to V at position 231.
+The protein's natural variant, known as in DDIB, features a modification of the amino acid from K to E at position 298.
+The protein's natural variant, known as in DDIB, features a modification of the amino acid from D to A at position 305.
+The protein's natural variant, known as in DDIB; unknown pathological significance, features a modification of the amino acid from L to F at position 315.
+The protein's natural variant, known as in DDIB; affects neuron maturation and migration, features a modification of the amino acid from L to P at position 548.
+The protein's natural variant, known as in tg, features a modification of the amino acid from P to L at position 649.
+The protein's natural variant, known as in MC1DN1;, features a modification of the amino acid from D to H at position 119.
+The protein's natural variant, known as in FSGS1, features a modification of the amino acid from W to R at position 59.
+The protein's natural variant, known as in FSGS1, features a modification of the amino acid from E to Q at position 72.
+The protein's natural variant, known as in FSGS1; unknown pathological significance, features a modification of the amino acid from F to L at position 153.
+The protein's natural variant, known as in FSGS1; no effect on protein abundance; no effect on homodimerization; loss of localization to the nucleus; prevents nuclear localization of the wild-type protein; decreased interaction with PPARG and RARA; loss of transcriptional coactivator activity; dominant negative effect on nuclear receptors-mediated transcription; increased actin-binding affinity;, features a modification of the amino acid from K to E at position 255.
+The protein's natural variant, known as in FSGS1; no effect on protein abundance; no effect on homodimerization; loss of localization to the nucleus; prevents nuclear localization of the wild-type protein; decreased interaction with PPARG and RARA; loss of transcriptional coactivator activity; dominant negative effect on nuclear receptors-mediated transcription; increased actin-binding affinity;, features a modification of the amino acid from T to I at position 259.
+The protein's natural variant, known as in FSGS1, features a modification of the amino acid from S to F at position 262.
+The protein's natural variant, known as in FSGS1; no effect on protein abundance; no effect on homodimerization; loss of localization to the nucleus; prevents nuclear localization of the wild-type protein; decreased interaction with PPARG and RARA; loss of transcriptional coactivator activity; dominant negative effect on nuclear receptors-mediated transcription; increased actin-binding affinity;, features a modification of the amino acid from S to P at position 262.
+The protein's natural variant, known as in FSGS1; unknown pathological significance;, features a modification of the amino acid from R to Q at position 310.
+The protein's natural variant, known as in FSGS1;, features a modification of the amino acid from A to T at position 427.
+The protein's natural variant, known as in FSGS1, features a modification of the amino acid from N to D at position 748.
+The protein's natural variant, known as rare variant found in patients with IgA nephropathy; unknown pathological significance;, features a modification of the amino acid from A to V at position 784.
+The natural variant of this protein is characterized by an amino acid alteration from G to R at position 786.
+The natural variant of this protein is characterized by an amino acid alteration from P to L at position 787.
+The natural variant of this protein is characterized by an amino acid alteration from P to S at position 787.
+The protein's natural variant, known as rare variant found in patients with IgA nephropathy; unknown pathological significance, features a modification of the amino acid from C to Y at position 793.
+The protein's natural variant, known as rare variant found in patients with IgA nephropathy; unknown pathological significance, features a modification of the amino acid from G to D at position 798.
+The protein's natural variant, known as in JVS, features a modification of the amino acid from L to R at position 352.
+The protein's natural variant, known as found in patients with non-obstructive azoospermia; unknown pathological significance;, features a modification of the amino acid from P to S at position 334.
+The protein's natural variant, known as in CDG1T; strongly reduces phosphoglucomutase activity;, features a modification of the amino acid from T to A at position 19.
+The protein's natural variant, known as in CDG1T; strongly reduces solubility; increases aggregation;, features a modification of the amino acid from N to Y at position 38.
+The protein's natural variant, known as in CDG1T; reduces solubility; increases aggregation;, features a modification of the amino acid from Q to R at position 41.
+The protein's natural variant, known as in CDG1T; reduces solubility; reduces strongly phosphoglucomutase activity;, features a modification of the amino acid from D to H at position 62.
+The protein's natural variant, known as in allele PGM1*7+, allele PGM1*7-, allele PGM1*3+ and allele PGM1*3-; phosphoglucomutase activity is similar to wild-type;, features a modification of the amino acid from K to M at position 68.
+The protein's natural variant, known as in CDG1T; reduces mildly phosphoglucomutase activity;, features a modification of the amino acid from T to A at position 115.
+The protein's natural variant, known as in CDG1T; there is 7% enzyme residual phosphoglucomutase activity;, features a modification of the amino acid from G to R at position 121.
+The protein's natural variant, known as in allele PGM1*2+, allele PGM1*2-, allele PGM1*3+ and allele PGM1*3-; phosphoglucomutase activity is similar to wild-type;, features a modification of the amino acid from R to C at position 221.
+The protein's natural variant, known as in CDG1T; strongly reduces phosphoglucomutase activity;, features a modification of the amino acid from D to G at position 263.
+The protein's natural variant, known as in CDG1T; strongly reduces phosphoglucomutase activity;, features a modification of the amino acid from D to Y at position 263.
+The protein's natural variant, known as in CDG1T; strongly reduces phosphoglucomutase activity;, features a modification of the amino acid from G to R at position 291.
+The protein's natural variant, known as in CDG1T; decreases mildly solubility;, features a modification of the amino acid from G to R at position 330.
+The protein's natural variant, known as in CDG1T; decreases strongly solubility, features a modification of the amino acid from E to K at position 377.
+The protein's natural variant, known as in CDG1T; decreases strongly solubility;, features a modification of the amino acid from E to K at position 388.
+The protein's natural variant, known as in allele PGM1*1-, allele PGM1*2-, allele PGM1*3- and allele PGM1*7-; phosphoglucomutase activity is similar to wild-type;, features a modification of the amino acid from Y to H at position 420.
+The protein's natural variant, known as in CDG1T; decreases strongly solubility;, features a modification of the amino acid from L to P at position 516.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from L to V at position 108.
+The protein's natural variant, known as in DRDSPRD; loss of sepiapterin reductase activity;, features a modification of the amino acid from R to G at position 150.
+The protein's natural variant, known as in DRDSPRD;, features a modification of the amino acid from P to L at position 163.
+The protein's natural variant, known as in strain: Serotype 5, features a modification of the amino acid from QYLLL to PIFVT at position 47.
+The protein's natural variant, known as in strain: Serotype 5, features a modification of the amino acid from WA to SR at position 60.
+The protein's natural variant, known as in DFNB59; causes hypervulnerability to sound;, features a modification of the amino acid from T to I at position 54.
+The protein's natural variant, known as in DFNB59;, features a modification of the amino acid from R to W at position 183.
+The protein's natural variant, known as in DFNB59; unknown pathological significance, features a modification of the amino acid from L to R at position 244.
+The natural variant of this protein is characterized by an amino acid alteration from L to R at position 299.
+The protein's natural variant, known as in DFNB59;, features a modification of the amino acid from C to S at position 343.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from S to R at position 516.
+The protein's natural variant, known as in MPPH3;, features a modification of the amino acid from T to A at position 280.
+The protein's natural variant, known as in MPPH3;, features a modification of the amino acid from T to N at position 280.
+The protein's natural variant, known as in MPPH3;, features a modification of the amino acid from P to L at position 281.
+The protein's natural variant, known as in MPPH3;, features a modification of the amino acid from P to R at position 281.
+The protein's natural variant, known as in MPPH3;, features a modification of the amino acid from V to G at position 284.
+The protein's natural variant, known as in XLHR, features a modification of the amino acid from C to S at position 77.
+The protein's natural variant, known as in XLHR; sporadic, features a modification of the amino acid from F to S at position 80.
+The protein's natural variant, known as in XLHR; sporadic, features a modification of the amino acid from C to F at position 85.
+The protein's natural variant, known as in XLHR;, features a modification of the amino acid from C to R at position 85.
+The protein's natural variant, known as in XLHR;, features a modification of the amino acid from C to Y at position 85.
+The protein's natural variant, known as in XLHR, features a modification of the amino acid from L to P at position 138.
+The protein's natural variant, known as in XLHR; sporadic, features a modification of the amino acid from S to P at position 141.
+The protein's natural variant, known as in XLHR, features a modification of the amino acid from C to F at position 142.
+The protein's natural variant, known as in XLHR, features a modification of the amino acid from L to R at position 160.
+The protein's natural variant, known as in XLHR;, features a modification of the amino acid from R to C at position 166.
+The protein's natural variant, known as in XLHR; sporadic, features a modification of the amino acid from D to G at position 237.
+The protein's natural variant, known as in XLHR;, features a modification of the amino acid from F to S at position 252.
+The protein's natural variant, known as in XLHR;, features a modification of the amino acid from M to I at position 253.
+The protein's natural variant, known as in XLHR, features a modification of the amino acid from Y to F at position 317.
+The protein's natural variant, known as in XLHR, features a modification of the amino acid from W to WN at position 444.
+The protein's natural variant, known as in XLHR;, features a modification of the amino acid from W to C at position 530.
+The protein's natural variant, known as in XLHR;, features a modification of the amino acid from P to L at position 534.
+The protein's natural variant, known as in XLHR;, features a modification of the amino acid from L to P at position 555.
+The protein's natural variant, known as in XLHR; sporadic;, features a modification of the amino acid from R to P at position 567.
+The protein's natural variant, known as in XLHR; sporadic;, features a modification of the amino acid from A to D at position 573.
+The protein's natural variant, known as in XLHR;, features a modification of the amino acid from G to R at position 579.
+The protein's natural variant, known as in XLHR;, features a modification of the amino acid from G to V at position 579.
+The protein's natural variant, known as in XLHR, features a modification of the amino acid from Q to R at position 621.
+The protein's natural variant, known as in XLHR;, features a modification of the amino acid from R to P at position 651.
+The protein's natural variant, known as in XLHR; sporadic;, features a modification of the amino acid from N to K at position 680.
+The protein's natural variant, known as in XLHR; sporadic;, features a modification of the amino acid from C to Y at position 693.
+The protein's natural variant, known as in XLHR, features a modification of the amino acid from A to T at position 720.
+The protein's natural variant, known as in XLHR, features a modification of the amino acid from F to Y at position 731.
+The protein's natural variant, known as in XLHR; sporadic;, features a modification of the amino acid from C to S at position 733.
+The protein's natural variant, known as in XLHR; sporadic, features a modification of the amino acid from C to W at position 746.
+The protein's natural variant, known as in XLHR;, features a modification of the amino acid from W to R at position 749.
+The protein's natural variant, known as in PNCA5; associated with disease susceptibility;, features a modification of the amino acid from R to Q at position 184.
+The protein's natural variant, known as in a family with non-syndromic hearing loss; reduces hyaluronic acid degradation activity;, features a modification of the amino acid from R to C at position 187.
+The protein's natural variant, known as in two unrelated families with non-syndromic hearing loss; reduces hyaluronic acid (HA) degradation activity;, features a modification of the amino acid from R to H at position 187.
+The protein's natural variant, known as does not inhibit hyaluronic acid degradation activity;, features a modification of the amino acid from H to R at position 783.
+The protein's natural variant, known as in a sporadic case of non-syndromic hearing loss;, features a modification of the amino acid from H to Y at position 783.
+The protein's natural variant, known as does not inhibit hyaluronic acid degradation activity;, features a modification of the amino acid from V to I at position 1109.
+The protein's natural variant, known as in NDNC1; also found in a patient with neural tube defects; the mutant protein localizes to the lysosomes compared to wild-type;, features a modification of the amino acid from R to C at position 511.
+The protein's natural variant, known as in a patient with neural tube defects;, features a modification of the amino acid from R to H at position 511.
+The protein's natural variant, known as in a colon cancer cell line, features a modification of the amino acid from A to D at position 185.
+The protein's natural variant, known as in VDDR1A;, features a modification of the amino acid from Q to H at position 65.
+The protein's natural variant, known as in VDDR1A; complete loss of activity;, features a modification of the amino acid from R to H at position 107.
+The protein's natural variant, known as in VDDR1A; complete loss of activity;, features a modification of the amino acid from G to E at position 125.
+The protein's natural variant, known as in VDDR1A; 22% of wild-type activity;, features a modification of the amino acid from E to G at position 189.
+The protein's natural variant, known as in VDDR1A; 11% of wild-type activity, features a modification of the amino acid from E to K at position 189.
+The protein's natural variant, known as in VDDR1A; complete loss of activity;, features a modification of the amino acid from T to R at position 321.
+The protein's natural variant, known as in VDDR1A, features a modification of the amino acid from S to Y at position 323.
+The protein's natural variant, known as in VDDR1A; complete loss of activity;, features a modification of the amino acid from R to P at position 335.
+The protein's natural variant, known as in VDDR1A; 2.3% of wild-type activity;, features a modification of the amino acid from L to F at position 343.
+The protein's natural variant, known as in VDDR1A; complete loss of activity;, features a modification of the amino acid from P to S at position 382.
+The protein's natural variant, known as in VDDR1A; complete loss of activity;, features a modification of the amino acid from R to C at position 389.
+The protein's natural variant, known as in VDDR1A; complete loss of activity;, features a modification of the amino acid from R to G at position 389.
+The protein's natural variant, known as in VDDR1A; complete loss of activity;, features a modification of the amino acid from R to H at position 389.
+The protein's natural variant, known as in VDDR1A;, features a modification of the amino acid from T to I at position 409.
+The protein's natural variant, known as in VDDR1A;, features a modification of the amino acid from R to P at position 429.
+The protein's natural variant, known as in VDDR1A;, features a modification of the amino acid from R to C at position 453.
+The protein's natural variant, known as in VDDR1A, features a modification of the amino acid from V to G at position 478.
+The protein's natural variant, known as in VDDR1A;, features a modification of the amino acid from P to R at position 497.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from A to T at position 26.
+The protein's natural variant, known as in oncogenic NEU, features a modification of the amino acid from V to E at position 661.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from G to E at position 186.
+The protein's natural variant, known as in mutant nfx13E; loss of DNA binding and regulator activity, features a modification of the amino acid from R to G at position 42.
+The protein's natural variant, known as in RP42;, features a modification of the amino acid from S to N at position 150.
+The protein's natural variant, known as in RP42; impairs interaction with CUL3 and ubiquitin ligase activity of the BCR(KLHL7) complex;, features a modification of the amino acid from A to T at position 153.
+The protein's natural variant, known as in RP42; impairs interaction with CUL3 and ubiquitin ligase activity of the BCR(KLHL7) complex;, features a modification of the amino acid from A to V at position 153.
+The protein's natural variant, known as in a patient with retinitis pigmentosa; uncertain pathological significance;, features a modification of the amino acid from D to N at position 255.
+The protein's natural variant, known as in PERCHING; subcellular localization in punctate structures at the perinuclear region of cytoplasm is similar to wild-type and colocalized with CUL3;, features a modification of the amino acid from R to Q at position 372.
+The protein's natural variant, known as in PERCHING; subcellular localization in punctate structures at the perinuclear region of cytoplasm is similar to wild-type and colocalized with CUL3;, features a modification of the amino acid from R to C at position 420.
+The protein's natural variant, known as in PERCHING; subcellular localization in punctate structures at the perinuclear region of cytoplasm is similar to wild-type and colocalized with CUL3;, features a modification of the amino acid from C to S at position 421.
+The natural variant of this protein is characterized by an amino acid alteration from H to Y at position 423.
+The protein's natural variant, known as in a patient with retinitis pigmentosa; uncertain pathological significance, features a modification of the amino acid from K to Q at position 472.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from G to V at position 1669.
+The protein's natural variant, known as in CLABARS; unknown pathological significance;, features a modification of the amino acid from P to L at position 5.
+The protein's natural variant, known as in CLABARS;, features a modification of the amino acid from A to V at position 761.
+The protein's natural variant, known as in CLABARS, features a modification of the amino acid from D to H at position 1557.
+The protein's natural variant, known as in CLABARS;, features a modification of the amino acid from R to Q at position 1595.
+The protein's natural variant, known as in CLABARS;, features a modification of the amino acid from S to L at position 1840.
+The natural variant of this protein is characterized by an amino acid alteration from A to P at position 29.
+The protein's natural variant, known as found in a patient with a neurodevelopmental disorder; unknown pathological significance;, features a modification of the amino acid from W to R at position 20.
+The protein's natural variant, known as found in a patient with a neurodevelopmental disorder; unknown pathological significance;, features a modification of the amino acid from N to S at position 216.
+The protein's natural variant, known as found in a patient with a neurodevelopmental disorder; unknown pathological significance;, features a modification of the amino acid from V to M at position 286.
+The protein's natural variant, known as found in a patient with a neurodevelopmental disorder; unknown pathological significance;, features a modification of the amino acid from L to F at position 298.
+The protein's natural variant, known as found in a patient with a neurodevelopmental disorder; unknown pathological significance;, features a modification of the amino acid from R to Q at position 611.
+The protein's natural variant, known as in DEE106; decreased function in deUFMylation; reduced UFSP2 abundance and increased abundance of UFMylated targets in homozygous patient-derived fibroblasts, features a modification of the amino acid from V to E at position 115.
+The protein's natural variant, known as in BFHD; loss of protease activity toward the C-terminal of UFM1;, features a modification of the amino acid from Y to H at position 290.
+The protein's natural variant, known as in SEMDDR;, features a modification of the amino acid from D to A at position 426.
+The protein's natural variant, known as in SEMDDR, features a modification of the amino acid from H to R at position 428.
+The protein's natural variant, known as in LUSYAM;, features a modification of the amino acid from R to H at position 70.
+The protein's natural variant, known as in LUSYAM; unknown pathological significance, features a modification of the amino acid from S to R at position 82.
+The protein's natural variant, known as in plasmid pCP301, features a modification of the amino acid from A to T at position 57.
+The natural variant of this protein is characterized by an amino acid alteration from V to L at position 43.
+The protein's natural variant, known as found in a male with undermasculinised genitalia and intra-abdominal testes; unknown pathological significance;, features a modification of the amino acid from P to S at position 49.
+The protein's natural variant, known as in CRYPTO;, features a modification of the amino acid from P to L at position 93.
+The protein's natural variant, known as in CRYPTO;, features a modification of the amino acid from R to C at position 102.
+The protein's natural variant, known as in CRYPTO;, features a modification of the amino acid from N to K at position 110.
+The protein's natural variant, known as in allele SULT1A1*2; has a lower sulfotransferase activity;, features a modification of the amino acid from R to H at position 213.
+The protein's natural variant, known as in STWS1, features a modification of the amino acid from S to P at position 279.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from F to L at position 1068.
+The protein's natural variant, known as in strain: RM 7004, features a modification of the amino acid from D to H at position 107.
+The protein's natural variant, known as in strain: RM 7004, features a modification of the amino acid from D to N at position 145.
+The protein's natural variant, known as in strain: RM 7004, features a modification of the amino acid from A to V at position 321.
+The protein's natural variant, known as in strain: RM 7004, features a modification of the amino acid from A to T at position 331.
+The protein's natural variant, known as in strain: RM 7004, features a modification of the amino acid from S to A at position 353.
+The protein's natural variant, known as in suppressor mutant, features a modification of the amino acid from W to L at position 427.
+The protein's natural variant, known as in strain: CER 89L1216, features a modification of the amino acid from K to E at position 2.
+The protein's natural variant, known as in strain: 8-6, features a modification of the amino acid from I to V at position 10.
+The protein's natural variant, known as in strain: CER 89L1105 and CER 89L1216, features a modification of the amino acid from TLA to ALR at position 15.
+The protein's natural variant, known as in strain: 8-6, KZ211, L9, NCIB 10691, BP6K and KZ1340, features a modification of the amino acid from T to A at position 13.
+The protein's natural variant, known as in strain: 8-6, features a modification of the amino acid from A to V at position 15.
+The protein's natural variant, known as in strain: L9 and BP6K, features a modification of the amino acid from A to T at position 22.
+The protein's natural variant, known as in strain: 8-6, features a modification of the amino acid from A to V at position 22.
+The protein's natural variant, known as in strain: NCIB 10691, features a modification of the amino acid from V to A at position 43.
+The protein's natural variant, known as in strain: L9 and KZ1340, features a modification of the amino acid from V to I at position 47.
+The protein's natural variant, known as in strain: 8-6, features a modification of the amino acid from L to M at position 54.
+The protein's natural variant, known as in strain: 8-6, features a modification of the amino acid from E to D at position 71.
+The protein's natural variant, known as in strain: KZ1340, features a modification of the amino acid from D to N at position 91.
+The protein's natural variant, known as in strain: 8-6, features a modification of the amino acid from D to N at position 103.
+The protein's natural variant, known as in strain: KZ1340; probably inactive, features a modification of the amino acid from H to Y at position 176.
+The protein's natural variant, known as in strain: 8-6, NCIB 10663 and NCIB 10748, features a modification of the amino acid from A to V at position 195.
+The protein's natural variant, known as in strain: NCIB 10691 and CER 89L1105, features a modification of the amino acid from D to A at position 202.
+The protein's natural variant, known as in strain: NCIB 10691 and CER 89L1105, features a modification of the amino acid from A to T at position 205.
+The protein's natural variant, known as in strain: 8-6, features a modification of the amino acid from K to N at position 281.
+The protein's natural variant, known as in strain: 8-6, features a modification of the amino acid from T to A at position 329.
+The protein's natural variant, known as in strain: NCIB 10691 and CER 89L1105, features a modification of the amino acid from P to S at position 363.
+The protein's natural variant, known as in strain: PB6K, features a modification of the amino acid from I to L at position 373.
+The protein's natural variant, known as in strain: 8-6, NCIB 10662, L9, NCIB 10663, NCIB 10748, CER 89L43 and KZ1340, features a modification of the amino acid from I to V at position 373.
+The protein's natural variant, known as in strain: 941 and 3114, features a modification of the amino acid from L to F at position 23.
+The protein's natural variant, known as in strain: ACV2, features a modification of the amino acid from M to V at position 40.
+The protein's natural variant, known as in strain: CB4853 and CB4858, features a modification of the amino acid from I to M at position 181.
+The protein's natural variant, known as in strain: Bristol N2, CB4855, CB4857, CB4858 and KR314, features a modification of the amino acid from K to N at position 238.
+The protein's natural variant, known as in strain: CB4854, features a modification of the amino acid from S to I at position 246.
+The protein's natural variant, known as in MC4DN11; reduced protein expression; defective mitochondrial respiratory chain complex IV assembly; decreased interaction with MT-CO2/COX2; increased interaction with TMEM177;, features a modification of the amino acid from T to P at position 52.
+The protein's natural variant, known as in strain: wtf18-2; suppresses meiotic drive by wtf13 isoform 2, features a modification of the amino acid from E to GGLGNAFG at position 331.
+The protein's natural variant, known as in strain: wtf18-2; suppresses meiotic drive by wtf13 isoform 2, features a modification of the amino acid from NNIPLEETEA to DIPLGEMDV at position 368.
+The protein's natural variant, known as in NATD; reduced N-terminal acetyltransferase activity; impaired interaction with NAA15 and NAA50; does not affect cytoplasmic localization;, features a modification of the amino acid from S to P at position 37.
+The protein's natural variant, known as in NATD; decreased protein stability; strong decrease in N-terminal acetylation activity in vitro;, features a modification of the amino acid from Y to S at position 43.
+The protein's natural variant, known as in NATD; reduced monomeric N-terminal acetyltransferase activity in vitro;, features a modification of the amino acid from R to H at position 83.
+The protein's natural variant, known as in strain: 129/Ola, BALB/c and FVB/NJ, features a modification of the amino acid from N to S at position 14.
+The protein's natural variant, known as in strain: ATCC 50502 / ECIII, features a modification of the amino acid from L to F at position 288.
+The protein's natural variant, known as probable disease-associated variant found in patients with ASD, features a modification of the amino acid from E to K at position 1040.
+The protein's natural variant, known as in strain: NIH, features a modification of the amino acid from V to A at position 226.
+The protein's natural variant, known as in strain: NIH, features a modification of the amino acid from G to E at position 249.
+The protein's natural variant, known as in strain: BL21 and MRE-600; increased termination efficiency, features a modification of the amino acid from T to A at position 246.
+The natural variant of this protein is characterized by an amino acid alteration from Y to H at position 255.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from P to S at position 604.
+The protein's natural variant, known as in MODY10;, features a modification of the amino acid from R to C at position 6.
+The protein's natural variant, known as in MODY10;, features a modification of the amino acid from R to H at position 6.
+The protein's natural variant, known as in PNDM4;, features a modification of the amino acid from A to D at position 24.
+The protein's natural variant, known as in PNDM4;, features a modification of the amino acid from H to D at position 29.
+The protein's natural variant, known as in PNDM4;, features a modification of the amino acid from G to R at position 32.
+The protein's natural variant, known as in PNDM4;, features a modification of the amino acid from G to S at position 32.
+The protein's natural variant, known as in HPRI; Providence;, features a modification of the amino acid from H to D at position 34.
+The protein's natural variant, known as in PNDM4;, features a modification of the amino acid from L to P at position 35.
+The protein's natural variant, known as in PNDM4;, features a modification of the amino acid from C to G at position 43.
+The protein's natural variant, known as in MODY10; reduces binding affinity to INSR; reduces biological activity; reduces folding properties;, features a modification of the amino acid from R to Q at position 46.
+The protein's natural variant, known as in PNDM4;, features a modification of the amino acid from G to V at position 47.
+The protein's natural variant, known as in PNDM4;, features a modification of the amino acid from F to C at position 48.
+The protein's natural variant, known as associated with diabetes mellitus type-II; Los-Angeles;, features a modification of the amino acid from F to S at position 48.
+The protein's natural variant, known as in Chicago;, features a modification of the amino acid from F to L at position 49.
+The protein's natural variant, known as in T1D2;, features a modification of the amino acid from R to C at position 55.
+The protein's natural variant, known as in PNDM4; uncertain pathological significance;, features a modification of the amino acid from G to R at position 84.
+The protein's natural variant, known as in PNDM4;, features a modification of the amino acid from R to C at position 89.
+The protein's natural variant, known as in HPRI; impairs post-translational cleavage;, features a modification of the amino acid from R to H at position 89.
+The protein's natural variant, known as in HPRI; Kyoto;, features a modification of the amino acid from R to L at position 89.
+The protein's natural variant, known as in PNDM4;, features a modification of the amino acid from G to C at position 90.
+The protein's natural variant, known as in Wakayama;, features a modification of the amino acid from V to L at position 92.
+The protein's natural variant, known as in PNDM4;, features a modification of the amino acid from C to S at position 96.
+The protein's natural variant, known as in PNDM4;, features a modification of the amino acid from C to Y at position 96.
+The protein's natural variant, known as in PNDM4;, features a modification of the amino acid from S to C at position 101.
+The protein's natural variant, known as in PNDM4;, features a modification of the amino acid from Y to C at position 103.
+The protein's natural variant, known as in PNDM4;, features a modification of the amino acid from Y to C at position 108.
+The protein's natural variant, known as in strain: Isolate SO-2000/12/28-1, features a modification of the amino acid from I to M at position 92.
+The protein's natural variant, known as in strain: Isolate SO-2000/12/28-1, features a modification of the amino acid from I to T at position 334.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from K to N at position 450.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from T to S at position 354.
+The protein's natural variant, known as found in siblings with a novel form of progressive myoclonus epilepsy; unknown pathological significance; no effect on expression levels, cell surface location, signaling activity or ubiquitination;, features a modification of the amino acid from K to N at position 349.
+The protein's natural variant, known as in strain: CA7, features a modification of the amino acid from P to S at position 35.
+The protein's natural variant, known as in strain: PBre and 21343WI, features a modification of the amino acid from K to N at position 39.
+The protein's natural variant, known as in strain: 42373NY3, features a modification of the amino acid from D to H at position 59.
+The protein's natural variant, known as in strain: CA8, features a modification of the amino acid from I to V at position 90.
+The protein's natural variant, known as in strain: PBre, features a modification of the amino acid from V to A at position 114.
+The protein's natural variant, known as in strain: CA8, features a modification of the amino acid from N to S at position 127.
+The protein's natural variant, known as in strain: CA8, features a modification of the amino acid from VS to LP at position 133.
+The protein's natural variant, known as in strain: 21343WI, features a modification of the amino acid from R to K at position 144.
+The protein's natural variant, known as in strain: PBre and 42373NY3, features a modification of the amino acid from G to E at position 149.
+The protein's natural variant, known as in strain: PBre, features a modification of the amino acid from G to S at position 164.
+The protein's natural variant, known as in strain: CA8 and 21343WI, features a modification of the amino acid from E to A at position 196.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from H to R at position 416.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from E to K at position 240.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from V to M at position 226.
+The protein's natural variant, known as in an osteogenic sarcoma sample; somatic mutation; might influence susceptibility to breast cancer; does not cause protein abrogation in familial colorectal cancer;, features a modification of the amino acid from A to S at position 17.
+The protein's natural variant, known as in multiple cancers;, features a modification of the amino acid from T to K at position 59.
+The protein's natural variant, known as in prostate cancer; somatic mutation;, features a modification of the amino acid from E to K at position 64.
+The protein's natural variant, known as in an osteogenic sarcoma sample; neutral allele among Ashkenazi Jewish women;, features a modification of the amino acid from P to L at position 85.
+The protein's natural variant, known as in BC;, features a modification of the amino acid from R to G at position 117.
+The protein's natural variant, known as might influence susceptibility to breast cancer; does not cause protein abrogation in familial colorectal cancer;, features a modification of the amino acid from R to Q at position 137.
+The protein's natural variant, known as in prostate cancer; somatic mutation;, features a modification of the amino acid from R to P at position 145.
+The protein's natural variant, known as in colon cancer and LFS2; does not cause protein abrogation in familial colorectal cancer; loss of the ability to interact with and phosphorylate CDC25A and to promote CDC25A degradation in response to ionizing radiation;, features a modification of the amino acid from R to W at position 145.
+The protein's natural variant, known as might influence susceptibility to different types of cancer; does not cause protein abrogation in familial colorectal cancer; loss of the ability to interact with and phosphorylate CDC25A and to promote CDC25A degradation in response to ionizing radiation;, features a modification of the amino acid from I to T at position 157.
+The protein's natural variant, known as in prostate cancer; somatic mutation;, features a modification of the amino acid from G to R at position 167.
+The protein's natural variant, known as in prostate cancer; somatic mutation;, features a modification of the amino acid from R to C at position 180.
+The protein's natural variant, known as in prostate cancer; somatic mutation;, features a modification of the amino acid from R to H at position 180.
+The protein's natural variant, known as in prostate cancer; somatic mutation;, features a modification of the amino acid from R to C at position 181.
+The protein's natural variant, known as in prostate cancer; somatic mutation;, features a modification of the amino acid from R to H at position 181.
+The protein's natural variant, known as in prostate cancer; germline mutation;, features a modification of the amino acid from E to K at position 239.
+The protein's natural variant, known as in prostate cancer; unknown pathological significance;, features a modification of the amino acid from I to F at position 251.
+The protein's natural variant, known as in prostate cancer; unknown pathological significance; somatic mutation;, features a modification of the amino acid from R to H at position 318.
+The protein's natural variant, known as in prostate cancer; somatic mutation;, features a modification of the amino acid from T to P at position 323.
+The protein's natural variant, known as in prostate cancer; unknown pathological significance; somatic mutation;, features a modification of the amino acid from Y to C at position 327.
+The protein's natural variant, known as confers a moderate risk of breast cancer; partially reduces kinase activity;, features a modification of the amino acid from H to Y at position 371.
+The protein's natural variant, known as in BC; does not phosphorylate p53/TP53;, features a modification of the amino acid from Y to C at position 390.
+The protein's natural variant, known as may increase breast cancer risk;, features a modification of the amino acid from S to F at position 428.
+The protein's natural variant, known as in prostate cancer; somatic mutation, features a modification of the amino acid from T to K at position 476.
+The protein's natural variant, known as in strain: CNTC 1/82, features a modification of the amino acid from T to I at position 54.
+The protein's natural variant, known as in strain: CNTC 1/82, features a modification of the amino acid from S to N at position 167.
+The protein's natural variant, known as in strain: CNTC 1/82, features a modification of the amino acid from V to I at position 173.
+The protein's natural variant, known as in strain: CNTC 1/82, features a modification of the amino acid from G to GDYG at position 219.
+The protein's natural variant, known as in PRAAS3; digenic inheritance; patient also carries a mutation in PSMB4; patients' cells show reduction of proteasome content and cysteine-type endopeptidase activity of the proteasome;, features a modification of the amino acid from G to D at position 165.
+The protein's natural variant, known as in IDDAS; unknown pathological significance; does not affect nuclear localization; no effect on transcriptional repression of FEZF2; does not affect homodimerization; does not affect interaction with FOXP2;, features a modification of the amino acid from Q to E at position 178.
+The protein's natural variant, known as in IDDAS; de novo variant; localizes to the nucleus but forms abnormal aggregates; no effect on transcriptional repression of FEZF2; does not affect homodimerization; abolishes interaction with FOXP2; does not affect interaction with BCL11A, features a modification of the amino acid from K to E at position 228.
+The protein's natural variant, known as in IDDAS; de novo variant; localizes to the nucleus but forms abnormal aggregates; no effect on transcriptional repression of FEZF2; does not affect homodimerization; severely decreased interaction with FOXP2; loss of interaction with FOXP1; does not affect interaction with BCL11A;, features a modification of the amino acid from W to C at position 271.
+The protein's natural variant, known as in IDDAS; de novo variant; does not affect nuclear localization; no effect on transcriptional repression of FEZF2; does not affect homodimerization; does not affect interaction with FOXP2; does not affect interaction with BCL11A;, features a modification of the amino acid from W to R at position 271.
+The protein's natural variant, known as in IDDAS; unknown pathological significance; does not affect nuclear localization; no effect on transcriptional repression of FEZF2; does not affect homodimerization; does not affect interaction with FOXP2; does not affect interaction with BCL11A;, features a modification of the amino acid from V to M at position 356.
+The protein's natural variant, known as in IDDAS; de novo variant; localizes to the nucleus but forms abnormal aggregates; no effect on transcriptional repression of FEZF2; does not affect homodimerization; abolishes interaction with FOXP2; does not affect interaction with BCL11A;, features a modification of the amino acid from N to H at position 374.
+The protein's natural variant, known as in IDDAS; de novo variant; localizes to the nucleus but forms abnormal aggregates; no effect on transcriptional repression of FEZF2; does not affect homodimerization; severely decreased interaction with FOXP2; loss of interaction with FOXP1; does not affect interaction with BCL11A;, features a modification of the amino acid from K to E at position 389.
+The protein's natural variant, known as in IDDAS; unknown pathological significance; does not affect nuclear localization; no effect on transcriptional repression of FEZF2; does not affect homodimerization; decreased interaction with FOXP2; loss of interaction with BCL11A;, features a modification of the amino acid from Q to R at position 418.
+The protein's natural variant, known as in IDDAS; unknown pathological significance; does not affect nuclear localization; no effect on transcriptional repression of FEZF2; does not affect homodimerization; does not affect interaction with FOXP2; does not affect interaction with BCL11A, features a modification of the amino acid from P to R at position 542.
+The natural variant of this protein is characterized by an amino acid alteration from L to F at position 119.
+The natural variant of this protein is characterized by an amino acid alteration from G to A at position 261.
+The natural variant of this protein is characterized by an amino acid alteration from R to Q at position 323.
+The natural variant of this protein is characterized by an amino acid alteration from F to S at position 379.
+The protein's natural variant, known as in strain: cv. Idared, features a modification of the amino acid from E to K at position 105.
+The protein's natural variant, known as in strain: cv. Aotea, features a modification of the amino acid from I to V at position 113.
+The protein's natural variant, known as in strain: cv. Aotea, features a modification of the amino acid from G to A at position 129.
+The protein's natural variant, known as in strain: cv. Idared, features a modification of the amino acid from T to A at position 130.
+The protein's natural variant, known as in strain: cv. Aotea, features a modification of the amino acid from N to D at position 237.
+The protein's natural variant, known as in strain: cv. Idared, cv. Pinkie, cv. Ralls and cv. Royal Gala, features a modification of the amino acid from I to F at position 281.
+The protein's natural variant, known as in strain: cv. Idared, features a modification of the amino acid from R to G at position 291.
+The protein's natural variant, known as in strain: cv. cv. Idared, cv. Pinkie, cv. Ralls and cv. Royal Gala, features a modification of the amino acid from A to S at position 297.
+The protein's natural variant, known as in strain: cv. Aotea, features a modification of the amino acid from E to Q at position 381.
+The protein's natural variant, known as in strain: cv. Ralls, features a modification of the amino acid from D to G at position 451.
+The protein's natural variant, known as in strain: cv. Aotea, features a modification of the amino acid from K to E at position 505.
+The protein's natural variant, known as in strain: cv. Aotea, features a modification of the amino acid from F to S at position 530.
+The protein's natural variant, known as in strain: cv. Aotea, features a modification of the amino acid from H to Q at position 565.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from V to A at position 275.
+The protein's natural variant, known as in SPGF75; unknown pathological significance, features a modification of the amino acid from A to T at position 660.
+The protein's natural variant, known as in SPGF75; unknown pathological significance, features a modification of the amino acid from R to H at position 1425.
+The protein's natural variant, known as in clone A3, features a modification of the amino acid from E to K at position 59.
+The natural variant of this protein is characterized by an amino acid alteration from T to A at position 103.
+The protein's natural variant, known as in mutant tri3; temporarily insensitive to red light, features a modification of the amino acid from V to F at position 238.
+The protein's natural variant, known as in NFSRA;, features a modification of the amino acid from D to Y at position 165.
+The protein's natural variant, known as in NFSRA, features a modification of the amino acid from F to S at position 176.
+The protein's natural variant, known as in NFSRA, features a modification of the amino acid from R to S at position 189.
+The protein's natural variant, known as in CMT2N;, features a modification of the amino acid from N to Y at position 71.
+The protein's natural variant, known as in DEE29; hypomorphic allele; results in only 2-fold reduction in aminoacylation efficiency;, features a modification of the amino acid from K to T at position 81.
+The protein's natural variant, known as in HDLS2; unknown pathological significance, features a modification of the amino acid from C to F at position 152.
+The protein's natural variant, known as in CMT2N; severely reduces enzyme activity;, features a modification of the amino acid from R to H at position 329.
+The protein's natural variant, known as found in a patient with distal hereditary motor neuropathy; unknown pathological significance, features a modification of the amino acid from T to M at position 608.
+The protein's natural variant, known as in TTD8; unknown pathological significance, features a modification of the amino acid from I to T at position 699.
+The protein's natural variant, known as in TTD8; unknown pathological significance, features a modification of the amino acid from T to A at position 726.
+The protein's natural variant, known as in DEE29; results in 10-fold reduction in aminoacylation efficiency;, features a modification of the amino acid from R to G at position 751.
+The protein's natural variant, known as in TTD8; unknown pathological significance, features a modification of the amino acid from T to I at position 756.
+The protein's natural variant, known as in TTD8; unknown pathological significance, features a modification of the amino acid from C to Y at position 901.
+The protein's natural variant, known as in DEE29; decreases protein abundance; decreases aminoacylation activity; no effect on the editing activity;, features a modification of the amino acid from G to D at position 913.
+The protein's natural variant, known as in par, features a modification of the amino acid from R to G at position 389.
+The protein's natural variant, known as in allele E2063, features a modification of the amino acid from T to I at position 142.
+The protein's natural variant, known as in allele E2006, features a modification of the amino acid from M to I at position 159.
+The protein's natural variant, known as in allele Q77, features a modification of the amino acid from P to S at position 299.
+The protein's natural variant, known as in allele E2143, features a modification of the amino acid from E to K at position 360.
+The protein's natural variant, known as in WNCHRS; results in increased MMP14 proteasomal degradation and reduced protein localization to cell membrane;, features a modification of the amino acid from T to R at position 17.
+The protein's natural variant, known as in strain: W, features a modification of the amino acid from R to Q at position 11.
+The protein's natural variant, known as in strain: W, features a modification of the amino acid from M to T at position 32.
+The protein's natural variant, known as in strain: W, features a modification of the amino acid from T to S at position 45.
+The protein's natural variant, known as in KFS1;, features a modification of the amino acid from G to V at position 42.
+The protein's natural variant, known as in LCA17; reduced protein expression associated with decrease in growth factor activity;, features a modification of the amino acid from D to H at position 57.
+The protein's natural variant, known as in MCOP4;, features a modification of the amino acid from Q to R at position 119.
+The protein's natural variant, known as in LCA17; found also in a patient with microphthalmia isolated with coloboma type 6 carrying a mutation in GDF3; reduced protein expression associated with decrease in growth factor activity;, features a modification of the amino acid from A to T at position 199.
+The protein's natural variant, known as in MCOP4, features a modification of the amino acid from D to G at position 216.
+The protein's natural variant, known as in KFS1, MCOP4 and LCA17; reduced protein expression associated with decrease in growth factor activity;, features a modification of the amino acid from A to E at position 249.
+The protein's natural variant, known as in MCOP4;, features a modification of the amino acid from Q to L at position 253.
+The protein's natural variant, known as in KFS1;, features a modification of the amino acid from L to P at position 289.
+The protein's natural variant, known as in LCA17; increased protein expression associated with decrease in growth factor activity;, features a modification of the amino acid from E to D at position 292.
+The protein's natural variant, known as in MCOP4;, features a modification of the amino acid from P to H at position 327.
+The protein's natural variant, known as in KFS1;, features a modification of the amino acid from K to R at position 424.
+The protein's natural variant, known as in SYNS4; unknown pathological significance;, features a modification of the amino acid from S to R at position 429.
+The protein's natural variant, known as in SYNS4; increases chondrogenic activity; increases SMAD1/5/8 signaling pathway activation; not inhibited by NOG;, features a modification of the amino acid from Y to N at position 444.
+The protein's natural variant, known as in CHTE; impairs IGSF1 trafficking to the plasma membrane, features a modification of the amino acid from S to N at position 765.
+The natural variant of this protein is characterized by an amino acid alteration from E to G at position 774.
+The protein's natural variant, known as in CHTE; impairs IGSF1 trafficking to the plasma membrane;, features a modification of the amino acid from S to F at position 858.
+The protein's natural variant, known as in CHTE; impairs IGSF1 trafficking to the plasma membrane, features a modification of the amino acid from C to R at position 942.
+The protein's natural variant, known as in DIGFAN; increases HUSH-dependent gene silencing;, features a modification of the amino acid from T to I at position 24.
+The protein's natural variant, known as in DIGFAN; increases HUSH-dependent gene silencing;, features a modification of the amino acid from E to K at position 27.
+The protein's natural variant, known as in CMT2Z and DIGFAN; decreased ATPase activity; ATP-independent homodimerization; increases HUSH-dependent gene silencing;, features a modification of the amino acid from S to L at position 87.
+The protein's natural variant, known as in DIGFAN;, features a modification of the amino acid from A to V at position 88.
+The protein's natural variant, known as in CMT2Z; unknown pathological significance;, features a modification of the amino acid from Q to E at position 96.
+The protein's natural variant, known as in DIGFAN; increases HUSH-dependent gene silencing;, features a modification of the amino acid from R to C at position 132.
+The protein's natural variant, known as in CMT2Z; increases HUSH-dependent gene silencing;, features a modification of the amino acid from E to G at position 236.
+The protein's natural variant, known as in CMT2Z; slightly decreased ATPase activity; increases HUSH-dependent gene silencing;, features a modification of the amino acid from R to W at position 252.
+The protein's natural variant, known as in DIGFAN; increases HUSH-dependent gene silencing;, features a modification of the amino acid from R to S at position 266.
+The protein's natural variant, known as in DIGFAN;, features a modification of the amino acid from S to R at position 388.
+The protein's natural variant, known as in DIGFAN and CMT2Z;, features a modification of the amino acid from Y to C at position 394.
+The protein's natural variant, known as in CMT2Z, features a modification of the amino acid from Q to R at position 400.
+The protein's natural variant, known as in CMT2Z;, features a modification of the amino acid from C to Y at position 407.
+The protein's natural variant, known as in DIGFAN; increases HUSH-dependent gene silencing;, features a modification of the amino acid from V to F at position 413.
+The protein's natural variant, known as probable disease-associated variant found in a child with spinal atrophy-phenotype, cerebellar atrophy and diaphragmatic paralysis; also found in a second child with early onset cerebellar ataxia, axonal polyneuropathy and nocturanl hypoventilation; increased ATPase activity; increased rate of dimer assembly and disassembly; decreased HUSH-dependent gene silencing, features a modification of the amino acid from T to R at position 424.
+The protein's natural variant, known as in CMT2Z;, features a modification of the amino acid from A to V at position 431.
+The protein's natural variant, known as in CMT2Z; unknown pathological significance, features a modification of the amino acid from G to R at position 444.
+The natural variant of this protein is characterized by an amino acid alteration from D to H at position 466.
+The protein's natural variant, known as in CMT2Z; unknown pathological significance, features a modification of the amino acid from D to N at position 466.
+The protein's natural variant, known as in CMT2Z; unknown pathological significance;, features a modification of the amino acid from H to R at position 798.
+The protein's natural variant, known as in allele A22, features a modification of the amino acid from P to S at position 171.
+The protein's natural variant, known as in allele A206, features a modification of the amino acid from S to L at position 261.
+The protein's natural variant, known as no effect on binding of the molybdenum cofactor; no significant effect on catalytic efficiency toward benzamidoxime; no significant effect on affinity for benzamidoxime;, features a modification of the amino acid from V to L at position 96.
+The protein's natural variant, known as no effect on binding of the molybdenum cofactor; no significant effect on catalytic efficiency toward benzamidoxime; no significant effect on affinity for benzamidoxime;, features a modification of the amino acid from T to A at position 165.
+The protein's natural variant, known as no effect on binding of the molybdenum cofactor; no significant effect on catalytic efficiency toward benzamidoxime; no significant effect on affinity for benzamidoxime;, features a modification of the amino acid from M to K at position 187.
+The protein's natural variant, known as no effect on binding of the molybdenum cofactor; no significant effect on catalytic efficiency toward benzamidoxime; no significant effect on affinity for benzamidoxime;, features a modification of the amino acid from C to S at position 246.
+The protein's natural variant, known as no effect on binding of the molybdenum cofactor; no significant effect on catalytic efficiency toward benzamidoxime; no significant effect on affinity for benzamidoxime;, features a modification of the amino acid from D to H at position 247.
+The protein's natural variant, known as no effect on binding of the molybdenum cofactor; no significant effect on catalytic efficiency toward benzamidoxime; no significant effect on affinity for benzamidoxime;, features a modification of the amino acid from M to I at position 268.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from L to P at position 140.
+The protein's natural variant, known as depending on subunit, features a modification of the amino acid from P to D at position 24.
+The protein's natural variant, known as depending on subunit, features a modification of the amino acid from K to E at position 26.
+The protein's natural variant, known as depending on subunit, features a modification of the amino acid from K to E at position 29.
+The protein's natural variant, known as depending on subunit, features a modification of the amino acid from NP to DE at position 39.
+The protein's natural variant, known as depending on subunit, features a modification of the amino acid from K to E at position 59.
+The protein's natural variant, known as depending on subunit, features a modification of the amino acid from R to H at position 80.
+The protein's natural variant, known as depending on subunit, features a modification of the amino acid from A to E at position 84.
+The protein's natural variant, known as depending on subunit, features a modification of the amino acid from A to Q at position 84.
+The protein's natural variant, known as depending on subunit, features a modification of the amino acid from Q to K at position 174.
+The protein's natural variant, known as depending on subunit, features a modification of the amino acid from R to K at position 177.
+The protein's natural variant, known as depending on subunit, features a modification of the amino acid from TH to IR at position 276.
+The protein's natural variant, known as depending on subunit, features a modification of the amino acid from R to H at position 287.
+The protein's natural variant, known as depending on subunit, features a modification of the amino acid from N to S at position 294.
+The protein's natural variant, known as depending on subunit, features a modification of the amino acid from DNIAI to NGVPL at position 418.
+The protein's natural variant, known as depending on subunit, features a modification of the amino acid from H to R at position 421.
+The protein's natural variant, known as depending on subunit, features a modification of the amino acid from T to I at position 423.
+The protein's natural variant, known as depending on subunit, features a modification of the amino acid from E to K at position 444.
+The protein's natural variant, known as depending on subunit, features a modification of the amino acid from E to A at position 447.
+The protein's natural variant, known as depending on subunit, features a modification of the amino acid from D to E at position 463.
+The protein's natural variant, known as depending on subunit, features a modification of the amino acid from D to I at position 463.
+The protein's natural variant, known as depending on subunit, features a modification of the amino acid from E to D at position 465.
+The protein's natural variant, known as depending on subunit, features a modification of the amino acid from R to L at position 467.
+The protein's natural variant, known as depending on subunit, features a modification of the amino acid from R to S at position 467.
+The protein's natural variant, known as depending on subunit, features a modification of the amino acid from H to N at position 469.
+The protein's natural variant, known as depending on subunit, features a modification of the amino acid from E to D at position 471.
+The protein's natural variant, known as depending on subunit, features a modification of the amino acid from K to H at position 474.
+The protein's natural variant, known as depending on subunit, features a modification of the amino acid from L to Q at position 615.
+The protein's natural variant, known as depending on subunit, features a modification of the amino acid from L to S at position 626.
+The protein's natural variant, known as depending on subunit, features a modification of the amino acid from D to N at position 652.
+The protein's natural variant, known as in CASVDD; unknown pathological significance;, features a modification of the amino acid from P to L at position 261.
+The protein's natural variant, known as found in a patient with progressive myoclonus epilepsy and developmental delay; unknown pathological significance, features a modification of the amino acid from Y to C at position 371.
+The protein's natural variant, known as in CASVDD; impaired regulation of current density and inactivation kinetics of N- and L-type calcium channels;, features a modification of the amino acid from L to P at position 1047.
+The protein's natural variant, known as in CASVDD; unknown pathological significance;, features a modification of the amino acid from L to P at position 1053.
+The natural variant of this protein is characterized by an amino acid alteration from E to Q at position 188.
+The protein's natural variant, known as in strain: 386A and 387A, features a modification of the amino acid from F to L at position 13.
+The protein's natural variant, known as in strain: 405A, features a modification of the amino acid from H to P at position 19.
+The protein's natural variant, known as in strain: 509A, features a modification of the amino acid from T to A at position 38.
+The protein's natural variant, known as in strain: 10A, 100A, 101A, 149A, 158A, 189A, 195A, 223A, 233A, 237A, 28A, 303A, 312A, 319A, 324A, 325A, 32A, 335A, 340A, 348A, 350A, 352A, 356A, 358A, 359A, 360A, 362A, 365A, 367A, 371A, 380A, 383A, 386A, 387A, 390A, 393A, 398A, 40A, 405A, 41A, 443A, 486A, 514A, 517A, 528A, 554A, 59A, 627A, 639A, 672A, 703A, 707A, 712A, 730A, 739A, 761A, 762A, 767A, 770A, 786A, 788A, 793A, 804A, 820A, 833A, 834A, 836A, 849A, 850A, 851A, 852A, 853A and 855A, features a modification of the amino acid from E to D at position 82.
+The protein's natural variant, known as in strain: 10A, 336A, 338A, 581A, 663A, 786A and 911A, features a modification of the amino acid from T to S at position 117.
+The protein's natural variant, known as in strain: 788A, features a modification of the amino acid from L to R at position 140.
+The protein's natural variant, known as in allele HCR*WWCC; associated with psoriasis;, features a modification of the amino acid from R to W at position 103.
+The protein's natural variant, known as in allele HCR*WWCC; associated with psoriasis;, features a modification of the amino acid from R to W at position 109.
+The protein's natural variant, known as in allele HCR*WWCC; associated with psoriasis;, features a modification of the amino acid from G to C at position 575.
+The protein's natural variant, known as in allele HCR*WWCC; associated with psoriasis;, features a modification of the amino acid from S to C at position 776.
+The protein's natural variant, known as in DFNA15, features a modification of the amino acid from D to V at position 64.
+The protein's natural variant, known as in DFNA15; unknown pathological significance;, features a modification of the amino acid from P to R at position 164.
+The protein's natural variant, known as in DFNA15, features a modification of the amino acid from F to Y at position 194.
+The protein's natural variant, known as in DFNA15, features a modification of the amino acid from S to L at position 222.
+The protein's natural variant, known as in DFNA15; decreases subcellular localization in the nucleus; decreases DNA-binding activity; decreases transcriptional activity;, features a modification of the amino acid from L to P at position 223.
+The protein's natural variant, known as in DFNA15; unknown pathological significance, features a modification of the amino acid from E to K at position 232.
+The protein's natural variant, known as in DFNA15, features a modification of the amino acid from N to Y at position 240.
+The protein's natural variant, known as in DFNA15, features a modification of the amino acid from I to V at position 281.
+The protein's natural variant, known as in DFNA15; decreases subcellular localization in the nucleus; decreases DNA-binding activity; decreases transcriptional activity;, features a modification of the amino acid from L to F at position 289.
+The protein's natural variant, known as in DFNA15, features a modification of the amino acid from P to L at position 299.
+The protein's natural variant, known as in DFNA15;, features a modification of the amino acid from R to K at position 326.
+The protein's natural variant, known as in DFNA15; decreases subcellular localization in the nucleus;, features a modification of the amino acid from K to E at position 328.
+The protein's natural variant, known as in strain: W, features a modification of the amino acid from I to V at position 132.
+The protein's natural variant, known as in strain: W, features a modification of the amino acid from I to V at position 344.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from G to D at position 86.
+The protein's natural variant, known as in strain: NCTC 11638, features a modification of the amino acid from S to G at position 2.
+The protein's natural variant, known as in strain: NCTC 11638, features a modification of the amino acid from D to N at position 14.
+The protein's natural variant, known as in strain: NCTC 11638, features a modification of the amino acid from S to N at position 33.
+The protein's natural variant, known as in strain: NCTC 11638, features a modification of the amino acid from K to E at position 192.
+The protein's natural variant, known as in strain: NCTC 11638, features a modification of the amino acid from V to VQNA at position 196.
+The protein's natural variant, known as found in a renal cell carcinoma sample; somatic mutation, features a modification of the amino acid from R to P at position 1400.
+The protein's natural variant, known as found in familial late-onset hereditary ataxia; unknown pathological significance;, features a modification of the amino acid from E to V at position 85.
+The protein's natural variant, known as in PCH4;, features a modification of the amino acid from S to P at position 93.
+The protein's natural variant, known as in PCH2A, features a modification of the amino acid from Y to D at position 119.
+The protein's natural variant, known as in PCH2A and PCH4;, features a modification of the amino acid from A to S at position 307.
+The protein's natural variant, known as in strain: ECOR 30, features a modification of the amino acid from I to V at position 9.
+The protein's natural variant, known as in strain: ECOR 30, features a modification of the amino acid from SPH to HPQ at position 24.
+The protein's natural variant, known as in strain: ECOR 30, features a modification of the amino acid from K to R at position 30.
+The protein's natural variant, known as in strain: ECOR 30, features a modification of the amino acid from V to I at position 43.
+The protein's natural variant, known as in strain: ECOR 30, features a modification of the amino acid from E to Q at position 51.
+The protein's natural variant, known as in strain: ECOR 30, features a modification of the amino acid from L to M at position 57.
+The protein's natural variant, known as in strain: ECOR 30, features a modification of the amino acid from S to I at position 63.
+The protein's natural variant, known as in ALS6;, features a modification of the amino acid from G to S at position 191.
+The protein's natural variant, known as in ALS6 and ETM4;, features a modification of the amino acid from R to C at position 216.
+The protein's natural variant, known as in ALS6;, features a modification of the amino acid from G to V at position 225.
+The protein's natural variant, known as in ALS6;, features a modification of the amino acid from G to C at position 230.
+The protein's natural variant, known as in ALS6;, features a modification of the amino acid from R to C at position 234.
+The protein's natural variant, known as in ALS6;, features a modification of the amino acid from R to C at position 244.
+The protein's natural variant, known as found in a patient with frontotemporal lobar degeneration;, features a modification of the amino acid from M to V at position 254.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from K to Q at position 312.
+The protein's natural variant, known as in ETM4;, features a modification of the amino acid from P to L at position 431.
+The protein's natural variant, known as in ALS6;, features a modification of the amino acid from G to D at position 507.
+The protein's natural variant, known as in ALS6;, features a modification of the amino acid from R to G at position 514.
+The protein's natural variant, known as in ALS6, features a modification of the amino acid from R to S at position 514.
+The protein's natural variant, known as in ALS6;, features a modification of the amino acid from G to C at position 515.
+The protein's natural variant, known as does not affect protein nuclear localization;, features a modification of the amino acid from H to Q at position 517.
+The protein's natural variant, known as in ALS6;, features a modification of the amino acid from R to K at position 518.
+The protein's natural variant, known as in ALS6; results in aberrant trafficking and cytoplasmic retention of the protein;, features a modification of the amino acid from R to C at position 521.
+The protein's natural variant, known as in ALS6; results in aberrant trafficking and cytoplasmic retention of the protein;, features a modification of the amino acid from R to G at position 521.
+The protein's natural variant, known as in ALS6; results in aberrant trafficking and cytoplasmic retention of the protein;, features a modification of the amino acid from R to H at position 521.
+The protein's natural variant, known as in ALS6;, features a modification of the amino acid from R to G at position 522.
+The protein's natural variant, known as in ALS6;, features a modification of the amino acid from R to S at position 524.
+The protein's natural variant, known as in ALS6;, features a modification of the amino acid from R to T at position 524.
+The protein's natural variant, known as in ALS6;, features a modification of the amino acid from P to L at position 525.
+The protein's natural variant, known as in ALS6; unknown pathological significance, features a modification of the amino acid from Y to YY at position 526.
+The natural variant of this protein is characterized by an amino acid alteration from F to C at position 166.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from L to R at position 152.
+The protein's natural variant, known as in DFNA10;, features a modification of the amino acid from G to R at position 171.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from D to N at position 301.
+The protein's natural variant, known as in DFNA10, features a modification of the amino acid from T to R at position 548.
+The protein's natural variant, known as in MRXSBA; unknown pathological significance;, features a modification of the amino acid from L to P at position 308.
+The protein's natural variant, known as may be a risk factor for autism;, features a modification of the amino acid from I to T at position 869.
+The protein's natural variant, known as in strain: 84-183, features a modification of the amino acid from A to T at position 59.
+The protein's natural variant, known as in strain: 84-183, features a modification of the amino acid from K to R at position 231.
+The protein's natural variant, known as in strain: 84-183, features a modification of the amino acid from I to V at position 259.
+The protein's natural variant, known as in strain: 84-183, features a modification of the amino acid from N to T at position 376.
+The protein's natural variant, known as in strain: 84-183, features a modification of the amino acid from K to Q at position 407.
+The protein's natural variant, known as in strain: 84-183, features a modification of the amino acid from L to S at position 443.
+The protein's natural variant, known as in strain: 84-183, features a modification of the amino acid from A to V at position 475.
+The protein's natural variant, known as in strain: 84-183, features a modification of the amino acid from I to V at position 501.
+The protein's natural variant, known as in strain: 84-183, features a modification of the amino acid from R to K at position 607.
+The protein's natural variant, known as in strain: 84-183, features a modification of the amino acid from CT to HA at position 637.
+The protein's natural variant, known as in MMDS2;, features a modification of the amino acid from I to N at position 67.
+The protein's natural variant, known as in MMDS2;, features a modification of the amino acid from H to R at position 96.
+The protein's natural variant, known as in MPPH2 and melanoma; results in activation of AKT;, features a modification of the amino acid from E to K at position 17.
+The protein's natural variant, known as in a glioblastoma multiforme sample; somatic mutation;, features a modification of the amino acid from G to R at position 171.
+The protein's natural variant, known as in MPPH2;, features a modification of the amino acid from N to S at position 229.
+The protein's natural variant, known as in MPPH2; disease phenotype overlaps with megalencephaly-capillary malformation syndrome;, features a modification of the amino acid from R to W at position 465.
+The protein's natural variant, known as in COQ10D7;, features a modification of the amino acid from L to S at position 52.
+The protein's natural variant, known as in COQ10D7;, features a modification of the amino acid from P to S at position 64.
+The protein's natural variant, known as in COQ10D7;, features a modification of the amino acid from R to G at position 145.
+The protein's natural variant, known as in COQ10D7;, features a modification of the amino acid from R to C at position 240.
+The protein's natural variant, known as in allele TUM-, features a modification of the amino acid from S to N at position 139.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from Q to H at position 21.
+The protein's natural variant, known as in strain: msh9, features a modification of the amino acid from G to S at position 220.
+The protein's natural variant, known as in strain: afc1, afc7, f17, m32, msh9, msh37, ps1, ps2, ps3, ps9, ps10, ps11, ps12, ps14 and ps15, features a modification of the amino acid from H to P at position 221.
+The protein's natural variant, known as in strain: m32, msh37, ps14 and ps15, features a modification of the amino acid from S to T at position 267.
+The protein's natural variant, known as in strain: afc1, m32, msh37, ps14 and ps15, features a modification of the amino acid from I to V at position 289.
+The protein's natural variant, known as in strain: ps4, features a modification of the amino acid from T to A at position 315.
+The protein's natural variant, known as in strain: f17, features a modification of the amino acid from T to A at position 367.
+The protein's natural variant, known as in strain: f17, features a modification of the amino acid from K to R at position 382.
+The protein's natural variant, known as in THMD5;, features a modification of the amino acid from L to P at position 40.
+The protein's natural variant, known as in THMD5;, features a modification of the amino acid from N to H at position 50.
+The protein's natural variant, known as in THMD5;, features a modification of the amino acid from N to S at position 219.
+The protein's natural variant, known as in a lung large cell carcinoma sample; somatic mutation, features a modification of the amino acid from R to G at position 47.
+The protein's natural variant, known as in a melanoma sample; somatic mutation, features a modification of the amino acid from R to K at position 166.
+The protein's natural variant, known as in CHDSKM; increases kinase activity; no effect on protein levels;, features a modification of the amino acid from Y to C at position 226.
+The protein's natural variant, known as in CHDSKM; increases kinase activity; no effect on protein levels;, features a modification of the amino acid from A to T at position 337.
+The protein's natural variant, known as in CMT1J; decreased inositol trisphosphate-mediated calcium release and altered calcium homeostasis in patient fibroblasts, features a modification of the amino acid from V to M at position 615.
+The protein's natural variant, known as in CMT1J; unknown pathological significance, features a modification of the amino acid from T to M at position 1424.
+The protein's natural variant, known as in CMT1J, features a modification of the amino acid from R to C at position 2524.
+The protein's natural variant, known as in TRPS3; in heterozygous status has a milder effect causing TRPS1, features a modification of the amino acid from V to D at position 894.
+The protein's natural variant, known as in TRPS3; severe;, features a modification of the amino acid from T to P at position 901.
+The protein's natural variant, known as in TRPS3; severe, features a modification of the amino acid from R to P at position 908.
+The protein's natural variant, known as in TRPS3;, features a modification of the amino acid from R to Q at position 908.
+The protein's natural variant, known as in TRPS3;, features a modification of the amino acid from A to T at position 919.
+The protein's natural variant, known as in TRPS1; prevents the transport into the nucleus and thus reduces the nuclear TRPS1 concentration consistent with haploinsufficiency;, features a modification of the amino acid from R to C at position 952.
+The protein's natural variant, known as in TRPS1; prevents the transport into the nucleus and thus reduces the nuclear TRPS1 concentration consistent with haploinsufficiency;, features a modification of the amino acid from R to H at position 952.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from G to S at position 188.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from E to K at position 242.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from G to R at position 358.
+The protein's natural variant, known as in BBIS; localizes to the cytoplasm and not to the nucleus;, features a modification of the amino acid from G to R at position 46.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from I to V at position 367.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from K to R at position 379.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from I to M at position 405.
+The protein's natural variant, known as in strain: CWL029 and TW-183, features a modification of the amino acid from T to M at position 140.
+The protein's natural variant, known as in AGS6;, features a modification of the amino acid from P to A at position 193.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from E to V at position 806.
+The protein's natural variant, known as in AGS6;, features a modification of the amino acid from A to T at position 870.
+The protein's natural variant, known as in AGS6;, features a modification of the amino acid from I to T at position 872.
+The protein's natural variant, known as in AGS6;, features a modification of the amino acid from R to H at position 892.
+The protein's natural variant, known as in DSH;, features a modification of the amino acid from L to P at position 923.
+The protein's natural variant, known as in DSH, features a modification of the amino acid from C to F at position 966.
+The protein's natural variant, known as in AGS6;, features a modification of the amino acid from K to N at position 999.
+The protein's natural variant, known as in AGS6;, features a modification of the amino acid from G to R at position 1007.
+The protein's natural variant, known as in AGS6;, features a modification of the amino acid from Y to F at position 1112.
+The protein's natural variant, known as in AGS6;, features a modification of the amino acid from D to H at position 1113.
+The protein's natural variant, known as in DSH;, features a modification of the amino acid from R to W at position 1155.
+The protein's natural variant, known as in DSH;, features a modification of the amino acid from F to S at position 1165.
+The protein's natural variant, known as in strain: CC-503, features a modification of the amino acid from R to Q at position 476.
+The protein's natural variant, known as in strain: CC-503, features a modification of the amino acid from Q to R at position 529.
+The protein's natural variant, known as in FHA1; Alabama;, features a modification of the amino acid from P to L at position 85.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from E to D at position 210.
+The protein's natural variant, known as associated with a decreased severity of CAD;, features a modification of the amino acid from R to K at position 219.
+The protein's natural variant, known as in TGD; deficient cellular cholesterol efflux;, features a modification of the amino acid from A to T at position 255.
+The protein's natural variant, known as in TGD, features a modification of the amino acid from E to K at position 284.
+The protein's natural variant, known as in TGD, features a modification of the amino acid from Y to C at position 482.
+The protein's natural variant, known as associated with increased plasma HDL cholesterol;, features a modification of the amino acid from R to W at position 496.
+The protein's natural variant, known as in TGD;, features a modification of the amino acid from R to W at position 587.
+The protein's natural variant, known as in TGD;, features a modification of the amino acid from W to L at position 590.
+The protein's natural variant, known as in TGD; moderately decreased protein abundance; highly decreased ATPase activity; highly decreased phospholipid translocase activity;, features a modification of the amino acid from W to S at position 590.
+The protein's natural variant, known as in TGD;, features a modification of the amino acid from Q to R at position 597.
+The protein's natural variant, known as associated with reduced plasma HDL cholesterol;, features a modification of the amino acid from R to Q at position 638.
+The protein's natural variant, known as associated with HDL cholesterol;, features a modification of the amino acid from V to M at position 771.
+The natural variant of this protein is characterized by an amino acid alteration from T to S at position 774.
+The protein's natural variant, known as may be associated with increased risk of ischemic heart disease;, features a modification of the amino acid from K to N at position 776.
+The protein's natural variant, known as associated with reduced plasma HDL cholesterol;, features a modification of the amino acid from E to G at position 815.
+The protein's natural variant, known as associated with higher plasma cholesterol;, features a modification of the amino acid from V to I at position 825.
+The protein's natural variant, known as in TGD;, features a modification of the amino acid from W to R at position 840.
+The protein's natural variant, known as associated with higher plasma cholesterol;, features a modification of the amino acid from I to M at position 883.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from D to Y at position 917.
+The protein's natural variant, known as in TGD; moderately decreased protein abundance; highly decreased ATPase activity; highly decreased phospholipid translocase activity; loss protein subcellular localization to the plasma membrane, features a modification of the amino acid from T to I at position 929.
+The protein's natural variant, known as in TGD;, features a modification of the amino acid from N to H at position 935.
+The protein's natural variant, known as in TGD; moderately decreased protein abundance; highly decreased ATPase activity; highly decreased phospholipid translocase activity;, features a modification of the amino acid from N to S at position 935.
+The protein's natural variant, known as in TGD;, features a modification of the amino acid from A to V at position 937.
+The protein's natural variant, known as in TGD;, features a modification of the amino acid from A to D at position 1046.
+The natural variant of this protein is characterized by an amino acid alteration from P to S at position 1065.
+The protein's natural variant, known as in TGD;, features a modification of the amino acid from R to C at position 1068.
+The protein's natural variant, known as in FHA1; loss of localization to plasma membrane; decreased cholesterol efflux; decreased phospholipid efflux, features a modification of the amino acid from M to T at position 1091.
+The protein's natural variant, known as in FHA1;, features a modification of the amino acid from D to Y at position 1099.
+The protein's natural variant, known as associated with premature coronary heart disease;, features a modification of the amino acid from E to D at position 1172.
+The protein's natural variant, known as associated with reduced plasma HDL cholesterol;, features a modification of the amino acid from S to F at position 1181.
+The protein's natural variant, known as in TGD;, features a modification of the amino acid from D to N at position 1289.
+The protein's natural variant, known as associated with reduced plasma HDL cholesterol;, features a modification of the amino acid from R to T at position 1341.
+The protein's natural variant, known as in TGD; the mutant protein is retained in the endoplasmic reticulum while the wild-type protein is located at the plasma membrane, features a modification of the amino acid from L to F at position 1379.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from A to T at position 1407.
+The protein's natural variant, known as in TGD; loss of interaction with APOE; unable to generate APOE-containing high density lipoproteins; moderately decreased protein abundance; moderately decreased ATPase activity; moderately decreased phospholipid translocase activity;, features a modification of the amino acid from C to R at position 1477.
+The protein's natural variant, known as in TGD;, features a modification of the amino acid from S to L at position 1506.
+The protein's natural variant, known as in TGD, features a modification of the amino acid from I to R at position 1517.
+The protein's natural variant, known as associated with HDL cholesterol;, features a modification of the amino acid from K to R at position 1587.
+The protein's natural variant, known as probable disease-associated variant; associated with atherosclerosis; deficient cellular cholesterol efflux, features a modification of the amino acid from N to D at position 1611.
+The protein's natural variant, known as associated with reduced plasma HDL cholesterol;, features a modification of the amino acid from R to Q at position 1615.
+The protein's natural variant, known as associated with reduced plasma HDL cholesterol;, features a modification of the amino acid from A to T at position 1670.
+The protein's natural variant, known as associated with increased plasma HDL cholesterol;, features a modification of the amino acid from R to Q at position 1680.
+The protein's natural variant, known as in TGD;, features a modification of the amino acid from R to W at position 1680.
+The protein's natural variant, known as in TGD; the mutant protein is retained in the endoplasmic reticulum while the wild-type protein is located at the plasma membrane, features a modification of the amino acid from V to D at position 1704.
+The protein's natural variant, known as in TGD;, features a modification of the amino acid from N to H at position 1800.
+The protein's natural variant, known as in TGD;, features a modification of the amino acid from R to Q at position 1851.
+The protein's natural variant, known as in FHA1; uncertain pathological significance;, features a modification of the amino acid from R to W at position 1897.
+The protein's natural variant, known as in TGD, features a modification of the amino acid from R to S at position 1901.
+The protein's natural variant, known as in Scott syndrome; shows impaired trafficking of the mutant protein to the plasma membrane;, features a modification of the amino acid from R to Q at position 1925.
+The protein's natural variant, known as in FHA1;, features a modification of the amino acid from F to S at position 2009.
+The protein's natural variant, known as in TGD; highly decreased protein abundance; highly decreased ATPase activity; highly decreased phospholipid translocase activity; loss protein subcellular localization to the plasma membrane;, features a modification of the amino acid from R to W at position 2081.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from A to T at position 2109.
+The protein's natural variant, known as in FHA1; moderately decreased protein abundance; does not affect ATPase activity; moderately decreased phospholipid translocase activity;, features a modification of the amino acid from P to L at position 2150.
+The protein's natural variant, known as could be associated with reduced plasma HDL cholesterol, features a modification of the amino acid from F to S at position 2163.
+The protein's natural variant, known as in TGD;, features a modification of the amino acid from Q to H at position 2196.
+The protein's natural variant, known as could be associated with reduced plasma HDL cholesterol;, features a modification of the amino acid from V to I at position 2244.
+The protein's natural variant, known as in CTRCT50, features a modification of the amino acid from I to M at position 65.
+The protein's natural variant, known as in NEDFSS; gain-of-function variant resulting in increased calcium ion transmembrane transport; basal channel activity is increased and the channel is more sensitive to stimulation by heat or the neurosteroid pregnenolone sulfate; the mutant channel can be down-regulated by the TRPM3 antagonist and anti-epileptic drug primidone, features a modification of the amino acid from V to M at position 1015.
+The protein's natural variant, known as in NEDFSS; gain-of-function variant resulting in increased calcium ion transmembrane transport; basal channel activity is increased and the channel is more sensitive to stimulation by heat or the neurosteroid pregnenolone sulfate; the mutant channel can be inhibited by the TRPM3 antagonist and anti-epileptic drug primidone, features a modification of the amino acid from P to Q at position 1115.
+The protein's natural variant, known as in NEDFSS; unknown pathological significance, features a modification of the amino acid from S to T at position 1380.
+The protein's natural variant, known as in CRJS; constitutive activation of the smoothened signaling pathway;, features a modification of the amino acid from L to F at position 412.
+The protein's natural variant, known as in basal cell carcinoma and ameloblastoma samples; somatic mutation; constitutive activation of the smoothened signaling pathway;, features a modification of the amino acid from W to L at position 535.
+The protein's natural variant, known as in basal cell carcinoma samples; somatic mutation;, features a modification of the amino acid from R to Q at position 562.
+The protein's natural variant, known as in strain: CWL029 and TW-183, features a modification of the amino acid from G to R at position 353.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from M to T at position 248.
+The protein's natural variant, known as in MRLS; unknown pathological significance;, features a modification of the amino acid from G to S at position 80.
+The protein's natural variant, known as in SEMDX; reduced protein stability;, features a modification of the amino acid from K to E at position 147.
+The protein's natural variant, known as in SEMDX;, features a modification of the amino acid from G to V at position 259.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from R to T at position 266.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from K to N at position 288.
+The protein's natural variant, known as in MRLS; unknown pathological significance;, features a modification of the amino acid from Q to P at position 303.
+The natural variant of this protein is characterized by an amino acid alteration from V to A at position 215.
+The natural variant of this protein is characterized by an amino acid alteration from L to S at position 241.
+The natural variant of this protein is characterized by an amino acid alteration from F to L at position 303.
+The natural variant of this protein is characterized by an amino acid alteration from T to I at position 369.
+The protein's natural variant, known as in DBA1; affects protein stability; does not localize to the nucleolus;, features a modification of the amino acid from V to F at position 15.
+The protein's natural variant, known as in DBA1;, features a modification of the amino acid from A to P at position 17.
+The protein's natural variant, known as in DBA1, features a modification of the amino acid from LA to E at position 19.
+The protein's natural variant, known as in DBA1; affects protein stability; does not localize to the nucleolus; affects assembly into a functional ribosomal subunit, features a modification of the amino acid from L to P at position 18.
+The protein's natural variant, known as in DBA1, features a modification of the amino acid from L to R at position 18.
+The protein's natural variant, known as in DBA1, features a modification of the amino acid from F to S at position 21.
+The protein's natural variant, known as in DBA1; affects assembly into a functional ribosomal subunit, features a modification of the amino acid from P to L at position 47.
+The protein's natural variant, known as in DBA1, features a modification of the amino acid from W to C at position 52.
+The protein's natural variant, known as in DBA1; affects assembly into a functional ribosomal subunit, features a modification of the amino acid from W to R at position 52.
+The protein's natural variant, known as in DBA1;, features a modification of the amino acid from T to M at position 55.
+The protein's natural variant, known as in DBA1; affects assembly into a functional ribosomal subunit, features a modification of the amino acid from R to Q at position 56.
+The protein's natural variant, known as in DBA1; affects protein stability; does not localize to the nucleolus; affects assembly into a functional ribosomal subunit, features a modification of the amino acid from A to P at position 57.
+The protein's natural variant, known as in DBA1, features a modification of the amino acid from S to F at position 59.
+The protein's natural variant, known as in DBA1; does not localize to the nucleolus; affects assembly into a functional ribosomal subunit, features a modification of the amino acid from A to E at position 61.
+The protein's natural variant, known as in DBA1; affects assembly into a functional ribosomal subunit;, features a modification of the amino acid from R to Q at position 62.
+The protein's natural variant, known as in DBA1; increased protein degradation; affects assembly into a functional ribosomal subunit;, features a modification of the amino acid from R to W at position 62.
+The protein's natural variant, known as in DBA1, features a modification of the amino acid from L to P at position 64.
+The protein's natural variant, known as in DBA1, features a modification of the amino acid from T to P at position 76.
+The protein's natural variant, known as in DBA1, features a modification of the amino acid from IYGGRQ to R at position 83.
+The protein's natural variant, known as in DBA1; increased protein degradation; affects assembly into a functional ribosomal subunit, features a modification of the amino acid from R to H at position 101.
+The protein's natural variant, known as in DBA1, features a modification of the amino acid from G to R at position 120.
+The protein's natural variant, known as in DBA1; affects protein stability; does not localize to the nucleolus; affects assembly into a functional ribosomal subunit;, features a modification of the amino acid from G to E at position 127.
+The protein's natural variant, known as in DBA1, features a modification of the amino acid from L to P at position 131.
+The protein's natural variant, known as in DBA1, features a modification of the amino acid from L to R at position 131.
+The protein's natural variant, known as in DBA1, features a modification of the amino acid from A to T at position 135.
+The protein's natural variant, known as in strain: W, features a modification of the amino acid from K to E at position 42.
+The protein's natural variant, known as in strain: W, features a modification of the amino acid from L to I at position 59.
+The protein's natural variant, known as in CDG1P; does not affect subcellular localization; results in the accumulation of under-glycosylated proteins;, features a modification of the amino acid from L to S at position 86.
+The protein's natural variant, known as in CDG1P;, features a modification of the amino acid from Y to S at position 279.
+The protein's natural variant, known as in CDG1P;, features a modification of the amino acid from Q to P at position 318.
+The protein's natural variant, known as in CDG1P;, features a modification of the amino acid from L to S at position 381.
+The protein's natural variant, known as in CDG1P;, features a modification of the amino acid from E to K at position 398.
+The protein's natural variant, known as in strain: ATCC 6633, features a modification of the amino acid from ND to TE at position 85.
+The protein's natural variant, known as in strain: ATCC 6633, features a modification of the amino acid from M to K at position 88.
+The protein's natural variant, known as in strain: ATCC 6633, features a modification of the amino acid from S to N at position 118.
+The protein's natural variant, known as in strain: ATCC 6633, features a modification of the amino acid from A to S at position 155.
+The protein's natural variant, known as in strain: ATCC 6633, features a modification of the amino acid from H to Q at position 171.
+The protein's natural variant, known as in strain: PAZ11; resistant to triadimenol; a sterol demethylation-inhibiting fungicide, features a modification of the amino acid from Y to F at position 136.
+The protein's natural variant, known as found in a patient with autism spectrum disorder; unknown pathological significance;, features a modification of the amino acid from D to N at position 11.
+The protein's natural variant, known as in IECEE3; unknown pathological significance;, features a modification of the amino acid from P to R at position 27.
+The protein's natural variant, known as in ARCL2D;, features a modification of the amino acid from G to D at position 72.
+The protein's natural variant, known as in IECEE3; loss-of-function variant leading to increased pH in intracellular organelles; affects neurite arborization and impairs the formation and maintenance of excitatory synapses, when tested in a heterologous system; not effect on subcellular location;, features a modification of the amino acid from D to Y at position 100.
+The protein's natural variant, known as found in a patient with severe developmental disorder; unknown pathological significance, features a modification of the amino acid from P to R at position 249.
+The protein's natural variant, known as in ARCL2D;, features a modification of the amino acid from R to C at position 338.
+The protein's natural variant, known as in IECEE3; gain-of-function variant leading to decreased pH in intracellular organelles; affects neurite arborization and impairs the formation and maintenance of excitatory synapses, when tested in a heterologous system; not effect on subcellular location;, features a modification of the amino acid from D to N at position 349.
+The protein's natural variant, known as in IECEE3; unknown pathological significance, features a modification of the amino acid from D to G at position 371.
+The protein's natural variant, known as in C9D;, features a modification of the amino acid from C to G at position 119.
+The protein's natural variant, known as in ARMD15;, features a modification of the amino acid from P to S at position 167.
+The natural variant of this protein is characterized by an amino acid alteration from S to N at position 162.
+The natural variant of this protein is characterized by an amino acid alteration from T to P at position 790.
+The protein's natural variant, known as in AAT9; expression of the mutant protein is significantly decreased;, features a modification of the amino acid from W to L at position 21.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from V to D at position 61.
+The protein's natural variant, known as in second component, features a modification of the amino acid from A to T at position 48.
+The protein's natural variant, known as found in a patient with autism spectrum disorder; unknown pathological significance, features a modification of the amino acid from R to G at position 111.
+The protein's natural variant, known as found in a patient with autism spectrum disorder; unknown pathological significance, features a modification of the amino acid from G to R at position 373.
+The protein's natural variant, known as found in a patient with autism spectrum disorder; unknown pathological significance;, features a modification of the amino acid from V to L at position 641.
+The protein's natural variant, known as found in a patient with schizophrenia; unknown pathological significance;, features a modification of the amino acid from I to N at position 1028.
+The protein's natural variant, known as in allele CYP8A1*2;, features a modification of the amino acid from P to L at position 38.
+The protein's natural variant, known as in allele CYP8A1*3;, features a modification of the amino acid from S to R at position 118.
+The protein's natural variant, known as in allele CYP8A1*4;, features a modification of the amino acid from R to S at position 379.
+The protein's natural variant, known as in allele CYP8A1*5; results in a significantly decreased enzyme activity;, features a modification of the amino acid from A to T at position 447.
+The protein's natural variant, known as in an ovarian mucinous carcinoma sample; somatic mutation;, features a modification of the amino acid from V to M at position 104.
+The protein's natural variant, known as in VSCN1; almost complete loss of ERBB2 and ERBB3 phosphorylation in the presence or in the absence of NRG1 stimulation, suggesting alteration of downstream signaling; does not affect the subcellular localization at the cell membrane, features a modification of the amino acid from T to P at position 787.
+The protein's natural variant, known as in VSCN1; unknown pathological significance; some decrease in ERBB2 phosphorylation upon NG1 treatment, compared to wild-type; does not affect the subcellular localization at the cell membrane, features a modification of the amino acid from T to S at position 873.
+The protein's natural variant, known as in VSCN1; almost complete loss of ERBB2 and ERBB3 phosphorylation in the presence or in the absence of NRG1 stimulation, suggesting alteration of downstream signaling; does not affect the subcellular localization at the cell membrane, features a modification of the amino acid from V to M at position 899.
+The protein's natural variant, known as in VSCN1; unknown pathological significance; some decrease in ERBB2 phosphorylation upon NG1 treatment, compared to wild-type; does not affect the subcellular localization at the cell membrane, features a modification of the amino acid from Q to R at position 932.
+The protein's natural variant, known as in FERLK; risk factor for erythroleukemia; results in increased ERBB-mediated signaling; results in a block of erythroid differentiation and increased cell proliferation;, features a modification of the amino acid from A to T at position 1337.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from E to K at position 7.
+The protein's natural variant, known as in MDDGC7, features a modification of the amino acid from A to T at position 53.
+The protein's natural variant, known as in MDDGC7; decreased alpha-dystroglycan glycosylation;, features a modification of the amino acid from G to A at position 54.
+The protein's natural variant, known as in MDDGA7;, features a modification of the amino acid from A to P at position 122.
+The protein's natural variant, known as in MDDGA7; also found in a patient with an atypical phenotype presenting with limb-girdle muscular dystrophy, ocular features and cerebellar involvement;, features a modification of the amino acid from R to H at position 126.
+The protein's natural variant, known as in MDDGC7; atypical form presenting with congenital muscular dystrophy;, features a modification of the amino acid from P to L at position 149.
+The protein's natural variant, known as in MDDGA7;, features a modification of the amino acid from D to N at position 156.
+The protein's natural variant, known as in MDDGA7;, features a modification of the amino acid from R to H at position 205.
+The protein's natural variant, known as in MDDGA7;, features a modification of the amino acid from M to R at position 213.
+The protein's natural variant, known as in MDDGA7;, features a modification of the amino acid from A to D at position 216.
+The protein's natural variant, known as in MDDGC7; atypical form with learning difficulties;, features a modification of the amino acid from Y to C at position 226.
+The protein's natural variant, known as in MDDGA7;, features a modification of the amino acid from Y to H at position 226.
+The protein's natural variant, known as in MDDGA7;, features a modification of the amino acid from T to I at position 238.
+The protein's natural variant, known as in CLIFAHDD;, features a modification of the amino acid from Q to P at position 177.
+The protein's natural variant, known as in CLIFAHDD;, features a modification of the amino acid from L to I at position 312.
+The protein's natural variant, known as found in patients with neurodevelopmental disease and hypotonia; unknown pathological significance, features a modification of the amino acid from L to V at position 312.
+The protein's natural variant, known as in CLIFAHDD;, features a modification of the amino acid from V to G at position 313.
+The protein's natural variant, known as found in patients with distal arthrogryposis and central hypertonia; unknown pathological significance;, features a modification of the amino acid from F to C at position 317.
+The protein's natural variant, known as in CLIFAHDD and IHPRF1; nearly eliminates wild-type protein expression; dominant-negative mutation; decreases membrane expression; induces higher current density and slower inactivation;, features a modification of the amino acid from L to S at position 509.
+The protein's natural variant, known as in CLIFAHDD and IHPRF1; nearly eliminates wild-type protein expression; dominant-negative mutation; decreases membrane expressioninduces higher current density and slower inactivation;, features a modification of the amino acid from Y to S at position 578.
+The protein's natural variant, known as in CLIFAHDD;, features a modification of the amino acid from L to F at position 590.
+The protein's natural variant, known as found in patients with distal arthrogryposis and central hypertonia; unknown pathological significance;, features a modification of the amino acid from V to F at position 595.
+The protein's natural variant, known as found in patients with neurodevelopmental disease and hypotonia; unknown pathological significance, features a modification of the amino acid from V to F at position 1020.
+The protein's natural variant, known as in CLIFAHDD;, features a modification of the amino acid from T to P at position 1165.
+The protein's natural variant, known as in CLIFAHDD; found in patients with neurodevelopmental disease and hypotonia; unknown pathological significance;, features a modification of the amino acid from R to Q at position 1181.
+The protein's natural variant, known as in IHPRF1; loss of function;, features a modification of the amino acid from W to L at position 1287.
+The protein's natural variant, known as in CLIFAHDD;, features a modification of the amino acid from I to M at position 1446.
+The protein's natural variant, known as in strain: Isolate LVT 403, features a modification of the amino acid from V to G at position 123.
+The protein's natural variant, known as in strain: Isolate LVT 403, features a modification of the amino acid from T to A at position 323.
+The protein's natural variant, known as in ARCL1B; does not affect secretion; decreased elastic fiber assembly; loss of interaction with collagen type IV trimer, FBN1, highly glycosylated form of LOX and LTBP1; Does not affect interaction with LOX when LOX is non-glycosylated; proteolyzed by PLG;, features a modification of the amino acid from E to K at position 57.
+The protein's natural variant, known as in ARCL1B; slightly decreased protein abundance in patient dermal fibroblasts; increased transforming growth factor beta receptor signaling pathway in patient fibroblasts; strongly decreased secretion; decreased elastic fiber assembly; loss of interaction with collagen type IV trimer, FBN1 and LTBP1; decreased interaction with LOXL2; new fragments proteolyzed by ELANE; new one fragment proteolyzed by MMP2, features a modification of the amino acid from E to K at position 126.
+The protein's natural variant, known as in ARCL1B, features a modification of the amino acid from E to V at position 126.
+The protein's natural variant, known as in ARCL1B, features a modification of the amino acid from D to A at position 203.
+The protein's natural variant, known as in ARCL1B, features a modification of the amino acid from R to C at position 227.
+The protein's natural variant, known as in ARCL1B; loss of protein expression in patient dermal fibroblasts; increased transforming growth factor beta receptor signaling pathway in patient fibroblasts; loss of protein expression; strongly decreased secretion;, features a modification of the amino acid from C to Y at position 267.
+The protein's natural variant, known as in ARCL1B; loss of secretion;, features a modification of the amino acid from R to C at position 279.
+The protein's natural variant, known as in ARCL1B; increased N-glycosylation; introduced an extra O-glycosylation site; does not affect secretion; decreased elastic fiber assembly; decreased interaction with collagen type IV trimer, FBN1, ELN, LTBP1, LOXL1 and LOXL2; new fragments proteolyzed by ELANE, features a modification of the amino acid from A to T at position 397.
+The protein's natural variant, known as in strain: MT-10509, features a modification of the amino acid from D to N at position 157.
+The protein's natural variant, known as in strain: MT-10509, features a modification of the amino acid from F to Y at position 212.
+The protein's natural variant, known as in strain: MT-10509, features a modification of the amino acid from R to S at position 397.
+The protein's natural variant, known as in strain: MT-10509, features a modification of the amino acid from V to I at position 420.
+The protein's natural variant, known as in allele FN18-, features a modification of the amino acid from E to G at position 67.
+The protein's natural variant, known as in allele FN18-, features a modification of the amino acid from R to Q at position 72.
+The protein's natural variant, known as in BCKDKD; partial loss of kinase activity, features a modification of the amino acid from R to G at position 174.
+The protein's natural variant, known as in BCKDKD;, features a modification of the amino acid from R to P at position 224.
+The protein's natural variant, known as in BCKDKD; complete loss of kinase activity, features a modification of the amino acid from L to P at position 389.
+The protein's natural variant, known as in streptomycin resistant strA1, features a modification of the amino acid from K to R at position 43.
+The protein's natural variant, known as in streptomycin resistant stra1, features a modification of the amino acid from L to V at position 81.
+The protein's natural variant, known as in CMH10; with mid-left ventricular chamber thickening; decrease calcium binding affinity; large increase in its calcium binding affinity upon phosphorylation;, features a modification of the amino acid from A to T at position 13.
+The protein's natural variant, known as in CMH10; decrease calcium binding affinity;, features a modification of the amino acid from F to L at position 18.
+The protein's natural variant, known as in CMH10; some patients present with mid-left ventricular chamber thickening; significantly decrease calcium binding affinity; loss of phosphorylation;, features a modification of the amino acid from E to K at position 22.
+The protein's natural variant, known as in CMH10; impairs calcium binding; bind calcium upon phosphorylation;, features a modification of the amino acid from R to Q at position 58.
+The protein's natural variant, known as in CMH10; with mid-left ventricular chamber thickening; decrease calcium binding affinity;, features a modification of the amino acid from P to A at position 95.
+The protein's natural variant, known as in CMH10;, features a modification of the amino acid from D to V at position 166.
+The protein's natural variant, known as in haplotypes F, G and H, features a modification of the amino acid from M to T at position 41.
+The protein's natural variant, known as in haplotype A, features a modification of the amino acid from P to T at position 340.
+The protein's natural variant, known as in haplotype G, features a modification of the amino acid from L to F at position 451.
+The protein's natural variant, known as in haplotypes K and L, features a modification of the amino acid from T to S at position 477.
+The protein's natural variant, known as in a light-sensitive mutant with reduced activity, features a modification of the amino acid from S to Y at position 222.
+The protein's natural variant, known as in allele Mx1-a, features a modification of the amino acid from M to MVREHET at position 24.
+The natural variant of this protein is characterized by an amino acid alteration from I to M at position 120.
+The protein's natural variant, known as in allele C/D, features a modification of the amino acid from H to P at position 143.
+The protein's natural variant, known as in strain: ATCC 17587, features a modification of the amino acid from S to A at position 38.
+The protein's natural variant, known as in strain: ATCC 17587, features a modification of the amino acid from A to E at position 81.
+The protein's natural variant, known as in strain: ATCC 17587, features a modification of the amino acid from R to K at position 84.
+The protein's natural variant, known as in strain: ATCC 17587, features a modification of the amino acid from S to A at position 87.
+The protein's natural variant, known as in strain: ATCC 17587, features a modification of the amino acid from A to T at position 161.
+The protein's natural variant, known as in strain: ATCC 17587, features a modification of the amino acid from DQAF to GKGI at position 267.
+The protein's natural variant, known as in strain: ATCC 17587, features a modification of the amino acid from I to V at position 273.
+The protein's natural variant, known as in strain: ATCC 17587, features a modification of the amino acid from S to N at position 295.
+The protein's natural variant, known as in strain: ATCC 17587, features a modification of the amino acid from E to D at position 310.
+The protein's natural variant, known as in strain: ATCC 17587, features a modification of the amino acid from Q to R at position 316.
+The protein's natural variant, known as in strain: ATCC 17587, features a modification of the amino acid from A to D at position 324.
+The protein's natural variant, known as in strain: ATCC 17587, features a modification of the amino acid from TSANTKATPVA to VSGGSKANVVT at position 339.
+The protein's natural variant, known as in strain: ATCC 17587, features a modification of the amino acid from I to L at position 347.
+The protein's natural variant, known as in allele KIR3DS1*010;, features a modification of the amino acid from L to S at position 2.
+The protein's natural variant, known as in allele KIR3DS1*014;, features a modification of the amino acid from L to F at position 13.
+The protein's natural variant, known as in allele KIR3DS1*014, features a modification of the amino acid from REW to KEG at position 159.
+The protein's natural variant, known as in allele KIR3DS1*010, features a modification of the amino acid from R to K at position 157.
+The protein's natural variant, known as in allele KIR3DS1*010, features a modification of the amino acid from KCCCNGPRACREQK to NAAVMDQEPAGNRSEQRGF at position 382.
+The protein's natural variant, known as in IMD104;, features a modification of the amino acid from P to S at position 132.
+The protein's natural variant, known as in strain: 61, features a modification of the amino acid from K to R at position 159.
+The protein's natural variant, known as in strain: JHCC4835 and HD-1, features a modification of the amino acid from D to Y at position 233.
+The protein's natural variant, known as in strain: AB88, features a modification of the amino acid from A to V at position 443.
+The protein's natural variant, known as in strain: HD-1 and 61, features a modification of the amino acid from KQ to NE at position 712.
+The protein's natural variant, known as in SFD;, features a modification of the amino acid from S to C at position 179.
+The protein's natural variant, known as in SFD;, features a modification of the amino acid from G to C at position 189.
+The protein's natural variant, known as in SFD, features a modification of the amino acid from G to C at position 190.
+The protein's natural variant, known as in SFD;, features a modification of the amino acid from Y to C at position 191.
+The protein's natural variant, known as in SFD;, features a modification of the amino acid from S to C at position 204.
+The protein's natural variant, known as in CS;, features a modification of the amino acid from Y to C at position 105.
+The protein's natural variant, known as in PS; requires 2 nucleotide substitutions, features a modification of the amino acid from A to F at position 172.
+The protein's natural variant, known as in breast cancer samples; infiltrating ductal carcinoma; somatic mutation, features a modification of the amino acid from R to C at position 203.
+The protein's natural variant, known as in PS;, features a modification of the amino acid from SP to FS at position 253.
+The protein's natural variant, known as in APRS; requires 2 nucleotide substitutions;, features a modification of the amino acid from S to F at position 252.
+The protein's natural variant, known as in APRS and PS; common mutation;, features a modification of the amino acid from S to W at position 252.
+The protein's natural variant, known as in APRS; common mutation;, features a modification of the amino acid from P to R at position 253.
+The protein's natural variant, known as in CS;, features a modification of the amino acid from P to L at position 263.
+The protein's natural variant, known as in CS;, features a modification of the amino acid from S to P at position 267.
+The protein's natural variant, known as in CS, features a modification of the amino acid from T to TG at position 268.
+The protein's natural variant, known as in an ovarian serous carcinoma sample; somatic mutation, features a modification of the amino acid from G to V at position 272.
+The protein's natural variant, known as in CS;, features a modification of the amino acid from F to V at position 276.
+The protein's natural variant, known as in CS, JWS and PS; forms disulfide-linked dimers with constitutive kinase activity, is retained in an intracellular compartment and not detected at the cell surface;, features a modification of the amino acid from C to F at position 278.
+The protein's natural variant, known as in CS;, features a modification of the amino acid from C to Y at position 278.
+The protein's natural variant, known as in CS;, features a modification of the amino acid from Y to C at position 281.
+The protein's natural variant, known as in a lung squamous cell carcinoma sample; somatic mutation, features a modification of the amino acid from D to N at position 283.
+The protein's natural variant, known as in CS, features a modification of the amino acid from I to S at position 288.
+The protein's natural variant, known as in CS and JWS;, features a modification of the amino acid from Q to P at position 289.
+The protein's natural variant, known as in PS; severe; also in a lung squamous cell carcinoma sample; somatic mutation;, features a modification of the amino acid from W to C at position 290.
+The protein's natural variant, known as in CS;, features a modification of the amino acid from W to G at position 290.
+The protein's natural variant, known as in CS;, features a modification of the amino acid from W to R at position 290.
+The protein's natural variant, known as in CS;, features a modification of the amino acid from K to E at position 292.
+The protein's natural variant, known as in CS;, features a modification of the amino acid from Y to C at position 301.
+The protein's natural variant, known as in craniosynostosis;, features a modification of the amino acid from A to S at position 314.
+The protein's natural variant, known as in a non-syndromic craniosynostosis patient with abnormal intrauterine history; confers predisposition to craniosynostosis;, features a modification of the amino acid from A to S at position 315.
+The protein's natural variant, known as in PS;, features a modification of the amino acid from D to A at position 321.
+The protein's natural variant, known as in CS;, features a modification of the amino acid from Y to C at position 328.
+The protein's natural variant, known as in CS, features a modification of the amino acid from N to I at position 331.
+The protein's natural variant, known as in CS, features a modification of the amino acid from A to ANA at position 337.
+The protein's natural variant, known as in CS;, features a modification of the amino acid from A to P at position 337.
+The protein's natural variant, known as in CS;, features a modification of the amino acid from G to E at position 338.
+The protein's natural variant, known as in CS;, features a modification of the amino acid from G to R at position 338.
+The protein's natural variant, known as in PS;, features a modification of the amino acid from Y to C at position 340.
+The protein's natural variant, known as in CS;, features a modification of the amino acid from Y to H at position 340.
+The protein's natural variant, known as in PS and CS;, features a modification of the amino acid from T to P at position 341.
+The protein's natural variant, known as in CS;, features a modification of the amino acid from C to F at position 342.
+The protein's natural variant, known as in PS;, features a modification of the amino acid from C to G at position 342.
+The protein's natural variant, known as in CS, JWS, PS and ABS2;, features a modification of the amino acid from C to R at position 342.
+The protein's natural variant, known as in CS, JWS, PS and ABS2;, features a modification of the amino acid from C to S at position 342.
+The protein's natural variant, known as in CS;, features a modification of the amino acid from C to W at position 342.
+The protein's natural variant, known as in CS and PS;, features a modification of the amino acid from C to Y at position 342.
+The protein's natural variant, known as in CS and JWS;, features a modification of the amino acid from A to G at position 344.
+The protein's natural variant, known as in CS and PS, features a modification of the amino acid from A to P at position 344.
+The protein's natural variant, known as in CS;, features a modification of the amino acid from S to C at position 347.
+The protein's natural variant, known as in CS, PS and ABS2;, features a modification of the amino acid from S to C at position 351.
+The protein's natural variant, known as in CS;, features a modification of the amino acid from S to C at position 354.
+The protein's natural variant, known as in CS, features a modification of the amino acid from S to Y at position 354.
+The protein's natural variant, known as in CS and PS, features a modification of the amino acid from V to F at position 359.
+The protein's natural variant, known as in CS, features a modification of the amino acid from A to S at position 362.
+The protein's natural variant, known as in BSTVS;, features a modification of the amino acid from S to C at position 372.
+The protein's natural variant, known as in PS and BSTVS;, features a modification of the amino acid from Y to C at position 375.
+The protein's natural variant, known as in BBDS1;, features a modification of the amino acid from Y to D at position 381.
+The protein's natural variant, known as in CS;, features a modification of the amino acid from G to R at position 384.
+The protein's natural variant, known as in BBDS1; the mutation selectively reduces plasma-membrane levels of the protein and markedly diminishes the receptor's responsiveness to extracellular FGF;, features a modification of the amino acid from M to R at position 391.
+The protein's natural variant, known as in FSPC; constitutive kinase activity;, features a modification of the amino acid from K to E at position 526.
+The protein's natural variant, known as in CS; constitutive kinase activity;, features a modification of the amino acid from N to H at position 549.
+The protein's natural variant, known as in PS; constitutive kinase activity;, features a modification of the amino acid from E to G at position 565.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation, features a modification of the amino acid from R to T at position 612.
+The natural variant of this protein is characterized by an amino acid alteration from G to R at position 613.
+The protein's natural variant, known as in LADD1; strongly reduced kinase activity;, features a modification of the amino acid from A to T at position 628.
+The protein's natural variant, known as in PS; constitutive kinase activity;, features a modification of the amino acid from K to R at position 641.
+The protein's natural variant, known as in LADD1;, features a modification of the amino acid from A to T at position 648.
+The protein's natural variant, known as in LADD1, features a modification of the amino acid from RD to S at position 650.
+The protein's natural variant, known as in craniosynostosis; constitutive kinase activity;, features a modification of the amino acid from K to N at position 659.
+The protein's natural variant, known as in PS, features a modification of the amino acid from G to E at position 663.
+The protein's natural variant, known as in CS;, features a modification of the amino acid from R to G at position 678.
+The protein's natural variant, known as in NEDDFAC; unknown pathological significance, features a modification of the amino acid from I to V at position 162.
+The protein's natural variant, known as in NEDDFAC; unknown pathological significance, features a modification of the amino acid from L to P at position 432.
+The protein's natural variant, known as in NEDDFAC; unknown pathological significance, features a modification of the amino acid from N to S at position 571.
+The protein's natural variant, known as in NEDDFAC; unknown pathological significance, features a modification of the amino acid from R to W at position 734.
+The protein's natural variant, known as in strain: RM220-3, features a modification of the amino acid from N to T at position 64.
+The protein's natural variant, known as in strain: RM220-3, features a modification of the amino acid from L to G at position 71.
+The protein's natural variant, known as in strain: RM220-3, features a modification of the amino acid from S to P at position 90.
+The protein's natural variant, known as in strain: RM220-3, features a modification of the amino acid from I to N at position 100.
+The protein's natural variant, known as in strain: RM220-3, features a modification of the amino acid from S to R at position 164.
+The protein's natural variant, known as in strain: RM220-3, features a modification of the amino acid from F to L at position 174.
+The protein's natural variant, known as in strain: RM220-3, features a modification of the amino acid from A to G at position 184.
+The protein's natural variant, known as in strain: RM220-3, features a modification of the amino acid from EHR to KQK at position 214.
+The protein's natural variant, known as in strain: RM220-3, features a modification of the amino acid from E to K at position 219.
+The protein's natural variant, known as in strain: RM220-3, features a modification of the amino acid from E to G at position 254.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from L to S at position 270.
+The protein's natural variant, known as associated with atopic asthma and cedar pollen sensitization;, features a modification of the amino acid from I to V at position 75.
+The protein's natural variant, known as associated with cedar pollen sensitization;, features a modification of the amino acid from E to A at position 400.
+The protein's natural variant, known as lowered total IgE concentration;, features a modification of the amino acid from S to P at position 503.
+The protein's natural variant, known as associated with atopic dermatitis; lowered total IgE concentration; no effect on IL4-induced signal transduction;, features a modification of the amino acid from Q to R at position 576.
+The protein's natural variant, known as in 1.8% of the population;, features a modification of the amino acid from S to P at position 786.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from K to N at position 956.
+The protein's natural variant, known as in strain: ATCC 44827 and ATCC 7754, features a modification of the amino acid from A to V at position 8.
+The protein's natural variant, known as in strain: ATCC 44827 and ATCC 7754, features a modification of the amino acid from V to I at position 22.
+The protein's natural variant, known as in strain: ATCC 44827 and ATCC 7754, features a modification of the amino acid from P to S at position 38.
+The protein's natural variant, known as in strain: ATCC 44827 and ATCC 7754, features a modification of the amino acid from I to R at position 87.
+The protein's natural variant, known as in strain: ATCC 44827 and ATCC 7754, features a modification of the amino acid from T to A at position 107.
+The protein's natural variant, known as in strain: ATCC 44827, features a modification of the amino acid from GLDINVKGTLNRR to VRYQCKRHVKPQ at position 123.
+The protein's natural variant, known as in strain: ATCC 7754, features a modification of the amino acid from K to R at position 117.
+The protein's natural variant, known as in strain: ATCC 44827, features a modification of the amino acid from KG to N at position 132.
+The protein's natural variant, known as in strain: ATCC 44827 and ATCC 7754, features a modification of the amino acid from A to D at position 149.
+The protein's natural variant, known as in strain: ATCC 44827 and ATCC 7754, features a modification of the amino acid from Q to K at position 177.
+The protein's natural variant, known as in strain: ATCC 44827 and ATCC 7754, features a modification of the amino acid from P to Q at position 184.
+The protein's natural variant, known as in strain: ATCC 44827 and ATCC 7754, features a modification of the amino acid from I to V at position 198.
+The protein's natural variant, known as in strain: ATCC 44827 and ATCC 7754, features a modification of the amino acid from K to R at position 204.
+The protein's natural variant, known as in strain: ATCC 44827 and ATCC 7754, features a modification of the amino acid from DKGH to GL at position 214.
+The protein's natural variant, known as in strain: ATCC 44827, features a modification of the amino acid from LPP to QPR at position 222.
+The protein's natural variant, known as in strain: ATCC 44827, features a modification of the amino acid from DPSR to NSSP at position 228.
+The protein's natural variant, known as in strain: ATCC 44827, features a modification of the amino acid from N to S at position 231.
+The protein's natural variant, known as in strain: ATCC 44827 and ATCC 7754, features a modification of the amino acid from SLT to NLI at position 241.
+The protein's natural variant, known as in strain: ATCC 44827 and ATCC 7754, features a modification of the amino acid from E to A at position 246.
+The protein's natural variant, known as in strain: ATCC 44827 and ATCC 7754, features a modification of the amino acid from G to S at position 253.
+The protein's natural variant, known as in strain: ATCC 7754, features a modification of the amino acid from K to R at position 261.
+The protein's natural variant, known as in strain: ATCC 44827 and ATCC 7754, features a modification of the amino acid from T to A at position 270.
+The protein's natural variant, known as in strain: ATCC 44827 and ATCC 7754, features a modification of the amino acid from DG to NE at position 373.
+The protein's natural variant, known as found in a patient affected by oligo-astheno-teratozoospermia also carrying Y-276 on the same allele; unknown pathological significance;, features a modification of the amino acid from R to H at position 246.
+The protein's natural variant, known as found in a patient affected by oligo-astheno-teratozoospermia also carrying H-246 on the same allele; requires 2 nucleotide substitutions; unknown pathological significance;, features a modification of the amino acid from R to Y at position 276.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from G to V at position 92.
+The protein's natural variant, known as no effect on exonuclease activity;, features a modification of the amino acid from V to I at position 114.
+The protein's natural variant, known as in WRN;, features a modification of the amino acid from K to N at position 125.
+The protein's natural variant, known as in WRN;, features a modification of the amino acid from K to E at position 135.
+The protein's natural variant, known as no effect on exonuclease activity;, features a modification of the amino acid from T to P at position 172.
+The natural variant of this protein is characterized by an amino acid alteration from L to W at position 383.
+The natural variant of this protein is characterized by an amino acid alteration from Q to L at position 724.
+The protein's natural variant, known as associated with a higher risk of myocardial infarction;, features a modification of the amino acid from C to R at position 1367.
+The protein's natural variant, known as in congenital scoliosis; unknown pathological significance; decreases transcriptional activity, features a modification of the amino acid from M to I at position 111.
+The protein's natural variant, known as in SCDO5; unknown pathological significance;, features a modification of the amino acid from P to L at position 145.
+The protein's natural variant, known as in congenital scoliosis; unknown pathological significance; not change transcriptional activity;, features a modification of the amino acid from R to C at position 150.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from Q to P at position 95.
+The protein's natural variant, known as in CSNB1A;, features a modification of the amino acid from C to S at position 31.
+The protein's natural variant, known as in CSNB1A;, features a modification of the amino acid from A to P at position 143.
+The protein's natural variant, known as in CSNB1A;, features a modification of the amino acid from P to L at position 151.
+The protein's natural variant, known as in CSNB1A, features a modification of the amino acid from L to LSVPERLL at position 155.
+The protein's natural variant, known as in CSNB1A;, features a modification of the amino acid from P to R at position 175.
+The protein's natural variant, known as in CSNB1A;, features a modification of the amino acid from L to P at position 184.
+The protein's natural variant, known as in CSNB1A; requires 2 nucleotide substitutions;, features a modification of the amino acid from A to K at position 187.
+The protein's natural variant, known as in CSNB1A, features a modification of the amino acid from R to RLLR at position 207.
+The protein's natural variant, known as in CSNB1A, features a modification of the amino acid from R to RCLR at position 209.
+The protein's natural variant, known as in CSNB1A;, features a modification of the amino acid from L to Q at position 213.
+The protein's natural variant, known as in CSNB1A, features a modification of the amino acid from N to S at position 216.
+The protein's natural variant, known as in CSNB1A;, features a modification of the amino acid from L to P at position 232.
+The protein's natural variant, known as in CSNB1A;, features a modification of the amino acid from N to K at position 264.
+The protein's natural variant, known as in CSNB1A;, features a modification of the amino acid from L to P at position 285.
+The protein's natural variant, known as in CSNB1A;, features a modification of the amino acid from F to S at position 298.
+The protein's natural variant, known as in CSNB1A, features a modification of the amino acid from L to P at position 307.
+The protein's natural variant, known as in CSNB1A;, features a modification of the amino acid from N to S at position 312.
+The protein's natural variant, known as in CSNB1A;, features a modification of the amino acid from L to P at position 347.
+The protein's natural variant, known as in CSNB1A;, features a modification of the amino acid from G to V at position 370.
+The natural variant of this protein is characterized by an amino acid alteration from N to Y at position 14.
+The natural variant of this protein is characterized by an amino acid alteration from F to L at position 352.
+The natural variant of this protein is characterized by an amino acid alteration from S to A at position 72.
+The natural variant of this protein is characterized by an amino acid alteration from T to A at position 87.
+The natural variant of this protein is characterized by an amino acid alteration from T to L at position 123.
+The natural variant of this protein is characterized by an amino acid alteration from A to S at position 128.
+The protein's natural variant, known as in CLSD; loss of COPII vesicle coating; results in absence of incorporation of cargo proteins into vesicles;, features a modification of the amino acid from F to L at position 382.
+The protein's natural variant, known as in strain: +D4, features a modification of the amino acid from A to S at position 160.
+The protein's natural variant, known as in strain: Mz10, Mz16 and Mz36, features a modification of the amino acid from M to I at position 16.
+The protein's natural variant, known as in strain: Sn34, features a modification of the amino acid from M to L at position 16.
+The protein's natural variant, known as in strain: cv. Elstar, features a modification of the amino acid from R to L at position 108.
+The protein's natural variant, known as in strain: cv. Elstar, features a modification of the amino acid from P to S at position 338.
+The protein's natural variant, known as in IDDMDS; severely reduced secretion due to retention of the mutant in the Golgi apparatus, features a modification of the amino acid from L to H at position 141.
+The protein's natural variant, known as in IDDMDS; severely reduced secretion due to retention of the mutant in the Golgi apparatus, features a modification of the amino acid from D to N at position 331.
+The protein's natural variant, known as in SPATCCM; does not affect localization at the cell surface; decreased uptake of L-serine and L-alanine; Vmax is decreased by at least 50% for both substrates; 3-fold increase of affinity for L-serine; 2-fold increase of affinity for L-alanine;, features a modification of the amino acid from E to K at position 256.
+The protein's natural variant, known as in SPATCCM; does not affect localization at the cell surface; loss of uptake of L-serine and L-alanine;, features a modification of the amino acid from R to W at position 457.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from A to V at position 292.
+The protein's natural variant, known as found in a patient with a neurodevelopmental disorder; unknown pathological significance, features a modification of the amino acid from G to R at position 53.
+The protein's natural variant, known as found in a patient with a neurodevelopmental disorder; unknown pathological significance, features a modification of the amino acid from S to L at position 145.
+The protein's natural variant, known as found in a patient with a neurodevelopmental disorder; unknown pathological significance; gain-of-function mutation in signal transduction; changed regulation of ERK1 and ERK2 cascade; increased interaction with BRAF; increased interaction with RAF1; loss of phosphorylation by CK1 at Thr-232, features a modification of the amino acid from S to W at position 230.
+The protein's natural variant, known as in DEE90, features a modification of the amino acid from I to S at position 5.
+The protein's natural variant, known as in DEE90; loss of ability to induce SCN8A long-term inactivation; no effect on pro-excitatory properties; no effect on interaction with SCN8A;, features a modification of the amino acid from R to C at position 11.
+The protein's natural variant, known as in DEE90; loss of ability to induce SCN8A long-term inactivation; no effect on pro-excitatory properties; no effect on interaction with SCN8A; unknown pathological significance;, features a modification of the amino acid from R to P at position 11.
+The protein's natural variant, known as in DEE90; loss of ability to induce SCN8A long-term inactivation; no effect on pro-excitatory properties; no effect on interaction with SCN8A;, features a modification of the amino acid from R to T at position 14.
+The natural variant of this protein is characterized by an amino acid alteration from L to F at position 120.
+The protein's natural variant, known as confirmed at protein level;, features a modification of the amino acid from R to L at position 786.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation, features a modification of the amino acid from P to L at position 746.
+The protein's natural variant, known as in strain: MT4239, features a modification of the amino acid from S to T at position 62.
+The protein's natural variant, known as in strain: GS-5, features a modification of the amino acid from T to I at position 65.
+The protein's natural variant, known as in strain: GS-5, MT4245, MT4251, MT4467 and MT8148, features a modification of the amino acid from V to A at position 68.
+The protein's natural variant, known as in strain: MT4251, features a modification of the amino acid from Q to P at position 78.
+The protein's natural variant, known as in strain: GS-5, MT4245, MT4251, MT4467 and MT8148, features a modification of the amino acid from I to S at position 86.
+The protein's natural variant, known as in strain: MT4251, features a modification of the amino acid from S to F at position 89.
+The protein's natural variant, known as in strain: MT4251, features a modification of the amino acid from K to N at position 168.
+The protein's natural variant, known as in strain: GS-5, MT4467 and MT8148, features a modification of the amino acid from S to D at position 276.
+The protein's natural variant, known as in strain: MT4239, features a modification of the amino acid from N to R at position 399.
+The protein's natural variant, known as in strain: MT4239, features a modification of the amino acid from I to T at position 474.
+The protein's natural variant, known as in strain: MT8148, features a modification of the amino acid from K to R at position 512.
+The protein's natural variant, known as in strain: MT8148, features a modification of the amino acid from F to Y at position 519.
+The protein's natural variant, known as in strain: MT8148, features a modification of the amino acid from T to I at position 701.
+The protein's natural variant, known as in strain: MT8148, features a modification of the amino acid from A to V at position 708.
+The protein's natural variant, known as in strain: MT8148, features a modification of the amino acid from F to L at position 938.
+The protein's natural variant, known as in strain: GS-5, MT4239 and MT4467, features a modification of the amino acid from FGKPVE to YGTPVA at position 957.
+The protein's natural variant, known as in strain: GS-5, MT4239 and MT4467, features a modification of the amino acid from SV to NT at position 964.
+The protein's natural variant, known as in strain: GS-5, MT4239 and MT4467, features a modification of the amino acid from ADS to VDG at position 970.
+The protein's natural variant, known as in strain: MT4239, features a modification of the amino acid from A to T at position 1086.
+The protein's natural variant, known as in strain: MT4239, features a modification of the amino acid from S to N at position 1158.
+The protein's natural variant, known as in strain: MT4251, features a modification of the amino acid from H to Y at position 1163.
+The protein's natural variant, known as in strain: MT8148, features a modification of the amino acid from E to K at position 1168.
+The protein's natural variant, known as in strain: MT8148, features a modification of the amino acid from Y to C at position 1182.
+The protein's natural variant, known as in strain: MT4239, features a modification of the amino acid from A to P at position 1234.
+The protein's natural variant, known as in strain: GS-5 and MT4467, features a modification of the amino acid from R to H at position 1263.
+The protein's natural variant, known as in strain: MT8148, features a modification of the amino acid from R to P at position 1263.
+The protein's natural variant, known as in strain: GS-5, MT4239, MT4467 and MT8148, features a modification of the amino acid from Y to H at position 1264.
+The protein's natural variant, known as in strain: GS-5, MT4239, MT4467 and MT8148, features a modification of the amino acid from S to G at position 1272.
+The protein's natural variant, known as in strain: GS-5 and MT4467, features a modification of the amino acid from H to Y at position 1329.
+The protein's natural variant, known as in strain: GS-5, MT4239, MT4467 and MT8148, features a modification of the amino acid from Y to H at position 1394.
+The protein's natural variant, known as in strain: GS-5, MT4239, MT4467 and MT8148, features a modification of the amino acid from S to G at position 1402.
+The protein's natural variant, known as in strain: MT4467, features a modification of the amino acid from Y to H at position 1459.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from Y to S at position 174.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from V to M at position 699.
+The protein's natural variant, known as in strain: Czech II, features a modification of the amino acid from G to A at position 478.
+The natural variant of this protein is characterized by an amino acid alteration from D to G at position 26.
+The natural variant of this protein is characterized by an amino acid alteration from K to E at position 35.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 83.
+The natural variant of this protein is characterized by an amino acid alteration from K to N at position 129.
+The natural variant of this protein is characterized by an amino acid alteration from N to S at position 184.
+The natural variant of this protein is characterized by an amino acid alteration from S to K at position 230.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 298.
+The natural variant of this protein is characterized by an amino acid alteration from S to Y at position 309.
+The natural variant of this protein is characterized by an amino acid alteration from N to D at position 361.
+The natural variant of this protein is characterized by an amino acid alteration from Q to E at position 393.
+The protein's natural variant, known as in TAM1; myoblasts with the mutation have significantly increased clustering of STIM1, regardless of calcium levels, indicating that calcium sensing in the sarcoplasmic reticulum is impaired;, features a modification of the amino acid from H to Q at position 72.
+The protein's natural variant, known as in TAM1; myoblasts with the mutation have significantly increased clustering of STIM1, regardless of calcium levels, indicating that calcium sensing in the sarcoplasmic reticulum is impaired;, features a modification of the amino acid from N to T at position 80.
+The protein's natural variant, known as in TAM1; increases store-operated Ca(2+) influx, features a modification of the amino acid from G to D at position 81.
+The protein's natural variant, known as in TAM1; myoblasts with the mutation have significantly increased clustering of STIM1, regardless of calcium levels, indicating that calcium sensing in the sarcoplasmic reticulum is impaired;, features a modification of the amino acid from D to G at position 84.
+The protein's natural variant, known as in TAM1; myoblasts with the mutation have significantly increased clustering of STIM1, regardless of calcium levels, indicating that calcium sensing in the sarcoplasmic reticulum is impaired, features a modification of the amino acid from L to V at position 96.
+The protein's natural variant, known as in TAM1; myoblasts with the mutation have significantly increased clustering of STIM1, regardless of calcium levels, indicating that calcium sensing in the sarcoplasmic reticulum is impaired, features a modification of the amino acid from F to I at position 108.
+The protein's natural variant, known as in TAM1; myoblasts with the mutation have significantly increased clustering of STIM1, regardless of calcium levels, indicating that calcium sensing in the sarcoplasmic reticulum is impaired, features a modification of the amino acid from F to L at position 108.
+The protein's natural variant, known as in TAM1; myoblasts with the mutation have significantly increased clustering of STIM1, regardless of calcium levels, indicating that calcium sensing in the sarcoplasmic reticulum is impaired;, features a modification of the amino acid from H to N at position 109.
+The protein's natural variant, known as in TAM1; myoblasts with the mutation have significantly increased clustering of STIM1, regardless of calcium levels, indicating that calcium sensing in the sarcoplasmic reticulum is impaired;, features a modification of the amino acid from H to R at position 109.
+The protein's natural variant, known as in STRMK and TAM1;, features a modification of the amino acid from I to F at position 115.
+The protein's natural variant, known as in STRMK; autosomal dominant; promotes constitutive activation of the Ca(2+) release-activated Ca(2+) (CRAC) channel;, features a modification of the amino acid from R to W at position 304.
+The protein's natural variant, known as probable disease-associated variant found in a patient with autosomal recessive hypomaturation enamel malformations, nail dysplasia and frequent throat infections;, features a modification of the amino acid from R to C at position 426.
+The protein's natural variant, known as in IMD10;, features a modification of the amino acid from R to C at position 429.
+The protein's natural variant, known as in CSBS; affects subcellular location; the mutant protein is localized in the cytoplasm;, features a modification of the amino acid from V to D at position 124.
+The natural variant of this protein is characterized by an amino acid alteration from S to N at position 92.
+The protein's natural variant, known as in SRXY6; increases phosphorylation of the downstream target MAPK3/MAPK1 compared to wild-type and enhances binding of RHOA to the mutant MAP3K1 complex;, features a modification of the amino acid from L to P at position 189.
+The protein's natural variant, known as in SRXY6; increases phosphorylation of the downstream targets MAPK14 and MAPK3/MAPK1 compared to wild-type and enhances binding of RHOA to the mutant MAP3K1 complex;, features a modification of the amino acid from L to R at position 189.
+The protein's natural variant, known as in SRXY6, features a modification of the amino acid from V to VIQ at position 211.
+The natural variant of this protein is characterized by an amino acid alteration from C to S at position 443.
+The protein's natural variant, known as in SRXY6; unknown pathological significance;, features a modification of the amino acid from G to R at position 616.
+The protein's natural variant, known as in RCDP2;, features a modification of the amino acid from R to C at position 211.
+The protein's natural variant, known as in RCDP2; complete loss of activity;, features a modification of the amino acid from R to H at position 211.
+The protein's natural variant, known as in RCDP2; 70% reduction in activity;, features a modification of the amino acid from D to G at position 519.
+The protein's natural variant, known as in SCA42ND; gain-of-function mutation; results in slower channel inactivation and negatively shifted potential for half-inactivation;, features a modification of the amino acid from A to T at position 961.
+The protein's natural variant, known as in SCA42ND; gain-of-function mutation; results in slower channel inactivation and negatively shifted potential for half-inactivation;, features a modification of the amino acid from M to V at position 1531.
+The protein's natural variant, known as in SCA42; changed voltage-gated calcium channel activity; membrane potential dependency is shifted toward more positive potentials;, features a modification of the amino acid from R to H at position 1715.
+The natural variant of this protein is characterized by an amino acid alteration from P to R at position 391.
+The natural variant of this protein is characterized by an amino acid alteration from V to M at position 63.
+The natural variant of this protein is characterized by an amino acid alteration from I to M at position 297.
+The protein's natural variant, known as in strain: Isolate 1119hy, features a modification of the amino acid from S to M at position 16.
+The protein's natural variant, known as in strain: Isolate 1119hy, features a modification of the amino acid from P to K at position 319.
+The natural variant of this protein is characterized by an amino acid alteration from K to R at position 10.
+The protein's natural variant, known as in isoform SI, features a modification of the amino acid from P to S at position 22.
+The protein's natural variant, known as in isoform SI, features a modification of the amino acid from L to I at position 25.
+The protein's natural variant, known as found in patients with late onset progressive myoclonus epilepsy; unknown pathological significance;, features a modification of the amino acid from S to T at position 1473.
+The protein's natural variant, known as in strain: BALB/c, features a modification of the amino acid from Q to R at position 31.
+The protein's natural variant, known as in strain: BALB/c, features a modification of the amino acid from Y to C at position 89.
+The protein's natural variant, known as in strain: BALB/c, features a modification of the amino acid from E to K at position 567.
+The protein's natural variant, known as in ALAZS; reduced 2'-O-methylation of U6 snRNAs and defects in mRNA splicing, features a modification of the amino acid from ITKAEKIRLAKTQQASKHIRFSEYD to KRLDWQRLNKRVNI at position 582.
+The protein's natural variant, known as in HMNDYT2; no effect on protein abundance; no effect on subcellular localization at the plasma membrane and within the cytoplasm; decreased manganese ion transmembrane transporter activity;, features a modification of the amino acid from F to V at position 98.
+The protein's natural variant, known as in HMNDYT2; no effect on protein abundance; no effect on subcellular localization at the plasma membrane and within the cytoplasm; decreased manganese ion transmembrane transporter activity;, features a modification of the amino acid from G to R at position 383.
+The protein's natural variant, known as in HCIN; loss of localization at the plasma membrane; loss of Zn uptake activity;, features a modification of the amino acid from L to R at position 441.
+The protein's natural variant, known as in HMNDYT2; no effect on protein abundance; no effect on subcellular localization at the plasma membrane and within the cytoplasm; decreased manganese ion transmembrane transporter activity;, features a modification of the amino acid from N to K at position 469.
+The protein's natural variant, known as in NEPPK;, features a modification of the amino acid from K to I at position 74.
+The protein's natural variant, known as in EHK;, features a modification of the amino acid from V to D at position 155.
+The protein's natural variant, known as in EHK;, features a modification of the amino acid from V to G at position 155.
+The protein's natural variant, known as in EHK;, features a modification of the amino acid from L to P at position 161.
+The protein's natural variant, known as in EHK;, features a modification of the amino acid from S to P at position 186.
+The protein's natural variant, known as in EHK;, features a modification of the amino acid from N to K at position 188.
+The protein's natural variant, known as in EHK;, features a modification of the amino acid from N to S at position 188.
+The protein's natural variant, known as in EHK; severe;, features a modification of the amino acid from N to T at position 188.
+The protein's natural variant, known as in EHK;, features a modification of the amino acid from S to P at position 193.
+The protein's natural variant, known as in EHK;, features a modification of the amino acid from L to P at position 214.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 312.
+The natural variant of this protein is characterized by an amino acid alteration from I to T at position 330.
+The protein's natural variant, known as in EHK;, features a modification of the amino acid from D to V at position 340.
+The protein's natural variant, known as in EHK;, features a modification of the amino acid from E to Q at position 478.
+The protein's natural variant, known as in AEI2;, features a modification of the amino acid from I to F at position 479.
+The protein's natural variant, known as in AEI2 and EHK;, features a modification of the amino acid from I to T at position 479.
+The protein's natural variant, known as in EHK;, features a modification of the amino acid from Y to C at position 482.
+The protein's natural variant, known as in EHK;, features a modification of the amino acid from L to P at position 485.
+The protein's natural variant, known as in EHK;, features a modification of the amino acid from L to P at position 486.
+The protein's natural variant, known as in EHK;, features a modification of the amino acid from E to K at position 490.
+The protein's natural variant, known as in EHK;, features a modification of the amino acid from E to Q at position 490.
+The natural variant of this protein is characterized by an amino acid alteration from G to C at position 537.
+The protein's natural variant, known as in SMC1; does not affect protein localization;, features a modification of the amino acid from E to K at position 87.
+The protein's natural variant, known as in DMC; results in protein mis-localization and aggregation;, features a modification of the amino acid from N to Y at position 469.
+The protein's natural variant, known as in SMC1;, features a modification of the amino acid from C to R at position 542.
+The protein's natural variant, known as in AAMR; drastically reduced protein expression;, features a modification of the amino acid from G to D at position 182.
+The protein's natural variant, known as in AAMR;, features a modification of the amino acid from T to M at position 334.
+The protein's natural variant, known as in AAMR; drastically reduced protein expression;, features a modification of the amino acid from T to P at position 334.
+The protein's natural variant, known as in AAMR; drastically reduced protein expression;, features a modification of the amino acid from R to P at position 390.
+The protein's natural variant, known as in AAMR; drastically reduced protein expression, features a modification of the amino acid from N to T at position 401.
+The protein's natural variant, known as associated with atypical swirled coat pattern, features a modification of the amino acid from A to N at position 139.
+The protein's natural variant, known as no effect on coat pattern, features a modification of the amino acid from A to T at position 139.
+The protein's natural variant, known as associated with blotched coat pattern, features a modification of the amino acid from D to N at position 228.
+The protein's natural variant, known as in minor component, features a modification of the amino acid from M to V at position 52.
+The protein's natural variant, known as in minor component, features a modification of the amino acid from N to S at position 55.
+The protein's natural variant, known as found in a renal cell carcinoma case; somatic mutation;, features a modification of the amino acid from G to R at position 194.
+The protein's natural variant, known as associated with low viral load in HIV patients;, features a modification of the amino acid from V to G at position 112.
+The protein's natural variant, known as in DEE88; decreased protein expression; increased levels of glutamate and glycerol-3-phosphate, features a modification of the amino acid from A to V at position 120.
+The protein's natural variant, known as in SPGFX2;, features a modification of the amino acid from M to V at position 171.
+The protein's natural variant, known as in SPGFX2;, features a modification of the amino acid from A to T at position 698.
+The protein's natural variant, known as in GALAC3;, features a modification of the amino acid from A to V at position 25.
+The protein's natural variant, known as in GALAC3; peripheral; nearly normal activity towards UDP-galactose;, features a modification of the amino acid from N to S at position 34.
+The protein's natural variant, known as in GALAC3;, features a modification of the amino acid from R to C at position 40.
+The protein's natural variant, known as in GALAC3;, features a modification of the amino acid from D to E at position 69.
+The protein's natural variant, known as in GALAC3; 800-fold decrease in UDP-galactose epimerization activity;, features a modification of the amino acid from G to E at position 90.
+The protein's natural variant, known as in GALAC3; generalized; 30-fold decrease in UDP-galactose epimerization activity; 2-fold decrease in affinity for UDP-galactose; 24% of normal activity with respect to UDP-N-acetylgalactosamine;, features a modification of the amino acid from V to M at position 94.
+The protein's natural variant, known as in GALAC3; 7-fold decrease in UDP-galactose epimerization activity; very mild decrease in activity towards UDP-N-acetylgalactosamine;, features a modification of the amino acid from D to G at position 103.
+The protein's natural variant, known as in GALAC3;, features a modification of the amino acid from E to K at position 165.
+The protein's natural variant, known as in GALAC3;, features a modification of the amino acid from R to W at position 169.
+The protein's natural variant, known as in GALAC3; peripheral; 3-fold decrease in UDP-galactose epimerization activity;, features a modification of the amino acid from L to P at position 183.
+The protein's natural variant, known as in GALAC3;, features a modification of the amino acid from R to W at position 239.
+The protein's natural variant, known as in GALAC3; 7-fold decrease in UDP-galactose epimerization activity; does not affect affinity for UDP-galactose;, features a modification of the amino acid from K to R at position 257.
+The protein's natural variant, known as in GALAC3;, features a modification of the amino acid from G to D at position 302.
+The protein's natural variant, known as in GALAC3; 6-fold decrease in UDP-galactose epimerization activity; very mild decrease in activity towards UDP-N-acetylgalactosamine;, features a modification of the amino acid from L to M at position 313.
+The protein's natural variant, known as in GALAC3; nearly normal activity towards UDP-galactose; mild impairment under conditions of substrate limitation;, features a modification of the amino acid from G to E at position 319.
+The protein's natural variant, known as in GALAC3; 2-fold decrease in UDP-galactose epimerization activity;, features a modification of the amino acid from R to H at position 335.
+The protein's natural variant, known as in MC3DN10; loss of localization to mitochondrial inner membrane; the mutant protein is distributed over the entire cytosol and in the nucleus;, features a modification of the amino acid from V to D at position 14.
+The protein's natural variant, known as in a sporadic colorectal carcinoma; somatic mutation;, features a modification of the amino acid from S to W at position 79.
+The protein's natural variant, known as in BHD, features a modification of the amino acid from S to I at position 108.
+The protein's natural variant, known as in PSP, features a modification of the amino acid from E to K at position 132.
+The protein's natural variant, known as in a renal cell carcinoma cell line, features a modification of the amino acid from A to V at position 238.
+The protein's natural variant, known as in RCC; impaired protein stability;, features a modification of the amino acid from R to C at position 239.
+The protein's natural variant, known as in a primary colorectal cancer;, features a modification of the amino acid from R to Q at position 320.
+The protein's natural variant, known as found in a colorectal cell line; impaired protein stability;, features a modification of the amino acid from R to C at position 362.
+The protein's natural variant, known as in a primary colorectal cancer; somatic mutation;, features a modification of the amino acid from R to G at position 392.
+The protein's natural variant, known as in PSP;, features a modification of the amino acid from H to Y at position 429.
+The protein's natural variant, known as in a primary clear-cell renal cell carcinoma; somatic mutation, features a modification of the amino acid from A to S at position 444.
+The protein's natural variant, known as in a sporadic colorectal carcinoma; somatic mutation;, features a modification of the amino acid from A to T at position 445.
+The protein's natural variant, known as in BHD; does not impair protein stability, growth suppression activity or intracellular localization of folliculin;, features a modification of the amino acid from K to R at position 508.
+The natural variant of this protein is characterized by an amino acid alteration from Q to R at position 32.
+The natural variant of this protein is characterized by an amino acid alteration from H to D at position 68.
+The natural variant of this protein is characterized by an amino acid alteration from E to S at position 84.
+The natural variant of this protein is characterized by an amino acid alteration from G to D at position 96.
+The natural variant of this protein is characterized by an amino acid alteration from SCGRN to TCERF at position 104.
+The protein's natural variant, known as in NPHS19; unknown pathological significance;, features a modification of the amino acid from E to K at position 803.
+The protein's natural variant, known as in OFC11; also found in renal hypodysplasia patients;, features a modification of the amino acid from S to C at position 91.
+The protein's natural variant, known as in MCOPS6;, features a modification of the amino acid from E to G at position 93.
+The protein's natural variant, known as in a renal hypodysplasia patient;, features a modification of the amino acid from T to S at position 116.
+The protein's natural variant, known as in a renal hypodysplasia patient;, features a modification of the amino acid from N to K at position 150.
+The protein's natural variant, known as in OFC11;, features a modification of the amino acid from R to Q at position 162.
+The natural variant of this protein is characterized by an amino acid alteration from G to A at position 168.
+The protein's natural variant, known as in OFC11;, features a modification of the amino acid from R to H at position 287.
+The protein's natural variant, known as in OFC11;, features a modification of the amino acid from A to V at position 346.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from N to S at position 25.
+The protein's natural variant, known as decreases cell surface expression; decreases phagocytosis activity;, features a modification of the amino acid from G to R at position 150.
+The protein's natural variant, known as may influence susceptibility to multiple sclerosis in the presence of variant S-135 in P2RX4; decreases cell surface expression; decreases pore complex assembly; decreases phagocytosis activity;, features a modification of the amino acid from T to M at position 205.
+The protein's natural variant, known as results in a loss of function;, features a modification of the amino acid from R to Q at position 307.
+The protein's natural variant, known as may influence susceptibility to multiple sclerosis in the presence of variant S-135 in P2RX4; no effect on cell surface expression; no effect on pore complex assembly;, features a modification of the amino acid from N to S at position 361.
+The protein's natural variant, known as results in a loss of function;, features a modification of the amino acid from E to A at position 496.
+The protein's natural variant, known as results in trafficking defect and around 50% loss of function;, features a modification of the amino acid from I to N at position 568.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from R to L at position 574.
+The protein's natural variant, known as in AH2; activity abolished;, features a modification of the amino acid from A to E at position 10.
+The protein's natural variant, known as in AH2; nonsalt-wasting form;, features a modification of the amino acid from A to V at position 10.
+The protein's natural variant, known as in AH2; activity abolished, features a modification of the amino acid from G to D at position 15.
+The protein's natural variant, known as in AH2, features a modification of the amino acid from A to P at position 82.
+The protein's natural variant, known as in AH2;, features a modification of the amino acid from A to T at position 82.
+The protein's natural variant, known as in AH2; nonsalt-wasting form;, features a modification of the amino acid from N to S at position 100.
+The protein's natural variant, known as in AH2; activity abolished, features a modification of the amino acid from L to W at position 108.
+The protein's natural variant, known as in AH2; nonsalt-wasting form;, features a modification of the amino acid from G to R at position 129.
+The protein's natural variant, known as in AH2; activity abolished;, features a modification of the amino acid from E to K at position 142.
+The protein's natural variant, known as in AH2; nonsalt-wasting form;, features a modification of the amino acid from P to L at position 155.
+The protein's natural variant, known as in AH2; late onset; almost normal activity;, features a modification of the amino acid from A to V at position 167.
+The protein's natural variant, known as in AH2; nonsalt-wasting form;, features a modification of the amino acid from L to R at position 173.
+The protein's natural variant, known as in AH2; activity abolished, features a modification of the amino acid from P to L at position 186.
+The protein's natural variant, known as in AH2, features a modification of the amino acid from L to P at position 205.
+The protein's natural variant, known as in AH2; late onset; partial loss of activity;, features a modification of the amino acid from S to G at position 213.
+The protein's natural variant, known as in AH2; late onset; partial loss of activity, features a modification of the amino acid from K to E at position 216.
+The protein's natural variant, known as in AH2; nonsalt-wasting form; activity abolished, features a modification of the amino acid from P to H at position 222.
+The protein's natural variant, known as in AH2; activity abolished;, features a modification of the amino acid from P to Q at position 222.
+The protein's natural variant, known as in AH2;, features a modification of the amino acid from P to T at position 222.
+The protein's natural variant, known as in AH2; mild; 100% of activity;, features a modification of the amino acid from L to S at position 236.
+The protein's natural variant, known as in AH2; loss of 88% of activity, features a modification of the amino acid from A to P at position 245.
+The protein's natural variant, known as in AH2; nonsalt-wasting form; loss of 75% of enzymatic activity for the conversion of pregnenolone to progesterone and dehydroepiandrosterone to androstenedione; no effect on endoplasmic reticulum location, features a modification of the amino acid from G to V at position 250.
+The protein's natural variant, known as in AH2; activity abolished;, features a modification of the amino acid from Y to N at position 253.
+The protein's natural variant, known as in AH2; activity abolished;, features a modification of the amino acid from Y to D at position 254.
+The protein's natural variant, known as in AH2; activity abolished;, features a modification of the amino acid from T to M at position 259.
+The protein's natural variant, known as in AH2; activity abolished, features a modification of the amino acid from T to R at position 259.
+The protein's natural variant, known as in AH2; nonsalt-wasting form; activity abolished, features a modification of the amino acid from G to V at position 294.
+The protein's natural variant, known as in AH2; strongly reduced activity;, features a modification of the amino acid from P to L at position 341.
+The protein's natural variant, known as in AOA; impairs binding to adenosine-5'-diphospho-5'-(DNA) and deadenylation activity, features a modification of the amino acid from K to Q at position 211.
+The protein's natural variant, known as in AOA; heterozygous;, features a modification of the amino acid from A to V at position 212.
+The protein's natural variant, known as in AOA;, features a modification of the amino acid from R to H at position 213.
+The protein's natural variant, known as in AOA;, features a modification of the amino acid from H to R at position 215.
+The protein's natural variant, known as in AOA;, features a modification of the amino acid from P to L at position 220.
+The protein's natural variant, known as in AOA;, features a modification of the amino acid from L to P at position 237.
+The protein's natural variant, known as in AOA; abolishes DNA-binding and enzymatic activity towards Ap(4)A;, features a modification of the amino acid from V to G at position 277.
+The protein's natural variant, known as in AOA; heterozygous, features a modification of the amino acid from D to G at position 281.
+The protein's natural variant, known as in AOA; heterozygous;, features a modification of the amino acid from W to R at position 293.
+The protein's natural variant, known as in GSD9C;, features a modification of the amino acid from V to E at position 106.
+The protein's natural variant, known as in GSD9C;, features a modification of the amino acid from E to K at position 157.
+The protein's natural variant, known as in GSD9C;, features a modification of the amino acid from G to E at position 189.
+The protein's natural variant, known as in GSD9C;, features a modification of the amino acid from D to N at position 215.
+The protein's natural variant, known as in CMD2A;, features a modification of the amino acid from A to V at position 2.
+The protein's natural variant, known as in CMD1FF;, features a modification of the amino acid from K to Q at position 36.
+The protein's natural variant, known as risk factor for CMH7;, features a modification of the amino acid from P to S at position 82.
+The protein's natural variant, known as in CMD1FF;, features a modification of the amino acid from A to G at position 116.
+The protein's natural variant, known as in CMH7;, features a modification of the amino acid from R to Q at position 141.
+The protein's natural variant, known as in RCM1;, features a modification of the amino acid from L to Q at position 144.
+The protein's natural variant, known as in CMH7;, features a modification of the amino acid from R to G at position 145.
+The protein's natural variant, known as in RCM1;, features a modification of the amino acid from R to W at position 145.
+The protein's natural variant, known as in CMH7;, features a modification of the amino acid from A to V at position 157.
+The protein's natural variant, known as in CMH7;, features a modification of the amino acid from R to P at position 162.
+The protein's natural variant, known as in CMH7;, features a modification of the amino acid from R to Q at position 162.
+The protein's natural variant, known as in CMH7;, features a modification of the amino acid from S to F at position 166.
+The protein's natural variant, known as in RCM1;, features a modification of the amino acid from A to T at position 171.
+The protein's natural variant, known as in RCM1;, features a modification of the amino acid from K to E at position 178.
+The protein's natural variant, known as in CMD1FF;, features a modification of the amino acid from N to K at position 185.
+The protein's natural variant, known as in CMH7;, features a modification of the amino acid from R to Q at position 186.
+The protein's natural variant, known as in CMH7 and RCM1, features a modification of the amino acid from D to H at position 190.
+The protein's natural variant, known as in RCM1;, features a modification of the amino acid from R to H at position 192.
+The protein's natural variant, known as in CMH7;, features a modification of the amino acid from D to N at position 196.
+The protein's natural variant, known as in CMH7;, features a modification of the amino acid from R to H at position 204.
+The protein's natural variant, known as in CMH7;, features a modification of the amino acid from K to Q at position 206.
+The protein's natural variant, known as in strain: MT-4, features a modification of the amino acid from G to S at position 14.
+The protein's natural variant, known as in strain: MT-4, features a modification of the amino acid from S to A at position 131.
+The protein's natural variant, known as in strain: MT-4, features a modification of the amino acid from A to S at position 150.
+The protein's natural variant, known as in strain: MT-4, features a modification of the amino acid from S to P at position 174.
+The protein's natural variant, known as in IDDHBA; decreased protein kinase activity, features a modification of the amino acid from V to L at position 27.
+The protein's natural variant, known as in IDDHBA; decreased protein kinase activity;, features a modification of the amino acid from R to G at position 29.
+The protein's natural variant, known as in IDDHBA; decreased protein kinase activity;, features a modification of the amino acid from G to S at position 30.
+The protein's natural variant, known as in IDDHBA; decreased protein kinase activity;, features a modification of the amino acid from S to L at position 62.
+The protein's natural variant, known as in IDDHBA; unknown pathological significance, features a modification of the amino acid from F to L at position 97.
+The protein's natural variant, known as in IDDHBA; decreased protein kinase activity;, features a modification of the amino acid from R to Q at position 178.
+The protein's natural variant, known as in a lung neuroendocrine carcinoma sample; somatic mutation, features a modification of the amino acid from D to N at position 189.
+The protein's natural variant, known as in IDDHBA; decreased protein kinase activity;, features a modification of the amino acid from V to G at position 193.
+The protein's natural variant, known as in IDDHBA; decreased protein kinase activity;, features a modification of the amino acid from I to M at position 223.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation, features a modification of the amino acid from R to C at position 424.
+The protein's natural variant, known as in strain: Rev.1; induces streptomycin resistance in this live attenuated vaccine strain, features a modification of the amino acid from P to L at position 91.
+The protein's natural variant, known as in MC5DN1;, features a modification of the amino acid from W to R at position 94.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from G to R at position 41.
+The protein's natural variant, known as in strain: Breinl, features a modification of the amino acid from S to G at position 33.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from T to A at position 195.
+The protein's natural variant, known as has a protective role in both obesity and diabetes;, features a modification of the amino acid from T to A at position 237.
+The protein's natural variant, known as in strain: MB15b and MB25a, features a modification of the amino acid from I to L at position 8.
+The protein's natural variant, known as in strain: MB13a, MB15b, MB25a, MB34a, MB37a and MB63a, features a modification of the amino acid from N to S at position 44.
+The protein's natural variant, known as in strain: MB01a and MB33a, features a modification of the amino acid from S to G at position 100.
+The protein's natural variant, known as in strain: MB08b, MB29b, MB36a, MB40b, MB47a, MB48b, MB52b and MB58b, features a modification of the amino acid from V to I at position 116.
+The protein's natural variant, known as in strain: MB08b, MB29b, MB40b, MB45b, MB47a, MB48b, MB52b and MB80b, features a modification of the amino acid from E to Q at position 186.
+The protein's natural variant, known as in strain: MB01a, MB08b, MB29b, MB36a, MB45b, MB47a, MB48b and MB52b and MB80b, features a modification of the amino acid from G to E at position 305.
+The protein's natural variant, known as in strain: MB48b and MB52b, features a modification of the amino acid from I to V at position 313.
+The protein's natural variant, known as in strain: MB34a and MB39b, features a modification of the amino acid from V to E at position 399.
+The protein's natural variant, known as in strain: MB08b, MB15b, MB25a, MB29b, MB33a, MB34a, MB36a, MB39b, MB45b, MB46b, MB47a, MB48b, MB52b, MB58b, MB63a and MB80b, features a modification of the amino acid from G to S at position 403.
+The protein's natural variant, known as in a bob-tailed dog; alters the ability of the protein to bind to its consensus DNA target, features a modification of the amino acid from I to M at position 63.
+The protein's natural variant, known as in MAHCX; unknown pathological significance;, features a modification of the amino acid from S to N at position 225.
+The protein's natural variant, known as in strain: 66, features a modification of the amino acid from V to A at position 65.
+The natural variant of this protein is characterized by an amino acid alteration from N to K at position 3.
+The natural variant of this protein is characterized by an amino acid alteration from P to H at position 202.
+The protein's natural variant, known as in CRPT1, features a modification of the amino acid from M to K at position 12.
+The protein's natural variant, known as in CRPT1, features a modification of the amino acid from C to R at position 85.
+The natural variant of this protein is characterized by an amino acid alteration from L to S at position 14.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to H at position 212.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from T to M at position 248.
+The natural variant of this protein is characterized by an amino acid alteration from G to V at position 14.
+The protein's natural variant, known as may represent an allelic difference or a cloning artifact, features a modification of the amino acid from M to T at position 166.
+The protein's natural variant, known as in clone 2C, features a modification of the amino acid from K to R at position 50.
+The protein's natural variant, known as in clone 2C, features a modification of the amino acid from Y to H at position 70.
+The natural variant of this protein is characterized by an amino acid alteration from I to S at position 39.
+The protein's natural variant, known as in WBRS; impairs the helicase activity by perturbing its DNA binding and DNA-dependent ATPase activity; reduces binding to rDNA promoter and promotion of rDNA transcription;, features a modification of the amino acid from R to Q at position 263.
+The protein's natural variant, known as in strain: M110 and St Louis, features a modification of the amino acid from K to G at position 19.
+The protein's natural variant, known as in strain: M110 and St Louis, features a modification of the amino acid from S to A at position 30.
+The protein's natural variant, known as in strain: M110 and St Louis, features a modification of the amino acid from A to V at position 38.
+The protein's natural variant, known as in strain: M110 and St Louis, features a modification of the amino acid from A to K at position 42.
+The protein's natural variant, known as in strain: M110 and St Louis, features a modification of the amino acid from T to A at position 76.
+The protein's natural variant, known as in strain: M110 and St Louis, features a modification of the amino acid from A to D at position 79.
+The protein's natural variant, known as in strain: M110 and St Louis, features a modification of the amino acid from N to H at position 89.
+The protein's natural variant, known as in strain: M110, features a modification of the amino acid from D to E at position 90.
+The protein's natural variant, known as in strain: M110 and St Louis, features a modification of the amino acid from AE to GA at position 94.
+The protein's natural variant, known as in strain: M110 and St Louis, features a modification of the amino acid from AT to GA at position 105.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from E to K at position 77.
+The protein's natural variant, known as in strain: Isolate 1019, features a modification of the amino acid from T to A at position 23.
+The protein's natural variant, known as in strain: Isolate 1019, features a modification of the amino acid from SL to GV at position 242.
+The protein's natural variant, known as in strain: Isolate 1019, features a modification of the amino acid from N to K at position 255.
+The protein's natural variant, known as in strain: Isolate 1019, features a modification of the amino acid from V to M at position 327.
+The protein's natural variant, known as in CTRCT11;, features a modification of the amino acid from S to N at position 13.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from A to T at position 226.
+The protein's natural variant, known as in IMD77; unknown pathological significance; decreased defense response to bacterium;, features a modification of the amino acid from T to A at position 73.
+The protein's natural variant, known as decreased defense response to bacterium;, features a modification of the amino acid from P to S at position 316.
+The protein's natural variant, known as in IMD77; unknown pathological significance; decreased defense response to bacterium;, features a modification of the amino acid from P to T at position 405.
+The protein's natural variant, known as in BFH;, features a modification of the amino acid from G to E at position 116.
+The natural variant of this protein is characterized by an amino acid alteration from E to Q at position 570.
+The protein's natural variant, known as in BFH;, features a modification of the amino acid from G to E at position 897.
+The protein's natural variant, known as in BFH;, features a modification of the amino acid from G to R at position 960.
+The protein's natural variant, known as in BFH;, features a modification of the amino acid from G to E at position 999.
+The protein's natural variant, known as in ATS2;, features a modification of the amino acid from G to V at position 1030.
+The protein's natural variant, known as in BFH, features a modification of the amino acid from P to L at position 1132.
+The protein's natural variant, known as in ATS2;, features a modification of the amino acid from G to S at position 1201.
+The natural variant of this protein is characterized by an amino acid alteration from P to S at position 1402.
+The protein's natural variant, known as in ATS2;, features a modification of the amino acid from P to L at position 1572.
+The protein's natural variant, known as in allele A, features a modification of the amino acid from N to S at position 49.
+The protein's natural variant, known as in allele A, features a modification of the amino acid from P to A at position 57.
+The protein's natural variant, known as in allele A, features a modification of the amino acid from MK to VQ at position 75.
+The protein's natural variant, known as in allele A, features a modification of the amino acid from N to S at position 119.
+The protein's natural variant, known as in allele A, features a modification of the amino acid from D to E at position 128.
+The protein's natural variant, known as in allele A, features a modification of the amino acid from K to R at position 143.
+The natural variant of this protein is characterized by an amino acid alteration from P to S at position 62.
+The protein's natural variant, known as in GEFSP5; reduced receptor current amplitudes;, features a modification of the amino acid from E to A at position 177.
+The protein's natural variant, known as in GEFSP5; unknown pathological significance; does not affect receptor current amplitudes;, features a modification of the amino acid from R to C at position 220.
+The protein's natural variant, known as is a risk factor for epilepsy; reduced receptor current amplitudes;, features a modification of the amino acid from R to H at position 220.
+The protein's natural variant, known as found in a patient with childhood onset epileptic encephalopathy; unknown pathological significance;, features a modification of the amino acid from V to I at position 370.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from P to L at position 188.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from P to L at position 247.
+The protein's natural variant, known as in strain: Isolate 3, features a modification of the amino acid from V to I at position 356.
+The protein's natural variant, known as in strain: Isolate 223, features a modification of the amino acid from S to L at position 377.
+The protein's natural variant, known as in strain: NOD, features a modification of the amino acid from G to R at position 201.
+The protein's natural variant, known as in EDSSPD1;, features a modification of the amino acid from A to D at position 186.
+The protein's natural variant, known as in EDSSPD1;, features a modification of the amino acid from L to P at position 206.
+The protein's natural variant, known as in EVC;, features a modification of the amino acid from I to R at position 283.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from A to S at position 630.
+The protein's natural variant, known as in EVC;, features a modification of the amino acid from R to W at position 950.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from L to V at position 994.
+The protein's natural variant, known as in CSS12; unknown pathological significance, features a modification of the amino acid from E to D at position 64.
+The protein's natural variant, known as in CSS12; unknown pathological significance, features a modification of the amino acid from E to K at position 1423.
+The protein's natural variant, known as in strain: Torino, features a modification of the amino acid from I to T at position 63.
+The protein's natural variant, known as in strain: Torino, features a modification of the amino acid from W to L at position 133.
+The protein's natural variant, known as in strain: Torino, features a modification of the amino acid from LQQ to P at position 145.
+The protein's natural variant, known as in strain: Torino, features a modification of the amino acid from H to Q at position 209.
+The protein's natural variant, known as in strain: Torino, features a modification of the amino acid from E to Q at position 211.
+The protein's natural variant, known as in strain: cv. An-2, cv. Bs-1, cv. Bu-0, cv. Chi-1, cv. Co-1, cv. Cvi-0, cv. El-0, cv. Gr-3, cv. Ita-0, cv. Jl-3, cv. Kas-1, cv. Landsberg erecta, cv. Lisse-2, cv. Lu-1, cv. Pi-0 and cv. Sf-1, features a modification of the amino acid from K to T at position 42.
+The protein's natural variant, known as in strain: cv. An-2, cv. Bs-1, cv. Bu-0, cv. Chi-1, cv. Co-1, cv. Cvi-0, cv. El-0, cv. Gr-3, cv. Ita-0, cv. Jl-3, cv. Kas-1, cv. Landsberg erecta, cv. Lisse-2, cv. Lu-1, cv. Pi-0 and cv. Sf-1, features a modification of the amino acid from H to R at position 89.
+The protein's natural variant, known as in strain: cv. An-2, cv. Bs-1, cv. Bu-0, cv. Chi-1, cv. Co-1, cv. Cvi-0, cv. El-0, cv. Gr-3, cv. Ita-0, cv. Jl-3, cv. Kas-1, cv. Landsberg erecta, cv. Lisse-2, cv. Lu-1, cv. Pi-0 and cv. Sf-1, features a modification of the amino acid from K to Q at position 97.
+The protein's natural variant, known as in strain: cv. An-2, cv. Bs-1, cv. Bu-0, cv. Chi-1, cv. Co-1, cv. Cvi-0, cv. El-0, cv. Gr-3, cv. Ita-0, cv. Jl-3, cv. Kas-1, cv. Landsberg erecta, cv. Lisse-2, cv. Lu-1, cv. Pi-0 and cv. Sf-1, features a modification of the amino acid from I to V at position 108.
+The protein's natural variant, known as in strain: cv. An-2, cv. Bs-1, cv. Bu-0, cv. Chi-1, cv. Co-1, cv. Cvi-0, cv. El-0, cv. Gr-3, cv. Ita-0, cv. Jl-3, cv. Kas-1, cv. Landsberg erecta, cv. Lisse-2, cv. Lu-1, cv. Pi-0 and cv. Sf-1, features a modification of the amino acid from L to I at position 116.
+The protein's natural variant, known as in strain: cv. An-2, cv. Bs-1, cv. Bu-0, cv. Chi-1, cv. Co-1, cv. Cvi-0, cv. El-0, cv. Gr-3, cv. Ita-0, cv. Jl-3, cv. Kas-1, cv. Landsberg erecta, cv. Lisse-2, cv. Lu-1, cv. Pi-0 and cv. Sf-1, features a modification of the amino acid from DLT to HLK at position 125.
+The protein's natural variant, known as in strain: cv. An-2, cv. Bs-1, cv. Bu-0, cv. Chi-1, cv. Co-1, cv. Cvi-0, cv. El-0, cv. Gr-3, cv. Ita-0, cv. Jl-3, cv. Kas-1, cv. Landsberg erecta, cv. Lisse-2, cv. Lu-1, cv. Pi-0 and cv. Sf-1, features a modification of the amino acid from D to N at position 130.
+The protein's natural variant, known as in strain: cv. An-2, cv. Bs-1, cv. Bu-0, cv. Chi-1, cv. Co-1, cv. Cvi-0, cv. El-0, cv. Gr-3, cv. Ita-0, cv. Jl-3, cv. Kas-1, cv. Landsberg erecta, cv. Lisse-2, cv. Lu-1, cv. Pi-0 and cv. Sf-1, features a modification of the amino acid from W to L at position 133.
+The protein's natural variant, known as in strain: cv. An-2, cv. Bs-1, cv. Bu-0, cv. Chi-1, cv. Co-1, cv. Cvi-0, cv. El-0, cv. Gr-3, cv. Ita-0, cv. Jl-3, cv. Kas-1, cv. Landsberg erecta, cv. Lisse-2, cv. Lu-1, cv. Pi-0 and cv. Sf-1, features a modification of the amino acid from Q to H at position 140.
+The protein's natural variant, known as in strain: cv. An-2, cv. Bs-1, cv. Bu-0, cv. Chi-1, cv. Co-1, cv. Cvi-0, cv. El-0, cv. Gr-3, cv. Ita-0, cv. Jl-3, cv. Kas-1, cv. Landsberg erecta, cv. Lisse-2, cv. Lu-1, cv. Pi-0 and cv. Sf-1, features a modification of the amino acid from H to Q at position 147.
+The protein's natural variant, known as in strain: cv. An-2, cv. Bs-1, cv. Bu-0, cv. Chi-1, cv. Co-1, cv. Cvi-0, cv. El-0, cv. Gr-3, cv. Ita-0, cv. Jl-3, cv. Kas-1, cv. Landsberg erecta, cv. Lisse-2, cv. Lu-1, cv. Pi-0 and cv. Sf-1, features a modification of the amino acid from T to M at position 150.
+The protein's natural variant, known as in strain: cv. An-2, cv. Bs-1, cv. Bu-0, cv. Chi-1, cv. Co-1, cv. Cvi-0, cv. El-0, cv. Gr-3, cv. Ita-0, cv. Jl-3, cv. Kas-1, cv. Landsberg erecta, cv. Lisse-2, cv. Lu-1, cv. Pi-0 and cv. Sf-1, features a modification of the amino acid from H to N at position 167.
+The protein's natural variant, known as in strain: cv. An-2, cv. Bs-1, cv. Bu-0, cv. Chi-1, cv. Co-1, cv. Cvi-0, cv. El-0, cv. Gr-3, cv. Ita-0, cv. Jl-3, cv. Landsberg erecta, cv. Lisse-2, cv. Lu-1, cv. Pi-0 and cv. Sf-1, features a modification of the amino acid from K to R at position 188.
+The protein's natural variant, known as in strain: cv. An-2, cv. Bs-1, cv. Bu-0, cv. Chi-1, cv. Co-1, cv. Cvi-0, cv. El-0, cv. Gr-3, cv. Ita-0, cv. Jl-3, cv. Landsberg erecta, cv. Lisse-2, cv. Lu-1, cv. Pi-0 and cv. Sf-1, features a modification of the amino acid from FQR to SQE at position 193.
+The protein's natural variant, known as in strain: cv. An-2, cv. Bs-1, cv. Bu-0, cv. Chi-1, cv. Co-1, cv. Cvi-0, cv. El-0, cv. Gr-3, cv. Ita-0, cv. Jl-3, cv. Landsberg erecta, cv. Lisse-2, cv. Lu-1, cv. Pi-0 and cv. Sf-1, features a modification of the amino acid from EI to VN at position 198.
+The protein's natural variant, known as in NDHMSR; changed glutamate-gated calcium ion channel activity; increased inhibition by zinc;, features a modification of the amino acid from R to W at position 217.
+The protein's natural variant, known as in NDHMSR; unknown pathological significance;, features a modification of the amino acid from D to H at position 227.
+The protein's natural variant, known as found in a patient with schizophrenia; unknown pathological significance, features a modification of the amino acid from R to Q at position 306.
+The protein's natural variant, known as in NDHMSD; changed localization to the cell membrane; decreased glutamate-gated calcium ion channel activity;, features a modification of the amino acid from D to E at position 552.
+The protein's natural variant, known as in NDHMSD; changed localization to the cell membrane; loss of glutamate-gated calcium ion channel activity;, features a modification of the amino acid from P to R at position 557.
+The protein's natural variant, known as in NDHMSD; there is near abolition of the activity of the NMDA receptor in Xenopus oocytes; alters the 3-dimensional structure at the receptor's channel pore entrance, features a modification of the amino acid from S to SS at position 560.
+The protein's natural variant, known as in NDHMSD; loss of function in calcium ion transmembrane import into cytosol;, features a modification of the amino acid from G to R at position 618.
+The protein's natural variant, known as in NDHMSD; decreased localization to the plasma membrane of GRIN1/GRIN2BNMDA receptor complexes; changed glutamate-gated calcium ion channel activity; decreased activation by glutamate and glycine; decreased sensitivity to magnesium block; loss of function in calcium ion transmembrane import into cytosol;, features a modification of the amino acid from G to R at position 620.
+The protein's natural variant, known as in NDHMSD; unknown pathological significance;, features a modification of the amino acid from M to I at position 641.
+The protein's natural variant, known as in NDHMSD; unknown pathological significance; no effect on glutamate-gated calcium ion channel activity;, features a modification of the amino acid from A to S at position 645.
+The protein's natural variant, known as in NDHMSD; loss of glutamate-gated calcium ion channel activity, features a modification of the amino acid from Y to S at position 647.
+The protein's natural variant, known as in NDHMSD; unknown pathological significance;, features a modification of the amino acid from N to K at position 650.
+The protein's natural variant, known as in NDHMSD; this mutation produces a significant increase in NMDA receptor-induced calcium currents; excessive calcium influx through NMDA receptor could lead to excitotoxic neuronal cell damage;, features a modification of the amino acid from E to K at position 662.
+The protein's natural variant, known as in NDHMSD, features a modification of the amino acid from S to Y at position 688.
+The protein's natural variant, known as in NDHMSD; loss of glutamate-gated calcium ion channel activity;, features a modification of the amino acid from G to R at position 815.
+The protein's natural variant, known as in NDHMSD, features a modification of the amino acid from G to V at position 815.
+The protein's natural variant, known as in NDHMSD; decreased glutamate-gated calcium ion channel activity;, features a modification of the amino acid from F to L at position 817.
+The protein's natural variant, known as in NDHMSD; loss of function in calcium ion transmembrane import into cytosol;, features a modification of the amino acid from G to R at position 827.
+The protein's natural variant, known as in NDHMSD; no effect on glutamate-gated calcium ion channel activity;, features a modification of the amino acid from R to C at position 844.
+The protein's natural variant, known as requires 2 nucleotide substitutions;, features a modification of the amino acid from K to A at position 200.
+The protein's natural variant, known as in histatin-3-2; loss of the proteolytic cleavage site;, features a modification of the amino acid from R to Q at position 41.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from H to Q at position 7.
+The protein's natural variant, known as decreased mineralocorticoid receptor activity;, features a modification of the amino acid from V to I at position 180.
+The protein's natural variant, known as variant of uncertain significance; changed mineralocorticoid receptor activity; changed response curve to aldosterone stimulation, features a modification of the amino acid from V to A at position 241.
+The protein's natural variant, known as in PHA1A; reduces transcription transactivation upon aldosterone binding;, features a modification of the amino acid from G to R at position 633.
+The protein's natural variant, known as in PHA1A, features a modification of the amino acid from C to S at position 645.
+The protein's natural variant, known as in PHA1A, features a modification of the amino acid from R to S at position 659.
+The protein's natural variant, known as in PHA1A, features a modification of the amino acid from P to S at position 759.
+The protein's natural variant, known as in PHA1A, features a modification of the amino acid from L to P at position 769.
+The protein's natural variant, known as in PHA1A, features a modification of the amino acid from N to K at position 770.
+The protein's natural variant, known as in PHA1A; reduces aldosterone binding;, features a modification of the amino acid from Q to R at position 776.
+The protein's natural variant, known as in PHA1A, features a modification of the amino acid from S to P at position 805.
+The protein's natural variant, known as in EOHSEP; alters receptor specificity and leads to constitutive activation;, features a modification of the amino acid from S to L at position 810.
+The protein's natural variant, known as in PHA1A, features a modification of the amino acid from S to R at position 815.
+The protein's natural variant, known as in PHA1A; abolishes translocation to the nucleus and transcription transactivation upon aldosterone binding;, features a modification of the amino acid from S to L at position 818.
+The protein's natural variant, known as in PHA1A; abolishes transcription transactivation upon aldosterone binding;, features a modification of the amino acid from L to P at position 924.
+The protein's natural variant, known as in PHA1A; reduces affinity for aldosterone and transcription transactivation;, features a modification of the amino acid from E to G at position 972.
+The protein's natural variant, known as in PHA1A; loss of aldosterone binding and transcription transactivation;, features a modification of the amino acid from L to P at position 979.
+The protein's natural variant, known as in ARCS1; effect on interaction with VIPAS39 is reported conflictingly but disrupts colocalization with VIPAS39 at cytoplasmic organelle; impairs localization to VIPAS39-containing endosomal compartment; and induces fragmentation of the VIPAS39-containing endosomal compartment; no effect on interaction with STX7 and association with the HOPS complex;, features a modification of the amino acid from L to P at position 30.
+The protein's natural variant, known as in KDIDAR; disrupts vesicular trafficking of LH3 to intracellular collagen; does not affect interaction with VIPAS39; decreased interaction with RAB25 and RAB11A;, features a modification of the amino acid from G to E at position 131.
+The protein's natural variant, known as in ARCS1; no effect on interaction with VIPAS39; impairs localization to VIPAS39-containing endosomal compartment;, features a modification of the amino acid from S to F at position 243.
+The protein's natural variant, known as in PFIC12; disrupts colocalization with VIPAS39 at cytoplasmic organelle; decreased protein expression;, features a modification of the amino acid from C to R at position 576.
+The natural variant of this protein is characterized by an amino acid alteration from D to G at position 169.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 42.
+The protein's natural variant, known as in SCA5;, features a modification of the amino acid from L to P at position 253.
+The protein's natural variant, known as in SCA5;, features a modification of the amino acid from R to W at position 480.
+The protein's natural variant, known as in SCA5, features a modification of the amino acid from LAAARR to W at position 634.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from E to K at position 774.
+The protein's natural variant, known as in allele CYP2J2*2; significantly reduced metabolism of both arachidonic acid and linoleic acid;, features a modification of the amino acid from T to A at position 143.
+The protein's natural variant, known as in allele CYP2J2*3; significantly reduced metabolism of both arachidonic acid and linoleic acid;, features a modification of the amino acid from R to C at position 158.
+The protein's natural variant, known as in allele CYP2J2*4; significantly reduced metabolism of arachidonic acid only;, features a modification of the amino acid from I to N at position 192.
+The protein's natural variant, known as in allele CYP2J2*5; no change in activity;, features a modification of the amino acid from D to N at position 342.
+The protein's natural variant, known as in allele CYP2J2*6; significantly reduced metabolism of both arachidonic acid and linoleic acid;, features a modification of the amino acid from N to Y at position 404.
+The protein's natural variant, known as in strain: Isolate MSB 53282/NK 7980, features a modification of the amino acid from A to T at position 122.
+The protein's natural variant, known as in strain: Isolate MSB 53282/NK 7980, features a modification of the amino acid from L to F at position 233.
+The protein's natural variant, known as in strain: Isolate MSB 53282/NK 7980, features a modification of the amino acid from M to L at position 360.
+The protein's natural variant, known as in DSS;, features a modification of the amino acid from H to Q at position 12.
+The protein's natural variant, known as in CMT1A and DSS;, features a modification of the amino acid from L to P at position 16.
+The protein's natural variant, known as in DSS, features a modification of the amino acid from L to P at position 19.
+The protein's natural variant, known as in HNPP and CMT1A;, features a modification of the amino acid from S to F at position 22.
+The protein's natural variant, known as in CMT1E;, features a modification of the amino acid from T to R at position 23.
+The protein's natural variant, known as in CMT1E;, features a modification of the amino acid from W to R at position 28.
+The protein's natural variant, known as in HNPP;, features a modification of the amino acid from V to M at position 30.
+The protein's natural variant, known as in CMT1A; with focally folded myelin sheaths;, features a modification of the amino acid from D to V at position 37.
+The protein's natural variant, known as in CMT1A, features a modification of the amino acid from V to F at position 65.
+The protein's natural variant, known as in CMT1E;, features a modification of the amino acid from A to P at position 67.
+The protein's natural variant, known as in HNPP;, features a modification of the amino acid from A to T at position 67.
+The protein's natural variant, known as in DSS;, features a modification of the amino acid from M to K at position 69.
+The protein's natural variant, known as in DSS, features a modification of the amino acid from L to P at position 71.
+The protein's natural variant, known as in DSS and CMT1A;, features a modification of the amino acid from S to L at position 72.
+The protein's natural variant, known as in DSS, features a modification of the amino acid from S to P at position 72.
+The protein's natural variant, known as in DSS, features a modification of the amino acid from S to W at position 72.
+The protein's natural variant, known as in DSS, features a modification of the amino acid from S to I at position 76.
+The protein's natural variant, known as in CMT1A;, features a modification of the amino acid from S to C at position 79.
+The protein's natural variant, known as in DSS, features a modification of the amino acid from S to P at position 79.
+The protein's natural variant, known as in DSS, features a modification of the amino acid from L to P at position 80.
+The protein's natural variant, known as in DSS, features a modification of the amino acid from L to R at position 80.
+The protein's natural variant, known as in CMT1A;, features a modification of the amino acid from G to R at position 93.
+The protein's natural variant, known as in DSS, features a modification of the amino acid from G to E at position 100.
+The protein's natural variant, known as in DSS, features a modification of the amino acid from G to R at position 100.
+The protein's natural variant, known as in CMT1A and DSS, features a modification of the amino acid from L to R at position 105.
+The protein's natural variant, known as in CMT1A, features a modification of the amino acid from G to V at position 107.
+The protein's natural variant, known as in DSS, features a modification of the amino acid from C to R at position 109.
+The protein's natural variant, known as in CMT1A;, features a modification of the amino acid from T to M at position 118.
+The protein's natural variant, known as in CMT1A, features a modification of the amino acid from L to R at position 147.
+The protein's natural variant, known as in DSS;, features a modification of the amino acid from S to R at position 149.
+The protein's natural variant, known as in DSS;, features a modification of the amino acid from G to C at position 150.
+The protein's natural variant, known as in DSS;, features a modification of the amino acid from G to D at position 150.
+The protein's natural variant, known as in DSS;, features a modification of the amino acid from R to W at position 157.
+The protein's natural variant, known as in PEAMO; decreased function in the organization of microtubule cytoskeleton and mitotic splindle;, features a modification of the amino acid from I to N at position 155.
+The protein's natural variant, known as in VDDR2A;, features a modification of the amino acid from G to D at position 33.
+The protein's natural variant, known as in VDDR2A, features a modification of the amino acid from H to Q at position 35.
+The protein's natural variant, known as in VDDR2A, features a modification of the amino acid from K to E at position 45.
+The protein's natural variant, known as in VDDR2A;, features a modification of the amino acid from G to D at position 46.
+The protein's natural variant, known as in VDDR2A, features a modification of the amino acid from F to I at position 47.
+The protein's natural variant, known as in VDDR2A;, features a modification of the amino acid from R to Q at position 50.
+The protein's natural variant, known as in VDDR2A;, features a modification of the amino acid from R to Q at position 73.
+The protein's natural variant, known as in VDDR2A;, features a modification of the amino acid from R to Q at position 80.
+The protein's natural variant, known as in VDDR2A; loss of calcitriol receptor activity; decreased affinity for calcitriol by a factor of 1000; no effect on interaction with RXRA; changed interaction with NCOR1; loss of interaction with NCOA1; no effect on sequence-specific DNA-binding;, features a modification of the amino acid from R to L at position 274.
+The protein's natural variant, known as in VDDR2A; loss of calcitriol receptor activity; no effect on interaction with RXRA; changed interaction with NCOR1; loss of interaction with NCOA1; no effect on sequence-specific DNA-binding;, features a modification of the amino acid from H to Q at position 305.
+The protein's natural variant, known as in VDDR2A;, features a modification of the amino acid from I to S at position 314.
+The protein's natural variant, known as in VDDR2A; decreased calcitriol receptor activity; decreased affinity for calcitriol; decreased ligand-independent localization to the nucleus; loss of interaction with RXRA; decreased interaction with NCOR1; decreased interaction with NCOA1; decreased sequence-specific DNA-binding;, features a modification of the amino acid from V to M at position 346.
+The protein's natural variant, known as in VDDR2A; loss of calcitriol receptor activity; loss of affinity for calcitriol; decreased ligand-independent localization to the nucleus; loss of interaction with RXRA; loss of interaction with NCOR1; loss of interaction with NCOA1; loss of sequence-specific DNA-binding, features a modification of the amino acid from S to P at position 360.
+The protein's natural variant, known as in VDDR2A;, features a modification of the amino acid from R to C at position 391.
+The protein's natural variant, known as in strain: Italian bred, features a modification of the amino acid from S to G at position 8.
+The protein's natural variant, known as in IGAN3; no effect on protein expression; negatively regulates ERK1 and ERK2 cascade;, features a modification of the amino acid from R to W at position 119.
+The protein's natural variant, known as in FFEVF3; unknown pathological significance;, features a modification of the amino acid from R to Q at position 92.
+The protein's natural variant, known as in FFEVF3; unknown pathological significance;, features a modification of the amino acid from E to K at position 249.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 31.
+The natural variant of this protein is characterized by an amino acid alteration from L to G at position 34.
+The natural variant of this protein is characterized by an amino acid alteration from K to L at position 45.
+The natural variant of this protein is characterized by an amino acid alteration from K to T at position 45.
+The natural variant of this protein is characterized by an amino acid alteration from M to D at position 66.
+The natural variant of this protein is characterized by an amino acid alteration from M to V at position 66.
+The natural variant of this protein is characterized by an amino acid alteration from E to M at position 67.
+The natural variant of this protein is characterized by an amino acid alteration from T to I at position 72.
+The natural variant of this protein is characterized by an amino acid alteration from N to K at position 74.
+The natural variant of this protein is characterized by an amino acid alteration from T to D at position 102.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 113.
+The natural variant of this protein is characterized by an amino acid alteration from L to N at position 131.
+The protein's natural variant, known as in JEB7, features a modification of the amino acid from G to R at position 125.
+The protein's natural variant, known as in JEB7;, features a modification of the amino acid from R to Q at position 274.
+The protein's natural variant, known as in JEB7;, features a modification of the amino acid from R to P at position 628.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from H to N at position 236.
+The protein's natural variant, known as in strain: WS576 and WS380B, features a modification of the amino acid from T to S at position 233.
+The protein's natural variant, known as in strain: WS576 and WS380B, features a modification of the amino acid from T to S at position 237.
+The protein's natural variant, known as in strain: WS380B, features a modification of the amino acid from PTYPPTQ to RSYPQTP at position 258.
+The protein's natural variant, known as in strain: WS576, features a modification of the amino acid from TY to SC at position 254.
+The protein's natural variant, known as in strain: WS380B, features a modification of the amino acid from T to S at position 261.
+The protein's natural variant, known as in strain: WS576, features a modification of the amino acid from P to S at position 315.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from A to S at position 913.
+The protein's natural variant, known as in SPG46; loss of glucosylceramide catabolic process;, features a modification of the amino acid from D to H at position 594.
+The protein's natural variant, known as in SPG46; loss of glucosylceramide catabolic process;, features a modification of the amino acid from R to W at position 630.
+The protein's natural variant, known as in SPG46; loss of glucosylceramide catabolic process;, features a modification of the amino acid from R to H at position 873.
+The protein's natural variant, known as in MLD; enzyme activity reduced to 5% of wild-type enzyme;, features a modification of the amino acid from A to D at position 18.
+The protein's natural variant, known as in MLD; infantile-onset; causes a severe reduction of enzyme activity;, features a modification of the amino acid from D to N at position 29.
+The protein's natural variant, known as in MLD; enzyme activity reduced to 2.4% of wild-type enzyme;, features a modification of the amino acid from D to H at position 30.
+The protein's natural variant, known as in MLD; late-infantile form;, features a modification of the amino acid from G to S at position 32.
+The protein's natural variant, known as in MLD; loss of enzymatic activity;, features a modification of the amino acid from L to P at position 52.
+The protein's natural variant, known as in MLD; late-infantile form;, features a modification of the amino acid from L to P at position 68.
+The protein's natural variant, known as in MLD; late-infantile-onset;, features a modification of the amino acid from P to L at position 82.
+The protein's natural variant, known as in MLD; mild;, features a modification of the amino acid from R to Q at position 84.
+The protein's natural variant, known as in MLD; juvenile form;, features a modification of the amino acid from R to W at position 84.
+The protein's natural variant, known as in MLD; severe; no enzyme residual activity; leads to a decreased stability of the mutant enzyme; causes an arrest of the mutant enzyme polypeptide in a prelysosomal compartment;, features a modification of the amino acid from G to D at position 86.
+The protein's natural variant, known as in MLD; adult form;, features a modification of the amino acid from P to A at position 94.
+The protein's natural variant, known as in MLD;, features a modification of the amino acid from S to N at position 95.
+The protein's natural variant, known as in MLD; severe;, features a modification of the amino acid from S to F at position 96.
+The protein's natural variant, known as in MLD; severe; no enzyme residual activity;, features a modification of the amino acid from S to L at position 96.
+The protein's natural variant, known as in MLD; adult type;, features a modification of the amino acid from G to D at position 99.
+The protein's natural variant, known as in MLD; late-infantile form;, features a modification of the amino acid from G to V at position 99.
+The protein's natural variant, known as in MLD; juvenile-onset;, features a modification of the amino acid from G to R at position 119.
+The protein's natural variant, known as in MLD; adult type;, features a modification of the amino acid from G to S at position 122.
+The protein's natural variant, known as in MLD;, features a modification of the amino acid from L to P at position 135.
+The protein's natural variant, known as in MLD; severe late-infantile type; loss of enzymatic activity;, features a modification of the amino acid from P to L at position 136.
+The protein's natural variant, known as in MLD; late-infantile form;, features a modification of the amino acid from P to S at position 136.
+The protein's natural variant, known as in MLD; significantly lower activity than wild-type protein;, features a modification of the amino acid from H to D at position 138.
+The protein's natural variant, known as in MLD; juvenile/adult-onset; generates 5% as much activity as the parallel normal control;, features a modification of the amino acid from R to G at position 143.
+The protein's natural variant, known as in MLD; juvenile-onset;, features a modification of the amino acid from P to L at position 148.
+The protein's natural variant, known as in MLD;, features a modification of the amino acid from D to Y at position 152.
+The protein's natural variant, known as in MLD; late-infantile form; no enzyme residual activity;, features a modification of the amino acid from Q to H at position 153.
+The protein's natural variant, known as in MLD;, features a modification of the amino acid from G to D at position 154.
+The protein's natural variant, known as in MLD; juvenile-onset;, features a modification of the amino acid from P to L at position 155.
+The protein's natural variant, known as in MLD;, features a modification of the amino acid from P to R at position 155.
+The protein's natural variant, known as in MLD; adult type; enzyme activity reduced to 50% of wild-type enzyme;, features a modification of the amino acid from C to R at position 156.
+The protein's natural variant, known as in MLD;, features a modification of the amino acid from P to R at position 167.
+The protein's natural variant, known as in MLD;, features a modification of the amino acid from D to N at position 169.
+The protein's natural variant, known as in MLD; juvenile-onset;, features a modification of the amino acid from C to Y at position 172.
+The protein's natural variant, known as in MLD; mild;, features a modification of the amino acid from I to S at position 179.
+The protein's natural variant, known as in MLD; infantile form;, features a modification of the amino acid from L to Q at position 181.
+The protein's natural variant, known as in MLD; no enzyme residual activity;, features a modification of the amino acid from Q to H at position 190.
+The protein's natural variant, known as in MLD; juvenile-onset;, features a modification of the amino acid from P to T at position 191.
+The protein's natural variant, known as in MLD; juvenile-onset; results in highly reduced enzyme activity and stability; the mutant enzyme is kept in a prelysosomal compartment;, features a modification of the amino acid from Y to C at position 201.
+The protein's natural variant, known as in MLD; loss of enzymatic activity;, features a modification of the amino acid from A to P at position 212.
+The protein's natural variant, known as in MLD;, features a modification of the amino acid from A to V at position 212.
+The protein's natural variant, known as in MLD; enzyme activity reduced to 15.6% of wild-type enzyme;, features a modification of the amino acid from R to H at position 217.
+The protein's natural variant, known as in MLD; enzyme activity reduced to less than 1% of normal activity;, features a modification of the amino acid from F to V at position 219.
+The protein's natural variant, known as in MLD;, features a modification of the amino acid from A to V at position 224.
+The protein's natural variant, known as in MLD; late-infantile form;, features a modification of the amino acid from H to Y at position 227.
+The protein's natural variant, known as in MLD;, features a modification of the amino acid from P to T at position 231.
+The protein's natural variant, known as in MLD; juvenile-onset;, features a modification of the amino acid from R to C at position 244.
+The protein's natural variant, known as in MLD; infantile-onset;, features a modification of the amino acid from R to H at position 244.
+The protein's natural variant, known as in MLD; severe;, features a modification of the amino acid from G to R at position 245.
+The protein's natural variant, known as in MLD;, features a modification of the amino acid from F to S at position 247.
+The protein's natural variant, known as in MLD; infantile-onset;, features a modification of the amino acid from S to Y at position 250.
+The protein's natural variant, known as in MLD; late-infantile; decreased enzymatic activity;, features a modification of the amino acid from E to K at position 253.
+The protein's natural variant, known as in MLD; late-infantile form; no enzyme residual activity; leads to a decreased stability of the mutant enzyme; causes an arrest of the mutant enzyme polypeptide in a prelysosomal compartment;, features a modification of the amino acid from D to H at position 255.
+The protein's natural variant, known as in MLD; severe; 35% of normal activity;, features a modification of the amino acid from T to M at position 274.
+The protein's natural variant, known as in MLD;, features a modification of the amino acid from D to Y at position 281.
+The protein's natural variant, known as in MLD; enzyme activity reduced to 0.6% of wild-type enzyme;, features a modification of the amino acid from N to S at position 282.
+The protein's natural variant, known as in MLD; adult type;, features a modification of the amino acid from T to P at position 286.
+The protein's natural variant, known as in MLD;, features a modification of the amino acid from R to C at position 288.
+The protein's natural variant, known as in MLD; adult form;, features a modification of the amino acid from R to H at position 288.
+The protein's natural variant, known as in MLD; late-onset;, features a modification of the amino acid from G to D at position 293.
+The protein's natural variant, known as in MLD; adult type; causes a severe reduction of enzyme activity;, features a modification of the amino acid from G to S at position 293.
+The protein's natural variant, known as in MLD; juvenile-onset; causes a severe reduction of enzyme activity;, features a modification of the amino acid from C to Y at position 294.
+The protein's natural variant, known as in MLD; severe;, features a modification of the amino acid from S to Y at position 295.
+The protein's natural variant, known as in MLD; late-infantile form; complete loss of enzyme activity;, features a modification of the amino acid from L to S at position 298.
+The protein's natural variant, known as in MLD; late-infantile-onset; enzyme activity reduced to less than 1%; the mutant protein is more rapidly degraded in lysosomes; strongly interferes with the octamerization process of the enzyme at low pH;, features a modification of the amino acid from C to F at position 300.
+The protein's natural variant, known as in MLD; enzyme activity reduced to 2.8% of wild-type enzyme;, features a modification of the amino acid from K to N at position 302.
+The protein's natural variant, known as in MLD; loss of enzymatic activity;, features a modification of the amino acid from T to M at position 304.
+The protein's natural variant, known as in MLD; juvenile-onset;, features a modification of the amino acid from Y to H at position 306.
+The protein's natural variant, known as in MLD; loss of enzymatic activity;, features a modification of the amino acid from E to K at position 307.
+The protein's natural variant, known as in MLD; late-infantile form;, features a modification of the amino acid from G to D at position 308.
+The protein's natural variant, known as in MLD; late-infantile form; no enzyme residual activity;, features a modification of the amino acid from G to V at position 308.
+The protein's natural variant, known as in MLD; severe; 13% of normal activity;, features a modification of the amino acid from G to S at position 309.
+The protein's natural variant, known as in MLD; juvenile-onset;, features a modification of the amino acid from R to Q at position 311.
+The protein's natural variant, known as in MLD; low amounts of residual enzyme activity; leads to a decreased stability of the mutant enzyme;, features a modification of the amino acid from E to D at position 312.
+The protein's natural variant, known as in MLD; infantile-onset;, features a modification of the amino acid from A to T at position 314.
+The protein's natural variant, known as in MLD; juvenile-onset;, features a modification of the amino acid from G to S at position 325.
+The protein's natural variant, known as in MLD; late-infantile form, features a modification of the amino acid from T to I at position 327.
+The protein's natural variant, known as in MLD; late-infantile-onset; loss of enzymatic activity;, features a modification of the amino acid from D to V at position 335.
+The protein's natural variant, known as often found in association with a nucleotide substitution in the polyadenylation signal downstream of the stop codon; this association defines an ARSA pseudodeficiency allele found in individuals with low enzymatic activities but no clinical manifestations; no effect on activity; no effect on protein abundance; loss of N-glycosylation;, features a modification of the amino acid from N to S at position 350.
+The protein's natural variant, known as in MLD;, features a modification of the amino acid from K to N at position 367.
+The protein's natural variant, known as in MLD; mild;, features a modification of the amino acid from R to Q at position 370.
+The protein's natural variant, known as in MLD; severe; no enzyme residual activity;, features a modification of the amino acid from R to W at position 370.
+The protein's natural variant, known as in MLD; enzyme activity reduced to 4.7% of wild-type enzyme;, features a modification of the amino acid from Y to N at position 376.
+The protein's natural variant, known as in MLD; severe;, features a modification of the amino acid from P to L at position 377.
+The protein's natural variant, known as in MLD; early-infantile form;, features a modification of the amino acid from D to E at position 381.
+The protein's natural variant, known as in MLD; intermediate;, features a modification of the amino acid from E to K at position 382.
+The protein's natural variant, known as in MLD;, features a modification of the amino acid from R to C at position 384.
+The protein's natural variant, known as in MLD; juvenile-onset;, features a modification of the amino acid from R to Q at position 390.
+The protein's natural variant, known as in MLD; late-infantile and juvenile-onset;, features a modification of the amino acid from R to W at position 390.
+The protein's natural variant, known as retains 90% of activity;, features a modification of the amino acid from T to S at position 391.
+The protein's natural variant, known as in MLD; adult-onset;, features a modification of the amino acid from H to Y at position 397.
+The protein's natural variant, known as in MLD; loss of enzymatic activity;, features a modification of the amino acid from S to G at position 406.
+The protein's natural variant, known as in MLD; adult type;, features a modification of the amino acid from T to I at position 408.
+The protein's natural variant, known as in MLD; mild;, features a modification of the amino acid from T to I at position 409.
+The protein's natural variant, known as in MLD; juvenile-onset; retains about 12% of specific enzyme activity; the mutant protein is unstable; results in more rapid enzyme degradation in lysosomes; addition of the cysteine protease inhibitor leupeptin increases the amount of the enzyme activity; displays a modest reduction in the octamerization process of the enzyme at low pH;, features a modification of the amino acid from P to T at position 425.
+The protein's natural variant, known as in MLD; juvenile/adult-onset; mild; common mutation; decreased enzyme activity;, features a modification of the amino acid from P to L at position 426.
+The protein's natural variant, known as in MLD; late-infantile form;, features a modification of the amino acid from L to P at position 428.
+The protein's natural variant, known as in MLD; adult-onset;, features a modification of the amino acid from Y to S at position 429.
+The protein's natural variant, known as in MLD; early-infantile form;, features a modification of the amino acid from A to G at position 469.
+The protein's natural variant, known as in MLD; late-onset;, features a modification of the amino acid from C to G at position 489.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation, features a modification of the amino acid from K to N at position 240.
+The protein's natural variant, known as in a pancreatic ductal adenocarcinoma sample; somatic mutation, features a modification of the amino acid from S to R at position 693.
+The protein's natural variant, known as in allele CYP2C19*14;, features a modification of the amino acid from L to P at position 17.
+The protein's natural variant, known as in allele CYP2C19*15;, features a modification of the amino acid from I to L at position 19.
+The protein's natural variant, known as in allele CYP2C19*19;, features a modification of the amino acid from S to G at position 51.
+The protein's natural variant, known as in allele CYP2C19*8; loss of activity;, features a modification of the amino acid from W to R at position 120.
+The protein's natural variant, known as in allele CYP2C19*6; loss of activity;, features a modification of the amino acid from R to Q at position 132.
+The protein's natural variant, known as in allele CYP2C19*9;, features a modification of the amino acid from R to H at position 144.
+The protein's natural variant, known as in allele CYP2C19*11;, features a modification of the amino acid from R to H at position 150.
+The protein's natural variant, known as in allele CYP2C19*10;, features a modification of the amino acid from P to L at position 227.
+The protein's natural variant, known as in allele CYP2C19*18;, features a modification of the amino acid from R to H at position 329.
+The protein's natural variant, known as in allele CYP2C19*1B, allele CYP2C19*1C, allele CYP2C19*2A, allele CYP2C19*2B, allele CYP2C19*2C, allele CYP2C19*2E, allele CYP2C19*2F, allele CYP2C19*2G, allele CYP2C19*2H, allele CYP2C19*2J, allele CYP2C19*3A, allele CYP2C19*3B, allele CYP2C19*3C, allele CYP2C19*4A, allele CYP2C19*4B, allele CYP2C19*6, allele CYP2C19*9, allele CYP2C19*10, allele CYP2C19*11, allele CYP2C19*12, allele CYP2C19*13, allele CYP2C19*14, allele CYP2C19*15, allele CYP2C19*18, allele CYP2C19*19, allele CYP2C19*22, allele CYP2C19*23, allele CYP2C19*24, allele CYP2C19*25, allele CYP2C19*26, allele CYP2C19*27, allele CYP2C19*28, allele CYP2C19*29, allele CYP2C19*31, allele CYP2C19*32, allele CYP2C19*33 and allele CYP2C19*35;, features a modification of the amino acid from I to V at position 331.
+The protein's natural variant, known as in allele CYP2C19*13;, features a modification of the amino acid from R to C at position 410.
+The protein's natural variant, known as in allele CYP2C19*5A and allele CYP2C19*5B; loss of activity;, features a modification of the amino acid from R to W at position 433.
+The protein's natural variant, known as in allele CYP2C19*16; lowered catalytic activity;, features a modification of the amino acid from R to C at position 442.
+The protein's natural variant, known as in strain: NCTC 10294, features a modification of the amino acid from G to A at position 50.
+The protein's natural variant, known as in strain: Vedros M601 and LCDC 81-176, features a modification of the amino acid from AQET to GQDV at position 60.
+The protein's natural variant, known as in strain: NCTC 10294, features a modification of the amino acid from A to G at position 57.
+The protein's natural variant, known as in strain: NCTC 10294, features a modification of the amino acid from T to V at position 60.
+The protein's natural variant, known as in strain: Vedros M601, LCDC 81-176 and NCTC 10294, features a modification of the amino acid from I to V at position 108.
+The protein's natural variant, known as in strain: NCTC 10294, features a modification of the amino acid from A to G at position 116.
+The protein's natural variant, known as in strain: NCTC 10294, features a modification of the amino acid from V to I at position 121.
+The protein's natural variant, known as in strain: NCTC 10294, features a modification of the amino acid from KT to QS at position 137.
+The protein's natural variant, known as in strain: NCTC 10294, features a modification of the amino acid from NIVARARAVAE to GIIAAAHAAAK at position 153.
+The protein's natural variant, known as in strain: NCTC 10294, features a modification of the amino acid from G to A at position 157.
+The protein's natural variant, known as in strain: NCTC 10294, features a modification of the amino acid from L to T at position 160.
+The protein's natural variant, known as in strain: NCTC 10294, features a modification of the amino acid from TK to AH at position 166.
+The protein's natural variant, known as in strain: NCTC 10294, features a modification of the amino acid from GA to NV at position 172.
+The protein's natural variant, known as in strain: Vedros M601 and LCDC 81-176, features a modification of the amino acid from E to D at position 205.
+The protein's natural variant, known as in strain: Vedros M601, LCDC 81-176 and NCTC 10294, features a modification of the amino acid from V to A at position 209.
+The protein's natural variant, known as in strain: Vedros M601, LCDC 81-176 and NCTC 10294, features a modification of the amino acid from SK to PQ at position 214.
+The protein's natural variant, known as in IPHAK; unknown pathological significance; due to a nucleotide substitution that creates a novel donor splice site resulting in aberrant splicing; small amounts of canonically spliced transcripts with the missense variant are also produced; decreased protein abundance in patient cells, features a modification of the amino acid from N to S at position 168.
+The protein's natural variant, known as in inhibitor 2 and inhibitor 4, features a modification of the amino acid from K to N at position 25.
+The protein's natural variant, known as in inhibitor 2 and inhibitor 4, features a modification of the amino acid from T to S at position 40.
+The protein's natural variant, known as in inhibitor 3, features a modification of the amino acid from K to E at position 65.
+The natural variant of this protein is characterized by an amino acid alteration from K to R at position 65.
+The protein's natural variant, known as in LRAM;, features a modification of the amino acid from S to N at position 342.
+The protein's natural variant, known as in strain: C3H/An, features a modification of the amino acid from EPF to DHL at position 19.
+The protein's natural variant, known as in strain: 297, features a modification of the amino acid from V to I at position 28.
+The protein's natural variant, known as in strain: 297, features a modification of the amino acid from K to E at position 72.
+The protein's natural variant, known as in strain: 297, features a modification of the amino acid from KMIKA to EMMKS at position 79.
+The protein's natural variant, known as in strain: 297, features a modification of the amino acid from M to I at position 184.
+The protein's natural variant, known as in strain: 297, features a modification of the amino acid from L to F at position 206.
+The protein's natural variant, known as in LCATD, features a modification of the amino acid from L to LLLPPAAPFWL at position 17.
+The protein's natural variant, known as in LCATD, features a modification of the amino acid from N to I at position 29.
+The protein's natural variant, known as in FED;, features a modification of the amino acid from P to L at position 34.
+The protein's natural variant, known as in FED, features a modification of the amino acid from P to Q at position 34.
+The protein's natural variant, known as in LCATD;, features a modification of the amino acid from T to M at position 37.
+The protein's natural variant, known as in LCATD;, features a modification of the amino acid from G to S at position 54.
+The protein's natural variant, known as in LCATD, features a modification of the amino acid from G to R at position 57.
+The protein's natural variant, known as in FED;, features a modification of the amino acid from V to E at position 70.
+The protein's natural variant, known as found in a patient with intermediate phenotype between LCATD and FED; reduction of activity, features a modification of the amino acid from G to R at position 95.
+The protein's natural variant, known as in FED; loss of activity, features a modification of the amino acid from W to S at position 99.
+The protein's natural variant, known as in LCATD;, features a modification of the amino acid from A to T at position 117.
+The protein's natural variant, known as in FED;, features a modification of the amino acid from R to C at position 123.
+The protein's natural variant, known as in a patient with low HDL-cholesterol levels; results in reduced activity, features a modification of the amino acid from EY to DN at position 135.
+The protein's natural variant, known as in FED;, features a modification of the amino acid from T to I at position 147.
+The protein's natural variant, known as in FED;, features a modification of the amino acid from R to Q at position 159.
+The protein's natural variant, known as in LCATD;, features a modification of the amino acid from R to W at position 159.
+The protein's natural variant, known as in LCATD;, features a modification of the amino acid from R to C at position 164.
+The protein's natural variant, known as in LCATD; also found in a patient with intermediate phenotype between LCATD and FED; loss of activity;, features a modification of the amino acid from R to H at position 164.
+The protein's natural variant, known as in LCATD, features a modification of the amino acid from R to W at position 171.
+The protein's natural variant, known as in LCATD;, features a modification of the amino acid from Y to N at position 180.
+The protein's natural variant, known as in LCATD, features a modification of the amino acid from S to N at position 205.
+The protein's natural variant, known as in LCATD;, features a modification of the amino acid from L to P at position 233.
+The protein's natural variant, known as in LCATD, features a modification of the amino acid from K to N at position 242.
+The protein's natural variant, known as in a patient with low HDL-cholesterol levels; the mutant is hardly secreted and is catalytically inactive, features a modification of the amino acid from V to F at position 246.
+The protein's natural variant, known as in LCATD;, features a modification of the amino acid from N to K at position 252.
+The protein's natural variant, known as in a patient with low HDL-cholesterol levels; the mutant is hardly secreted and is catalytically inactive;, features a modification of the amino acid from R to C at position 268.
+The protein's natural variant, known as in LCATD;, features a modification of the amino acid from R to H at position 268.
+The protein's natural variant, known as in FED;, features a modification of the amino acid from M to K at position 276.
+The protein's natural variant, known as in FED and LCATD, features a modification of the amino acid from T to A at position 298.
+The protein's natural variant, known as in LCATD, features a modification of the amino acid from T to I at position 298.
+The protein's natural variant, known as in LCATD; partially defective enzyme;, features a modification of the amino acid from M to I at position 317.
+The protein's natural variant, known as in a patient with low HDL-cholesterol levels; reduced protein secretion;, features a modification of the amino acid from R to C at position 322.
+The protein's natural variant, known as in LCATD, features a modification of the amino acid from P to S at position 331.
+The protein's natural variant, known as in LCATD;, features a modification of the amino acid from V to M at position 333.
+The protein's natural variant, known as in FED; results in reduced protein secretion and activity;, features a modification of the amino acid from L to F at position 338.
+The protein's natural variant, known as in LCATD;, features a modification of the amino acid from T to M at position 345.
+The protein's natural variant, known as in FED; results in reduced activity;, features a modification of the amino acid from R to C at position 347.
+The protein's natural variant, known as in FED;, features a modification of the amino acid from T to M at position 371.
+The protein's natural variant, known as in a patient with LCATD, features a modification of the amino acid from L to R at position 396.
+The protein's natural variant, known as in LCATD, features a modification of the amino acid from F to V at position 406.
+The protein's natural variant, known as in HLD11;, features a modification of the amino acid from T to I at position 26.
+The protein's natural variant, known as in HLD11; decreased localization to the nucleus and retained in the cytoplasm; loss of association with RNA polymerase III-transcribed genes; decreased association with RNA polymerase III complex; probably prevents RNA polymerase III complex assembly and activity;, features a modification of the amino acid from N to I at position 32.
+The protein's natural variant, known as in HLD11;, features a modification of the amino acid from M to V at position 65.
+The protein's natural variant, known as in HLD11; decreased localization to the nucleus and retained in the cytoplasm; loss of association with RNA polymerase III-transcribed genes; decreased association with RNA polymerase III complex; probably prevents RNA polymerase III complex assembly and activity;, features a modification of the amino acid from N to S at position 74.
+The protein's natural variant, known as in HLD11;, features a modification of the amino acid from V to A at position 94.
+The protein's natural variant, known as in HLD11;, features a modification of the amino acid from R to H at position 109.
+The protein's natural variant, known as in HLD11;, features a modification of the amino acid from G to D at position 132.
+The protein's natural variant, known as in HLD11;, features a modification of the amino acid from C to R at position 146.
+The protein's natural variant, known as in HLD11;, features a modification of the amino acid from R to Q at position 191.
+The protein's natural variant, known as in HLD11;, features a modification of the amino acid from I to T at position 262.
+The protein's natural variant, known as in TCS3; no effect on localization to the nucleus; no effect on association with RNA polymerase I and RNA polymerase III complexes;, features a modification of the amino acid from R to Q at position 279.
+The protein's natural variant, known as in TCS3;, features a modification of the amino acid from R to W at position 279.
+The protein's natural variant, known as in HLD11;, features a modification of the amino acid from E to K at position 324.
+The protein's natural variant, known as in strain: FVB/N, features a modification of the amino acid from A to T at position 77.
+The protein's natural variant, known as in strain: FVB/N, features a modification of the amino acid from T to I at position 506.
+The protein's natural variant, known as in strain: FVB/N, features a modification of the amino acid from L to S at position 535.
+The protein's natural variant, known as in NPCA3;, features a modification of the amino acid from R to H at position 306.
+The protein's natural variant, known as in NPCA3; unknown pathological significance;, features a modification of the amino acid from A to T at position 327.
+The protein's natural variant, known as in NPCA3; unknown pathological significance;, features a modification of the amino acid from V to G at position 670.
+The protein's natural variant, known as in NPCA3; unknown pathological significance;, features a modification of the amino acid from A to T at position 973.
+The protein's natural variant, known as in strain: 83-210, features a modification of the amino acid from VH to IS at position 60.
+The protein's natural variant, known as in strain: 83-210, features a modification of the amino acid from DR to SV at position 131.
+The protein's natural variant, known as in strain: 83-210, features a modification of the amino acid from S to N at position 139.
+The protein's natural variant, known as in strain: 83-210, features a modification of the amino acid from A to V at position 241.
+The protein's natural variant, known as in strain: 83-210, features a modification of the amino acid from P to S at position 246.
+The protein's natural variant, known as in strain: 83-210, features a modification of the amino acid from V to A at position 304.
+The protein's natural variant, known as in strain: Sim1, Sim2, Sim3, Sim4, Sim5, Sim6, Sim7 and Sim8, features a modification of the amino acid from Q to R at position 127.
+The protein's natural variant, known as in strain: Sim2, Sim3, Sim6, Sim7 and Sim8, features a modification of the amino acid from K to R at position 138.
+The protein's natural variant, known as in strain: Sim5, features a modification of the amino acid from A to T at position 171.
+The protein's natural variant, known as in allele CYP1A2*2;, features a modification of the amino acid from F to L at position 21.
+The protein's natural variant, known as in allele CYP1A2*15;, features a modification of the amino acid from P to R at position 42.
+The protein's natural variant, known as in allele CYP1A2*9;, features a modification of the amino acid from T to M at position 83.
+The protein's natural variant, known as in allele CYP1A2*10;, features a modification of the amino acid from E to Q at position 168.
+The protein's natural variant, known as in allele CYP1A2*11; drastic reduction in O-deethylation of phenacetin and 7-ethoxyresorufin; has a Vmax of approximately 5% of that of the wild-type and 5-fold lower Km value;, features a modification of the amino acid from F to L at position 186.
+The protein's natural variant, known as in allele CYP1A2*12;, features a modification of the amino acid from S to C at position 212.
+The protein's natural variant, known as in allele CYP1A2*13;, features a modification of the amino acid from G to S at position 299.
+The protein's natural variant, known as in allele CYP1A2*3; increases N-hydroxylation activity of heterocyclic amines; reduces phenacetin O-deethylation activity;, features a modification of the amino acid from D to N at position 348.
+The protein's natural variant, known as in allele CYP1A2*16;, features a modification of the amino acid from R to Q at position 377.
+The protein's natural variant, known as in allele CYP1A2*4; increases catalytic efficiency of N-hydroxylation towards some heterocyclic amines and reduces towards others; reduces catalytic efficiency of phenacetin O-deethylation due to a high decrease in the affinity for phenacetin;, features a modification of the amino acid from I to F at position 386.
+The protein's natural variant, known as in allele CYP1A2*5; increases N-hydroxylation activity of heterocyclic amines; reduces catalytic efficiency of phenacetin O-deethylation;, features a modification of the amino acid from C to Y at position 406.
+The protein's natural variant, known as in allele CYP1A2*6; not detected when expressed in heterologous system as it may be critical for maintenance of protein tertiary structure;, features a modification of the amino acid from R to W at position 431.
+The protein's natural variant, known as in allele CYP1A2*14;, features a modification of the amino acid from T to I at position 438.
+The protein's natural variant, known as in allele CYP1A2*8;, features a modification of the amino acid from R to H at position 456.
+The protein's natural variant, known as in CGD2;, features a modification of the amino acid from N to S at position 42.
+The protein's natural variant, known as in CGD2;, features a modification of the amino acid from G to C at position 44.
+The protein's natural variant, known as in CGD2;, features a modification of the amino acid from G to R at position 44.
+The protein's natural variant, known as in CGD2;, features a modification of the amino acid from R to Q at position 77.
+The protein's natural variant, known as in CGD2;, features a modification of the amino acid from G to E at position 78.
+The protein's natural variant, known as in CGD2;, features a modification of the amino acid from D to E at position 93.
+The protein's natural variant, known as in CGD2;, features a modification of the amino acid from R to P at position 102.
+The protein's natural variant, known as in CGD2;, features a modification of the amino acid from D to V at position 108.
+The protein's natural variant, known as in CGD2;, features a modification of the amino acid from A to V at position 128.
+The protein's natural variant, known as in CGD2;, features a modification of the amino acid from W to R at position 137.
+The protein's natural variant, known as in CGD2;, features a modification of the amino acid from A to D at position 140.
+The protein's natural variant, known as in CGD2, features a modification of the amino acid from DK to EV at position 161.
+The protein's natural variant, known as in CGD2;, features a modification of the amino acid from Q to E at position 169.
+The protein's natural variant, known as in CGD2;, features a modification of the amino acid from R to P at position 184.
+The protein's natural variant, known as in CGD2;, features a modification of the amino acid from A to V at position 202.
+The protein's natural variant, known as impairs interaction with NCF4;, features a modification of the amino acid from R to W at position 395.
+The protein's natural variant, known as in allele NAT1*17; a slow acetylator; has defective enzyme activity;, features a modification of the amino acid from R to W at position 64.
+The protein's natural variant, known as in allele NAT1*5;, features a modification of the amino acid from R to T at position 117.
+The protein's natural variant, known as in allele NAT1*11; catalyzes the N-acetylation of aromatic amines and the O- and N,O-acetylation of their N-hydroxylated metabolites at rates up to 2-fold higher;, features a modification of the amino acid from V to I at position 149.
+The protein's natural variant, known as in allele NAT1*5;, features a modification of the amino acid from RE to TQ at position 167.
+The protein's natural variant, known as in allele NAT1*14; a slow acetylator;, features a modification of the amino acid from R to Q at position 187.
+The protein's natural variant, known as in allele NAT1*21;, features a modification of the amino acid from M to V at position 205.
+The protein's natural variant, known as in allele NAT1*11;, features a modification of the amino acid from S to A at position 214.
+The protein's natural variant, known as in allele NAT1*22;, features a modification of the amino acid from D to V at position 251.
+The protein's natural variant, known as in allele NAT1*24;, features a modification of the amino acid from E to K at position 261.
+The protein's natural variant, known as in allele NAT1*25;, features a modification of the amino acid from I to V at position 263.
+The protein's natural variant, known as in AML; no effect on expression; no effect on DNA-binding or transactivation activity;, features a modification of the amino acid from H to L at position 84.
+The protein's natural variant, known as in AML; nuclear; no effect on expression; loss of DNA-binding and transactivation activity, features a modification of the amino acid from Q to QK at position 312.
+The protein's natural variant, known as in strain: B293, Z3910 and Z3918, features a modification of the amino acid from R to C at position 168.
+The protein's natural variant, known as in strain: Z3524, features a modification of the amino acid from A to S at position 192.
+The protein's natural variant, known as in strain: B293, Z3524, Z3910, Z3915 and Z3918, features a modification of the amino acid from I to L at position 237.
+The protein's natural variant, known as in strain: Z3915 and Z3524, features a modification of the amino acid from D to E at position 240.
+The protein's natural variant, known as in strain: B293, Z3910 and Z3918, features a modification of the amino acid from G to D at position 289.
+The protein's natural variant, known as in strain: Z4296, features a modification of the amino acid from T to S at position 336.
+The protein's natural variant, known as in pallidipin-1, features a modification of the amino acid from V to G at position 97.
+The protein's natural variant, known as in RP90; unknown pathological significance;, features a modification of the amino acid from A to T at position 122.
+The protein's natural variant, known as in RP90; unknown pathological significance;, features a modification of the amino acid from A to V at position 175.
+The protein's natural variant, known as in RP90; unknown pathological significance, features a modification of the amino acid from M to I at position 204.
+The protein's natural variant, known as in RP90; unknown pathological significance;, features a modification of the amino acid from M to T at position 239.
+The protein's natural variant, known as in RP90; unknown pathological significance;, features a modification of the amino acid from P to H at position 304.
+The protein's natural variant, known as in RP90; unknown pathological significance;, features a modification of the amino acid from M to T at position 313.
+The protein's natural variant, known as in RP90; unknown pathological significance;, features a modification of the amino acid from R to C at position 316.
+The protein's natural variant, known as in strain: Isolate TK 20569, features a modification of the amino acid from Q to H at position 162.
+The protein's natural variant, known as in strain: Isolate TK 4812, features a modification of the amino acid from I to T at position 371.
+The protein's natural variant, known as in strain: Linda, features a modification of the amino acid from A to S at position 45.
+The protein's natural variant, known as in strain: Linda, features a modification of the amino acid from E to K at position 481.
+The protein's natural variant, known as in strain: Linda, features a modification of the amino acid from AD to TE at position 492.
+The protein's natural variant, known as in strain: Linda, features a modification of the amino acid from A to S at position 508.
+The protein's natural variant, known as in strain: Linda, features a modification of the amino acid from A to T at position 525.
+The protein's natural variant, known as in strain: Linda, features a modification of the amino acid from A to P at position 527.
+The protein's natural variant, known as in amoxcillin-resistant strain, features a modification of the amino acid from A to S at position 82.
+The protein's natural variant, known as in amoxcillin-resistant strain, features a modification of the amino acid from A to E at position 116.
+The protein's natural variant, known as in VAIHS; there is a decreased expression of the mutant protein compared to wild-type;, features a modification of the amino acid from G to R at position 47.
+The protein's natural variant, known as in VAIHS;, features a modification of the amino acid from G to V at position 47.
+The protein's natural variant, known as in VAIHS;, features a modification of the amino acid from A to D at position 109.
+The protein's natural variant, known as in VAIHS;, features a modification of the amino acid from H to Q at position 112.
+The protein's natural variant, known as in SNDNS, features a modification of the amino acid from V to A at position 119.
+The protein's natural variant, known as in SNDNS, features a modification of the amino acid from G to S at position 142.
+The protein's natural variant, known as in VAIHS;, features a modification of the amino acid from R to Q at position 169.
+The protein's natural variant, known as in VAIHS;, features a modification of the amino acid from P to L at position 251.
+The protein's natural variant, known as in VAIHS;, features a modification of the amino acid from W to S at position 264.
+The protein's natural variant, known as in VAIHS;, features a modification of the amino acid from Y to C at position 453.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from I to M at position 342.
+The protein's natural variant, known as in CDCBM11; unknown pathological significance; results in increased microtubule depolymerization, features a modification of the amino acid from R to C at position 721.
+The protein's natural variant, known as in CDCBM11; unknown pathological significance; results in increased microtubule depolymerization, features a modification of the amino acid from P to S at position 949.
+The protein's natural variant, known as in CDCBM11; unknown pathological significance; results in increased microtubule depolymerization, features a modification of the amino acid from A to V at position 1559.
+The protein's natural variant, known as in CDCBM11; unknown pathological significance, features a modification of the amino acid from R to W at position 1602.
+The protein's natural variant, known as in CDCBM11; unknown pathological significance; results in increased microtubule depolymerization, features a modification of the amino acid from R to C at position 1624.
+The natural variant of this protein is characterized by an amino acid alteration from A to T at position 128.
+The protein's natural variant, known as in JBTS9; unknown pathological significance;, features a modification of the amino acid from S to R at position 117.
+The protein's natural variant, known as in JBTS9; benign variant;, features a modification of the amino acid from K to E at position 507.
+The protein's natural variant, known as in JBTS9;, features a modification of the amino acid from L to P at position 559.
+The protein's natural variant, known as in JBTS9;, features a modification of the amino acid from P to S at position 721.
+The protein's natural variant, known as in RP93;, features a modification of the amino acid from R to P at position 925.
+The protein's natural variant, known as in JBTS9;, features a modification of the amino acid from V to A at position 1045.
+The protein's natural variant, known as in JBTS9;, features a modification of the amino acid from Q to H at position 1096.
+The protein's natural variant, known as in MKS6 and JBTS9;, features a modification of the amino acid from T to M at position 1114.
+The protein's natural variant, known as in COACH2 and JBTS9;, features a modification of the amino acid from T to M at position 1116.
+The protein's natural variant, known as in JBTS9;, features a modification of the amino acid from P to S at position 1122.
+The protein's natural variant, known as in JBTS9;, features a modification of the amino acid from E to K at position 1126.
+The protein's natural variant, known as in JBTS9;, features a modification of the amino acid from V to A at position 1151.
+The protein's natural variant, known as in JBTS9;, features a modification of the amino acid from W to R at position 1182.
+The protein's natural variant, known as in JBTS9;, features a modification of the amino acid from R to C at position 1284.
+The protein's natural variant, known as in JBTS9;, features a modification of the amino acid from R to H at position 1284.
+The protein's natural variant, known as in JBTS9; unknown pathological significance;, features a modification of the amino acid from R to Q at position 1330.
+The protein's natural variant, known as in MKS6; unknown pathological significance, features a modification of the amino acid from G to V at position 1363.
+The protein's natural variant, known as in JBTS9;, features a modification of the amino acid from V to A at position 1430.
+The protein's natural variant, known as in JBTS9; digenic inheritance; the patient also carries mutation C-360 in CEP41;, features a modification of the amino acid from E to A at position 1447.
+The protein's natural variant, known as in MKS6; unknown pathological significance;, features a modification of the amino acid from T to S at position 1517.
+The protein's natural variant, known as in MKS6; unknown pathological significance, features a modification of the amino acid from W to G at position 1519.
+The protein's natural variant, known as in JBTS9;, features a modification of the amino acid from N to S at position 1520.
+The protein's natural variant, known as in JBTS9 and COACH2;, features a modification of the amino acid from R to C at position 1528.
+The protein's natural variant, known as in JBTS9;, features a modification of the amino acid from L to P at position 1551.
+The protein's natural variant, known as in JBTS9;, features a modification of the amino acid from D to V at position 1556.
+The protein's natural variant, known as in JBTS9, features a modification of the amino acid from Y to H at position 1568.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from M to I at position 228.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from P to T at position 416.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from Q to H at position 746.
+The protein's natural variant, known as in CMT2R; reduced stability of the mutant protein;, features a modification of the amino acid from E to V at position 227.
+The protein's natural variant, known as in OAS;, features a modification of the amino acid from R to C at position 278.
+The protein's natural variant, known as in OAS, features a modification of the amino acid from T to N at position 283.
+The protein's natural variant, known as in OAS;, features a modification of the amino acid from R to H at position 286.
+The protein's natural variant, known as in some patients with endometrial cancer, features a modification of the amino acid from P to S at position 8.
+The protein's natural variant, known as in ameloblastoma, features a modification of the amino acid from M to T at position 11.
+The protein's natural variant, known as in an ameloblastoma sample, features a modification of the amino acid from RT to GA at position 397.
+The protein's natural variant, known as in an ameloblastoma sample;, features a modification of the amino acid from H to R at position 439.
+The protein's natural variant, known as in HHT5; impaired protein processing and function;, features a modification of the amino acid from R to L at position 68.
+The protein's natural variant, known as in HHT5; impaired protein processing and function;, features a modification of the amino acid from P to L at position 85.
+The protein's natural variant, known as in HHT5; impaired protein processing and function;, features a modification of the amino acid from R to W at position 333.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from P to T at position 471.
+The protein's natural variant, known as in breast cancer; somatic mutation, features a modification of the amino acid from K to R at position 326.
+The protein's natural variant, known as in CPT-resistant leukemia, features a modification of the amino acid from M to T at position 370.
+The protein's natural variant, known as in CPT-resistant leukemia;, features a modification of the amino acid from D to G at position 533.
+The protein's natural variant, known as in CPT-resistant leukemia, features a modification of the amino acid from N to S at position 722.
+The protein's natural variant, known as in CPT-resistant lung cancer, features a modification of the amino acid from T to A at position 729.
+The protein's natural variant, known as in ICF2;, features a modification of the amino acid from C to G at position 408.
+The protein's natural variant, known as in strain: Isolate AMCC 122019, features a modification of the amino acid from F to I at position 220.
+The natural variant of this protein is characterized by an amino acid alteration from R to C at position 162.
+The protein's natural variant, known as originally reported as risk factor for Alzheimer disease; unknown pathological significance; does not reduce either amyloid-beta levels or APP expression;, features a modification of the amino acid from V to M at position 232.
+The natural variant of this protein is characterized by an amino acid alteration from P to L at position 297.
+The protein's natural variant, known as in SCA46; unknown pathological significance; reduced lysosomal localization; induces retention in the ER; reduction of proteolityc cleavage; loss of exonuclease activity;, features a modification of the amino acid from L to P at position 308.
+The protein's natural variant, known as in strain: 129/Ola and NIHSwiss, features a modification of the amino acid from R to P at position 138.
+The protein's natural variant, known as in strain: 129/Ola and NIHSwiss, features a modification of the amino acid from I to R at position 161.
+The protein's natural variant, known as in strain: 129/Ola and NIHSwiss, features a modification of the amino acid from N to D at position 165.
+The protein's natural variant, known as in strain: 129/Ola and NIHSwiss, features a modification of the amino acid from S to A at position 288.
+The protein's natural variant, known as in strain: 129/Ola and NIHSwiss, features a modification of the amino acid from L to R at position 296.
+The protein's natural variant, known as associated with decreased risk for Parkinson disease; gain-of-function variant; does not affect lysosomal localization;, features a modification of the amino acid from Q to P at position 65.
+The protein's natural variant, known as associated with increased risk for Parkinson disease; reduced potassium channel activity; does not affect lysosomal localization;, features a modification of the amino acid from M to T at position 393.
+The protein's natural variant, known as in CTRCT42, features a modification of the amino acid from V to M at position 50.
+The protein's natural variant, known as in dw, features a modification of the amino acid from W to C at position 261.
+The natural variant of this protein is characterized by an amino acid alteration from D to N at position 427.
+The protein's natural variant, known as in BSPC 111; spectinomycin resistant, features a modification of the amino acid from K to I at position 26.
+The protein's natural variant, known as in rpsE1; spectinomycin restistant, not a ram mutant, features a modification of the amino acid from G to V at position 28.
+The protein's natural variant, known as in rpsE9; suppresses S12 mutation K55D. Lethal in the absence of the S12 mutation, features a modification of the amino acid from G to R at position 104.
+The protein's natural variant, known as in rpsE8; suppresses S12 mutant K55D. RspE8 is lethal in the absence of the S12 mutation, features a modification of the amino acid from R to C at position 112.
+The protein's natural variant, known as in rpsE7; suppresses S12 mutant K55D. A ram mutation, features a modification of the amino acid from R to H at position 112.
+The protein's natural variant, known as found in patient with Joubert syndrome; unknown pathological significance;, features a modification of the amino acid from L to F at position 64.
+The protein's natural variant, known as found in patient with Joubert syndrome; unknown pathological significance;, features a modification of the amino acid from R to W at position 630.
+The protein's natural variant, known as in allele chain C(1) and in strain: NB, features a modification of the amino acid from G to V at position 26.
+The protein's natural variant, known as in allele chain C(1) and in strain: NB, features a modification of the amino acid from V to I at position 63.
+The protein's natural variant, known as in allele chains A, C(2), D(2), F, G(1) and G(2) and in strain: C57BL, features a modification of the amino acid from S to N at position 69.
+The protein's natural variant, known as in allele chain B(2) and in 1 BALB/C strain sequence, features a modification of the amino acid from S to T at position 69.
+The protein's natural variant, known as in allele chains F and G(2), features a modification of the amino acid from G to A at position 79.
+The protein's natural variant, known as in OOMD9; decreased protein level in patient cells;, features a modification of the amino acid from H to R at position 26.
+The protein's natural variant, known as in OOMD9; unknown pathological significance;, features a modification of the amino acid from R to Q at position 173.
+The protein's natural variant, known as in OOMD9; unknown pathological significance;, features a modification of the amino acid from I to V at position 198.
+The protein's natural variant, known as in OOMD9; unknown pathological significance;, features a modification of the amino acid from V to M at position 247.
+The protein's natural variant, known as in OOMD9; unknown pathological significance;, features a modification of the amino acid from E to K at position 303.
+The protein's natural variant, known as in strain: E32511, features a modification of the amino acid from D to G at position 15.
+The protein's natural variant, known as in strain: E32511, features a modification of the amino acid from I to T at position 35.
+The protein's natural variant, known as in strain: E32511, features a modification of the amino acid from T to A at position 65.
+The protein's natural variant, known as in strain: E32511, features a modification of the amino acid from S to N at position 77.
+The natural variant of this protein is characterized by an amino acid alteration from P to T at position 74.
+The protein's natural variant, known as in MRD54; decreased protein abundance; increased autophosphorylation; decreased neuronal migration;, features a modification of the amino acid from E to K at position 110.
+The protein's natural variant, known as in MRD54; decreased protein abundance; increased autophosphorylation; decreased neuronal migration;, features a modification of the amino acid from P to L at position 139.
+The protein's natural variant, known as in MRD54;, features a modification of the amino acid from P to L at position 213.
+The protein's natural variant, known as in MRD54; no effect on protein abundance; increased autophosphorylation; decreased neuronal migration;, features a modification of the amino acid from E to K at position 237.
+The protein's natural variant, known as in MRD54;, features a modification of the amino acid from R to S at position 284.
+The protein's natural variant, known as in MRD54; no effect on protein abundance; loss of autophosphorylation; changed function in neuronal migration;, features a modification of the amino acid from K to E at position 301.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from P to L at position 489.
+The natural variant of this protein is characterized by an amino acid alteration from V to M at position 13.
+The protein's natural variant, known as in CMT4H; found in patient's fibroblasts but absent from peripheral nerve where splicing defects and aberrant transcripts are detected;, features a modification of the amino acid from M to R at position 298.
+The protein's natural variant, known as in CMT4H;, features a modification of the amino acid from M to T at position 298.
+The protein's natural variant, known as in OPA11; does not affect localization to mitochondria; abolishes processing to mature form by MPP; results in decreased mitochondrial protein catabolism; has very low protease activity; results in mitochondrial fragmentation;, features a modification of the amino acid from R to W at position 206.
+The protein's natural variant, known as in RP54; induces proteasomal degradation;, features a modification of the amino acid from I to F at position 201.
+The protein's natural variant, known as in RP54; unknown pathological significance;, features a modification of the amino acid from R to C at position 320.
+The protein's natural variant, known as in RP54;, features a modification of the amino acid from D to N at position 372.
+The protein's natural variant, known as in RP54;, features a modification of the amino acid from L to P at position 612.
+The protein's natural variant, known as in RP54;, features a modification of the amino acid from V to D at position 615.
+The natural variant of this protein is characterized by an amino acid alteration from A to P at position 648.
+The protein's natural variant, known as found in patients with pathologic myopia; unknown pathological significance;, features a modification of the amino acid from Q to R at position 1176.
+The natural variant of this protein is characterized by an amino acid alteration from S to SS at position 1225.
+The protein's natural variant, known as in STHAG9;, features a modification of the amino acid from A to V at position 13.
+The protein's natural variant, known as in STHAG9;, features a modification of the amino acid from Q to E at position 76.
+The protein's natural variant, known as in STHAG9;, features a modification of the amino acid from E to D at position 136.
+The protein's natural variant, known as in strain: cv. Alc-0, features a modification of the amino acid from T to S at position 151.
+The protein's natural variant, known as in strain: cv. Ita-0, features a modification of the amino acid from S to C at position 170.
+The protein's natural variant, known as in strain: cv. Cle-1, cv. Cyr, cv. Ge-0, cv. Jea, cv. Kn-0, cv. Lz-0, cv. Mar1-2, cv. Mol-1, cv. Par-2, cv. Pon, cv. Rom-1, cv. St-0, cv. Tsu-0, cv. Vou-3, cv. Wha1 and cv. Wha2, features a modification of the amino acid from Q to K at position 329.
+The protein's natural variant, known as in strain: cv. Mar-2, features a modification of the amino acid from Q to R at position 445.
+The protein's natural variant, known as in strain: cv. Cvi-0, features a modification of the amino acid from A to C at position 457.
+The protein's natural variant, known as in strain: cv. Cle-1, cv. Cyr, cv. Ge-0, cv. Jea, cv. Kn-0, cv. Lz-0, cv. Mar1-2, cv. Mol-1, cv. Par-2, cv. Pon, cv. Rom-1, cv. St-0, cv. Tsu-0, cv. Vou-3, cv. Wha1 and cv. Wha2, features a modification of the amino acid from P to A at position 479.
+The protein's natural variant, known as in strain: cv. Bur-0, features a modification of the amino acid from V to G at position 518.
+The protein's natural variant, known as in strain: cv. Cro-1, cv. Lac-1, cv. Sakata and cv. Sha, features a modification of the amino acid from V to F at position 536.
+The protein's natural variant, known as in strain: cv. Sakata and cv. Sha, features a modification of the amino acid from V to I at position 542.
+The protein's natural variant, known as in strain: cv. Akita, features a modification of the amino acid from R to Q at position 618.
+The protein's natural variant, known as in strain: cv. Lac-1, features a modification of the amino acid from P to L at position 761.
+The protein's natural variant, known as in strain: cv. Cro-1, cv. Ita-0 and cv. Lac-1, features a modification of the amino acid from Q to QQ at position 848.
+The protein's natural variant, known as in strain: cv. Blh-1, features a modification of the amino acid from Q to QQQ at position 848.
+The protein's natural variant, known as in strain: cv. Sakata and cv. Sha, features a modification of the amino acid from Q to QQQQQ at position 848.
+The protein's natural variant, known as in strain: cv. Kn-0, cv. Lz-0, cv. Par-2 and cv. Pon, features a modification of the amino acid from R to S at position 858.
+The protein's natural variant, known as in strain: cv. Cro-1, cv. Sakata and cv. Sha, features a modification of the amino acid from S to T at position 874.
+The protein's natural variant, known as in strain: cv. Cro-1, features a modification of the amino acid from N to K at position 879.
+The protein's natural variant, known as in strain: cv. Lac-1, features a modification of the amino acid from H to R at position 884.
+The protein's natural variant, known as in strain: cv. Cle-1, cv. Cro-1, cv. Cyr, cv. Ge-0, cv. Ita-0, cv. Jea, cv. Kn-0, cv. Lac-1, cv. Lz-0, cv. Mar1-2, cv. Mol-1, cv. Par-2, cv. Pon, cv. Rom-1, cv. Sakata, cv. Sha, cv. St-0, cv. Tsu-0, cv. Vou-3, cv. Wha1 and cv. Wha2, features a modification of the amino acid from A to G at position 892.
+The protein's natural variant, known as in strain: cv. St-0 and cv. Tsu-0, features a modification of the amino acid from N to S at position 923.
+The protein's natural variant, known as in ODDD, features a modification of the amino acid from G to V at position 2.
+The protein's natural variant, known as in ODDD, features a modification of the amino acid from L to V at position 7.
+The protein's natural variant, known as in PPKCA1; can form functional gap junctions; results in enhanced hemichannel activity that causes increased cell death;, features a modification of the amino acid from G to V at position 8.
+The protein's natural variant, known as in ODDD, features a modification of the amino acid from L to I at position 11.
+The protein's natural variant, known as in ODDD;, features a modification of the amino acid from L to P at position 11.
+The protein's natural variant, known as in ODDD;, features a modification of the amino acid from Y to S at position 17.
+The protein's natural variant, known as in ODDD;, features a modification of the amino acid from S to P at position 18.
+The protein's natural variant, known as in ODDD;, features a modification of the amino acid from G to R at position 21.
+The protein's natural variant, known as in ODDD;, features a modification of the amino acid from G to E at position 22.
+The protein's natural variant, known as in ODDD, features a modification of the amino acid from K to T at position 23.
+The protein's natural variant, known as in ODDD, features a modification of the amino acid from S to P at position 27.
+The protein's natural variant, known as in ODDD, features a modification of the amino acid from I to M at position 31.
+The protein's natural variant, known as in ODDD;, features a modification of the amino acid from A to V at position 40.
+The protein's natural variant, known as found in a patient with hidrotic ectodermal dysplasia, abortive features of oculodentodigital dysplasia and extensive hyperkeratosis of the skin; unknown pathological significance; the patient also carries GJB2 variant H-127, features a modification of the amino acid from V to L at position 41.
+The protein's natural variant, known as in EKVP3; loss of localization to the plasma membrane, retention in the Golgi apparatus;, features a modification of the amino acid from A to V at position 44.
+The protein's natural variant, known as in ODDD, features a modification of the amino acid from D to H at position 47.
+The protein's natural variant, known as in ODDD, features a modification of the amino acid from Q to K at position 49.
+The protein's natural variant, known as in ODDD, features a modification of the amino acid from Q to P at position 49.
+The protein's natural variant, known as in ODDD, features a modification of the amino acid from Q to QQ at position 49.
+The protein's natural variant, known as in ODDD, features a modification of the amino acid from F to FF at position 52.
+The protein's natural variant, known as in ODDD, features a modification of the amino acid from P to H at position 59.
+The protein's natural variant, known as in ODDD, features a modification of the amino acid from S to Y at position 69.
+The protein's natural variant, known as in HSS; overlapping features with oculodentodigital dysplasia;, features a modification of the amino acid from R to H at position 76.
+The protein's natural variant, known as in ODDD;, features a modification of the amino acid from R to S at position 76.
+The protein's natural variant, known as in ODDD; de novo mutation found in a sporadic case, features a modification of the amino acid from S to Y at position 86.
+The protein's natural variant, known as in ODDD, features a modification of the amino acid from L to V at position 90.
+The protein's natural variant, known as in ODDD, features a modification of the amino acid from H to R at position 95.
+The protein's natural variant, known as in ODDD, features a modification of the amino acid from V to A at position 96.
+The protein's natural variant, known as in ODDD, features a modification of the amino acid from V to E at position 96.
+The protein's natural variant, known as in ODDD;, features a modification of the amino acid from V to M at position 96.
+The protein's natural variant, known as in ODDD, features a modification of the amino acid from Y to C at position 98.
+The protein's natural variant, known as in ODDD;, features a modification of the amino acid from K to N at position 102.
+The protein's natural variant, known as in ODDD, features a modification of the amino acid from L to P at position 106.
+The protein's natural variant, known as in ODDD, features a modification of the amino acid from L to R at position 106.
+The protein's natural variant, known as in ODDD, features a modification of the amino acid from E to D at position 110.
+The protein's natural variant, known as in ODDD, features a modification of the amino acid from L to P at position 113.
+The protein's natural variant, known as in ODDD;, features a modification of the amino acid from I to T at position 130.
+The protein's natural variant, known as in ODDD, features a modification of the amino acid from K to E at position 134.
+The protein's natural variant, known as in ODDD, features a modification of the amino acid from K to N at position 134.
+The protein's natural variant, known as in ODDD, features a modification of the amino acid from G to R at position 138.
+The protein's natural variant, known as in SDTY3;, features a modification of the amino acid from G to S at position 143.
+The protein's natural variant, known as in ODDD;, features a modification of the amino acid from M to T at position 147.
+The protein's natural variant, known as in ODDD;, features a modification of the amino acid from R to Q at position 148.
+The protein's natural variant, known as in ODDD, features a modification of the amino acid from T to A at position 154.
+The protein's natural variant, known as in ODDD, features a modification of the amino acid from T to N at position 154.
+The protein's natural variant, known as in ODDD; atypical form of ODDD characterized by the predominance of the ocular involvement and by the absence of hand and/or foot syndactyly and absence of any neurologic signs;, features a modification of the amino acid from H to P at position 194.
+The protein's natural variant, known as in ODDD, features a modification of the amino acid from S to F at position 201.
+The protein's natural variant, known as in ODDD;, features a modification of the amino acid from R to H at position 202.
+The protein's natural variant, known as in ODDD;, features a modification of the amino acid from K to R at position 206.
+The protein's natural variant, known as in ODDD;, features a modification of the amino acid from V to L at position 216.
+The protein's natural variant, known as in ODDD, features a modification of the amino acid from S to Y at position 220.
+The protein's natural variant, known as in EKVP3; loss of localization to the plasma membrane, retention in the Golgi apparatus;, features a modification of the amino acid from E to D at position 227.
+The protein's natural variant, known as in CMDR;, features a modification of the amino acid from R to Q at position 239.
+The protein's natural variant, known as in congenital heart malformations, features a modification of the amino acid from R to W at position 239.
+The protein's natural variant, known as in congenital heart malformations, features a modification of the amino acid from S to T at position 251.
+The protein's natural variant, known as in congenital heart malformations, features a modification of the amino acid from A to P at position 253.
+The protein's natural variant, known as in congenital heart malformations, features a modification of the amino acid from P to L at position 283.
+The protein's natural variant, known as in congenital heart malformations, features a modification of the amino acid from T to N at position 290.
+The natural variant of this protein is characterized by an amino acid alteration from T to A at position 326.
+The protein's natural variant, known as in heart malformations, features a modification of the amino acid from E to G at position 352.
+The protein's natural variant, known as in HLHS1 and AVSD3; unknown pathological significance; associated with Q-376 in one individual with atrioventricular septal defect; abolishes phosphorylation by PKA and PKC;, features a modification of the amino acid from R to Q at position 362.
+The protein's natural variant, known as in heart malformations; shows abnormalities in the regulation of cell-cell communication as compared with cells expressing normal GJA1, features a modification of the amino acid from S to P at position 364.
+The protein's natural variant, known as in heart malformations, features a modification of the amino acid from S to N at position 365.
+The natural variant of this protein is characterized by an amino acid alteration from S to G at position 373.
+The protein's natural variant, known as in HLHS1 and AVSD3; unknown pathological significance; associated with Q-362 in one individual with atrioventricular septal defect; abolishes phosphorylation by PKA and PKC;, features a modification of the amino acid from R to Q at position 376.
+The protein's natural variant, known as in GSD2;, features a modification of the amino acid from S to P at position 46.
+The protein's natural variant, known as in allele GAA*2; lower affinity for glycogen and starch but not for lower-molecular weight substrates;, features a modification of the amino acid from D to N at position 91.
+The protein's natural variant, known as in GSD2; infantile form; severe; loss of activity; shows enzyme localization primarily in the ER-Golgi compartment suggesting that mutation could affect the normal processing and stability of the enzyme;, features a modification of the amino acid from C to G at position 103.
+The protein's natural variant, known as in GSD2, features a modification of the amino acid from C to R at position 103.
+The protein's natural variant, known as in GSD2, features a modification of the amino acid from C to G at position 108.
+The protein's natural variant, known as in GSD2, features a modification of the amino acid from C to F at position 127.
+The protein's natural variant, known as in GSD2;, features a modification of the amino acid from R to H at position 190.
+The protein's natural variant, known as in GSD2; extremely low residual enzymatic activity, features a modification of the amino acid from Y to C at position 191.
+The protein's natural variant, known as in GSD2, features a modification of the amino acid from L to P at position 208.
+The protein's natural variant, known as in GSD2, features a modification of the amino acid from P to L at position 217.
+The protein's natural variant, known as in GSD2; infantile form; severe; loss of activity;, features a modification of the amino acid from G to R at position 219.
+The protein's natural variant, known as in GSD2;, features a modification of the amino acid from R to P at position 224.
+The protein's natural variant, known as in GSD2;, features a modification of the amino acid from R to Q at position 224.
+The protein's natural variant, known as in GSD2; infantile; mild partial loss of activity;, features a modification of the amino acid from R to W at position 224.
+The protein's natural variant, known as in GSD2, features a modification of the amino acid from T to K at position 234.
+The protein's natural variant, known as in GSD2, features a modification of the amino acid from T to R at position 234.
+The protein's natural variant, known as in GSD2;, features a modification of the amino acid from A to V at position 237.
+The protein's natural variant, known as in GSD2;, features a modification of the amino acid from S to L at position 251.
+The protein's natural variant, known as in GSD2;, features a modification of the amino acid from S to L at position 254.
+The protein's natural variant, known as in GSD2; infantile; severe;, features a modification of the amino acid from E to K at position 262.
+The protein's natural variant, known as in GSD2;, features a modification of the amino acid from P to S at position 266.
+The natural variant of this protein is characterized by an amino acid alteration from T to A at position 271.
+The protein's natural variant, known as in GSD2; juvenile form; mild; partial loss of activity;, features a modification of the amino acid from P to R at position 285.
+The protein's natural variant, known as in GSD2;, features a modification of the amino acid from P to S at position 285.
+The protein's natural variant, known as in GSD2;, features a modification of the amino acid from L to F at position 291.
+The protein's natural variant, known as in GSD2, features a modification of the amino acid from L to P at position 291.
+The protein's natural variant, known as in GSD2; juvenile form; mild; partial loss of activity;, features a modification of the amino acid from Y to C at position 292.
+The protein's natural variant, known as in GSD2; infantile form; severe; almost complete loss of activity;, features a modification of the amino acid from G to R at position 293.
+The protein's natural variant, known as in GSD2; infantile form;, features a modification of the amino acid from L to R at position 299.
+The protein's natural variant, known as in GSD2, features a modification of the amino acid from H to L at position 308.
+The protein's natural variant, known as in GSD2; infantile form; severe; complete loss of activity, features a modification of the amino acid from H to P at position 308.
+The protein's natural variant, known as in GSD2; severe;, features a modification of the amino acid from G to R at position 309.
+The protein's natural variant, known as found in a patient with GSD2; unknown pathological significance;, features a modification of the amino acid from V to G at position 310.
+The protein's natural variant, known as in GSD2; infantile form; severe; loss of activity, features a modification of the amino acid from L to R at position 312.
+The protein's natural variant, known as in GSD2, features a modification of the amino acid from N to I at position 316.
+The protein's natural variant, known as in GSD2, features a modification of the amino acid from M to K at position 318.
+The protein's natural variant, known as in GSD2; severe;, features a modification of the amino acid from M to T at position 318.
+The protein's natural variant, known as in GSD2;, features a modification of the amino acid from P to L at position 324.
+The protein's natural variant, known as in GSD2; infantile form; severe, features a modification of the amino acid from W to G at position 330.
+The protein's natural variant, known as in GSD2;, features a modification of the amino acid from G to E at position 335.
+The protein's natural variant, known as in GSD2;, features a modification of the amino acid from G to R at position 335.
+The protein's natural variant, known as in GSD2, features a modification of the amino acid from P to R at position 347.
+The protein's natural variant, known as in GSD2; infantile form; severe; loss of activity;, features a modification of the amino acid from L to P at position 355.
+The natural variant of this protein is characterized by an amino acid alteration from G to R at position 359.
+The protein's natural variant, known as in GSD2; juvenile form; severe;, features a modification of the amino acid from P to L at position 361.
+The protein's natural variant, known as in GSD2; infantile form; severe; loss of activity, features a modification of the amino acid from C to R at position 374.
+The protein's natural variant, known as in GSD2; extremely low residual enzymatic activity;, features a modification of the amino acid from R to L at position 375.
+The protein's natural variant, known as in GSD2; severe;, features a modification of the amino acid from G to R at position 377.
+The protein's natural variant, known as found in a patient with GSD2; unknown pathological significance;, features a modification of the amino acid from M to V at position 391.
+The protein's natural variant, known as in GSD2;, features a modification of the amino acid from P to L at position 397.
+The protein's natural variant, known as in GSD2; extremely low residual enzymatic activity, features a modification of the amino acid from Q to R at position 401.
+The protein's natural variant, known as in GSD2; severe, features a modification of the amino acid from W to R at position 402.
+The protein's natural variant, known as in GSD2; severe;, features a modification of the amino acid from D to N at position 404.
+The protein's natural variant, known as in GSD2; infantile form; severe; loss of activity, features a modification of the amino acid from L to P at position 405.
+The protein's natural variant, known as in GSD2; juvenile form; severe;, features a modification of the amino acid from M to V at position 408.
+The protein's natural variant, known as in GSD2, features a modification of the amino acid from D to V at position 419.
+The protein's natural variant, known as in GSD2; juvenile form; severe;, features a modification of the amino acid from R to C at position 437.
+The protein's natural variant, known as in GSD2; unknown pathological significance;, features a modification of the amino acid from R to H at position 437.
+The protein's natural variant, known as in GSD2, features a modification of the amino acid from A to P at position 445.
+The protein's natural variant, known as in GSD2; juvenile form; almost complete loss of activity, features a modification of the amino acid from Y to F at position 455.
+The protein's natural variant, known as in GSD2, features a modification of the amino acid from P to H at position 457.
+The protein's natural variant, known as in GSD2; juvenile form, features a modification of the amino acid from P to L at position 457.
+The protein's natural variant, known as in GSD2; severe; loss of activity;, features a modification of the amino acid from G to R at position 478.
+The protein's natural variant, known as in GSD2; severe; loss of activity;, features a modification of the amino acid from W to R at position 481.
+The protein's natural variant, known as in GSD2, features a modification of the amino acid from P to R at position 482.
+The protein's natural variant, known as in GSD2, features a modification of the amino acid from G to V at position 483.
+The protein's natural variant, known as in GSD2, features a modification of the amino acid from A to P at position 486.
+The protein's natural variant, known as in GSD2; severe;, features a modification of the amino acid from D to N at position 489.
+The protein's natural variant, known as in GSD2; severe; loss of activity;, features a modification of the amino acid from M to T at position 519.
+The protein's natural variant, known as in GSD2, features a modification of the amino acid from M to V at position 519.
+The protein's natural variant, known as in GSD2; severe;, features a modification of the amino acid from E to K at position 521.
+The protein's natural variant, known as in GSD2, features a modification of the amino acid from E to Q at position 521.
+The protein's natural variant, known as in GSD2; no residual enzymatic activity;, features a modification of the amino acid from P to A at position 522.
+The protein's natural variant, known as in GSD2;, features a modification of the amino acid from P to S at position 522.
+The protein's natural variant, known as in GSD2, features a modification of the amino acid from S to Y at position 523.
+The protein's natural variant, known as in GSD2, features a modification of the amino acid from F to Y at position 525.
+The protein's natural variant, known as in GSD2; mild; requires 2 nucleotide substitutions;, features a modification of the amino acid from S to V at position 529.
+The protein's natural variant, known as in GSD2; mild; partial loss of activity;, features a modification of the amino acid from P to L at position 545.
+The protein's natural variant, known as in GSD2; juvenile form; mild; partial loss of activity, features a modification of the amino acid from G to R at position 549.
+The protein's natural variant, known as in GSD2; infantile/juvenile form; severe; loss of activity;, features a modification of the amino acid from L to P at position 552.
+The protein's natural variant, known as in GSD2;, features a modification of the amino acid from I to F at position 557.
+The protein's natural variant, known as in GSD2, features a modification of the amino acid from C to S at position 558.
+The protein's natural variant, known as in GSD2; infantile form, features a modification of the amino acid from S to P at position 566.
+The protein's natural variant, known as in GSD2, features a modification of the amino acid from H to L at position 568.
+The protein's natural variant, known as in GSD2;, features a modification of the amino acid from N to K at position 570.
+The protein's natural variant, known as in GSD2;, features a modification of the amino acid from H to Q at position 572.
+The protein's natural variant, known as in GSD2, features a modification of the amino acid from Y to C at position 575.
+The protein's natural variant, known as in GSD2; juvenile form, features a modification of the amino acid from Y to S at position 575.
+The natural variant of this protein is characterized by an amino acid alteration from G to A at position 576.
+The protein's natural variant, known as in GSD2, features a modification of the amino acid from G to R at position 576.
+The protein's natural variant, known as retains about half of the activity compared with the wild-type;, features a modification of the amino acid from G to S at position 576.
+The protein's natural variant, known as in GSD2; infantile form; severe; loss of activity;, features a modification of the amino acid from E to K at position 579.
+The protein's natural variant, known as in GSD2, features a modification of the amino acid from R to M at position 585.
+The protein's natural variant, known as in GSD2;, features a modification of the amino acid from R to H at position 594.
+The protein's natural variant, known as in GSD2;, features a modification of the amino acid from R to P at position 594.
+The protein's natural variant, known as in GSD2; no residual enzymatic activity;, features a modification of the amino acid from S to Y at position 599.
+The protein's natural variant, known as in GSD2; juvenile form; loss of activity;, features a modification of the amino acid from R to C at position 600.
+The protein's natural variant, known as in GSD2; infantile form;, features a modification of the amino acid from R to H at position 600.
+The protein's natural variant, known as in GSD2;, features a modification of the amino acid from S to L at position 601.
+The protein's natural variant, known as in GSD2;, features a modification of the amino acid from T to A at position 602.
+The protein's natural variant, known as in GSD2; infantile form; severe; loss of activity;, features a modification of the amino acid from G to D at position 607.
+The protein's natural variant, known as in GSD2, features a modification of the amino acid from A to V at position 610.
+The protein's natural variant, known as found in a patient with GSD2; unknown pathological significance;, features a modification of the amino acid from G to D at position 611.
+The protein's natural variant, known as in GSD2;, features a modification of the amino acid from H to Q at position 612.
+The protein's natural variant, known as in GSD2, features a modification of the amino acid from H to Y at position 612.
+The protein's natural variant, known as in GSD2;, features a modification of the amino acid from T to K at position 614.
+The protein's natural variant, known as in GSD2; infantile/adult form;, features a modification of the amino acid from G to R at position 615.
+The protein's natural variant, known as in GSD2; loss of function of the mutant enzyme;, features a modification of the amino acid from S to R at position 619.
+The protein's natural variant, known as in GSD2, features a modification of the amino acid from S to P at position 627.
+The protein's natural variant, known as in GSD2;, features a modification of the amino acid from N to K at position 635.
+The protein's natural variant, known as in GSD2, features a modification of the amino acid from G to V at position 638.
+The protein's natural variant, known as in GSD2;, features a modification of the amino acid from G to W at position 638.
+The protein's natural variant, known as in GSD2; unknown pathological significance;, features a modification of the amino acid from L to V at position 641.
+The protein's natural variant, known as in GSD2; infantile form;, features a modification of the amino acid from G to R at position 643.
+The protein's natural variant, known as in GSD2; infantile form; most common mutation; deficient in phosphorylation and in proteolytic processing;, features a modification of the amino acid from D to E at position 645.
+The protein's natural variant, known as in GSD2; almost complete loss of activity;, features a modification of the amino acid from D to H at position 645.
+The protein's natural variant, known as in GSD2;, features a modification of the amino acid from D to N at position 645.
+The protein's natural variant, known as in GSD2;, features a modification of the amino acid from C to W at position 647.
+The protein's natural variant, known as in GSD2;, features a modification of the amino acid from G to D at position 648.
+The protein's natural variant, known as in GSD2;, features a modification of the amino acid from G to S at position 648.
+The protein's natural variant, known as in GSD2; loss of function of the mutant enzyme;, features a modification of the amino acid from R to H at position 660.
+The protein's natural variant, known as in GSD2;, features a modification of the amino acid from R to Q at position 672.
+The protein's natural variant, known as in GSD2, features a modification of the amino acid from R to T at position 672.
+The protein's natural variant, known as in GSD2;, features a modification of the amino acid from R to W at position 672.
+The protein's natural variant, known as in allele GAA*4;, features a modification of the amino acid from E to K at position 689.
+The protein's natural variant, known as in GSD2; no enzymatic activity; shows enzyme localization primarily in the ER-Golgi compartment suggesting that mutation could affect the normal processing and stability of the enzyme;, features a modification of the amino acid from R to C at position 702.
+The protein's natural variant, known as in GSD2;, features a modification of the amino acid from R to L at position 702.
+The protein's natural variant, known as in GSD2; unknown pathological significance, features a modification of the amino acid from L to P at position 705.
+The protein's natural variant, known as in GSD2; adult form;, features a modification of the amino acid from R to W at position 725.
+The protein's natural variant, known as in GSD2;, features a modification of the amino acid from T to N at position 737.
+The protein's natural variant, known as in GSD2, features a modification of the amino acid from Q to K at position 743.
+The protein's natural variant, known as in GSD2;, features a modification of the amino acid from W to C at position 746.
+The protein's natural variant, known as in GSD2;, features a modification of the amino acid from W to G at position 746.
+The protein's natural variant, known as in GSD2;, features a modification of the amino acid from W to S at position 746.
+The protein's natural variant, known as in GSD2;, features a modification of the amino acid from Y to C at position 766.
+The protein's natural variant, known as in GSD2; infantile form, features a modification of the amino acid from P to R at position 768.
+The protein's natural variant, known as in GSD2, features a modification of the amino acid from R to P at position 819.
+The protein's natural variant, known as in GSD2; infantile form; severe; loss of activity, features a modification of the amino acid from A to D at position 880.
+The protein's natural variant, known as in GSD2; infantile form; severe, features a modification of the amino acid from L to Q at position 901.
+The protein's natural variant, known as in GSD2;, features a modification of the amino acid from P to R at position 913.
+The protein's natural variant, known as in GSD2;, features a modification of the amino acid from V to F at position 916.
+The protein's natural variant, known as in GSD2, features a modification of the amino acid from N to NGVPVSN at position 925.
+The protein's natural variant, known as loss of glycosylation site;, features a modification of the amino acid from T to I at position 927.
+The protein's natural variant, known as in GSD2, features a modification of the amino acid from L to P at position 935.
+The protein's natural variant, known as in GSD2;, features a modification of the amino acid from V to D at position 949.
+The protein's natural variant, known as decreased transport reaction kinetics; decreased affinity for zinc ions; decreased zinc ion import into organelle; no effect on protein abundance;, features a modification of the amino acid from R to W at position 325.
+The natural variant of this protein is characterized by an amino acid alteration from R to H at position 42.
+The protein's natural variant, known as in Sol i 4.02, features a modification of the amino acid from R to K at position 51.
+The natural variant of this protein is characterized by an amino acid alteration from W to I at position 56.
+The protein's natural variant, known as in Sol i 4.02, features a modification of the amino acid from W to L at position 56.
+The protein's natural variant, known as in Sol i 4.02, features a modification of the amino acid from A to I at position 84.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 111.
+The protein's natural variant, known as in HH12; uncertain pathological significance; the patient also carries mutations in PROKR2 and FGFR1, features a modification of the amino acid from R to C at position 31.
+The protein's natural variant, known as in CMH15;, features a modification of the amino acid from L to M at position 277.
+The protein's natural variant, known as in CMD1W; significantly alters metavinculin-mediated cross-linking of actin filaments;, features a modification of the amino acid from R to W at position 975.
+The natural variant of this protein is characterized by an amino acid alteration from P to R at position 14.
+The natural variant of this protein is characterized by an amino acid alteration from K to E at position 50.
+The natural variant of this protein is characterized by an amino acid alteration from F to L at position 100.
+The natural variant of this protein is characterized by an amino acid alteration from L to P at position 118.
+The natural variant of this protein is characterized by an amino acid alteration from G to A at position 243.
+The natural variant of this protein is characterized by an amino acid alteration from D to G at position 268.
+The natural variant of this protein is characterized by an amino acid alteration from E to D at position 320.
+The natural variant of this protein is characterized by an amino acid alteration from V to L at position 337.
+The natural variant of this protein is characterized by an amino acid alteration from F to S at position 338.
+The natural variant of this protein is characterized by an amino acid alteration from D to G at position 504.
+The natural variant of this protein is characterized by an amino acid alteration from L to P at position 508.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 510.
+The natural variant of this protein is characterized by an amino acid alteration from Q to R at position 528.
+The natural variant of this protein is characterized by an amino acid alteration from D to V at position 570.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from G to R at position 126.
+The natural variant of this protein is characterized by an amino acid alteration from A to AA at position 110.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from V to I at position 537.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from A to E at position 1571.
+The protein's natural variant, known as in allele 4, features a modification of the amino acid from G to D at position 75.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from E to K at position 21.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from D to G at position 81.
+The protein's natural variant, known as in XLID104;, features a modification of the amino acid from C to R at position 553.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from N to D at position 297.
+The protein's natural variant, known as in MRT60; impairs interaction with TAF11;, features a modification of the amino acid from L to H at position 31.
+The protein's natural variant, known as in MRT60; impairs interaction with TAF11;, features a modification of the amino acid from M to K at position 40.
+The protein's natural variant, known as in strain: XA, features a modification of the amino acid from S to N at position 51.
+The protein's natural variant, known as in strain: XA, features a modification of the amino acid from T to A at position 266.
+The protein's natural variant, known as in strain: XA, features a modification of the amino acid from A to S at position 270.
+The protein's natural variant, known as in strain: XA, features a modification of the amino acid from C to S at position 274.
+The protein's natural variant, known as in strain: XA, features a modification of the amino acid from L to F at position 319.
+The protein's natural variant, known as in strain: XA, features a modification of the amino acid from T to I at position 378.
+The protein's natural variant, known as in strain: XA, features a modification of the amino acid from P to S at position 400.
+The protein's natural variant, known as in strain: XA, features a modification of the amino acid from S to N at position 411.
+The protein's natural variant, known as in strain: XA, features a modification of the amino acid from T to A at position 422.
+The protein's natural variant, known as in PGL6; loss of protein expression;, features a modification of the amino acid from E to K at position 141.
+The protein's natural variant, known as in PGL6; loss of protein expression;, features a modification of the amino acid from M to V at position 147.
+The protein's natural variant, known as in PGL6; loss of protein expression;, features a modification of the amino acid from P to T at position 239.
+The protein's natural variant, known as in strain: Isolate French, features a modification of the amino acid from S to F at position 29.
+The protein's natural variant, known as in strain: Isolate French, features a modification of the amino acid from A to G at position 39.
+The protein's natural variant, known as in strain: Isolate French, features a modification of the amino acid from S to C at position 247.
+The protein's natural variant, known as in strain: Isolate French, features a modification of the amino acid from P to A at position 267.
+The protein's natural variant, known as in SGBS1;, features a modification of the amino acid from W to R at position 296.
+The protein's natural variant, known as in strain: SIKA1 and SIKA2, features a modification of the amino acid from SL to FF at position 20.
+The protein's natural variant, known as in strain: VS102, features a modification of the amino acid from V to I at position 90.
+The protein's natural variant, known as in ECTD14; unknown pathological significance, features a modification of the amino acid from C to W at position 80.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from A to T at position 166.
+The protein's natural variant, known as in DFNB98; unknown pathological significance, features a modification of the amino acid from P to L at position 178.
+The protein's natural variant, known as in DFNB98; unknown pathological significance, features a modification of the amino acid from V to A at position 388.
+The protein's natural variant, known as in STHAG10; unknown pathological significance, features a modification of the amino acid from R to Q at position 444.
+The protein's natural variant, known as in STHAG10; unknown pathological significance, features a modification of the amino acid from R to W at position 444.
+The protein's natural variant, known as in ECTD14; unknown pathological significance, features a modification of the amino acid from L to Q at position 490.
+The protein's natural variant, known as in ECTD14; unknown pathological significance, features a modification of the amino acid from G to D at position 525.
+The protein's natural variant, known as in ECTD14; unknown pathological significance;, features a modification of the amino acid from V to F at position 576.
+The protein's natural variant, known as in ECTD14; unknown pathological significance, features a modification of the amino acid from S to I at position 585.
+The protein's natural variant, known as in ECTD14; unknown pathological significance;, features a modification of the amino acid from Y to N at position 618.
+The protein's natural variant, known as in STHAG10; unknown pathological significance, features a modification of the amino acid from F to S at position 626.
+The protein's natural variant, known as in ECTD14 and STHAG10; unknown pathological significance;, features a modification of the amino acid from D to N at position 639.
+The protein's natural variant, known as in rs, features a modification of the amino acid from R to W at position 886.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 171.
+The natural variant of this protein is characterized by an amino acid alteration from D to E at position 175.
+The protein's natural variant, known as in strain: IFO 1060, features a modification of the amino acid from P to S at position 12.
+The protein's natural variant, known as in strain: GA2181, features a modification of the amino acid from GE to RG at position 23.
+The protein's natural variant, known as in strain: MNb027, features a modification of the amino acid from S to N at position 47.
+The protein's natural variant, known as in strain: UT.002, features a modification of the amino acid from L to F at position 254.
+The protein's natural variant, known as in strain: OH.036, features a modification of the amino acid from N to K at position 312.
+The protein's natural variant, known as in strain: GA2181, MNb027, OH.036 and UT.002, features a modification of the amino acid from L to V at position 315.
+The protein's natural variant, known as in strain: UT.002, features a modification of the amino acid from S to A at position 339.
+The protein's natural variant, known as found in patients with amyotrophic lateral sclerosis;, features a modification of the amino acid from L to P at position 199.
+The protein's natural variant, known as in AHUS6, features a modification of the amino acid from D to E at position 34.
+The protein's natural variant, known as in AHUS6; cells transfected with the mutant are less effective in converting C3b to iC3b on the cell surface after complement activation;, features a modification of the amino acid from A to T at position 43.
+The protein's natural variant, known as in AHUS6; cells transfected with the mutant are less effective in converting C3b to iC3b on the cell surface after complement activation;, features a modification of the amino acid from D to G at position 53.
+The protein's natural variant, known as in AHUS6; cells transfected with the mutant are less effective in converting C3b to iC3b on the cell surface after complement activation;, features a modification of the amino acid from V to L at position 81.
+The protein's natural variant, known as in AHUS6;, features a modification of the amino acid from A to G at position 236.
+The protein's natural variant, known as in THPH12 and AHUS6; cells transfected with the mutant are less effective in converting C3b to iC3b on the cell surface after complement activation;, features a modification of the amino acid from D to Y at position 486.
+The protein's natural variant, known as in AHUS6; cells transfected with the mutant are less effective in converting C3b to iC3b on the cell surface after complement activation;, features a modification of the amino acid from P to S at position 495.
+The protein's natural variant, known as in AHUS6; cells transfected with the mutant are less effective in converting C3b to iC3b on the cell surface after complement activation;, features a modification of the amino acid from P to L at position 501.
+The protein's natural variant, known as found in patients with acute myeloid leukemia; unknown pathological significance, features a modification of the amino acid from K to R at position 287.
+The protein's natural variant, known as found in patients with acute myeloid leukemia; unknown pathological significance; loss of the ability to negatively regulate signaling pathways; promotes cell cycle progression; decreases apoptosis, features a modification of the amino acid from Q to QSK at position 365.
+The protein's natural variant, known as in NSLL;, features a modification of the amino acid from Q to P at position 367.
+The protein's natural variant, known as found in patients with acute myeloid leukemia; unknown pathological significance; loss of the ability to negatively regulate signaling pathways; promotes cell cycle progression; decreases apoptosis;, features a modification of the amino acid from Y to H at position 371.
+The protein's natural variant, known as in NSLL; dominant-negative; impairs CBL-mediated ubiquitination, internalization and degradation of the EGF receptor/EGFR; decreases the ability to negatively regulate EGFR signaling;, features a modification of the amino acid from K to E at position 382.
+The protein's natural variant, known as in NSLL; dominant-negative; impairs CBL-mediated ubiquitination, internalization and degradation of the EGF receptor/EGFR; decreases the ability to negatively regulate EGFR signaling;, features a modification of the amino acid from D to Y at position 390.
+The protein's natural variant, known as in NSLL; dominant-negative; impairs CBL-mediated ubiquitination, internalization and degradation of the EGF receptor/EGFR; decreases the ability to negatively regulate EGFR signaling;, features a modification of the amino acid from R to Q at position 420.
+The protein's natural variant, known as found in patients with acute myeloid leukemia; unknown pathological significance, features a modification of the amino acid from R to L at position 499.
+The protein's natural variant, known as in minor component, features a modification of the amino acid from D to G at position 77.
+The protein's natural variant, known as in CHTD4; the mutation results in reduced transcription activation of the EGR1 promoter; does not affect transcription activation of the APOBFT promoter, features a modification of the amino acid from Q to QQ at position 75.
+The protein's natural variant, known as in CHTD4, features a modification of the amino acid from D to V at position 170.
+The protein's natural variant, known as in CHTD4; the mutation results in increased transcription activation of the EGR1 promoter; transcription activation of the APOB promoter is decreased;, features a modification of the amino acid from N to I at position 205.
+The protein's natural variant, known as in CHTD4, features a modification of the amino acid from E to D at position 251.
+The protein's natural variant, known as in CHTD4; the mutation results in reduced transcriptional activity;, features a modification of the amino acid from S to Y at position 341.
+The protein's natural variant, known as in CHTD4;, features a modification of the amino acid from A to S at position 412.
+The protein's natural variant, known as in strain: HK104 and HK105, features a modification of the amino acid from L to F at position 4.
+The protein's natural variant, known as in strain: BW287, EG4181, EG4207A, HK104, HK105, JU403, JU439, JU516, JU793, PB800 and PB826, features a modification of the amino acid from I to T at position 46.
+The protein's natural variant, known as in strain: HK104 and HK105, features a modification of the amino acid from L to F at position 86.
+The protein's natural variant, known as in strain: ED3092 and ED3101, features a modification of the amino acid from M to L at position 97.
+The protein's natural variant, known as in strain: JU725, features a modification of the amino acid from E to K at position 98.
+The protein's natural variant, known as in strain: ED3092 and ED3101, features a modification of the amino acid from T to A at position 100.
+The protein's natural variant, known as in strain: ZBMEL157 and ZBMEL377, features a modification of the amino acid from T to S at position 17.
+The protein's natural variant, known as in strain: ZBMEL186 and ZBMEL191, features a modification of the amino acid from E to ELETE at position 22.
+The protein's natural variant, known as in strain: MEL02, ZBMEL84, ZBMEL145, ZBMEL157, ZBMEL186, ZBMEL191, ZBMEL229, ZBMEL377, ZBMEL384 and ZBMEL398, features a modification of the amino acid from Y to D at position 73.
+The protein's natural variant, known as in strain: ZBMEL95, features a modification of the amino acid from T to S at position 163.
+The protein's natural variant, known as in strain: ZBMEL229, features a modification of the amino acid from R to Q at position 169.
+The protein's natural variant, known as in strain: ZBMEL145, ZBMEL191, features a modification of the amino acid from LV to II at position 310.
+The protein's natural variant, known as in strain: ZBMEL84, ZBMEL384 and ZBMEL398, features a modification of the amino acid from L to I at position 309.
+The protein's natural variant, known as in strain: MEL18, features a modification of the amino acid from E to K at position 325.
+The protein's natural variant, known as in strain: ZBMEL384, features a modification of the amino acid from P to S at position 333.
+The protein's natural variant, known as in strain: ZBMEL186, features a modification of the amino acid from H to R at position 335.
+The protein's natural variant, known as in strain: MEL17, features a modification of the amino acid from E to Q at position 364.
+The protein's natural variant, known as in strain: ZBMEL186 and ZBMEL384, features a modification of the amino acid from S to T at position 385.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from V to L at position 424.
+The natural variant of this protein is characterized by an amino acid alteration from V to G at position 17.
+The protein's natural variant, known as in strain: 200:NIH, features a modification of the amino acid from A to D at position 113.
+The protein's natural variant, known as in strain: 200:NIH, features a modification of the amino acid from R to T at position 116.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from G to S at position 141.
+The natural variant of this protein is characterized by an amino acid alteration from E to G at position 155.
+The natural variant of this protein is characterized by an amino acid alteration from S to G at position 158.
+The protein's natural variant, known as in DFNB24;, features a modification of the amino acid from D to N at position 578.
+The protein's natural variant, known as in strain: 212, features a modification of the amino acid from S to A at position 45.
+The protein's natural variant, known as in strain: B31, features a modification of the amino acid from A to T at position 233.
+The protein's natural variant, known as in strain: B31, features a modification of the amino acid from V to I at position 318.
+The protein's natural variant, known as in a gastric cancer sample, features a modification of the amino acid from H to Y at position 123.
+The protein's natural variant, known as in a diffuse gastric cancer sample, features a modification of the amino acid from T to P at position 193.
+The protein's natural variant, known as in DGLBC;, features a modification of the amino acid from D to G at position 244.
+The protein's natural variant, known as in BCDS1; abolishes protein abundance; loss of cell membrane localization;, features a modification of the amino acid from D to Y at position 254.
+The protein's natural variant, known as in BCDS1; slightly decreases protein abundance; loss of cell membrane localization, features a modification of the amino acid from D to V at position 257.
+The protein's natural variant, known as may contribute to prostate cancer;, features a modification of the amino acid from S to A at position 270.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from M to I at position 282.
+The protein's natural variant, known as in lobular breast carcinoma, features a modification of the amino acid from N to S at position 315.
+The protein's natural variant, known as found in gastric and colorectal cancer samples; cells exhibited decreased aggregation increased invasiveness and non-uniform migration in vitro compared to cells transfected with wild-type sequence;, features a modification of the amino acid from T to A at position 340.
+The protein's natural variant, known as in a diffuse gastric cancer sample, features a modification of the amino acid from D to A at position 370.
+The protein's natural variant, known as in a gastric carcinoma sample, features a modification of the amino acid from E to Q at position 463.
+The protein's natural variant, known as in a diffuse gastric cancer sample, features a modification of the amino acid from V to D at position 473.
+The protein's natural variant, known as in DGLBC, features a modification of the amino acid from V to A at position 487.
+The protein's natural variant, known as in a thyroid cancer sample; may play a role in colorectal carcinogenesis;, features a modification of the amino acid from A to T at position 592.
+The protein's natural variant, known as in a gastric cancer sample;, features a modification of the amino acid from R to Q at position 598.
+The protein's natural variant, known as detected in an endometrial cancer sample; loss of heterozygosity; cells exhibited an intermediate phenotype concerning aggregation invasiveness and migration in vitro compared to cells transfected with wild-type sequence;, features a modification of the amino acid from A to T at position 617.
+The protein's natural variant, known as found in a gastric cancer sample; cells exhibited decreased aggregation increased invasiveness and non-uniform migration in vitro compared to cells transfected with wild-type sequence;, features a modification of the amino acid from A to V at position 634.
+The protein's natural variant, known as detected in an endometrial cancer sample;, features a modification of the amino acid from L to V at position 711.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from D to N at position 777.
+The protein's natural variant, known as in DGLBC;, features a modification of the amino acid from V to M at position 832.
+The protein's natural variant, known as in an ovarian carcinoma sample; somatic mutation; loss of heterozygosity;, features a modification of the amino acid from S to G at position 838.
+The protein's natural variant, known as found in a family with Barrett esophagus and esophageal adenocarcinoma; unknown pathological significance;, features a modification of the amino acid from S to G at position 631.
+The protein's natural variant, known as found in esophageal adenocarcinoma; somatic mutation; unknown pathological significance;, features a modification of the amino acid from G to S at position 769.
+The protein's natural variant, known as in NPHS12; doesnt affect nuclear envelope localization; impairs nuclear pore complex assembly; doesn't abrogate interaction with NUP205; doesn't affect SMAD4 interaction; doesn't affect IPO7 interaction; impairs SMAD4 protein import into nucleus; impairs SMAD4 protein signal transduction;, features a modification of the amino acid from R to W at position 388.
+The protein's natural variant, known as in NPHS12; doesnt affect nuclear envelope localization; doesn't affect nuclear pore complex assembly; doesn't abrogate interaction with NUP205; abrogates SMAD4 interaction; abrogates IPO7 interaction; impairs SMAD4 protein import into nucleus; impairs SMAD4 protein signal transduction;, features a modification of the amino acid from G to V at position 591.
+The protein's natural variant, known as in NPHS12; doesnt affect nuclear envelope localization; doesn't affect nuclear pore complex assembly; doesn't abrogate interaction with NUP205; abrogates SMAD4 interaction; abrogates IPO7 interaction; impairs SMAD4 protein import; impairs SMAD4 protein signal transduction into nucleus;;, features a modification of the amino acid from Y to C at position 629.
+The natural variant of this protein is characterized by an amino acid alteration from M to I at position 136.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation, features a modification of the amino acid from G to D at position 453.
+The protein's natural variant, known as found in a patient with X-linked intellectual disability; unknown pathological significance;, features a modification of the amino acid from N to D at position 472.
+The protein's natural variant, known as in MRXS33;, features a modification of the amino acid from P to S at position 575.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation, features a modification of the amino acid from E to K at position 651.
+The protein's natural variant, known as in a lung bronchoalveolar carcinoma sample; somatic mutation, features a modification of the amino acid from M to I at position 691.
+The protein's natural variant, known as in MRXS33;, features a modification of the amino acid from C to R at position 786.
+The protein's natural variant, known as in MRXS33;, features a modification of the amino acid from D to H at position 955.
+The protein's natural variant, known as found in a patient with X-linked intellectual disability; unknown pathological significance;, features a modification of the amino acid from R to C at position 1169.
+The protein's natural variant, known as in MRXS33;, features a modification of the amino acid from R to W at position 1225.
+The protein's natural variant, known as in MRXS33;, features a modification of the amino acid from I to T at position 1316.
+The protein's natural variant, known as in MRXS33; unknown pathological significance, features a modification of the amino acid from R to H at position 1431.
+The protein's natural variant, known as in MRXS33; unknown pathological significance, features a modification of the amino acid from N to H at position 1496.
+The protein's natural variant, known as in VMD2, features a modification of the amino acid from I to T at position 3.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from T to P at position 6.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from T to R at position 6.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from V to A at position 9.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from V to M at position 9.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from A to T at position 10.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from A to V at position 10.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from N to I at position 11.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from R to H at position 13.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from S to F at position 16.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from F to C at position 17.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from L to V at position 21.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from W to C at position 24.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from R to Q at position 25.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from R to W at position 25.
+The protein's natural variant, known as in VMD2, features a modification of the amino acid from G to R at position 26.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from S to R at position 27.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from Y to H at position 29.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from K to R at position 30.
+The protein's natural variant, known as in ARB; unknown pathological significance; no effect on subcellular location in transfected HEK293T cells; loss of chloride conductance, features a modification of the amino acid from L to P at position 40.
+The protein's natural variant, known as in VMD2 and ARB; no effect on subcellular location in transfected MDCK.2 cells; possible decrease in protein stability; reduced chloride conductance;, features a modification of the amino acid from L to P at position 41.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from R to H at position 47.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from Q to L at position 58.
+The natural variant of this protein is characterized by an amino acid alteration from L to V at position 67.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from I to N at position 73.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from F to L at position 80.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from L to V at position 82.
+The protein's natural variant, known as in VMD2; decreased chloride and bicarbonate conductance;, features a modification of the amino acid from Y to H at position 85.
+The protein's natural variant, known as in VRCP;, features a modification of the amino acid from V to M at position 86.
+The protein's natural variant, known as in VMD2, features a modification of the amino acid from V to A at position 89.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from T to I at position 91.
+The protein's natural variant, known as in VMD2; loss of cloride and bicarbonate conductance;, features a modification of the amino acid from R to C at position 92.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from R to H at position 92.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from R to S at position 92.
+The protein's natural variant, known as in VMD2; no effect on subcellular location in transfected HEK293T cells; loss of cloride and bicarbonate conductance;, features a modification of the amino acid from W to C at position 93.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from Q to H at position 96.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from N to K at position 99.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from L to R at position 100.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from P to T at position 101.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from W to R at position 102.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from D to E at position 104.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from D to H at position 104.
+The protein's natural variant, known as in age-related macular degeneration;, features a modification of the amino acid from R to C at position 105.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from F to L at position 113.
+The protein's natural variant, known as in a sporadic case of concentric annular macular dystrophy;, features a modification of the amino acid from E to Q at position 119.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from N to K at position 133.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from G to S at position 135.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from L to R at position 140.
+The protein's natural variant, known as in RP50 and ARB; possible decrease in protein stability; causes protein mislocalization to the cytoplasm and reduction of channel activity;, features a modification of the amino acid from L to V at position 140.
+The protein's natural variant, known as in VMD2 and ARB; no effect on subcellular location in induced pluripotent stem cell-derived retinal pigment epithelial cells; loss of cell membrane localization in transfected MDCK.2 cells; possible decrease in protein stability; reduced chloride conductance;, features a modification of the amino acid from R to H at position 141.
+The protein's natural variant, known as in VMD2; sporadic; requires 2 nucleotide substitutions;, features a modification of the amino acid from A to K at position 146.
+The protein's natural variant, known as in ARB; no effect on protein stability; loss of cell membrane localization in transfected MDCK.2 cells; reduced whole-cell conductance;, features a modification of the amino acid from P to A at position 152.
+The protein's natural variant, known as in ARB and VMD2; no effect on subcellular location in transfected MDCK.2 and HEK293T cells; possible decrease in protein stability; reduced chloride conductance;, features a modification of the amino acid from A to V at position 195.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from I to T at position 201.
+The protein's natural variant, known as in ARB; possible decrease in protein stability; loss of cell membrane localization in transfected MDCK.2 cells; reduced chloride conductance;, features a modification of the amino acid from R to W at position 202.
+The protein's natural variant, known as in RP50; reduced channel activity;, features a modification of the amino acid from I to T at position 205.
+The protein's natural variant, known as in VMD2; benign variant;, features a modification of the amino acid from L to I at position 207.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from S to N at position 209.
+The protein's natural variant, known as in a sporadic case of age-related macular degeneration;, features a modification of the amino acid from T to I at position 216.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from R to C at position 218.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from R to H at position 218.
+The protein's natural variant, known as in VMD2, features a modification of the amino acid from R to Q at position 218.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from R to S at position 218.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from C to W at position 221.
+The protein's natural variant, known as in a family affected by Leber congenital amaurosis/VMD2;, features a modification of the amino acid from G to V at position 222.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from L to M at position 224.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from L to P at position 224.
+The protein's natural variant, known as in RP50;, features a modification of the amino acid from Y to C at position 227.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from Y to N at position 227.
+The protein's natural variant, known as in RP50; causes protein mislocalization to the cytoplasm;, features a modification of the amino acid from D to N at position 228.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from S to R at position 231.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from V to L at position 235.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from V to M at position 235.
+The protein's natural variant, known as in VRCP;, features a modification of the amino acid from Y to C at position 236.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from T to R at position 237.
+The protein's natural variant, known as in VRCP;, features a modification of the amino acid from V to M at position 239.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from T to N at position 241.
+The protein's natural variant, known as in VMD2; late-onset of visual disturbance, features a modification of the amino acid from V to M at position 242.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from A to T at position 243.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from A to V at position 243.
+The protein's natural variant, known as in age-related macular degeneration;, features a modification of the amino acid from V to I at position 275.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from F to L at position 276.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from Q to K at position 293.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from L to V at position 294.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from I to T at position 295.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from N to H at position 296.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from N to S at position 296.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from P to A at position 297.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from P to S at position 297.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from F to S at position 298.
+The protein's natural variant, known as in VMD2, features a modification of the amino acid from G to A at position 299.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from G to E at position 299.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from E to D at position 300.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from E to K at position 300.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from D to E at position 301.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from D to N at position 301.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from D to G at position 302.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from D to H at position 302.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from D to V at position 302.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from D to E at position 303.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from F to S at position 305.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from E to D at position 306.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from E to G at position 306.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from T to A at position 307.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from T to I at position 307.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from N to S at position 308.
+The protein's natural variant, known as in VMD2;, features a modification of the amino acid from I to T at position 310.
+The protein's natural variant, known as in VMD2, features a modification of the amino acid from V to G at position 311.
+The protein's natural variant, known as in VMD2 and ARB; no effect on protein stability; loss of cell membrane localization in transfected MDCK.2 cells; reduced chloride conductance;, features a modification of the amino acid from D to N at position 312.
+The protein's natural variant, known as in ARB; no effect on protein stability; loss of cell membrane localization in transfected MDCK.2 cells; reduced chloride conductance;, features a modification of the amino acid from V to M at position 317.
+The protein's natural variant, known as in ARB; possible decrease in protein stability; loss of cell membrane localization in transfected MDCK.2 cells; reduced chloride conductance;, features a modification of the amino acid from M to T at position 325.
+The protein's natural variant, known as in a sporadic case of age-related macular degeneration; unknown pathological significance;, features a modification of the amino acid from L to F at position 567.
+The protein's natural variant, known as in an ovarian mucinous carcinoma sample; somatic mutation;, features a modification of the amino acid from A to V at position 66.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation, features a modification of the amino acid from E to K at position 379.
+The protein's natural variant, known as in CILD44; unknown pathological significance;, features a modification of the amino acid from P to L at position 748.
+The protein's natural variant, known as in CILD44; unknown pathological significance;, features a modification of the amino acid from R to C at position 773.
+The protein's natural variant, known as in allele b, features a modification of the amino acid from K to S at position 49.
+The protein's natural variant, known as in allele b, features a modification of the amino acid from A to T at position 55.
+The protein's natural variant, known as in allele b, features a modification of the amino acid from G to V at position 70.
+The protein's natural variant, known as in allele b, features a modification of the amino acid from L to T at position 73.
+The protein's natural variant, known as in allele b, features a modification of the amino acid from N to G at position 74.
+The protein's natural variant, known as in allele b, features a modification of the amino acid from P to L at position 75.
+The protein's natural variant, known as in allele b, features a modification of the amino acid from D to N at position 76.
+The protein's natural variant, known as in allele b, features a modification of the amino acid from D to S at position 86.
+The protein's natural variant, known as in allele b, features a modification of the amino acid from M to T at position 88.
+The protein's natural variant, known as in allele b, features a modification of the amino acid from K to Q at position 90.
+The protein's natural variant, known as in allele b, features a modification of the amino acid from G to E at position 92.
+The protein's natural variant, known as in allele b, features a modification of the amino acid from E to V at position 99.
+The protein's natural variant, known as in allele b, features a modification of the amino acid from R to G at position 118.
+The protein's natural variant, known as in allele b, features a modification of the amino acid from A to P at position 119.
+The protein's natural variant, known as in allele b, features a modification of the amino acid from F to I at position 125.
+The protein's natural variant, known as in allele b, features a modification of the amino acid from Q to K at position 127.
+The protein's natural variant, known as in strain: CLIB 219, CLIB 410 and CLIB 413, features a modification of the amino acid from A to V at position 11.
+The protein's natural variant, known as in strain: CLIB 219, CLIB 410 and CLIB 413, features a modification of the amino acid from S to I at position 18.
+The protein's natural variant, known as in strain: CLIB 382, CLIB 556 and CLIB 630, features a modification of the amino acid from L to F at position 67.
+The protein's natural variant, known as in strain: CLIB 382, CLIB 556 and CLIB 630, features a modification of the amino acid from V to L at position 70.
+The protein's natural variant, known as in strain: CLIB 382, CLIB 556 and CLIB 630, features a modification of the amino acid from D to N at position 78.
+The protein's natural variant, known as in strain: CLIB 219, CLIB 382, CLIB 413, CLIB 556 and CLIB 630, features a modification of the amino acid from F to L at position 81.
+The protein's natural variant, known as in strain: CLIB 382, CLIB 556 and CLIB 630, features a modification of the amino acid from R to Q at position 92.
+The protein's natural variant, known as in strain: CLIB 413, features a modification of the amino acid from M to G at position 99.
+The protein's natural variant, known as in strain: CLIB 382, CLIB 413, CLIB 556 and CLIB 630, features a modification of the amino acid from V to L at position 100.
+The protein's natural variant, known as in strain: CLIB 382, CLIB 556 and CLIB 630, features a modification of the amino acid from S to L at position 106.
+The protein's natural variant, known as in strain: CLIB 382 haplotype Ha2, features a modification of the amino acid from K to N at position 119.
+The protein's natural variant, known as in strain: CLIB 382, CLIB 556, CLIB 630, K1 and R13 haplotype Ha2, features a modification of the amino acid from S to P at position 203.
+The natural variant of this protein is characterized by an amino acid alteration from R to C at position 25.
+The natural variant of this protein is characterized by an amino acid alteration from A to V at position 80.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to Q at position 296.
+The protein's natural variant, known as found in a patient with sclerosing cholangitis short stature hypothyroidism and abnormal tongue pigmentation; unknown pathological significance;, features a modification of the amino acid from R to C at position 302.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from Q to K at position 417.
+The natural variant of this protein is characterized by an amino acid alteration from V to A at position 345.
+The protein's natural variant, known as in LWD;, features a modification of the amino acid from L to V at position 132.
+The protein's natural variant, known as in LWD;, features a modification of the amino acid from R to L at position 153.
+The protein's natural variant, known as in LMD;, features a modification of the amino acid from R to W at position 168.
+The protein's natural variant, known as in LWD;, features a modification of the amino acid from R to C at position 173.
+The protein's natural variant, known as in HH21; rare variant associated with susceptibility to disease; the patient has a second mutation in the HH-associated gene FGFR1;, features a modification of the amino acid from Q to K at position 69.
+The protein's natural variant, known as in HH21; rare variant associated with susceptibility to disease; patients have a second mutation in another HH-associated gene including FGFR1, HS6ST1 and FGF17;, features a modification of the amino acid from E to G at position 97.
+The protein's natural variant, known as in HH21; rare variant associated with susceptibility to disease; patients have a second mutation in another HH-associated gene including FGFR1, HS6ST1 and FGF17;, features a modification of the amino acid from S to I at position 144.
+The protein's natural variant, known as in HH21;, features a modification of the amino acid from K to R at position 339.
+The protein's natural variant, known as found in a renal cell carcinoma case; somatic mutation;, features a modification of the amino acid from I to V at position 452.
+The protein's natural variant, known as in MDDGC2;, features a modification of the amino acid from T to M at position 184.
+The protein's natural variant, known as in MDDGA2;, features a modification of the amino acid from I to N at position 198.
+The protein's natural variant, known as in MDDGB2;, features a modification of the amino acid from G to D at position 246.
+The protein's natural variant, known as in MDDGA2;, features a modification of the amino acid from G to S at position 353.
+The protein's natural variant, known as in MDDGA2;, features a modification of the amino acid from V to F at position 373.
+The protein's natural variant, known as in MDDGA2;, features a modification of the amino acid from R to P at position 413.
+The protein's natural variant, known as in MDDGA2, features a modification of the amino acid from IN to LLWQ at position 445.
+The protein's natural variant, known as in MDDGA2;, features a modification of the amino acid from H to R at position 478.
+The protein's natural variant, known as in MDDGA2;, features a modification of the amino acid from G to V at position 482.
+The protein's natural variant, known as in MDDGB2 and MDDGA2;, features a modification of the amino acid from Y to C at position 666.
+The protein's natural variant, known as in MDDGB2, features a modification of the amino acid from F to S at position 717.
+The protein's natural variant, known as in MDDGA2 and MDDGB2;, features a modification of the amino acid from G to E at position 726.
+The protein's natural variant, known as in MDDGB2;, features a modification of the amino acid from W to R at position 748.
+The protein's natural variant, known as in MDDGC2;, features a modification of the amino acid from W to S at position 748.
+The protein's natural variant, known as in IDDRP; unknown pathological significance;, features a modification of the amino acid from S to N at position 1219.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from K to N at position 568.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from D to V at position 939.
+The protein's natural variant, known as in MDDGC4;, features a modification of the amino acid from A to T at position 114.
+The protein's natural variant, known as in a patient diagnosed with Walker-Warburg syndrome;, features a modification of the amino acid from G to S at position 125.
+The protein's natural variant, known as in MDDGA4;, features a modification of the amino acid from A to E at position 170.
+The protein's natural variant, known as in MDDGC4;, features a modification of the amino acid from F to S at position 176.
+The protein's natural variant, known as in CMD1X;, features a modification of the amino acid from R to T at position 179.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from D to E at position 225.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from D to N at position 225.
+The protein's natural variant, known as in MDDGB4, features a modification of the amino acid from R to G at position 246.
+The protein's natural variant, known as in MDDGA4, features a modification of the amino acid from C to G at position 250.
+The protein's natural variant, known as in MDDGB4 and MDDGC4; the mutant protein is expressed and localized correctly within the cell, decrease in ribitol-5-phosphate transferase activity.;, features a modification of the amino acid from R to Q at position 307.
+The protein's natural variant, known as in CMD1X;, features a modification of the amino acid from Q to P at position 358.
+The protein's natural variant, known as in MDDGA4; loss of normal location in Golgi membranes;, features a modification of the amino acid from Y to C at position 371.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from V to M at position 448.
+The protein's natural variant, known as in recessive downless Jackson, features a modification of the amino acid from E to K at position 379.
+The protein's natural variant, known as found in an esophageal cancer sample; esophageal squamous cell carcinoma; somatic mutation;, features a modification of the amino acid from R to K at position 102.
+The protein's natural variant, known as found in an esophageal cancer sample; esophageal squamous cell carcinoma; somatic mutation;, features a modification of the amino acid from A to T at position 242.
+The protein's natural variant, known as found in an esophageal cancer sample; esophageal squamous cell carcinoma; somatic mutation;, features a modification of the amino acid from G to D at position 244.
+The protein's natural variant, known as in MRD3; uncertain pathological significance;, features a modification of the amino acid from V to L at position 8.
+The protein's natural variant, known as in MRD3; affects cell-cell adhesion but not surface expression of the protein;, features a modification of the amino acid from R to C at position 60.
+The protein's natural variant, known as in MRD3; affects cell-cell adhesion but not surface expression of the protein;, features a modification of the amino acid from R to W at position 92.
+The protein's natural variant, known as in MRD3; affects cell-cell adhesion but not surface expression of the protein;, features a modification of the amino acid from A to V at position 122.
+The protein's natural variant, known as in microphthalmia-eyeless-white/mi-ew, features a modification of the amino acid from ACIFPTESEARALAKERQKKDNHNLI to V at position 319.
+The protein's natural variant, known as in microphthalmia-white/mi-wh, features a modification of the amino acid from I to N at position 319.
+The protein's natural variant, known as in microphthalmia-vitiligo/mi-vi, features a modification of the amino acid from D to N at position 329.
+The protein's natural variant, known as in strain: Serogroup H1 isolate VCS1215, features a modification of the amino acid from A to E at position 91.
+The protein's natural variant, known as in strain: Serogroup H1 isolate VCS1215, features a modification of the amino acid from E to G at position 105.
+The protein's natural variant, known as in strain: Serogroup H1 isolate VCS1215, features a modification of the amino acid from K to Q at position 156.
+The protein's natural variant, known as in strain: 1161, features a modification of the amino acid from ET to DP at position 198.
+The protein's natural variant, known as in strain: 1161, features a modification of the amino acid from E to Q at position 333.
+The natural variant of this protein is characterized by an amino acid alteration from P to D at position 234.
+The natural variant of this protein is characterized by an amino acid alteration from H to R at position 21.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 77.
+The protein's natural variant, known as this variant seems to have a modifier effect on LDLR mutation and familial hypercholesterolemia, features a modification of the amino acid from L to LL at position 23.
+The protein's natural variant, known as associated with lower plasma levels of low-density lipoprotein cholesterol; reduced phosphorylation at Ser-47;, features a modification of the amino acid from R to L at position 46.
+The protein's natural variant, known as associated with reduced phosphorylation at Ser-47;, features a modification of the amino acid from A to V at position 53.
+The natural variant of this protein is characterized by an amino acid alteration from G to R at position 106.
+The protein's natural variant, known as in FHCL3;, features a modification of the amino acid from S to R at position 127.
+The protein's natural variant, known as in FHCL3;, features a modification of the amino acid from D to G at position 129.
+The protein's natural variant, known as found in patients with familial hypercholesterolemia carrying a homozygous LDLR mutation; acts as a disease modifier resulting in a mild phenotype;, features a modification of the amino acid from P to S at position 174.
+The protein's natural variant, known as in FHCL3;, features a modification of the amino acid from R to H at position 215.
+The protein's natural variant, known as in FHCL3; partial loss of cleavage by furin and PCSK5;, features a modification of the amino acid from F to L at position 216.
+The protein's natural variant, known as in FHCL3; complete loss of cleavage by furin and PCSK5; reduces glycosylation levels; no effect on protein sulfation and phosphorylation; no effect on protein sulfation but inhibits phosphorylation when associated with Y-374; highly reduces LDL uptake when associated with Y-374;, features a modification of the amino acid from R to S at position 218.
+The natural variant of this protein is characterized by an amino acid alteration from A to D at position 239.
+The protein's natural variant, known as associated with lower plasma levels of low-density lipoprotein cholesterol;, features a modification of the amino acid from L to F at position 253.
+The protein's natural variant, known as in FHCL3;, features a modification of the amino acid from R to H at position 357.
+The protein's natural variant, known as in FHCL3;, features a modification of the amino acid from D to H at position 374.
+The protein's natural variant, known as in FHCL3; partial loss of cleavage by furin and PCSK5; no effect on protein sulfation but inhibits phosphorylation when associated with S-218; highly increases LDL uptake when associated with S-218;, features a modification of the amino acid from D to Y at position 374.
+The protein's natural variant, known as found in a patient associated with autosomal dominant hypercholesterolemia; unknown pathological significance;, features a modification of the amino acid from G to S at position 394.
+The protein's natural variant, known as associated with lower plasma levels of low-density lipoprotein cholesterol; more extensive cleavage by furin and PCSK5;, features a modification of the amino acid from A to T at position 443.
+The natural variant of this protein is characterized by an amino acid alteration from G to D at position 452.
+The protein's natural variant, known as no effect on interaction with ANXA2, features a modification of the amino acid from E to Q at position 482.
+The protein's natural variant, known as in FHCL3;, features a modification of the amino acid from R to W at position 496.
+The protein's natural variant, known as increases interaction with ANXA2;, features a modification of the amino acid from Q to E at position 554.
+The protein's natural variant, known as in NAGSD; unknown pathological significance;, features a modification of the amino acid from M to V at position 167.
+The protein's natural variant, known as in NAGSD; markedly decreases activity;, features a modification of the amino acid from C to R at position 200.
+The protein's natural variant, known as in NAGSD; unknown pathological significance, features a modification of the amino acid from P to L at position 260.
+The protein's natural variant, known as in NAGSD; unknown pathological significance;, features a modification of the amino acid from T to M at position 264.
+The protein's natural variant, known as in NAGSD, features a modification of the amino acid from A to P at position 279.
+The protein's natural variant, known as in NAGSD; unknown pathological significance, features a modification of the amino acid from I to N at position 291.
+The protein's natural variant, known as in NAGSD; unknown pathological significance, features a modification of the amino acid from L to R at position 391.
+The protein's natural variant, known as in NAGSD; unknown pathological significance;, features a modification of the amino acid from S to C at position 398.
+The protein's natural variant, known as in NAGSD; markedly decreases activity, features a modification of the amino acid from S to P at position 410.
+The protein's natural variant, known as in NAGSD; markedly decreases activity;, features a modification of the amino acid from L to P at position 430.
+The protein's natural variant, known as in NAGSD; unknown pathological significance;, features a modification of the amino acid from G to D at position 457.
+The protein's natural variant, known as in NAGSD; markedly decreases activity;, features a modification of the amino acid from W to R at position 484.
+The protein's natural variant, known as in NAGSD; unknown pathological significance;, features a modification of the amino acid from Y to C at position 512.
+The protein's natural variant, known as in NAGSD; markedly decreases activity;, features a modification of the amino acid from A to T at position 518.
+The protein's natural variant, known as in strain: RMSCC 1695 / CA3, features a modification of the amino acid from T to S at position 75.
+The protein's natural variant, known as in strain: RMSCC 1695 / CA3 and RMSCC 2267 /CA1, features a modification of the amino acid from I to V at position 76.
+The protein's natural variant, known as in retinal dystrophy; exhibits a profound loss of catalytic activity;, features a modification of the amino acid from A to T at position 47.
+The protein's natural variant, known as in LCA13; abolishes protection against the toxicity of 4-hydroxynonenal in the retina; results in aberrant activity in interconverting isomers of retinol and retinal; the activity profiles depend on presence or absence of variant Q-161; genetic background may act as a modifier of variant effect;, features a modification of the amino acid from T to M at position 49.
+The protein's natural variant, known as in LCA13;, features a modification of the amino acid from I to N at position 51.
+The protein's natural variant, known as in retinal dystrophy; exhibits a profound loss of catalytic activity;, features a modification of the amino acid from T to M at position 55.
+The protein's natural variant, known as in RP53;, features a modification of the amino acid from G to R at position 76.
+The protein's natural variant, known as found in a patient with LCA13;, features a modification of the amino acid from A to V at position 79.
+The protein's natural variant, known as in LCA13; exhibits a profound loss of catalytic activity;, features a modification of the amino acid from L to I at position 99.
+The protein's natural variant, known as in retinal dystrophy; exhibits a profound loss of catalytic activity, features a modification of the amino acid from N to K at position 125.
+The protein's natural variant, known as in RP53;, features a modification of the amino acid from A to V at position 126.
+The protein's natural variant, known as in retinal dystrophy; exhibits a profound loss of catalytic activity;, features a modification of the amino acid from G to E at position 145.
+The protein's natural variant, known as in RP53; early onset; unknown pathological significance;, features a modification of the amino acid from V to D at position 146.
+The protein's natural variant, known as in LCA13; exhibits a profound loss of catalytic activity;, features a modification of the amino acid from H to D at position 151.
+The protein's natural variant, known as in LCA13;, features a modification of the amino acid from H to N at position 151.
+The protein's natural variant, known as in retinal dystrophy; exhibits a profound loss of catalytic activity;, features a modification of the amino acid from T to I at position 155.
+The protein's natural variant, known as does not affect the protection against the toxicity of 4-hydroxynonenal in the retina;, features a modification of the amino acid from R to Q at position 161.
+The protein's natural variant, known as in LCA13;, features a modification of the amino acid from S to P at position 175.
+The protein's natural variant, known as in retinal dystrophy; unknown pathological significance;, features a modification of the amino acid from R to C at position 193.
+The protein's natural variant, known as in retinal dystrophy; exhibits a profound loss of catalytic activity, features a modification of the amino acid from A to D at position 206.
+The protein's natural variant, known as in retinal dystrophy; unknown pathological significance;, features a modification of the amino acid from A to V at position 206.
+The protein's natural variant, known as in LCA13; diminished activity in interconverting isomers of retinol and retinal;, features a modification of the amino acid from Y to C at position 226.
+The protein's natural variant, known as in LCA13;, features a modification of the amino acid from P to A at position 230.
+The protein's natural variant, known as in retinal dystrophy; unknown pathological significance, features a modification of the amino acid from P to L at position 230.
+The protein's natural variant, known as in retinal dystrophy; unknown pathological significance; exhibits a loss of catalytic activity;, features a modification of the amino acid from R to H at position 234.
+The protein's natural variant, known as in retinal dystrophy; exhibits a profound loss of catalytic activity;, features a modification of the amino acid from R to W at position 239.
+The protein's natural variant, known as in retinal dystrophy; exhibits a profound loss of catalytic activity, features a modification of the amino acid from L to P at position 274.
+The protein's natural variant, known as in retinal dystrophy; exhibits a profound loss of catalytic activity;, features a modification of the amino acid from C to Y at position 285.
+The protein's natural variant, known as in strain: C3H/HeJ, features a modification of the amino acid from T to I at position 87.
+The protein's natural variant, known as in allele GUS-SA, features a modification of the amino acid from I to T at position 233.
+The protein's natural variant, known as in allele GUS-SA, features a modification of the amino acid from E to K at position 428.
+The protein's natural variant, known as in allele GUS-SA, features a modification of the amino acid from F to L at position 616.
+The protein's natural variant, known as in allele W26; reduced retention in the endoplasmic reticulum, features a modification of the amino acid from G to R at position 642.
+The protein's natural variant, known as in RCDP3; severely reduced protein levels, features a modification of the amino acid from R to Q at position 182.
+The protein's natural variant, known as in RCDP3;, features a modification of the amino acid from T to I at position 309.
+The protein's natural variant, known as in RCDP3; loss of enzyme activity;, features a modification of the amino acid from R to H at position 419.
+The protein's natural variant, known as in RCDP3;, features a modification of the amino acid from L to P at position 469.
+The protein's natural variant, known as in RCDP3; severely reduced protein levels, features a modification of the amino acid from E to K at position 471.
+The protein's natural variant, known as in RCDP3; does not affect protein levels;, features a modification of the amino acid from T to M at position 568.
+The protein's natural variant, known as in strain: BALB/c, features a modification of the amino acid from Q to QQ at position 327.
+The protein's natural variant, known as in strain: BALB/c, features a modification of the amino acid from D to N at position 392.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation, features a modification of the amino acid from G to E at position 35.
+The protein's natural variant, known as could be a sequencing error, features a modification of the amino acid from W to L at position 70.
+The protein's natural variant, known as could be a sequencing error, features a modification of the amino acid from V to L at position 113.
+The protein's natural variant, known as in RCD3B;, features a modification of the amino acid from L to Q at position 126.
+The protein's natural variant, known as in RCD3B;, features a modification of the amino acid from W to C at position 188.
+The protein's natural variant, known as in RCD3B; loss of interaction with KCNB1, features a modification of the amino acid from R to P at position 244.
+The protein's natural variant, known as in RCD3B;, features a modification of the amino acid from S to W at position 256.
+The protein's natural variant, known as in RCD3B, features a modification of the amino acid from A to V at position 259.
+The protein's natural variant, known as in RCD3B;, features a modification of the amino acid from G to D at position 459.
+The natural variant of this protein is characterized by an amino acid alteration from I to M at position 377.
+The protein's natural variant, known as in strain: ATCC 7744, features a modification of the amino acid from N to D at position 3.
+The protein's natural variant, known as in strain: ATCC 7744, features a modification of the amino acid from T to S at position 115.
+The protein's natural variant, known as in strain: ATCC 7744, features a modification of the amino acid from E to K at position 211.
+The protein's natural variant, known as in strain: ATCC 7744, features a modification of the amino acid from N to S at position 250.
+The protein's natural variant, known as in strain: cv. Quasifalcata K93, features a modification of the amino acid from T to TKPPVNKPPHK at position 37.
+The protein's natural variant, known as in strain: cv. Quasifalcata K93, features a modification of the amino acid from E to K at position 68.
+The protein's natural variant, known as in strain: TB2, features a modification of the amino acid from K to N at position 5.
+The protein's natural variant, known as in strain: TB1, features a modification of the amino acid from K to Q at position 5.
+The protein's natural variant, known as in strain: OH3, features a modification of the amino acid from I to T at position 58.
+The protein's natural variant, known as in strain: OH2, features a modification of the amino acid from K to R at position 201.
+The protein's natural variant, known as in strain: OH3, features a modification of the amino acid from A to V at position 214.
+The protein's natural variant, known as in strain: TB1, features a modification of the amino acid from S to G at position 286.
+The protein's natural variant, known as in strain: OH3, features a modification of the amino acid from N to D at position 289.
+The protein's natural variant, known as in strain: TB2, features a modification of the amino acid from N to S at position 289.
+The protein's natural variant, known as in strain: TB6, features a modification of the amino acid from T to A at position 306.
+The protein's natural variant, known as in DEE42;, features a modification of the amino acid from E to Q at position 101.
+The protein's natural variant, known as in FHM1;, features a modification of the amino acid from R to Q at position 192.
+The protein's natural variant, known as in FHM1;, features a modification of the amino acid from R to K at position 195.
+The protein's natural variant, known as in FHM1;, features a modification of the amino acid from S to L at position 218.
+The protein's natural variant, known as in EA2;, features a modification of the amino acid from Y to C at position 248.
+The protein's natural variant, known as in EA2;, features a modification of the amino acid from H to Y at position 253.
+The protein's natural variant, known as in EA2;, features a modification of the amino acid from C to R at position 256.
+The protein's natural variant, known as in EA2;, features a modification of the amino acid from C to Y at position 287.
+The protein's natural variant, known as in EA2 and SCA6;, features a modification of the amino acid from G to R at position 293.
+The protein's natural variant, known as in EA2, features a modification of the amino acid from E to K at position 388.
+The protein's natural variant, known as in EA2;, features a modification of the amino acid from L to F at position 389.
+The protein's natural variant, known as in SCA6;, features a modification of the amino acid from A to T at position 405.
+The protein's natural variant, known as in EA2;, features a modification of the amino acid from T to M at position 500.
+The protein's natural variant, known as in FHM1 and SCA6;, features a modification of the amino acid from R to Q at position 582.
+The protein's natural variant, known as in EA2; reduces P/Q current densities;, features a modification of the amino acid from G to D at position 637.
+The protein's natural variant, known as in FHM1 and EA2;, features a modification of the amino acid from T to M at position 665.
+The protein's natural variant, known as in DEE42;, features a modification of the amino acid from A to T at position 712.
+The protein's natural variant, known as in FHM1;, features a modification of the amino acid from V to A at position 713.
+The protein's natural variant, known as in FHM1;, features a modification of the amino acid from D to E at position 714.
+The protein's natural variant, known as in EA2;, features a modification of the amino acid from M to T at position 797.
+The protein's natural variant, known as in EA2;, features a modification of the amino acid from P to R at position 896.
+The protein's natural variant, known as in FHM1;, features a modification of the amino acid from K to E at position 1334.
+The protein's natural variant, known as in SCA6;, features a modification of the amino acid from D to Y at position 1337.
+The protein's natural variant, known as in FHM1; with progressive cerebellar ataxia;, features a modification of the amino acid from R to Q at position 1345.
+The protein's natural variant, known as in FHM1;, features a modification of the amino acid from Y to C at position 1383.
+The protein's natural variant, known as in EA2; loss of function;, features a modification of the amino acid from F to C at position 1402.
+The protein's natural variant, known as in DEE42, features a modification of the amino acid from W to R at position 1435.
+The protein's natural variant, known as in FHM1;, features a modification of the amino acid from V to L at position 1455.
+The protein's natural variant, known as in EA2;, features a modification of the amino acid from G to R at position 1481.
+The protein's natural variant, known as in EA2;, features a modification of the amino acid from F to S at position 1489.
+The protein's natural variant, known as in EA2;, features a modification of the amino acid from V to I at position 1492.
+The protein's natural variant, known as in DEE42;, features a modification of the amino acid from A to S at position 1507.
+The protein's natural variant, known as found in a patient with late onset progressive myoclonus epilepsy; unknown pathological significance;, features a modification of the amino acid from D to N at position 1633.
+The protein's natural variant, known as in EA2;, features a modification of the amino acid from R to H at position 1660.
+The protein's natural variant, known as in SCA6; also found in patients with global developmental delay and congenital ataxia; loss of function observed in the Drosophila homolog;, features a modification of the amino acid from R to Q at position 1663.
+The protein's natural variant, known as in FHM1;, features a modification of the amino acid from R to W at position 1666.
+The protein's natural variant, known as also found in patients with global developmental delay and congenital ataxia; gain of function observed in the Drosophila homolog;, features a modification of the amino acid from R to P at position 1672.
+The protein's natural variant, known as in EA2;, features a modification of the amino acid from R to C at position 1678.
+The protein's natural variant, known as in FHM1;, features a modification of the amino acid from W to R at position 1682.
+The protein's natural variant, known as in FHM1;, features a modification of the amino acid from V to I at position 1694.
+The protein's natural variant, known as in EA2; changed high voltage-gated calcium channel activity;, features a modification of the amino acid from H to L at position 1735.
+The protein's natural variant, known as in EA2;, features a modification of the amino acid from E to K at position 1755.
+The protein's natural variant, known as in FHM1;, features a modification of the amino acid from I to L at position 1809.
+The protein's natural variant, known as in EA2;, features a modification of the amino acid from C to R at position 1868.
+The protein's natural variant, known as in EA2;, features a modification of the amino acid from R to C at position 2134.
+The protein's natural variant, known as in COXPD57; decreased function in cardiolipin synthesis; reduced cardiolipin and increased phosphatidylglycerol levels in fibroblasts from a homozygous patient, features a modification of the amino acid from I to N at position 109.
+The protein's natural variant, known as in COXPD57; unknown pathological significance, features a modification of the amino acid from A to D at position 172.
+The protein's natural variant, known as in COXPD57; unknown pathological significance, features a modification of the amino acid from L to F at position 217.
+The protein's natural variant, known as in SCAR2;, features a modification of the amino acid from S to L at position 96.
+The protein's natural variant, known as in SCAR2;, features a modification of the amino acid from V to M at position 256.
+The protein's natural variant, known as in SCAR2; impairs cleavage of FXN; does not impair cleavage of DLD, NFS1 and PRDX3;, features a modification of the amino acid from A to T at position 377.
+The protein's natural variant, known as in SCAR2;, features a modification of the amino acid from G to R at position 515.
+The protein's natural variant, known as in Nv1-11, features a modification of the amino acid from A to T at position 2.
+The protein's natural variant, known as in Nv1-11, features a modification of the amino acid from R to S at position 22.
+The protein's natural variant, known as in Nv1-16, features a modification of the amino acid from D to N at position 24.
+The protein's natural variant, known as in Nv3-1, features a modification of the amino acid from D to T at position 29.
+The protein's natural variant, known as in Nv1-11, features a modification of the amino acid from L to R at position 31.
+The protein's natural variant, known as in Nv3-1, features a modification of the amino acid from D to E at position 32.
+The protein's natural variant, known as in Nv3-1 and Nv3-3, features a modification of the amino acid from Y to L at position 35.
+The protein's natural variant, known as in Nv3-1 and Nv3-3, features a modification of the amino acid from IP to FA at position 41.
+The protein's natural variant, known as in Nv3-1 and Nv3-3, features a modification of the amino acid from DGPD to PG at position 50.
+The protein's natural variant, known as in Nv3-1, features a modification of the amino acid from M to V at position 62.
+The protein's natural variant, known as in Nv3-1, features a modification of the amino acid from I to V at position 78.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from A to D at position 337.
+The protein's natural variant, known as in UPB1D; strongly reduced activity; reduced formation of higher oligomers;, features a modification of the amino acid from L to S at position 13.
+The protein's natural variant, known as in UPB1D; complete loss of activity;, features a modification of the amino acid from A to E at position 85.
+The protein's natural variant, known as in UPB1D; complete loss of activity;, features a modification of the amino acid from G to R at position 235.
+The protein's natural variant, known as in UPB1D; complete loss of activity;, features a modification of the amino acid from R to W at position 236.
+The protein's natural variant, known as in UPB1D; complete loss of activity, features a modification of the amino acid from S to R at position 264.
+The protein's natural variant, known as in UPB1D; complete loss of activity; abolishes formation of higher oligomers;, features a modification of the amino acid from E to K at position 271.
+The protein's natural variant, known as in UPB1D; unknown pathological significance; mildly reduced enzyme activity; no effect on formation of higher oligomers;, features a modification of the amino acid from I to T at position 286.
+The protein's natural variant, known as in UPB1D; complete loss of activity; abolishes formation of higher oligomers;, features a modification of the amino acid from R to Q at position 326.
+The protein's natural variant, known as in UPB1D; complete loss of activity;, features a modification of the amino acid from T to M at position 359.
+The protein's natural variant, known as in N antigen and M(g) antigen;, features a modification of the amino acid from S to L at position 20.
+The protein's natural variant, known as in M(g) antigen, features a modification of the amino acid from T to N at position 23.
+The protein's natural variant, known as in N antigen, M(c) antigen and M(g) antigen;, features a modification of the amino acid from G to E at position 24.
+The protein's natural variant, known as in Ny(a) antigen, features a modification of the amino acid from D to E at position 46.
+The protein's natural variant, known as in ENEH/Hut antigen, features a modification of the amino acid from T to K at position 47.
+The protein's natural variant, known as in ENEH/Vw antigen, features a modification of the amino acid from T to M at position 47.
+The protein's natural variant, known as in Or antigen, features a modification of the amino acid from R to W at position 50.
+The protein's natural variant, known as in Vr antigen;, features a modification of the amino acid from S to Y at position 66.
+The protein's natural variant, known as in Os(a) antigen, features a modification of the amino acid from P to S at position 73.
+The protein's natural variant, known as in Ri(a) antigen, features a modification of the amino acid from E to K at position 76.
+The protein's natural variant, known as in Mt(a) antigen;, features a modification of the amino acid from T to I at position 77.
+The protein's natural variant, known as in ERIK antigen;, features a modification of the amino acid from G to R at position 78.
+The protein's natural variant, known as in ENAV/MARS antigen, features a modification of the amino acid from Q to K at position 82.
+The protein's natural variant, known as in ENEP/HAG antigen, features a modification of the amino acid from A to P at position 84.
+The natural variant of this protein is characterized by an amino acid alteration from K to T at position 372.
+The protein's natural variant, known as in strain: Isolate Sve2, features a modification of the amino acid from L to V at position 281.
+The protein's natural variant, known as in CPT-resistant cell, features a modification of the amino acid from S to G at position 505.
+The protein's natural variant, known as in FGLDS1;, features a modification of the amino acid from R to H at position 393.
+The protein's natural variant, known as in FGLDS1;, features a modification of the amino acid from R to S at position 393.
+The protein's natural variant, known as in FGLDS1;, features a modification of the amino acid from R to H at position 394.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from P to T at position 869.
+The protein's natural variant, known as in a breast pleomorphic lobular carcinoma sample; somatic mutation, features a modification of the amino acid from S to L at position 925.
+The protein's natural variant, known as in an ovarian endometrioid cancer sample; somatic mutation, features a modification of the amino acid from T to I at position 968.
+The natural variant of this protein is characterized by an amino acid alteration from N to T at position 52.
+The natural variant of this protein is characterized by an amino acid alteration from Q to V at position 265.
+The protein's natural variant, known as in FANCR; causes dominant negative loss of function in interstrand cross-link repair; shows high basal DNA-independent ATPase activity; results in decreased DNA binding, features a modification of the amino acid from T to P at position 131.
+The protein's natural variant, known as in BC; decreased ATPase activity in the presence of stoichiometric ss-DNA concentrations with respect to RAD51; 3 to 4-fold decrease of affinity for ATP;, features a modification of the amino acid from R to Q at position 150.
+The protein's natural variant, known as in FANCR; dominant negative; impaired function in DNA repair via homologous recombination; impaired DNA-binding and formation of nucleoprotein filaments; impaired DNA-dependent ATPase activity; no effect on subcellular location;, features a modification of the amino acid from A to T at position 293.
+The protein's natural variant, known as in strain: cv. Ta-0, features a modification of the amino acid from S to N at position 128.
+The protein's natural variant, known as in strain: cv. Ba-1, features a modification of the amino acid from T to K at position 261.
+The protein's natural variant, known as in strain: cv. Ba-1, features a modification of the amino acid from K to Q at position 264.
+The protein's natural variant, known as in strain: cv. Ag-0, cv. Ba-1, cv. Mh-0, cv. Mr-0 and Tac-0, features a modification of the amino acid from G to A at position 427.
+The protein's natural variant, known as in strain: cv. Su-0, features a modification of the amino acid from N to G at position 459.
+The protein's natural variant, known as in strain: cv. No-0, cv. Rsch-0 and cv. Ta-0, features a modification of the amino acid from V to I at position 489.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from G to E at position 43.
+The protein's natural variant, known as in OOMD8; loss-of-function variant resulting in impaired maternal mRNA decay in fertilized oocytes from the affected individual; abolishes the interaction with CNOT7;, features a modification of the amino acid from A to T at position 56.
+The protein's natural variant, known as in strain: IL1403, features a modification of the amino acid from A to E at position 38.
+The protein's natural variant, known as in strain: IL1403, features a modification of the amino acid from N to S at position 43.
+The protein's natural variant, known as in strain: IL1403, features a modification of the amino acid from R to P at position 69.
+The protein's natural variant, known as in strain: IL1403, features a modification of the amino acid from A to T at position 74.
+The protein's natural variant, known as in strain: IL1403, features a modification of the amino acid from A to T at position 164.
+The protein's natural variant, known as in strain: IL1403, features a modification of the amino acid from K to E at position 245.
+The protein's natural variant, known as in strain: IL1403, features a modification of the amino acid from K to N at position 248.
+The protein's natural variant, known as in strain: IL1403, features a modification of the amino acid from R to S at position 295.
+The protein's natural variant, known as in strain: IL1403, features a modification of the amino acid from SIR to YIS at position 303.
+The protein's natural variant, known as in strain: IL1403, features a modification of the amino acid from D to E at position 316.
+The protein's natural variant, known as in strain: IL1403, features a modification of the amino acid from D to A at position 403.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from A to G at position 669.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from T to I at position 1875.
+The protein's natural variant, known as in IDDNPF; no effect on protein abundance; no effect on glucose transport activity;, features a modification of the amino acid from I to T at position 90.
+The protein's natural variant, known as in IDDNPF; no effect on protein abundance; decreased glucose transport activity;, features a modification of the amino acid from R to W at position 210.
+The protein's natural variant, known as in IDDNPF; no effect on protein abundance; decreased glucose transport activity;, features a modification of the amino acid from A to V at position 244.
+The protein's natural variant, known as in strain: Holstein, features a modification of the amino acid from E to Q at position 60.
+The protein's natural variant, known as in strain: Jersey, features a modification of the amino acid from L to P at position 67.
+The protein's natural variant, known as in strain: Hereford, features a modification of the amino acid from S to T at position 96.
+The protein's natural variant, known as in strain: Jersey, features a modification of the amino acid from R to T at position 216.
+The protein's natural variant, known as in HLD19; loss of mechanosensitive ion channel activity;, features a modification of the amino acid from G to E at position 168.
+The protein's natural variant, known as in HLD19; loss of mechanosensitive ion channel activity;, features a modification of the amino acid from I to N at position 462.
+The protein's natural variant, known as in HLD19; loss of mechanosensitive ion channel activity;, features a modification of the amino acid from G to S at position 567.
+The protein's natural variant, known as in strain: BALB/c, features a modification of the amino acid from M to R at position 32.
+The natural variant of this protein is characterized by an amino acid alteration from C to R at position 197.
+The natural variant of this protein is characterized by an amino acid alteration from F to S at position 457.
+The natural variant of this protein is characterized by an amino acid alteration from F to L at position 711.
+The natural variant of this protein is characterized by an amino acid alteration from T to I at position 794.
+The protein's natural variant, known as in strain: KN-28, features a modification of the amino acid from A to S at position 11.
+The protein's natural variant, known as in strain: KN-22 and KN-23, features a modification of the amino acid from A to V at position 16.
+The protein's natural variant, known as in strain: KN-3, KN-9, KN-10 and L16, features a modification of the amino acid from S to R at position 71.
+The protein's natural variant, known as in strain: TN256, 1420#1 and KO140, features a modification of the amino acid from D to G at position 121.
+The protein's natural variant, known as in strain: KN-3, KN-9, KN-10 and L16, features a modification of the amino acid from D to N at position 121.
+The protein's natural variant, known as in strain: JP-75, KN-7, KN-15, KN-17, KN-21 and KN-23, features a modification of the amino acid from S to T at position 138.
+The protein's natural variant, known as in strain: Canton-S, features a modification of the amino acid from Y to H at position 144.
+The protein's natural variant, known as in strain: 1420#1, KN-3, KN-9, KN-10, KO140, L16 and TN256, features a modification of the amino acid from S to R at position 156.
+The protein's natural variant, known as in strain: Canton-S, features a modification of the amino acid from Y to N at position 181.
+The protein's natural variant, known as in strain: JP-70, KN-17 and KN-21, features a modification of the amino acid from A to S at position 231.
+The protein's natural variant, known as in strain: 1420#1, KO140, KN-3, KN-9, KN-10 and L16, features a modification of the amino acid from D to N at position 278.
+The protein's natural variant, known as in strain: KN-21, features a modification of the amino acid from T to I at position 284.
+The protein's natural variant, known as in strain: 1420#1, J87, JP-60, JP-70, JP-75, KO123, KO140, KN-9, KN-15, KN-21, L16 and TN256, features a modification of the amino acid from T to A at position 398.
+The protein's natural variant, known as in strain: Berkeley, features a modification of the amino acid from S to L at position 401.
+The protein's natural variant, known as in strain: J87, JP-60 and KO123, features a modification of the amino acid from E to A at position 403.
+The protein's natural variant, known as in strain: 1420#1, features a modification of the amino acid from V to I at position 465.
+The protein's natural variant, known as in strain: KN-23, features a modification of the amino acid from S to Y at position 474.
+The protein's natural variant, known as in strain: Berkeley, JP-1, JP-5, JP-15, JP-35, JP-55, JP-65, JP-84, KN-12, KN-22 and KN-27, features a modification of the amino acid from N to Y at position 476.
+The protein's natural variant, known as in PCC; does not repress MYC transcriptional activity;, features a modification of the amino acid from V to L at position 9.
+The protein's natural variant, known as in PCC; unknown pathological significance; does not affect MYC transcriptional activity, features a modification of the amino acid from D to N at position 23.
+The protein's natural variant, known as in PCC; does not repress MYC transcriptional activity, features a modification of the amino acid from R to W at position 25.
+The protein's natural variant, known as in PCC; does not repress MYC transcriptional activity, features a modification of the amino acid from R to C at position 35.
+The protein's natural variant, known as in PCC; does not repress MYC transcriptional activity;, features a modification of the amino acid from R to W at position 60.
+The protein's natural variant, known as in PCC; does not repress MYC transcriptional activity, features a modification of the amino acid from I to S at position 71.
+The protein's natural variant, known as in PCC; does not repress MYC transcriptional activity, features a modification of the amino acid from M to V at position 74.
+The protein's natural variant, known as in PCC; does not repress MYC transcriptional activity, features a modification of the amino acid from R to P at position 90.
+The protein's natural variant, known as in PCC; does not repress MYC transcriptional activity, features a modification of the amino acid from L to P at position 94.
+The protein's natural variant, known as in PCC; does not repress MYC transcriptional activity, features a modification of the amino acid from L to P at position 102.
+The protein's natural variant, known as does not affect MYC transcriptional activity;, features a modification of the amino acid from N to T at position 114.
+The protein's natural variant, known as does not affect MYC transcriptional activity;, features a modification of the amino acid from S to L at position 142.
+The protein's natural variant, known as in strain: N-2; inactive, features a modification of the amino acid from P to L at position 285.
+The protein's natural variant, known as in MODY6, features a modification of the amino acid from R to P at position 103.
+The protein's natural variant, known as in MODY6; unknown pathological significance;, features a modification of the amino acid from E to K at position 110.
+The protein's natural variant, known as in T2D;, features a modification of the amino acid from R to L at position 111.
+The protein's natural variant, known as found in one consanguineous family with non-syndromic autosomal recessive retinitis pigmentosa; unknown pathological significance;, features a modification of the amino acid from V to I at position 242.
+The protein's natural variant, known as in clone PCT21, features a modification of the amino acid from N to K at position 40.
+The protein's natural variant, known as in clone PCT21, features a modification of the amino acid from G to E at position 57.
+The protein's natural variant, known as in clone PCT21, features a modification of the amino acid from K to R at position 72.
+The protein's natural variant, known as in clone PCT21, features a modification of the amino acid from R to G at position 86.
+The protein's natural variant, known as probable disease-associated variant found in autosomal dominant self-limited delayed puberty; the mutant protein is not secreted;, features a modification of the amino acid from R to L at position 156.
+The protein's natural variant, known as probable disease-associated variant found in autosomal dominant self-limited delayed puberty; the mutant protein is not secreted;, features a modification of the amino acid from E to K at position 161.
+The protein's natural variant, known as found in autosomal dominant self-limited delayed puberty; unknown pathological significance;, features a modification of the amino acid from E to G at position 2264.
+The protein's natural variant, known as found in autosomal dominant self-limited delayed puberty; unknown pathological significance;, features a modification of the amino acid from D to N at position 2614.
+The protein's natural variant, known as in strain: PB921, features a modification of the amino acid from L to P at position 150.
+The protein's natural variant, known as in SPG76;, features a modification of the amino acid from R to P at position 295.
+The protein's natural variant, known as in strain: WPP3, features a modification of the amino acid from VNA to LPF at position 17.
+The protein's natural variant, known as in strain: WPP3, features a modification of the amino acid from LV to WH at position 24.
+The protein's natural variant, known as in strain: WPP3, features a modification of the amino acid from P to R at position 32.
+The protein's natural variant, known as in strain: WPP7, features a modification of the amino acid from I to M at position 49.
+The protein's natural variant, known as in strain: WPP25, features a modification of the amino acid from PL to LC at position 107.
+The protein's natural variant, known as in strain: WPP25, features a modification of the amino acid from V to D at position 111.
+The protein's natural variant, known as in strain: WPP3 and WPP8, features a modification of the amino acid from S to N at position 117.
+The protein's natural variant, known as in strain: WPP3, features a modification of the amino acid from TE to AQ at position 134.
+The protein's natural variant, known as in strain: WPP19, features a modification of the amino acid from EAKA to KPKQ at position 140.
+The protein's natural variant, known as in strain: WPP3, features a modification of the amino acid from E to K at position 137.
+The protein's natural variant, known as in strain: WPP25, features a modification of the amino acid from G to R at position 141.
+The protein's natural variant, known as in strain: WPP9 and WPP10, features a modification of the amino acid from G to A at position 142.
+The protein's natural variant, known as in strain: WPP25, features a modification of the amino acid from GQVPG to ARLPA at position 154.
+The protein's natural variant, known as in strain: WPP20, WPP22 and WPP7, features a modification of the amino acid from VPG to AAR at position 154.
+The protein's natural variant, known as in strain: WPP5, features a modification of the amino acid from VPG to AGR at position 154.
+The protein's natural variant, known as in strain: WPP12 and WPP21, features a modification of the amino acid from VP to AA at position 153.
+The protein's natural variant, known as in strain: WPP24, features a modification of the amino acid from V to A at position 152.
+The protein's natural variant, known as in strain: WPP4, features a modification of the amino acid from P to A at position 153.
+The protein's natural variant, known as in PNLIPD; loss of function in lipid catabolic process; the mutant is not secreted;, features a modification of the amino acid from T to M at position 221.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation, features a modification of the amino acid from R to C at position 162.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation, features a modification of the amino acid from R to H at position 162.
+The protein's natural variant, known as in CEP; no residual activity;, features a modification of the amino acid from V to F at position 3.
+The protein's natural variant, known as in CEP;, features a modification of the amino acid from L to F at position 4.
+The protein's natural variant, known as in CEP, features a modification of the amino acid from Y to C at position 19.
+The protein's natural variant, known as in CEP; severe cutaneous lesions; less than 3% wild-type activity;, features a modification of the amino acid from S to P at position 47.
+The protein's natural variant, known as in CEP; severe phenotype; no detectable activity;, features a modification of the amino acid from P to L at position 53.
+The protein's natural variant, known as in CEP; the effect on catalytic activity is controversial;, features a modification of the amino acid from T to A at position 62.
+The protein's natural variant, known as in CEP; mild phenotype; strong decrease in enzymatic activity, when tested in vitro; may affect thermal stability;, features a modification of the amino acid from A to V at position 66.
+The protein's natural variant, known as in CEP; less than 2% wild-type activity, features a modification of the amino acid from A to T at position 69.
+The protein's natural variant, known as in CEP; frequent mutation in Western countries; severe phenotype; loss of enzymatic activity, when tested in vitro;, features a modification of the amino acid from C to R at position 73.
+The protein's natural variant, known as in CEP; mild phenotype; high residual activity;, features a modification of the amino acid from V to F at position 82.
+The protein's natural variant, known as in CEP, features a modification of the amino acid from V to A at position 99.
+The protein's natural variant, known as in CEP; residual activity;, features a modification of the amino acid from A to V at position 104.
+The protein's natural variant, known as in CEP; no residual activity, features a modification of the amino acid from I to T at position 129.
+The protein's natural variant, known as in CEP; less than 5% wild-type activity;, features a modification of the amino acid from G to R at position 188.
+The protein's natural variant, known as in CEP; mild phenotype; less than 2% wild-type activity;, features a modification of the amino acid from G to W at position 188.
+The protein's natural variant, known as in CEP, features a modification of the amino acid from EL to HIQSQAQSQAQDN at position 211.
+The protein's natural variant, known as in CEP; no residual activity;, features a modification of the amino acid from S to P at position 212.
+The protein's natural variant, known as in CEP; moderately-severe phenotype; less than 2% wild-type activity;, features a modification of the amino acid from I to S at position 219.
+The protein's natural variant, known as in CEP;, features a modification of the amino acid from G to S at position 225.
+The protein's natural variant, known as in CEP; loss of enzymatic activity, when tested in vitro;, features a modification of the amino acid from T to M at position 228.
+The protein's natural variant, known as in CEP;, features a modification of the amino acid from L to P at position 237.
+The protein's natural variant, known as in CEP;, features a modification of the amino acid from P to Q at position 248.
+The protein's natural variant, known as in IGKCD, features a modification of the amino acid from W to R at position 41.
+The natural variant of this protein is characterized by an amino acid alteration from V to L at position 84.
+The protein's natural variant, known as in GLC3A;, features a modification of the amino acid from S to W at position 28.
+The protein's natural variant, known as in allele CYP1B1*2, allele CYP1B1*5, allele CYP1B1*6 and allele CYP1B1*7;, features a modification of the amino acid from R to G at position 48.
+The protein's natural variant, known as in GLC3A; juvenile onset; allele CYP1B1*11;, features a modification of the amino acid from W to C at position 57.
+The protein's natural variant, known as in GLC3A; allele CYP1B1*12; reduces enzymatic activity;, features a modification of the amino acid from G to E at position 61.
+The protein's natural variant, known as in GLC3A, features a modification of the amino acid from L to P at position 77.
+The protein's natural variant, known as in GLC3A; adult-onset; hypomorphic allele; reduces the abundance of the enzyme;, features a modification of the amino acid from Y to N at position 81.
+The protein's natural variant, known as in GLC3A;, features a modification of the amino acid from A to P at position 115.
+The protein's natural variant, known as in allele CYP1B1*2, allele CYP1B1*6 and allele CYP1B1*7; significantly associated with breast or lung cancer; no significant change in 17beta-estradiol 2- and 4-hydroxylation activities and 17beta-estradiol affinity; 1.5-fold reduction in testosterone affinity but nearly no change in testosterone 6beta-hydroxylation activity; 2-fold increase in progesterone 6beta- and 16alpha-hydroxylation activities and 5-fold reduction in progesterone affinity;, features a modification of the amino acid from A to S at position 119.
+The protein's natural variant, known as in GLC3A, features a modification of the amino acid from M to R at position 132.
+The natural variant of this protein is characterized by an amino acid alteration from Q to H at position 144.
+The protein's natural variant, known as in GLC3A, features a modification of the amino acid from Q to P at position 144.
+The protein's natural variant, known as in GLC3A;, features a modification of the amino acid from Q to R at position 144.
+The protein's natural variant, known as in GLC3A, features a modification of the amino acid from R to W at position 145.
+The natural variant of this protein is characterized by an amino acid alteration from G to S at position 184.
+The protein's natural variant, known as associated with ocular hypertension susceptibility;, features a modification of the amino acid from A to P at position 189.
+The protein's natural variant, known as in GLC3A, features a modification of the amino acid from D to V at position 192.
+The protein's natural variant, known as in GLC3A;, features a modification of the amino acid from P to L at position 193.
+The protein's natural variant, known as in GLC3A;, features a modification of the amino acid from V to I at position 198.
+The protein's natural variant, known as in GLC3A; reduces enzymatic activity;, features a modification of the amino acid from N to S at position 203.
+The protein's natural variant, known as in GLC3A;, features a modification of the amino acid from S to I at position 215.
+The protein's natural variant, known as in GLC3A; juvenile-onset; hypomorphic allele; reduces the abundance of the enzyme;, features a modification of the amino acid from E to K at position 229.
+The protein's natural variant, known as in GLC3A; adult-onset;, features a modification of the amino acid from G to R at position 232.
+The protein's natural variant, known as in GLC3A, features a modification of the amino acid from S to R at position 239.
+The protein's natural variant, known as in GLC3A; unknown pathological significance;, features a modification of the amino acid from V to L at position 320.
+The protein's natural variant, known as in GLC3A; requires 2 nucleotide substitutions; unknown pathological significance, features a modification of the amino acid from A to F at position 330.
+The protein's natural variant, known as associated with ocular hypertension susceptibility;, features a modification of the amino acid from A to S at position 330.
+The protein's natural variant, known as in GLC3A;, features a modification of the amino acid from L to F at position 345.
+The protein's natural variant, known as in GLC3A;, features a modification of the amino acid from V to M at position 364.
+The protein's natural variant, known as in GLC3A; allele CYP1B1*18;, features a modification of the amino acid from G to W at position 365.
+The protein's natural variant, known as in GLC3A and GLC1A; acts as GLC1A disease modifier in patients also carrying Val-399 mutation in MYOC;, features a modification of the amino acid from R to H at position 368.
+The protein's natural variant, known as in GLC3A;, features a modification of the amino acid from D to N at position 374.
+The protein's natural variant, known as in allele CYP1B1*19;, features a modification of the amino acid from P to L at position 379.
+The protein's natural variant, known as in GLC3A; allele CYP1B1*20;, features a modification of the amino acid from E to K at position 387.
+The protein's natural variant, known as in GLC3A, features a modification of the amino acid from A to T at position 388.
+The protein's natural variant, known as in GLC3A;, features a modification of the amino acid from R to C at position 390.
+The protein's natural variant, known as in GLC3A; allele CYP1B1*21;, features a modification of the amino acid from R to H at position 390.
+The protein's natural variant, known as in GLC3A;, features a modification of the amino acid from R to S at position 390.
+The protein's natural variant, known as in GLC3A;, features a modification of the amino acid from I to S at position 399.
+The protein's natural variant, known as in GLC3A;, features a modification of the amino acid from V to F at position 409.
+The natural variant of this protein is characterized by an amino acid alteration from V to G at position 422.
+The protein's natural variant, known as in GLC3A; juvenile-onset;, features a modification of the amino acid from N to Y at position 423.
+The protein's natural variant, known as in allele CYP1B1*3, allele CYP1B1*5, allele CYP1B1*6 and allele CYP1B1*7; 1.6-fold increase in 17beta-estradiol 4-hydroxylation activity but no change in 17beta-estradiol 2-hydroxylation activity; 2-fold reduction in testosterone 6beta-hydroxylation activity and 3-fold reduction in testosterone affinity; 6-fold and 4-fold increase in progesterone 6beta- and 16alpha-hydroxylation activity, respectively and 7-fold reduction in progesterone affinity;, features a modification of the amino acid from L to V at position 432.
+The protein's natural variant, known as in GLC3A; allele CYP1B1*23;, features a modification of the amino acid from P to L at position 437.
+The protein's natural variant, known as in GLC3A; allele CYP1B1*7; unknown pathological significance;, features a modification of the amino acid from A to G at position 443.
+The protein's natural variant, known as in GLC3A;, features a modification of the amino acid from R to Q at position 444.
+The protein's natural variant, known as in GLC3A, features a modification of the amino acid from F to C at position 445.
+The protein's natural variant, known as in allele CYP1B1*4;, features a modification of the amino acid from N to S at position 453.
+The protein's natural variant, known as in GLC3A;, features a modification of the amino acid from G to D at position 466.
+The protein's natural variant, known as in GLC3A; allele CYP1B1*25;, features a modification of the amino acid from R to W at position 469.
+The protein's natural variant, known as in GLC3A;, features a modification of the amino acid from E to G at position 499.
+The protein's natural variant, known as in GLC3A; unknown pathological significance, features a modification of the amino acid from S to L at position 515.
+The natural variant of this protein is characterized by an amino acid alteration from V to A at position 518.
+The protein's natural variant, known as in GLC3A; juvenile-onset, features a modification of the amino acid from R to T at position 523.
+The protein's natural variant, known as in GLC3A, features a modification of the amino acid from D to G at position 530.
+The protein's natural variant, known as in strain: NVIII-2, NVIII-5 and NVIII-m15, features a modification of the amino acid from T to I at position 114.
+The protein's natural variant, known as in strain: NVIII-m11 and NVIII-m19, features a modification of the amino acid from A to T at position 133.
+The protein's natural variant, known as in strain: NVIII-m19, features a modification of the amino acid from D to N at position 134.
+The protein's natural variant, known as in strain: NVIII-m19, features a modification of the amino acid from D to V at position 141.
+The protein's natural variant, known as in strain: NVIII-m12, features a modification of the amino acid from P to T at position 174.
+The protein's natural variant, known as in strain: HL250; loss of activity, features a modification of the amino acid from G to D at position 108.
+The natural variant of this protein is characterized by an amino acid alteration from Q to T at position 58.
+The protein's natural variant, known as in strain: Serotype O16, features a modification of the amino acid from K to R at position 22.
+The protein's natural variant, known as in strain: Serotype O16, features a modification of the amino acid from L to I at position 110.
+The protein's natural variant, known as in strain: Serotype O16, features a modification of the amino acid from G to S at position 134.
+The natural variant of this protein is characterized by an amino acid alteration from I to L at position 236.
+The protein's natural variant, known as requires 2 nucleotide substitutions, features a modification of the amino acid from H to C at position 14.
+The natural variant of this protein is characterized by an amino acid alteration from D to Y at position 257.
+The natural variant of this protein is characterized by an amino acid alteration from A to E at position 377.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from P to S at position 89.
+The natural variant of this protein is characterized by an amino acid alteration from S to T at position 4.
+The protein's natural variant, known as in strain: 22000, A128 and Nine, features a modification of the amino acid from T to S at position 33.
+The protein's natural variant, known as in strain: 22000, A128 and Nine, features a modification of the amino acid from S to T at position 40.
+The protein's natural variant, known as in strain: 22000, A128 and Nine, features a modification of the amino acid from T to A at position 54.
+The protein's natural variant, known as in strain: 22000, A128 and Nine, features a modification of the amino acid from K to E at position 69.
+The protein's natural variant, known as in strain: 22000, A128 and Nine, features a modification of the amino acid from E to A at position 439.
+The protein's natural variant, known as in strain: CC-1373, features a modification of the amino acid from I to T at position 317.
+The protein's natural variant, known as in strain: ATCC 6633 / PCI 219, features a modification of the amino acid from A to V at position 30.
+The protein's natural variant, known as in strain: ATCC 6633 / PCI 219, features a modification of the amino acid from A to V at position 43.
+The protein's natural variant, known as in strain: ATCC 6633 / PCI 219, features a modification of the amino acid from F to Y at position 50.
+The protein's natural variant, known as in strain: ATCC 6633 / PCI 219, features a modification of the amino acid from L to I at position 89.
+The protein's natural variant, known as in strain: ATCC 6633 / PCI 219, features a modification of the amino acid from I to V at position 108.
+The protein's natural variant, known as in strain: ATCC 6633 / PCI 219, features a modification of the amino acid from I to T at position 189.
+The protein's natural variant, known as in strain: ATCC 6633 / PCI 219, features a modification of the amino acid from V to I at position 196.
+The protein's natural variant, known as in strain: ATCC 6633 / PCI 219, features a modification of the amino acid from L to I at position 201.
+The protein's natural variant, known as in strain: ATCC 6633 / PCI 219, features a modification of the amino acid from L to I at position 205.
+The protein's natural variant, known as in strain: CA4098, features a modification of the amino acid from T to M at position 3.
+The protein's natural variant, known as in strain: CA4098, features a modification of the amino acid from D to E at position 224.
+The protein's natural variant, known as in strain: CA4098, features a modification of the amino acid from I to K at position 232.
+The protein's natural variant, known as in strain: CA4098, features a modification of the amino acid from T to S at position 254.
+The protein's natural variant, known as in strain: CA4098, features a modification of the amino acid from A to T at position 349.
+The protein's natural variant, known as in strain: CA4098, features a modification of the amino acid from S to N at position 470.
+The protein's natural variant, known as in strain: CA4098, features a modification of the amino acid from F to Y at position 524.
+The protein's natural variant, known as in strain: CA4098, features a modification of the amino acid from Q to P at position 569.
+The protein's natural variant, known as in strain: CA4098, features a modification of the amino acid from I to A at position 586.
+The protein's natural variant, known as in strain: CA4098, features a modification of the amino acid from N to S at position 657.
+The protein's natural variant, known as in strain: CA4098, features a modification of the amino acid from T to K at position 740.
+The protein's natural variant, known as in strain: CA4098, features a modification of the amino acid from NKA to YKS at position 791.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from P to Q at position 19.
+The protein's natural variant, known as in chymosin A, features a modification of the amino acid from G to D at position 302.
+The protein's natural variant, known as in MDDGC9; no effect on dystroglycan expression; impairs alpha-dystroglycan glycosylation;, features a modification of the amino acid from V to I at position 74.
+The protein's natural variant, known as in MDDGC9; does not affect dystroglycan expression; impairs alpha-dystroglycan glycosylation;, features a modification of the amino acid from D to N at position 111.
+The protein's natural variant, known as in MDDGC9; results in impaired interaction with LARGE1 and incomplete DAG1 glycosylation;, features a modification of the amino acid from T to M at position 192.
+The protein's natural variant, known as in MDDGA9;, features a modification of the amino acid from C to F at position 669.
+The protein's natural variant, known as in allele FLD2J; causes the fatty liver dystrophy phenotype (fld), characterized by neonatal fatty liver and hypertriglyceridemia that resolve at weaning and neuropathy affecting peripheral nerve in adulthood, features a modification of the amino acid from G to R at position 84.
+The protein's natural variant, known as in RP3;, features a modification of the amino acid from G to E at position 43.
+The protein's natural variant, known as in RP3;, features a modification of the amino acid from G to R at position 43.
+The protein's natural variant, known as in RP3;, features a modification of the amino acid from G to V at position 60.
+The protein's natural variant, known as in RP3; benign variant;, features a modification of the amino acid from I to V at position 75.
+The protein's natural variant, known as in RP3; reduces interaction with PDE6D;, features a modification of the amino acid from H to Q at position 98.
+The protein's natural variant, known as in RP3;, features a modification of the amino acid from T to N at position 99.
+The protein's natural variant, known as in RP3;, features a modification of the amino acid from R to G at position 127.
+The protein's natural variant, known as in RP3; reduces interaction with PDE6D;, features a modification of the amino acid from F to C at position 130.
+The protein's natural variant, known as in RP3, features a modification of the amino acid from S to L at position 152.
+The protein's natural variant, known as in RP3 and RPSRDF;, features a modification of the amino acid from G to R at position 173.
+The protein's natural variant, known as in RP3; reduces interaction with PDE6D;, features a modification of the amino acid from G to V at position 215.
+The protein's natural variant, known as in RP3; reduces interaction with PDE6D;, features a modification of the amino acid from P to S at position 235.
+The protein's natural variant, known as in RP3; reduces interaction with PDE6D;, features a modification of the amino acid from C to R at position 250.
+The protein's natural variant, known as in RP3;, features a modification of the amino acid from C to Y at position 250.
+The protein's natural variant, known as in RP3; unknown pathological significance;, features a modification of the amino acid from A to G at position 262.
+The protein's natural variant, known as in RP3, features a modification of the amino acid from G to E at position 267.
+The protein's natural variant, known as in RP3, features a modification of the amino acid from G to R at position 267.
+The protein's natural variant, known as in RP3; reduces interaction with PDE6D;, features a modification of the amino acid from G to S at position 275.
+The protein's natural variant, known as in RP3, features a modification of the amino acid from E to G at position 285.
+The protein's natural variant, known as in RP3;, features a modification of the amino acid from I to V at position 289.
+The protein's natural variant, known as in RP3;, features a modification of the amino acid from C to R at position 302.
+The protein's natural variant, known as in RP3;, features a modification of the amino acid from C to Y at position 302.
+The protein's natural variant, known as in RP3, features a modification of the amino acid from D to N at position 312.
+The protein's natural variant, known as in RP3, features a modification of the amino acid from D to Y at position 312.
+The protein's natural variant, known as in RP3; impairs protein folding;, features a modification of the amino acid from G to R at position 320.
+The protein's natural variant, known as in RP3;, features a modification of the amino acid from G to D at position 436.
+The protein's natural variant, known as in XLID30;, features a modification of the amino acid from R to C at position 67.
+The protein's natural variant, known as in XLID30;, features a modification of the amino acid from A to E at position 380.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation, features a modification of the amino acid from T to S at position 440.
+The protein's natural variant, known as in an ovarian mucinous carcinoma; somatic mutation;, features a modification of the amino acid from M to I at position 432.
+The protein's natural variant, known as in AD; associated with susceptibility to late-onset disease; increased susceptibility to neuronal cell death;, features a modification of the amino acid from T to M at position 835.
+The protein's natural variant, known as in alleles AADAC*2 and AADAC*3; mildly decreased enzyme activity;, features a modification of the amino acid from V to I at position 281.
+The protein's natural variant, known as in allele AADAC*3; decreased enzyme activity, features a modification of the amino acid from L to LQ at position 399.
+The protein's natural variant, known as in strain: NCIB 8346, features a modification of the amino acid from VN to TD at position 30.
+The protein's natural variant, known as in strain: NCIB 8346, features a modification of the amino acid from A to K at position 33.
+The protein's natural variant, known as in strain: NCIB 8346, features a modification of the amino acid from VKK to TQA at position 41.
+The protein's natural variant, known as in strain: NCIB 8346, features a modification of the amino acid from G to S at position 44.
+The protein's natural variant, known as in strain: NCIB 8346, features a modification of the amino acid from L to Q at position 47.
+The protein's natural variant, known as in strain: NCIB 8346, features a modification of the amino acid from G to E at position 52.
+The protein's natural variant, known as in strain: NCIB 8346, features a modification of the amino acid from E to A at position 56.
+The protein's natural variant, known as in strain: NCIB 8346, features a modification of the amino acid from GD to AN at position 60.
+The protein's natural variant, known as in strain: NCIB 8346, features a modification of the amino acid from S to A at position 69.
+The protein's natural variant, known as in strain: NCIB 8346, features a modification of the amino acid from K to T at position 71.
+The protein's natural variant, known as in strain: NCIB 8346, features a modification of the amino acid from K to Q at position 74.
+The protein's natural variant, known as in strain: NCIB 8346, features a modification of the amino acid from G to A at position 104.
+The protein's natural variant, known as in strain: NCIB 8346, features a modification of the amino acid from SN to PD at position 109.
+The protein's natural variant, known as in strain: NCIB 8346, features a modification of the amino acid from M to Q at position 116.
+The protein's natural variant, known as in strain: NCIB 8346, features a modification of the amino acid from K to G at position 125.
+The protein's natural variant, known as in strain: NCIB 8346, features a modification of the amino acid from I to V at position 128.
+The protein's natural variant, known as in strain: NCIB 8346, features a modification of the amino acid from A to K at position 140.
+The protein's natural variant, known as in strain: NCIB 8346, features a modification of the amino acid from PYAPK to AWPWQ at position 149.
+The protein's natural variant, known as in strain: NCIB 8346, features a modification of the amino acid from I to L at position 153.
+The protein's natural variant, known as in strain: NCIB 8346, features a modification of the amino acid from R to K at position 155.
+The protein's natural variant, known as in strain: NCIB 8346, features a modification of the amino acid from I to M at position 160.
+The protein's natural variant, known as in strain: NCIB 8346, features a modification of the amino acid from S to Y at position 162.
+The protein's natural variant, known as in strain: NCIB 8346, features a modification of the amino acid from I to V at position 169.
+The protein's natural variant, known as in strain: NCIB 8346, features a modification of the amino acid from EM to KF at position 188.
+The protein's natural variant, known as in strain: NCIB 8346, features a modification of the amino acid from S to A at position 208.
+The protein's natural variant, known as in strain: NCIB 8346, features a modification of the amino acid from I to V at position 217.
+The protein's natural variant, known as in strain: NCIB 8346, features a modification of the amino acid from H to Q at position 223.
+The protein's natural variant, known as in strain: NCIB 8346, features a modification of the amino acid from E to K at position 249.
+The protein's natural variant, known as in strain: NCIB 8346, features a modification of the amino acid from K to E at position 261.
+The protein's natural variant, known as in strain: NCIB 8346, features a modification of the amino acid from V to A at position 272.
+The protein's natural variant, known as in strain: NCIB 8346, features a modification of the amino acid from KF to EY at position 279.
+The natural variant of this protein is characterized by an amino acid alteration from A to T at position 38.
+The natural variant of this protein is characterized by an amino acid alteration from A to T at position 89.
+The protein's natural variant, known as in strain: various strains, features a modification of the amino acid from P to A at position 12.
+The protein's natural variant, known as in strain: various strains, features a modification of the amino acid from A to G at position 25.
+The protein's natural variant, known as in PREMBL2;, features a modification of the amino acid from H to Q at position 211.
+The protein's natural variant, known as in PREMBL2;, features a modification of the amino acid from G to R at position 540.
+The protein's natural variant, known as in MICCAP, features a modification of the amino acid from R to P at position 14.
+The protein's natural variant, known as in MICCAP;, features a modification of the amino acid from R to C at position 38.
+The protein's natural variant, known as in MICCAP;, features a modification of the amino acid from E to G at position 42.
+The protein's natural variant, known as in MICCAP;, features a modification of the amino acid from Y to C at position 63.
+The protein's natural variant, known as in MICCAP;, features a modification of the amino acid from F to Y at position 100.
+The protein's natural variant, known as in MICCAP;, features a modification of the amino acid from T to I at position 313.
+The protein's natural variant, known as in DEE82; decreased glutamate oxaloacetate transferase activity;, features a modification of the amino acid from R to G at position 262.
+The protein's natural variant, known as in DEE82; unknown pathological significance;, features a modification of the amino acid from R to G at position 337.
+The protein's natural variant, known as in DEE82; unknown pathological significance; decreased glutamate oxaloacetate transferase activity;, features a modification of the amino acid from G to V at position 366.
+The protein's natural variant, known as in GNASHYP;, features a modification of the amino acid from A to D at position 436.
+The protein's natural variant, known as in GNAS hyperfunction, features a modification of the amino acid from A to APADPDSGAAPDA at position 437.
+The protein's natural variant, known as in GNASHYP;, features a modification of the amino acid from P to R at position 459.
+The protein's natural variant, known as in strain: Md199, features a modification of the amino acid from L to M at position 135.
+The protein's natural variant, known as in strain: Md106, Md199 and NewC, features a modification of the amino acid from E to V at position 163.
+The protein's natural variant, known as in strain: Md199, NewC, features a modification of the amino acid from K to R at position 165.
+The protein's natural variant, known as in strain: Md199, NewC, features a modification of the amino acid from A to V at position 167.
+The protein's natural variant, known as in strain: C1674, Md106, Md199, NewC, Sim and W501, features a modification of the amino acid from F to L at position 207.
+The protein's natural variant, known as in strain: Md199, features a modification of the amino acid from I to V at position 212.
+The protein's natural variant, known as in strain: Md199, features a modification of the amino acid from D to N at position 223.
+The protein's natural variant, known as in strain: Md199, features a modification of the amino acid from K to T at position 364.
+The protein's natural variant, known as in strain: Md106, Md199 and NewC, features a modification of the amino acid from L to F at position 381.
+The protein's natural variant, known as in strain: NewC, features a modification of the amino acid from K to Q at position 392.
+The protein's natural variant, known as in HYPTRP; reduced tryptophan 2,3-dioxygenase activity; does not affect homotetramerization;, features a modification of the amino acid from M to I at position 108.
+The protein's natural variant, known as in POF16; unknown pathological significance; affects nuclear localization; the mutant exhibits a punctate localization in the nucleus;, features a modification of the amino acid from L to P at position 532.
+The protein's natural variant, known as in minor variant, features a modification of the amino acid from P to S at position 71.
+The protein's natural variant, known as in CMD2H; contrary to the wild type, the mutant is unable to rescue cardiac failure in zebrafish lacking GET3; results in decreased function in tail-anchored membrane protein insertion into ER membrane; has no effect on thermal stability, features a modification of the amino acid from V to A at position 163.
+The protein's natural variant, known as in CMD2H; when associated in cis with 305-Q--Q-348 del, features a modification of the amino acid from C to W at position 289.
+The protein's natural variant, known as abolishes catalytic activity;, features a modification of the amino acid from G to V at position 277.
+The protein's natural variant, known as in ETL1; probably affects signal sequence processing and secretion, features a modification of the amino acid from L to R at position 26.
+The protein's natural variant, known as in ETL1;, features a modification of the amino acid from C to G at position 42.
+The protein's natural variant, known as in ETL1;, features a modification of the amino acid from C to R at position 42.
+The protein's natural variant, known as in ETL1; loss of protein secretion; does not affect glycosylation status of the protein;, features a modification of the amino acid from C to R at position 46.
+The protein's natural variant, known as in ETL1, features a modification of the amino acid from A to D at position 110.
+The protein's natural variant, known as in ETL1;, features a modification of the amino acid from I to K at position 122.
+The protein's natural variant, known as in ETL1, features a modification of the amino acid from E to K at position 123.
+The protein's natural variant, known as in ETL1;, features a modification of the amino acid from R to W at position 136.
+The protein's natural variant, known as in ETL1; loss of protein secretion; does not affect glycosylation status of the protein, features a modification of the amino acid from S to R at position 145.
+The protein's natural variant, known as in ETL1, features a modification of the amino acid from L to P at position 154.
+The protein's natural variant, known as in ETL1; loss of protein secretion; does not affect glycosylation status of the protein, features a modification of the amino acid from C to R at position 200.
+The protein's natural variant, known as in ETL1; loss of protein secretion;, features a modification of the amino acid from L to P at position 232.
+The protein's natural variant, known as in ETL1, features a modification of the amino acid from I to T at position 298.
+The protein's natural variant, known as in ETL1; loss of protein secretion; protein is retained in the endoplasmic reticulum; does not affect glycosylation status of the protein;, features a modification of the amino acid from F to C at position 318.
+The protein's natural variant, known as in ETL1; loss of protein secretion; protein is retained in the endoplasmic reticulum; does not affect glycosylation status of the protein;, features a modification of the amino acid from E to A at position 383.
+The protein's natural variant, known as in ETL1, features a modification of the amino acid from V to E at position 432.
+The protein's natural variant, known as in ETL1;, features a modification of the amino acid from S to L at position 473.
+The protein's natural variant, known as in MDPT2; no effect on VCL-binding;, features a modification of the amino acid from R to C at position 54.
+The protein's natural variant, known as in MDPT2; no effect on VCL-binding;, features a modification of the amino acid from E to K at position 307.
+The protein's natural variant, known as in MDPT2; no effect on VCL-binding;, features a modification of the amino acid from L to S at position 318.
+The protein's natural variant, known as in MDPT2; no effect on VCL-binding;, features a modification of the amino acid from I to M at position 431.
+The natural variant of this protein is characterized by an amino acid alteration from P to S at position 17.
+The protein's natural variant, known as in LS;, features a modification of the amino acid from F to L at position 124.
+The protein's natural variant, known as in MELAS;, features a modification of the amino acid from E to G at position 145.
+The natural variant of this protein is characterized by an amino acid alteration from G to D at position 146.
+The natural variant of this protein is characterized by an amino acid alteration from A to V at position 160.
+The protein's natural variant, known as in LHON;, features a modification of the amino acid from A to V at position 171.
+The protein's natural variant, known as in MELAS;, features a modification of the amino acid from A to T at position 236.
+The protein's natural variant, known as in MELAS; disease features overlapping with Leber optic atrophy and Leigh syndrome;, features a modification of the amino acid from M to L at position 237.
+The protein's natural variant, known as in LS;, features a modification of the amino acid from S to C at position 250.
+The protein's natural variant, known as found in a patient with mitochondrial complex I deficiency; unknown pathological significance;, features a modification of the amino acid from V to A at position 253.
+The protein's natural variant, known as in MELAS;, features a modification of the amino acid from D to N at position 393.
+The protein's natural variant, known as found in a patient with mitochondrial complex I deficiency; unknown pathological significance;, features a modification of the amino acid from N to S at position 447.
+The protein's natural variant, known as in LHON; secondary mutation; does not seem to directly cause the disease;, features a modification of the amino acid from A to T at position 458.
+The protein's natural variant, known as in LHON; primary rare mutation;, features a modification of the amino acid from G to E at position 465.
+The natural variant of this protein is characterized by an amino acid alteration from D to G at position 503.
+The protein's natural variant, known as in strain: 129/SvJ, features a modification of the amino acid from E to K at position 242.
+The protein's natural variant, known as probable disease-associated variant found in autism; hypomorphic variant affecting dendritic spines development and maintenance; results in reduced interaction with CTNNB1;, features a modification of the amino acid from G to S at position 34.
+The protein's natural variant, known as probable disease-associated variant found in autism; hypomorphic variant affecting Wnt signaling;, features a modification of the amino acid from P to L at position 189.
+The protein's natural variant, known as probable disease-associated variant found in autism; hypomorphic variant affecting Wnt signaling;, features a modification of the amino acid from P to L at position 224.
+The protein's natural variant, known as found in patients with autism; unknown pathological significance; has no effect on Wnt signaling;, features a modification of the amino acid from G to C at position 275.
+The protein's natural variant, known as has no effect on Wnt signaling;, features a modification of the amino acid from R to H at position 330.
+The protein's natural variant, known as probable disease-associated variant found in autism; hypomorphic variant affecting Wnt signaling;, features a modification of the amino acid from R to H at position 454.
+The protein's natural variant, known as has no effect on Wnt signaling;, features a modification of the amino acid from D to N at position 465.
+The protein's natural variant, known as has no effect on Wnt signaling;, features a modification of the amino acid from A to T at position 482.
+The protein's natural variant, known as probable disease-associated variant found in autism; hypomorphic variant affecting Wnt signaling;, features a modification of the amino acid from Q to P at position 507.
+The protein's natural variant, known as probable disease-associated variant found in autism; loss-of-function variant affecting dendritic spines development and maintenance; results in reduced interaction with CTNNB1;, features a modification of the amino acid from R to C at position 713.
+The protein's natural variant, known as has no effect on Wnt signaling;, features a modification of the amino acid from G to R at position 810.
+The protein's natural variant, known as found in patients with autism; unknown pathological significance; has no effect on Wnt signaling;, features a modification of the amino acid from T to M at position 862.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from P to S at position 1159.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation, features a modification of the amino acid from S to F at position 89.
+The protein's natural variant, known as in a lung neuroendocrine carcinoma sample; somatic mutation, features a modification of the amino acid from M to I at position 316.
+The protein's natural variant, known as in AGS7; enhances the interferon signaling pathway activation; enhances the stability of filament formation; enhances dsRNA binding activity; no loss of ATP hydrolysis;, features a modification of the amino acid from R to G at position 337.
+The protein's natural variant, known as in IMD95; does not bind the double-stranded RNA analog poly(I:C); loss of IFNB1 and NFKB promoter activation after stimulation with poly(I:C), when tested in a luciferase reporter assay, features a modification of the amino acid from K to E at position 365.
+The protein's natural variant, known as in AGS7; enhances IFNB1 promoter activation; loss of ligand-induced responsiveness;, features a modification of the amino acid from L to F at position 372.
+The protein's natural variant, known as in AGS7; enhances the interferon signaling pathway activation; enhances the stability of filament formation; enhances dsRNA binding activity; no loss of ATP hydrolysis;, features a modification of the amino acid from D to V at position 393.
+The protein's natural variant, known as in AGS7; enhances IFNB1 promoter activation; loss of ligand-induced responsiveness;, features a modification of the amino acid from A to T at position 452.
+The protein's natural variant, known as in AGS7; enhances the interferon signaling pathway activation; enhances the stability of filament formation; enhances dsRNA binding activity; no loss of ATP hydrolysis;, features a modification of the amino acid from G to R at position 495.
+The protein's natural variant, known as in AGS7; enhances the interferon signaling pathway activation; enhances the stability of filament formation; enhances dsRNA binding activity; no loss of ATP hydrolysis;, features a modification of the amino acid from R to Q at position 720.
+The protein's natural variant, known as in AGS7; enhances the interferon signaling pathway activation; enhances the stability of filament formation; enhances dsRNA binding activity; no loss of ATP hydrolysis;, features a modification of the amino acid from R to C at position 779.
+The protein's natural variant, known as in AGS7; enhances the interferon signaling pathway activation; enhances the stability of filament formation; enhances dsRNA binding activity; enhances IFNB1 promoter activation; no loss of ATP hydrolysis;, features a modification of the amino acid from R to H at position 779.
+The protein's natural variant, known as in SGMRT1; gain-of-function mutation resulting in enhanced INFB1 induction;, features a modification of the amino acid from R to Q at position 822.
+The protein's natural variant, known as associated with susceptibility to T1D19;, features a modification of the amino acid from A to T at position 946.
+The protein's natural variant, known as in AISIMD; loss of inhibition of cytokine-induced STAT phosphorylation, including IFNG-induced STAT1 phosphorylation, IL2-induced STAT5 phosphorylation and IL4-induced STAT6 phosphorylation, features a modification of the amino acid from R to W at position 22.
+The protein's natural variant, known as in AISIMD; loss of inhibition of cytokine-induced STAT phosphorylation, including IFNG-induced STAT1 phosphorylation, IL2-induced STAT5 phosphorylation and IL4-induced STAT6 phosphorylation, features a modification of the amino acid from P to R at position 123.
+The protein's natural variant, known as in AISIMD; unknown pathological significance; when transfected into HEK293T cells, shows impaired suppression of IFNG-mediated gene expression compared to wild-type, features a modification of the amino acid from Y to H at position 154.
+The protein's natural variant, known as in strain: RDD012, features a modification of the amino acid from P to A at position 61.
+The protein's natural variant, known as in strain: RDD012, features a modification of the amino acid from K to E at position 70.
+The natural variant of this protein is characterized by an amino acid alteration from L to Y at position 48.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from R to G at position 8.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from A to E at position 342.
+The protein's natural variant, known as in strain: 0811.4, features a modification of the amino acid from T to A at position 611.
+The protein's natural variant, known as in strain: 0811.4, features a modification of the amino acid from S to F at position 617.
+The protein's natural variant, known as in strain: Guana, features a modification of the amino acid from G to V at position 622.
+The protein's natural variant, known as in strain: Manaus 2, features a modification of the amino acid from G to A at position 724.
+The protein's natural variant, known as in strain: Santa Maria, features a modification of the amino acid from G to S at position 726.
+The protein's natural variant, known as in strain: Porto Alegre 4, features a modification of the amino acid from G to V at position 733.
+The protein's natural variant, known as in strain: Guadeloupe and Guana, features a modification of the amino acid from S to A at position 747.
+The protein's natural variant, known as in strain: 0811.4, features a modification of the amino acid from A to T at position 886.
+The protein's natural variant, known as in strain: TW18/TW5, features a modification of the amino acid from Q to QQQ at position 70.
+The protein's natural variant, known as in HCAD;, features a modification of the amino acid from R to C at position 754.
+The protein's natural variant, known as in LGMDR1;, features a modification of the amino acid from V to I at position 4.
+The protein's natural variant, known as in LGMDR1;, features a modification of the amino acid from P to L at position 26.
+The protein's natural variant, known as in LGMDR1, features a modification of the amino acid from D to N at position 77.
+The protein's natural variant, known as in LGMDR1; severe;, features a modification of the amino acid from S to F at position 86.
+The protein's natural variant, known as in LGMDR1;, features a modification of the amino acid from R to G at position 118.
+The protein's natural variant, known as in LGMDR1, features a modification of the amino acid from C to R at position 137.
+The protein's natural variant, known as in LGMDR1, features a modification of the amino acid from I to L at position 162.
+The protein's natural variant, known as in LGMDR1, features a modification of the amino acid from L to Q at position 182.
+The protein's natural variant, known as in LGMDR1, features a modification of the amino acid from P to L at position 183.
+The protein's natural variant, known as in LGMDR1;, features a modification of the amino acid from L to P at position 189.
+The protein's natural variant, known as in LGMDR1;, features a modification of the amino acid from G to S at position 214.
+The protein's natural variant, known as in LGMDR1, features a modification of the amino acid from S to P at position 215.
+The protein's natural variant, known as in LGMDR1;, features a modification of the amino acid from E to K at position 217.
+The protein's natural variant, known as in LGMDR1;, features a modification of the amino acid from G to R at position 222.
+The protein's natural variant, known as in LGMDR1, features a modification of the amino acid from E to K at position 226.
+The protein's natural variant, known as in LGMDR1, features a modification of the amino acid from T to I at position 232.
+The protein's natural variant, known as in LGMDR1;, features a modification of the amino acid from G to E at position 234.
+The protein's natural variant, known as in LGMDR1;, features a modification of the amino acid from P to L at position 319.
+The protein's natural variant, known as in LGMDR1, features a modification of the amino acid from H to Q at position 334.
+The protein's natural variant, known as in LGMDR1, features a modification of the amino acid from Y to N at position 336.
+The protein's natural variant, known as in LGMDR1;, features a modification of the amino acid from V to G at position 354.
+The protein's natural variant, known as in LGMDR1;, features a modification of the amino acid from W to C at position 360.
+The protein's natural variant, known as in LGMDR1;, features a modification of the amino acid from R to C at position 437.
+The protein's natural variant, known as in LGMDR1;, features a modification of the amino acid from R to W at position 440.
+The protein's natural variant, known as in LGMDR1, features a modification of the amino acid from G to D at position 441.
+The protein's natural variant, known as in LGMDR1;, features a modification of the amino acid from G to R at position 445.
+The protein's natural variant, known as in LGMDR1;, features a modification of the amino acid from R to C at position 448.
+The protein's natural variant, known as in LGMDR1;, features a modification of the amino acid from R to G at position 448.
+The protein's natural variant, known as in LGMDR1;, features a modification of the amino acid from R to H at position 448.
+The protein's natural variant, known as in LGMDR1;, features a modification of the amino acid from S to G at position 479.
+The protein's natural variant, known as in LGMDR1, features a modification of the amino acid from Q to E at position 486.
+The protein's natural variant, known as in LGMDR1;, features a modification of the amino acid from R to Q at position 489.
+The protein's natural variant, known as in LGMDR1;, features a modification of the amino acid from R to W at position 489.
+The protein's natural variant, known as in LGMDR1;, features a modification of the amino acid from R to Q at position 490.
+The protein's natural variant, known as in LGMDR1;, features a modification of the amino acid from R to W at position 490.
+The protein's natural variant, known as in LGMDR1;, features a modification of the amino acid from R to W at position 493.
+The protein's natural variant, known as in LGMDR1;, features a modification of the amino acid from G to R at position 496.
+The protein's natural variant, known as in LGMDR1;, features a modification of the amino acid from I to T at position 502.
+The protein's natural variant, known as in LGMDR1;, features a modification of the amino acid from R to Q at position 541.
+The protein's natural variant, known as in LGMDR1;, features a modification of the amino acid from G to W at position 567.
+The protein's natural variant, known as in LGMDR1;, features a modification of the amino acid from R to Q at position 572.
+The protein's natural variant, known as in LGMDR1;, features a modification of the amino acid from R to W at position 572.
+The protein's natural variant, known as in LGMDR1;, features a modification of the amino acid from S to L at position 606.
+The protein's natural variant, known as in LGMDR1, features a modification of the amino acid from Q to P at position 638.
+The protein's natural variant, known as in LGMDR1, features a modification of the amino acid from R to P at position 698.
+The protein's natural variant, known as in LGMDR1;, features a modification of the amino acid from A to V at position 702.
+The protein's natural variant, known as in LGMDR1, features a modification of the amino acid from D to G at position 705.
+The protein's natural variant, known as in LGMDR1, features a modification of the amino acid from D to H at position 705.
+The protein's natural variant, known as in LGMDR1, features a modification of the amino acid from F to S at position 731.
+The protein's natural variant, known as in LGMDR1;, features a modification of the amino acid from S to G at position 744.
+The protein's natural variant, known as in LGMDR1;, features a modification of the amino acid from R to Q at position 748.
+The protein's natural variant, known as in LGMDR1;, features a modification of the amino acid from R to Q at position 769.
+The protein's natural variant, known as in LGMDR1; unknown pathological significance, features a modification of the amino acid from H to D at position 774.
+The protein's natural variant, known as in LGMDR1; unknown pathological significance;, features a modification of the amino acid from A to E at position 798.
+The protein's natural variant, known as in strain: CLIB 95, CLIB 219, CLIB 382, CLIB 388, CLIB 413, CLIB 556, CLIB 630, K1, R12, R13, YIIc12 and YIIc17, features a modification of the amino acid from E to K at position 58.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from E to Q at position 53.
+The protein's natural variant, known as in MYP21; unknown pathological significance;, features a modification of the amino acid from T to M at position 242.
+The protein's natural variant, known as in MYP21; unknown pathological significance;, features a modification of the amino acid from E to V at position 274.
+The protein's natural variant, known as in MYP21; unknown pathological significance;, features a modification of the amino acid from E to K at position 305.
+The protein's natural variant, known as variant of uncertain significance, features a modification of the amino acid from K to M at position 369.
+The protein's natural variant, known as in MYP21; unknown pathological significance, features a modification of the amino acid from T to A at position 401.
+The protein's natural variant, known as in MYP21;, features a modification of the amino acid from I to V at position 587.
+The protein's natural variant, known as in MYP21;, features a modification of the amino acid from S to G at position 672.
+The protein's natural variant, known as in MYP21, features a modification of the amino acid from R to G at position 680.
+The protein's natural variant, known as in MYP21; unknown pathological significance;, features a modification of the amino acid from R to T at position 683.
+The protein's natural variant, known as in MYP21, features a modification of the amino acid from C to Y at position 699.
+The protein's natural variant, known as in MYP21; unknown pathological significance, features a modification of the amino acid from D to H at position 851.
+The protein's natural variant, known as in MYP21; unknown pathological significance;, features a modification of the amino acid from T to S at position 956.
+The protein's natural variant, known as in MYP21; unknown pathological significance;, features a modification of the amino acid from Y to C at position 1089.
+The protein's natural variant, known as in MYP21; unknown pathological significance, features a modification of the amino acid from E to G at position 1278.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from T to K at position 297.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from R to Q at position 303.
+The protein's natural variant, known as rare variant; found in individuals suffering from stuttering; unknown pathological significance, features a modification of the amino acid from L to LARL at position 5.
+The protein's natural variant, known as rare variant; found in individuals suffering from stuttering; unknown pathological significance;, features a modification of the amino acid from A to E at position 25.
+The protein's natural variant, known as in MLIIIC; decreased localization to Golgi apparatus;, features a modification of the amino acid from G to S at position 106.
+The protein's natural variant, known as in MLIIIC; loss of localization to Golgi apparatus;, features a modification of the amino acid from G to S at position 126.
+The protein's natural variant, known as in MLIIIC; decreased localization to Golgi apparatus, features a modification of the amino acid from C to Y at position 142.
+The protein's natural variant, known as rare variant; found in individuals suffering from stuttering; unknown pathological significance;, features a modification of the amino acid from L to V at position 230.
+The protein's natural variant, known as does not affect localization to Golgi apparatus;, features a modification of the amino acid from T to M at position 286.
+The natural variant of this protein is characterized by an amino acid alteration from M to T at position 117.
+The protein's natural variant, known as in DFNA77; unknown pathological significance, features a modification of the amino acid from G to D at position 231.
+The natural variant of this protein is characterized by an amino acid alteration from W to C at position 242.
+The protein's natural variant, known as in DFNA77; unknown pathological significance, features a modification of the amino acid from E to V at position 296.
+The protein's natural variant, known as in DFNA77; changes protein subcellular localization expressed in both membrane and cytoplasm; produces unstable mRNA, features a modification of the amino acid from N to S at position 590.
+The protein's natural variant, known as no effect on leukotriene C4 and estradiol glucuronide transport;, features a modification of the amino acid from G to V at position 671.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 886.
+The natural variant of this protein is characterized by an amino acid alteration from G to R at position 1007.
+The natural variant of this protein is characterized by an amino acid alteration from M to T at position 1086.
+The protein's natural variant, known as in SULEHS;, features a modification of the amino acid from T to M at position 234.
+The protein's natural variant, known as in OOMD4;, features a modification of the amino acid from L to R at position 189.
+The protein's natural variant, known as in OOMD4;, features a modification of the amino acid from Y to N at position 217.
+The protein's natural variant, known as in OOMD4; unknown pathological significance;, features a modification of the amino acid from R to Q at position 280.
+The protein's natural variant, known as in OOMD4; unknown pathological significance;, features a modification of the amino acid from I to T at position 318.
+The protein's natural variant, known as in OOMD4; unknown pathological significance;, features a modification of the amino acid from G to R at position 370.
+The protein's natural variant, known as in CPRF;, features a modification of the amino acid from E to K at position 379.
+The protein's natural variant, known as in CPRF;, features a modification of the amino acid from D to G at position 556.
+The protein's natural variant, known as in CPRF;, features a modification of the amino acid from Y to H at position 761.
+The natural variant of this protein is characterized by an amino acid alteration from PP to RR at position 42.
+The natural variant of this protein is characterized by an amino acid alteration from V to F at position 55.
+The protein's natural variant, known as in NS3;, features a modification of the amino acid from K to E at position 5.
+The protein's natural variant, known as in GASC; found also in a patient with Costello syndrome; exhibits only minor alterations in its in vitro biochemical behavior compared to wild-type protein;, features a modification of the amino acid from K to N at position 5.
+The protein's natural variant, known as in AML; expression in 3T3 cell causes cellular transformation; expression in COS cells activates the Ras-MAPK signaling pathway; lower GTPase activity; faster GDP dissociation rate, features a modification of the amino acid from G to GG at position 10.
+The protein's natural variant, known as in colorectal cancer samples; somatic mutation;, features a modification of the amino acid from G to A at position 12.
+The protein's natural variant, known as in lung carcinoma; somatic mutation; also found in metastatic colorectal cancer;, features a modification of the amino acid from G to C at position 12.
+The protein's natural variant, known as in GASC, JMML and SFM; somatic mutation; also found in pancreatic carcinoma and lung carcinoma; also found in metastatic colorectal cancer;, features a modification of the amino acid from G to D at position 12.
+The protein's natural variant, known as in lung cancer and bladder cancer; somatic mutation;, features a modification of the amino acid from G to R at position 12.
+The protein's natural variant, known as in GASC and JMML; also found in lung carcinoma; somatic mutation;, features a modification of the amino acid from G to S at position 12.
+The protein's natural variant, known as in GASC; also found in lung carcinoma, pancreatic carcinoma and colon cancer; also found in metastatic colorectal cancer; somatic mutation; it is constitutively activated and stimulates transcription activation of tumor suppressor genes in non-transformed fibroblasts;, features a modification of the amino acid from G to V at position 12.
+The protein's natural variant, known as in GASC, JMML and OES; also found in a breast carcinoma cell line; somatic mutation;, features a modification of the amino acid from G to D at position 13.
+The protein's natural variant, known as in pylocytic astrocytoma; somatic mutation; increase activation of the Ras pathway;, features a modification of the amino acid from G to R at position 13.
+The protein's natural variant, known as in NS3; affects activity and impairs responsiveness to GTPase activating proteins; characterized by a strong increase of both intrinsic and guanine nucleotide exchanged factor-catalyzed nucleotide exchange leading to an increased level of the activated state;, features a modification of the amino acid from V to I at position 14.
+The protein's natural variant, known as in OES; somatic mutation;, features a modification of the amino acid from L to F at position 19.
+The protein's natural variant, known as in CFC2; exhibits an increase in intrinsic and guanine nucleotide exchange factor catalyzed nucleotide exchange in combination with an impaired GTPase-activating protein-stimulated GTP hydrolysis but functional in interaction with effectors;, features a modification of the amino acid from Q to E at position 22.
+The protein's natural variant, known as in NS3; impairs GTPase-activating protein stimulated GTP hydrolysis with unaffected intrinsic functions and a virtually functional effector interaction;, features a modification of the amino acid from Q to R at position 22.
+The protein's natural variant, known as in NS3; characterized by a defective GTPase-activating protein sensitivity and a strongly reduced interaction with effectors;, features a modification of the amino acid from P to L at position 34.
+The protein's natural variant, known as in NS3, features a modification of the amino acid from P to Q at position 34.
+The protein's natural variant, known as in CFC2; characterized by a defective GTPase-activating protein sensitivity and a strongly reduced interaction with effectors;, features a modification of the amino acid from P to R at position 34.
+The protein's natural variant, known as in NS3;, features a modification of the amino acid from I to M at position 36.
+The protein's natural variant, known as in NS3; affects activity and impairs responsiveness to GTPase activating proteins; exhibits only minor alterations in its in vitro biochemical behavior compared to wild-type protein;, features a modification of the amino acid from T to I at position 58.
+The protein's natural variant, known as in GASC; also found in bladder cancer; somatic mutation;, features a modification of the amino acid from A to T at position 59.
+The protein's natural variant, known as in CFC2; characterized by a defective GTPase-activating protein sensitivity and a strongly reduced interaction with effectors;, features a modification of the amino acid from G to R at position 60.
+The protein's natural variant, known as in NS3;, features a modification of the amino acid from G to S at position 60.
+The protein's natural variant, known as in lung carcinoma;, features a modification of the amino acid from Q to H at position 61.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from Q to R at position 61.
+The protein's natural variant, known as in CFC2;, features a modification of the amino acid from Y to H at position 71.
+The protein's natural variant, known as in colorectal cancer samples; somatic mutation;, features a modification of the amino acid from K to N at position 117.
+The protein's natural variant, known as in OES; somatic mutation; also found in colorectal cancer samples;, features a modification of the amino acid from A to T at position 146.
+The protein's natural variant, known as in OES; somatic mutation;, features a modification of the amino acid from A to V at position 146.
+The protein's natural variant, known as in CFC2;, features a modification of the amino acid from K to E at position 147.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from L to M at position 309.
+The protein's natural variant, known as requires 2 nucleotide substitutions;, features a modification of the amino acid from A to K at position 758.
+The protein's natural variant, known as found in a patient with global delayed development; unknown pathological significance;, features a modification of the amino acid from R to W at position 123.
+The protein's natural variant, known as confirmed at protein level;, features a modification of the amino acid from E to G at position 2017.
+The protein's natural variant, known as in alpha-2, features a modification of the amino acid from A to D at position 5.
+The protein's natural variant, known as in alpha-2, features a modification of the amino acid from N to H at position 9.
+The protein's natural variant, known as in a patient with retinal dytrophy; unknown pathological significance; loss of interaction with BSG; loss of ability to sustain retinal cone survival;, features a modification of the amino acid from E to K at position 64.
+The natural variant of this protein is characterized by an amino acid alteration from G to W at position 112.
+The protein's natural variant, known as no effect on recombination activity;, features a modification of the amino acid from A to V at position 156.
+The protein's natural variant, known as in CHIDG; reduced recombination activity;, features a modification of the amino acid from R to W at position 314.
+The protein's natural variant, known as in OS;, features a modification of the amino acid from C to Y at position 328.
+The protein's natural variant, known as found in a patient with common variable immunodeficiency with B cell deficiency; decreased recombinant activity, features a modification of the amino acid from C to Y at position 358.
+The protein's natural variant, known as found in a patient with T and B cell immunodeficiency and progressive multifocal leukoencephalopathy; unknown pathological significance;, features a modification of the amino acid from H to D at position 375.
+The protein's natural variant, known as in OS;, features a modification of the amino acid from R to C at position 396.
+The protein's natural variant, known as in OS;, features a modification of the amino acid from R to H at position 396.
+The protein's natural variant, known as in OS;, features a modification of the amino acid from R to L at position 396.
+The protein's natural variant, known as in OS;, features a modification of the amino acid from S to P at position 401.
+The protein's natural variant, known as in OS; found in patients with an atypical form of severe combined immunodeficiency/Omenn syndrome;, features a modification of the amino acid from R to Q at position 410.
+The protein's natural variant, known as in OS;, features a modification of the amino acid from D to G at position 429.
+The protein's natural variant, known as in OS and T(-)B(-)NK(+) SCID; found in a patient with an atypical form of severe combined immunodeficiency/Omenn syndrome;, features a modification of the amino acid from V to M at position 433.
+The protein's natural variant, known as in OS;, features a modification of the amino acid from M to V at position 435.
+The protein's natural variant, known as in OS; found in patients with an atypical form of severe combined immunodeficiency/Omenn syndrome;, features a modification of the amino acid from A to V at position 444.
+The protein's natural variant, known as in OS;, features a modification of the amino acid from L to Q at position 454.
+The protein's natural variant, known as probable disease-associated variant found in a patient with relatively late onset of infections and isolated T-cell lymphopenia; also found in a patient with T and B cell immunodeficiency and progressive multifocal leukoencephalopathy; decreases recombination activity; no effect on protein abundance;, features a modification of the amino acid from R to C at position 474.
+The protein's natural variant, known as in OS; found in patients with an atypical form of severe combined immunodeficiency/Omenn syndrome;, features a modification of the amino acid from R to H at position 474.
+The protein's natural variant, known as in CHIDG and OS; found in patients with an atypical form of severe combined immunodeficiency/Omenn syndrome; reduced recombination activity when associated with H-737;, features a modification of the amino acid from R to W at position 507.
+The protein's natural variant, known as in OS; also found in patients with an atypical form of severe combined immunodeficiency/Omenn syndrome;, features a modification of the amino acid from W to C at position 522.
+The protein's natural variant, known as in T(-)B(-)NK(+) SCID and OS; also found in a patient with an atypical form of severe combined immunodeficiency/Omenn syndrome; decreased recombination activity;, features a modification of the amino acid from R to S at position 559.
+The protein's natural variant, known as in OS;, features a modification of the amino acid from R to C at position 561.
+The protein's natural variant, known as in OS;, features a modification of the amino acid from R to H at position 561.
+The protein's natural variant, known as found in a patient with an atypical form of combined immunodeficiency; unknown pathological significance;, features a modification of the amino acid from H to R at position 612.
+The protein's natural variant, known as in OS;, features a modification of the amino acid from R to C at position 624.
+The protein's natural variant, known as in T(-)B(-)NK(+) SCID; decreased recombination activity;, features a modification of the amino acid from R to H at position 624.
+The protein's natural variant, known as in OS;, features a modification of the amino acid from E to G at position 669.
+The protein's natural variant, known as in OS; also in a patient with multiple autoimmune disorders;, features a modification of the amino acid from R to W at position 699.
+The protein's natural variant, known as in T(-)B(-)NK(+) SCID; decreased recombination activity;, features a modification of the amino acid from E to K at position 722.
+The protein's natural variant, known as in OS and CHIDG; reduced recombination activity when associated with T-507;, features a modification of the amino acid from R to H at position 737.
+The protein's natural variant, known as in OS; found in patients with an atypical form of severe combined immunodeficiency/Omenn syndrome;, features a modification of the amino acid from H to L at position 753.
+The protein's natural variant, known as in CHIDG; reduced recombination activity;, features a modification of the amino acid from R to Q at position 778.
+The protein's natural variant, known as in T-CMVA; also found in a patient with an atypical form of severe combined immunodeficiency /Omenn syndrome;, features a modification of the amino acid from R to W at position 841.
+The protein's natural variant, known as probable disease-associated variant found in a patient with severe combined immunodeficiency with maternal fetal engraftment;, features a modification of the amino acid from N to I at position 855.
+The protein's natural variant, known as in OS;, features a modification of the amino acid from L to R at position 885.
+The protein's natural variant, known as in OS;, features a modification of the amino acid from Y to C at position 912.
+The protein's natural variant, known as in OS;, features a modification of the amino acid from R to Q at position 975.
+The protein's natural variant, known as in CHIDG; reduced recombination activity;, features a modification of the amino acid from R to W at position 975.
+The protein's natural variant, known as in T-CMVA;, features a modification of the amino acid from Q to P at position 981.
+The natural variant of this protein is characterized by an amino acid alteration from S to N at position 114.
+The natural variant of this protein is characterized by an amino acid alteration from V to A at position 142.
+The natural variant of this protein is characterized by an amino acid alteration from M to I at position 218.
+The natural variant of this protein is characterized by an amino acid alteration from D to H at position 399.
+The natural variant of this protein is characterized by an amino acid alteration from N to S at position 450.
+The protein's natural variant, known as in strain: Isolate JLP 16556, features a modification of the amino acid from W to L at position 175.
+The protein's natural variant, known as in strain: Isolate JLP 16556, features a modification of the amino acid from C to F at position 187.
+The protein's natural variant, known as in strain: Isolate JLP 16556, features a modification of the amino acid from V to M at position 240.
+The protein's natural variant, known as in strain: Isolate JLP 16556, features a modification of the amino acid from S to T at position 246.
+The protein's natural variant, known as in strain: Isolate JLP 16556, features a modification of the amino acid from V to M at position 302.
+The protein's natural variant, known as in strain: Isolate JLP 16556, features a modification of the amino acid from V to I at position 334.
+The protein's natural variant, known as in strain: Isolate JLP 16556, features a modification of the amino acid from V to L at position 353.
+The protein's natural variant, known as in IMD56; loss of function mutation; the mutation results in defective trafficking of the protein, with misfolding, impaired processing and abnormal subcellular distribution rather than proper expression at the plasma membrane;, features a modification of the amino acid from R to L at position 201.
+The natural variant of this protein is characterized by an amino acid alteration from A to L at position 1.
+The natural variant of this protein is characterized by an amino acid alteration from A to S at position 1.
+The natural variant of this protein is characterized by an amino acid alteration from P to R at position 131.
+The protein's natural variant, known as in EPEDD; affects the development of synapses in a mouse model overexpressing the human protein harboring this variant, features a modification of the amino acid from Q to R at position 269.
+The protein's natural variant, known as in EPEDD; affects the development of synapses in a mouse model overexpressing the human protein harboring this variant, features a modification of the amino acid from R to C at position 913.
+The protein's natural variant, known as in EPEDD; affects the development of synapses in a mouse model overexpressing the human protein harboring this variant;, features a modification of the amino acid from G to R at position 1369.
+The protein's natural variant, known as in EPEDD; affects the development of synapses in a mouse model overexpressing the human protein harboring this variant;, features a modification of the amino acid from R to H at position 1392.
+The protein's natural variant, known as in NEDSID; causes DNA damage repair defects associated with nucleolytic degradation of nascent DNA at stalled replication forks, features a modification of the amino acid from Y to D at position 1499.
+The protein's natural variant, known as in some liver tumors, features a modification of the amino acid from A to V at position 12.
+The protein's natural variant, known as in strain: 020, BALB/c, BALB/cJ, C3H/21BG, C3H/HeJ, CBA/J, MA/M4J and PL/J, features a modification of the amino acid from H to P at position 18.
+The protein's natural variant, known as in some liver tumors, features a modification of the amino acid from G to E at position 27.
+The protein's natural variant, known as in strain: BALB/c and BALB/cJ, features a modification of the amino acid from V to I at position 51.
+The protein's natural variant, known as in some liver tumors, features a modification of the amino acid from P to L at position 73.
+The protein's natural variant, known as in plasmacytoma cell lines, features a modification of the amino acid from V to M at position 74.
+The protein's natural variant, known as in plasmacytoma cell lines, features a modification of the amino acid from H to Y at position 75.
+The protein's natural variant, known as in strain: BALB/cJ, C57BL/6J and MOLF/Ei, features a modification of the amino acid from H to Q at position 90.
+The protein's natural variant, known as in plasmacytoma cell lines, features a modification of the amino acid from H to R at position 90.
+The protein's natural variant, known as in strain: BALB/cJ, C57BL/6J and MOLF/Ei, features a modification of the amino acid from C to S at position 127.
+The protein's natural variant, known as in strain: cv. Bla-10, cv. Bl-0, cv. Can-0, cv. Cnt-1, cv. Cvi-0, cv. Di-G, cv. Ema-1, cv. Ka-0, cv. Kas-1, cv. Landsberg erecta, cv. Lip-0, cv. No-0, cv. Pa-1, cv. Petergof, cv. Sei-0, cv. Sorbo, cv. Tac-0 and cv. Tsu-0, features a modification of the amino acid from V to D at position 40.
+The protein's natural variant, known as in strain: cv. Bla-10, cv. Bl-0, cv. Can-0, cv. Cnt-1, cv. Cvi-0, cv. Di-G, cv. Ema-1, cv. Ka-0, cv. Kas-1, cv. Landsberg erecta, cv. Lip-0, cv. No-0, cv. Pa-1, cv. Petergof, cv. Sei-0, cv. Sorbo, cv. Tac-0 and cv. Tsu-0, features a modification of the amino acid from Q to R at position 45.
+The protein's natural variant, known as in strain: cv. Per-1, cv. Su-0 and cv. Yo-0, features a modification of the amino acid from S to SSL at position 54.
+The protein's natural variant, known as in strain: cv. Bla-10, cv. Bl-0, cv. Can-0, cv. Cnt-1, cv. Cvi-0, cv. Di-G, cv. Ema-1, cv. Ka-0, cv. Kas-1, cv. Landsberg erecta, cv. Lip-0, cv. No-0, cv. Pa-1, cv. Petergof, cv. Sei-0, cv. Sorbo, cv. Tac-0 and cv. Tsu-0, features a modification of the amino acid from L to LSLSPS at position 56.
+The protein's natural variant, known as in strain: cv. Bla-10, cv. Bl-0, cv. Can-0, cv. Cnt-1, cv. Cvi-0, cv. Di-G, cv. Ema-1, cv. Ka-0, cv. Kas-1, cv. Landsberg erecta, cv. Lip-0, cv. No-0, cv. Pa-1, cv. Petergof, cv. Sei-0, cv. Sorbo, cv. Tac-0 and cv. Tsu-0, features a modification of the amino acid from D to N at position 80.
+The protein's natural variant, known as in strain: cv. Bla-10, cv. Bl-0, cv. Can-0, cv. Cnt-1, cv. Cvi-0, cv. Di-G, cv. Ema-1, cv. Ka-0, cv. Kas-1, cv. Landsberg erecta, cv. Lip-0, cv. No-0, cv. Pa-1, cv. Petergof, cv. Sei-0, cv. Sorbo, cv. Tac-0 and cv. Tsu-0, features a modification of the amino acid from V to I at position 104.
+The protein's natural variant, known as in strain: cv. Bla-10, cv. Bl-0, cv. Can-0, cv. Cnt-1, cv. Cvi-0, cv. Di-G, cv. Ema-1, cv. Ka-0, cv. Kas-1, cv. Landsberg erecta, cv. Lip-0, cv. No-0, cv. Pa-1, cv. Petergof, cv. Sei-0, cv. Sorbo, cv. Tac-0 and cv. Tsu-0, features a modification of the amino acid from E to G at position 111.
+The protein's natural variant, known as in strain: cv. Bla-10, cv. Bl-0, cv. Cal-0, cv. Can-0, cv. Cnt-1, cv. Cvi-0, cv. Di-G, cv. Di-1, cv. Ema-1, cv. Ka-0, cv. Kas-1, cv. Landsberg erecta, cv. Lip-0, cv. No-0, cv. Pa-1, cv. Per-1, cv. Petergof, cv. Sei-0, cv. Sorbo, cv. Su-0, cv. Tac-0, cv. Tsu-0 and cv. Yo-0, features a modification of the amino acid from Y to H at position 114.
+The protein's natural variant, known as in strain: cv. Di-1, features a modification of the amino acid from T to A at position 126.
+The protein's natural variant, known as in strain: cv. Bl-0, cv. Cnt-1, cv. Ema-1, cv. Ka-0, cv. Kas-1, cv. No-0, cv. Sei-0 and cv. Tac-0, features a modification of the amino acid from H to N at position 142.
+The protein's natural variant, known as in strain: cv. Bla-10, cv. Bl-0, cv. Can-0, cv. Cnt-1, cv. Cvi-0, cv. Di-G, cv. Ema-1, cv. Ka-0, cv. Kas-1, cv. Landsberg erecta, cv. No-0, cv. Pa-1, cv. Petergof, cv. Sei-0, cv. Sorbo, cv. Tac-0 and cv. Tsu-0, features a modification of the amino acid from HGI to QGV at position 149.
+The protein's natural variant, known as in strain: cv. Bla-10, cv. Bl-0, cv. Can-0, cv. Cnt-1, cv. Cvi-0, cv. Di-G, cv. Ema-1, cv. Ka-0, cv. Kas-1, cv. Landsberg erecta, cv. No-0, cv. Pa-1, cv. Petergof, cv. Sei-0, cv. Sorbo, cv. Tac-0 and cv. Tsu-0, features a modification of the amino acid from D to E at position 177.
+The protein's natural variant, known as in strain: cv. Sorbo, features a modification of the amino acid from I to M at position 237.
+The protein's natural variant, known as in strain: cv. Bla-10, cv. Bl-0, cv. Cnt-1, cv. Ema-1, cv. Ka-0, cv. Kas-1, cv. No-0, cv. Pa-1, cv. Sei-0 and cv. Tac-0, features a modification of the amino acid from L to Q at position 269.
+The protein's natural variant, known as in strain: cv. Can-0, cv. Cvi-0, cv. Di-G, cv. Landsberg erecta, cv. Lip-0, cv. Petergof, cv. Sorbo and cv. Tsu-0, features a modification of the amino acid from V to M at position 297.
+The protein's natural variant, known as in strain: cv. Can-0, cv. Cvi-0, cv. Di-G, cv. Landsberg erecta, cv. Lip-0, cv. Petergof, cv. Sorbo and cv. Tsu-0, features a modification of the amino acid from A to E at position 301.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from K to R at position 734.
+The protein's natural variant, known as in torS729; partial activation, features a modification of the amino acid from H to L at position 408.
+The protein's natural variant, known as in torS13; partial activation, features a modification of the amino acid from A to P at position 414.
+The protein's natural variant, known as in DMJDS2; decreased protein abundance; decreased nuclear localization; increased localization to the cytoplasm; changed regulation of gene expression;, features a modification of the amino acid from Q to R at position 251.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation, features a modification of the amino acid from R to S at position 676.
+The protein's natural variant, known as in DYT32; unknown pathological significance, features a modification of the amino acid from P to S at position 46.
+The protein's natural variant, known as in HLD12, features a modification of the amino acid from C to G at position 846.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from V to M at position 330.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to H at position 587.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to C at position 855.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from A to E at position 1315.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from D to Y at position 129.
+The protein's natural variant, known as in a breast infiltrating ductal carcinoma sample; somatic mutation, features a modification of the amino acid from K to T at position 347.
+The protein's natural variant, known as in a lung large cell carcinoma sample; somatic mutation, features a modification of the amino acid from Q to L at position 717.
+The protein's natural variant, known as in a lung squamous cell carcinoma sample; somatic mutation, features a modification of the amino acid from R to L at position 736.
+The protein's natural variant, known as in a lung neuroendocrine carcinoma sample; somatic mutation, features a modification of the amino acid from E to K at position 764.
+The protein's natural variant, known as in strain: K1 / E44, features a modification of the amino acid from I to V at position 114.
+The protein's natural variant, known as in strain: ATCC 13869, features a modification of the amino acid from KH to ND at position 79.
+The protein's natural variant, known as in allele ALDH3A1*2;, features a modification of the amino acid from P to A at position 329.
+The protein's natural variant, known as in strain: Serotype A2 / PH278 and Serotype A2 / PH494, features a modification of the amino acid from S to A at position 46.
+The protein's natural variant, known as in strain: Serotype A2 / PH494, features a modification of the amino acid from I to V at position 65.
+The protein's natural variant, known as in strain: Serotype A2 / PH494, features a modification of the amino acid from N to D at position 101.
+The protein's natural variant, known as in strain: Serotype A2 / PH494, features a modification of the amino acid from Q to K at position 104.
+The protein's natural variant, known as in strain: Serotype A2 / PH278, features a modification of the amino acid from D to E at position 322.
+The protein's natural variant, known as in strain: Serotype A2 / PH278 and Serotype A2 / PH494, features a modification of the amino acid from Y to D at position 468.
+The protein's natural variant, known as in strain: Serotype A2 / PH278, features a modification of the amino acid from G to D at position 655.
+The protein's natural variant, known as in SPGF16; loss of protein expression; impaired localization to nuclear inner membrane, features a modification of the amino acid from G to R at position 114.
+The protein's natural variant, known as in SPGF16; unknown pathological significance; in mouse model increases interaction with DNAJB13; impaired localization to nuclear inner membrane;, features a modification of the amino acid from M to K at position 162.
+The protein's natural variant, known as in SPGF16; unknown pathological significance; in mouse model decreases protein solubility as well as impairs nuclear inner membrane location and decreases interaction with DNAJB13;, features a modification of the amino acid from V to M at position 261.
+The protein's natural variant, known as in SPGF16; significant reduction in protein expression; impaired localization to nuclear inner membrane; in mouse model decreases interaction with DNAJB13;, features a modification of the amino acid from T to M at position 275.
+The protein's natural variant, known as in SPGF16; loss of protein expression; in mouse model impairs nuclear inner membrane location and decreases interaction with DNAJB13;, features a modification of the amino acid from N to I at position 348.
+The protein's natural variant, known as in SPGF16; unknown pathological significance; in mouse model impairs nuclear inner membrane location and decreases interaction with DNAJB13;, features a modification of the amino acid from R to C at position 356.
+The protein's natural variant, known as in HCC;, features a modification of the amino acid from Q to K at position 75.
+The protein's natural variant, known as in HNSCC cell lines;, features a modification of the amino acid from T to S at position 186.
+The protein's natural variant, known as in HCC, features a modification of the amino acid from A to S at position 563.
+The protein's natural variant, known as in HCC;, features a modification of the amino acid from N to H at position 873.
+The protein's natural variant, known as in HCC;, features a modification of the amino acid from Q to R at position 1201.
+The protein's natural variant, known as in NDCAGF; unknown pathological significance;, features a modification of the amino acid from R to C at position 77.
+The protein's natural variant, known as in NDCAGF;, features a modification of the amino acid from M to V at position 549.
+The protein's natural variant, known as in NDCAGF; unknown pathological significance;, features a modification of the amino acid from P to L at position 1874.
+The protein's natural variant, known as in NDCAGF; unknown pathological significance;, features a modification of the amino acid from L to P at position 2164.
+The protein's natural variant, known as in allele DRB5*02:02; requires 2 nucleotide substitutions, features a modification of the amino acid from K to V at position 14.
+The natural variant of this protein is characterized by an amino acid alteration from L to S at position 28.
+The protein's natural variant, known as in allele DRB5*02:02, allele DRB5*02:04 and allele DRB5*02:05;, features a modification of the amino acid from R to C at position 35.
+The protein's natural variant, known as in allele DRB5*01:02, allele DRB5*01:03, allele DRB5*02:02, allele DRB5*02:03, allele DRB5*02:04 and allele DRB5*02:05;, features a modification of the amino acid from D to G at position 59.
+The protein's natural variant, known as in allele DRB5*01:02, allele DRB5*01:03, allele DRB5*02:02, allele DRB5*02:03, allele DRB5*02:04 and allele DRB5*02:05;, features a modification of the amino acid from D to N at position 66.
+The protein's natural variant, known as in allele DRB5*01:14;, features a modification of the amino acid from D to Y at position 66.
+The protein's natural variant, known as in allele DRB5*01:02, allele DRB5*01:03, allele DRB5*01:05, allele DRB5*01:14, allele DRB5*02:02, allele DRB5*02:03, allele DRB5*02:04 and allele DRB5*02:05;, features a modification of the amino acid from L to V at position 67.
+The protein's natural variant, known as in allele DRB5*01:13, features a modification of the amino acid from A to E at position 87.
+The protein's natural variant, known as in allele DRB5*01:12;, features a modification of the amino acid from Y to S at position 89.
+The protein's natural variant, known as in allele DRB5*01:06, allele DRB5*01:07, allele DRB5*01:11, allele DRB5*02:02 and allele DRB5*02:03;, features a modification of the amino acid from F to I at position 96.
+The protein's natural variant, known as in allele DRB5*02:05;, features a modification of the amino acid from F to L at position 96.
+The protein's natural variant, known as in allele DRB5*01:09;, features a modification of the amino acid from D to N at position 99.
+The protein's natural variant, known as in allele DRB5*01:06, allele DRB5*01:11, allele DRB5*02:02, allele DRB5*02:03, allele DRB5*02:04 and allele DRB5*02:05; requires 2 nucleotide substitutions, features a modification of the amino acid from D to Q at position 99.
+The protein's natural variant, known as in allele DRB5*01:12; requires 2 nucleotide substitutions, features a modification of the amino acid from D to R at position 99.
+The protein's natural variant, known as in allele DRB5*01:06, allele DRB5*01:11, allele DRB5*02:02, allele DRB5*02:03 and allele DRB5*02:04; requires 2 nucleotide substitutions, features a modification of the amino acid from R to A at position 100.
+The protein's natural variant, known as in allele DRB5*01:03;, features a modification of the amino acid from R to T at position 100.
+The protein's natural variant, known as in allele DRB5*01:12;, features a modification of the amino acid from A to E at position 103.
+The protein's natural variant, known as in allele DRB5*01:04; requires 2 nucleotide substitutions, features a modification of the amino acid from A to L at position 103.
+The protein's natural variant, known as in allele DRB5*01:12; requires 2 nucleotide substitutions, features a modification of the amino acid from Y to V at position 107.
+The protein's natural variant, known as in allele DRB5*01:06, allele DRB5*02:02, allele DRB5*02:04 and allele DRB5*02:05;, features a modification of the amino acid from V to A at position 114.
+The protein's natural variant, known as in allele DRB5*01:06, allele DRB5*02:02, allele DRB5*02:04 and allele DRB5*02:05;, features a modification of the amino acid from G to V at position 115.
+The protein's natural variant, known as in allele DRB5*02:02;, features a modification of the amino acid from S to G at position 164.
+The protein's natural variant, known as in allele DRB5*02:02;, features a modification of the amino acid from T to I at position 186.
+The protein's natural variant, known as in allele DRB5*02:02;, features a modification of the amino acid from V to I at position 232.
+The protein's natural variant, known as in Hong Kong; does not predispose to clinical thrombosis;, features a modification of the amino acid from R to G at position 334.
+The protein's natural variant, known as in THPH2; Cambridge;, features a modification of the amino acid from R to T at position 334.
+The protein's natural variant, known as in THPH2; Liverpool; mutant protein is expressed with an additional carbohydrate chain;, features a modification of the amino acid from I to T at position 387.
+The protein's natural variant, known as in THPH2; factor VLeiden; associated with susceptibility to Budd-Chiari syndrome; associated with susceptibility to ischemic stroke;, features a modification of the amino acid from R to Q at position 534.
+The protein's natural variant, known as in THPH2; Nijkerk;, features a modification of the amino acid from C to R at position 613.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from S to A at position 775.
+The protein's natural variant, known as in FA5D; Seoul 2;, features a modification of the amino acid from Y to C at position 1730.
+The protein's natural variant, known as in FA5D; impairs both factor V secretion and activity;, features a modification of the amino acid from R to C at position 2102.
+The protein's natural variant, known as in THPH2, features a modification of the amino acid from R to H at position 2102.
+The protein's natural variant, known as in strain: SPCR9; spectinomycin resistant. Not a ram mutation, features a modification of the amino acid from R to L at position 20.
+The protein's natural variant, known as in strain: SPCR7; spectinomycin resistant. Not a ram mutation, features a modification of the amino acid from V to E at position 21.
+The protein's natural variant, known as in strain: SPCR13 and SPCR15; spectinomycin resistant. Not a ram mutation, features a modification of the amino acid from S to P at position 22.
+The protein's natural variant, known as in strain: N-660; suppresses S12 streptomycin dependence, features a modification of the amino acid from G to R at position 104.
+The protein's natural variant, known as in strain: NEA-314; neamycin resistant, features a modification of the amino acid from R to G at position 112.
+The protein's natural variant, known as in strain: N-421 and D-1023; suppresses S12 streptomycin-dependence, features a modification of the amino acid from R to L at position 112.
+The protein's natural variant, known as in strain: NEA-319; neamycin resistant, features a modification of the amino acid from R to S at position 112.
+The protein's natural variant, known as in strain: B, features a modification of the amino acid from E to S at position 151.
+The protein's natural variant, known as in strain: 0-1; suppresses an alanyl-tRNA synthetase mutation. Blocks ribosome assembly below 25 degrees Celsius, features a modification of the amino acid from EEILGK to G at position 167.
+The protein's natural variant, known as in FADS4; no effect on localization to the nuclear pore complex; no effect on interaction with NUP214 and NUP62;, features a modification of the amino acid from D to Y at position 434.
+The protein's natural variant, known as in LICS; creates novel endoproteolytic cleavage sites compared to wild-type; loss of interaction with NSMCE4; loss of interaction with NSMCE1;, features a modification of the amino acid from P to L at position 209.
+The protein's natural variant, known as in LICS; no loss of protein stability; loss of interaction with NSMCE4; decreased interaction with NSMCE1; decreased association with the SMC5-SMC6 complex; decreased DNA repair;, features a modification of the amino acid from L to F at position 264.
+The protein's natural variant, known as in HPMRS6; may diminish protein expression and/or stability; decreases cell surface expression of GPI-anchored proteins, including CD55 and CD59, in skin fibroblasts from affected individual;, features a modification of the amino acid from L to P at position 46.
+The protein's natural variant, known as in a lung neuroendocrine carcinoma sample; somatic mutation; requires 2 nucleotide substitutions, features a modification of the amino acid from G to K at position 514.
+The protein's natural variant, known as in an ovarian mucinous carcinoma sample; somatic mutation, features a modification of the amino acid from T to I at position 852.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from K to M at position 418.
+The protein's natural variant, known as in a pancreatic ductal adenocarcinoma sample; somatic mutation, features a modification of the amino acid from R to L at position 193.
+The protein's natural variant, known as in strain: NZB, features a modification of the amino acid from G to E at position 102.
+The protein's natural variant, known as in RP95; unknown pathological significance, features a modification of the amino acid from S to P at position 49.
+The protein's natural variant, known as in RP95, features a modification of the amino acid from P to R at position 52.
+The protein's natural variant, known as in ARMD6; associated with disease susceptibility; increased transactivation and DNA-binding activity;, features a modification of the amino acid from R to Q at position 87.
+The protein's natural variant, known as in CORD11; unknown pathological significance; decreased interaction with CRX and transactivation activity;, features a modification of the amino acid from G to R at position 137.
+The protein's natural variant, known as in CORD11; unknown pathological significance; decreased interaction with CRX and increased transactivation activity, features a modification of the amino acid from P to PGP at position 140.
+The protein's natural variant, known as in FND1;, features a modification of the amino acid from L to V at position 168.
+The protein's natural variant, known as in FND1;, features a modification of the amino acid from R to W at position 183.
+The protein's natural variant, known as in FND1;, features a modification of the amino acid from R to W at position 196.
+The protein's natural variant, known as in FND1;, features a modification of the amino acid from N to S at position 203.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from S to G at position 437.
+The protein's natural variant, known as in minor component B', features a modification of the amino acid from D to E at position 32.
+The protein's natural variant, known as in minor component B', features a modification of the amino acid from H to Q at position 49.
+The protein's natural variant, known as in minor component B', features a modification of the amino acid from S to G at position 122.
+The protein's natural variant, known as in minor component B', features a modification of the amino acid from D to K at position 130.
+The protein's natural variant, known as in minor component B', features a modification of the amino acid from I to V at position 132.
+The protein's natural variant, known as in minor component B', features a modification of the amino acid from S to A at position 561.
+The protein's natural variant, known as found in a renal cell carcinoma sample; somatic mutation;, features a modification of the amino acid from Y to C at position 16.
+The protein's natural variant, known as acts as suppressor of deafness and is associated with normal hearing in individuals homozygous for a deafness-associated mutation in the GAB1 gene;, features a modification of the amino acid from R to Q at position 544.
+The protein's natural variant, known as in strain: cv. Cvi-0, features a modification of the amino acid from V to A at position 29.
+The protein's natural variant, known as in strain: cv. Co-1, features a modification of the amino acid from L to P at position 38.
+The protein's natural variant, known as in strain: cv. Lisse, features a modification of the amino acid from N to D at position 51.
+The protein's natural variant, known as in strain: cv. Co-1, features a modification of the amino acid from K to M at position 73.
+The protein's natural variant, known as in strain: cv. Kent, features a modification of the amino acid from S to P at position 75.
+The protein's natural variant, known as in strain: cv. Gr-3, features a modification of the amino acid from N to D at position 89.
+The protein's natural variant, known as in strain: cv. Lisse, features a modification of the amino acid from D to G at position 112.
+The protein's natural variant, known as in strain: cv. Gr-3, features a modification of the amino acid from E to G at position 125.
+The protein's natural variant, known as in strain: cv. Corsacalla-1, features a modification of the amino acid from M to I at position 140.
+The protein's natural variant, known as in strain: cv. Kent, features a modification of the amino acid from I to V at position 142.
+The protein's natural variant, known as in strain: cv. Kent, features a modification of the amino acid from L to I at position 160.
+The protein's natural variant, known as in strain: cv. Cvi-0, features a modification of the amino acid from M to T at position 203.
+The protein's natural variant, known as in PHA1B2;, features a modification of the amino acid from G to S at position 37.
+The protein's natural variant, known as in BESC1;, features a modification of the amino acid from S to C at position 82.
+The protein's natural variant, known as in BESC1; decreased channel activity;, features a modification of the amino acid from P to L at position 267.
+The protein's natural variant, known as in BESC1;, features a modification of the amino acid from N to S at position 288.
+The protein's natural variant, known as in BESC1; increased channel activity;, features a modification of the amino acid from G to S at position 294.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from A to V at position 311.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from A to V at position 314.
+The natural variant of this protein is characterized by an amino acid alteration from A to P at position 336.
+The protein's natural variant, known as in BESC1;, features a modification of the amino acid from V to M at position 348.
+The protein's natural variant, known as in BESC1;, features a modification of the amino acid from P to T at position 369.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from L to V at position 387.
+The protein's natural variant, known as in BESC1; decreased channel activity;, features a modification of the amino acid from E to K at position 539.
+The protein's natural variant, known as associated with hypertension in South African Black;, features a modification of the amino acid from R to Q at position 563.
+The protein's natural variant, known as in LIDLS1;, features a modification of the amino acid from P to L at position 616.
+The protein's natural variant, known as in LIDLS1, features a modification of the amino acid from P to S at position 616.
+The protein's natural variant, known as in LIDLS1;, features a modification of the amino acid from P to S at position 617.
+The protein's natural variant, known as in LIDLS1;, features a modification of the amino acid from P to R at position 618.
+The protein's natural variant, known as in LIDLS1; constitutive channel activation;, features a modification of the amino acid from Y to H at position 620.
+The natural variant of this protein is characterized by an amino acid alteration from E to G at position 632.
+The protein's natural variant, known as in 33% of the molecules, features a modification of the amino acid from V to L at position 2.
+The protein's natural variant, known as in strain: LM0230, features a modification of the amino acid from A to S at position 103.
+The protein's natural variant, known as in strain: LM0230, features a modification of the amino acid from A to G at position 223.
+The protein's natural variant, known as in strain: LM0230, features a modification of the amino acid from E to D at position 537.
+The protein's natural variant, known as in strain: LM0230, features a modification of the amino acid from GQ to SE at position 585.
+The protein's natural variant, known as in strain: LM0230, features a modification of the amino acid from A to G at position 592.
+The protein's natural variant, known as in strain: LM0230, features a modification of the amino acid from D to A at position 596.
+The natural variant of this protein is characterized by an amino acid alteration from HAL to YAF at position 50.
+The natural variant of this protein is characterized by an amino acid alteration from R to G at position 61.
+The natural variant of this protein is characterized by an amino acid alteration from A to V at position 128.
+The natural variant of this protein is characterized by an amino acid alteration from R to H at position 312.
+The protein's natural variant, known as in a lung small cell carcinoma sample; somatic mutation, features a modification of the amino acid from G to A at position 47.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation, features a modification of the amino acid from L to F at position 750.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation, features a modification of the amino acid from L to I at position 762.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation, features a modification of the amino acid from E to D at position 794.
+The protein's natural variant, known as in a glioblastoma multiforme sample; somatic mutation;, features a modification of the amino acid from H to Y at position 1549.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation, features a modification of the amino acid from H to Q at position 1824.
+The protein's natural variant, known as in DEE84, features a modification of the amino acid from Y to C at position 14.
+The protein's natural variant, known as in DEE84; unknown pathological significance, features a modification of the amino acid from A to T at position 24.
+The protein's natural variant, known as in DEE84; unknown pathological significance, features a modification of the amino acid from I to T at position 42.
+The protein's natural variant, known as in DEE84; severely decreased protein stability; decreased hexamer formation; severe decrease of UDP-glucose 6-dehydrogenase activity;, features a modification of the amino acid from A to V at position 44.
+The protein's natural variant, known as in DEE84, features a modification of the amino acid from S to A at position 72.
+The protein's natural variant, known as in DEE84; decreased function in glycosaminoglycan biosynthetic process in patient cells; severely decreased protein stability; decreased hexamer formation; severe decrease of UDP-glucose 6-dehydrogenase activity, features a modification of the amino acid from A to T at position 82.
+The protein's natural variant, known as in DEE84; unknown pathological significance, features a modification of the amino acid from I to T at position 116.
+The protein's natural variant, known as in DEE84; unknown pathological significance;, features a modification of the amino acid from P to A at position 175.
+The protein's natural variant, known as in DEE84; unknown pathological significance, features a modification of the amino acid from E to D at position 217.
+The protein's natural variant, known as in DEE84; unknown pathological significance;, features a modification of the amino acid from I to T at position 255.
+The protein's natural variant, known as in DEE84; unknown pathological significance, features a modification of the amino acid from G to R at position 271.
+The protein's natural variant, known as in DEE84; unknown pathological significance; may affect splicing, features a modification of the amino acid from V to I at position 303.
+The protein's natural variant, known as in DEE84; unknown pathological significance, features a modification of the amino acid from M to V at position 306.
+The protein's natural variant, known as in DEE84; unknown pathological significance;, features a modification of the amino acid from R to Q at position 317.
+The protein's natural variant, known as in DEE84, features a modification of the amino acid from Y to C at position 367.
+The protein's natural variant, known as in DEE84; unknown pathological significance;, features a modification of the amino acid from R to W at position 393.
+The protein's natural variant, known as in DEE84; unknown pathological significance;, features a modification of the amino acid from A to S at position 410.
+The protein's natural variant, known as in DEE84; unknown pathological significance;, features a modification of the amino acid from R to W at position 442.
+The protein's natural variant, known as in DEE84; unknown pathological significance, features a modification of the amino acid from R to H at position 443.
+The protein's natural variant, known as in DEE84; unknown pathological significance, features a modification of the amino acid from H to R at position 449.
+The protein's natural variant, known as in DTDP2; the mutant protein does not translocate into the endoplasmic reticulum;, features a modification of the amino acid from Y to D at position 6.
+The protein's natural variant, known as in DGI2; dominant negative mutation; results in signal peptide retention; the mutant protein is retained within the rough ER membrane;, features a modification of the amino acid from A to V at position 15.
+The protein's natural variant, known as in DGI3; the mutant protein is largely retained in the ER, features a modification of the amino acid from P to L at position 17.
+The protein's natural variant, known as in DGI2 and DGI3; dominant negative mutation; the mutant protein is retained intracellularly;, features a modification of the amino acid from P to S at position 17.
+The protein's natural variant, known as in DFNA39/DGI1; dominant negative mutation; the mutant protein is retained intracellularly;, features a modification of the amino acid from P to T at position 17.
+The protein's natural variant, known as in DGI2; dominant negative mutation; the mutant protein is retained intracellularly, features a modification of the amino acid from V to D at position 18.
+The protein's natural variant, known as in DFNA39/DGI1 and DGI3;, features a modification of the amino acid from V to F at position 18.
+The protein's natural variant, known as in DGI2;, features a modification of the amino acid from R to W at position 68.
+The protein's natural variant, known as in MMDS3; loss of stability and consequently decrease in various mitochondrial 4Fe-4S proteins and in proteins covalently linked to lipoic acid;, features a modification of the amino acid from Q to P at position 314.
+The protein's natural variant, known as exist in both chains, features a modification of the amino acid from Y to F at position 25.
+The protein's natural variant, known as in fast chain, features a modification of the amino acid from K to Q at position 61.
+The protein's natural variant, known as in 3KTD; decreased acetyl-CoAC-acyltransferase activity; less than 10% of the degradative/thiolase activity;, features a modification of the amino acid from N to S at position 93.
+The protein's natural variant, known as in 3KTD;, features a modification of the amino acid from G to A at position 152.
+The protein's natural variant, known as in 3KTD; loss of acetyl-CoAC-acyltransferase activity; no degradative/thiolase activity;, features a modification of the amino acid from N to D at position 158.
+The protein's natural variant, known as in 3KTD; no activity;, features a modification of the amino acid from G to R at position 183.
+The protein's natural variant, known as in 3KTD; decreased protein abundance; decreased acetyl-CoAC-acyltransferase activity; less than 10% of the degradative/thiolase activity;, features a modification of the amino acid from T to M at position 297.
+The protein's natural variant, known as in 3KTD; loss of acetyl-CoAC-acyltransferase activity; no degradative/thiolase activity;, features a modification of the amino acid from A to P at position 301.
+The protein's natural variant, known as in 3KTD; decreased protein stability; decreased acetyl-CoAC-acyltransferase activity; less than 10% of the degradative/thiolase activity;, features a modification of the amino acid from I to T at position 312.
+The protein's natural variant, known as in 3KTD; loss of protein solubility; loss of acetyl-CoAC-acyltransferase activity; no degradative/thiolase activity;, features a modification of the amino acid from A to P at position 333.
+The protein's natural variant, known as in 3KTD;, features a modification of the amino acid from G to V at position 379.
+The protein's natural variant, known as in 3KTD; decreased protein stability;, features a modification of the amino acid from A to T at position 380.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from S to G at position 345.
+The protein's natural variant, known as in RP4, features a modification of the amino acid from T to K at position 4.
+The protein's natural variant, known as in RP4;, features a modification of the amino acid from N to S at position 15.
+The protein's natural variant, known as in RP4;, features a modification of the amino acid from T to M at position 17.
+The protein's natural variant, known as in RP4; most common variant; impairs protein folding; leads to interaction with EDEM1 followed by degradation by the ERAD system;, features a modification of the amino acid from P to H at position 23.
+The protein's natural variant, known as in RP4, features a modification of the amino acid from P to L at position 23.
+The protein's natural variant, known as in RP4, features a modification of the amino acid from Q to H at position 28.
+The protein's natural variant, known as in RP4, features a modification of the amino acid from L to R at position 40.
+The protein's natural variant, known as in RP4;, features a modification of the amino acid from M to T at position 44.
+The protein's natural variant, known as in RP4;, features a modification of the amino acid from F to L at position 45.
+The protein's natural variant, known as in RP4;, features a modification of the amino acid from L to R at position 46.
+The protein's natural variant, known as in RP4;, features a modification of the amino acid from G to R at position 51.
+The protein's natural variant, known as in RP4, features a modification of the amino acid from G to V at position 51.
+The protein's natural variant, known as in RP4;, features a modification of the amino acid from P to R at position 53.
+The protein's natural variant, known as in RP4;, features a modification of the amino acid from T to R at position 58.
+The protein's natural variant, known as in RP4;, features a modification of the amino acid from V to D at position 87.
+The protein's natural variant, known as in RP4;, features a modification of the amino acid from G to D at position 89.
+The protein's natural variant, known as in CSNBAD1; constitutive activity in the absence of bound retinal;, features a modification of the amino acid from G to D at position 90.
+The protein's natural variant, known as in CSNBAD1;, features a modification of the amino acid from T to I at position 94.
+The protein's natural variant, known as found in patients with pathologic myopia; unknown pathological significance;, features a modification of the amino acid from V to I at position 104.
+The protein's natural variant, known as in RP4;, features a modification of the amino acid from G to R at position 106.
+The protein's natural variant, known as in RP4;, features a modification of the amino acid from G to W at position 106.
+The protein's natural variant, known as in RP4;, features a modification of the amino acid from G to R at position 109.
+The protein's natural variant, known as in RP4, features a modification of the amino acid from C to F at position 110.
+The protein's natural variant, known as in RP4;, features a modification of the amino acid from C to Y at position 110.
+The protein's natural variant, known as in RP4;, features a modification of the amino acid from G to D at position 114.
+The protein's natural variant, known as in RP4, features a modification of the amino acid from L to R at position 125.
+The protein's natural variant, known as in RP4, features a modification of the amino acid from S to F at position 127.
+The protein's natural variant, known as in RP4;, features a modification of the amino acid from L to P at position 131.
+The protein's natural variant, known as in RP4, features a modification of the amino acid from R to G at position 135.
+The protein's natural variant, known as in RP4;, features a modification of the amino acid from R to L at position 135.
+The protein's natural variant, known as in RP4;, features a modification of the amino acid from R to W at position 135.
+The protein's natural variant, known as in RP4, features a modification of the amino acid from C to S at position 140.
+The protein's natural variant, known as in RP4; autosomal recessive;, features a modification of the amino acid from E to K at position 150.
+The protein's natural variant, known as in RP4;, features a modification of the amino acid from A to E at position 164.
+The protein's natural variant, known as in RP4;, features a modification of the amino acid from A to V at position 164.
+The protein's natural variant, known as in RP4, features a modification of the amino acid from C to R at position 167.
+The protein's natural variant, known as in RP4;, features a modification of the amino acid from P to L at position 171.
+The protein's natural variant, known as in RP4, features a modification of the amino acid from P to Q at position 171.
+The protein's natural variant, known as in RP4;, features a modification of the amino acid from P to S at position 171.
+The protein's natural variant, known as in RP4;, features a modification of the amino acid from Y to C at position 178.
+The protein's natural variant, known as in RP4, features a modification of the amino acid from Y to N at position 178.
+The protein's natural variant, known as in RP4, features a modification of the amino acid from P to S at position 180.
+The protein's natural variant, known as in RP4;, features a modification of the amino acid from E to K at position 181.
+The protein's natural variant, known as in RP4;, features a modification of the amino acid from G to S at position 182.
+The protein's natural variant, known as in RP4, features a modification of the amino acid from S to P at position 186.
+The protein's natural variant, known as in RP4;, features a modification of the amino acid from G to E at position 188.
+The protein's natural variant, known as in RP4;, features a modification of the amino acid from G to R at position 188.
+The protein's natural variant, known as in RP4;, features a modification of the amino acid from D to G at position 190.
+The protein's natural variant, known as in RP4;, features a modification of the amino acid from D to N at position 190.
+The protein's natural variant, known as in RP4;, features a modification of the amino acid from D to Y at position 190.
+The protein's natural variant, known as in RP4;, features a modification of the amino acid from M to R at position 207.
+The protein's natural variant, known as found in a patient with retinitis pigmentosa; unknown pathological significance;, features a modification of the amino acid from V to M at position 209.
+The protein's natural variant, known as in RP4;, features a modification of the amino acid from H to P at position 211.
+The protein's natural variant, known as in RP4, features a modification of the amino acid from H to R at position 211.
+The protein's natural variant, known as in RP4, features a modification of the amino acid from I to N at position 214.
+The protein's natural variant, known as in RP4, features a modification of the amino acid from M to K at position 216.
+The protein's natural variant, known as in RP4;, features a modification of the amino acid from F to C at position 220.
+The protein's natural variant, known as in RP4, features a modification of the amino acid from C to R at position 222.
+The protein's natural variant, known as in RP4;, features a modification of the amino acid from P to L at position 267.
+The protein's natural variant, known as in RP4, features a modification of the amino acid from P to R at position 267.
+The protein's natural variant, known as in CSNBAD1;, features a modification of the amino acid from A to E at position 292.
+The protein's natural variant, known as in RP4;, features a modification of the amino acid from K to E at position 296.
+The protein's natural variant, known as in RP4;, features a modification of the amino acid from S to R at position 297.
+The protein's natural variant, known as in RP4;, features a modification of the amino acid from T to M at position 342.
+The protein's natural variant, known as in RP4;, features a modification of the amino acid from V to L at position 345.
+The protein's natural variant, known as in RP4;, features a modification of the amino acid from V to M at position 345.
+The protein's natural variant, known as in RP4, features a modification of the amino acid from P to A at position 347.
+The protein's natural variant, known as in RP4; common variant;, features a modification of the amino acid from P to L at position 347.
+The protein's natural variant, known as in RP4;, features a modification of the amino acid from P to Q at position 347.
+The protein's natural variant, known as in RP4;, features a modification of the amino acid from P to R at position 347.
+The protein's natural variant, known as in RP4;, features a modification of the amino acid from P to S at position 347.
+The protein's natural variant, known as in strain: Isolate Egran655, features a modification of the amino acid from V to I at position 189.
+The protein's natural variant, known as in strain: Isolate Egran655, features a modification of the amino acid from A to V at position 193.
+The protein's natural variant, known as in strain: Isolate Egran655, features a modification of the amino acid from V to L at position 334.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from S to C at position 60.
+The protein's natural variant, known as in strain: Huiyang bearded, features a modification of the amino acid from G to R at position 35.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation, features a modification of the amino acid from G to E at position 155.
+The protein's natural variant, known as in 18% of the CIII, features a modification of the amino acid from V to I at position 11.
+The protein's natural variant, known as in 18% of the CIII, features a modification of the amino acid from V to P at position 11.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from P to Q at position 1086.
+The protein's natural variant, known as in strain: ZBMEL229, features a modification of the amino acid from V to L at position 228.
+The protein's natural variant, known as in strain: ZBMEL131, ZBMEL157, ZBMEL186 and ZBMEL191, features a modification of the amino acid from V to I at position 266.
+The protein's natural variant, known as in strain: ZBMEL131, ZBMEL186, ZBMEL229, ZBMEL377 and ZBMEL398, features a modification of the amino acid from N to S at position 296.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from A to P at position 32.
+The protein's natural variant, known as in PCH7;, features a modification of the amino acid from R to S at position 73.
+The protein's natural variant, known as in PCH7; reduced protein levels; decreased function in snRNA 3'-end processing;, features a modification of the amino acid from A to T at position 103.
+The protein's natural variant, known as in PCH7; reduced protein levels; decreased function in snRNA 3'-end processing;, features a modification of the amino acid from F to Y at position 148.
+The protein's natural variant, known as in PCH7; reduced protein levels;, features a modification of the amino acid from V to G at position 173.
+The protein's natural variant, known as in PCH7; reduced protein levels; decreased function in snRNA 3'-end processing;, features a modification of the amino acid from E to K at position 220.
+The protein's natural variant, known as in PCH7;, features a modification of the amino acid from F to S at position 239.
+The protein's natural variant, known as in PCH7;, features a modification of the amino acid from R to W at position 253.
+The protein's natural variant, known as in PCH7;, features a modification of the amino acid from H to Q at position 319.
+The protein's natural variant, known as in PCH7;, features a modification of the amino acid from H to Y at position 319.
+The protein's natural variant, known as in PCH7;, features a modification of the amino acid from S to F at position 496.
+The natural variant of this protein is characterized by an amino acid alteration from E to D at position 9.
+The protein's natural variant, known as in GAMOS10; slightly decreased formation of tRNA threonylcarbamoyladenosine modification, features a modification of the amino acid from A to V at position 84.
+The protein's natural variant, known as in GAMOS10; decreased formation of tRNA threonylcarbamoyladenosine modification, features a modification of the amino acid from I to T at position 221.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 520.
+The natural variant of this protein is characterized by an amino acid alteration from K to E at position 771.
+The protein's natural variant, known as in toxin 9BB, features a modification of the amino acid from K to R at position 37.
+The protein's natural variant, known as in DA2B2;, features a modification of the amino acid from R to C at position 74.
+The protein's natural variant, known as in DA2B2;, features a modification of the amino acid from R to H at position 74.
+The protein's natural variant, known as in CMT2B; increases GTP hydrolysis; decreases affinity for GTP and GDP; does not affect interaction with NTRK1; results in higher levels of NTRK1 and MAPK1/MAPK3 phosphorylation after NGF stimulation consistent with enhanced MAPK signaling; increases interaction with PRPH;, features a modification of the amino acid from L to F at position 129.
+The protein's natural variant, known as in CMT2B; does not affect interaction with NTRK1; results in higher levels of NTRK1 and MAPK1/MAPK3 phosphorylation after NGF stimulation consistent with enhanced MAPK signaling; increases interaction with PRPH;, features a modification of the amino acid from K to N at position 157.
+The protein's natural variant, known as in CMT2B; does not affect interaction with NTRK1; results in higher levels of NTRK1 and MAPK1/MAPK3 phosphorylation after NGF stimulation consistent with enhanced MAPK signaling; increases interaction with PRPH;, features a modification of the amino acid from N to T at position 161.
+The protein's natural variant, known as in CMT2B; increases GTP hydrolysis; decreases affinity for GTP and GDP; does not affect interaction with NTRK1; results in higher levels of NTRK1 and MAPK1/MAPK3 phosphorylation after NGF stimulation consistent with enhanced MAPK signaling; increases interaction with PRPH;, features a modification of the amino acid from V to M at position 162.
+The protein's natural variant, known as in BANDDOS; impairs phosphorylation of JNK kinases upon stimulation with CSF1;, features a modification of the amino acid from P to L at position 132.
+The protein's natural variant, known as in HDLS1, features a modification of the amino acid from GKTLGAGAFGKVVEATAFGLGKEDAVLKVAVKMLK to A at position 619.
+The protein's natural variant, known as in HDLS1;, features a modification of the amino acid from G to E at position 589.
+The protein's natural variant, known as in HDLS1; impairs autophosphorylation upon stimulation with CSF1;, features a modification of the amino acid from E to K at position 633.
+The protein's natural variant, known as in BANDDOS;, features a modification of the amino acid from H to Q at position 643.
+The protein's natural variant, known as in HDLS1;, features a modification of the amino acid from C to R at position 653.
+The protein's natural variant, known as in a lung squamous cell carcinoma sample; somatic mutation, features a modification of the amino acid from P to H at position 693.
+The protein's natural variant, known as in HDLS1; impairs autophosphorylation upon stimulation with CSF1;, features a modification of the amino acid from G to D at position 765.
+The protein's natural variant, known as in HDLS1; impairs autophosphorylation upon stimulation with CSF1;, features a modification of the amino acid from M to T at position 766.
+The protein's natural variant, known as in HDLS1;, features a modification of the amino acid from A to P at position 770.
+The protein's natural variant, known as in HDLS1; impairs autophosphorylation upon stimulation with CSF1;, features a modification of the amino acid from I to N at position 775.
+The protein's natural variant, known as in HDLS1; impairs autophosphorylation upon stimulation with CSF1;, features a modification of the amino acid from A to E at position 781.
+The protein's natural variant, known as in HDLS1; impairs autophosphorylation upon stimulation with CSF1;, features a modification of the amino acid from R to H at position 782.
+The protein's natural variant, known as in HDLS1; impairs autophosphorylation upon stimulation with CSF1;, features a modification of the amino acid from I to T at position 794.
+The protein's natural variant, known as in HDLS1; impairs autophosphorylation upon stimulation with CSF1, features a modification of the amino acid from P to S at position 824.
+The protein's natural variant, known as in HDLS1;, features a modification of the amino acid from D to Y at position 837.
+The protein's natural variant, known as in HDLS1;, features a modification of the amino acid from I to F at position 843.
+The protein's natural variant, known as in HDLS1;, features a modification of the amino acid from F to S at position 849.
+The protein's natural variant, known as in HDLS1;, features a modification of the amino acid from L to P at position 868.
+The protein's natural variant, known as in HDLS1; impairs autophosphorylation upon stimulation with CSF1;, features a modification of the amino acid from M to T at position 875.
+The protein's natural variant, known as in HDLS1;, features a modification of the amino acid from P to T at position 878.
+The protein's natural variant, known as in HDLS1;, features a modification of the amino acid from I to T at position 906.
+The protein's natural variant, known as in strain: 523-80, features a modification of the amino acid from A to V at position 194.
+The protein's natural variant, known as in FEB2; affects channel activity resulting in faster kinetics and increased current density at higher temperature compared to wild type, features a modification of the amino acid from S to L at position 126.
+The protein's natural variant, known as in EIG17; associated with disease susceptibility; gain-of-function variant; affects channel activity resulting in a depolarizing shift in activation and faster activation kinetics compared to controls, features a modification of the amino acid from V to M at position 246.
+The protein's natural variant, known as does not affect channel activity;, features a modification of the amino acid from E to K at position 280.
+The protein's natural variant, known as de novo variant found in a patient with childhood apraxia of speech; unknown pathological significance, features a modification of the amino acid from L to V at position 418.
+The protein's natural variant, known as in EIG17; associated with disease susceptibility; causes a large negative shift of the activation curve; homomeric mutant channels transfected into rat cortical neurons lower the threshold of action potential firing and strongly increase cell excitability when compared with wild-type channels, features a modification of the amino acid from E to K at position 515.
+The protein's natural variant, known as in EIG17; associated with disease susceptibility; gain-of-function variant; affects channel activity resulting in a depolarizing shift in activation and faster activation kinetics compared to controls, features a modification of the amino acid from S to W at position 632.
+The protein's natural variant, known as does not affect channel activity;, features a modification of the amino acid from A to T at position 705.
+The protein's natural variant, known as in EIG17; unknown pathological significance; does not affect channel activity;, features a modification of the amino acid from R to C at position 756.
+The protein's natural variant, known as in a breast infiltrating ductal carcinoma sample; somatic mutation, features a modification of the amino acid from N to K at position 123.
+The protein's natural variant, known as in a gastric adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from R to C at position 179.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation, features a modification of the amino acid from R to L at position 198.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation, features a modification of the amino acid from P to L at position 860.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to H at position 306.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from E to K at position 518.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from A to V at position 534.
+The protein's natural variant, known as in allele ALS4-2, features a modification of the amino acid from T to A at position 169.
+The protein's natural variant, known as in allele ALS4-2, features a modification of the amino acid from Y to F at position 484.
+The protein's natural variant, known as in allele ALS4-2, features a modification of the amino acid from Y to F at position 520.
+The protein's natural variant, known as in allele ALS4-2, features a modification of the amino acid from Y to F at position 592.
+The protein's natural variant, known as in allele ALS4-2, features a modification of the amino acid from F to Y at position 664.
+The protein's natural variant, known as in allele ALS4-2, features a modification of the amino acid from FATTTTV to YVTTSTI at position 742.
+The protein's natural variant, known as in allele ALS4-2, features a modification of the amino acid from S to T at position 751.
+The protein's natural variant, known as in allele ALS4-2, features a modification of the amino acid from P to Y at position 760.
+The protein's natural variant, known as in allele ALS4-2, features a modification of the amino acid from F to Y at position 772.
+The protein's natural variant, known as in allele ALS4-2, features a modification of the amino acid from G to A at position 852.
+The protein's natural variant, known as in allele ALS4-2, features a modification of the amino acid from N to S at position 867.
+The protein's natural variant, known as in allele ALS4-2, features a modification of the amino acid from S to A at position 888.
+The protein's natural variant, known as in allele ALS4-2, features a modification of the amino acid from F to Y at position 1168.
+The protein's natural variant, known as in allele ALS4-2, features a modification of the amino acid from T to S at position 1255.
+The protein's natural variant, known as in allele ALS4-2, features a modification of the amino acid from T to P at position 1789.
+The protein's natural variant, known as in allele ALS4-2, features a modification of the amino acid from K to E at position 1806.
+The protein's natural variant, known as in allele ALS4-2, features a modification of the amino acid from T to P at position 1837.
+The protein's natural variant, known as in allele ALS4-2, features a modification of the amino acid from T to P at position 1842.
+The protein's natural variant, known as in allele ALS4-2, features a modification of the amino acid from T to P at position 1844.
+The protein's natural variant, known as in allele ALS4-2, features a modification of the amino acid from V to A at position 1947.
+The protein's natural variant, known as in allele ALS4-2, features a modification of the amino acid from S to G at position 1969.
+The protein's natural variant, known as in allele ALS4-2, features a modification of the amino acid from G to R at position 1975.
+The protein's natural variant, known as in allele ALS4-2, features a modification of the amino acid from S to F at position 2016.
+The protein's natural variant, known as in allele ALS4-2, features a modification of the amino acid from I to T at position 2022.
+The protein's natural variant, known as in allele ALS4-2, features a modification of the amino acid from D to G at position 2046.
+The protein's natural variant, known as in allele ALS4-2, features a modification of the amino acid from I to T at position 2053.
+The protein's natural variant, known as in strain: 912, features a modification of the amino acid from D to E at position 129.
+The protein's natural variant, known as in brevinin-1Ec, features a modification of the amino acid from L to F at position 60.
+The protein's natural variant, known as in dfw; results in impaired long-term Ca2+ export at stereocilia, features a modification of the amino acid from G to S at position 283.
+The natural variant of this protein is characterized by an amino acid alteration from E to K at position 412.
+The protein's natural variant, known as in SAM, features a modification of the amino acid from P to Q at position 28.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from E to G at position 265.
+The protein's natural variant, known as in strain: Isolate AMNH 101520, features a modification of the amino acid from F to L at position 234.
+The protein's natural variant, known as in strain: Isolate AMNH 101520, features a modification of the amino acid from V to L at position 371.
+The natural variant of this protein is characterized by an amino acid alteration from F to S at position 21.
+The protein's natural variant, known as in MC5DM2 and CMHI;, features a modification of the amino acid from W to R at position 55.
+The protein's natural variant, known as found in a renal cell carcinoma case; somatic mutation, features a modification of the amino acid from P to S at position 329.
+The protein's natural variant, known as found in a renal cell carcinoma sample; somatic mutation, features a modification of the amino acid from L to P at position 136.
+The protein's natural variant, known as in OS1; associated with disease susceptibility; has diminished ability to antagonize Wnt signaling, in vitro;, features a modification of the amino acid from R to G at position 324.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from N to S at position 139.
+The protein's natural variant, known as in LCCS9; decreases the autoprocessing/cleavage of the receptor, features a modification of the amino acid from V to E at position 741.
+The protein's natural variant, known as in LCCS9;, features a modification of the amino acid from V to E at position 769.
+The protein's natural variant, known as found in patients with aggressive periodontitis; impairs cAMP production; abrogates osteoblastic differentiation;, features a modification of the amino acid from R to Q at position 1057.
+The protein's natural variant, known as in CSS5;, features a modification of the amino acid from Y to C at position 73.
+The protein's natural variant, known as in CSS5;, features a modification of the amino acid from Y to S at position 73.
+The protein's natural variant, known as in MNGMA; found in a case of childhood clear cell meningioma; associated with disease susceptibility, features a modification of the amino acid from EYNESMKA to GLHRFIVL at position 132.
+The protein's natural variant, known as in HHF1;, features a modification of the amino acid from G to R at position 7.
+The protein's natural variant, known as in HHF1;, features a modification of the amino acid from V to D at position 21.
+The protein's natural variant, known as in HHF1, features a modification of the amino acid from F to S at position 27.
+The protein's natural variant, known as in PNDM3;, features a modification of the amino acid from P to L at position 45.
+The protein's natural variant, known as in HHF1; altered intracellular trafficking, features a modification of the amino acid from G to E at position 70.
+The protein's natural variant, known as in PNDM3; mosaic;, features a modification of the amino acid from N to S at position 72.
+The protein's natural variant, known as in HHF1;, features a modification of the amino acid from R to Q at position 74.
+The protein's natural variant, known as in HHF1;, features a modification of the amino acid from R to W at position 74.
+The protein's natural variant, known as in PNDM3;, features a modification of the amino acid from V to A at position 86.
+The protein's natural variant, known as in PNDM3;, features a modification of the amino acid from V to G at position 86.
+The protein's natural variant, known as in HHF1; altered intracellular trafficking;, features a modification of the amino acid from G to R at position 111.
+The protein's natural variant, known as in HHF1;, features a modification of the amino acid from A to P at position 116.
+The protein's natural variant, known as in HHF1; mild;, features a modification of the amino acid from H to Q at position 125.
+The protein's natural variant, known as in PNDM3; with neurologic features; reduces the sensitivity of the K(ATP) channel to inhibition by MgATP; increases whole-cell K(ATP) current;, features a modification of the amino acid from F to L at position 132.
+The protein's natural variant, known as in PNDM3;, features a modification of the amino acid from F to V at position 132.
+The protein's natural variant, known as in HHF1; severe; high prevalence in Finland; loss of channel activity;, features a modification of the amino acid from V to D at position 187.
+The protein's natural variant, known as in HHF1; severe;, features a modification of the amino acid from N to S at position 188.
+The protein's natural variant, known as in PNDM3; reduced inhibition by ATP, features a modification of the amino acid from P to S at position 207.
+The protein's natural variant, known as in PNDM3, features a modification of the amino acid from E to K at position 208.
+The protein's natural variant, known as in PNDM3;, features a modification of the amino acid from D to E at position 209.
+The protein's natural variant, known as in PNDM3;, features a modification of the amino acid from Q to K at position 211.
+The protein's natural variant, known as in PNDM3;, features a modification of the amino acid from L to R at position 213.
+The protein's natural variant, known as in PNDM3;, features a modification of the amino acid from L to P at position 225.
+The protein's natural variant, known as in PNDM3; highly reduced inhibition by ATP when associated with L-1523;, features a modification of the amino acid from T to I at position 229.
+The protein's natural variant, known as in HHF1, features a modification of the amino acid from M to R at position 233.
+The protein's natural variant, known as in PNDM3;, features a modification of the amino acid from Y to D at position 263.
+The protein's natural variant, known as in HHF1;, features a modification of the amino acid from D to N at position 310.
+The protein's natural variant, known as in PNDM3;, features a modification of the amino acid from E to K at position 382.
+The protein's natural variant, known as in HHF1;, features a modification of the amino acid from N to D at position 406.
+The protein's natural variant, known as in HHF1;, features a modification of the amino acid from C to R at position 418.
+The protein's natural variant, known as in TNDM2, features a modification of the amino acid from C to R at position 435.
+The protein's natural variant, known as in HHF1;, features a modification of the amino acid from R to Q at position 495.
+The protein's natural variant, known as in HHF1;, features a modification of the amino acid from E to K at position 501.
+The protein's natural variant, known as in HHF1;, features a modification of the amino acid from L to P at position 503.
+The protein's natural variant, known as in HHF1;, features a modification of the amino acid from L to P at position 508.
+The protein's natural variant, known as in HHF1; no effect on cell membrane expression; no effect on traffic efficiency; dramatically reduced potassium channel response to activators such as MgADP or to diazoxide, features a modification of the amino acid from L to M at position 511.
+The protein's natural variant, known as in HHF1, features a modification of the amino acid from P to R at position 551.
+The protein's natural variant, known as in TNDM2;, features a modification of the amino acid from L to V at position 582.
+The protein's natural variant, known as in HHF1;, features a modification of the amino acid from F to L at position 591.
+The protein's natural variant, known as in HHF1;, features a modification of the amino acid from R to C at position 620.
+The protein's natural variant, known as in HHF1, features a modification of the amino acid from F to S at position 686.
+The protein's natural variant, known as in HHF1;, features a modification of the amino acid from G to D at position 716.
+The protein's natural variant, known as in HHF1;, features a modification of the amino acid from G to V at position 716.
+The protein's natural variant, known as in HHF1, features a modification of the amino acid from K to T at position 719.
+The protein's natural variant, known as in HHF1; no effect on cell membrane expression; no effect on traffic efficiency; dramatically reduced potassium channel response to activators such as MgADP or to diazoxide, features a modification of the amino acid from E to K at position 824.
+The protein's natural variant, known as in HHF1, features a modification of the amino acid from R to G at position 841.
+The protein's natural variant, known as in HHF1; no effect on cell membrane expression; no effect on traffic efficiency; reduced potassium channel response to activators such as MgADP or to diazoxide;, features a modification of the amino acid from K to T at position 889.
+The protein's natural variant, known as in HHF1; no effect on cell membrane expression; no effect on traffic efficiency; dramatically reduced potassium channel response to activators such as MgADP or to diazoxide, features a modification of the amino acid from L to P at position 890.
+The protein's natural variant, known as in HHF1;, features a modification of the amino acid from S to F at position 956.
+The protein's natural variant, known as in TNDM2; overactive channel, features a modification of the amino acid from H to Y at position 1023.
+The protein's natural variant, known as in HHF1, features a modification of the amino acid from T to P at position 1130.
+The protein's natural variant, known as in HHF1;, features a modification of the amino acid from T to M at position 1138.
+The protein's natural variant, known as in HHF1;, features a modification of the amino acid from L to R at position 1147.
+The protein's natural variant, known as in TNDM2;, features a modification of the amino acid from R to Q at position 1182.
+The protein's natural variant, known as in PNDM3; slightly reduced inhibition by ATP;, features a modification of the amino acid from A to E at position 1184.
+The protein's natural variant, known as in HHF1; severe;, features a modification of the amino acid from R to Q at position 1214.
+The protein's natural variant, known as in HHF1;, features a modification of the amino acid from R to W at position 1214.
+The protein's natural variant, known as in HHF1;, features a modification of the amino acid from N to K at position 1295.
+The protein's natural variant, known as in PNDM3;, features a modification of the amino acid from E to K at position 1326.
+The protein's natural variant, known as in HHF1;, features a modification of the amino acid from K to N at position 1336.
+The protein's natural variant, known as in HHF1; altered intracellular trafficking, features a modification of the amino acid from G to E at position 1342.
+The protein's natural variant, known as in HHF1, features a modification of the amino acid from L to Q at position 1349.
+The protein's natural variant, known as in LIH; partially impairs ATP-dependent potassium channel function;, features a modification of the amino acid from R to H at position 1352.
+The protein's natural variant, known as in HHF1;, features a modification of the amino acid from R to P at position 1352.
+The natural variant of this protein is characterized by an amino acid alteration from V to G at position 1360.
+The protein's natural variant, known as in HHF1;, features a modification of the amino acid from V to M at position 1360.
+The protein's natural variant, known as in HHF1;, features a modification of the amino acid from G to R at position 1378.
+The protein's natural variant, known as in HHF1; highly decreases cell membrane expression; highly reduced traffic efficiency; dramatically reduced potassium channel response to activators such as MgADP or to diazoxide;, features a modification of the amino acid from G to S at position 1378.
+The protein's natural variant, known as in TNDM2;, features a modification of the amino acid from R to C at position 1379.
+The protein's natural variant, known as in HHF1;, features a modification of the amino acid from G to S at position 1381.
+The protein's natural variant, known as in HHF1, features a modification of the amino acid from K to Q at position 1384.
+The protein's natural variant, known as in HHF1;, features a modification of the amino acid from S to F at position 1386.
+The protein's natural variant, known as in HHF1, features a modification of the amino acid from S to Y at position 1388.
+The protein's natural variant, known as in HHF1, features a modification of the amino acid from L to P at position 1389.
+The protein's natural variant, known as in HHF1; severe; loss of channel activity;, features a modification of the amino acid from R to H at position 1393.
+The protein's natural variant, known as in HHF1 and PNDM3;, features a modification of the amino acid from G to R at position 1400.
+The protein's natural variant, known as in HHF1; altered intracellular trafficking;, features a modification of the amino acid from R to H at position 1418.
+The protein's natural variant, known as in HHF1; modest impairment of channel function;, features a modification of the amino acid from R to C at position 1420.
+The protein's natural variant, known as in PNDM3; overactive channel;, features a modification of the amino acid from I to V at position 1424.
+The protein's natural variant, known as in HHF1; cannot form a functional channel, due to protein instability or defective transport to the membrane;, features a modification of the amino acid from R to Q at position 1436.
+The protein's natural variant, known as in HHF1;, features a modification of the amino acid from L to P at position 1450.
+The protein's natural variant, known as in HHF1;, features a modification of the amino acid from A to T at position 1457.
+The protein's natural variant, known as in HHF1, features a modification of the amino acid from A to V at position 1457.
+The protein's natural variant, known as in HHF1, features a modification of the amino acid from D to H at position 1471.
+The protein's natural variant, known as in HHF1;, features a modification of the amino acid from D to N at position 1471.
+The protein's natural variant, known as in HHF1; channels insensitive to metabolic inhibition and to activation by ADP;, features a modification of the amino acid from G to R at position 1478.
+The protein's natural variant, known as in HHF1; no effect on cell membrane expression; no effect on traffic efficiency; dramatically reduced potassium channel response to activators such as MgADP or to diazoxide, features a modification of the amino acid from N to I at position 1480.
+The protein's natural variant, known as in HHF1, features a modification of the amino acid from R to K at position 1486.
+The protein's natural variant, known as in HHF1;, features a modification of the amino acid from R to Q at position 1493.
+The protein's natural variant, known as in HHF1; altered intracellular trafficking;, features a modification of the amino acid from R to W at position 1493.
+The protein's natural variant, known as in HHF1; no effect on cell membrane expression; no effect on traffic efficiency; dramatically reduced potassium channel response to activators such as MgADP or to diazoxide, features a modification of the amino acid from D to E at position 1505.
+The protein's natural variant, known as in HHF1; mild; dominantly inherited; channels insensitive to metabolic inhibition and to activation by ADP;, features a modification of the amino acid from E to K at position 1506.
+The protein's natural variant, known as in HHF1, features a modification of the amino acid from A to AAS at position 1507.
+The protein's natural variant, known as in HHF1; no effect on cell membrane expression; no effect on traffic efficiency; dramatically reduced potassium channel response to activators such as MgADP or to diazoxide, features a modification of the amino acid from I to S at position 1511.
+The protein's natural variant, known as in PNDM3; highly reduced inhibition by ATP when associated with I-229, features a modification of the amino acid from V to L at position 1522.
+The protein's natural variant, known as in HHF1; reduced channels surface expression and response to ADP;, features a modification of the amino acid from L to P at position 1543.
+The protein's natural variant, known as in HHF1;, features a modification of the amino acid from V to D at position 1550.
+The protein's natural variant, known as in HHF1;, features a modification of the amino acid from L to V at position 1551.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from T to A at position 108.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from S to C at position 585.
+The protein's natural variant, known as in a patient with amyotrophic lateral sclerosis;, features a modification of the amino acid from E to V at position 954.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from S to F at position 514.
+The protein's natural variant, known as in toxin CM-8A, features a modification of the amino acid from Y to H at position 4.
+The natural variant of this protein is characterized by an amino acid alteration from Q to H at position 20.
+The natural variant of this protein is characterized by an amino acid alteration from M to T at position 218.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from K to R at position 249.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from T to A at position 276.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from K to R at position 285.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from E to G at position 286.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from K to N at position 273.
+The protein's natural variant, known as in FEPS3;, features a modification of the amino acid from R to H at position 222.
+The protein's natural variant, known as in FEPS3, features a modification of the amino acid from R to S at position 222.
+The protein's natural variant, known as in FEPS3;, features a modification of the amino acid from R to C at position 225.
+The protein's natural variant, known as in FEPS3; causes hyperexcitability of dorsal root ganglion neurons; depolarizes resting membrane potential; enhances spontaneous firing; hyperpolarizes channel activation; slows deactivation; decreases rates of current decay; does not change slow-inactivation;, features a modification of the amino acid from I to T at position 381.
+The natural variant of this protein is characterized by an amino acid alteration from A to D at position 681.
+The protein's natural variant, known as in FEPS3; causes hyperexcitability of dorsal root ganglion neurons; hyperpolarizes channel activation; slows deactivation; depolarizes steady-state fast-inactivation;, features a modification of the amino acid from G to R at position 699.
+The protein's natural variant, known as in FEPS3;, features a modification of the amino acid from A to G at position 808.
+The protein's natural variant, known as in HSAN7; results in excessive channel activity at resting voltages; causes sustained depolarization of nociceptors and impaired generation of action potentials; causes aberrant synaptic transmission; causes transient hyperexcitability of dorsal root ganglion neurons;, features a modification of the amino acid from L to P at position 811.
+The protein's natural variant, known as in FEPS3; slows deactivation; depolarizes resting membrane potential; enhances spontaneous firing; decreases rates of current decay; does not change fast-inactivation; does not change slow-inactivation;, features a modification of the amino acid from L to P at position 1158.
+The protein's natural variant, known as in HSAN7; cold-aggravated peripheral pain seen in some patients; enhances the channel activity by shifting the voltage dependence of channel opening to hyperpolarized potentials thereby giving rise to hyperexcitability of nociceptors; causes hyperexcitability and reduced cold-sensitivity of dorsal root ganglion neurons, features a modification of the amino acid from V to A at position 1184.
+The protein's natural variant, known as in allele LP; loss of neuronal function and disruption of interactions between the SH3 and guanylate kinase-like domains, features a modification of the amino acid from L to P at position 1642.
+The protein's natural variant, known as in MTDPS15;, features a modification of the amino acid from P to L at position 178.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from H to Y at position 6.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from M to I at position 264.
+The protein's natural variant, known as in ESTRR; results in highly reduced activity;, features a modification of the amino acid from Q to H at position 375.
+The protein's natural variant, known as in ESTRR; highly decreased estrogen receptor activity;, features a modification of the amino acid from R to H at position 394.
+The protein's natural variant, known as destabilizes the receptor and decreases its affinity for estradiol at 25 degrees Celsius, but not at 4 degrees Celsius, features a modification of the amino acid from G to V at position 400.
+The protein's natural variant, known as in a 80 kDa form found in a breast cancer line; contains an in-frame duplication of exons 6 and 7, features a modification of the amino acid from D to RNQGKCVEGMVEIFDMLLATSSRFRMMNLQGEEFVCLKSIILLNSGVYTFLSSTLKSLEEKDHIHRVLDKITDTLIHLMAKAGLTLQQQHQRLAQLLLILSHIRHM at position 411.
+The protein's natural variant, known as in spf, features a modification of the amino acid from H to N at position 117.
+The protein's natural variant, known as in isoform LM-70B, features a modification of the amino acid from F to Y at position 82.
+The protein's natural variant, known as in strain: NRRLB8079, features a modification of the amino acid from S to P at position 59.
+The protein's natural variant, known as in strain: NRRLB8079, features a modification of the amino acid from K to Q at position 95.
+The protein's natural variant, known as in strain: NRRLB8079, features a modification of the amino acid from N to D at position 150.
+The protein's natural variant, known as in strain: NRRLB8079, features a modification of the amino acid from S to A at position 230.
+The protein's natural variant, known as in strain: NRRLB8079, features a modification of the amino acid from G to S at position 242.
+The protein's natural variant, known as in strain: NRRLB8079, features a modification of the amino acid from K to R at position 246.
+The protein's natural variant, known as in strain: NRRLB8079, features a modification of the amino acid from S to A at position 251.
+The protein's natural variant, known as in strain: NRRLB8079, features a modification of the amino acid from A to S at position 291.
+The protein's natural variant, known as in strain: NRRLB8079, features a modification of the amino acid from V to A at position 343.
+The protein's natural variant, known as in strain: NRRLB8079, features a modification of the amino acid from K to E at position 390.
+The protein's natural variant, known as in strain: NRRLB8079, features a modification of the amino acid from L to V at position 463.
+The protein's natural variant, known as in strain: Canton-S, KY02013G20 and KY02073G20, features a modification of the amino acid from V to I at position 10.
+The protein's natural variant, known as in strain: KY02106G9 and MEL6G59, features a modification of the amino acid from D to E at position 28.
+The protein's natural variant, known as in strain: Canton-S, KY02010G20, KY02013G20 and KY02073G20, features a modification of the amino acid from T to I at position 58.
+The protein's natural variant, known as in strain: KY02106G9, features a modification of the amino acid from D to E at position 87.
+The protein's natural variant, known as in strain: Canton-S, KY02010G20, KY02073G20 and KY02013G20, features a modification of the amino acid from D to N at position 87.
+The protein's natural variant, known as in strain: KY02106G9, features a modification of the amino acid from A to T at position 99.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to Q at position 1687.
+The protein's natural variant, known as frequency <0.004; may play a role in breast cancer susceptibility;, features a modification of the amino acid from A to V at position 2271.
+The protein's natural variant, known as in a glioblastoma multiforme sample; somatic mutation, features a modification of the amino acid from V to M at position 412.
+The protein's natural variant, known as in a breast pleomorphic lobular carcinoma sample; somatic mutation, features a modification of the amino acid from Q to H at position 421.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation, features a modification of the amino acid from S to G at position 690.
+The protein's natural variant, known as in allele D, features a modification of the amino acid from D to H at position 20.
+The protein's natural variant, known as in allele E, features a modification of the amino acid from Q to H at position 86.
+The protein's natural variant, known as in allele E, features a modification of the amino acid from K to R at position 103.
+The protein's natural variant, known as in allele E, features a modification of the amino acid from L to V at position 124.
+The protein's natural variant, known as in HSN1F; causes mislocalization of the protein; the mutant protein accumulates in condensed structures near the nucleus and localizes to unbranched tubules; has a dominant-negative disruptive effect on the regular structure of the endoplasmic reticulum;, features a modification of the amino acid from Y to C at position 192.
+The protein's natural variant, known as in strain: 569B, features a modification of the amino acid from M to I at position 45.
+The protein's natural variant, known as in strain: 569B and 86015, features a modification of the amino acid from V to A at position 100.
+The protein's natural variant, known as in strain: 569B, features a modification of the amino acid from V to A at position 272.
+The protein's natural variant, known as in strain: 569B, features a modification of the amino acid from V to A at position 281.
+The protein's natural variant, known as in strain: 86015, features a modification of the amino acid from A to S at position 349.
+The protein's natural variant, known as in strain: 86015, features a modification of the amino acid from K to R at position 381.
+The natural variant of this protein is characterized by an amino acid alteration from H to Q at position 81.
+The protein's natural variant, known as in strain: Isolate Mar AMO 01, features a modification of the amino acid from F to L at position 176.
+The protein's natural variant, known as in strain: Isolate 24/2 AMO 02 and Isolate Mar AMO 01, features a modification of the amino acid from P to L at position 242.
+The protein's natural variant, known as in strain: Isolate Mar AMO 01, features a modification of the amino acid from T to A at position 367.
+The protein's natural variant, known as in strain: Isolate 24/2 AMO 02, features a modification of the amino acid from T to I at position 367.
+The protein's natural variant, known as in strain: Isolate 24/2 AMO 02, features a modification of the amino acid from T to M at position 467.
+The protein's natural variant, known as in strain: Isolate 24/2 AMO 02, features a modification of the amino acid from F to L at position 495.
+The protein's natural variant, known as in strain: Isolate 24/2 AMO 02, features a modification of the amino acid from L to F at position 509.
+The natural variant of this protein is characterized by an amino acid alteration from N to D at position 90.
+The protein's natural variant, known as in HOGA; loss of protein stability; loss of ornithine aminotransferase activity;, features a modification of the amino acid from G to D at position 51.
+The protein's natural variant, known as in HOGA;, features a modification of the amino acid from N to K at position 54.
+The protein's natural variant, known as in HOGA; decreased protein abundance;, features a modification of the amino acid from Y to H at position 55.
+The protein's natural variant, known as in HOGA; no effect on protein abundance;, features a modification of the amino acid from N to K at position 89.
+The protein's natural variant, known as in HOGA; mistargeted, accumulates in cytoplasm;, features a modification of the amino acid from Q to E at position 90.
+The protein's natural variant, known as in HOGA; no effect on protein abundance;, features a modification of the amino acid from C to F at position 93.
+The protein's natural variant, known as in HOGA; loss of protein stability; loss of ornithine aminotransferase activity;, features a modification of the amino acid from Q to R at position 104.
+The protein's natural variant, known as in HOGA; no effect on protein abundance; loss of ornithine aminotransferase activity;, features a modification of the amino acid from R to L at position 154.
+The protein's natural variant, known as in HOGA; no effect on protein abundance; loss of ornithine aminotransferase activity;, features a modification of the amino acid from R to T at position 180.
+The protein's natural variant, known as in HOGA; loss of protein stability; loss of ornithine aminotransferase activity;, features a modification of the amino acid from P to Q at position 199.
+The protein's natural variant, known as in HOGA; loss of protein stability; loss of ornithine aminotransferase activity;, features a modification of the amino acid from A to V at position 226.
+The protein's natural variant, known as in HOGA; no effect on protein abundance;, features a modification of the amino acid from P to L at position 241.
+The protein's natural variant, known as in HOGA; no effect on protein abundance;, features a modification of the amino acid from Y to C at position 245.
+The protein's natural variant, known as in HOGA; no effect on protein abundance;, features a modification of the amino acid from R to P at position 250.
+The protein's natural variant, known as in HOGA; decreased protein abundance;, features a modification of the amino acid from T to I at position 267.
+The protein's natural variant, known as decreased protein abundance;, features a modification of the amino acid from A to P at position 270.
+The protein's natural variant, known as in HOGA; no effect on protein abundance; loss of ornithine aminotransferase activity;, features a modification of the amino acid from R to K at position 271.
+The protein's natural variant, known as in HOGA; loss of protein stability; loss of ornithine aminotransferase activity;, features a modification of the amino acid from E to K at position 318.
+The protein's natural variant, known as in HOGA;, features a modification of the amino acid from H to Y at position 319.
+The protein's natural variant, known as in HOGA; loss of protein stability; loss of ornithine aminotransferase activityx;, features a modification of the amino acid from V to M at position 332.
+The protein's natural variant, known as in HOGA; decreased protein abundance;, features a modification of the amino acid from G to D at position 353.
+The protein's natural variant, known as in HOGA; decreased protein abundance;, features a modification of the amino acid from G to A at position 375.
+The protein's natural variant, known as in HOGA; no effect on protein abundance;, features a modification of the amino acid from C to R at position 394.
+The protein's natural variant, known as in HOGA; loss of protein stability; loss of ornithine aminotransferase activity;, features a modification of the amino acid from C to Y at position 394.
+The protein's natural variant, known as in HOGA; may affect protein stability; loss of ornithine aminotransferase activity;, features a modification of the amino acid from L to P at position 402.
+The protein's natural variant, known as in HOGA; loss of protein stability; loss of ornithine aminotransferase activity;, features a modification of the amino acid from P to L at position 417.
+The protein's natural variant, known as in HOGA; loss of protein stability; loss of ornithine aminotransferase activity;, features a modification of the amino acid from I to N at position 436.
+The protein's natural variant, known as in HOGA; no effect on protein stability; increased ornithine aminotransferase activity;, features a modification of the amino acid from L to F at position 437.
+The protein's natural variant, known as in clade 1A and clade 1B, features a modification of the amino acid from N to S at position 16.
+The protein's natural variant, known as in clade 1B, features a modification of the amino acid from L to M at position 82.
+The protein's natural variant, known as in clade 1A and clade 1B, features a modification of the amino acid from T to A at position 329.
+The protein's natural variant, known as in IMD43; lower levels of B2M, MHC class I and FCGRT proteins;, features a modification of the amino acid from A to P at position 11.
+The protein's natural variant, known as in AMYL8; reduced stability; in contrast to the wild-type, the mutant aggregates into fibrils with classic amyloid-like properties under physiologic solvent conditions;, features a modification of the amino acid from D to N at position 96.
+The protein's natural variant, known as in UBB(+1); loss of polyubiquitination; impairs the ubiquitin-proteasome pathway; refractory to disassembly by DUBs; slow degradation by UCHL3, features a modification of the amino acid from GMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGC to YADLREDPDRQDHHPGSGAQ at position 229.
+The protein's natural variant, known as in strain: BSm300, features a modification of the amino acid from A to R at position 124.
+The protein's natural variant, known as in plasmid pTiBo542, features a modification of the amino acid from V to I at position 33.
+The protein's natural variant, known as in plasmid pTiBo542, features a modification of the amino acid from V to G at position 82.
+The protein's natural variant, known as in plasmid pTiBo542, features a modification of the amino acid from I to T at position 132.
+The protein's natural variant, known as requires 2 nucleotide substitutions, features a modification of the amino acid from A to I at position 228.
+The protein's natural variant, known as requires 2 nucleotide substitutions, features a modification of the amino acid from A to R at position 228.
+The protein's natural variant, known as in SMDP1;, features a modification of the amino acid from R to C at position 236.
+The natural variant of this protein is characterized by an amino acid alteration from V to T at position 133.
+The natural variant of this protein is characterized by an amino acid alteration from R to Q at position 152.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 244.
+The natural variant of this protein is characterized by an amino acid alteration from N to D at position 248.
+The natural variant of this protein is characterized by an amino acid alteration from N to S at position 398.
+The protein's natural variant, known as in HH1; phenotype consistent with Kallmann syndrome, features a modification of the amino acid from C to G at position 134.
+The protein's natural variant, known as in HH1; phenotype consistent with Kallmann syndrome, features a modification of the amino acid from C to R at position 163.
+The protein's natural variant, known as in HH1; phenotype consistent with Kallmann syndrome, features a modification of the amino acid from C to Y at position 163.
+The protein's natural variant, known as in HH1; phenotype consistent with Kallmann syndrome;, features a modification of the amino acid from C to R at position 172.
+The protein's natural variant, known as probable disease-associated variant found in a patient with Kallmann syndrome; the patient also carries mutation Ala-688 in SEMA3A, features a modification of the amino acid from Y to D at position 217.
+The protein's natural variant, known as in HH1; phenotype consistent with Kallmann syndrome, features a modification of the amino acid from R to P at position 262.
+The protein's natural variant, known as in HH1; phenotype consistent with Kallmann syndrome; loss of effect on the migratory activity of GnRH neurons; complete loss of FGFR1-binding, features a modification of the amino acid from N to K at position 267.
+The protein's natural variant, known as in HH1; phenotype consistent with Kallmann syndrome;, features a modification of the amino acid from N to S at position 304.
+The protein's natural variant, known as in HH1; phenotype consistent with Kallmann syndrome;, features a modification of the amino acid from S to L at position 396.
+The protein's natural variant, known as in HH1; phenotype consistent with Kallmann syndrome; loss of effect on the migratory activity of GnRH neurons; reduced FGFR1-binding;, features a modification of the amino acid from E to K at position 514.
+The protein's natural variant, known as in HH1; phenotype consistent with Kallmann syndrome; loss of effect on the migratory activity of GnRH neurons; Reduced FGFR1-binding, features a modification of the amino acid from F to L at position 517.
+The protein's natural variant, known as in HH1;, features a modification of the amino acid from E to K at position 539.
+The protein's natural variant, known as in HH1; phenotype consistent with Kallmann syndrome;, features a modification of the amino acid from W to R at position 571.
+The protein's natural variant, known as in HH1; phenotype consistent with normosmic idiopathic hypogonadotropic hypogonadism; the patient also carries a mutation in FGFR1;, features a modification of the amino acid from V to L at position 587.
+The natural variant of this protein is characterized by an amino acid alteration from K to M at position 666.
+The protein's natural variant, known as in HH1; phenotype consistent with Kallmann syndrome;, features a modification of the amino acid from H to R at position 672.
+The natural variant of this protein is characterized by an amino acid alteration from A to T at position 1803.
+The natural variant of this protein is characterized by an amino acid alteration from L to F at position 1824.
+The natural variant of this protein is characterized by an amino acid alteration from S to N at position 1847.
+The natural variant of this protein is characterized by an amino acid alteration from D to G at position 1927.
+The protein's natural variant, known as in COXPD27;, features a modification of the amino acid from P to L at position 251.
+The protein's natural variant, known as in Nessy, features a modification of the amino acid from I to N at position 15.
+The protein's natural variant, known as found in an acute myeloid leukemia sample; somatic mutation;, features a modification of the amino acid from P to L at position 1004.
+The protein's natural variant, known as in RP75; unknown pathological significance, features a modification of the amino acid from P to R at position 108.
+The protein's natural variant, known as in RP75; unknown pathological significance, features a modification of the amino acid from V to G at position 251.
+The protein's natural variant, known as in RP75;, features a modification of the amino acid from R to W at position 276.
+The protein's natural variant, known as in RP75; unknown pathological significance;, features a modification of the amino acid from R to C at position 281.
+The protein's natural variant, known as in RP75;, features a modification of the amino acid from D to N at position 295.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from A to D at position 569.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from G to R at position 2026.
+The protein's natural variant, known as in HVLI; reduced catalytic activity;, features a modification of the amino acid from R to Q at position 170.
+The protein's natural variant, known as in HVLI; reduced catalytic activity;, features a modification of the amino acid from E to K at position 264.
+The protein's natural variant, known as in strain: NFS97, features a modification of the amino acid from P to H at position 2.
+The protein's natural variant, known as in strain: 3CPA86 and T32, features a modification of the amino acid from D to E at position 43.
+The protein's natural variant, known as in strain: 3CPA86 and 3CPA126, features a modification of the amino acid from E to D at position 129.
+The protein's natural variant, known as in strain: 3CPA86 and 3CPA126, features a modification of the amino acid from D to E at position 138.
+The protein's natural variant, known as in strain: QD18, features a modification of the amino acid from F to L at position 195.
+The protein's natural variant, known as in strain: A28, features a modification of the amino acid from M to I at position 516.
+The protein's natural variant, known as in strain: A28, features a modification of the amino acid from A to V at position 524.
+The protein's natural variant, known as in strain: AUS and Berkeley, features a modification of the amino acid from F to Y at position 545.
+The protein's natural variant, known as in strain: AUS, features a modification of the amino acid from P to T at position 555.
+The protein's natural variant, known as in strain: A28, features a modification of the amino acid from E to D at position 573.
+The protein's natural variant, known as in strain: 3CPA126 and QD18, features a modification of the amino acid from K to T at position 606.
+The protein's natural variant, known as in COXPD50; severe reduction of MRPS25 protein levels resulting in destabilization of the entire small ribosomal subunit and a decrease of mitochondrial translation rate; causes oxidative phosphorylation defects in patient cells;, features a modification of the amino acid from P to L at position 72.
+The protein's natural variant, known as in IMD58; decreased protein expression in patient's cells;, features a modification of the amino acid from R to T at position 50.
+The protein's natural variant, known as in IMD58; decreased protein expression in patient's leukocytes; no effect on homodimerization;, features a modification of the amino acid from L to R at position 372.
+The protein's natural variant, known as in IMD58; decreased protein expression in patient's leukocytes; no effect on homodimerization;, features a modification of the amino acid from L to Q at position 525.
+The protein's natural variant, known as in IMD58;, features a modification of the amino acid from L to H at position 639.
+The protein's natural variant, known as in MDRCMTT; unknown pathological significance;, features a modification of the amino acid from N to K at position 92.
+The protein's natural variant, known as in MDRCMTT; unknown pathological significance;, features a modification of the amino acid from P to L at position 97.
+The protein's natural variant, known as in MDRCMTT; unknown pathological significance;, features a modification of the amino acid from L to P at position 323.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from F to L at position 1325.
+The protein's natural variant, known as in IMD91; unknown pathological significance, features a modification of the amino acid from R to Q at position 377.
+The protein's natural variant, known as in IMD91; unknown pathological significance, features a modification of the amino acid from L to P at position 1051.
+The protein's natural variant, known as in IMD91; unknown pathological significance, features a modification of the amino acid from I to T at position 1154.
+The protein's natural variant, known as in IMD91; unknown pathological significance, features a modification of the amino acid from C to S at position 1264.
+The protein's natural variant, known as in IMD91; unknown pathological significance, features a modification of the amino acid from C to S at position 1292.
+The protein's natural variant, known as in mutant RPB3-1, features a modification of the amino acid from A to D at position 30.
+The protein's natural variant, known as probable disease-associated variant found in a patient with Parkinson's disease; 40 % reduction in prenyltransferase activity, features a modification of the amino acid from G to C at position 91.
+The protein's natural variant, known as in CDG1AA; loss of function in protein glycosylation; 5-fold reduction in catalytic activity and reduced affinity for FPP and IPP.;, features a modification of the amino acid from R to H at position 290.
+The protein's natural variant, known as possible deamidation, features a modification of the amino acid from N to D at position 31.
+The natural variant of this protein is characterized by an amino acid alteration from V to M at position 73.
+The protein's natural variant, known as in BTHLM1;, features a modification of the amino acid from G to S at position 271.
+The protein's natural variant, known as in UCMD1;, features a modification of the amino acid from G to R at position 283.
+The protein's natural variant, known as in UCMD1;, features a modification of the amino acid from R to H at position 498.
+The protein's natural variant, known as in UCMD1, features a modification of the amino acid from G to R at position 531.
+The protein's natural variant, known as in BTHLM1;, features a modification of the amino acid from D to N at position 621.
+The protein's natural variant, known as in BTHLM1;, features a modification of the amino acid from G to S at position 700.
+The protein's natural variant, known as in BTHLM1;, features a modification of the amino acid from C to R at position 777.
+The protein's natural variant, known as in UCMD1; prevents collagen VI assembly;, features a modification of the amino acid from L to P at position 837.
+The protein's natural variant, known as in UCMD1;, features a modification of the amino acid from R to S at position 876.
+The protein's natural variant, known as in BTHLM1; results in reduced intracellular collagen VI assembly and secretion;, features a modification of the amino acid from P to L at position 932.
+The protein's natural variant, known as in strain: cv. An-1, cv. Br-0, cv. Ct-1, cv. Cvi-1, cv. Edi-0, cv. Ga-0, cv. Kas-1, cv. Kin-0, cv. Landsberg erecta, cv. Ll-0, cv. Lz-0, cv. Ms-0, cv. Mt-0, cv. Nok-3, cv. Oy-0, cv. Se-0, cv. Sorbo, cv. Tsu-1, cv. Van-0, cv. Wa-1 and cv. Wassilewskija, features a modification of the amino acid from M to L at position 225.
+The protein's natural variant, known as in strain: cv. Kas-1 and cv. Sorbo, features a modification of the amino acid from G to E at position 231.
+The protein's natural variant, known as in strain: cv. Cvi-1, features a modification of the amino acid from A to T at position 248.
+The protein's natural variant, known as in MC5DN5; no effect on protein abundance; decreased mitochondrial proton-transporting ATP synthase complex assembly; decreased aerobic respiration in patient cells homozygous for the mutation; partial loss of function confirmed by complementation assays;, features a modification of the amino acid from P to L at position 82.
+The protein's natural variant, known as in MC5DN5; no effect on protein abundance; decreased mitochondrial proton-transporting ATP synthase complex assembly; decreased aerobic respiration in patient cells homozygous for the mutation; partial loss of function confirmed by complementation assays;, features a modification of the amino acid from V to G at position 106.
+The protein's natural variant, known as in NPS, features a modification of the amino acid from C to R at position 59.
+The protein's natural variant, known as in NPS, features a modification of the amino acid from C to S at position 59.
+The protein's natural variant, known as in NPS, features a modification of the amino acid from H to N at position 77.
+The protein's natural variant, known as in NPS, features a modification of the amino acid from H to Q at position 77.
+The protein's natural variant, known as in NPS, features a modification of the amino acid from H to Y at position 77.
+The protein's natural variant, known as in NPS, features a modification of the amino acid from C to R at position 80.
+The protein's natural variant, known as in NPS, features a modification of the amino acid from L to W at position 81.
+The protein's natural variant, known as in NPS, features a modification of the amino acid from C to F at position 83.
+The protein's natural variant, known as in NPS, features a modification of the amino acid from C to G at position 83.
+The protein's natural variant, known as in NPS, features a modification of the amino acid from C to W at position 83.
+The protein's natural variant, known as in NPS, features a modification of the amino acid from C to Y at position 83.
+The protein's natural variant, known as in NPS, features a modification of the amino acid from C to R at position 86.
+The protein's natural variant, known as in NPS, features a modification of the amino acid from C to W at position 103.
+The protein's natural variant, known as in NPS, features a modification of the amino acid from D to G at position 106.
+The protein's natural variant, known as in NPS;, features a modification of the amino acid from C to F at position 118.
+The protein's natural variant, known as in NPS, features a modification of the amino acid from C to Y at position 118.
+The protein's natural variant, known as in NPS, features a modification of the amino acid from H to Y at position 137.
+The protein's natural variant, known as in NPS, features a modification of the amino acid from C to Y at position 140.
+The protein's natural variant, known as in NPS, features a modification of the amino acid from C to S at position 143.
+The protein's natural variant, known as in NPS, features a modification of the amino acid from C to F at position 146.
+The protein's natural variant, known as in NPS, features a modification of the amino acid from C to Y at position 146.
+The protein's natural variant, known as in NPS, features a modification of the amino acid from C to W at position 165.
+The protein's natural variant, known as in NPS;, features a modification of the amino acid from R to Q at position 223.
+The protein's natural variant, known as in NPS;, features a modification of the amino acid from A to P at position 236.
+The protein's natural variant, known as in NPS, features a modification of the amino acid from S to P at position 241.
+The protein's natural variant, known as in FSGS10;, features a modification of the amino acid from R to P at position 246.
+The protein's natural variant, known as in FSGS10; decreased transcriptional activity;, features a modification of the amino acid from R to Q at position 246.
+The protein's natural variant, known as in NPS;, features a modification of the amino acid from R to P at position 249.
+The protein's natural variant, known as in NPS, features a modification of the amino acid from L to P at position 252.
+The protein's natural variant, known as in NPS, features a modification of the amino acid from A to V at position 253.
+The protein's natural variant, known as in NPS, features a modification of the amino acid from W to C at position 266.
+The protein's natural variant, known as in NPS;, features a modification of the amino acid from N to K at position 269.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from G to W at position 40.
+The natural variant of this protein is characterized by an amino acid alteration from L to F at position 66.
+The natural variant of this protein is characterized by an amino acid alteration from Q to L at position 151.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 181.
+The protein's natural variant, known as affects localization at the plasma membrane; loss of cholesterol efflux to APOA1;, features a modification of the amino acid from P to R at position 649.
+The protein's natural variant, known as in strain: Guangxi Huang, features a modification of the amino acid from H to Y at position 45.
+The natural variant of this protein is characterized by an amino acid alteration from P to S at position 8.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 417.
+The protein's natural variant, known as in MCOPS15; unknown pathological significance;, features a modification of the amino acid from A to G at position 1349.
+The protein's natural variant, known as in MCOPS15; unknown pathological significance;, features a modification of the amino acid from R to W at position 2563.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from K to N at position 694.
+The protein's natural variant, known as probable disease-associated variant found in a patient with drug-resistant generalized epilepsy, cognitive impairment and autism spectrum disorder;, features a modification of the amino acid from R to Q at position 170.
+The protein's natural variant, known as probable disease-associated variant found in a patient with West syndrome;, features a modification of the amino acid from A to P at position 195.
+The protein's natural variant, known as in MRD5; the disease phenotype consists of intellectual disability, autism and epilepsy; the mutant protein is less efficient in inhibiting ERK phosphorylation induced by neuronal activity, features a modification of the amino acid from W to R at position 362.
+The protein's natural variant, known as in MRD5; the disease phenotype consists of intellectual disability and autism; the mutant protein is less efficient in inhibiting ERK phosphorylation induced by neuronal activity;, features a modification of the amino acid from P to L at position 562.
+The natural variant of this protein is characterized by an amino acid alteration from R to Q at position 749.
+The protein's natural variant, known as in allele KIR3DL3*00401, allele KIR3DL3*00402, allele KIR3DL3*00801, allele KIR3DL3*00802 and allele KIR3DL3*026;, features a modification of the amino acid from R to H at position 52.
+The protein's natural variant, known as in allele KIR3DL3*00601, allele KIR3DL3*00602, allele KIR3DL3*01501 and allele KIR3DL3*01601;, features a modification of the amino acid from N to K at position 56.
+The protein's natural variant, known as in allele KIR3DL3*010 and allele KIR3DL3*028;, features a modification of the amino acid from R to W at position 77.
+The protein's natural variant, known as in allele KIR3DL3*00601, allele KIR3DL3*00602, allele KIR3DL3*01501 and allele KIR3DL3*01601;, features a modification of the amino acid from R to S at position 149.
+The protein's natural variant, known as in allele KIR3DL3*007, allele KIR3DL3*030 and allele KIR3DL3*031;, features a modification of the amino acid from R to H at position 152.
+The protein's natural variant, known as in allele KIR3DL3*00101, allele KIR3DL3*00102, allele KIR3DL3*00103, allele KIR3DL3*0030101, allele KIR3DL3*00901, allele KIR3DL3*00902, allele KIR3DL3*010 and allele KIR3DL3*028;, features a modification of the amino acid from V to I at position 168.
+The protein's natural variant, known as in allele KIR3DL3*005;, features a modification of the amino acid from G to D at position 231.
+The protein's natural variant, known as in allele KIR3DL3*00601, allele KIR3DL3*00602, allele KIR3DL3*01101, allele KIR3DL3*01102, allele KIR3DL3*01501, allele KIR3DL3*01601 and allele KIR3DL3*017;, features a modification of the amino acid from N to T at position 290.
+The protein's natural variant, known as in allele KIR3DL3*00101, allele KIR3DL3*00102, allele KIR3DL3*00103, allele KIR3DL3*00601, allele KIR3DL3*00602, allele KIR3DL3*01302, allele KIR3DL3*01305, allele KIR3DL3*01306, allele KIR3DL3*01307, allele KIR3DL3*017 and allele KIR3DL3*026;, features a modification of the amino acid from H to N at position 321.
+The protein's natural variant, known as in allele KIR3DL3*00101, allele KIR3DL3*0030101, allele KIR3DL3*00401, allele KIR3DL3*00402, allele KIR3DL3*007, allele KIR3DL3*01404, allele KIR3DL3*01405, allele KIR3DL3*01601 and allele KIR3DL3*028;, features a modification of the amino acid from H to Y at position 321.
+The protein's natural variant, known as in allele KIR3DL3*0030101, allele KIR3DL3*00401, allele KIR3DL3*00402, allele KIR3DL3*007, allele KIR3DL3*01404, allele KIR3DL3*01405, allele KIR3DL3*01601 and allele KIR3DL3*028;, features a modification of the amino acid from V to A at position 324.
+The protein's natural variant, known as in allele KIR3DL3*029;, features a modification of the amino acid from V to D at position 324.
+The protein's natural variant, known as in allele KIR3DL3*027, allele KIR3DL3*029 and allele KIR3DL3*031;, features a modification of the amino acid from A to P at position 348.
+The protein's natural variant, known as in allele KIR3DL3*027, allele KIR3DL3*029 and allele KIR3DL3*031;, features a modification of the amino acid from E to D at position 373.
+The protein's natural variant, known as in THC7; unknown pathological significance, features a modification of the amino acid from Q to H at position 16.
+The protein's natural variant, known as in THC7; unknown pathological significance, features a modification of the amino acid from S to P at position 119.
+The protein's natural variant, known as in nepenthesin-1b, features a modification of the amino acid from D to V at position 233.
+The protein's natural variant, known as in nepenthesin-1b, features a modification of the amino acid from N to T at position 251.
+The protein's natural variant, known as in nepenthesin-1b, features a modification of the amino acid from G to E at position 392.
+The protein's natural variant, known as in alpha-1 A variant, features a modification of the amino acid from S to G at position 12.
+The protein's natural variant, known as in alpha-1 A variant, features a modification of the amino acid from S to N at position 78.
+The protein's natural variant, known as in alpha-1 A variant, features a modification of the amino acid from A to S at position 102.
+The protein's natural variant, known as in alpha-1 A variant, features a modification of the amino acid from A to E at position 115.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to Q at position 297.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from G to R at position 280.
+The protein's natural variant, known as in strain: Mackaness, features a modification of the amino acid from S to T at position 94.
+The protein's natural variant, known as in strain: Mackaness, features a modification of the amino acid from A to V at position 167.
+The protein's natural variant, known as in strain: Mackaness, features a modification of the amino acid from V to I at position 196.
+The protein's natural variant, known as in JBTS38; unknown pathological significance, features a modification of the amino acid from R to G at position 257.
+The protein's natural variant, known as in IMD55; lower GINS1 protein levels and defective DNA replication are observed in patient cells; the mutant does not interact with GINS3 and GINS4;, features a modification of the amino acid from R to C at position 83.
+The protein's natural variant, known as in IMD55; lower GINS1 protein levels and defective DNA replication are observed in patient cells;, features a modification of the amino acid from C to Y at position 152.
+The natural variant of this protein is characterized by an amino acid alteration from P to PN at position 202.
+The protein's natural variant, known as in a patient affected by schizophrenia, features a modification of the amino acid from D to G at position 222.
+The protein's natural variant, known as in strain: cv. No-0 and cv. Wassilewskija, features a modification of the amino acid from N to K at position 478.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from T to S at position 299.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from R to Q at position 806.
+The protein's natural variant, known as in NEDSIS; gain-of-function variant; affects voltage-gated calcium channel activity by altering channel gating properties; changes current kinetics and left-shifts the voltage dependence of activation; when expressed in chromaffin cells it affects the mode of action potential firing, features a modification of the amino acid from I to M at position 860.
+The protein's natural variant, known as in NEDSIS; gain-of-function variant; affects voltage-gated calcium channel activity by altering channel gating properties; changes current kinetics and left-shifts the voltage dependence of activation; lower channel deactivation kinetics compared to wild type; when expressed in chromaffin cells it affects the mode of action potential firing, features a modification of the amino acid from I to N at position 860.
+The protein's natural variant, known as in NEDSIS; gain-of-function variant; affects voltage-gated calcium channel activity by altering channel gating properties; changes current kinetics and left-shifts the voltage dependence of activation; lower channel deactivation kinetics compared to wild type, features a modification of the amino acid from I to T at position 1306.
+The protein's natural variant, known as in NEDSIS; gain-of-function variant; affects voltage-gated calcium channel activity by altering channel gating properties; changes current kinetics and left-shifts the voltage dependence of activation; lower channel deactivation kinetics compared to wild type, features a modification of the amino acid from M to I at position 1425.
+The protein's natural variant, known as in GSD and early-onset dementia;, features a modification of the amino acid from P to L at position 102.
+The protein's natural variant, known as in GSD;, features a modification of the amino acid from P to L at position 105.
+The protein's natural variant, known as linked to development of dementing Gerstmann-Straussler disease;, features a modification of the amino acid from A to V at position 117.
+The protein's natural variant, known as variant that has been selected for in response to the Kuru epidemic and confers resistance to prion disease by acting as a 'dominant negative' inhibitor of prion conversion; is not only itself resistant to conformational conversion, but also inhibits conversion of wild-type proteins; confers protection against classical Creutzfeldt-Jakob disease (CJD) and Kuru in the heterozygous state, but can be infected with variant CJD prions, resulting from exposure to bovine spongiform encephalopathy prions; confers complete resistance to all prion strains when homozygous. Always associated with M-129 variant;, features a modification of the amino acid from G to V at position 127.
+The protein's natural variant, known as confers relative protection against acquired, sporadic and some inherited prion diseases in the heterozygous state, possibly by preventing homodimerization; determines the disease phenotype in patients who have a PrP mutation at position 178; patients with M-129 develop FFI, those with V-129 develop CJD;, features a modification of the amino acid from M to V at position 129.
+The protein's natural variant, known as in GSD;, features a modification of the amino acid from G to V at position 131.
+The protein's natural variant, known as in schizoaffective disorder;, features a modification of the amino acid from N to S at position 171.
+The protein's natural variant, known as in FFI and CJD;, features a modification of the amino acid from D to N at position 178.
+The protein's natural variant, known as in CJD;, features a modification of the amino acid from V to I at position 180.
+The protein's natural variant, known as in SENF and early-onset dementia; induces loss of glycosylation at N-181;, features a modification of the amino acid from T to A at position 183.
+The protein's natural variant, known as in GSD;, features a modification of the amino acid from H to R at position 187.
+The protein's natural variant, known as in early-onset dementia; dementia associated to prion diseases, features a modification of the amino acid from T to K at position 188.
+The protein's natural variant, known as in CJD, features a modification of the amino acid from E to K at position 196.
+The protein's natural variant, known as in GSD; atypical form with neurofibrillary tangles;, features a modification of the amino acid from F to S at position 198.
+The protein's natural variant, known as in CJD;, features a modification of the amino acid from E to K at position 200.
+The protein's natural variant, known as in GSD;, features a modification of the amino acid from D to N at position 202.
+The protein's natural variant, known as in CJD; unknown pathological significance;, features a modification of the amino acid from V to I at position 203.
+The protein's natural variant, known as in CJD;, features a modification of the amino acid from R to H at position 208.
+The protein's natural variant, known as in CJD;, features a modification of the amino acid from V to I at position 210.
+The protein's natural variant, known as in CJD;, features a modification of the amino acid from E to Q at position 211.
+The protein's natural variant, known as in GSD;, features a modification of the amino acid from Q to P at position 212.
+The protein's natural variant, known as in GSD; with neurofibrillary tangles;, features a modification of the amino acid from Q to R at position 217.
+The protein's natural variant, known as confers relative protection against sporadic Creutzfeldt-Jakob disease (CJD) in the heterozygous state;, features a modification of the amino acid from E to K at position 219.
+The protein's natural variant, known as in CJD;, features a modification of the amino acid from M to R at position 232.
+The natural variant of this protein is characterized by an amino acid alteration from P to S at position 238.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from L to F at position 6.
+The protein's natural variant, known as in IMGTALLELETRBV7-9*02, features a modification of the amino acid from K to N at position 30.
+The protein's natural variant, known as in PRIMS; does not affect subcellular location; strongly reduced DNA binding; reduced ability to repress transcription; dominant-negative effect of the mutant on the wild-type allele;, features a modification of the amino acid from K to Q at position 590.
+The protein's natural variant, known as in PRIMS; strongly reduced DNA binding; strongly reduced ability to repress transcription; dominant-negative effect of the mutant on the wild-type allele;, features a modification of the amino acid from H to R at position 596.
+The protein's natural variant, known as in PRIMS; strongly reduced DNA binding; strongly reduced ability to repress transcription; dominant-negative effect of the mutant on the wild-type allele;, features a modification of the amino acid from G to A at position 602.
+The protein's natural variant, known as in PRIMS; strongly reduced DNA binding; reduced ability to repress transcription; dominant-negative effect of the mutant on the wild-type allele;, features a modification of the amino acid from L to F at position 621.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation, features a modification of the amino acid from R to H at position 912.
+The protein's natural variant, known as in strain: cv. Osvals's 72, cv. Cluster and cv. Nugget, features a modification of the amino acid from A to E at position 232.
+The protein's natural variant, known as in strain: cv. Osvals's 72, features a modification of the amino acid from V to L at position 385.
+The protein's natural variant, known as in strain: CLIB 95, CLIB 219, CLIB 382, CLIB 388, CLIB 556, CLIB 630, K1, R12, R13, YIIc12 and YIIc17, features a modification of the amino acid from S to T at position 34.
+The protein's natural variant, known as in strain: CLIB 95, CLIB 382, CLIB 388, CLIB 556, CLIB 630, K1, R12, R13, YIIc12 and YIIc17, features a modification of the amino acid from A to T at position 176.
+The protein's natural variant, known as in strain: CLIB 95, CLIB 219, CLIB 382, CLIB 388, CLIB 556, CLIB 630, K1, R12, R13, YIIc12 and YIIc17, features a modification of the amino acid from D to G at position 201.
+The protein's natural variant, known as in strain: CLIB 630 haplotype Ha2, features a modification of the amino acid from M to I at position 294.
+The protein's natural variant, known as in strain: CLIB 388, YIIc12 haplotype Ha2 and YIIc17 haplotype Ha2, features a modification of the amino acid from K to E at position 337.
+The protein's natural variant, known as in strain: CLIB 95, CLIB 219, CLIB 382, CLIB 388, CLIB 556, CLIB 630, K1, R12, R13, YIIc12 and YIIc17, features a modification of the amino acid from D to N at position 370.
+The protein's natural variant, known as in strain: R12 haplotype Ha2, features a modification of the amino acid from F to L at position 394.
+The protein's natural variant, known as in ab, features a modification of the amino acid from S to SP at position 278.
+The protein's natural variant, known as in strain: Samarkand-pk1, features a modification of the amino acid from T to A at position 62.
+The protein's natural variant, known as in strain: Berkeley, features a modification of the amino acid from P to A at position 106.
+The protein's natural variant, known as in strain: Berkeley, features a modification of the amino acid from T to A at position 159.
+The protein's natural variant, known as in strain: Berkeley, features a modification of the amino acid from C to S at position 177.
+The protein's natural variant, known as in strain: Karsnas, features a modification of the amino acid from HHHNR to LILPT at position 208.
+The protein's natural variant, known as in strain: Berkeley and Oregon-R(2/10), features a modification of the amino acid from P to S at position 247.
+The protein's natural variant, known as in strain: Berkeley, Oregon-R and Oregon-R(2/10), features a modification of the amino acid from P to S at position 249.
+The protein's natural variant, known as in strain: Berkeley, Oregon-R and Oregon-R(2/10), features a modification of the amino acid from S to SCKPA at position 252.
+The protein's natural variant, known as in strain: Samarkand-pSW9, features a modification of the amino acid from S to SRKPS at position 252.
+The protein's natural variant, known as in strain: Berkeley, Oregon-R and Oregon-R(2/10), features a modification of the amino acid from T to A at position 267.
+The protein's natural variant, known as in strain: Oregon-R, features a modification of the amino acid from A to V at position 275.
+The protein's natural variant, known as variant found in a clone obtained from a fibroblast cell line; does not form the essential disulfide bond; results in loss of antiviral activity, features a modification of the amino acid from C to Y at position 162.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from W to C at position 164.
+The protein's natural variant, known as in strain: BEN2908 / O2:K1:H5 / APEC, features a modification of the amino acid from V to M at position 158.
+The protein's natural variant, known as in strain: BEN2908 / O2:K1:H5 / APEC, features a modification of the amino acid from V to A at position 182.
+The protein's natural variant, known as in strain: BEN2908 / O2:K1:H5 / APEC, features a modification of the amino acid from I to V at position 267.
+The protein's natural variant, known as in strain: BEN2908 / O2:K1:H5 / APEC, features a modification of the amino acid from LI to FV at position 290.
+The protein's natural variant, known as in strain: BEN2908 / O2:K1:H5 / APEC, features a modification of the amino acid from V to L at position 293.
+The protein's natural variant, known as in strain: BEN2908 / O2:K1:H5 / APEC, features a modification of the amino acid from V to I at position 322.
+The protein's natural variant, known as in CRS5; low-penetrance mutation associated with disease susceptibility; results in gain-of-function;, features a modification of the amino acid from V to F at position 7.
+The protein's natural variant, known as in CRS5; low-penetrance mutation associated with disease susceptibility; results in gain-of-function;, features a modification of the amino acid from K to E at position 211.
+The protein's natural variant, known as in PFM2;, features a modification of the amino acid from R to Q at position 218.
+The protein's natural variant, known as in PFM2;, features a modification of the amino acid from R to P at position 272.
+The protein's natural variant, known as in IMD98; gain-of-function variant resulting in increased NF-kappa-B activation measured in a reporter assay, features a modification of the amino acid from P to L at position 432.
+The protein's natural variant, known as in IMD98; gain-of-function variant resulting in increased NF-kappa-B activation measured in a reporter assay, features a modification of the amino acid from F to L at position 494.
+The protein's natural variant, known as in IMD98; gain-of-function variant resulting in increased NF-kappa-B activation measured in a reporter assay;, features a modification of the amino acid from G to D at position 572.
+The protein's natural variant, known as in IMD98; increased NF-kappa-B activation measured in a reporter assay; results in increased TLR8 protein degradation, features a modification of the amino acid from G to V at position 572.
+The protein's natural variant, known as in strain: CBS 6556, features a modification of the amino acid from F to L at position 3.
+The protein's natural variant, known as in strain: CBS 6556, features a modification of the amino acid from E to Q at position 165.
+The protein's natural variant, known as in strain: CBS 6556, features a modification of the amino acid from T to S at position 168.
+The protein's natural variant, known as in strain: CBS 6556, features a modification of the amino acid from V to A at position 251.
+The protein's natural variant, known as in strain: CBS 6556, features a modification of the amino acid from D to DS at position 252.
+The protein's natural variant, known as in strain: CBS 6556, features a modification of the amino acid from G to D at position 299.
+The protein's natural variant, known as in strain: CBS 834, features a modification of the amino acid from N to I at position 393.
+The protein's natural variant, known as in strain: CBS 6556, features a modification of the amino acid from T to N at position 479.
+The protein's natural variant, known as in CIRRH;, features a modification of the amino acid from T to A at position 103.
+The protein's natural variant, known as in CIRRH; interfers with the ability to form normal filaments;, features a modification of the amino acid from H to L at position 128.
+The protein's natural variant, known as in CIRRH;, features a modification of the amino acid from R to Q at position 261.
+The protein's natural variant, known as in CIRRH;, features a modification of the amino acid from G to R at position 340.
+The protein's natural variant, known as in NEDCAS and RMFSL; unknown pathological significance;, features a modification of the amino acid from L to P at position 140.
+The protein's natural variant, known as in NEDCAS; unknown pathological significance;, features a modification of the amino acid from R to W at position 609.
+The protein's natural variant, known as in NEDCAS; unknown pathological significance;, features a modification of the amino acid from A to E at position 642.
+The protein's natural variant, known as in allele VN1R1*2;, features a modification of the amino acid from I to T at position 139.
+The protein's natural variant, known as in allele VN1R1*3;, features a modification of the amino acid from S to F at position 241.
+The protein's natural variant, known as in allele VN1R1*3;, features a modification of the amino acid from A to D at position 269.
+The protein's natural variant, known as in YHFS;, features a modification of the amino acid from P to L at position 260.
+The protein's natural variant, known as in YHFS;, features a modification of the amino acid from C to F at position 367.
+The protein's natural variant, known as in YHFS;, features a modification of the amino acid from R to H at position 609.
+The protein's natural variant, known as in YHFS;, features a modification of the amino acid from D to V at position 720.
+The protein's natural variant, known as in YHFS;, features a modification of the amino acid from V to M at position 766.
+The protein's natural variant, known as in TMBTS; gain-of-function mutation resulting in a decreased threshold of channel activation and slower deactivation compared to wild-type;, features a modification of the amino acid from K to N at position 217.
+The protein's natural variant, known as in ZLS1; gain-of-function effect; accelerated channel activation and slower deactivation; associated in cis with L-383;, features a modification of the amino acid from S to Y at position 352.
+The protein's natural variant, known as in ZLS1; gain-of-function effect; accelerated channel activation and slower deactivation;, features a modification of the amino acid from G to R at position 375.
+The protein's natural variant, known as in ZLS1;, features a modification of the amino acid from L to V at position 379.
+The protein's natural variant, known as in ZLS1; gain-of-function effect; accelerated channel activation and slower deactivation; associated in cis with Y-352;, features a modification of the amino acid from V to L at position 383.
+The protein's natural variant, known as in TMBTS; gain-of-function mutation resulting in a decreased threshold of channel activation and slower deactivation compared to wild-type;, features a modification of the amino acid from L to F at position 489.
+The protein's natural variant, known as in TMBTS and ZLS1; gain-of-function effect; resulting in a decreased threshold of channel activation and slower deactivation;, features a modification of the amino acid from I to V at position 494.
+The protein's natural variant, known as in ZLS1; gain-of-function effect; increased conductance at negative potentials;, features a modification of the amino acid from G to R at position 496.
+The protein's natural variant, known as in TMBTS; gain-of-function mutation resulting in a decreased threshold of channel activation and slower deactivation compared to wild-type;, features a modification of the amino acid from Q to R at position 503.
+The protein's natural variant, known as in AMYL8;, features a modification of the amino acid from I to T at position 74.
+The protein's natural variant, known as in AMYL8;, features a modification of the amino acid from D to H at position 85.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation, features a modification of the amino acid from G to E at position 40.
+The protein's natural variant, known as in MMDS4;, features a modification of the amino acid from G to S at position 77.
+The protein's natural variant, known as in strain: ECOR 31, features a modification of the amino acid from P to Q at position 99.
+The protein's natural variant, known as in strain: ECOR 28, features a modification of the amino acid from T to M at position 110.
+The protein's natural variant, known as in strain: ECOR 60, features a modification of the amino acid from L to V at position 111.
+The protein's natural variant, known as in strain: ECOR 52, features a modification of the amino acid from P to S at position 114.
+The protein's natural variant, known as in strain: ECOR 28, features a modification of the amino acid from S to L at position 117.
+The protein's natural variant, known as in PC deficiency; mild; strongly reduced pyruvate carboxylase activity;, features a modification of the amino acid from V to A at position 145.
+The protein's natural variant, known as in PC deficiency;, features a modification of the amino acid from R to Q at position 156.
+The protein's natural variant, known as in PC deficiency;, features a modification of the amino acid from R to W at position 270.
+The protein's natural variant, known as in PC deficiency, features a modification of the amino acid from Y to C at position 304.
+The protein's natural variant, known as in PC deficiency; mild; strongly reduced pyruvate carboxylase activity;, features a modification of the amino acid from R to C at position 451.
+The protein's natural variant, known as in PC deficiency;, features a modification of the amino acid from R to L at position 583.
+The protein's natural variant, known as in PC deficiency; mild;, features a modification of the amino acid from A to T at position 610.
+The protein's natural variant, known as in PC deficiency;, features a modification of the amino acid from R to Q at position 631.
+The protein's natural variant, known as in PC deficiency; mild;, features a modification of the amino acid from M to I at position 743.
+The protein's natural variant, known as associated with SHEP10;, features a modification of the amino acid from M to L at position 484.
+The protein's natural variant, known as associated with SHEP10;, features a modification of the amino acid from G to E at position 734.
+The protein's natural variant, known as in strain: MT4239, features a modification of the amino acid from Q to H at position 255.
+The natural variant of this protein is characterized by an amino acid alteration from A to AA at position 393.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from A to G at position 122.
+The protein's natural variant, known as no effect on subcellular location; no effect on glycine transport;, features a modification of the amino acid from A to E at position 89.
+The protein's natural variant, known as no effect on glycine transport, features a modification of the amino acid from Q to R at position 184.
+The protein's natural variant, known as in HKPX3; compound heterozygote with S-509; impairment of glycine transport when coexpressed with S-509 in vitro;, features a modification of the amino acid from L to V at position 306.
+The protein's natural variant, known as in HKPX3; no effect on subcellular location; impairs glycine transport;, features a modification of the amino acid from T to M at position 425.
+The protein's natural variant, known as in HKPX3; impairs glycine transport; no effect on subcellular location;, features a modification of the amino acid from P to L at position 429.
+The protein's natural variant, known as no effect on glycine transport;, features a modification of the amino acid from D to N at position 463.
+The protein's natural variant, known as in HKPX3; no effect on subcellular location; impairs glycine transport, features a modification of the amino acid from W to C at position 482.
+The protein's natural variant, known as in HKPX3; no effect on subcellular location; impairs glycine transport;, features a modification of the amino acid from Y to C at position 491.
+The protein's natural variant, known as in HKPX3; compound heterozygote with V-306; no effect on subcellular location; impairs glycine transport;, features a modification of the amino acid from N to S at position 509.
+The protein's natural variant, known as in HKPX3; results in the formation of large aggregates in the cytoplasm; loss of glycine transport;, features a modification of the amino acid from S to R at position 510.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from V to E at position 632.
+The protein's natural variant, known as mild decrease of glycine transport; Vmax of the mutant is reduced to 60% compared to wild-type; decreased expression at the cell surface;, features a modification of the amino acid from Y to C at position 705.
+The protein's natural variant, known as no effect on glycine transport, features a modification of the amino acid from V to A at position 751.
+The protein's natural variant, known as associated with susceptibility to HBV infection; higher cell surface levels;, features a modification of the amino acid from K to E at position 47.
+The protein's natural variant, known as in DPYDD; allele DPYD*9A and allele DPYD*9B; loss of activity;, features a modification of the amino acid from C to R at position 29.
+The protein's natural variant, known as in DPYDD; allele DPYD*8; loss of activity;, features a modification of the amino acid from R to W at position 235.
+The protein's natural variant, known as in allele DPYD*4;, features a modification of the amino acid from S to N at position 534.
+The protein's natural variant, known as in allele DPYD*5;, features a modification of the amino acid from I to V at position 543.
+The protein's natural variant, known as in DPYDD; allele DPYD*9B; 25% of activity;, features a modification of the amino acid from R to H at position 886.
+The protein's natural variant, known as in allele DPYD*10; low activity;, features a modification of the amino acid from V to F at position 995.
+The protein's natural variant, known as in allele pot-1, features a modification of the amino acid from L to F at position 48.
+The protein's natural variant, known as in allele pot1(2), haplotypes 1 and 4, features a modification of the amino acid from V to K at position 54.
+The protein's natural variant, known as in haplotype 2, features a modification of the amino acid from L to V at position 58.
+The protein's natural variant, known as in allele pot-1, features a modification of the amino acid from N to K at position 68.
+The protein's natural variant, known as in allele pot-1, features a modification of the amino acid from P to S at position 69.
+The protein's natural variant, known as in allele pot-1, features a modification of the amino acid from A to D at position 77.
+The protein's natural variant, known as in allele pot-1, features a modification of the amino acid from V to L at position 85.
+The protein's natural variant, known as in allele pot-1, features a modification of the amino acid from M to I at position 109.
+The protein's natural variant, known as in allele pot1(2), haplotype 4, features a modification of the amino acid from D to G at position 112.
+The protein's natural variant, known as in allele pot-1, features a modification of the amino acid from K to Q at position 123.
+The protein's natural variant, known as in haplotype 3, features a modification of the amino acid from T to M at position 151.
+The protein's natural variant, known as in allele pot-1, features a modification of the amino acid from N to S at position 224.
+The protein's natural variant, known as in GLC1F; uncertain pathological significance;, features a modification of the amino acid from T to S at position 48.
+The protein's natural variant, known as in GLC1F; uncertain pathological significance;, features a modification of the amino acid from G to E at position 65.
+The protein's natural variant, known as in GLC1F; uncertain pathological significance;, features a modification of the amino acid from V to M at position 67.
+The protein's natural variant, known as in GLC1F; uncertain pathological significance;, features a modification of the amino acid from R to H at position 72.
+The protein's natural variant, known as in GLC1F; uncertain pathological significance;, features a modification of the amino acid from R to Q at position 94.
+The protein's natural variant, known as in GLC1F; uncertain pathological significance;, features a modification of the amino acid from D to E at position 97.
+The protein's natural variant, known as in GLC1F; uncertain pathological significance;, features a modification of the amino acid from R to C at position 183.
+The protein's natural variant, known as in GLC1F; uncertain pathological significance;, features a modification of the amino acid from A to V at position 197.
+The protein's natural variant, known as in GLC1F; uncertain pathological significance;, features a modification of the amino acid from V to L at position 207.
+The protein's natural variant, known as in GLC1F; uncertain pathological significance;, features a modification of the amino acid from R to H at position 272.
+The protein's natural variant, known as in GLC1F; uncertain pathological significance;, features a modification of the amino acid from Q to L at position 295.
+The protein's natural variant, known as in GLC1F; uncertain pathological significance;, features a modification of the amino acid from A to T at position 320.
+The protein's natural variant, known as in GLC1F; uncertain pathological significance;, features a modification of the amino acid from H to Q at position 332.
+The protein's natural variant, known as in GLC1F; uncertain pathological significance;, features a modification of the amino acid from H to Y at position 356.
+The protein's natural variant, known as in GLC1F; uncertain pathological significance;, features a modification of the amino acid from R to H at position 360.
+The protein's natural variant, known as in GLC1F; uncertain pathological significance;, features a modification of the amino acid from S to G at position 440.
+The natural variant of this protein is characterized by an amino acid alteration from S to R at position 763.
+The protein's natural variant, known as in AFND;, features a modification of the amino acid from R to W at position 1163.
+The protein's natural variant, known as found in a patient with hereditary motor neuropathy; unknown pathological significance;, features a modification of the amino acid from K to N at position 39.
+The protein's natural variant, known as in CMT2K; dominant form;, features a modification of the amino acid from R to G at position 120.
+The protein's natural variant, known as in CMT4A; no effect on mitochondrial localization but impairment in the ability to induce mitochondrial fragmentation;, features a modification of the amino acid from R to Q at position 120.
+The protein's natural variant, known as in CMT2K; dominant form; no effect on mitochondrial localization;, features a modification of the amino acid from R to W at position 120.
+The protein's natural variant, known as in CMT2K; dominant form;;, features a modification of the amino acid from H to R at position 123.
+The protein's natural variant, known as in CMT2K; dominant form; unknown pathological significance;, features a modification of the amino acid from E to K at position 126.
+The protein's natural variant, known as in CMT2K; dominant form;, features a modification of the amino acid from A to G at position 156.
+The protein's natural variant, known as in CMT4A; no effect on mitochondrial localization but abolishes mitochondrial fission;, features a modification of the amino acid from R to H at position 161.
+The protein's natural variant, known as in CMT2K; dominant form; unknown pathological significance;, features a modification of the amino acid from Q to E at position 218.
+The protein's natural variant, known as in CMT2K; dominant form; unknown pathological significance;, features a modification of the amino acid from R to S at position 226.
+The protein's natural variant, known as in CMT2K; recessive form; unknown pathological significance;, features a modification of the amino acid from A to V at position 247.
+The protein's natural variant, known as in CMT2K; recessive form;, features a modification of the amino acid from H to R at position 256.
+The protein's natural variant, known as in CMTRIA; no effect on mitochondrial localization but impairment in the ability to induce mitochondrial fragmentation;, features a modification of the amino acid from R to C at position 282.
+The protein's natural variant, known as in CMT2K; recessive form;, features a modification of the amino acid from R to H at position 282.
+The protein's natural variant, known as in CMT2RV; Abolishes mitochondrial fission;, features a modification of the amino acid from R to Q at position 310.
+The protein's natural variant, known as in CMT2K; recessive form;, features a modification of the amino acid from R to W at position 310.
+The protein's natural variant, known as in KNDLRS;, features a modification of the amino acid from S to P at position 400.
+The protein's natural variant, known as in KNDLRS;, features a modification of the amino acid from W to R at position 559.
+The protein's natural variant, known as in CMH28; unknown pathological significance;, features a modification of the amino acid from A to V at position 321.
+The protein's natural variant, known as in CMH28; unknown pathological significance;, features a modification of the amino acid from G to R at position 351.
+The protein's natural variant, known as in CMH28; unknown pathological significance, features a modification of the amino acid from R to C at position 363.
+The protein's natural variant, known as in CMH28; unknown pathological significance, features a modification of the amino acid from K to R at position 371.
+The protein's natural variant, known as in CMH28; unknown pathological significance, features a modification of the amino acid from Q to H at position 383.
+The protein's natural variant, known as in CMH28; unknown pathological significance, features a modification of the amino acid from V to E at position 419.
+The protein's natural variant, known as in CMH28; unknown pathological significance, features a modification of the amino acid from P to L at position 440.
+The protein's natural variant, known as in CMH28; unknown pathological significance, features a modification of the amino acid from R to G at position 459.
+The protein's natural variant, known as in CMH28; unknown pathological significance, features a modification of the amino acid from R to G at position 462.
+The protein's natural variant, known as in CMH28; unknown pathological significance, features a modification of the amino acid from R to P at position 462.
+The protein's natural variant, known as in CMH28; unknown pathological significance;, features a modification of the amino acid from R to W at position 462.
+The protein's natural variant, known as in CMH28; unknown pathological significance;, features a modification of the amino acid from R to S at position 466.
+The protein's natural variant, known as in CMH28; unknown pathological significance;, features a modification of the amino acid from R to S at position 469.
+The protein's natural variant, known as in CMH28; unknown pathological significance;, features a modification of the amino acid from N to K at position 479.
+The protein's natural variant, known as in CMH28; unknown pathological significance;, features a modification of the amino acid from E to K at position 640.
+The protein's natural variant, known as in CMH28; unknown pathological significance, features a modification of the amino acid from G to C at position 653.
+The protein's natural variant, known as in CMH28; unknown pathological significance;, features a modification of the amino acid from A to T at position 657.
+The protein's natural variant, known as in CMH28; unknown pathological significance, features a modification of the amino acid from D to N at position 770.
+The protein's natural variant, known as in CMH28; unknown pathological significance, features a modification of the amino acid from P to L at position 865.
+The protein's natural variant, known as in CMH28; unknown pathological significance, features a modification of the amino acid from A to T at position 871.
+The protein's natural variant, known as in CMH28; unknown pathological significance, features a modification of the amino acid from R to Q at position 1194.
+The protein's natural variant, known as in CMH28; unknown pathological significance, features a modification of the amino acid from N to H at position 1356.
+The protein's natural variant, known as in CMH28; unknown pathological significance, features a modification of the amino acid from V to G at position 1376.
+The natural variant of this protein is characterized by an amino acid alteration from Q to R at position 920.
+The natural variant of this protein is characterized by an amino acid alteration from R to W at position 1954.
+The natural variant of this protein is characterized by an amino acid alteration from S to C at position 2290.
+The protein's natural variant, known as in a lung squamous cell carcinoma sample; somatic mutation, features a modification of the amino acid from E to D at position 2467.
+The protein's natural variant, known as in plasmid pCP301, features a modification of the amino acid from L to I at position 13.
+The protein's natural variant, known as in plasmid pMYSH6000 and plasmid pCP301, features a modification of the amino acid from L to S at position 143.
+The protein's natural variant, known as in strain: PA103 and CS32, features a modification of the amino acid from T to S at position 166.
+The protein's natural variant, known as in strain: PA103, features a modification of the amino acid from K to R at position 235.
+The protein's natural variant, known as in strain: DG1, features a modification of the amino acid from TDVRML to DLQACV at position 352.
+The protein's natural variant, known as in strain: PA103 and CS32, features a modification of the amino acid from E to Q at position 430.
+The protein's natural variant, known as in strain: PA103, features a modification of the amino acid from N to D at position 433.
+The protein's natural variant, known as in FABAS; in yeast, exhibits reduced ribosome binding, reduced levels of hypusination and transfected cells show impaired synthesis of proteins containing poly-proline tracts, features a modification of the amino acid from T to N at position 48.
+The protein's natural variant, known as in FABAS; in yeast, exhibits reduced ribosome binding and cells show impaired synthesis of proteins containing poly-proline tracts, features a modification of the amino acid from G to R at position 106.
+The protein's natural variant, known as in FABAS, features a modification of the amino acid from R to G at position 109.
+The protein's natural variant, known as in FABAS, features a modification of the amino acid from P to S at position 115.
+The protein's natural variant, known as in FABAS; in yeast, exhibits reduced ribosome binding and cells show impaired synthesis of proteins containing poly-proline tracts, features a modification of the amino acid from E to K at position 122.
+The natural variant of this protein is characterized by an amino acid alteration from P to T at position 158.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from V to M at position 713.
+The protein's natural variant, known as in SRTD5;, features a modification of the amino acid from L to P at position 7.
+The protein's natural variant, known as in SLSN8;, features a modification of the amino acid from A to P at position 30.
+The protein's natural variant, known as in SLSN8;, features a modification of the amino acid from V to D at position 68.
+The protein's natural variant, known as in SLSN8;, features a modification of the amino acid from G to E at position 109.
+The protein's natural variant, known as in SLSN8;, features a modification of the amino acid from R to C at position 272.
+The protein's natural variant, known as in NPHP13;, features a modification of the amino acid from V to G at position 345.
+The protein's natural variant, known as in SLSN8;, features a modification of the amino acid from D to H at position 493.
+The protein's natural variant, known as in CED4 and SLSN8;, features a modification of the amino acid from L to S at position 710.
+The protein's natural variant, known as in SLSN8;, features a modification of the amino acid from R to Q at position 1178.
+The protein's natural variant, known as in SLSN8;, features a modification of the amino acid from E to K at position 1235.
+The protein's natural variant, known as in SPGF72; unknown pathological significance; the mutant is absent from sperm neck and flagellum, features a modification of the amino acid from K to E at position 1271.
+The protein's natural variant, known as in strain: azole-resistant isolates, features a modification of the amino acid from A to V at position 351.
+The protein's natural variant, known as in strain: MA-6, features a modification of the amino acid from S to C at position 24.
+The protein's natural variant, known as in strain: MA-3, features a modification of the amino acid from D to N at position 57.
+The natural variant of this protein is characterized by an amino acid alteration from T to A at position 123.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from S to L at position 822.
+The protein's natural variant, known as in IMD89; unknown pathological significance; decreased protein expression compared to wild type when transfected in HEK293T cells, features a modification of the amino acid from R to C at position 420.
+The protein's natural variant, known as in BVVLS2; strong decrease in riboflavin transport; no effect on localization to plasma membrane; no effect on protein abundance;, features a modification of the amino acid from W to S at position 31.
+The protein's natural variant, known as in BVVLS2; decreased riboflavin transport;, features a modification of the amino acid from S to F at position 52.
+The protein's natural variant, known as in BVVLS2; strongly decreased riboflavin transport;, features a modification of the amino acid from L to P at position 123.
+The protein's natural variant, known as in BVVLS2; decreased riboflavin transport; no effect on localization to plasma membrane;, features a modification of the amino acid from P to T at position 141.
+The protein's natural variant, known as in BVVLS2; loss of riboflavin transport; loss of localization to plasma membrane; no effect on protein abundance;, features a modification of the amino acid from A to D at position 284.
+The protein's natural variant, known as in BVVLS2; decreased riboflavin transport; decreased localization to plasma membrane; no effect on protein abundance;, features a modification of the amino acid from Y to C at position 305.
+The protein's natural variant, known as in BVVLS2; decreased riboflavin transport; decreased localization to plasma membrane; no effect on protein abundance;, features a modification of the amino acid from G to R at position 306.
+The protein's natural variant, known as in BVVLS2; decreased riboflavin transport; decreased localization to plasma membrane; no effect on protein abundance;, features a modification of the amino acid from L to P at position 312.
+The protein's natural variant, known as in BVVLS2; loss of riboflavin transport; loss of localization to plasma membrane; no effect on protein abundance;, features a modification of the amino acid from L to P at position 339.
+The protein's natural variant, known as in BVVLS2; decreased riboflavin transport;, features a modification of the amino acid from G to S at position 419.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from G to C at position 6.
+The protein's natural variant, known as increases cell surface expression and NPS-dependent calcium mobilization; does not affect affinity for NPS.;, features a modification of the amino acid from N to I at position 107.
+The protein's natural variant, known as in allele NKG2-C*I01, features a modification of the amino acid from N to D at position 60.
+The natural variant of this protein is characterized by an amino acid alteration from A to P at position 79.
+The protein's natural variant, known as in MELAS;, features a modification of the amino acid from T to A at position 109.
+The natural variant of this protein is characterized by an amino acid alteration from T to P at position 109.
+The natural variant of this protein is characterized by an amino acid alteration from M to T at position 294.
+The protein's natural variant, known as in LDYT; possible rare primary mutation; decrease in enzyme activity;, features a modification of the amino acid from V to I at position 313.
+The protein's natural variant, known as in LHON; primary mutation; almost no vision recovery; most frequent mutation; seems to have no effect on electron transfer activity of the complex in inner mitochondrial membrane preparations;, features a modification of the amino acid from R to H at position 340.
+The protein's natural variant, known as detected in a patient with mitochondrial complex I deficiency; uncertain pathological significance;, features a modification of the amino acid from T to A at position 420.
+The protein's natural variant, known as found in a child with sporadic epilepsy; unknown pathological significance;, features a modification of the amino acid from R to H at position 327.
+The protein's natural variant, known as in ANXD2;, features a modification of the amino acid from D to Y at position 511.
+The protein's natural variant, known as in ANXD2;, features a modification of the amino acid from P to S at position 582.
+The protein's natural variant, known as in ANXD2;, features a modification of the amino acid from G to E at position 583.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from E to Q at position 675.
+The protein's natural variant, known as in strain: swamp breed, features a modification of the amino acid from N to S at position 34.
+The protein's natural variant, known as in strain: swamp breed, features a modification of the amino acid from E to K at position 61.
+The protein's natural variant, known as in strain: swamp breed, features a modification of the amino acid from Y to F at position 120.
+The protein's natural variant, known as in a Hurthle cell variant of papillary carcinoma sample;, features a modification of the amino acid from K to N at position 5.
+The protein's natural variant, known as in MC1DN28; reduced NDUFA13 protein level resulting in complex I instability;, features a modification of the amino acid from R to H at position 57.
+The protein's natural variant, known as in a Hurthle cell variant of papillary carcinoma sample, features a modification of the amino acid from R to P at position 115.
+The protein's natural variant, known as in HFE2B;, features a modification of the amino acid from R to G at position 59.
+The protein's natural variant, known as in HFE2B;, features a modification of the amino acid from C to R at position 70.
+The protein's natural variant, known as in HFE2B;, features a modification of the amino acid from G to D at position 71.
+The protein's natural variant, known as in HFE2B;, features a modification of the amino acid from C to Y at position 78.
+The protein's natural variant, known as found in a patient with intellectual disability and ataxia; unknown pathological significance;, features a modification of the amino acid from R to W at position 166.
+The protein's natural variant, known as in isozyme B, features a modification of the amino acid from I to T at position 5.
+The protein's natural variant, known as in strain: ECOR 28, ECOR 31, ECOR 37, ECOR 46, ECOR 50, ECOR 52, ECOR 60 and ECOR 71, features a modification of the amino acid from T to A at position 51.
+The protein's natural variant, known as in strain: ECOR 31, features a modification of the amino acid from E to K at position 70.
+The protein's natural variant, known as in strain: ECOR 37 and ECOR 71, features a modification of the amino acid from V to A at position 87.
+The protein's natural variant, known as in strain: ECOR 50, features a modification of the amino acid from P to PKP at position 102.
+The protein's natural variant, known as in strain: ECOR 28, features a modification of the amino acid from V to I at position 114.
+The protein's natural variant, known as in strain: ECOR 16, ECOR 31, ECOR 46, ECOR 50, ECOR 52 and ECOR 60, features a modification of the amino acid from L to P at position 133.
+The protein's natural variant, known as in strain: ECOR 60, features a modification of the amino acid from V to I at position 176.
+The protein's natural variant, known as in prostate cancer;, features a modification of the amino acid from E to A at position 152.
+The protein's natural variant, known as in HUPRAS;, features a modification of the amino acid from D to G at position 390.
+The protein's natural variant, known as found in a patient with primary congenital glaucoma; unknown pathological significance;, features a modification of the amino acid from V to M at position 23.
+The protein's natural variant, known as found in a patient with secondary congenital glaucoma associated with anterior segment dysgenesis and microphthalmia; unknown pathological significance;, features a modification of the amino acid from R to C at position 137.
+The protein's natural variant, known as found in patients with primary congenital glaucoma; unknown pathological significance; slightly increased transactivation activity on CXCR4 promoter; no effect on nuclear localization;, features a modification of the amino acid from N to S at position 234.
+The protein's natural variant, known as found in a patient with primary congenital glaucoma; unknown pathological significance; slightly increased transactivation activity on CXCR4 promoter; no effect on nuclear localization;, features a modification of the amino acid from G to E at position 475.
+The protein's natural variant, known as in RDCCAS;, features a modification of the amino acid from I to N at position 59.
+The protein's natural variant, known as in MCOPCB10; dramatic reduction in retinol binding; has greater affinity for the STRA6 receptor;, features a modification of the amino acid from A to T at position 73.
+The protein's natural variant, known as in MCOPCB10; dramatic reduction in retinol binding; has greater affinity for the STRA6 receptor;, features a modification of the amino acid from A to T at position 75.
+The protein's natural variant, known as in RDCCAS;, features a modification of the amino acid from G to D at position 93.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from G to S at position 8.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from V to A at position 127.
+The protein's natural variant, known as in strain: B, features a modification of the amino acid from M to L at position 165.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from T to M at position 7.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to C at position 252.
+The protein's natural variant, known as in CMT1G;, features a modification of the amino acid from I to N at position 43.
+The protein's natural variant, known as in CMT1G;, features a modification of the amino acid from T to P at position 51.
+The protein's natural variant, known as in CMT1G;, features a modification of the amino acid from I to T at position 52.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from C to R at position 257.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from Y to C at position 609.
+The natural variant of this protein is characterized by an amino acid alteration from S to L at position 71.
+The protein's natural variant, known as in strain: Isolate NL1, features a modification of the amino acid from Q to R at position 28.
+The protein's natural variant, known as in IMD82; constitutively active protein tyrosine kinase activity, features a modification of the amino acid from P to T at position 342.
+The protein's natural variant, known as in IMD82; constitutively active protein tyrosine kinase activity, features a modification of the amino acid from A to T at position 353.
+The protein's natural variant, known as in IMD82; constitutively active protein tyrosine kinase activity, features a modification of the amino acid from M to I at position 450.
+The protein's natural variant, known as in IMD82; constitutively active protein tyrosine kinase activity, features a modification of the amino acid from S to F at position 550.
+The protein's natural variant, known as in IMD82; constitutively active protein tyrosine kinase activity, features a modification of the amino acid from S to Y at position 550.
+The protein's natural variant, known as in LCA2;, features a modification of the amino acid from L to P at position 22.
+The protein's natural variant, known as in LCA2, features a modification of the amino acid from G to D at position 40.
+The protein's natural variant, known as in LCA2; reduced protein levels; decreased function in the retinoid cycle;, features a modification of the amino acid from G to S at position 40.
+The protein's natural variant, known as in LCA2; severely decreased retinol isomerase activity;, features a modification of the amino acid from R to Q at position 44.
+The protein's natural variant, known as in RP20;, features a modification of the amino acid from L to P at position 60.
+The protein's natural variant, known as in LCA2; unknown pathological significance;, features a modification of the amino acid from L to R at position 67.
+The protein's natural variant, known as in LCA2;, features a modification of the amino acid from H to Y at position 68.
+The protein's natural variant, known as in LCA2 and RP20, features a modification of the amino acid from F to V at position 70.
+The protein's natural variant, known as in RP20;, features a modification of the amino acid from Y to H at position 79.
+The protein's natural variant, known as in RP20; uncertain pathological significance;, features a modification of the amino acid from R to H at position 85.
+The protein's natural variant, known as in LCA2;, features a modification of the amino acid from R to P at position 91.
+The protein's natural variant, known as in LCA2; severely decreased retinol isomerase activity;, features a modification of the amino acid from R to Q at position 91.
+The protein's natural variant, known as in RP20 and LCA2; reduced protein levels; decreased function in the retinoid cycle;, features a modification of the amino acid from R to W at position 91.
+The protein's natural variant, known as in RP20;, features a modification of the amino acid from E to Q at position 95.
+The protein's natural variant, known as in LCA2; unknown pathological significance;, features a modification of the amino acid from V to I at position 99.
+The protein's natural variant, known as in LCA2; severely decreased retinol isomerase activity;, features a modification of the amino acid from T to I at position 101.
+The protein's natural variant, known as in RP20 and LCA2;, features a modification of the amino acid from E to K at position 102.
+The protein's natural variant, known as in LCA2; unknown pathological significance;, features a modification of the amino acid from R to S at position 118.
+The protein's natural variant, known as in RP20; unknown pathological significance;, features a modification of the amino acid from A to T at position 132.
+The protein's natural variant, known as in LCA2;, features a modification of the amino acid from Y to D at position 144.
+The protein's natural variant, known as in LCA2;, features a modification of the amino acid from E to D at position 148.
+The protein's natural variant, known as in LCA2; unknown pathological significance;, features a modification of the amino acid from T to P at position 162.
+The protein's natural variant, known as in RP20 and LCA2;, features a modification of the amino acid from D to Y at position 167.
+The protein's natural variant, known as in LCA2;, features a modification of the amino acid from H to N at position 182.
+The protein's natural variant, known as in LCA2;, features a modification of the amino acid from H to Y at position 182.
+The protein's natural variant, known as in LCA2 and RP20; severely decreased retinol isomerase activity;, features a modification of the amino acid from Y to D at position 239.
+The protein's natural variant, known as in LCA2;, features a modification of the amino acid from V to F at position 287.
+The protein's natural variant, known as in RP20; likely benign variant; very mild decrease of retinol isomerase activity;, features a modification of the amino acid from K to T at position 294.
+The protein's natural variant, known as in LCA2;, features a modification of the amino acid from H to R at position 313.
+The protein's natural variant, known as in LCA2; severely decreased retinol isomerase activity;, features a modification of the amino acid from Y to N at position 318.
+The protein's natural variant, known as no effect on retinol isomerase activity;, features a modification of the amino acid from N to K at position 321.
+The protein's natural variant, known as in LCA2;, features a modification of the amino acid from C to Y at position 330.
+The protein's natural variant, known as in LCA2; unknown pathological significance;, features a modification of the amino acid from G to R at position 333.
+The protein's natural variant, known as in RP20;, features a modification of the amino acid from L to S at position 341.
+The protein's natural variant, known as in LCA2;, features a modification of the amino acid from P to T at position 363.
+The protein's natural variant, known as in LCA2; unknown pathological significance;, features a modification of the amino acid from Y to C at position 368.
+The protein's natural variant, known as in RP20;, features a modification of the amino acid from Y to H at position 368.
+The protein's natural variant, known as in LCA2, features a modification of the amino acid from A to E at position 393.
+The protein's natural variant, known as in LCA2;, features a modification of the amino acid from A to G at position 393.
+The protein's natural variant, known as in LCA2; severely decreased retinol isomerase activity;, features a modification of the amino acid from L to P at position 408.
+The protein's natural variant, known as in LCA2;, features a modification of the amino acid from E to Q at position 417.
+The protein's natural variant, known as in LCA2;, features a modification of the amino acid from Y to C at position 431.
+The protein's natural variant, known as in LCA2; benign variant; no effect on retinol isomerase activity;, features a modification of the amino acid from A to V at position 434.
+The protein's natural variant, known as in LCA2;, features a modification of the amino acid from Y to C at position 435.
+The protein's natural variant, known as in RP20;, features a modification of the amino acid from G to V at position 436.
+The protein's natural variant, known as in LCA2; unknown pathological significance;, features a modification of the amino acid from V to A at position 443.
+The protein's natural variant, known as in RP20;, features a modification of the amino acid from V to G at position 452.
+The protein's natural variant, known as in LCA2;, features a modification of the amino acid from P to L at position 470.
+The protein's natural variant, known as in RP20;, features a modification of the amino acid from V to D at position 473.
+The protein's natural variant, known as in RP87; unknown pathological significance; does not affect protein abundance; does not affect subcellular localization; does not affect isomerization activity; may cause abnormal splicing mRNAs thereby decreasing protein levels;, features a modification of the amino acid from D to G at position 477.
+The protein's natural variant, known as in RP20;, features a modification of the amino acid from R to W at position 515.
+The protein's natural variant, known as in RP20;, features a modification of the amino acid from G to V at position 528.
+The protein's natural variant, known as in LCA2; unknown pathological significance;, features a modification of the amino acid from S to T at position 533.
+The protein's natural variant, known as in strain: HFL97e3_15, features a modification of the amino acid from S to N at position 194.
+The protein's natural variant, known as in strain: ZIM(S)e3_24, features a modification of the amino acid from S to T at position 252.
+The protein's natural variant, known as in strain: SC96e3_12.3 and ZIM(S)e3_35, features a modification of the amino acid from S to N at position 380.
+The protein's natural variant, known as in strain: DPF96e3_23.1, SC96e3_12.3, HFL97e3_8, HFL97e3_12, HFL97e3_16, ZIM(S)e3_24 and ZIM(S)e3_35, features a modification of the amino acid from S to N at position 484.
+The protein's natural variant, known as in strain: DPF96e3_23.1, SC96e3_12.3, HFL97e3_8, HFL97e3_12, HFL97e3_16 and ZIM(S)e3_24, features a modification of the amino acid from L to I at position 486.
+The protein's natural variant, known as in strain: BFM/2Msf, C57BL/10SnJ and pgn2, features a modification of the amino acid from G to S at position 46.
+The protein's natural variant, known as in strain: BFM/2Msf, C57BL/10SnJ and pgn2, features a modification of the amino acid from A to G at position 50.
+The protein's natural variant, known as in strain: CAST/Ei, features a modification of the amino acid from P to A at position 62.
+The protein's natural variant, known as in strain: BFM/2Msf and C57BL/10SnJ, features a modification of the amino acid from H to Q at position 150.
+The protein's natural variant, known as in strain: pgn2, features a modification of the amino acid from R to H at position 214.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from AL to SF at position 112.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from D to G at position 329.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from V to M at position 335.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from T to I at position 444.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from N to S at position 697.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from A to S at position 814.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from K to M at position 816.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from A to T at position 930.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from H to Q at position 963.
+The protein's natural variant, known as in strain: SK1, features a modification of the amino acid from S to C at position 969.
+The protein's natural variant, known as in alpha-2, features a modification of the amino acid from N to H at position 21.
+The protein's natural variant, known as in ts ET12; a temperature-sensitive mutant; cells undergo apoptosis 48 hours after a temperature-shift to 39.5 degrees Celsius, features a modification of the amino acid from G to R at position 321.
+The protein's natural variant, known as in NPHP15;, features a modification of the amino acid from Q to P at position 11.
+The protein's natural variant, known as in NPHP15;, features a modification of the amino acid from R to W at position 93.
+The protein's natural variant, known as in HLS1; altered subcellular localization, becomes localized to nuclear structures;, features a modification of the amino acid from D to G at position 211.
+The protein's natural variant, known as it may act as a disease modifier preserving from severe HLPP1D when associated with R-68 or F-89; results in increased GPIHBP1 expression at the cell surface; does not affect interaction with LPL when associated in cis with R-68 in one individual;, features a modification of the amino acid from F to C at position 14.
+The protein's natural variant, known as no discernible effect on interaction with LPL, chylomicrons or APOA5;, features a modification of the amino acid from G to R at position 56.
+The protein's natural variant, known as in HLPP1D; does not affect protein expression at the cell surface; does not interact with LPL; promotes formation of dimers and oligomers severely reducing number of monomers;, features a modification of the amino acid from C to S at position 65.
+The protein's natural variant, known as in HLPP1D; does not interact with LPL; promotes formation of dimers and oligomers severely reducing number of monomers;, features a modification of the amino acid from C to Y at position 65.
+The protein's natural variant, known as in HLPP1D; does not affect protein expression at the cell surface; does not interact with LPL; promotes formation of dimers and oligomers reducing number of monomers;, features a modification of the amino acid from C to G at position 68.
+The protein's natural variant, known as in HLPP1D; unknown pathological significance; results in decreased GPIHBP1 expression; promotes formation of dimers and oligomers severely reducing number of monomers; does not affect interaction with LPL when associated in cis with F-14 in one individual;, features a modification of the amino acid from C to R at position 68.
+The protein's natural variant, known as in HLPP1D; does not interact with LPL; promotes formation of dimers and oligomers severely reducing number of monomers, features a modification of the amino acid from C to Y at position 68.
+The protein's natural variant, known as in HLPP1D, features a modification of the amino acid from C to R at position 83.
+The protein's natural variant, known as in HLPP1D; drastically affects interaction with LPL; promotes formation of dimers and oligomers reducing number of monomers;, features a modification of the amino acid from C to F at position 89.
+The protein's natural variant, known as in HLPP1D; does not interact with LPL; promotes formation of dimers and oligomers reducing number of monomers, features a modification of the amino acid from T to R at position 108.
+The protein's natural variant, known as in HLPP1D; a patient with chylomicronemia; no effect on protein expression at the cell surface; loss of interaction with LPL; loss of interaction with chylomicrons; promotes formation of dimers and oligomers reducing number of monomers;, features a modification of the amino acid from Q to P at position 115.
+The protein's natural variant, known as in HLPP1D;, features a modification of the amino acid from S to F at position 144.
+The protein's natural variant, known as in HLPP1D; affects protein expression at the cell surface; reduces interaction with LPL;, features a modification of the amino acid from G to R at position 175.
+The protein's natural variant, known as in strain: 1014 and 418, features a modification of the amino acid from VGC to ARH at position 4.
+The protein's natural variant, known as in strain: 1014 and 418, features a modification of the amino acid from L to F at position 31.
+The protein's natural variant, known as in strain: 418, features a modification of the amino acid from P to L at position 68.
+The protein's natural variant, known as in strain: 1014, features a modification of the amino acid from P to S at position 75.
+The protein's natural variant, known as in strain: 1014 and 418, features a modification of the amino acid from S to P at position 84.
+The protein's natural variant, known as in strain: 418, features a modification of the amino acid from A to E at position 87.
+The protein's natural variant, known as in strain: 1014, features a modification of the amino acid from A to V at position 87.
+The protein's natural variant, known as in strain: 1014 and 418, features a modification of the amino acid from H to R at position 102.
+The protein's natural variant, known as in strain: 418, features a modification of the amino acid from V to I at position 105.
+The protein's natural variant, known as in strain: 418, features a modification of the amino acid from I to V at position 115.
+The protein's natural variant, known as in strain: 418, features a modification of the amino acid from T to N at position 125.
+The protein's natural variant, known as in strain: 418, features a modification of the amino acid from L to V at position 130.
+The protein's natural variant, known as in strain: 418, features a modification of the amino acid from C to R at position 135.
+The protein's natural variant, known as in strain: 1014, features a modification of the amino acid from Q to R at position 147.
+The protein's natural variant, known as in strain: 1014, features a modification of the amino acid from K to E at position 151.
+The protein's natural variant, known as in strain: 418, features a modification of the amino acid from N to T at position 152.
+The protein's natural variant, known as in strain: 418, features a modification of the amino acid from A to S at position 174.
+The protein's natural variant, known as in strain: 418, features a modification of the amino acid from T to I at position 188.
+The protein's natural variant, known as in strain: 1014, features a modification of the amino acid from C to G at position 194.
+The protein's natural variant, known as in strain: 418, features a modification of the amino acid from C to GSG at position 194.
+The protein's natural variant, known as in strain: 418, features a modification of the amino acid from T to P at position 198.
+The protein's natural variant, known as in strain: 1014 and 418, features a modification of the amino acid from T to A at position 204.
+The protein's natural variant, known as in strain: 1014 and 418, features a modification of the amino acid from Y to F at position 218.
+The protein's natural variant, known as in strain: 1014, features a modification of the amino acid from S to R at position 228.
+The protein's natural variant, known as in strain: 418, features a modification of the amino acid from M to T at position 229.
+The protein's natural variant, known as in strain: 1014, features a modification of the amino acid from I to V at position 230.
+The protein's natural variant, known as in strain: 418, features a modification of the amino acid from TD to AN at position 238.
+The protein's natural variant, known as in strain: 418, features a modification of the amino acid from A to E at position 241.
+The protein's natural variant, known as in strain: 1014 and 418, features a modification of the amino acid from G to V at position 243.
+The protein's natural variant, known as in strain: 1014 and 418, features a modification of the amino acid from A to S at position 253.
+The protein's natural variant, known as in strain: 1014, features a modification of the amino acid from A to R at position 255.
+The protein's natural variant, known as in strain: 1014 and 418, features a modification of the amino acid from K to Q at position 259.
+The protein's natural variant, known as in strain: 1014 and 418, features a modification of the amino acid from A to V at position 275.
+The protein's natural variant, known as in CILD26; unknown pathological significance; hypomorphic mutation;, features a modification of the amino acid from D to G at position 141.
+The protein's natural variant, known as rare variant detected in patients with Gaucher disease type 1;, features a modification of the amino acid from E to K at position 74.
+The protein's natural variant, known as common variant detected in patients with Gaucher disease type 1 as well as healthy individuals; slightly reduced activity towards 4-methylumbelliferyl-chitotrioside but no effect on activity towards 4-methylumbelliferyl-deoxychitobioside;, features a modification of the amino acid from G to S at position 102.
+The natural variant of this protein is characterized by an amino acid alteration from S to V at position 2.
+The protein's natural variant, known as in DEE44; reduces UFM1 activating enzyme activity;, features a modification of the amino acid from R to H at position 55.
+The protein's natural variant, known as in DEE44; reduces UFM1 activating enzyme activity; reduces UFM1-DDRGK1 formation;, features a modification of the amino acid from M to V at position 57.
+The protein's natural variant, known as in DEE44; abolishes UFM1 activating enzyme activity;, features a modification of the amino acid from G to E at position 168.
+The protein's natural variant, known as in DEE44; reduces UFM1 activating enzyme activity;, features a modification of the amino acid from V to M at position 260.
+The protein's natural variant, known as in SCAR24; does not affect cytoplasm localization; decreases protein stability; does not affect interaction with UFM1;, features a modification of the amino acid from K to E at position 310.
+The protein's natural variant, known as in DEE44; reduces UFM1 activating enzyme activity; reduces UFM1 activating enzyme activity; reduces UFM1-DDRGK1 formation;, features a modification of the amino acid from A to T at position 371.
+The protein's natural variant, known as in DEE44; no effect on UFM1 activating enzyme activity;, features a modification of the amino acid from D to Y at position 389.
+The protein's natural variant, known as in strain: HB101, features a modification of the amino acid from V to I at position 126.
+The protein's natural variant, known as in strain: HB101, features a modification of the amino acid from M to I at position 160.
+The protein's natural variant, known as in strain: HB101, features a modification of the amino acid from G to S at position 239.
+The protein's natural variant, known as in PCH15; in knockdown cells, unable to rescue higher intron retention levels and to restore normal cell viability, contrary to wild-type; reduced protein levels in homozygous patient's fibroblasts compared to heterozygous or wild-type cells;, features a modification of the amino acid from F to C at position 502.
+The protein's natural variant, known as in GPIBD17; decreased expression of GPI-anchored proteins, including FCGR3B/CD16B and CD55, in patient's granulocytes;, features a modification of the amino acid from S to P at position 103.
+The protein's natural variant, known as in ahl5, features a modification of the amino acid from G to R at position 115.
+The protein's natural variant, known as in a patient with amyotrophic lateral sclerosis;, features a modification of the amino acid from G to D at position 188.
+The protein's natural variant, known as in Api m 6.02 and Api m 6.04, features a modification of the amino acid from G to LPG at position 92.
+The natural variant of this protein is characterized by an amino acid alteration from L to K at position 62.
+The natural variant of this protein is characterized by an amino acid alteration from D to V at position 89.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 264.
+The protein's natural variant, known as in PARK19B; patient fibroblasts show decreased levels of the protein;, features a modification of the amino acid from R to G at position 870.
+The protein's natural variant, known as in strain: cv. Sorbo, features a modification of the amino acid from V to G at position 10.
+The protein's natural variant, known as in strain: cv. Ema-1 and cv. Pla-0, features a modification of the amino acid from N to K at position 42.
+The protein's natural variant, known as in strain: cv. Sorbo, features a modification of the amino acid from A to T at position 44.
+The protein's natural variant, known as in strain: cv. Sorbo, features a modification of the amino acid from N to T at position 505.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from A to E at position 386.
+The protein's natural variant, known as may be associated with susceptibility to dyslexia;, features a modification of the amino acid from A to T at position 311.
+The protein's natural variant, known as in FFEVF4; loss of localization at the cell surface, features a modification of the amino acid from L to P at position 247.
+The protein's natural variant, known as in FFEVF4; affects voltage-dependent sodium channel activity; smaller current density and slower activation compared to wild-type channels and increased current activation in response to depolarizing voltage ramps;, features a modification of the amino acid from R to Q at position 357.
+The natural variant of this protein is characterized by an amino acid alteration from S to T at position 606.
+The protein's natural variant, known as in FFEVF4; unknown pathological significance; increased current activation in response to depolarizing voltage ramps;, features a modification of the amino acid from D to N at position 815.
+The protein's natural variant, known as in DEE62; prominent gain of channel function, with markedly increased amplitude of the slowly inactivating current component and a leftward shift in the voltage dependence of activation to more hyperpolarized potentials;, features a modification of the amino acid from I to T at position 875.
+The protein's natural variant, known as in FFEVF4; affects voltage-dependent sodium channel activity; increased level of persistent sodium current compared to wild-type channels and increased current activation in response to depolarizing voltage ramps;, features a modification of the amino acid from E to K at position 1160.
+The protein's natural variant, known as in DEE62; prominent gain of channel function, with markedly increased amplitude of the slowly inactivating current component and a leftward shift in the voltage dependence of activation to more hyperpolarized potentials;, features a modification of the amino acid from P to L at position 1333.
+The protein's natural variant, known as in FFEVF4; unknown pathological significance; increased current activation in response to depolarizing voltage ramps;, features a modification of the amino acid from M to V at position 1372.
+The protein's natural variant, known as in DEE62; unknown pathological significance; no gain of function in channel activity; channel recovery from inactivation is more rapid than that of wild-type channel;, features a modification of the amino acid from R to C at position 1642.
+The protein's natural variant, known as in DEE62; prominent gain of channel function, with markedly increased amplitude of the slowly inactivating current component;, features a modification of the amino acid from V to A at position 1769.
+The protein's natural variant, known as in DEE62; unknown pathological significance; no gain of function in channel activity;, features a modification of the amino acid from K to Q at position 1799.
+The natural variant of this protein is characterized by an amino acid alteration from L to S at position 1813.
+The protein's natural variant, known as in strain: RAY-3AD, features a modification of the amino acid from V to A at position 113.
+The protein's natural variant, known as in strain: RAY-3AD, features a modification of the amino acid from T to S at position 117.
+The protein's natural variant, known as in strain: RAY-3AD, features a modification of the amino acid from S to STAAAVSQITDGQVQAAKSTAAAASQISDGQVQAAKS at position 144.
+The natural variant of this protein is characterized by an amino acid alteration from Y to D at position 194.
+The natural variant of this protein is characterized by an amino acid alteration from S to A at position 545.
+The natural variant of this protein is characterized by an amino acid alteration from I to S at position 838.
+The protein's natural variant, known as in strain: Pasteur, features a modification of the amino acid from K to Q at position 655.
+The protein's natural variant, known as in MASTC; unknown pathological significance, features a modification of the amino acid from S to C at position 451.
+The protein's natural variant, known as in MASTC; unknown pathological significance;, features a modification of the amino acid from A to D at position 533.
+The protein's natural variant, known as in GIST; somatic mutation, features a modification of the amino acid from K to I at position 550.
+The protein's natural variant, known as in GIST;, features a modification of the amino acid from V to A at position 559.
+The protein's natural variant, known as in GIST; somatic mutation;, features a modification of the amino acid from V to D at position 559.
+The protein's natural variant, known as in PBT;, features a modification of the amino acid from E to K at position 583.
+The protein's natural variant, known as in PBT;, features a modification of the amino acid from F to C at position 584.
+The protein's natural variant, known as in PBT;, features a modification of the amino acid from F to L at position 584.
+The protein's natural variant, known as in PBT, features a modification of the amino acid from G to R at position 601.
+The protein's natural variant, known as in PBT, features a modification of the amino acid from L to P at position 656.
+The protein's natural variant, known as in PBT;, features a modification of the amino acid from G to R at position 664.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from D to N at position 737.
+The protein's natural variant, known as in PBT;, features a modification of the amino acid from R to G at position 791.
+The protein's natural variant, known as in PBT; with sensorineural deafness;, features a modification of the amino acid from R to G at position 796.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from R to W at position 804.
+The protein's natural variant, known as in PBT, features a modification of the amino acid from G to V at position 812.
+The protein's natural variant, known as in MASTC; sporadic case; somatic mutation; requires 2 nucleotide substitutions; constitutively activated and is much more rapidly autophosphorylated than wild type, features a modification of the amino acid from D to F at position 816.
+The protein's natural variant, known as in a testicular tumor; seminoma; somatic mutation; constitutively activated;, features a modification of the amino acid from D to H at position 816.
+The protein's natural variant, known as in MASTC; somatic mutation; constitutively activated; requires 2 nucleotide substitutions;, features a modification of the amino acid from D to I at position 816.
+The protein's natural variant, known as in MASTSYS, MASTC and mast cell leukemia; somatic mutation; constitutively activated; loss of interaction with MPDZ;, features a modification of the amino acid from D to V at position 816.
+The protein's natural variant, known as in MASTSYS and MASTC; also found in acute myeloid leukemia and a germ cell tumor of the testis; somatic mutation; constitutively activated;, features a modification of the amino acid from D to Y at position 816.
+The protein's natural variant, known as in mast cell disease; systemic;, features a modification of the amino acid from D to G at position 820.
+The protein's natural variant, known as in MASTC; constitutively activated;, features a modification of the amino acid from N to I at position 822.
+The protein's natural variant, known as in a germ cell tumor of the testis; somatic mutation;, features a modification of the amino acid from N to K at position 822.
+The protein's natural variant, known as in a germ cell tumor of the testis; somatic mutation;, features a modification of the amino acid from A to P at position 829.
+The protein's natural variant, known as in MASTC; sporadic case; somatic mutation; dominant negative mutation; loss of autophosphorylation;, features a modification of the amino acid from E to K at position 839.
+The protein's natural variant, known as in PBT;, features a modification of the amino acid from T to P at position 847.
+The protein's natural variant, known as increased glucuronosyltransferase activity towards calcidiol;, features a modification of the amino acid from L to V at position 48.
+The protein's natural variant, known as in OCCM;, features a modification of the amino acid from G to R at position 350.
+The protein's natural variant, known as in RP33, features a modification of the amino acid from C to R at position 502.
+The protein's natural variant, known as in RP33;, features a modification of the amino acid from A to V at position 542.
+The protein's natural variant, known as in RP33;, features a modification of the amino acid from R to C at position 681.
+The protein's natural variant, known as in RP33;, features a modification of the amino acid from R to H at position 681.
+The protein's natural variant, known as in RP33, features a modification of the amino acid from P to S at position 682.
+The protein's natural variant, known as in RP33; unknown pathological significance;, features a modification of the amino acid from V to L at position 683.
+The protein's natural variant, known as in RP33, features a modification of the amino acid from Y to C at position 689.
+The protein's natural variant, known as in RP33;, features a modification of the amino acid from I to V at position 698.
+The protein's natural variant, known as in RP33;, features a modification of the amino acid from Q to E at position 885.
+The protein's natural variant, known as in RP33; strongly reduced RNA helicase activity;, features a modification of the amino acid from S to L at position 1087.
+The protein's natural variant, known as in RP33;, features a modification of the amino acid from R to L at position 1090.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from F to L at position 1736.
+The protein's natural variant, known as in RP33;, features a modification of the amino acid from R to H at position 1779.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from I to C at position 567.
+The protein's natural variant, known as in EDMD7; the mutant protein forms predominantly monomers with very few dimers indicating a defect in oligomerization; overexpression in HeLa cells results in abnormal nuclear structures and decreased nuclear localization of both EMD and SUN2 with mislocalization of EMD to the endoplasmic reticulum;, features a modification of the amino acid from E to K at position 85.
+The protein's natural variant, known as in EDMD7; the mutant protein is able to form oligomers; overexpression in HeLa cells results in abnormal nuclear structures and decreased nuclear localization of both EMD and SUN2 with mislocalization of EMD to the endoplasmic reticulum;, features a modification of the amino acid from I to V at position 91.
+The protein's natural variant, known as in ARVD5;, features a modification of the amino acid from S to L at position 358.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from E to K at position 29.
+The protein's natural variant, known as reduced affinity for MRLC and impairs cortical migration;, features a modification of the amino acid from R to W at position 828.
+The protein's natural variant, known as in strain: SPRET/Ei, features a modification of the amino acid from S to A at position 321.
+The protein's natural variant, known as in MCOP6;, features a modification of the amino acid from R to G at position 176.
+The protein's natural variant, known as in MCOP6;, features a modification of the amino acid from G to R at position 237.
+The protein's natural variant, known as in MCOP6;, features a modification of the amino acid from V to F at position 302.
+The protein's natural variant, known as in MCOP6;, features a modification of the amino acid from W to S at position 309.
+The protein's natural variant, known as in MCOP6;, features a modification of the amino acid from G to R at position 320.
+The protein's natural variant, known as in MCOP6;, features a modification of the amino acid from C to R at position 395.
+The protein's natural variant, known as in MCOP6;, features a modification of the amino acid from P to A at position 599.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from V to I at position 441.
+The protein's natural variant, known as in allele ALS5-2, features a modification of the amino acid from I to L at position 2.
+The protein's natural variant, known as in allele ALS5-2, features a modification of the amino acid from K to R at position 311.
+The protein's natural variant, known as in allele ALS5-2, features a modification of the amino acid from E to K at position 406.
+The protein's natural variant, known as in allele ALS5-1, features a modification of the amino acid from S to SESYATTETITTGPLGTDSVIIKEPHNPTVTTTVFWS at position 481.
+The protein's natural variant, known as in allele ALS5-1, features a modification of the amino acid from N to T at position 492.
+The protein's natural variant, known as in allele ALS5-1, features a modification of the amino acid from E to L at position 495.
+The protein's natural variant, known as in allele ALS5-1, features a modification of the amino acid from VR to IK at position 503.
+The protein's natural variant, known as in allele ALS5-1, features a modification of the amino acid from E to K at position 514.
+The protein's natural variant, known as in allele ALS5-1, features a modification of the amino acid from V to I at position 526.
+The protein's natural variant, known as in allele ALS5-1, features a modification of the amino acid from K to R at position 539.
+The protein's natural variant, known as in allele ALS5-2, features a modification of the amino acid from H to Y at position 542.
+The protein's natural variant, known as in allele ALS5-2, features a modification of the amino acid from A to T at position 1167.
+The protein's natural variant, known as in allele ALS5-2, features a modification of the amino acid from T to N at position 1202.
+The protein's natural variant, known as in allele ALS5-1, features a modification of the amino acid from AQV to SEA at position 1269.
+The protein's natural variant, known as in allele ALS5-2, features a modification of the amino acid from N to S at position 1271.
+The protein's natural variant, known as in allele ALS5-2, features a modification of the amino acid from L to S at position 1273.
+The protein's natural variant, known as in allele ALS5-2, features a modification of the amino acid from S to L at position 1278.
+The protein's natural variant, known as in allele ALS5-2, features a modification of the amino acid from M to T at position 1283.
+The protein's natural variant, known as in allele ALS5-2, features a modification of the amino acid from I to M at position 1291.
+The protein's natural variant, known as in a renal clear cell carcinoma sample; somatic mutation, features a modification of the amino acid from T to N at position 36.
+The protein's natural variant, known as in a gastric adenocarcinoma sample; somatic mutation, features a modification of the amino acid from A to T at position 161.
+The protein's natural variant, known as impairs interaction with calmodulin;, features a modification of the amino acid from I to N at position 393.
+The protein's natural variant, known as in CRS3;, features a modification of the amino acid from L to R at position 483.
+The protein's natural variant, known as in CRS3, features a modification of the amino acid from L to P at position 600.
+The protein's natural variant, known as in CRS3;, features a modification of the amino acid from Q to E at position 614.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from S to P at position 312.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation, features a modification of the amino acid from T to N at position 538.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation, features a modification of the amino acid from V to I at position 604.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation;, features a modification of the amino acid from G to S at position 704.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from L to P at position 280.
+The protein's natural variant, known as in strain: RM 7004, features a modification of the amino acid from I to V at position 221.
+The protein's natural variant, known as in strain: RM 7004, features a modification of the amino acid from I to V at position 229.
+The protein's natural variant, known as in strain: RM 7004, features a modification of the amino acid from E to D at position 334.
+The protein's natural variant, known as in EIG15;, features a modification of the amino acid from L to P at position 84.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from F to L at position 250.
+The protein's natural variant, known as in H-type BSE, features a modification of the amino acid from E to K at position 211.
+The natural variant of this protein is characterized by an amino acid alteration from D to DA at position 414.
+The protein's natural variant, known as in CPS1D, features a modification of the amino acid from A to V at position 43.
+The protein's natural variant, known as in CPS1D, features a modification of the amino acid from G to D at position 58.
+The protein's natural variant, known as in CPS1D;, features a modification of the amino acid from S to F at position 65.
+The protein's natural variant, known as in CPS1D, features a modification of the amino acid from V to G at position 71.
+The protein's natural variant, known as in CPS1D;, features a modification of the amino acid from G to E at position 79.
+The protein's natural variant, known as in CPS1D;, features a modification of the amino acid from P to S at position 87.
+The protein's natural variant, known as in CPS1D, features a modification of the amino acid from Y to D at position 89.
+The protein's natural variant, known as in CPS1D; modestly decreases enzyme activity, features a modification of the amino acid from S to F at position 123.
+The protein's natural variant, known as in CPS1D; unknown pathological significance, features a modification of the amino acid from S to Y at position 123.
+The protein's natural variant, known as in CPS1D, features a modification of the amino acid from D to G at position 165.
+The protein's natural variant, known as in CPS1D; unknown pathological significance;, features a modification of the amino acid from R to W at position 174.
+The protein's natural variant, known as in CPS1D, features a modification of the amino acid from Y to N at position 212.
+The protein's natural variant, known as in CPS1D, features a modification of the amino acid from D to V at position 224.
+The protein's natural variant, known as in CPS1D;, features a modification of the amino acid from R to C at position 233.
+The protein's natural variant, known as in CPS1D;, features a modification of the amino acid from H to P at position 243.
+The protein's natural variant, known as in CPS1D, features a modification of the amino acid from G to E at position 258.
+The protein's natural variant, known as in CPS1D;, features a modification of the amino acid from G to E at position 263.
+The protein's natural variant, known as in CPS1D;, features a modification of the amino acid from K to N at position 280.
+The protein's natural variant, known as in CPS1D;, features a modification of the amino acid from G to E at position 301.
+The protein's natural variant, known as in CPS1D; associated with T-986;, features a modification of the amino acid from A to V at position 304.
+The protein's natural variant, known as in CPS1D;, features a modification of the amino acid from G to E at position 317.
+The protein's natural variant, known as in CPS1D; modestly decreases enzyme activity;, features a modification of the amino acid from H to R at position 337.
+The protein's natural variant, known as in CPS1D, features a modification of the amino acid from L to S at position 341.
+The protein's natural variant, known as no negative effect on protein stability, enzyme activity and thermal stability;, features a modification of the amino acid from T to A at position 344.
+The protein's natural variant, known as in CPS1D; around 80% decrease in enzyme activity; significant reduction in thermal stability; approximately 4-fold decrease in the apparent Vmax for ATP, bicarbonate and ammonia;, features a modification of the amino acid from N to D at position 355.
+The protein's natural variant, known as in CPS1D;, features a modification of the amino acid from D to H at position 358.
+The protein's natural variant, known as in CPS1D;, features a modification of the amino acid from P to L at position 382.
+The protein's natural variant, known as in CPS1D; around 40% decrease in enzyme activity; significant loss of thermal stability, features a modification of the amino acid from Y to C at position 389.
+The protein's natural variant, known as in CPS1D; significant loss of protein stability, features a modification of the amino acid from L to R at position 390.
+The protein's natural variant, known as in CPS1D; unknown pathological significance; associated with N-937 in a patient;, features a modification of the amino acid from G to R at position 401.
+The protein's natural variant, known as in CPS1D;, features a modification of the amino acid from G to R at position 431.
+The protein's natural variant, known as in CPS1D, features a modification of the amino acid from G to V at position 432.
+The protein's natural variant, known as in CPS1D; almost complete loss of enzyme activity;, features a modification of the amino acid from A to P at position 438.
+The protein's natural variant, known as in CPS1D;, features a modification of the amino acid from A to T at position 438.
+The protein's natural variant, known as in CPS1D, features a modification of the amino acid from K to E at position 450.
+The protein's natural variant, known as in CPS1D;, features a modification of the amino acid from V to G at position 457.
+The protein's natural variant, known as in CPS1D, features a modification of the amino acid from T to N at position 471.
+The protein's natural variant, known as in CPS1D, features a modification of the amino acid from A to P at position 498.
+The protein's natural variant, known as found in a patient with VACTERL syndrome and postsurgical PHN; unknown pathological significance;, features a modification of the amino acid from G to V at position 530.
+The protein's natural variant, known as in CPS1D, features a modification of the amino acid from V to E at position 531.
+The protein's natural variant, known as in CPS1D, features a modification of the amino acid from V to G at position 531.
+The protein's natural variant, known as in CPS1D; almost complete loss of enzyme activity; approximately 60-fold increase in the apparent Km for bicarbonate and approximately 4-fold respective decrease and increase in the apparent Vmax and Km for ammonia;, features a modification of the amino acid from T to M at position 544.
+The protein's natural variant, known as in CPS1D;, features a modification of the amino acid from R to C at position 587.
+The protein's natural variant, known as in CPS1D;, features a modification of the amino acid from R to H at position 587.
+The protein's natural variant, known as in CPS1D, features a modification of the amino acid from R to L at position 587.
+The protein's natural variant, known as in CPS1D;, features a modification of the amino acid from A to T at position 589.
+The protein's natural variant, known as in CPS1D;, features a modification of the amino acid from G to R at position 593.
+The protein's natural variant, known as in CPS1D, features a modification of the amino acid from S to L at position 597.
+The protein's natural variant, known as in CPS1D;, features a modification of the amino acid from V to M at position 622.
+The protein's natural variant, known as in CPS1D;, features a modification of the amino acid from G to D at position 628.
+The protein's natural variant, known as in CPS1D;, features a modification of the amino acid from I to R at position 632.
+The protein's natural variant, known as in CPS1D;, features a modification of the amino acid from R to P at position 638.
+The protein's natural variant, known as in CPS1D;, features a modification of the amino acid from A to S at position 640.
+The protein's natural variant, known as in CPS1D, features a modification of the amino acid from C to Y at position 648.
+The protein's natural variant, known as in CPS1D, features a modification of the amino acid from E to K at position 651.
+The protein's natural variant, known as in CPS1D, features a modification of the amino acid from D to V at position 654.
+The protein's natural variant, known as in CPS1D, features a modification of the amino acid from G to R at position 661.
+The protein's natural variant, known as in CPS1D, features a modification of the amino acid from N to I at position 674.
+The protein's natural variant, known as in CPS1D;, features a modification of the amino acid from N to K at position 674.
+The protein's natural variant, known as in CPS1D; results in a poor enzyme expression and solubility; hampers correct enzyme folding, features a modification of the amino acid from Q to P at position 678.
+The protein's natural variant, known as in CPS1D, features a modification of the amino acid from N to S at position 698.
+The protein's natural variant, known as in CPS1D;, features a modification of the amino acid from N to K at position 716.
+The protein's natural variant, known as in CPS1D, features a modification of the amino acid from R to K at position 718.
+The protein's natural variant, known as in CPS1D;, features a modification of the amino acid from R to Q at position 721.
+The protein's natural variant, known as in CPS1D, features a modification of the amino acid from A to P at position 724.
+The protein's natural variant, known as in CPS1D, features a modification of the amino acid from A to T at position 726.
+The protein's natural variant, known as in CPS1D, features a modification of the amino acid from D to V at position 767.
+The protein's natural variant, known as in CPS1D; the enzyme is inactive, features a modification of the amino acid from P to L at position 774.
+The protein's natural variant, known as in CPS1D;, features a modification of the amino acid from R to H at position 780.
+The protein's natural variant, known as in CPS1D;, features a modification of the amino acid from M to I at position 792.
+The protein's natural variant, known as in CPS1D;, features a modification of the amino acid from R to C at position 803.
+The protein's natural variant, known as in CPS1D;, features a modification of the amino acid from R to G at position 803.
+The protein's natural variant, known as in CPS1D;, features a modification of the amino acid from R to S at position 803.
+The protein's natural variant, known as in CPS1D;, features a modification of the amino acid from F to L at position 805.
+The protein's natural variant, known as in CPS1D, features a modification of the amino acid from F to S at position 805.
+The protein's natural variant, known as in CPS1D;, features a modification of the amino acid from Q to R at position 810.
+The protein's natural variant, known as in CPS1D;, features a modification of the amino acid from R to W at position 814.
+The protein's natural variant, known as in CPS1D;, features a modification of the amino acid from C to R at position 816.
+The protein's natural variant, known as in CPS1D; associated in cis with E-875; causes 70% decrease of enzyme activity; significant decrease in protein yield, features a modification of the amino acid from L to S at position 843.
+The protein's natural variant, known as in CPS1D; moderate decrease in protein yield and partial loss of enzyme activity;, features a modification of the amino acid from R to C at position 850.
+The protein's natural variant, known as in CPS1D; partial loss of enzyme activity;, features a modification of the amino acid from R to H at position 850.
+The protein's natural variant, known as in CPS1D; significant decrease in protein yield and enzyme activity, features a modification of the amino acid from T to P at position 871.
+The protein's natural variant, known as associated in cis with S-843 in a patient with carbamoyl-phosphate synthase deficiency; does not affect enzyme activity; significant decrease in protein yield and thermal stability;, features a modification of the amino acid from K to E at position 875.
+The protein's natural variant, known as in CPS1D; significant decrease in protein yield and enzyme activity;, features a modification of the amino acid from G to E at position 911.
+The protein's natural variant, known as in CPS1D; significant decrease in protein yield and enzyme activity, features a modification of the amino acid from G to V at position 911.
+The protein's natural variant, known as in CPS1D; significant decrease in protein yield and partial loss of enzyme activity;, features a modification of the amino acid from S to L at position 913.
+The protein's natural variant, known as in CPS1D; significant decrease in protein yield and enzyme activity, features a modification of the amino acid from D to G at position 914.
+The protein's natural variant, known as in CPS1D; significant decrease in protein yield and enzyme activity;, features a modification of the amino acid from D to H at position 914.
+The protein's natural variant, known as in CPS1D; significant decrease in protein yield and enzyme activity, features a modification of the amino acid from S to P at position 918.
+The protein's natural variant, known as in CPS1D; significant decrease in protein yield and partial loss of enzyme activity, features a modification of the amino acid from R to T at position 932.
+The protein's natural variant, known as in CPS1D; associated with R-401; significant decrease in protein yield and enzyme activity;, features a modification of the amino acid from I to N at position 937.
+The protein's natural variant, known as in CPS1D; partial loss of enzyme activity and significant decrease in thermal stability;, features a modification of the amino acid from A to T at position 949.
+The protein's natural variant, known as in CPS1D; significant decrease in protein yield and enzyme activity, features a modification of the amino acid from L to P at position 958.
+The protein's natural variant, known as in CPS1D; significant decrease in protein yield and thermal stability; partial loss of enzyme activity;, features a modification of the amino acid from Y to C at position 959.
+The protein's natural variant, known as in CPS1D; significant decrease in protein yield and partial loss of enzyme activity;, features a modification of the amino acid from Y to C at position 962.
+The protein's natural variant, known as in CPS1D; significant decrease in protein yield and enzyme activity;, features a modification of the amino acid from G to D at position 964.
+The protein's natural variant, known as in CPS1D, features a modification of the amino acid from V to E at position 978.
+The protein's natural variant, known as in CPS1D;, features a modification of the amino acid from G to D at position 982.
+The protein's natural variant, known as in CPS1D;, features a modification of the amino acid from G to S at position 982.
+The protein's natural variant, known as in CPS1D;, features a modification of the amino acid from G to V at position 982.
+The protein's natural variant, known as in CPS1D, features a modification of the amino acid from Y to H at position 984.
+The protein's natural variant, known as in CPS1D; associated with V-304;, features a modification of the amino acid from I to T at position 986.
+The protein's natural variant, known as in CPS1D; may affect splicing;, features a modification of the amino acid from G to C at position 987.
+The protein's natural variant, known as in CPS1D;, features a modification of the amino acid from F to S at position 992.
+The protein's natural variant, known as in CPS1D;, features a modification of the amino acid from S to F at position 998.
+The protein's natural variant, known as in CPS1D;, features a modification of the amino acid from N to S at position 1016.
+The protein's natural variant, known as in CPS1D, features a modification of the amino acid from P to L at position 1017.
+The protein's natural variant, known as in CPS1D;, features a modification of the amino acid from T to I at position 1022.
+The protein's natural variant, known as in CPS1D, features a modification of the amino acid from E to G at position 1034.
+The protein's natural variant, known as in CPS1D;, features a modification of the amino acid from H to R at position 1045.
+The protein's natural variant, known as in CPS1D, features a modification of the amino acid from I to R at position 1054.
+The protein's natural variant, known as in CPS1D, features a modification of the amino acid from Q to R at position 1059.
+The protein's natural variant, known as in CPS1D;, features a modification of the amino acid from A to E at position 1065.
+The protein's natural variant, known as in CPS1D;, features a modification of the amino acid from R to C at position 1089.
+The protein's natural variant, known as in CPS1D;, features a modification of the amino acid from R to L at position 1089.
+The protein's natural variant, known as in CPS1D, features a modification of the amino acid from Q to R at position 1103.
+The protein's natural variant, known as in CPS1D, features a modification of the amino acid from V to G at position 1141.
+The protein's natural variant, known as in CPS1D, features a modification of the amino acid from A to E at position 1155.
+The protein's natural variant, known as in CPS1D;, features a modification of the amino acid from A to V at position 1155.
+The protein's natural variant, known as in CPS1D, features a modification of the amino acid from T to R at position 1167.
+The protein's natural variant, known as in CPS1D, features a modification of the amino acid from E to D at position 1194.
+The protein's natural variant, known as in CPS1D, features a modification of the amino acid from H to P at position 1195.
+The protein's natural variant, known as in CPS1D;, features a modification of the amino acid from S to L at position 1203.
+The protein's natural variant, known as in CPS1D;, features a modification of the amino acid from S to P at position 1203.
+The protein's natural variant, known as in CPS1D, features a modification of the amino acid from D to N at position 1205.
+The protein's natural variant, known as in CPS1D; unknown pathological significance;, features a modification of the amino acid from I to V at position 1215.
+The protein's natural variant, known as in CPS1D;, features a modification of the amino acid from R to Q at position 1228.
+The protein's natural variant, known as in CPS1D, features a modification of the amino acid from N to K at position 1241.
+The protein's natural variant, known as in CPS1D; unknown pathological significance, features a modification of the amino acid from I to F at position 1254.
+The protein's natural variant, known as in CPS1D, features a modification of the amino acid from E to D at position 1255.
+The protein's natural variant, known as in CPS1D, features a modification of the amino acid from R to P at position 1262.
+The protein's natural variant, known as in CPS1D;, features a modification of the amino acid from R to Q at position 1262.
+The protein's natural variant, known as in CPS1D, features a modification of the amino acid from D to H at position 1274.
+The protein's natural variant, known as in CPS1D, features a modification of the amino acid from C to R at position 1327.
+The protein's natural variant, known as in CPS1D, features a modification of the amino acid from S to P at position 1331.
+The protein's natural variant, known as in CPS1D;, features a modification of the amino acid from G to E at position 1333.
+The protein's natural variant, known as in CPS1D, features a modification of the amino acid from R to L at position 1371.
+The protein's natural variant, known as no functional consequences; no negative effect on protein stability, enzyme activity and thermal stability;, features a modification of the amino acid from G to S at position 1376.
+The protein's natural variant, known as in CPS1D; significant reduction in thermal stability;, features a modification of the amino acid from A to T at position 1378.
+The protein's natural variant, known as in CPS1D; significant loss of protein stability, features a modification of the amino acid from L to S at position 1381.
+The protein's natural variant, known as in CPS1D;, features a modification of the amino acid from T to M at position 1391.
+The protein's natural variant, known as in CPS1D, features a modification of the amino acid from L to V at position 1398.
+The protein's natural variant, known as associated with susceptibility to neonatal pulmonary hypertension; also highly associated with hepatocellular carcinoma progression;, features a modification of the amino acid from T to N at position 1406.
+The protein's natural variant, known as in CPS1D; modestly decreases enzyme activity;, features a modification of the amino acid from P to L at position 1411.
+The protein's natural variant, known as in CPS1D, features a modification of the amino acid from P to L at position 1439.
+The protein's natural variant, known as in CPS1D; almost complete loss of enzyme activity; approximately 10-fold decrease in the apparent Vmax for bicarbonate, ammonia and ATP; decreased affinity for NAG, features a modification of the amino acid from T to A at position 1443.
+The protein's natural variant, known as in CPS1D; the enzyme is inactive, features a modification of the amino acid from R to Q at position 1453.
+The protein's natural variant, known as in CPS1D; the enzyme is inactive;, features a modification of the amino acid from R to W at position 1453.
+The protein's natural variant, known as in CPS1D, features a modification of the amino acid from P to R at position 1462.
+The protein's natural variant, known as in CPS1D; triggers a large decrease in the apparent affinity for N-acetyl-L-glutamate (NAG);, features a modification of the amino acid from Y to H at position 1491.
+The protein's natural variant, known as in clone K12, features a modification of the amino acid from E to G at position 32.
+The protein's natural variant, known as in clone G2, features a modification of the amino acid from L to M at position 38.
+The protein's natural variant, known as in clone K12, features a modification of the amino acid from P to R at position 58.
+The protein's natural variant, known as in clones G2, G5, G11 and K1, features a modification of the amino acid from V to A at position 76.
+The protein's natural variant, known as in clone K7, features a modification of the amino acid from I to V at position 413.
+The protein's natural variant, known as in clones G2, G5 and G11, features a modification of the amino acid from R to Q at position 536.
+The protein's natural variant, known as in EORVA; decreased transcriptional activity and impaired nuclear localization;, features a modification of the amino acid from R to C at position 95.
+The protein's natural variant, known as in BDE2;, features a modification of the amino acid from L to P at position 44.
+The protein's natural variant, known as in BDE2;, features a modification of the amino acid from L to P at position 60.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from S to T at position 169.
+The protein's natural variant, known as in an ovarian serous carcinoma sample; somatic mutation, features a modification of the amino acid from I to M at position 275.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from R to H at position 333.
+The protein's natural variant, known as in MRXSPM; unknown pathological significance; reduced sulfotransferase activity; no effect on protein levels;, features a modification of the amino acid from G to R at position 306.
+The protein's natural variant, known as in strain: AKR/J, C3H and DBA/2, features a modification of the amino acid from E to K at position 358.
+The protein's natural variant, known as in strain: AKR/J, C3H and DBA/2; requires 2 nucleotide substitutions, features a modification of the amino acid from R to V at position 399.
+The protein's natural variant, known as in strain: AKR/J, C3H and DBA/2, features a modification of the amino acid from GLTSVGSVGVLSLSPWKHQSNS to TKL at position 459.
+The natural variant of this protein is characterized by an amino acid alteration from E to D at position 326.
+The protein's natural variant, known as in LHONAR; results in reduced turnover of N-module subunits of the respiratory chain complex I and reduced complex I activity in homozygous patient-derived cells;, features a modification of the amino acid from Y to C at position 51.
+The protein's natural variant, known as in LHONAR; results in reduced turnover of N-module subunits of the respiratory chain complex I and reduced complex I activity in homozygous patient-derived cells, features a modification of the amino acid from P to S at position 78.
+The protein's natural variant, known as in LHONAR; results in reduced turnover of N-module subunits of the respiratory chain complex I and reduced complex I activity in homozygous patient-derived cells, features a modification of the amino acid from L to Q at position 101.
+The protein's natural variant, known as in NEDMILG; unknown pathological significance; decreased protein levels in patient cells;, features a modification of the amino acid from R to P at position 11.
+The protein's natural variant, known as in NEDMILG; decreased protein levels in patient cells; decreased asparagine-tRNA ligase activity in patient cells;, features a modification of the amino acid from T to M at position 17.
+The protein's natural variant, known as in NEDMILG; unknown pathological significance, features a modification of the amino acid from K to E at position 60.
+The protein's natural variant, known as in NEDMILG; unknown pathological significance;, features a modification of the amino acid from G to C at position 132.
+The protein's natural variant, known as in NEDMILEG; unable to rescue growth defects in a yeast complementation assay, features a modification of the amino acid from R to L at position 322.
+The protein's natural variant, known as in NEDMILG; unknown pathological significance, features a modification of the amino acid from L to P at position 350.
+The protein's natural variant, known as in NEDMILG;, features a modification of the amino acid from D to A at position 356.
+The protein's natural variant, known as in NEDMILG; unknown pathological significance;, features a modification of the amino acid from A to T at position 422.
+The protein's natural variant, known as in NEDMILG; unknown pathological significance, features a modification of the amino acid from T to I at position 459.
+The protein's natural variant, known as in NEDMILEG; unknown pathological significance, features a modification of the amino acid from G to S at position 509.
+The protein's natural variant, known as in NEDMILG;, features a modification of the amino acid from R to C at position 545.
+The protein's natural variant, known as in a lung cancer patient;, features a modification of the amino acid from G to R at position 8.
+The protein's natural variant, known as in a colorectal cancer patient, features a modification of the amino acid from G to A at position 15.
+The protein's natural variant, known as in a lung cancer patient, features a modification of the amino acid from P to S at position 65.
+The protein's natural variant, known as in a lung cancer patient;, features a modification of the amino acid from G to D at position 90.
+The protein's natural variant, known as in a colon adenocarcinoma, features a modification of the amino acid from L to P at position 101.
+The protein's natural variant, known as in a lung cancer patient, features a modification of the amino acid from K to E at position 343.
+The protein's natural variant, known as in a colorectal cancer patient;, features a modification of the amino acid from S to P at position 365.
+The protein's natural variant, known as in a colon adenocarcinoma, features a modification of the amino acid from V to A at position 448.
+The protein's natural variant, known as in a colorectal cancer patient, features a modification of the amino acid from V to E at position 498.
+The protein's natural variant, known as in a colorectal cancer patient, features a modification of the amino acid from L to I at position 499.
+The protein's natural variant, known as in a colorectal cancer patient, features a modification of the amino acid from V to G at position 500.
+The protein's natural variant, known as in a lung cancer patient;, features a modification of the amino acid from D to G at position 504.
+The protein's natural variant, known as in a colon adenocarcinoma;, features a modification of the amino acid from V to A at position 545.
+The protein's natural variant, known as in AME; abolishes enzyme activity, features a modification of the amino acid from L to R at position 179.
+The protein's natural variant, known as in AME; reduces enzyme activity, features a modification of the amino acid from S to F at position 180.
+The protein's natural variant, known as in AME;, features a modification of the amino acid from R to C at position 186.
+The protein's natural variant, known as in AME; reduces enzyme activity by at least 95%;, features a modification of the amino acid from R to C at position 208.
+The protein's natural variant, known as in AME; abolishes enzyme activity;, features a modification of the amino acid from R to H at position 208.
+The protein's natural variant, known as in AME; reduces enzyme activity by 90%;, features a modification of the amino acid from R to C at position 213.
+The protein's natural variant, known as in AME; reduces enzyme activity to about 6% of wild type;, features a modification of the amino acid from D to N at position 223.
+The protein's natural variant, known as in hypertension; decreases affinity for cortisol;, features a modification of the amino acid from P to L at position 227.
+The protein's natural variant, known as in AME; reduces enzyme activity;, features a modification of the amino acid from A to V at position 237.
+The protein's natural variant, known as in AME; associated with R-250, features a modification of the amino acid from D to N at position 244.
+The protein's natural variant, known as in AME; abolishes enzyme activity, features a modification of the amino acid from LL to PS at position 251.
+The protein's natural variant, known as in AME; associated with N-244, features a modification of the amino acid from L to R at position 250.
+The protein's natural variant, known as in AME; decreases enzyme activity by 33%;, features a modification of the amino acid from R to C at position 279.
+The protein's natural variant, known as in AME; abolishes enzyme activity;, features a modification of the amino acid from A to V at position 328.
+The protein's natural variant, known as in AME; abolishes enzyme activity, features a modification of the amino acid from RY to H at position 338.
+The protein's natural variant, known as in AME; decreased half-life from 21 to 4 hours compared to wild-type, probably due to degradation via the proteasomal pathway;, features a modification of the amino acid from R to C at position 337.
+The protein's natural variant, known as in AME; abolishes enzyme activity; decreased half-life from 21 to 3 hours compared to wild-type, probably due to degradation via the proteasomal pathway;, features a modification of the amino acid from Y to H at position 338.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from M to I at position 669.
+The protein's natural variant, known as in a lung large cell carcinoma sample; somatic mutation, features a modification of the amino acid from R to P at position 806.
+The protein's natural variant, known as in NPHPL1;, features a modification of the amino acid from G to C at position 453.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from S to R at position 829.
+The protein's natural variant, known as in a glioblastoma multiforme sample; somatic mutation;, features a modification of the amino acid from T to I at position 60.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from I to K at position 684.
+The protein's natural variant, known as in CTRCT14; nuclear pulverulent and posterior polar cataract; the mutant affects the formation of gap junction plaques; affects hemichannel permeability;, features a modification of the amino acid from G to D at position 2.
+The protein's natural variant, known as in CTRCT14, features a modification of the amino acid from D to Y at position 3.
+The protein's natural variant, known as in CTRCT14; autosomal dominant congenital/infantile 'ant-egg' cataract, features a modification of the amino acid from L to S at position 11.
+The protein's natural variant, known as in CTRCT14; unknown pathological significance;, features a modification of the amino acid from T to M at position 19.
+The protein's natural variant, known as in CTRCT14;, features a modification of the amino acid from V to M at position 28.
+The protein's natural variant, known as in CTRCT14; nuclear pulverulent cataract, features a modification of the amino acid from F to L at position 32.
+The protein's natural variant, known as in CTRCT14, features a modification of the amino acid from R to L at position 33.
+The protein's natural variant, known as in CTRCT14; nuclear cataract;, features a modification of the amino acid from V to M at position 44.
+The protein's natural variant, known as in CTRCT14; nuclear progressive cataract, features a modification of the amino acid from W to S at position 45.
+The protein's natural variant, known as in CTRCT14; nuclear cataract, features a modification of the amino acid from D to N at position 47.
+The protein's natural variant, known as in CTRCT14, features a modification of the amino acid from E to G at position 48.
+The protein's natural variant, known as in CTRCT14; nuclear punctate cataract;, features a modification of the amino acid from P to L at position 59.
+The protein's natural variant, known as in CTRCT14;, features a modification of the amino acid from N to S at position 63.
+The protein's natural variant, known as in CTRCT14; nearly abolishes formation of gap junctions; no significant effect on formation of functional hemichannels, features a modification of the amino acid from R to G at position 76.
+The protein's natural variant, known as in CTRCT14; nearly abolishes formation of gap junctions; no significant effect on formation of functional hemichannels; not fully penetrant mutation;, features a modification of the amino acid from R to H at position 76.
+The protein's natural variant, known as in CTRCT14; pearl box cataract;, features a modification of the amino acid from T to M at position 87.
+The protein's natural variant, known as in CTRCT14, features a modification of the amino acid from G to E at position 143.
+The protein's natural variant, known as in CTRCT14; unknown pathological significance;, features a modification of the amino acid from K to Q at position 156.
+The protein's natural variant, known as in CTRCT14;, features a modification of the amino acid from P to L at position 187.
+The protein's natural variant, known as in CTRCT14; central nuclear cataract with punctate opacities, features a modification of the amino acid from P to S at position 187.
+The protein's natural variant, known as in CTRCT14;, features a modification of the amino acid from N to I at position 188.
+The protein's natural variant, known as in CTRCT14; nuclear pulverulent cataract;, features a modification of the amino acid from N to T at position 188.
+The protein's natural variant, known as in temperature-sensitive mutant HO202, features a modification of the amino acid from P to L at position 231.
+The protein's natural variant, known as in strain: cv. C24, features a modification of the amino acid from D to G at position 301.
+The protein's natural variant, known as in strain: cv. C24, features a modification of the amino acid from K to N at position 339.
+The protein's natural variant, known as in a patient with chronic myelomonocytic leukemia, features a modification of the amino acid from I to V at position 270.
+The protein's natural variant, known as in a patient with chronic myelomonocytic leukemia, features a modification of the amino acid from E to D at position 834.
+The protein's natural variant, known as in a patient with chronic myelomonocytic leukemia, features a modification of the amino acid from R to K at position 922.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from L to R at position 1106.
+The protein's natural variant, known as in MPOD; affects proteolytic processing and secretion;, features a modification of the amino acid from Y to C at position 173.
+The protein's natural variant, known as in MPOD;, features a modification of the amino acid from M to T at position 251.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to Q at position 447.
+The protein's natural variant, known as in MPOD; suppress post-translational processing;, features a modification of the amino acid from R to W at position 569.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to H at position 735.
+The protein's natural variant, known as in strain: Isolate MVZ 185904, features a modification of the amino acid from L to M at position 198.
+The protein's natural variant, known as in strain: Isolate MVZ 185904, features a modification of the amino acid from T to S at position 203.
+The protein's natural variant, known as in strain: Isolate MVZ 185904, features a modification of the amino acid from P to S at position 208.
+The protein's natural variant, known as in strain: Isolate MVZ 185904, features a modification of the amino acid from T to A at position 368.
+The protein's natural variant, known as associated with lower plasma levels of low-density lipoprotein cholesterol; reduces protein stability;, features a modification of the amino acid from L to I at position 25.
+The protein's natural variant, known as in allele A:2, features a modification of the amino acid from P to T at position 30.
+The protein's natural variant, known as in allele A:2, features a modification of the amino acid from P to PKPKEEP at position 40.
+The protein's natural variant, known as in allele A:2, features a modification of the amino acid from L to P at position 166.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from D to E at position 593.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from K to N at position 609.
+The protein's natural variant, known as in GBBB, features a modification of the amino acid from C to R at position 266.
+The protein's natural variant, known as in GBBB;, features a modification of the amino acid from L to P at position 295.
+The protein's natural variant, known as in GBBB, features a modification of the amino acid from LC to R at position 392.
+The protein's natural variant, known as in GBBB, features a modification of the amino acid from V to VFIDSGRHL at position 534.
+The protein's natural variant, known as in GBBB, features a modification of the amino acid from I to T at position 536.
+The protein's natural variant, known as in GBBB;, features a modification of the amino acid from L to P at position 626.
+The natural variant of this protein is characterized by an amino acid alteration from G to D at position 47.
+The natural variant of this protein is characterized by an amino acid alteration from A to V at position 174.
+The natural variant of this protein is characterized by an amino acid alteration from M to I at position 221.
+The protein's natural variant, known as in GSS deficiency;, features a modification of the amino acid from A to D at position 26.
+The protein's natural variant, known as in GSS deficiency; 100-fold decreased glutathione synthase activity, features a modification of the amino acid from L to P at position 188.
+The protein's natural variant, known as in GSS deficiency;, features a modification of the amino acid from D to A at position 219.
+The protein's natural variant, known as in GSS deficiency;, features a modification of the amino acid from D to G at position 219.
+The protein's natural variant, known as in GSS deficiency, features a modification of the amino acid from L to R at position 254.
+The protein's natural variant, known as in GSS deficiency;, features a modification of the amino acid from R to W at position 267.
+The protein's natural variant, known as in GSS deficiency; 100-fold decreased glutathione synthase activity;, features a modification of the amino acid from Y to C at position 270.
+The protein's natural variant, known as in GSS deficiency; 100-fold decreased glutathione synthase activity, features a modification of the amino acid from Y to H at position 270.
+The protein's natural variant, known as in GSS deficiency; 10-fold decreased glutathione synthase activity;, features a modification of the amino acid from R to C at position 283.
+The protein's natural variant, known as in GSS deficiency;, features a modification of the amino acid from L to Q at position 286.
+The protein's natural variant, known as in GSS deficiency, features a modification of the amino acid from L to P at position 301.
+The protein's natural variant, known as in GSS deficiency;, features a modification of the amino acid from R to C at position 330.
+The protein's natural variant, known as in GSS deficiency, features a modification of the amino acid from G to V at position 464.
+The protein's natural variant, known as in GSS deficiency;, features a modification of the amino acid from D to E at position 469.
+The protein's natural variant, known as in COD3; likely benign variant, features a modification of the amino acid from F to I at position 42.
+The protein's natural variant, known as in COD3; some subjects may present a moderately severe cone-rod dystrophy; unknown pathological significance; causes a decrease in the number of bound calcium ions from 3 to 2, without changing the activity profile;, features a modification of the amino acid from P to L at position 50.
+The protein's natural variant, known as in COD3; unknown pathological significance, features a modification of the amino acid from D to E at position 68.
+The protein's natural variant, known as in COD3; unknown pathological significance, features a modification of the amino acid from L to I at position 80.
+The protein's natural variant, known as in CORD14; affects guanylate cyclase regulator activity resulting in constitutive activation of GUCY2D at physiologic calcium concentrations; altered tertiary structure; no change of affinity for calcium ions; increased affinity for magnesium ions;, features a modification of the amino acid from L to F at position 84.
+The protein's natural variant, known as in CORD14; results in impaired guanylate cyclase regulator activity; interferes with GCAP1 calcium-dependent transition from activator to inhibitor of GUCY2D; the mutant protein remains active at high calcium concentrations causing persistent GUCY2D stimulation, features a modification of the amino acid from G to R at position 86.
+The protein's natural variant, known as in COD3; exhibits an about 6-fold shift of ionic calcium concentration at which the guanylate cyclase activity is halfmaximal;, features a modification of the amino acid from E to K at position 89.
+The protein's natural variant, known as in COD3; results in impaired guanylate cyclase regulator activity; at high calcium ion concentrations the mutant protein stimulates GUCY2D activity while the wild-type inhibits it;, features a modification of the amino acid from Y to C at position 99.
+The protein's natural variant, known as in COD3;, features a modification of the amino acid from Y to N at position 99.
+The protein's natural variant, known as in COD3, features a modification of the amino acid from Y to S at position 99.
+The protein's natural variant, known as in COD3; exhibits an about 28-fold shift of ionic calcium concentration at which the guanylate cyclase activity is halfmaximal, features a modification of the amino acid from D to E at position 100.
+The protein's natural variant, known as in CORD14;, features a modification of the amino acid from D to G at position 100.
+The protein's natural variant, known as in COD3; results in impaired guanylate cyclase regulator activity; at low calcium concentrations the mutant protein stimulates GUCY2D less efficiently than the wild-type but it remains active at high calcium concentrations causing persistent GUCY2D stimulation, features a modification of the amino acid from N to K at position 104.
+The protein's natural variant, known as in CORD14; affects guanylate cyclase regulator activity resulting in constitutive activation of GUCY2D at physiologic calcium concentrations; 10-fold lower affinity for calcium ions;, features a modification of the amino acid from I to T at position 107.
+The protein's natural variant, known as in CORD14; results in impaired guanylate cyclase regulator activity; at low calcium concentrations the mutant protein stimulates GUCY2D as the wild-type while at high calcium concentrations it does not fully inhibit GUCY2D; decreased affinity for calcium ions, features a modification of the amino acid from E to V at position 111.
+The protein's natural variant, known as in a patient with an atypical form of retinitis pigmentosa; unknown pathological significance;, features a modification of the amino acid from T to I at position 114.
+The protein's natural variant, known as in COD3;, features a modification of the amino acid from R to L at position 120.
+The protein's natural variant, known as in COD3, features a modification of the amino acid from I to NT at position 143.
+The protein's natural variant, known as in COD3; results in impaired guanylate cyclase regulator activity leading to increased GUCY2D activity;, features a modification of the amino acid from D to G at position 144.
+The protein's natural variant, known as in COD3; unknown pathological significance;, features a modification of the amino acid from D to E at position 148.
+The protein's natural variant, known as in COD3 and CORD14;, features a modification of the amino acid from L to F at position 151.
+The protein's natural variant, known as in COD3; constitutive activation of GUCY2D;, features a modification of the amino acid from E to G at position 155.
+The protein's natural variant, known as in COD3; exhibits an about 18-fold shift of ionic calcium concentration at which the guanylate cyclase activity is halfmaximal, features a modification of the amino acid from G to V at position 159.
+The protein's natural variant, known as found in autosomal dominant macular dystrophy; unknown pathological significance; affects guanylate cyclase regulator activity resulting in a constitutively active form at physiologic calcium concentrations; no change of affinity for calcium ions; increased affinity for magnesium ions;, features a modification of the amino acid from L to F at position 176.
+The protein's natural variant, known as in COD3; likely benign variant;, features a modification of the amino acid from Q to R at position 184.
+The protein's natural variant, known as in strain: Isolate BD, features a modification of the amino acid from N to D at position 16.
+The protein's natural variant, known as in strain: Isolate BD and Isolate LP, features a modification of the amino acid from G to V at position 189.
+The protein's natural variant, known as in strain: Isolate BD, features a modification of the amino acid from T to I at position 233.
+The protein's natural variant, known as in strain: Isolate LP, features a modification of the amino acid from S to Y at position 310.
+The protein's natural variant, known as in MODY14; no effect on protein abundance; loss of function in insulin receptor signaling pathway;, features a modification of the amino acid from D to N at position 94.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from E to Q at position 643.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from P to L at position 318.
+The protein's natural variant, known as in strain: Z17561, features a modification of the amino acid from T to S at position 20.
+The protein's natural variant, known as in strain: Z17561, features a modification of the amino acid from IQT to MQA at position 44.
+The protein's natural variant, known as in strain: Z17561, features a modification of the amino acid from A to S at position 56.
+The protein's natural variant, known as in strain: Z17561, features a modification of the amino acid from V to I at position 118.
+The protein's natural variant, known as in strain: Z17561, features a modification of the amino acid from T to M at position 199.
+The protein's natural variant, known as in strain: EF2, features a modification of the amino acid from K to Q at position 33.
+The protein's natural variant, known as in strain: TE3285, features a modification of the amino acid from V to I at position 156.
+The protein's natural variant, known as in strain: TE3285, features a modification of the amino acid from Q to H at position 202.
+The protein's natural variant, known as in strain: TE3285, features a modification of the amino acid from I to V at position 204.
+The protein's natural variant, known as in subspecies Rhodurus, features a modification of the amino acid from T to A at position 17.
+The protein's natural variant, known as in subspecies Rhodurus, features a modification of the amino acid from I to V at position 136.
+The natural variant of this protein is characterized by an amino acid alteration from L to S at position 30.
+The protein's natural variant, known as in strain: cv. Cnt-1, cv. Ema-1 and cv. Tac-0, features a modification of the amino acid from N to Y at position 13.
+The protein's natural variant, known as in strain: cv. Lip-0, features a modification of the amino acid from V to L at position 25.
+The protein's natural variant, known as in strain: cv. Can-0, features a modification of the amino acid from E to V at position 41.
+The protein's natural variant, known as in strain: cv. Sorbo, features a modification of the amino acid from Q to P at position 43.
+The protein's natural variant, known as in strain: cv. Cnt-1, cv. Ema-1 and cv. Tac-0, features a modification of the amino acid from T to I at position 144.
+The protein's natural variant, known as in strain: cv. Bla-10, cv. Bl-0, cv. Can-0, cv. Cvi-0, cv. Ka-0, cv. Kas-1, cv. Lip-0, cv. No-0, cv. Pa-1, cv. Per-1, cv. Sei-0 and cv. Sorbo, features a modification of the amino acid from N to K at position 228.
+The protein's natural variant, known as in strain: cv. Bla-10, cv. Bl-0, cv. Can-0, cv. Cvi-0, cv. Ka-0, cv. Kas-1, cv. No-0, cv. Pa-1, cv. Per-1, cv. Sei-0, cv. Sorbo, cv. Su-0 and cv. Yo-0, features a modification of the amino acid from V to L at position 269.
+The protein's natural variant, known as in strain: cv. Cvi-0, features a modification of the amino acid from M to T at position 271.
+The protein's natural variant, known as in MNK; loss of protein expression, features a modification of the amino acid from E to V at position 628.
+The protein's natural variant, known as in MNK;, features a modification of the amino acid from A to P at position 629.
+The protein's natural variant, known as in MNK; loss of protein expression, features a modification of the amino acid from K to R at position 633.
+The protein's natural variant, known as in OHS;, features a modification of the amino acid from S to L at position 637.
+The protein's natural variant, known as in MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity, features a modification of the amino acid from S to Y at position 653.
+The protein's natural variant, known as in MNK; subcellular location restricted to post-TGN compartments; impaired copper transport activity;, features a modification of the amino acid from G to R at position 666.
+The protein's natural variant, known as in MNK;, features a modification of the amino acid from L to R at position 706.
+The protein's natural variant, known as in MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity;, features a modification of the amino acid from G to R at position 727.
+The protein's natural variant, known as in MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity;, features a modification of the amino acid from G to D at position 728.
+The protein's natural variant, known as in MNK; has no effect on copper-dependent trafficking from TGN to post-TGN compartments; impaired copper transport activity, features a modification of the amino acid from S to P at position 761.
+The protein's natural variant, known as in MNK; loss of protein expression, features a modification of the amino acid from K to N at position 802.
+The protein's natural variant, known as in MNK; loss of protein expression;, features a modification of the amino acid from R to H at position 844.
+The protein's natural variant, known as in MNK, features a modification of the amino acid from G to R at position 853.
+The protein's natural variant, known as in MNK; decreased protein abundance; impaired copper transport activity, features a modification of the amino acid from G to V at position 860.
+The protein's natural variant, known as in MNK; increased protein abundance; does not affect interaction with ATOX1; does not affect interaction with COMMD1; increased localization at the plasma membrane; does not cycle back to TGN under conditions of copper depletion;, features a modification of the amino acid from L to R at position 873.
+The protein's natural variant, known as in MNK; subcellular location restricted to post-TGN compartments; impaired copper transport activity, features a modification of the amino acid from G to E at position 876.
+The protein's natural variant, known as in MNK; loss of protein expression, features a modification of the amino acid from G to R at position 876.
+The protein's natural variant, known as in OHS; has no effect on copper-dependent trafficking; impaired copper transport activity, features a modification of the amino acid from Q to R at position 924.
+The protein's natural variant, known as in DSMAX3; demonstrates impaired intracellular trafficking compared to control with some of the mutant protein remaining in the Golgi apparatus after exposure to copper;, features a modification of the amino acid from T to I at position 994.
+The protein's natural variant, known as in MNK; decreased protein abundance; increased protein degradation; does not affect interaction with ATOX1; does not affect interaction with COMMD1; subcellular location restricted to TGN; does not localizes to the plasma membrane in response to elevated copper levels; impaired copper transport activity, features a modification of the amino acid from C to R at position 1000.
+The protein's natural variant, known as in MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity;, features a modification of the amino acid from G to R at position 1005.
+The protein's natural variant, known as in MNK;, features a modification of the amino acid from L to P at position 1006.
+The protein's natural variant, known as in MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity, features a modification of the amino acid from A to V at position 1007.
+The protein's natural variant, known as in MNK; subcellular location restricted to post-TGN compartments; impaired copper transport activity, features a modification of the amino acid from G to D at position 1015.
+The protein's natural variant, known as in MNK;, features a modification of the amino acid from G to D at position 1019.
+The protein's natural variant, known as in MNK; loss of protein expression, features a modification of the amino acid from K to N at position 1037.
+The protein's natural variant, known as in MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity, features a modification of the amino acid from D to G at position 1044.
+The protein's natural variant, known as in MNK, features a modification of the amino acid from T to I at position 1048.
+The protein's natural variant, known as in MNK, features a modification of the amino acid from L to P at position 1100.
+The protein's natural variant, known as in MNK;, features a modification of the amino acid from G to D at position 1118.
+The protein's natural variant, known as in MNK; decreased protein abundance; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity;, features a modification of the amino acid from G to R at position 1255.
+The protein's natural variant, known as in MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity, features a modification of the amino acid from K to E at position 1282.
+The protein's natural variant, known as in MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity, features a modification of the amino acid from G to E at position 1300.
+The protein's natural variant, known as in MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity;, features a modification of the amino acid from D to G at position 1301.
+The protein's natural variant, known as in MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity, features a modification of the amino acid from G to E at position 1302.
+The protein's natural variant, known as in MNK;, features a modification of the amino acid from G to R at position 1302.
+The protein's natural variant, known as in MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity, features a modification of the amino acid from G to V at position 1302.
+The protein's natural variant, known as in MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity, features a modification of the amino acid from N to K at position 1304.
+The protein's natural variant, known as in OHS; has approximately 33% residual copper transport; increased protein abundance; increased localization at the plasma membrane; does not cycle back to TGN under conditions of copper depletion; does not affect interaction with ATOX1; does not affect interaction with COMMD1;, features a modification of the amino acid from N to S at position 1304.
+The protein's natural variant, known as in MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity, features a modification of the amino acid from D to A at position 1305.
+The protein's natural variant, known as in MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity, features a modification of the amino acid from D to G at position 1305.
+The protein's natural variant, known as in MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity, features a modification of the amino acid from A to D at position 1308.
+The protein's natural variant, known as in MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity;, features a modification of the amino acid from G to R at position 1315.
+The protein's natural variant, known as in MNK; subcellular location restricted to post-TGN compartments; impaired copper transport activity, features a modification of the amino acid from A to V at position 1325.
+The protein's natural variant, known as in MNK, features a modification of the amino acid from S to R at position 1344.
+The protein's natural variant, known as in MNK, features a modification of the amino acid from I to F at position 1345.
+The protein's natural variant, known as in MNK; decreased protein abundance; increased protein degradation; does not affect interaction with ATOX1; does not affect interaction with COMMD1; subcellular location restricted to TGN; does not localizes to the plasma membrane in response to elevated copper levels; impaired copper transport activity, features a modification of the amino acid from A to V at position 1362.
+The protein's natural variant, known as in MNK; loss of protein expression, features a modification of the amino acid from G to R at position 1369.
+The protein's natural variant, known as in MNK; loss of protein expression, features a modification of the amino acid from A to P at position 1373.
+The protein's natural variant, known as in DSMAX3; demonstrates impaired intracellular trafficking compared to control with some mutant protein remaining in the Golgi apparatus after exposure to copper;, features a modification of the amino acid from P to S at position 1386.
+The protein's natural variant, known as in MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity, features a modification of the amino acid from M to T at position 1393.
+The protein's natural variant, known as in MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity, features a modification of the amino acid from S to F at position 1397.
+The protein's natural variant, known as in MASNS; unknown pathological significance; requires 2 nucleotide substitutions; decreased basal PKA enzymatic activity in lysates from transfected cells, features a modification of the amino acid from Q to L at position 167.
+The protein's natural variant, known as in MASNS; decreased basal PKA enzymatic activity in lysates from transfected cells, features a modification of the amino acid from E to K at position 196.
+The protein's natural variant, known as in MASNS; decreased basal PKA enzymatic activity in lysates from transfected cells, features a modification of the amino acid from R to W at position 335.
+The natural variant of this protein is characterized by an amino acid alteration from A to P at position 411.
+The protein's natural variant, known as in strain: Z17561, features a modification of the amino acid from L to P at position 93.
+The protein's natural variant, known as in strain: Z17561, features a modification of the amino acid from V to A at position 202.
+The protein's natural variant, known as in strain: Z17561, features a modification of the amino acid from T to S at position 254.
+The protein's natural variant, known as in strain: Z17561, features a modification of the amino acid from KS to NA at position 267.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation, features a modification of the amino acid from A to V at position 246.
+The protein's natural variant, known as in a gastric adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from R to C at position 467.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from P to H at position 794.
+The protein's natural variant, known as in strain: cv. C24, features a modification of the amino acid from V to L at position 324.
+The protein's natural variant, known as in DFNB35;, features a modification of the amino acid from A to V at position 110.
+The protein's natural variant, known as in DFNB35, features a modification of the amino acid from L to P at position 320.
+The protein's natural variant, known as in DFNB35;, features a modification of the amino acid from V to L at position 342.
+The protein's natural variant, known as in DFNB35, features a modification of the amino acid from L to P at position 347.
+The protein's natural variant, known as in DFNB35; uncertain pathological significance;, features a modification of the amino acid from T to M at position 389.
+The natural variant of this protein is characterized by an amino acid alteration from S to R at position 47.
+The natural variant of this protein is characterized by an amino acid alteration from G to R at position 60.
+The natural variant of this protein is characterized by an amino acid alteration from E to D at position 98.
+The protein's natural variant, known as in allele UGT1A6*2, allele UGT1A6*3 and allele UGT1A6*4;, features a modification of the amino acid from S to A at position 7.
+The protein's natural variant, known as in allele UGT1A6*2;, features a modification of the amino acid from T to A at position 181.
+The protein's natural variant, known as in allele UGT1A6*2 and allele UGT1A6*4;, features a modification of the amino acid from R to S at position 184.
+The protein's natural variant, known as in GALAC4; unknown pathological significance; decreased protein stability;, features a modification of the amino acid from G to R at position 142.
+The protein's natural variant, known as in GALAC4; decreased protein stability, features a modification of the amino acid from R to G at position 267.
+The natural variant of this protein is characterized by an amino acid alteration from M to I at position 223.
+The protein's natural variant, known as in patients with sporadic hearing loss, features a modification of the amino acid from D to V at position 31.
+The protein's natural variant, known as in patients with sporadic hearing loss; no detectable proteolytic activity in a yeast-based protease assay, features a modification of the amino acid from A to S at position 317.
+The natural variant of this protein is characterized by an amino acid alteration from P to S at position 337.
+The protein's natural variant, known as reduced proteolytic activity in a yeast-based protease assay;, features a modification of the amino acid from F to L at position 369.
+The protein's natural variant, known as in MRT14; reduced enzyme activity; reduced protein stability; no effect on subcellular localization;, features a modification of the amino acid from P to L at position 182.
+The protein's natural variant, known as in LIS8, features a modification of the amino acid from H to D at position 67.
+The protein's natural variant, known as in LIS8, features a modification of the amino acid from G to E at position 384.
+The protein's natural variant, known as in ADLD; unknown pathological significance; no effect on localization to nuclear lamina;, features a modification of the amino acid from R to W at position 29.
+The protein's natural variant, known as in MCPH26; decreased localization to nuclear lamina; increased aggregation; changed nuclear envelope organization;, features a modification of the amino acid from K to E at position 33.
+The protein's natural variant, known as no effect on localization to nuclear lamina;, features a modification of the amino acid from K to T at position 33.
+The protein's natural variant, known as in MCPH26; decreased localization to nuclear lamina; changed nuclear envelope organization; increased aggregation, features a modification of the amino acid from R to W at position 42.
+The protein's natural variant, known as in MCPH26; increased aggregation; changed nuclear envelope organization;, features a modification of the amino acid from R to P at position 90.
+The protein's natural variant, known as in MCPH26; decreased protein abundance; changed localization to nuclear lamina; changed nuclear envelope organization, features a modification of the amino acid from A to G at position 152.
+The protein's natural variant, known as found in a family with amyotrophic lateral sclerosis carrying a probable causative mutation in MATR3; unknown pathological significance;, features a modification of the amino acid from A to V at position 436.
+The protein's natural variant, known as in beta', features a modification of the amino acid from L to I at position 78.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to W at position 134.
+The protein's natural variant, known as in cv. Borszczagowski, features a modification of the amino acid from V to A at position 102.
+The protein's natural variant, known as in cv. Borszczagowski, features a modification of the amino acid from E to G at position 217.
+The protein's natural variant, known as in cv. Borszczagowski, features a modification of the amino acid from GHPISKPTWIDSSDFDIIDRFLRISRNLSHYYRGSSKKKNLYRIQYILRLSCVKTLARKHKSTV to DIPLVSRPGSIRRILILLIDFCVYPEIFLIITEDPQKKRICIEYNIYFAFLVLKLWLVNTKVLY at position 447.
+The protein's natural variant, known as in strain: Isolate I995, features a modification of the amino acid from F to S at position 50.
+The protein's natural variant, known as in BBRSAY; decreased chromatin binding; the mutant binds to alternative chromatin binding sites compared to wild-type;, features a modification of the amino acid from E to A at position 75.
+The protein's natural variant, known as in AMS; decreased chromatin binding; the mutant binds to alternative chromatin binding sites compared to wild-type;, features a modification of the amino acid from E to K at position 75.
+The protein's natural variant, known as in BBRSAY; decreased chromatin binding; the mutant binds to alternative chromatin binding sites compared to wild-type;, features a modification of the amino acid from E to Q at position 75.
+The protein's natural variant, known as in BBRSAY; decreased chromatin binding; the mutant binds to alternative chromatin binding sites compared to wild-type, features a modification of the amino acid from R to RQR at position 78.
+The protein's natural variant, known as in FFDD3, features a modification of the amino acid from L to P at position 109.
+The protein's natural variant, known as in defensin B, features a modification of the amino acid from G to R at position 86.
+The protein's natural variant, known as in MFDA;, features a modification of the amino acid from Y to F at position 129.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from I to L at position 136.
+The protein's natural variant, known as in MFDA;, features a modification of the amino acid from E to K at position 303.
+The protein's natural variant, known as in PRLMNS; unknown pathological significance, features a modification of the amino acid from M to K at position 443.
+The protein's natural variant, known as probable disease-associated variant found in a patient with Wilms tumor; does not suppress anchorage-independent cell growth;, features a modification of the amino acid from R to G at position 483.
+The protein's natural variant, known as in PRLMNS;, features a modification of the amino acid from C to Y at position 489.
+The protein's natural variant, known as probable disease-associated variant found in a patient with Wilms tumor; does not suppress anchorage-independent cell growth;, features a modification of the amino acid from R to H at position 576.
+The protein's natural variant, known as in allele 2, features a modification of the amino acid from D to E at position 62.
+The protein's natural variant, known as in allele 2, features a modification of the amino acid from A to S at position 117.
+The protein's natural variant, known as in allele 2, features a modification of the amino acid from E to K at position 160.
+The protein's natural variant, known as in STHAG4; unknown pathological significance;, features a modification of the amino acid from R to W at position 70.
+The protein's natural variant, known as in STHAG4;, features a modification of the amino acid from E to K at position 95.
+The protein's natural variant, known as in STHAG4; unknown pathological significance;, features a modification of the amino acid from R to C at position 113.
+The protein's natural variant, known as in STHAG4; unknown pathological significance;, features a modification of the amino acid from G to S at position 126.
+The protein's natural variant, known as in OODD and STHAG4;, features a modification of the amino acid from R to Q at position 128.
+The protein's natural variant, known as in SSPS;, features a modification of the amino acid from A to T at position 131.
+The protein's natural variant, known as in OODD, features a modification of the amino acid from A to V at position 131.
+The protein's natural variant, known as in STHAG4; unknown pathological significance;, features a modification of the amino acid from H to Y at position 143.
+The protein's natural variant, known as in STHAG4; unknown pathological significance;, features a modification of the amino acid from V to M at position 145.
+The protein's natural variant, known as in STHAG4; unknown pathological significance;, features a modification of the amino acid from R to W at position 163.
+The protein's natural variant, known as in STHAG4; unknown pathological significance;, features a modification of the amino acid from R to C at position 171.
+The protein's natural variant, known as in STHAG4 and OODD; unknown pathological significance;, features a modification of the amino acid from G to S at position 213.
+The protein's natural variant, known as in STHAG4; unknown pathological significance;, features a modification of the amino acid from D to N at position 217.
+The protein's natural variant, known as in STHAG4; unknown pathological significance;, features a modification of the amino acid from R to C at position 223.
+The protein's natural variant, known as in OODD and STHAG4; also found in patients with an unclassified form of ectodermal dysplasia;, features a modification of the amino acid from F to I at position 228.
+The protein's natural variant, known as in SSPS, features a modification of the amino acid from G to C at position 266.
+The protein's natural variant, known as in STHAG4; unknown pathological significance;, features a modification of the amino acid from G to S at position 266.
+The protein's natural variant, known as in STHAG4;, features a modification of the amino acid from W to C at position 277.
+The protein's natural variant, known as found in a patient with dental anomalies; unknown pathological significance;, features a modification of the amino acid from S to G at position 292.
+The protein's natural variant, known as in STHAG4; unknown pathological significance;, features a modification of the amino acid from R to C at position 293.
+The protein's natural variant, known as in STHAG4; unknown pathological significance;, features a modification of the amino acid from N to K at position 306.
+The protein's natural variant, known as found in a patient with dental anomalies; unknown pathological significance;, features a modification of the amino acid from R to C at position 348.
+The protein's natural variant, known as in OODD; unknown pathological significance, features a modification of the amino acid from G to C at position 356.
+The protein's natural variant, known as in STHAG4; unknown pathological significance;, features a modification of the amino acid from T to I at position 357.
+The protein's natural variant, known as probable disease-associated variant found in patients with an unclassified form of ectodermal dysplasia, features a modification of the amino acid from R to C at position 360.
+The protein's natural variant, known as in STHAG4; unknown pathological significance;, features a modification of the amino acid from R to C at position 379.
+The protein's natural variant, known as in HH16; phenotype consistent with Kallmann syndrome;, features a modification of the amino acid from R to W at position 66.
+The protein's natural variant, known as in HH16; unknown pathological significance, features a modification of the amino acid from L to R at position 82.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from A to T at position 131.
+The protein's natural variant, known as in HH16; phenotype consistent with Kallmann syndrome;, features a modification of the amino acid from N to S at position 153.
+The protein's natural variant, known as in HH16; phenotype consistent with Kallmann syndrome, features a modification of the amino acid from M to T at position 342.
+The protein's natural variant, known as found in a renal cell carcinoma sample; somatic mutation;, features a modification of the amino acid from P to S at position 396.
+The protein's natural variant, known as in HH16; phenotype consistent with Kallmann syndrome; digenic; found in a patient also carrying mutation Cys-268 in PROKR2;, features a modification of the amino acid from I to V at position 400.
+The protein's natural variant, known as in HH16; phenotype consistent with Kallmann syndrome; digenic; found in patients also carrying mutation Cys-268 in PROKR2 or mutation Arg-687 in FGFR1;, features a modification of the amino acid from V to I at position 435.
+The protein's natural variant, known as in HH16; phenotype consistent with Kallmann syndrome;, features a modification of the amino acid from D to G at position 447.
+The protein's natural variant, known as in HH16; unknown pathological significance;, features a modification of the amino acid from R to W at position 484.
+The protein's natural variant, known as in HH16; phenotype consistent with Kallmann syndrome;, features a modification of the amino acid from I to M at position 657.
+The protein's natural variant, known as in HH16; phenotype consistent with Kallmann syndrome; digenic; found in a patient also carrying mutation Asp-217 in KAL1;, features a modification of the amino acid from T to A at position 688.
+The protein's natural variant, known as in HH16; phenotype consistent with Kallmann syndrome;, features a modification of the amino acid from R to Q at position 730.
+The protein's natural variant, known as in HH16; phenotype consistent with Kallmann syndrome;, features a modification of the amino acid from R to H at position 733.
+The natural variant of this protein is characterized by an amino acid alteration from R to K at position 165.
+The natural variant of this protein is characterized by an amino acid alteration from G to D at position 258.
+The natural variant of this protein is characterized by an amino acid alteration from P to L at position 1870.
+The protein's natural variant, known as in strain: CCUG 17874, features a modification of the amino acid from R to S at position 91.
+The protein's natural variant, known as in strain: CCUG 17874, features a modification of the amino acid from T to I at position 199.
+The protein's natural variant, known as in strain: CCUG 17874, features a modification of the amino acid from E to G at position 252.
+The protein's natural variant, known as in strain: CCUG 17874, features a modification of the amino acid from Q to E at position 279.
+The protein's natural variant, known as in strain: CCUG 17874, features a modification of the amino acid from D to N at position 349.
+The protein's natural variant, known as in strain: CCUG 17874, features a modification of the amino acid from R to K at position 354.
+The protein's natural variant, known as in strain: CCUG 17874, features a modification of the amino acid from KP to NA at position 357.
+The protein's natural variant, known as in strain: CCUG 17874, features a modification of the amino acid from SD to DN at position 374.
+The protein's natural variant, known as in strain: CCUG 17874, features a modification of the amino acid from Q to S at position 394.
+The protein's natural variant, known as in strain: CCUG 17874, features a modification of the amino acid from N to K at position 398.
+The protein's natural variant, known as in strain: CCUG 17874, features a modification of the amino acid from AG to MN at position 450.
+The protein's natural variant, known as in MRD41;, features a modification of the amino acid from G to D at position 70.
+The protein's natural variant, known as in MRD41;, features a modification of the amino acid from Y to C at position 245.
+The protein's natural variant, known as in MRD41, features a modification of the amino acid from L to P at position 282.
+The protein's natural variant, known as found in a patient with epilepsy; unknown pathological significance;, features a modification of the amino acid from G to E at position 405.
+The protein's natural variant, known as found in a patient with epilepsy; unknown pathological significance;, features a modification of the amino acid from N to S at position 407.
+The protein's natural variant, known as in PRPTS; does not affect assembly into the N-Cor repressor complex;, features a modification of the amino acid from Y to C at position 446.
+The protein's natural variant, known as in strain: r791; highly resistant to azithromycin, erythromycin and clarithromycin, less so to spiramycin, features a modification of the amino acid from GTG to TPS at position 71.
+The protein's natural variant, known as in strain: 237; resistant to azithromycin, erythromycin and spiramycin, features a modification of the amino acid from G to GKG at position 69.
+The protein's natural variant, known as in strain: 124; confers resistance to erythromycin and azithromycin, features a modification of the amino acid from R to RTG at position 72.
+The protein's natural variant, known as in strain:FVB/N, features a modification of the amino acid from V to L at position 260.
+The protein's natural variant, known as in strain:FVB/N, features a modification of the amino acid from V to L at position 453.
+The protein's natural variant, known as in strain:FVB/N, features a modification of the amino acid from P to S at position 617.
+The natural variant of this protein is characterized by an amino acid alteration from V to M at position 229.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 233.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from T to I at position 157.
+The protein's natural variant, known as in HACXL; decreased phosphatidylserine translocation from the outer to the inner leaflet of erythrocytes cell membrane;, features a modification of the amino acid from T to N at position 418.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from Q to P at position 931.
+The protein's natural variant, known as found in a clear cell renal carcinoma case; somatic mutation, features a modification of the amino acid from L to H at position 190.
+The protein's natural variant, known as in DFNA9, features a modification of the amino acid from G to D at position 38.
+The protein's natural variant, known as in DFNA9; some families may manifest Meniere disease-like symptoms; does not affect protein deposition to the extracellular matrix;, features a modification of the amino acid from P to S at position 51.
+The protein's natural variant, known as in DFNA9; affects protein deposition to the extracellular matrix;, features a modification of the amino acid from V to G at position 66.
+The protein's natural variant, known as in DFNA9, features a modification of the amino acid from G to V at position 87.
+The protein's natural variant, known as in DFNA9, features a modification of the amino acid from G to W at position 87.
+The protein's natural variant, known as in DFNA9; affects protein deposition to the extracellular matrix;, features a modification of the amino acid from G to E at position 88.
+The protein's natural variant, known as in DFNA9; affects protein deposition to the extracellular matrix;, features a modification of the amino acid from I to N at position 109.
+The protein's natural variant, known as in DFNA9;, features a modification of the amino acid from I to T at position 109.
+The protein's natural variant, known as in DFNA9; does not affect protein deposition to the extracellular matrix;, features a modification of the amino acid from W to R at position 117.
+The protein's natural variant, known as in DFNA9;, features a modification of the amino acid from A to T at position 119.
+The protein's natural variant, known as in DFNA9, features a modification of the amino acid from C to Y at position 162.
+The protein's natural variant, known as in DFNA9;, features a modification of the amino acid from M to T at position 512.
+The protein's natural variant, known as in DFNA9; induces disulfide bond dimer formation; keeps dimer in the cell and reduces secretion; monomeric and/or homodimeric mutant forms do not prevent interaction with type II collagen, features a modification of the amino acid from F to C at position 527.
+The protein's natural variant, known as in DFNA9;, features a modification of the amino acid from C to Y at position 542.
+The protein's natural variant, known as greater ability to inhibit tomato mosaic virus (ToMV/TMV) RNA replication and to bind ToMV replication proteins, features a modification of the amino acid from I to T at position 91.
+The natural variant of this protein is characterized by an amino acid alteration from S to T at position 326.
+The natural variant of this protein is characterized by an amino acid alteration from I to L at position 368.
+The protein's natural variant, known as in strain: CA-11.2A, features a modification of the amino acid from T to A at position 3.
+The protein's natural variant, known as in strain: CA-11.2A, features a modification of the amino acid from N to D at position 68.
+The protein's natural variant, known as in strain: CA-11.2A, features a modification of the amino acid from I to V at position 78.
+The protein's natural variant, known as in strain: CA-11.2A, features a modification of the amino acid from S to R at position 106.
+The protein's natural variant, known as in strain: CA-11.2A, features a modification of the amino acid from R to K at position 112.
+The protein's natural variant, known as in strain: CA-11.2A, features a modification of the amino acid from I to L at position 182.
+The protein's natural variant, known as in strain: CA-11.2A, features a modification of the amino acid from D to N at position 258.
+The natural variant of this protein is characterized by an amino acid alteration from S to R at position 347.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from P to T at position 712.
+The protein's natural variant, known as in strain: Moroccan, features a modification of the amino acid from L to P at position 109.
+The protein's natural variant, known as in strain: Moroccan, features a modification of the amino acid from K to E at position 931.
+The natural variant of this protein is characterized by an amino acid alteration from H to R at position 398.
+The protein's natural variant, known as expression is reduced by 1.86-fold; Vmax with methotrexate as substrate is significantly reduced resulting in significantly decreased intrinsic clearance of methotrexate; Km of glutamic acid is increased 3.5-fold and apparent Vmax of it is reduced 3.4-fold; reaction velocity at 100 nmol/L of pemetrexed is significantly reduced and folic acid dose-response curve is shifted to the right which corresponds to 4.32-fold increase in the EC(50) for folic acid; IC(50) of methotrexate is 1.84-fold higher and accumulation of a lower ratio of long-chain methotrexate polyglutamates to short-chain polyglutamates is detected; all results are for isoform 2 variant in comparison to the wild-type of it;, features a modification of the amino acid from R to C at position 466.
+The protein's natural variant, known as expression reduced by 2.11-fold; Vmax with methotrexate as substrate is significantly reduced resulting in significantly decreased intrinsic clearance of methotrexate; apparent Vmax for glutamic acid is reduced 5-fold; reaction velocity at 100 nmol/L of pemetrexed is significantly reduced and folic acid dose-response curve is shifted to the right which corresponds to 4.28-fold increase in the EC(50) for folic acid; IC(50) of methotrexate is 1.64-fold higher and accumulation of a lower ratio of long-chain methotrexate polyglutamates to short-chain polyglutamates is detected; all results are for isoform 2 variant in comparison to the wild-type of it;, features a modification of the amino acid from S to F at position 499.
+The protein's natural variant, known as exclusively found in the African American population; increased MPP(+) uptake when associated with V-408;, features a modification of the amino acid from S to F at position 14.
+The protein's natural variant, known as affects transporter activity; reduction of MPP(+) uptake; reduction of serum O-isobutanoyl-(R)-carnitine levels; reduction of MPP(+) uptake when associated with V-408;, features a modification of the amino acid from R to C at position 61.
+The protein's natural variant, known as no changes in MPP(+) uptake; when associated with V-408;, features a modification of the amino acid from L to F at position 85.
+The protein's natural variant, known as affects transporter activity; reduction of MPP(+), serotonin and TEA uptake;, features a modification of the amino acid from C to R at position 88.
+The protein's natural variant, known as no changes in both MPP(+) and TEA uptake; abolishes MPP(+) uptake when associated with S-401; largely localized to the plasma membrane;, features a modification of the amino acid from L to F at position 160.
+The protein's natural variant, known as no changes in MPP(+) uptake;, features a modification of the amino acid from S to L at position 189.
+The protein's natural variant, known as affects transporter activity; reduction of MPP(+) uptake when associated with V-408;, features a modification of the amino acid from G to V at position 220.
+The protein's natural variant, known as affects transporter activity; reduction of TEA uptake; reduction o MPP(+) uptake when associated with V-408; largely localized to the plasma membrane;, features a modification of the amino acid from P to L at position 341.
+The protein's natural variant, known as no changes in MPP(+) uptake when associated with V-408;, features a modification of the amino acid from R to H at position 342.
+The protein's natural variant, known as affects transporter activity; reduction of MPP(+), serotonin and TEA uptake; no MPP(+) uptake when associated with L-160;, features a modification of the amino acid from G to S at position 401.
+The protein's natural variant, known as does not affect transporter activity; no changes in MPP(+) uptake when associated with F-14; no changes in MPP(+) uptake when associated with F-85; no changes in MPP(+) uptake when associated with L-189; no changes in MPP(+) uptake when associated with H-342; no changes in MPP(+) uptake when associated with M-420 del; no changes in MPP(+) uptake when associated with I-440; no changes in MPP(+) uptake when associated with I-461; no changes in MPP(+) uptake when associated with M-488; reduction of MPP uptake when associated with C-61; no MPP(+) uptake when associated with V-220; reduction of MPP(+) uptake when associated with L-341; no MPP(+) uptake when associated with S-401; no MPP(+) uptake when associated with R-465;, features a modification of the amino acid from M to V at position 408.
+The protein's natural variant, known as no changes in MPP(+) uptake when associated with V-408;, features a modification of the amino acid from V to I at position 461.
+The protein's natural variant, known as reduction of the localization to the basolateral membrane; no MPP(+) uptake when associated with V-408;, features a modification of the amino acid from G to R at position 465.
+The protein's natural variant, known as no changes in MPP(+) uptake when associated with V-408;, features a modification of the amino acid from R to M at position 488.
+The protein's natural variant, known as in NEDBEH; unknown pathological significance;, features a modification of the amino acid from V to I at position 471.
+The protein's natural variant, known as in NEDBEH; unknown pathological significance;, features a modification of the amino acid from G to R at position 1156.
+The protein's natural variant, known as in NEDBEH; unknown pathological significance;, features a modification of the amino acid from P to R at position 1262.
+The protein's natural variant, known as in NEDBEH; unknown pathological significance;, features a modification of the amino acid from H to Q at position 1431.
+The protein's natural variant, known as in strain: B/r; AA sequence, features a modification of the amino acid from Q to E at position 88.
+The protein's natural variant, known as in strain: B/r; AA sequence, features a modification of the amino acid from E to G at position 139.
+The protein's natural variant, known as in strain: B/r; AA sequence, features a modification of the amino acid from Q to L at position 284.
+The protein's natural variant, known as in strain: 88A, 195A, 217A, 223A, 233A, 256A, 360A, 380A, 482A, 554A, 639A, 716A, 790A, 820A and 855A, features a modification of the amino acid from K to R at position 49.
+The protein's natural variant, known as in strain: 40A, 822A and 832A, features a modification of the amino acid from A to G at position 139.
+The protein's natural variant, known as de novo variant found in a patient with childhood apraxia of speech; unknown pathological significance, features a modification of the amino acid from T to M at position 208.
+The protein's natural variant, known as in strain: FA19, features a modification of the amino acid from DR to AA at position 73.
+The protein's natural variant, known as in WRS;, features a modification of the amino acid from R to Q at position 588.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to C at position 167.
+The protein's natural variant, known as in MC4DN7; severely reduced COX6B1 protein levels in patient muscle, features a modification of the amino acid from R to C at position 20.
+The protein's natural variant, known as in MC4DN7;, features a modification of the amino acid from R to H at position 20.
+The natural variant of this protein is characterized by an amino acid alteration from L to S at position 492.
+The protein's natural variant, known as in strain: PAC174, features a modification of the amino acid from R to G at position 4.
+The protein's natural variant, known as in strain: PAC174, features a modification of the amino acid from D to A at position 91.
+The protein's natural variant, known as in strain: PAC174, features a modification of the amino acid from Q to P at position 111.
+The protein's natural variant, known as in strain: PAC174, features a modification of the amino acid from S to P at position 114.
+The protein's natural variant, known as in strain: PAC174, features a modification of the amino acid from V to A at position 145.
+The protein's natural variant, known as in strain: PAC174, features a modification of the amino acid from R to C at position 337.
+The protein's natural variant, known as in FSGS6; results in altered clathrin-coated vesicle dynamics when expressed in a heterolgous system; severely decreased localization to cell-cell junctions and clathrin-coated vesicles, features a modification of the amino acid from T to I at position 119.
+The protein's natural variant, known as in FSGS6; the mutant shows diffuse cytosolic localization with a punctate pattern;, features a modification of the amino acid from A to P at position 159.
+The protein's natural variant, known as in FSGS6; loss of microfilament motor activity; results in altered clathrin-coated vesicle dynamics when expressed in a heterolgous system; no effect on localization to cell-cell junctions and clathrin-coated vesicles, features a modification of the amino acid from D to H at position 388.
+The protein's natural variant, known as probable disease-associated variant found in a patient with steroid-resistant nephrotic syndrome, features a modification of the amino acid from R to W at position 523.
+The protein's natural variant, known as in CRSD;, features a modification of the amino acid from R to C at position 124.
+The natural variant of this protein is characterized by an amino acid alteration from K to N at position 13.
+The protein's natural variant, known as in CSNB1F, features a modification of the amino acid from W to L at position 203.
+The protein's natural variant, known as in CSNB1F;, features a modification of the amino acid from C to Y at position 328.
+The protein's natural variant, known as in one non-syndromic craniosynostosis patient; unknown pathological significance, features a modification of the amino acid from S to T at position 494.
+The protein's natural variant, known as found in a patient with non-syndromic craniosynostosis; unknown pathological significance;, features a modification of the amino acid from C to Y at position 592.
+The protein's natural variant, known as found in a clear cell renal carcinoma case; somatic mutation, features a modification of the amino acid from T to P at position 173.
+The protein's natural variant, known as in PLGD; common mutation;, features a modification of the amino acid from K to E at position 38.
+The protein's natural variant, known as in PLGD;, features a modification of the amino acid from L to P at position 147.
+The protein's natural variant, known as in PLGD; severe type 1 deficiency;, features a modification of the amino acid from R to H at position 235.
+The protein's natural variant, known as in HAE4;, features a modification of the amino acid from K to E at position 330.
+The protein's natural variant, known as in PLGD; Nagoya-1;, features a modification of the amino acid from V to F at position 374.
+The protein's natural variant, known as in PLGD, features a modification of the amino acid from R to H at position 532.
+The protein's natural variant, known as in PLGD; may be associated with susceptibility to thrombosis;, features a modification of the amino acid from S to P at position 591.
+The protein's natural variant, known as in PLGD; type 2 plasminogen deficiency; decreased activity; Nagoya-2/Tochigi/Kagoshima; may be associated with susceptibility to thrombosis;, features a modification of the amino acid from A to T at position 620.
+The protein's natural variant, known as in HAE4; unknown pathological significance;, features a modification of the amino acid from V to E at position 728.
+The protein's natural variant, known as in PLGD; Kanagawa-1; 50% activity;, features a modification of the amino acid from G to R at position 751.
+The protein's natural variant, known as found in infertile men; unknown pathological significance; decreased induction of target genes expression;, features a modification of the amino acid from G to R at position 227.
+The protein's natural variant, known as in PFBMFT5; decreased levels of mature TERC in patient cells consistent with impaired function in RNA processing; decreased levels of mutant protein in patient cells, features a modification of the amino acid from P to L at position 186.
+The natural variant of this protein is characterized by an amino acid alteration from V to Q at position 39.
+The natural variant of this protein is characterized by an amino acid alteration from S to T at position 48.
+The natural variant of this protein is characterized by an amino acid alteration from V to A at position 56.
+The natural variant of this protein is characterized by an amino acid alteration from S to A at position 62.
+The natural variant of this protein is characterized by an amino acid alteration from S to A at position 63.
+The natural variant of this protein is characterized by an amino acid alteration from Y to I at position 76.
+The natural variant of this protein is characterized by an amino acid alteration from G to S at position 78.
+The natural variant of this protein is characterized by an amino acid alteration from G to Y at position 80.
+The natural variant of this protein is characterized by an amino acid alteration from F to Y at position 89.
+The protein's natural variant, known as in CARDAR; results in intracellular retention and degradation of the mutant protein;, features a modification of the amino acid from T to R at position 59.
+The protein's natural variant, known as in LYNCH1;, features a modification of the amino acid from A to T at position 2.
+The protein's natural variant, known as decreases protein levels;, features a modification of the amino acid from P to Q at position 5.
+The protein's natural variant, known as in CRC; unknown pathological significance;, features a modification of the amino acid from S to I at position 13.
+The protein's natural variant, known as in gastric cancer; unknown pathological significance; cryptic acceptor splice site suppressed on ex vivo splicing assay;, features a modification of the amino acid from V to F at position 17.
+The protein's natural variant, known as in LYNCH1; decreased mismatch repair activity;, features a modification of the amino acid from T to P at position 33.
+The protein's natural variant, known as in CRC; unknown pathological significance;, features a modification of the amino acid from G to S at position 40.
+The protein's natural variant, known as in LYNCH1; unknown pathological significance; no decrease in mismatch repair activity;, features a modification of the amino acid from T to M at position 44.
+The protein's natural variant, known as in LYNCH1; unknown pathological significance; no decrease in mismatch repair activity;, features a modification of the amino acid from A to V at position 45.
+The protein's natural variant, known as in LYNCH1;, features a modification of the amino acid from H to Q at position 46.
+The protein's natural variant, known as decreases protein levels;, features a modification of the amino acid from R to G at position 55.
+The protein's natural variant, known as in LYNCH1;, features a modification of the amino acid from L to F at position 93.
+The protein's natural variant, known as in LYNCH1; unknown pathological significance;, features a modification of the amino acid from Y to C at position 98.
+The protein's natural variant, known as in LYNCH1;, features a modification of the amino acid from V to I at position 102.
+The protein's natural variant, known as in LYNCH1; somatic mutation, features a modification of the amino acid from K to T at position 110.
+The protein's natural variant, known as in LYNCH1; presumed to enhance cancer risk considerably when associated with P-328; shows significantly decreased repair efficiency when associated with variant P-328;, features a modification of the amino acid from N to S at position 127.
+The protein's natural variant, known as in LYNCH1;, features a modification of the amino acid from N to S at position 139.
+The protein's natural variant, known as in LYNCH1; unknown pathological significance; normal mismatch repair activity;, features a modification of the amino acid from I to M at position 145.
+The protein's natural variant, known as in LYNCH1; decreased mismatch repair activity; affects protein stability; loss of protein expression;, features a modification of the amino acid from V to D at position 161.
+The protein's natural variant, known as in LYNCH1;, features a modification of the amino acid from G to A at position 162.
+The protein's natural variant, known as in LYNCH1; decreased mismatch repair activity; associated with an abnormal subcellular localization pattern; affects protein stability; loss of protein expression;, features a modification of the amino acid from G to R at position 162.
+The protein's natural variant, known as in LYNCH1;, features a modification of the amino acid from V to D at position 163.
+The protein's natural variant, known as in LYNCH1;, features a modification of the amino acid from V to G at position 163.
+The protein's natural variant, known as in LYNCH1; decreased mismatch repair activity; affects protein stability; loss of protein expression;, features a modification of the amino acid from G to R at position 164.
+The protein's natural variant, known as in LYNCH1; unknown pathological significance; decreased mismatch repair activity;, features a modification of the amino acid from Y to D at position 165.
+The protein's natural variant, known as in LYNCH1; shows reduced mismatch binding; does not show a decreased expression level of the MutS alpha complex; not associated with an abnormal subcellular localization pattern; normal mismatch repair activity;, features a modification of the amino acid from D to H at position 167.
+The protein's natural variant, known as in LYNCH1 and CRC; unknown pathological significance;, features a modification of the amino acid from I to V at position 169.
+The protein's natural variant, known as in LYNCH1; decreased mismatch repair activity; affects protein stability; loss of protein expression;, features a modification of the amino acid from L to P at position 173.
+The protein's natural variant, known as in LYNCH1;, features a modification of the amino acid from L to P at position 175.
+The protein's natural variant, known as in LYNCH1; requires 2 nucleotide substitutions; unknown pathological significance; normal mismatch repair activity, features a modification of the amino acid from E to H at position 177.
+The protein's natural variant, known as in LYNCH1; decreased mismatch repair activity; affects protein stability; loss of protein expression;, features a modification of the amino acid from L to P at position 187.
+The protein's natural variant, known as in LYNCH1; decreased mismatch repair activity; loss of protein expression;, features a modification of the amino acid from L to R at position 187.
+The protein's natural variant, known as in LYNCH1;, features a modification of the amino acid from E to G at position 198.
+The protein's natural variant, known as in glioma; also associated with LYNCH1; no effect on MSH2 splicing;, features a modification of the amino acid from C to R at position 199.
+The protein's natural variant, known as in CRC; unknown pathological significance; somatic mutation;, features a modification of the amino acid from G to R at position 203.
+The protein's natural variant, known as shows no defects; normal mismatch repair activity;, features a modification of the amino acid from E to Q at position 205.
+The protein's natural variant, known as in LYNCH1; unknown pathological significance; shows slightly reduced mismatch binding or release efficiency;, features a modification of the amino acid from I to V at position 216.
+The protein's natural variant, known as in LYNCH1; unknown pathological significance;, features a modification of the amino acid from K to Q at position 246.
+The protein's natural variant, known as in LYNCH1; unknown pathological significance; shows slightly reduced mismatch binding or release efficiency; results in partial MSH2 exon 5 skipping; normal mismatch repair activity;, features a modification of the amino acid from A to V at position 272.
+The protein's natural variant, known as in LYNCH1;, features a modification of the amino acid from D to Y at position 283.
+The protein's natural variant, known as in LYNCH1; normal mismatch repair activity;, features a modification of the amino acid from A to T at position 305.
+The protein's natural variant, known as may be associated with increased colorectal cancer susceptibility; shows significantly decreased repair efficiency when associated with variant E-487;, features a modification of the amino acid from G to D at position 322.
+The protein's natural variant, known as in LYNCH1; unknown pathological significance;, features a modification of the amino acid from S to C at position 323.
+The protein's natural variant, known as in LYNCH1; unknown pathological significance;, features a modification of the amino acid from S to Y at position 323.
+The protein's natural variant, known as shows significantly decreased repair efficiency when associated with variant S-127; presumed to enhance cancer risk considerably when associated with variant S-127;, features a modification of the amino acid from A to P at position 328.
+The protein's natural variant, known as in LYNCH1; no effect on MSH2 splicing;, features a modification of the amino acid from N to D at position 331.
+The protein's natural variant, known as in LYNCH1; decreased mismatch repair activity; affects protein stability; loss of protein expression;, features a modification of the amino acid from C to Y at position 333.
+The protein's natural variant, known as in LYNCH1; unknown pathological significance;, features a modification of the amino acid from T to I at position 335.
+The protein's natural variant, known as in LYNCH1;, features a modification of the amino acid from P to S at position 336.
+The protein's natural variant, known as in CRC; unknown pathological significance;, features a modification of the amino acid from V to I at position 342.
+The protein's natural variant, known as in LYNCH1;, features a modification of the amino acid from P to L at position 349.
+The protein's natural variant, known as in LYNCH1; shows a decreased expression level of the MutS alpha complex; associated with an abnormal subcellular localization pattern;, features a modification of the amino acid from R to S at position 359.
+The protein's natural variant, known as shows no defects; normal mismatch repair activity;, features a modification of the amino acid from V to I at position 367.
+The protein's natural variant, known as in LYNCH1; unknown pathological significance; normal mismatch repair activity;, features a modification of the amino acid from P to L at position 385.
+The protein's natural variant, known as in LYNCH1 and CRC; unknown pathological significance; may decrease mismatch repair activity;, features a modification of the amino acid from L to F at position 390.
+The protein's natural variant, known as in LYNCH1;, features a modification of the amino acid from K to M at position 393.
+The protein's natural variant, known as in CRC; unknown pathological significance; decreased mismatch repair activity;, features a modification of the amino acid from Q to K at position 419.
+The protein's natural variant, known as in LYNCH1; has no effect on ex vivo splicing assay;, features a modification of the amino acid from V to E at position 470.
+The protein's natural variant, known as decreased mismatch repair activity; shows significantly decreased repair efficiency when associated with variant D-322;, features a modification of the amino acid from D to E at position 487.
+The protein's natural variant, known as in LYNCH1, features a modification of the amino acid from M to V at position 492.
+The protein's natural variant, known as in LYNCH1 and CRC; sporadic early-onset CRC; decreased mismatch repair activity;, features a modification of the amino acid from D to Y at position 506.
+The protein's natural variant, known as in LYNCH1; unknown pathological significance; normal mismatch repair activity;, features a modification of the amino acid from F to L at position 519.
+The protein's natural variant, known as in LYNCH1; decreased mismatch repair activity;, features a modification of the amino acid from R to P at position 524.
+The protein's natural variant, known as no effect on protein levels;, features a modification of the amino acid from R to P at position 534.
+The protein's natural variant, known as in LYNCH1;, features a modification of the amino acid from T to P at position 552.
+The protein's natural variant, known as in LYNCH1; unknown pathological significance;, features a modification of the amino acid from S to R at position 554.
+The protein's natural variant, known as in LYNCH1;, features a modification of the amino acid from E to V at position 562.
+The protein's natural variant, known as in LYNCH1; unknown pathological significance;, features a modification of the amino acid from T to A at position 564.
+The protein's natural variant, known as in LYNCH1;, features a modification of the amino acid from N to S at position 583.
+The protein's natural variant, known as in LYNCH1; unknown pathological significance;, features a modification of the amino acid from N to S at position 596.
+The protein's natural variant, known as in LYNCH1;, features a modification of the amino acid from A to V at position 600.
+The protein's natural variant, known as in LYNCH1; decreased mismatch repair activity; affects protein stability; loss of protein expression;, features a modification of the amino acid from D to N at position 603.
+The protein's natural variant, known as in LYNCH1; has no effect on MSH2 splicing;, features a modification of the amino acid from H to N at position 610.
+The protein's natural variant, known as in CRC; unknown pathological significance;, features a modification of the amino acid from Y to C at position 619.
+The protein's natural variant, known as in LYNCH1; decreased mismatch repair activity; confers multiple biochemical defects;, features a modification of the amino acid from P to L at position 622.
+The protein's natural variant, known as in LYNCH1; unknown pathological significance;, features a modification of the amino acid from Q to R at position 629.
+The protein's natural variant, known as in LYNCH1; decreased mismatch binding activity;, features a modification of the amino acid from A to P at position 636.
+The protein's natural variant, known as in LYNCH1; has no effect on MSH2 splicing;, features a modification of the amino acid from R to G at position 638.
+The protein's natural variant, known as in LYNCH1; decreased mismatch repair activity;, features a modification of the amino acid from H to R at position 639.
+The protein's natural variant, known as in LYNCH1; the equivalent substitution in yeast does not affect mismatch repair efficiency in vitro;, features a modification of the amino acid from H to Y at position 639.
+The protein's natural variant, known as in LYNCH1; has no effect on MSH2 splicing;, features a modification of the amino acid from Q to E at position 645.
+The protein's natural variant, known as in LYNCH1, features a modification of the amino acid from E to K at position 647.
+The protein's natural variant, known as in LYNCH1; somatic mutation;, features a modification of the amino acid from Y to H at position 656.
+The protein's natural variant, known as in LYNCH1;, features a modification of the amino acid from D to G at position 660.
+The protein's natural variant, known as in LYNCH1;, features a modification of the amino acid from G to R at position 669.
+The protein's natural variant, known as in LYNCH1; unknown pathological significance;, features a modification of the amino acid from N to Y at position 671.
+The protein's natural variant, known as in LYNCH1; decreased mismatch repair activity;, features a modification of the amino acid from G to A at position 674.
+The protein's natural variant, known as in LYNCH1; decreased mismatch repair activity;, features a modification of the amino acid from G to R at position 674.
+The protein's natural variant, known as in LYNCH1; somatic mutation;, features a modification of the amino acid from G to S at position 674.
+The protein's natural variant, known as in LYNCH1; requires 2 nucleotide substitutions; unknown pathological significance; decreased mismatch repair activity;, features a modification of the amino acid from K to A at position 675.
+The protein's natural variant, known as in LYNCH1; somatic mutation, features a modification of the amino acid from I to T at position 679.
+The protein's natural variant, known as in LYNCH1;, features a modification of the amino acid from M to I at position 688.
+The protein's natural variant, known as in LYNCH1; loss of protein expression, features a modification of the amino acid from M to V at position 688.
+The protein's natural variant, known as in LYNCH1;, features a modification of the amino acid from G to R at position 692.
+The protein's natural variant, known as in LYNCH1; has no effect on ex vivo splicing assay;, features a modification of the amino acid from P to L at position 696.
+The protein's natural variant, known as in LYNCH1; decreased mismatch repair activity; loss of protein expression; confers multiple biochemical defects;, features a modification of the amino acid from C to F at position 697.
+The protein's natural variant, known as in LYNCH1; has no effect on MSH2 splicing;, features a modification of the amino acid from C to R at position 697.
+The protein's natural variant, known as in LYNCH1; unknown pathological significance;, features a modification of the amino acid from A to V at position 714.
+The protein's natural variant, known as in LYNCH1;, features a modification of the amino acid from V to I at position 722.
+The protein's natural variant, known as in LYNCH1; decreased mismatch repair activity; has no effect on MSH2 splicing;, features a modification of the amino acid from S to F at position 723.
+The protein's natural variant, known as in LYNCH1; somatic mutation;, features a modification of the amino acid from M to V at position 729.
+The protein's natural variant, known as in LYNCH1; somatic mutation;, features a modification of the amino acid from T to I at position 732.
+The protein's natural variant, known as in LYNCH1; has no effect on MSH2 splicing;, features a modification of the amino acid from D to Y at position 748.
+The protein's natural variant, known as in LYNCH1; decreased mismatch repair activity; no loss of protein expression;, features a modification of the amino acid from E to K at position 749.
+The protein's natural variant, known as in LYNCH1; unknown pathological significance; decreased mismatch repair activity;, features a modification of the amino acid from G to E at position 759.
+The protein's natural variant, known as in LYNCH1; unknown pathological significance; normal mismatch repair activity, features a modification of the amino acid from L to V at position 805.
+The protein's natural variant, known as no effect on protein levels;, features a modification of the amino acid from M to I at position 813.
+The protein's natural variant, known as in LYNCH1;, features a modification of the amino acid from M to V at position 813.
+The protein's natural variant, known as in gastric cancer; unknown pathological significance;, features a modification of the amino acid from Q to E at position 824.
+The protein's natural variant, known as in LYNCH1; decreased mismatch repair activity; shows no functional defects in gel shift assay;, features a modification of the amino acid from A to T at position 834.
+The protein's natural variant, known as in LYNCH1; has no effect on MSH2 splicing;, features a modification of the amino acid from H to Q at position 839.
+The protein's natural variant, known as in LYNCH1; decreases protein levels;, features a modification of the amino acid from H to R at position 839.
+The protein's natural variant, known as in LYNCH1; unknown pathological significance; normal mismatch repair activity, features a modification of the amino acid from C to G at position 843.
+The protein's natural variant, known as in LYNCH1;, features a modification of the amino acid from K to E at position 845.
+The protein's natural variant, known as in LYNCH1; unknown pathological significance;, features a modification of the amino acid from E to A at position 853.
+The protein's natural variant, known as in LYNCH1; unknown pathological significance; normal mismatch repair activity;, features a modification of the amino acid from S to L at position 860.
+The protein's natural variant, known as in gastric cancer; unknown pathological significance;, features a modification of the amino acid from P to A at position 868.
+The protein's natural variant, known as in gastric cancer; unknown pathological significance;, features a modification of the amino acid from A to G at position 870.
+The protein's natural variant, known as in gastric cancer; unknown pathological significance;, features a modification of the amino acid from C to G at position 873.
+The protein's natural variant, known as in LYNCH1; unknown pathological significance; normal mismatch repair activity;, features a modification of the amino acid from E to G at position 886.
+The protein's natural variant, known as in LYNCH1; unknown pathological significance;, features a modification of the amino acid from T to R at position 905.
+The protein's natural variant, known as found in a colorectal cancer sample; normal mismatch repair activity;, features a modification of the amino acid from K to I at position 909.
+The protein's natural variant, known as in LYNCH1; unknown pathological significance;, features a modification of the amino acid from V to E at position 923.
+The protein's natural variant, known as in LYNCH1;, features a modification of the amino acid from K to T at position 931.
+The natural variant of this protein is characterized by an amino acid alteration from R to Q at position 37.
+The natural variant of this protein is characterized by an amino acid alteration from W to S at position 42.
+The natural variant of this protein is characterized by an amino acid alteration from Q to K at position 46.
+The natural variant of this protein is characterized by an amino acid alteration from H to R at position 55.
+The natural variant of this protein is characterized by an amino acid alteration from G to S at position 67.
+The protein's natural variant, known as in CESD; significant loss of enzyme activity;, features a modification of the amino acid from H to P at position 129.
+The protein's natural variant, known as in CESD; significant loss of enzyme activity;, features a modification of the amino acid from H to R at position 129.
+The protein's natural variant, known as in CESD and WOD;, features a modification of the amino acid from L to P at position 200.
+The protein's natural variant, known as in 6B1-2 and 6B1-3, features a modification of the amino acid from N to D at position 24.
+The protein's natural variant, known as in 6B1-2 and 6B1-3, features a modification of the amino acid from NS to KC at position 156.
+The protein's natural variant, known as in 6B1-2, features a modification of the amino acid from K to R at position 243.
+The protein's natural variant, known as in 6B1-2, features a modification of the amino acid from A to S at position 285.
+The protein's natural variant, known as in 6B1-2, features a modification of the amino acid from I to V at position 293.
+The protein's natural variant, known as in 6B1-2, features a modification of the amino acid from M to V at position 458.
+The protein's natural variant, known as in 6B1-2, features a modification of the amino acid from P to E at position 475.
+The protein's natural variant, known as in 6B1-2, features a modification of the amino acid from L to I at position 495.
+The protein's natural variant, known as found in a kidney cancer sample; no effect on activity; abolishes mitochondrial localization;, features a modification of the amino acid from G to E at position 12.
+The protein's natural variant, known as found in a clear cell renal cell carcinoma sample; somatic mutation; diminished activity;, features a modification of the amino acid from R to Q at position 46.
+The protein's natural variant, known as found in a lung cancer sample;, features a modification of the amino acid from A to S at position 85.
+The protein's natural variant, known as found in a lung cancer sample; loss of activity;, features a modification of the amino acid from R to Q at position 131.
+The protein's natural variant, known as found in a gastric cancer sample; no effect on base-excision activity; alters substrate specificity and strongly increases mutagenic mis-repair;, features a modification of the amino acid from R to H at position 154.
+The protein's natural variant, known as found in a kidney cancer sample, features a modification of the amino acid from S to T at position 232.
+The protein's natural variant, known as in ANPH1; decreases protein stability; leads to microtubules disruption; exhibits multipolar spindles; exhibits abnormal cytokinesis, features a modification of the amino acid from D to N at position 518.
+The protein's natural variant, known as may confer susceptibility to leprosy;, features a modification of the amino acid from N to S at position 248.
+The protein's natural variant, known as severe impairment of activity;, features a modification of the amino acid from P to L at position 315.
+The protein's natural variant, known as severe impairment of activity;, features a modification of the amino acid from Y to C at position 554.
+The protein's natural variant, known as severe impairment of activity;, features a modification of the amino acid from S to I at position 602.
+The protein's natural variant, known as severe impairment of activity;, features a modification of the amino acid from V to A at position 651.
+The natural variant of this protein is characterized by an amino acid alteration from V to A at position 674.
+The protein's natural variant, known as severe impairment of activity;, features a modification of the amino acid from H to P at position 720.
+The protein's natural variant, known as in allele TAPBP*01;, features a modification of the amino acid from T to R at position 260.
+The protein's natural variant, known as in strain: 7549, features a modification of the amino acid from A to S at position 152.
+The protein's natural variant, known as in a bladder carcinoma NOS sample; somatic mutation;, features a modification of the amino acid from G to E at position 370.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation;, features a modification of the amino acid from S to F at position 399.
+The protein's natural variant, known as found in a consanguineous family with intellectual disability; unknown pathological significance;, features a modification of the amino acid from G to S at position 376.
+The protein's natural variant, known as in strain: cv. Ag-0, cv. An-1, cv. Cvi-0, cv. Edi-0, cv. Kas-2, cv. Ll-0, cv. Nok-3, cv. Wassilewskija, cv. Wei-0 and cv. Wt-5, features a modification of the amino acid from Y to F at position 414.
+The protein's natural variant, known as in strain: cv. Ag-0, cv. An-1, cv. Cvi-0, cv. Edi-0, cv. Ei-2, cv. Gy-2, cv. Kas-2, cv. Ll-0, cv. Mt-0, cv. Nok-3, cv. Wassilewskija, cv. Wei-0 and cv. Wt-5, features a modification of the amino acid from S to P at position 518.
+The protein's natural variant, known as in mutant form UV25, features a modification of the amino acid from I to V at position 106.
+The protein's natural variant, known as in mutant form UV25, features a modification of the amino acid from S to G at position 111.
+The protein's natural variant, known as in mutant form UV25, features a modification of the amino acid from L to Q at position 240.
+The protein's natural variant, known as in mutant form UV25, features a modification of the amino acid from F to L at position 339.
+The protein's natural variant, known as in LGMDR25; reduces membrane localization of BVES and POPDC2; decreases by 50% affinity for cAMP; disrupts enhancement of KCKN2 surface expression; increases KCKN2 outward currents; no effect on total protein levels;, features a modification of the amino acid from S to F at position 201.
+The protein's natural variant, known as in strain: 129/J, 129/SvEv, AKR/J, BALB/c, C3H/HeJ, DBA/2J and DBA/2J, features a modification of the amino acid from T to A at position 55.
+The protein's natural variant, known as in strain: 129/J, 129/SvEv, AKR/J, BALB/c, C3H/HeJ, DBA/2J and DBA/2J; may influence the ability to form dimers or bind sweeteners, features a modification of the amino acid from I to T at position 60.
+The protein's natural variant, known as in strain: 129/J, 129/SvEv, AKR/J, BALB/c, C3H/HeJ, CAST/Ei, DBA/2J, FVB/N, ST/bJ and SWR/J, features a modification of the amino acid from P to L at position 61.
+The protein's natural variant, known as in strain: FVB/N, ST/bJ, SWR/J, features a modification of the amino acid from R to C at position 261.
+The protein's natural variant, known as in strain: 129/J, 129/SvEv, AKR/J, BALB/c, CAST/Ei, C3H/HeJ, DBA/2J, FVB/N, ST/bJ and SWR/J, features a modification of the amino acid from R to Q at position 371.
+The protein's natural variant, known as in strain: FVB/N, ST/bJ and SWR/J, features a modification of the amino acid from L to S at position 692.
+The protein's natural variant, known as in strain: SWR/J, features a modification of the amino acid from I to N at position 706.
+The protein's natural variant, known as in strain: 129/J, 129/SvEv, AKR/J, BALB/c, C3H/HeJ, DBA/2J, DBA/2J, FVB/N, ST/bJ and SWR/J, features a modification of the amino acid from I to T at position 706.
+The protein's natural variant, known as in strain: 129/J, AKR/J, CAST/Ei, DBA/2J and SWR/J, features a modification of the amino acid from G to E at position 855.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from R to C at position 465.
+The protein's natural variant, known as found in a patient with delayed psychomotor development, no speech and cataracts; no effect on binding to subunit PPP2CA; no effect on binding to subunit PPP2R1A;, features a modification of the amino acid from P to S at position 53.
+The protein's natural variant, known as in MRD35; decreases binding to subunit PPP2CA; decreases binding to subunit PPP2R1A;, features a modification of the amino acid from E to K at position 198.
+The protein's natural variant, known as in MRD35; decreases binding to subunit PPP2CA; decreases binding to subunit PPP2R1A;, features a modification of the amino acid from E to K at position 200.
+The protein's natural variant, known as in MRD35; decreases binding to subunit PPP2CA; decreases binding to subunit PPP2R1A;, features a modification of the amino acid from P to R at position 201.
+The protein's natural variant, known as in MRD35; decreases binding to subunit PPP2CA; decreases binding to subunit PPP2R1A;, features a modification of the amino acid from W to R at position 207.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation, features a modification of the amino acid from E to K at position 170.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation, features a modification of the amino acid from G to R at position 232.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to W at position 371.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation, features a modification of the amino acid from P to S at position 903.
+The natural variant of this protein is characterized by an amino acid alteration from L to F at position 297.
+The natural variant of this protein is characterized by an amino acid alteration from H to Y at position 946.
+The natural variant of this protein is characterized by an amino acid alteration from L to V at position 948.
+The natural variant of this protein is characterized by an amino acid alteration from H to D at position 955.
+The natural variant of this protein is characterized by an amino acid alteration from E to G at position 974.
+The natural variant of this protein is characterized by an amino acid alteration from G to A at position 990.
+The natural variant of this protein is characterized by an amino acid alteration from A to V at position 1543.
+The protein's natural variant, known as in MCPH11; significant reduction in mutant protein levels which is shown to result from proteasome-mediated degradation; patient cells show increased expression of GMNN and decreased interaction between the protein and ubiquitinated H2AC17 compared to control cells;, features a modification of the amino acid from L to F at position 992.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from G to S at position 121.
+The protein's natural variant, known as in PKDYS1; loss of dopamine:sodium symporter activity;, features a modification of the amino acid from L to Q at position 368.
+The protein's natural variant, known as in PKDYS1; loss of dopamine:sodium symporter activity;, features a modification of the amino acid from P to L at position 395.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from R to S at position 544.
+The protein's natural variant, known as in strain: 042B, features a modification of the amino acid from E to K at position 87.
+The protein's natural variant, known as in Omenn syndrome;, features a modification of the amino acid from H to D at position 35.
+The protein's natural variant, known as in RSSCID, features a modification of the amino acid from G to V at position 118.
+The protein's natural variant, known as in RSSCID, features a modification of the amino acid from G to E at position 135.
+The protein's natural variant, known as in BMFDMS, features a modification of the amino acid from Y to C at position 142.
+The protein's natural variant, known as in BMFDMS; unknown pathological significance, features a modification of the amino acid from R to W at position 173.
+The protein's natural variant, known as in BMFDMS; unknown pathological significance, features a modification of the amino acid from Y to C at position 227.
+The protein's natural variant, known as in strain: C57BL/6, features a modification of the amino acid from K to R at position 95.
+The protein's natural variant, known as in strain: C57BL/6, features a modification of the amino acid from P to L at position 160.
+The protein's natural variant, known as in strain: C57BL/6, features a modification of the amino acid from A to T at position 344.
+The natural variant of this protein is characterized by an amino acid alteration from Q to K at position 5.
+The protein's natural variant, known as in strain: cv. Kas-1, features a modification of the amino acid from E to K at position 19.
+The protein's natural variant, known as in strain: cv. Kas-1, features a modification of the amino acid from I to L at position 143.
+The protein's natural variant, known as in strain: cv. Kas-1, features a modification of the amino acid from V to I at position 980.
+The protein's natural variant, known as in strain: cv. Kas-1, features a modification of the amino acid from L to V at position 1072.
+The protein's natural variant, known as in allele B, features a modification of the amino acid from P to L at position 124.
+The protein's natural variant, known as in allele B, features a modification of the amino acid from Q to E at position 172.
+The protein's natural variant, known as in allele B, features a modification of the amino acid from V to A at position 192.
+The natural variant of this protein is characterized by an amino acid alteration from A to V at position 144.
+The protein's natural variant, known as in ICH; the mutant protein is retained intracellularly and is not secreted normally;, features a modification of the amino acid from P to L at position 352.
+The protein's natural variant, known as in HANAC;, features a modification of the amino acid from G to R at position 498.
+The protein's natural variant, known as in HANAC;, features a modification of the amino acid from G to V at position 498.
+The protein's natural variant, known as in HANAC and RATOR;, features a modification of the amino acid from G to R at position 510.
+The protein's natural variant, known as in HANAC;, features a modification of the amino acid from G to R at position 519.
+The protein's natural variant, known as in HANAC; requires 2 nucleotide substitutions;, features a modification of the amino acid from G to L at position 525.
+The protein's natural variant, known as in HANAC;, features a modification of the amino acid from G to E at position 528.
+The protein's natural variant, known as in ICH; the mutant protein is retained intracellularly and is not secreted normally;, features a modification of the amino acid from R to G at position 538.
+The protein's natural variant, known as in BSVD1;, features a modification of the amino acid from G to E at position 562.
+The protein's natural variant, known as in SCHZC, features a modification of the amino acid from G to R at position 655.
+The protein's natural variant, known as in BSVD1;, features a modification of the amino acid from G to R at position 708.
+The protein's natural variant, known as in BSVD1; diffuse small vessel disease of the brain associated with Axenfeld-Rieger anomaly and leukoencephalopathy;, features a modification of the amino acid from G to D at position 720.
+The protein's natural variant, known as in BSVD1;, features a modification of the amino acid from G to S at position 749.
+The protein's natural variant, known as in BSVD1; associated with ocular anomalies of variable severity in some patients;, features a modification of the amino acid from G to R at position 755.
+The protein's natural variant, known as in BSVD1;, features a modification of the amino acid from G to R at position 773.
+The protein's natural variant, known as in BSVD1;, features a modification of the amino acid from G to R at position 805.
+The protein's natural variant, known as in SCHZC;, features a modification of the amino acid from G to R at position 870.
+The protein's natural variant, known as in BSVD1, features a modification of the amino acid from G to D at position 882.
+The protein's natural variant, known as in SCHZC, features a modification of the amino acid from G to S at position 897.
+The protein's natural variant, known as in SCHZC;, features a modification of the amino acid from G to S at position 948.
+The protein's natural variant, known as in SCHZC, features a modification of the amino acid from G to E at position 1041.
+The protein's natural variant, known as in SCHZC, features a modification of the amino acid from G to E at position 1082.
+The protein's natural variant, known as in BSVD1;, features a modification of the amino acid from G to D at position 1130.
+The protein's natural variant, known as in BSVD1;, features a modification of the amino acid from G to R at position 1236.
+The protein's natural variant, known as in BSVD1, features a modification of the amino acid from G to R at position 1266.
+The protein's natural variant, known as in SCHZC;, features a modification of the amino acid from G to R at position 1326.
+The protein's natural variant, known as in SCHZC;, features a modification of the amino acid from G to D at position 1332.
+The protein's natural variant, known as in BSVD1;, features a modification of the amino acid from G to R at position 1423.
+The protein's natural variant, known as in BSVD1;, features a modification of the amino acid from G to R at position 1580.
+The protein's natural variant, known as in SCHZC;, features a modification of the amino acid from E to K at position 1615.
+The protein's natural variant, known as in BSVD1;, features a modification of the amino acid from N to K at position 1627.
+The natural variant of this protein is characterized by an amino acid alteration from I to L at position 190.
+The natural variant of this protein is characterized by an amino acid alteration from Q to E at position 194.
+The natural variant of this protein is characterized by an amino acid alteration from E to D at position 223.
+The natural variant of this protein is characterized by an amino acid alteration from K to R at position 312.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 403.
+The natural variant of this protein is characterized by an amino acid alteration from K to E at position 405.
+The natural variant of this protein is characterized by an amino acid alteration from S to P at position 411.
+The protein's natural variant, known as in strain: G7, features a modification of the amino acid from E to Q at position 17.
+The protein's natural variant, known as in strain: G7, features a modification of the amino acid from I to F at position 19.
+The protein's natural variant, known as in strain: G7, features a modification of the amino acid from S to A at position 28.
+The protein's natural variant, known as in strain: G7, features a modification of the amino acid from TQ to NR at position 40.
+The protein's natural variant, known as in strain: G7, features a modification of the amino acid from V to I at position 99.
+The protein's natural variant, known as in strain: G7, features a modification of the amino acid from G to S at position 109.
+The protein's natural variant, known as in strain: G7, features a modification of the amino acid from M to R at position 127.
+The protein's natural variant, known as in strain: G7, features a modification of the amino acid from N to D at position 130.
+The protein's natural variant, known as in strain: G7, features a modification of the amino acid from K to E at position 132.
+The natural variant of this protein is characterized by an amino acid alteration from C to Y at position 44.
+The protein's natural variant, known as in AS; unknown pathological significance;, features a modification of the amino acid from T to K at position 129.
+The protein's natural variant, known as may be associated with AS;, features a modification of the amino acid from C to R at position 140.
+The protein's natural variant, known as may be associated with AS;, features a modification of the amino acid from V to G at position 156.
+The protein's natural variant, known as in AS; unknown pathological significance;, features a modification of the amino acid from D to V at position 235.
+The protein's natural variant, known as in AS; unknown pathological significance;, features a modification of the amino acid from L to H at position 260.
+The protein's natural variant, known as in AS; unknown pathological significance, features a modification of the amino acid from L to Q at position 260.
+The protein's natural variant, known as in AS; unknown pathological significance;, features a modification of the amino acid from L to W at position 286.
+The protein's natural variant, known as may be associated with AS;, features a modification of the amino acid from N to T at position 293.
+The protein's natural variant, known as may be associated with AS;, features a modification of the amino acid from S to T at position 358.
+The natural variant of this protein is characterized by an amino acid alteration from S to P at position 372.
+The protein's natural variant, known as in AS; unknown pathological significance;, features a modification of the amino acid from L to P at position 458.
+The protein's natural variant, known as in AS; unknown pathological significance;, features a modification of the amino acid from P to L at position 481.
+The protein's natural variant, known as in AS; unknown pathological significance;, features a modification of the amino acid from R to P at position 500.
+The protein's natural variant, known as may be associated with AS;, features a modification of the amino acid from M to I at position 501.
+The protein's natural variant, known as in AS; unknown pathological significance;, features a modification of the amino acid from G to R at position 568.
+The protein's natural variant, known as in AS; unknown pathological significance;, features a modification of the amino acid from M to K at position 589.
+The protein's natural variant, known as in AS; unknown pathological significance;, features a modification of the amino acid from E to Q at position 607.
+The protein's natural variant, known as may be associated with AS;, features a modification of the amino acid from Q to E at position 611.
+The protein's natural variant, known as may be associated with AS;, features a modification of the amino acid from Q to P at position 611.
+The protein's natural variant, known as in AS; unknown pathological significance;, features a modification of the amino acid from T to I at position 679.
+The protein's natural variant, known as may be associated with AS;, features a modification of the amino acid from L to R at position 696.
+The protein's natural variant, known as in AS; unknown pathological significance;, features a modification of the amino acid from F to C at position 713.
+The protein's natural variant, known as may be associated with AS;, features a modification of the amino acid from V to I at position 785.
+The protein's natural variant, known as in AS, features a modification of the amino acid from I to II at position 826.
+The protein's natural variant, known as in AS; unknown pathological significance;, features a modification of the amino acid from P to L at position 850.
+The protein's natural variant, known as in HHRRD; loss of LGR5-, RNF43- and ZNRF3-binding; decreased ability to amplify WNT3A signaling;, features a modification of the amino acid from R to C at position 69.
+The protein's natural variant, known as in MACID; significant decrease of GFAP transcriptional activation;, features a modification of the amino acid from K to T at position 114.
+The protein's natural variant, known as in MACID; significant decrease of GFAP transcriptional activation;, features a modification of the amino acid from K to E at position 126.
+The protein's natural variant, known as in MACID; significant decrease of GFAP transcriptional activation;, features a modification of the amino acid from L to P at position 132.
+The protein's natural variant, known as in MACID; likely benign variant; does not affect GFAP transcriptional activation;, features a modification of the amino acid from S to L at position 356.
+The protein's natural variant, known as in SPG11; unknown pathological significance;, features a modification of the amino acid from S to L at position 412.
+The protein's natural variant, known as in SPG11; unknown pathological significance;, features a modification of the amino acid from P to L at position 1208.
+The protein's natural variant, known as in SPG11; unknown pathological significance;, features a modification of the amino acid from V to D at position 1270.
+The protein's natural variant, known as in SPG11;, features a modification of the amino acid from F to I at position 1349.
+The protein's natural variant, known as in SPG11; unknown pathological significance;, features a modification of the amino acid from L to P at position 2300.
+The protein's natural variant, known as in SPG11; unknown pathological significance;, features a modification of the amino acid from A to P at position 2334.
+The protein's natural variant, known as in strain: ATCC 28383 and ATCC 204626, features a modification of the amino acid from K to E at position 229.
+The protein's natural variant, known as in strain: ATCC 28383 and ATCC 204626, features a modification of the amino acid from H to R at position 295.
+The protein's natural variant, known as in strain: ATCC 28383 and ATCC 204626, features a modification of the amino acid from N to D at position 384.
+The protein's natural variant, known as in SPH2; spectrin Kissimmee;, features a modification of the amino acid from W to R at position 202.
+The protein's natural variant, known as in EL3; Cagliary;, features a modification of the amino acid from A to G at position 2018.
+The protein's natural variant, known as in EL3; Providence;, features a modification of the amino acid from S to P at position 2019.
+The protein's natural variant, known as in EL3; Paris;, features a modification of the amino acid from A to V at position 2023.
+The protein's natural variant, known as in EL3; Linguere;, features a modification of the amino acid from W to R at position 2024.
+The protein's natural variant, known as in EL3; Buffalo;, features a modification of the amino acid from L to R at position 2025.
+The protein's natural variant, known as in EL3; Kayes;, features a modification of the amino acid from A to P at position 2053.
+The protein's natural variant, known as in isoform 1, features a modification of the amino acid from Q to H at position 31.
+The protein's natural variant, known as in isoform 1, features a modification of the amino acid from L to P at position 36.
+The protein's natural variant, known as in isoform 1, features a modification of the amino acid from C to G at position 144.
+The protein's natural variant, known as in SRXY5;, features a modification of the amino acid from P to L at position 98.
+The protein's natural variant, known as in SRXY5;, features a modification of the amino acid from R to P at position 443.
+The protein's natural variant, known as in PHOAR2;, features a modification of the amino acid from I to F at position 85.
+The protein's natural variant, known as in PHOAR2;, features a modification of the amino acid from R to H at position 97.
+The protein's natural variant, known as in PHOAR2, features a modification of the amino acid from G to A at position 181.
+The protein's natural variant, known as in PHOAR2, features a modification of the amino acid from G to D at position 181.
+The protein's natural variant, known as in PHOAR2, features a modification of the amino acid from G to R at position 181.
+The protein's natural variant, known as in PHOAR2;, features a modification of the amino acid from S to L at position 204.
+The protein's natural variant, known as in PHOAR2 and PHOAD;, features a modification of the amino acid from G to R at position 222.
+The protein's natural variant, known as in PHOAR2;, features a modification of the amino acid from G to E at position 255.
+The protein's natural variant, known as in PHOAR2, features a modification of the amino acid from G to R at position 255.
+The protein's natural variant, known as in PHOAR2; unknown pathological significance, features a modification of the amino acid from F to S at position 328.
+The protein's natural variant, known as in PHOAR2 and PHOAD; unknown pathological significance, features a modification of the amino acid from G to D at position 369.
+The protein's natural variant, known as in PHOAR2; unknown pathological significance, features a modification of the amino acid from P to L at position 374.
+The protein's natural variant, known as in PHOAR2; unknown pathological significance, features a modification of the amino acid from G to E at position 379.
+The protein's natural variant, known as in PHOAR2; reduced activity;, features a modification of the amino acid from C to F at position 420.
+The protein's natural variant, known as in PHOAR2; unknown pathological significance;, features a modification of the amino acid from E to K at position 465.
+The protein's natural variant, known as in PHOAD; unknown pathological significance, features a modification of the amino acid from G to R at position 554.
+The protein's natural variant, known as in PHOAR2, features a modification of the amino acid from Q to H at position 556.
+The protein's natural variant, known as in PHOAR2, features a modification of the amino acid from F to S at position 557.
+The protein's natural variant, known as in PHOAR2, features a modification of the amino acid from W to G at position 565.
+The protein's natural variant, known as in strain: TN106, features a modification of the amino acid from V to L at position 2.
+The protein's natural variant, known as in strain: TN106, features a modification of the amino acid from I to V at position 25.
+The protein's natural variant, known as in strain: TN106, features a modification of the amino acid from S to N at position 42.
+The protein's natural variant, known as in strain: TN106, features a modification of the amino acid from R to S at position 58.
+The protein's natural variant, known as in strain: TN106, features a modification of the amino acid from V to E at position 100.
+The protein's natural variant, known as in strain: TN106, features a modification of the amino acid from S to N at position 144.
+The protein's natural variant, known as in medjo, features a modification of the amino acid from A to T at position 1317.
+The protein's natural variant, known as in strain: CCRC 21164 and ATCC 26077 / CBS 2863, features a modification of the amino acid from M to K at position 32.
+The protein's natural variant, known as in strain: CCRC 21164, features a modification of the amino acid from S to G at position 36.
+The protein's natural variant, known as in strain: ATCC 26077 / CBS 2863, features a modification of the amino acid from Y to I at position 73.
+The protein's natural variant, known as in strain: CCRC 21164, features a modification of the amino acid from N to S at position 280.
+The protein's natural variant, known as in strain: CCRC 21164 and ATCC 26077 / CBS 2863, features a modification of the amino acid from D to A at position 350.
+The protein's natural variant, known as in strain: CCRC 21164 and ATCC 26077 / CBS 2863, features a modification of the amino acid from L to S at position 479.
+The protein's natural variant, known as in strain: CCRC 21164, features a modification of the amino acid from S to F at position 483.
+The protein's natural variant, known as in OCABSN; no effect on protein levels and cell membrane location; lower binding affinity for CXCL12;, features a modification of the amino acid from V to M at position 258.
+The natural variant of this protein is characterized by an amino acid alteration from L to Q at position 77.
+The natural variant of this protein is characterized by an amino acid alteration from K to R at position 101.
+The natural variant of this protein is characterized by an amino acid alteration from T to K at position 111.
+The natural variant of this protein is characterized by an amino acid alteration from Q to K at position 281.
+The protein's natural variant, known as in HPABH4C; severe;, features a modification of the amino acid from L to P at position 14.
+The protein's natural variant, known as in HPABH4C; severe;, features a modification of the amino acid from G to R at position 17.
+The protein's natural variant, known as in HPABH4C; severe, features a modification of the amino acid from G to V at position 17.
+The protein's natural variant, known as in HPABH4C; severe;, features a modification of the amino acid from G to D at position 18.
+The protein's natural variant, known as in HPABH4C; severe;, features a modification of the amino acid from G to D at position 23.
+The protein's natural variant, known as in HPABH4C;, features a modification of the amino acid from W to R at position 36.
+The natural variant of this protein is characterized by an amino acid alteration from S to T at position 51.
+The protein's natural variant, known as in HPABH4C; severe;, features a modification of the amino acid from Q to R at position 66.
+The protein's natural variant, known as in HPABH4C;, features a modification of the amino acid from L to P at position 74.
+The protein's natural variant, known as in HPABH4C;, features a modification of the amino acid from W to G at position 108.
+The protein's natural variant, known as in HPABH4C, features a modification of the amino acid from T to TT at position 123.
+The protein's natural variant, known as in HPABH4C;, features a modification of the amino acid from P to L at position 145.
+The protein's natural variant, known as in HPABH4C;, features a modification of the amino acid from G to R at position 149.
+The protein's natural variant, known as in HPABH4C; mild;, features a modification of the amino acid from Y to C at position 150.
+The protein's natural variant, known as in HPABH4C; mild, features a modification of the amino acid from G to S at position 151.
+The protein's natural variant, known as in HPABH4C; severe;, features a modification of the amino acid from H to Y at position 158.
+The protein's natural variant, known as in HPABH4C;, features a modification of the amino acid from G to S at position 170.
+The protein's natural variant, known as in HPABH4C; mild;, features a modification of the amino acid from F to C at position 212.
+The protein's natural variant, known as in HPABH4C; mild, features a modification of the amino acid from G to GITG at position 218.
+The protein's natural variant, known as in strain: NOD, features a modification of the amino acid from E to V at position 104.
+The protein's natural variant, known as in strain: C57BL/6J, features a modification of the amino acid from E to G at position 145.
+The protein's natural variant, known as in strain: C57BL/6, features a modification of the amino acid from T to P at position 180.
+The protein's natural variant, known as in strain: LG/J and NOD, features a modification of the amino acid from R to Q at position 261.
+The protein's natural variant, known as in strain: LG/J and NOD, features a modification of the amino acid from V to M at position 292.
+The protein's natural variant, known as in strain: C57BL/6J, features a modification of the amino acid from D to E at position 402.
+The protein's natural variant, known as in strain: C57BL/6J, features a modification of the amino acid from P to S at position 679.
+The protein's natural variant, known as in strain: LG/J and NOD, features a modification of the amino acid from E to D at position 694.
+The protein's natural variant, known as in strain: NOD, features a modification of the amino acid from I to F at position 696.
+The protein's natural variant, known as in strain: LG/J and NOD, features a modification of the amino acid from S to P at position 777.
+The protein's natural variant, known as in strain: LG/J and NOD, features a modification of the amino acid from E to G at position 782.
+The natural variant of this protein is characterized by an amino acid alteration from D to L at position 96.
+The protein's natural variant, known as in NBIA1; no effect on enzyme activity or its mitochondrial localization;, features a modification of the amino acid from E to G at position 134.
+The protein's natural variant, known as in NBIA1; atypical; loss of enzyme activity; no effect on its mitochondrial localization, features a modification of the amino acid from G to V at position 219.
+The protein's natural variant, known as in NBIA1; atypical; unknown pathological significance, features a modification of the amino acid from D to G at position 232.
+The protein's natural variant, known as in NBIA1; atypical; no effect on enzyme activity or its mitochondrial localization;, features a modification of the amino acid from T to A at position 234.
+The protein's natural variant, known as in NBIA1, features a modification of the amino acid from R to P at position 249.
+The protein's natural variant, known as in NBIA1; no effect on enzyme activity;, features a modification of the amino acid from R to W at position 264.
+The protein's natural variant, known as in NBIA1; atypical;, features a modification of the amino acid from R to C at position 278.
+The protein's natural variant, known as in NBIA1;, features a modification of the amino acid from R to L at position 278.
+The protein's natural variant, known as in NBIA1, features a modification of the amino acid from L to V at position 282.
+The protein's natural variant, known as in NBIA1; no effect on enzyme activity;, features a modification of the amino acid from R to C at position 286.
+The protein's natural variant, known as in NBIA1; atypical;, features a modification of the amino acid from E to D at position 322.
+The protein's natural variant, known as in NBIA1;, features a modification of the amino acid from E to G at position 322.
+The protein's natural variant, known as in NBIA1; no effect on enzyme activity, features a modification of the amino acid from T to I at position 327.
+The protein's natural variant, known as in NBIA1; atypical; no effect on enzyme activity;, features a modification of the amino acid from S to P at position 351.
+The protein's natural variant, known as in NBIA1; atypical;, features a modification of the amino acid from N to S at position 355.
+The protein's natural variant, known as in NBIA1;, features a modification of the amino acid from R to Q at position 357.
+The protein's natural variant, known as in NBIA1; atypical; unknown pathological significance, features a modification of the amino acid from F to S at position 377.
+The protein's natural variant, known as in NBIA1;, features a modification of the amino acid from A to T at position 398.
+The protein's natural variant, known as in NBIA1; atypical; no effect on enzyme activity or its inhibition by acetyl CoA;, features a modification of the amino acid from N to I at position 404.
+The protein's natural variant, known as in NBIA1;, features a modification of the amino acid from L to P at position 413.
+The protein's natural variant, known as in NBIA1;, features a modification of the amino acid from C to Y at position 428.
+The protein's natural variant, known as in NBIA1, features a modification of the amino acid from D to N at position 447.
+The protein's natural variant, known as in NBIA1; significant loss of enzyme activity; no effect on its mitochondrial localization or its inhibition by acetyl CoA;, features a modification of the amino acid from S to N at position 471.
+The protein's natural variant, known as in NBIA1; unknown pathological significance, features a modification of the amino acid from L to P at position 489.
+The protein's natural variant, known as in NBIA1, features a modification of the amino acid from I to T at position 497.
+The protein's natural variant, known as in NBIA1; significant loss of enzyme activity;, features a modification of the amino acid from N to I at position 500.
+The protein's natural variant, known as in NBIA1; atypical;, features a modification of the amino acid from I to T at position 501.
+The protein's natural variant, known as in NBIA1; no effect on enzyme activity, features a modification of the amino acid from A to V at position 509.
+The protein's natural variant, known as in NBIA1;, features a modification of the amino acid from N to D at position 511.
+The protein's natural variant, known as in NBIA1; classic and atypical forms; loss of enzyme activity; no effect on its mitochondrial localization; loss of proteolytic cleavage to yield the mature form;, features a modification of the amino acid from G to R at position 521.
+The protein's natural variant, known as in NBIA1; classic and atypical forms; unknown pathological significance; no effect on enzyme activity, mitochondrial localization or its inhibition by acetyl CoA;, features a modification of the amino acid from T to M at position 528.
+The protein's natural variant, known as in NBIA1; no effect on enzyme activity, features a modification of the amino acid from R to W at position 532.
+The protein's natural variant, known as in NBIA1; atypical; unknown pathological significance, features a modification of the amino acid from G to S at position 555.
+The protein's natural variant, known as in NBIA1;, features a modification of the amino acid from L to P at position 563.
+The protein's natural variant, known as in NBIA1; atypical;, features a modification of the amino acid from P to L at position 570.
+The protein's natural variant, known as in SRTD15;, features a modification of the amino acid from L to V at position 117.
+The protein's natural variant, known as in SRTD15;, features a modification of the amino acid from T to I at position 220.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to Q at position 637.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from A to V at position 763.
+The protein's natural variant, known as in strain: cv. Kinmaze, features a modification of the amino acid from M to V at position 737.
+The protein's natural variant, known as in strain: cv. Kinmaze, features a modification of the amino acid from L to F at position 781.
+The protein's natural variant, known as in Mr1.7b, features a modification of the amino acid from G to S at position 69.
+The protein's natural variant, known as in strain: cv. Lemont, features a modification of the amino acid from Y to S at position 224.
+The protein's natural variant, known as in strain: cv. Rexmont, features a modification of the amino acid from P to S at position 415.
+The natural variant of this protein is characterized by an amino acid alteration from N to I at position 146.
+The natural variant of this protein is characterized by an amino acid alteration from R to L at position 220.
+The natural variant of this protein is characterized by an amino acid alteration from D to G at position 228.
+The protein's natural variant, known as found in a family diagnosed with orofaciodigital syndrome; unknown pathological significance; reduced cilia formation in patient fibroblasts compared to control;, features a modification of the amino acid from N to K at position 102.
+The protein's natural variant, known as in strain: ct96_6.1s, hfl97_4.1s, ga96_2.1s and va96_8.1s, features a modification of the amino acid from F to L at position 127.
+The protein's natural variant, known as in MC1DN19; hypomorphic variant in vitro;, features a modification of the amino acid from R to W at position 352.
+The protein's natural variant, known as in MC1DN19; hypomorphic variant in vitro;, features a modification of the amino acid from N to S at position 430.
+The protein's natural variant, known as in MGORS7; decreased protein level;, features a modification of the amino acid from Q to R at position 68.
+The protein's natural variant, known as in MGORS7; decreased protein level;, features a modification of the amino acid from N to H at position 76.
+The protein's natural variant, known as in MGORS7; unknown pathological significance; associated in cis with T-321;, features a modification of the amino acid from E to G at position 155.
+The protein's natural variant, known as in MGORS7; decreased protein level;, features a modification of the amino acid from R to C at position 157.
+The protein's natural variant, known as in MGORS7; decreased protein level;, features a modification of the amino acid from D to G at position 226.
+The protein's natural variant, known as in MGORS7; unknown pathological significance;, features a modification of the amino acid from S to Y at position 264.
+The protein's natural variant, known as in MGORS7; decreased protein level;, features a modification of the amino acid from A to V at position 298.
+The protein's natural variant, known as in MGORS7; unknown pathological significance; associated in cis with G-155, features a modification of the amino acid from P to T at position 321.
+The protein's natural variant, known as in MGORS7; unknown pathological significance;, features a modification of the amino acid from P to L at position 463.
+The protein's natural variant, known as in MGORS7; unknown pathological significance;, features a modification of the amino acid from P to L at position 496.
+The protein's natural variant, known as in MGORS7; unknown pathological significance;, features a modification of the amino acid from R to W at position 554.
+The protein's natural variant, known as in rpsD101; suppresses a temperature-sensitive mutant of release factor 1, R137P. Not a ram mutation, features a modification of the amino acid from Y to D at position 51.
+The protein's natural variant, known as in rpsD12; suppresses streptomycin dependence in protein S12. A ram mutation, features a modification of the amino acid from KMEGTFKRKPERSDLSADINEHLIVELYSK to GRYV at position 206.
+The protein's natural variant, known as in rpsD14; suppresses streptomycin dependence in protein S12. A ram mutation, features a modification of the amino acid from EGTFKRKPERSDLSADINEHLIVELYSK to ARYV at position 206.
+The protein's natural variant, known as in IMD59; unknown pathological significance, features a modification of the amino acid from Y to H at position 231.
+The protein's natural variant, known as in IMD59; unknown pathological significance, features a modification of the amino acid from A to P at position 419.
+The protein's natural variant, known as in PAPAS; severely reduced binding with PTPN12; markedly increased binding to MEFV; accentuates IL1B secretion; no effect on filament formation; increased induction of MEFV in response to retroviral infection;, features a modification of the amino acid from A to T at position 230.
+The protein's natural variant, known as in PAPAS;, features a modification of the amino acid from E to K at position 250.
+The protein's natural variant, known as in PAPAS; severely reduced binding with PTPN12; markedly increased binding to MEFV; accentuates IL1B secretion; increased induction of MEFV in response to retroviral infection;, features a modification of the amino acid from E to Q at position 250.
+The natural variant of this protein is characterized by an amino acid alteration from N to D at position 393.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from R to Q at position 144.
+The protein's natural variant, known as in allele CYP3A4*14;, features a modification of the amino acid from L to P at position 15.
+The protein's natural variant, known as in allele CYP3A4*7;, features a modification of the amino acid from G to D at position 56.
+The protein's natural variant, known as in allele CYP3A4*4; significant decrease in catalytic efficiency;, features a modification of the amino acid from I to V at position 118.
+The protein's natural variant, known as in allele CYP3A4*8;, features a modification of the amino acid from R to Q at position 130.
+The protein's natural variant, known as in allele CYP3A4*15;, features a modification of the amino acid from R to Q at position 162.
+The protein's natural variant, known as in allele CYP3A4*9;, features a modification of the amino acid from V to I at position 170.
+The protein's natural variant, known as in allele CYP3A4*10;, features a modification of the amino acid from D to H at position 174.
+The protein's natural variant, known as in allele CYP3A4*16;, features a modification of the amino acid from T to S at position 185.
+The protein's natural variant, known as in allele CYP3A4*17; exhibits lower turnover numbers for testosterone and chlorpyrifos;, features a modification of the amino acid from F to S at position 189.
+The protein's natural variant, known as in allele CYP3A4*5;, features a modification of the amino acid from P to R at position 218.
+The protein's natural variant, known as in allele CYP3A4*2; exhibits a lower intrinsic clearance toward nifedipine;, features a modification of the amino acid from S to P at position 222.
+The protein's natural variant, known as in allele CYP3A4*18; exhibits higher turnover numbers for testosterone and chlorpyrifos;, features a modification of the amino acid from L to P at position 293.
+The protein's natural variant, known as in VDDR3; 10-fold increased activity towards calcitriol; no effect in protein abundance; decreased activity for non-vitamin D substrates;, features a modification of the amino acid from I to T at position 301.
+The protein's natural variant, known as in allele CYP3A4*11; unstable form;, features a modification of the amino acid from T to M at position 363.
+The protein's natural variant, known as in allele CYP3A4*12; has an altered testosterone hydroxylase activity;, features a modification of the amino acid from L to F at position 373.
+The protein's natural variant, known as in allele CYP3A4*13; lack of expression;, features a modification of the amino acid from P to L at position 416.
+The protein's natural variant, known as in allele CYP3A4*3;, features a modification of the amino acid from M to T at position 445.
+The protein's natural variant, known as in allele CYP3A4*19;, features a modification of the amino acid from P to S at position 467.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from T to M at position 108.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from E to K at position 492.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from D to N at position 617.
+The protein's natural variant, known as in strain: KH66, features a modification of the amino acid from L to P at position 262.
+The protein's natural variant, known as in strain: KH66, features a modification of the amino acid from E to K at position 278.
+The protein's natural variant, known as in strain: DI7, Draveil, Loua, Monty5, Tahiti, Texas, S30 and ZW141, features a modification of the amino acid from E to V at position 41.
+The protein's natural variant, known as in strain: DI7, Draveil, Loua, Monty5, Tahiti, Texas, S30 and ZW141, features a modification of the amino acid from T to A at position 62.
+The protein's natural variant, known as in strain: DI7, Draveil, Loua, Monty5, Tahiti, Texas, S30 and ZW141, features a modification of the amino acid from Q to R at position 68.
+The protein's natural variant, known as in strain: Loua, Monty5, P. bourg, Tahiti, Texas and S30, features a modification of the amino acid from S to F at position 183.
+The protein's natural variant, known as in ACDMPV, features a modification of the amino acid from P to Q at position 49.
+The protein's natural variant, known as in ACDMPV;, features a modification of the amino acid from P to S at position 49.
+The protein's natural variant, known as in ACDMPV, features a modification of the amino acid from S to F at position 52.
+The protein's natural variant, known as in ACDMPV, features a modification of the amino acid from Y to C at position 53.
+The protein's natural variant, known as in ACDMPV;, features a modification of the amino acid from I to N at position 74.
+The protein's natural variant, known as in ACDMPV, features a modification of the amino acid from F to L at position 77.
+The protein's natural variant, known as in ACDMPV, features a modification of the amino acid from F to I at position 85.
+The protein's natural variant, known as in ACDMPV, features a modification of the amino acid from F to L at position 85.
+The protein's natural variant, known as in ACDMPV, features a modification of the amino acid from F to S at position 85.
+The protein's natural variant, known as in ACDMPV, features a modification of the amino acid from R to W at position 86.
+The protein's natural variant, known as in ACDMPV, features a modification of the amino acid from G to E at position 91.
+The protein's natural variant, known as in ACDMPV, features a modification of the amino acid from G to V at position 91.
+The protein's natural variant, known as in ACDMPV, features a modification of the amino acid from V to M at position 96.
+The protein's natural variant, known as in ACDMPV, features a modification of the amino acid from R to H at position 97.
+The protein's natural variant, known as in ACDMPV;, features a modification of the amino acid from H to Q at position 98.
+The protein's natural variant, known as in ACDMPV;, features a modification of the amino acid from S to L at position 101.
+The protein's natural variant, known as in ACDMPV;, features a modification of the amino acid from F to L at position 106.
+The protein's natural variant, known as in ACDMPV, features a modification of the amino acid from G to D at position 119.
+The protein's natural variant, known as in ACDMPV, features a modification of the amino acid from P to L at position 126.
+The protein's natural variant, known as in ACDMPV, features a modification of the amino acid from R to L at position 139.
+The protein's natural variant, known as in ACDMPV; unknown pathological significance;, features a modification of the amino acid from R to W at position 330.
+The protein's natural variant, known as in variant A, features a modification of the amino acid from VP to A at position 32.
+The protein's natural variant, known as in variant E, features a modification of the amino acid from A to T at position 43.
+The protein's natural variant, known as in variant D, features a modification of the amino acid from A to S at position 46.
+The protein's natural variant, known as in variant A, features a modification of the amino acid from F to L at position 50.
+The protein's natural variant, known as in variant C, features a modification of the amino acid from T to A at position 55.
+The protein's natural variant, known as in variant A, features a modification of the amino acid from V to A at position 65.
+The protein's natural variant, known as in variant C, features a modification of the amino acid from T to A at position 66.
+The protein's natural variant, known as in variant C, features a modification of the amino acid from S to G at position 84.
+The protein's natural variant, known as in variant E, features a modification of the amino acid from A to T at position 92.
+The protein's natural variant, known as affecting excitation/contraction coupling in muscle fibers; the sensitivity of CACNA1S voltage sensor is shifted to higher depolarizing voltages in cells carrying this variant;, features a modification of the amino acid from P to L at position 108.
+The protein's natural variant, known as affecting excitation/contraction coupling in muscle fibers; the sensitivity of CACNA1S voltage sensor is shifted to higher depolarizing voltages in cells carrying this variant;, features a modification of the amino acid from G to A at position 150.
+The protein's natural variant, known as in FTDALS3;, features a modification of the amino acid from A to V at position 16.
+The protein's natural variant, known as in FTDALS3;, features a modification of the amino acid from A to V at position 33.
+The protein's natural variant, known as in FTDALS3;, features a modification of the amino acid from D to E at position 80.
+The protein's natural variant, known as in FTDALS3;, features a modification of the amino acid from V to M at position 90.
+The natural variant of this protein is characterized by an amino acid alteration from R to Q at position 107.
+The protein's natural variant, known as in FTDALS3;, features a modification of the amino acid from R to W at position 107.
+The natural variant of this protein is characterized by an amino acid alteration from D to Y at position 108.
+The protein's natural variant, known as in FTDALS3;, features a modification of the amino acid from D to N at position 129.
+The protein's natural variant, known as in FTDALS3;, features a modification of the amino acid from V to I at position 153.
+The protein's natural variant, known as in FTDALS3;, features a modification of the amino acid from R to C at position 212.
+The protein's natural variant, known as in FTDALS3, features a modification of the amino acid from G to V at position 219.
+The protein's natural variant, known as in FTDALS3;, features a modification of the amino acid from S to P at position 226.
+The protein's natural variant, known as in FTDALS3;, features a modification of the amino acid from P to L at position 228.
+The protein's natural variant, known as in FTDALS3;, features a modification of the amino acid from P to T at position 232.
+The protein's natural variant, known as confirmed at protein level;, features a modification of the amino acid from K to E at position 238.
+The protein's natural variant, known as in FTDALS3;, features a modification of the amino acid from D to N at position 258.
+The natural variant of this protein is characterized by an amino acid alteration from RS to SR at position 266.
+The natural variant of this protein is characterized by an amino acid alteration from E to Q at position 274.
+The protein's natural variant, known as in FTDALS3, features a modification of the amino acid from S to P at position 318.
+The protein's natural variant, known as in FTDALS3; likely benign variant;, features a modification of the amino acid from R to C at position 321.
+The protein's natural variant, known as in FTDALS3;, features a modification of the amino acid from D to G at position 329.
+The protein's natural variant, known as in FTDALS3;, features a modification of the amino acid from P to L at position 348.
+The protein's natural variant, known as in FTDALS3;, features a modification of the amino acid from S to P at position 370.
+The protein's natural variant, known as in FTDALS3;, features a modification of the amino acid from A to V at position 381.
+The protein's natural variant, known as in PDB3 and FTDALS3;, features a modification of the amino acid from P to L at position 387.
+The protein's natural variant, known as in PDB3 and FTDALS3; no effect on polyubiquitin-binding;, features a modification of the amino acid from P to L at position 392.
+The protein's natural variant, known as in PDB3;, features a modification of the amino acid from S to P at position 399.
+The protein's natural variant, known as in PDB3;, features a modification of the amino acid from M to T at position 404.
+The protein's natural variant, known as in PDB3; loss of polyubiquitin-binding;, features a modification of the amino acid from M to V at position 404.
+The protein's natural variant, known as in PDB3 and FTDALS3; no effect on polyubiquitin-binding;, features a modification of the amino acid from G to S at position 411.
+The protein's natural variant, known as in PDB3 and FTDALS3; loss of polyubiquitin-binding and increased activation of NF-kappa-B;, features a modification of the amino acid from G to R at position 425.
+The protein's natural variant, known as in FTDALS3;, features a modification of the amino acid from T to P at position 430.
+The protein's natural variant, known as in LIWAS; loss of voltage-gated potassium channel activity;, features a modification of the amino acid from G to R at position 375.
+The protein's natural variant, known as in PNKD3; may have a synergistic effect with ethanol in the triggering of symptoms;, features a modification of the amino acid from D to G at position 434.
+The protein's natural variant, known as found in a patient with epileptic encephalopathy; unknown pathological significance; no effect on voltage-dependent sensitivity;, features a modification of the amino acid from K to N at position 518.
+The protein's natural variant, known as found in a patient with epilepsy; unknown pathological significance; no effect on voltage-dependent sensitivity;, features a modification of the amino acid from E to A at position 656.
+The protein's natural variant, known as in PNKD3, features a modification of the amino acid from E to K at position 884.
+The protein's natural variant, known as in PNKD3 and EIG16; increased sensitivity to voltage-dependent activation resulting in increased channel activity; no change in calcium sensitivity;, features a modification of the amino acid from N to S at position 1053.
+The protein's natural variant, known as found in patient with epilepsy; unknown pathological significance;, features a modification of the amino acid from N to S at position 1217.
+The protein's natural variant, known as in GLC1O; unknown pathological significance, features a modification of the amino acid from C to Y at position 7.
+The protein's natural variant, known as in GLC1O; unknown pathological significance;, features a modification of the amino acid from E to K at position 84.
+The protein's natural variant, known as in GLC1O; unknown pathological significance;, features a modification of the amino acid from R to H at position 90.
+The protein's natural variant, known as in GLC1O; unknown pathological significance;, features a modification of the amino acid from R to Q at position 206.
+The protein's natural variant, known as in GLC1O; also found in patients with normal pressure glaucoma; unknown pathological significance; impaired ligand-mediated TRKB signaling and reduced neurite outgrowth;, features a modification of the amino acid from R to W at position 206.
+The natural variant of this protein is characterized by an amino acid alteration from T to S at position 207.
+The protein's natural variant, known as in GLC1O; unknown pathological significance;, features a modification of the amino acid from R to G at position 209.
+The protein's natural variant, known as in strain: CC-503, features a modification of the amino acid from LCCY to SVVD at position 431.
+The protein's natural variant, known as in strain: CC-503, features a modification of the amino acid from L to S at position 436.
+The protein's natural variant, known as in an atypical progeroid patient; diagnosed as Seip syndrome; unknown pathological significance;, features a modification of the amino acid from T to I at position 10.
+The protein's natural variant, known as in EDMD3, features a modification of the amino acid from T to S at position 24.
+The protein's natural variant, known as in EDMD2;, features a modification of the amino acid from R to G at position 25.
+The protein's natural variant, known as in EDMD2; mis-localized in the nucleus; causes nuclear deformations and LMNB1 redistribution;, features a modification of the amino acid from R to P at position 25.
+The protein's natural variant, known as in FPLD2;, features a modification of the amino acid from R to W at position 28.
+The protein's natural variant, known as in CMT2; autosomal dominant form;, features a modification of the amino acid from E to D at position 33.
+The protein's natural variant, known as in EDMD2;, features a modification of the amino acid from E to G at position 33.
+The protein's natural variant, known as in EDMD2;, features a modification of the amino acid from L to V at position 35.
+The protein's natural variant, known as in MDCL and EDMD2;, features a modification of the amino acid from N to S at position 39.
+The protein's natural variant, known as in EDMD2;, features a modification of the amino acid from A to T at position 43.
+The protein's natural variant, known as in EDMD2;, features a modification of the amino acid from Y to C at position 45.
+The protein's natural variant, known as in EDMD2 and MDCL;, features a modification of the amino acid from R to P at position 50.
+The protein's natural variant, known as in EDMD2;, features a modification of the amino acid from R to S at position 50.
+The protein's natural variant, known as in CMDHH; phenotype originally designated as atypical Werner syndrome;, features a modification of the amino acid from A to P at position 57.
+The protein's natural variant, known as in CMDHH;, features a modification of the amino acid from L to R at position 59.
+The protein's natural variant, known as in CMD1A and FPLD2; interacts with itself and with wild-type LMNA and LMNB1; no decrease in the stability compared with wild-type;, features a modification of the amino acid from R to G at position 60.
+The protein's natural variant, known as in FPLD2;, features a modification of the amino acid from R to G at position 62.
+The protein's natural variant, known as in EDMD2;, features a modification of the amino acid from I to N at position 63.
+The protein's natural variant, known as in EDMD2; no effect on protein level; no obvious effect on nuclear morphology in cultured skin fibroblasts from heterozygous patients;, features a modification of the amino acid from I to S at position 63.
+The protein's natural variant, known as in EDMD2, features a modification of the amino acid from E to G at position 65.
+The protein's natural variant, known as in CMD1A; interacts with itself and with wild-type LMNA and LMNB1; no decrease in the stability compared with wild-type;, features a modification of the amino acid from L to R at position 85.
+The protein's natural variant, known as in CMD1A; dramatically aberrant localization with almost no nuclear rim staining and formation of intranuclear foci;, features a modification of the amino acid from R to L at position 89.
+The protein's natural variant, known as in CMD1A;, features a modification of the amino acid from L to F at position 92.
+The protein's natural variant, known as in CMD1A;, features a modification of the amino acid from K to E at position 97.
+The protein's natural variant, known as in CMD1A; dramatically aberrant localization with almost no nuclear rim staining and formation of intranuclear foci;, features a modification of the amino acid from R to P at position 101.
+The protein's natural variant, known as found in patients with atrial fibrillation; unknown pathological significance;, features a modification of the amino acid from G to S at position 125.
+The protein's natural variant, known as in FPLD2;, features a modification of the amino acid from R to L at position 133.
+The protein's natural variant, known as in EDMD2;, features a modification of the amino acid from R to P at position 133.
+The protein's natural variant, known as in HGPS; might be associated with early and severe strokes;, features a modification of the amino acid from E to K at position 138.
+The protein's natural variant, known as in EDMD2;, features a modification of the amino acid from L to P at position 140.
+The protein's natural variant, known as in HGPS; phenotype originally designated as atypical Werner syndrome;, features a modification of the amino acid from L to R at position 140.
+The protein's natural variant, known as in HGPS;, features a modification of the amino acid from S to F at position 143.
+The protein's natural variant, known as in CMD1A;, features a modification of the amino acid from S to P at position 143.
+The protein's natural variant, known as in HGPS; atypical;, features a modification of the amino acid from E to K at position 145.
+The protein's natural variant, known as in EDMD2;, features a modification of the amino acid from T to P at position 150.
+The protein's natural variant, known as in CMD1A;, features a modification of the amino acid from E to K at position 161.
+The protein's natural variant, known as in CMD1A; dramatically aberrant localization with almost no nuclear rim staining and formation of intranuclear foci;, features a modification of the amino acid from R to P at position 166.
+The protein's natural variant, known as in EDMD2; found also in a patient with limb-girdle muscular dystrophy; sporadic;, features a modification of the amino acid from R to P at position 189.
+The protein's natural variant, known as in EDMD2 and CMD1A; aberrant localization with decreased nuclear rim staining and increased formation of intranuclear foci;, features a modification of the amino acid from R to Q at position 190.
+The protein's natural variant, known as in EDMD2, features a modification of the amino acid from R to RR at position 190.
+The protein's natural variant, known as in CMD1A;, features a modification of the amino acid from R to W at position 190.
+The protein's natural variant, known as in CMD1A; dramatically increases the size of intranuclear speckles and reduces their number; this phenotype is only partially reversed by coexpression of the G-192 mutation and wild-type lamin-C; precludes insertion of lamin-C into the nuclear envelope when co-transfected with the G-192 LMNA; G-192 lamin-C expression totally disrupts the SUMO1 pattern;, features a modification of the amino acid from D to G at position 192.
+The protein's natural variant, known as in CMD1A; dramatically aberrant localization with decreased nuclear rim staining and formation of intranuclear foci; distribution of endogenous LMNA, LMNB1 and LMNB2 are altered in cells expressing this mutant; causes an increased loss of endogenous EMD from the nuclear envelope; interacts with itself and with wild-type LMNA and LMNB1; no decrease in the stability compared with wild-type;, features a modification of the amino acid from N to K at position 195.
+The protein's natural variant, known as in EDMD2, features a modification of the amino acid from RLQT to S at position 199.
+The protein's natural variant, known as in CMD1A; interacts with itself and with wild-type LMNA and LMNB1; no decrease in the stability compared with wild-type; decreased sumoylation; aberrant localization with decreased nuclear rim staining and formation of intranuclear foci; associated with increased cell death;, features a modification of the amino acid from E to G at position 203.
+The protein's natural variant, known as in CMD1A; decreased sumoylation; aberrant localization with decreased nuclear rim staining and formation of intranuclear foci; associated with increased cell death;, features a modification of the amino acid from E to K at position 203.
+The protein's natural variant, known as in EDMD2;, features a modification of the amino acid from F to L at position 206.
+The protein's natural variant, known as in CMD1A; dramatically aberrant localization with almost no nuclear rim staining and increased formation of intranuclear foci;, features a modification of the amino acid from I to S at position 210.
+The protein's natural variant, known as in CMD1A; aberrant localization with decreased nuclear rim staining and formation of intranuclear foci;, features a modification of the amino acid from L to P at position 215.
+The protein's natural variant, known as in EDMD2;, features a modification of the amino acid from H to P at position 222.
+The protein's natural variant, known as in EDMD2;, features a modification of the amino acid from H to Y at position 222.
+The protein's natural variant, known as in EDMD3;, features a modification of the amino acid from R to Q at position 225.
+The protein's natural variant, known as in FPLD2;, features a modification of the amino acid from D to N at position 230.
+The protein's natural variant, known as in EDMD2;, features a modification of the amino acid from G to E at position 232.
+The protein's natural variant, known as in EDMD2;, features a modification of the amino acid from L to P at position 248.
+The protein's natural variant, known as in EDMD2; no obvious effect on nuclear morphology in cultured skin fibroblasts from heterozygous patients; no effect on protein level;, features a modification of the amino acid from R to Q at position 249.
+The protein's natural variant, known as in MDCL and EDMD2; mislocalized in the nucleus; causes nuclear deformations and LMNB1 redistribution;, features a modification of the amino acid from R to W at position 249.
+The protein's natural variant, known as in EDMD2, features a modification of the amino acid from Y to C at position 259.
+The protein's natural variant, known as in CMDA1, features a modification of the amino acid from K to N at position 260.
+The protein's natural variant, known as in EDMD2;, features a modification of the amino acid from Y to C at position 267.
+The protein's natural variant, known as in EDMD2;, features a modification of the amino acid from S to P at position 268.
+The protein's natural variant, known as in EDMD2;, features a modification of the amino acid from L to P at position 271.
+The protein's natural variant, known as in EDMD2;, features a modification of the amino acid from Q to P at position 294.
+The protein's natural variant, known as in EDMD2;, features a modification of the amino acid from S to P at position 295.
+The protein's natural variant, known as in CMT2B1;, features a modification of the amino acid from R to C at position 298.
+The protein's natural variant, known as in HGPS; atypical form with late onset; abnormal nuclear morphology with single or multple blebs, lobulation and occasional ringed or donut shaped nuclei;, features a modification of the amino acid from D to G at position 300.
+The protein's natural variant, known as in MDCL;, features a modification of the amino acid from L to P at position 302.
+The protein's natural variant, known as in EDMD2;, features a modification of the amino acid from S to P at position 303.
+The protein's natural variant, known as in CMD1A;, features a modification of the amino acid from E to K at position 317.
+The protein's natural variant, known as in CMD1A; no effect on nuclear morphology and lamin A localization;, features a modification of the amino acid from A to T at position 318.
+The protein's natural variant, known as in EDMD2;, features a modification of the amino acid from R to Q at position 336.
+The protein's natural variant, known as in EDMD2;, features a modification of the amino acid from R to Q at position 343.
+The protein's natural variant, known as in CMD1A;, features a modification of the amino acid from R to L at position 349.
+The protein's natural variant, known as in EDMD2 and MDCL; aberrant localization with decreased nuclear rim staining and formation of intranuclear foci when transfected in C2C12 myoblasts; no obvious effect on nuclear morphology in cultured skin fibroblasts from heterozygous patients; distribution of endogenous LMNA, LMNB1 and LMNB2 are altered in cells expressing this mutant; interacts with itself and with wild-type LMNA and LMNB1; no effect on protein level;, features a modification of the amino acid from E to K at position 358.
+The protein's natural variant, known as in EDMD2;, features a modification of the amino acid from E to K at position 361.
+The protein's natural variant, known as in EDMD2; dramatically aberrant localization with decreased nuclear rim staining and formation of intranuclear foci; distribution of endogenous LMNA, LMNB1 and LMNB2 are altered in cells expressing this mutant; causes an increased loss of endogenous EMD from the nuclear envelope; interacts with itself and with wild-type LMNA and LMNB1; no decrease in the stability compared with wild-type;, features a modification of the amino acid from M to K at position 371.
+The protein's natural variant, known as in EDMD2; no obvious effect on nuclear morphology in cultured skin fibroblasts from heterozygous patients; no effect on protein level;, features a modification of the amino acid from R to H at position 377.
+The protein's natural variant, known as in EDMD2;, features a modification of the amino acid from R to L at position 377.
+The protein's natural variant, known as in MDCL;, features a modification of the amino acid from L to S at position 380.
+The protein's natural variant, known as in EDMD2; dramatically aberrant localization with decreased nuclear rim staining and formation of intranuclear foci; distribution of endogenous LMNA, LMNB1 and LMNB2 are altered in cells expressing this mutant; causes an increased loss of endogenous EMD from the nuclear envelope; interacts with itself and with wild-type LMNA and LMNB1; no decrease in the stability compared with wild-type;, features a modification of the amino acid from R to K at position 386.
+The protein's natural variant, known as in CMD1A; no effect on nuclear morphology but restricts lamin A to the cytoplasm;, features a modification of the amino acid from R to H at position 388.
+The protein's natural variant, known as in FPLD2 and CMD1A; no effect on nuclear morphology and lamin A localization;, features a modification of the amino acid from R to C at position 399.
+The protein's natural variant, known as in EDMD2; abnormal nuclear localization in a honeycomb expression pattern in about 22% of cultured skin fibroblasts from heterozygous patients; enhances the interaction with SYNE2; no effect on nuclear localization; no effect on protein level;, features a modification of the amino acid from R to C at position 401.
+The protein's natural variant, known as probable disease-associated variant found in patients with metabolic syndromes; no effect on nuclear lamin A localization; no effect on the interaction with SYNE2;, features a modification of the amino acid from G to D at position 411.
+The protein's natural variant, known as found in patients with skeletal and cardiac muscular dystrophies; no effect on nuclear lamin A localization; no effect on the interaction with SYNE2;, features a modification of the amino acid from G to C at position 413.
+The protein's natural variant, known as rare variant; found in patients with atrial fibrillation; unknown pathological significance; no effect on nuclear lamin A localization; enhances the interaction with SYNE2; causes nuclear deformations in heat shock experiments;, features a modification of the amino acid from V to I at position 415.
+The protein's natural variant, known as found in patients with lipodystrophy; no effect on nuclear lamin A localization; no effect on the interaction with SYNE2;, features a modification of the amino acid from R to C at position 419.
+The protein's natural variant, known as probable disease-associated variant found in patient with severe metabolic syndrome; no effect on nuclear lamin A localization; no effect on the interaction with SYNE2;, features a modification of the amino acid from L to P at position 421.
+The protein's natural variant, known as found in patients with skeletal and cardiac muscular dystrophies; unknown pathological significance; no effect on nuclear lamin A localization; no effect on the interaction with SYNE2, features a modification of the amino acid from R to G at position 427.
+The protein's natural variant, known as in CMD1A;, features a modification of the amino acid from R to C at position 435.
+The protein's natural variant, known as in FPLD2; increase in nuclear blebbing and formation of honeycomb-like structures in the nuclei with no accumulation of prelamin A in skin fibroblasts; causes oligomerization of the C-terminal globular domain of lamins A and C under no-reducing conditions and increases binding affinity for DNA; increases sensitivity to oxidative stress; no significant differences in stability and structure compared with the wild-type;, features a modification of the amino acid from R to C at position 439.
+The protein's natural variant, known as in EDMD2;, features a modification of the amino acid from D to V at position 446.
+The protein's natural variant, known as in EDMD2;, features a modification of the amino acid from G to D at position 449.
+The protein's natural variant, known as in MDCL;, features a modification of the amino acid from R to P at position 453.
+The protein's natural variant, known as in EDMD2; abnormal nuclear localization; forms nuclear foci in about 8% of cultured skin fibroblasts from heterozygous patients; interacts with itself and with wild-type LMNA and LMNB1; no effect on protein level;, features a modification of the amino acid from R to W at position 453.
+The protein's natural variant, known as in EDMD2;, features a modification of the amino acid from L to P at position 454.
+The protein's natural variant, known as in MDCL;, features a modification of the amino acid from R to P at position 455.
+The protein's natural variant, known as in MDCL;, features a modification of the amino acid from N to D at position 456.
+The protein's natural variant, known as in EDMD2; mislocalized in the nucleus; does not alter nuclear size or shape;, features a modification of the amino acid from N to I at position 456.
+The protein's natural variant, known as in EDMD2;, features a modification of the amino acid from N to K at position 456.
+The protein's natural variant, known as in EDMD2;, features a modification of the amino acid from D to Y at position 461.
+The protein's natural variant, known as in FPLD2;, features a modification of the amino acid from G to D at position 465.
+The protein's natural variant, known as in EDMD2;, features a modification of the amino acid from W to R at position 467.
+The protein's natural variant, known as in EDMD2;, features a modification of the amino acid from I to T at position 469.
+The protein's natural variant, known as in HGPS;, features a modification of the amino acid from R to C at position 471.
+The protein's natural variant, known as in CMD1A; no effect on nuclear morphology and lamin A localization;, features a modification of the amino acid from R to H at position 471.
+The protein's natural variant, known as in EDMD2;, features a modification of the amino acid from Y to H at position 481.
+The protein's natural variant, known as in FPLD2; abnormal nuclear localization in a honeycomb expression pattern in about 10% of cultured skin fibroblasts from heterozygous patients; no effect on protein level;, features a modification of the amino acid from R to L at position 482.
+The protein's natural variant, known as in FPLD2; interacts with itself and with wild-type LMNA and LMNB1; no decrease in the stability compared with wild-type;, features a modification of the amino acid from R to Q at position 482.
+The protein's natural variant, known as in FPLD2; interacts with itself and with wild-type LMNA and LMNB1; no decrease in the stability compared with wild-type; decreases binding affinity for DNA; increases sensitivity to oxidative stress;, features a modification of the amino acid from R to W at position 482.
+The protein's natural variant, known as in FPLD2; interacts with itself and with wild-type LMNA and LMNB1; no decrease in the stability compared with wild-type;, features a modification of the amino acid from K to N at position 486.
+The protein's natural variant, known as found in patient with atrial fibrillation;, features a modification of the amino acid from T to P at position 488.
+The protein's natural variant, known as in FPLD2, features a modification of the amino acid from K to E at position 515.
+The protein's natural variant, known as in EDMD2; interacts with itself and with wild-type LMNA and LMNB1; no decrease in the stability compared with wild-type;, features a modification of the amino acid from W to S at position 520.
+The protein's natural variant, known as in CMD1A; unknown pathological significance;, features a modification of the amino acid from G to R at position 523.
+The protein's natural variant, known as in HGPS;, features a modification of the amino acid from R to C at position 527.
+The protein's natural variant, known as in MADA;, features a modification of the amino acid from R to H at position 527.
+The protein's natural variant, known as in EDMD2 and FPLD2; interacts with itself and with wild-type LMNA and LMNB1; reduced binding to SUN1; abnormal nuclear localization; forms nuclear foci in about 13% of cultured skin fibroblasts from heterozygous patients; no effect on protein level;, features a modification of the amino acid from R to P at position 527.
+The protein's natural variant, known as in EDMD2; interacts with itself and with wild-type LMNA and LMNB1; no decrease in the stability compared with wild-type;, features a modification of the amino acid from T to K at position 528.
+The protein's natural variant, known as in EDMD2;, features a modification of the amino acid from T to R at position 528.
+The protein's natural variant, known as in MADA;, features a modification of the amino acid from A to V at position 529.
+The protein's natural variant, known as in EDMD2; interacts with itself and with wild-type LMNA and LMNB1; reduced binding to SUN1; no decrease in the stability compared with wild-type;, features a modification of the amino acid from L to P at position 530.
+The protein's natural variant, known as in CMD1A; grossly abnormal nuclear shape with the nuclear envelope producing prominent lobules in about 10% of cultured skin fibroblasts from heterozygous patients;, features a modification of the amino acid from R to C at position 541.
+The protein's natural variant, known as in EDMD2;, features a modification of the amino acid from R to H at position 541.
+The protein's natural variant, known as in EDMD2; mis-localized in the nucleus; does not alter nuclear size or shape;, features a modification of the amino acid from R to P at position 541.
+The protein's natural variant, known as in EDMD2 and CMD1A; modest and non-specific nuclear membrane alterations; the phenotype is entirely reversed by coexpression of the S-541 mutation and wild-type lamin-C;, features a modification of the amino acid from R to S at position 541.
+The protein's natural variant, known as in HGPS;, features a modification of the amino acid from K to N at position 542.
+The protein's natural variant, known as in CMD1A, FPLD2 and MADA;, features a modification of the amino acid from S to L at position 573.
+The protein's natural variant, known as in an atypical progeroid patient; diagnosed as Werner syndrome;, features a modification of the amino acid from E to V at position 578.
+The protein's natural variant, known as in FPLD2;, features a modification of the amino acid from R to H at position 582.
+The protein's natural variant, known as in EDMD2;, features a modification of the amino acid from G to S at position 602.
+The protein's natural variant, known as in HGPS; reduced binding to SUN1; may affect splicing by activating a cryptic splice donor site;, features a modification of the amino acid from G to S at position 608.
+The protein's natural variant, known as in EDMD2;, features a modification of the amino acid from R to H at position 624.
+The protein's natural variant, known as probable disease-associated variant found in a patient with metabolic syndrome;, features a modification of the amino acid from G to D at position 631.
+The protein's natural variant, known as in HGPS and EDMD2; unknown pathological significance; partially inhibits tail cleavage;, features a modification of the amino acid from R to C at position 644.
+The natural variant of this protein is characterized by an amino acid alteration from L to V at position 45.
+The natural variant of this protein is characterized by an amino acid alteration from I to F at position 49.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 49.
+The natural variant of this protein is characterized by an amino acid alteration from F to R at position 52.
+The natural variant of this protein is characterized by an amino acid alteration from TS to AN at position 130.
+The natural variant of this protein is characterized by an amino acid alteration from AY to VF at position 136.
+The natural variant of this protein is characterized by an amino acid alteration from W to R at position 155.
+The natural variant of this protein is characterized by an amino acid alteration from IH to VV at position 159.
+The natural variant of this protein is characterized by an amino acid alteration from A to T at position 163.
+The natural variant of this protein is characterized by an amino acid alteration from M to A at position 166.
+The natural variant of this protein is characterized by an amino acid alteration from E to V at position 168.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from Y to H at position 627.
+The protein's natural variant, known as in a esophageal carcinoma;, features a modification of the amino acid from M to T at position 168.
+The protein's natural variant, known as in MRMV1; unknown pathological significance;, features a modification of the amino acid from R to P at position 597.
+The protein's natural variant, known as in HGPPS2; unknown pathological significance;, features a modification of the amino acid from Q to K at position 691.
+The protein's natural variant, known as in MRMV1; unknown pathological significance;, features a modification of the amino acid from M to L at position 743.
+The protein's natural variant, known as in MRMV1; unknown pathological significance;, features a modification of the amino acid from V to M at position 754.
+The protein's natural variant, known as in MRMV1;, features a modification of the amino acid from V to G at position 793.
+The protein's natural variant, known as in MRMV1;, features a modification of the amino acid from G to E at position 805.
+The protein's natural variant, known as in MRMV1; unknown pathological significance;, features a modification of the amino acid from A to T at position 893.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from F to S at position 1039.
+The protein's natural variant, known as in MRMV1; unknown pathological significance;, features a modification of the amino acid from M to V at position 1217.
+The protein's natural variant, known as in MRMV1; unknown pathological significance;, features a modification of the amino acid from A to T at position 1250.
+The protein's natural variant, known as in a colorectal carcinoma;, features a modification of the amino acid from P to H at position 1375.
+The protein's natural variant, known as in strain: Hawaii, New Caledonia and Tahiti, features a modification of the amino acid from V to I at position 450.
+The protein's natural variant, known as in strain: Hawaii, New Caledonia and Tahiti, features a modification of the amino acid from Y to F at position 468.
+The protein's natural variant, known as in DKCB6;, features a modification of the amino acid from A to V at position 383.
+The protein's natural variant, known as in PFBMFT4;, features a modification of the amino acid from K to R at position 421.
+The protein's natural variant, known as in CMH11;, features a modification of the amino acid from H to Y at position 90.
+The protein's natural variant, known as in CMH11;, features a modification of the amino acid from R to C at position 97.
+The protein's natural variant, known as in CMH11;, features a modification of the amino acid from E to K at position 101.
+The protein's natural variant, known as in ASD5; reduced affinity for myosin; normal actin filament polymerization ability; normal actomyosin motor function;, features a modification of the amino acid from M to V at position 125.
+The protein's natural variant, known as in CMH11;, features a modification of the amino acid from P to A at position 166.
+The protein's natural variant, known as in CMH11, features a modification of the amino acid from Y to C at position 168.
+The protein's natural variant, known as in CMH11;, features a modification of the amino acid from A to S at position 297.
+The protein's natural variant, known as in CMH11, features a modification of the amino acid from M to L at position 307.
+The protein's natural variant, known as in CMD1R;, features a modification of the amino acid from R to H at position 314.
+The protein's natural variant, known as in CMH11;, features a modification of the amino acid from A to P at position 333.
+The protein's natural variant, known as in CMD1R;, features a modification of the amino acid from E to G at position 363.
+The protein's natural variant, known as in allele 6M1-16*02;, features a modification of the amino acid from D to N at position 63.
+The protein's natural variant, known as in NM; results in decreased epimerase activity corresponding to 20% of wild-type activity; no effect on kinase activity;, features a modification of the amino acid from C to S at position 13.
+The protein's natural variant, known as in NM;, features a modification of the amino acid from P to S at position 27.
+The protein's natural variant, known as in NM, features a modification of the amino acid from P to L at position 36.
+The protein's natural variant, known as in NM; results in decreased epimerase activity corresponding to less than 10% of wild-type activity; impaired homohexamers formation, features a modification of the amino acid from H to Q at position 132.
+The protein's natural variant, known as in NM;, features a modification of the amino acid from R to C at position 162.
+The protein's natural variant, known as in NM;, features a modification of the amino acid from M to V at position 171.
+The protein's natural variant, known as in NM; results in decreased epimerase activity corresponding to 20% of wild-type activity; no effect on kinase activity; impaired homohexamers formation;, features a modification of the amino acid from D to V at position 176.
+The protein's natural variant, known as in NM; results in decreased epimerase activity corresponding to less than 20% of wild-type activity; no effect on kinase activity; impaired homohexamers formation;, features a modification of the amino acid from R to C at position 177.
+The protein's natural variant, known as in NM; unknown pathological significance; retains 90% of wild-type epimerase activity; retains 75% of wild-type kinase activity;, features a modification of the amino acid from I to F at position 200.
+The protein's natural variant, known as in NM; moderate phenotype with unusual involvement of quadriceps;, features a modification of the amino acid from G to S at position 206.
+The protein's natural variant, known as in NM;, features a modification of the amino acid from V to A at position 216.
+The protein's natural variant, known as in NM;, features a modification of the amino acid from D to N at position 225.
+The protein's natural variant, known as in NM;, features a modification of the amino acid from R to Q at position 246.
+The protein's natural variant, known as in NM;, features a modification of the amino acid from R to W at position 246.
+The protein's natural variant, known as in SIALURIA; strong reduction of feedback inhibition by CMP-Neu5Ac;, features a modification of the amino acid from R to L at position 263.
+The protein's natural variant, known as in SIALURIA; abolishes feedback inhibition by CMP-Neu5Ac;, features a modification of the amino acid from R to Q at position 266.
+The protein's natural variant, known as in sialuria;, features a modification of the amino acid from R to W at position 266.
+The protein's natural variant, known as in NM; retains 80% of wild-type epimerase activity; decreased kinase activity corresponding to 60% of wild-type; requires 2 nucleotide substitutions;, features a modification of the amino acid from C to V at position 303.
+The protein's natural variant, known as in NM;, features a modification of the amino acid from R to Q at position 306.
+The protein's natural variant, known as in NM; results in decreased epimerase activity corresponding to 20% of wild-type activity; no effect on kinase activity; impaired homohexamers formation, features a modification of the amino acid from V to A at position 331.
+The protein's natural variant, known as in NM; results in decreased epimerase activity corresponding to 10-30% of wild-type activity; decreased kinase activity; impaired homohexamers formation;, features a modification of the amino acid from D to Y at position 378.
+The protein's natural variant, known as in NM;, features a modification of the amino acid from A to V at position 460.
+The protein's natural variant, known as in NM; results in decreased epimerase activity corresponding to 50% of the wild-type; severely decreased kinase activity corresponding to less than 10% of wild-type activity, features a modification of the amino acid from I to T at position 472.
+The protein's natural variant, known as in NM; decreased epimerase activity; decreased kinase activity;, features a modification of the amino acid from N to S at position 519.
+The protein's natural variant, known as in NM; results in decreased epimerase activity corresponding to less than 10% of wild-type activity; decreased kinase activity; impaired homohexamers formation;, features a modification of the amino acid from A to V at position 524.
+The protein's natural variant, known as in NM; retains 70% of wild-type epimerase; decreased kinase activity;, features a modification of the amino acid from F to C at position 528.
+The protein's natural variant, known as in NM;, features a modification of the amino acid from I to T at position 557.
+The protein's natural variant, known as in NM; retains 70-80% of wild-type epimerase activity; severely decreased kinase activity corresponding to less than 10% of wild-type activity; does not affect homohexamers formation;, features a modification of the amino acid from V to L at position 572.
+The protein's natural variant, known as in NM; decreased epimerase activity; decreased kinase activity;, features a modification of the amino acid from G to E at position 576.
+The protein's natural variant, known as in NM; decreased epimerase activity; decreased kinase activity;, features a modification of the amino acid from I to T at position 587.
+The protein's natural variant, known as in NM;, features a modification of the amino acid from A to T at position 600.
+The protein's natural variant, known as in NM; decreased kinase activity; does not affect homohexamers formation;, features a modification of the amino acid from A to T at position 630.
+The protein's natural variant, known as in NM; retains 80% of wild-type epimerase activity; retains 75% of wild-type kinase activity;, features a modification of the amino acid from A to T at position 631.
+The protein's natural variant, known as in NM; retains 70% of wild-type epimerase activity; decreased kinase activity; does not affect homohexamers formation;, features a modification of the amino acid from A to V at position 631.
+The protein's natural variant, known as in NM;, features a modification of the amino acid from Y to H at position 675.
+The protein's natural variant, known as in NM;, features a modification of the amino acid from V to M at position 696.
+The protein's natural variant, known as in NM; decreased epimerase activity; severely decreased kinase activity;, features a modification of the amino acid from G to S at position 708.
+The protein's natural variant, known as in NM;, features a modification of the amino acid from M to T at position 712.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation, features a modification of the amino acid from G to R at position 61.
+The protein's natural variant, known as in MECIL; activation of guanylate cyclase activity is 60% lower than in wild-type;, features a modification of the amino acid from D to G at position 387.
+The protein's natural variant, known as in DIAR6; activating mutation; exposure of the mutant receptor to its ligands results in markedly increased production of cyclic guanosine monophosphate;, features a modification of the amino acid from S to I at position 840.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from N to S at position 324.
+The protein's natural variant, known as in strain: Isolate USNM 583155, features a modification of the amino acid from G to E at position 340.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from Y to H at position 276.
+The protein's natural variant, known as in FA7D; Morioka;, features a modification of the amino acid from L to P at position 13.
+The protein's natural variant, known as in FA7D, features a modification of the amino acid from R to RR at position 59.
+The protein's natural variant, known as in FA7D, features a modification of the amino acid from F to L at position 64.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from L to Q at position 73.
+The protein's natural variant, known as in FA7D, features a modification of the amino acid from E to Q at position 79.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from C to F at position 82.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from C to R at position 82.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from E to K at position 85.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from R to G at position 88.
+The protein's natural variant, known as in FA7D, features a modification of the amino acid from R to P at position 88.
+The protein's natural variant, known as in FA7D; exhibits no procoagulant activity and is unable to bind tissue factor;, features a modification of the amino acid from N to D at position 117.
+The protein's natural variant, known as in FA7D, features a modification of the amino acid from S to P at position 120.
+The protein's natural variant, known as in FA7D, features a modification of the amino acid from C to F at position 121.
+The protein's natural variant, known as in FA7D, features a modification of the amino acid from L to P at position 125.
+The protein's natural variant, known as in FA7D, features a modification of the amino acid from Y to C at position 128.
+The protein's natural variant, known as in FA7D, features a modification of the amino acid from G to D at position 138.
+The protein's natural variant, known as in FA7D, features a modification of the amino acid from R to K at position 139.
+The protein's natural variant, known as in FA7D; Charlotte;, features a modification of the amino acid from R to Q at position 139.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from R to W at position 139.
+The protein's natural variant, known as in FA7D, features a modification of the amino acid from C to S at position 151.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from E to K at position 154.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from G to S at position 156.
+The protein's natural variant, known as in FA7D, features a modification of the amino acid from G to C at position 157.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from G to S at position 157.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from G to V at position 157.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from Q to R at position 160.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from S to F at position 171.
+The protein's natural variant, known as in FA7D, features a modification of the amino acid from G to R at position 177.
+The protein's natural variant, known as in FA7D, features a modification of the amino acid from L to P at position 181.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from D to N at position 183.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from S to F at position 186.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from P to S at position 189.
+The protein's natural variant, known as in FA7D, features a modification of the amino acid from P to L at position 194.
+The protein's natural variant, known as in FA7D; Malta-I;, features a modification of the amino acid from P to T at position 194.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from C to R at position 195.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from K to E at position 197.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from I to T at position 198.
+The protein's natural variant, known as in FA7D; Charlotte;, features a modification of the amino acid from R to Q at position 212.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from G to D at position 216.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from C to Y at position 238.
+The protein's natural variant, known as in FA7D, features a modification of the amino acid from G to R at position 240.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from T to N at position 241.
+The protein's natural variant, known as in FA7D, features a modification of the amino acid from S to F at position 250.
+The protein's natural variant, known as in FA7D, features a modification of the amino acid from A to P at position 251.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from A to T at position 251.
+The protein's natural variant, known as in FA7D, features a modification of the amino acid from C to R at position 254.
+The protein's natural variant, known as in FA7D, features a modification of the amino acid from C to Y at position 254.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from L to P at position 264.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from A to T at position 266.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from D to N at position 272.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from D to N at position 277.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from R to W at position 283.
+The protein's natural variant, known as in FA7D, features a modification of the amino acid from T to I at position 298.
+The protein's natural variant, known as in FA7D, features a modification of the amino acid from H to Q at position 301.
+The protein's natural variant, known as in FA7D, features a modification of the amino acid from D to H at position 302.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from D to N at position 302.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from A to T at position 304.
+The protein's natural variant, known as in FA7D; Malta-II;, features a modification of the amino acid from A to V at position 304.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from R to C at position 307.
+The protein's natural variant, known as in FA7D; Mie;, features a modification of the amino acid from R to H at position 307.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from V to M at position 312.
+The protein's natural variant, known as in FA7D, features a modification of the amino acid from L to V at position 314.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from L to F at position 321.
+The protein's natural variant, known as in FA7D, features a modification of the amino acid from L to R at position 323.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from E to K at position 325.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from R to Q at position 326.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from T to M at position 332.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from R to C at position 337.
+The protein's natural variant, known as in FA7D, features a modification of the amino acid from V to F at position 341.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from G to S at position 343.
+The protein's natural variant, known as in FA7D, features a modification of the amino acid from W to G at position 344.
+The protein's natural variant, known as in FA7D, features a modification of the amino acid from W to R at position 344.
+The protein's natural variant, known as in FA7D, features a modification of the amino acid from G to S at position 345.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from R to C at position 350.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from A to V at position 354.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from M to I at position 358.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from M to V at position 358.
+The protein's natural variant, known as in FA7D, features a modification of the amino acid from L to P at position 360.
+The protein's natural variant, known as in FA7D, features a modification of the amino acid from P to H at position 363.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from P to R at position 363.
+The protein's natural variant, known as in FA7D; Harrow/Padua;, features a modification of the amino acid from R to Q at position 364.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from R to W at position 364.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from C to F at position 370.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from R to W at position 375.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from T to M at position 384.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from M to T at position 387.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from M to V at position 387.
+The protein's natural variant, known as in FA7D; reduces tissue factor binding; impairs activation by factor Xa; abolishes amidolytic and coagulant activities;, features a modification of the amino acid from F to S at position 388.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from C to G at position 389.
+The protein's natural variant, known as in FA7D, features a modification of the amino acid from G to C at position 391.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from G to S at position 391.
+The protein's natural variant, known as in FA7D, features a modification of the amino acid from D to E at position 398.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from K to E at position 401.
+The protein's natural variant, known as in FA7D, features a modification of the amino acid from G to E at position 402.
+The protein's natural variant, known as in FA7D, features a modification of the amino acid from G to R at position 402.
+The protein's natural variant, known as in FA7D, features a modification of the amino acid from D to H at position 403.
+The protein's natural variant, known as in FA7D, features a modification of the amino acid from S to N at position 404.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from H to Q at position 408.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from H to R at position 408.
+The protein's natural variant, known as in FA7D, features a modification of the amino acid from R to G at position 413.
+The protein's natural variant, known as may be associated with decreased susceptibility to myocardial infarction;, features a modification of the amino acid from R to Q at position 413.
+The protein's natural variant, known as in FA7D; results in severely impaired protein secretion;, features a modification of the amino acid from G to C at position 414.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from T to M at position 419.
+The protein's natural variant, known as in FA7D, features a modification of the amino acid from V to F at position 422.
+The protein's natural variant, known as in FA7D, features a modification of the amino acid from G to A at position 425.
+The protein's natural variant, known as in FA7D, features a modification of the amino acid from G to C at position 425.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from A to T at position 429.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from G to D at position 432.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from G to E at position 435.
+The protein's natural variant, known as in FA7D;, features a modification of the amino acid from Y to F at position 437.
+The natural variant of this protein is characterized by an amino acid alteration from T to I at position 1408.
+The protein's natural variant, known as in MCC(b) antigen;, features a modification of the amino acid from K to E at position 1590.
+The protein's natural variant, known as in Sl(2)/Vil antigen and Sl(3) antigen;, features a modification of the amino acid from R to G at position 1601.
+The protein's natural variant, known as in Sl(3) antigen;, features a modification of the amino acid from S to T at position 1610.
+The natural variant of this protein is characterized by an amino acid alteration from H to D at position 1850.
+The protein's natural variant, known as does not affect localization to centromeres;, features a modification of the amino acid from V to I at position 94.
+The protein's natural variant, known as does not affect localization to centromeres;, features a modification of the amino acid from N to D at position 647.
+The protein's natural variant, known as does not affect localization to centromeres;, features a modification of the amino acid from P to S at position 672.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from A to D at position 13.
+The protein's natural variant, known as in strain: PAK, features a modification of the amino acid from LG to FDF at position 109.
+The protein's natural variant, known as in strain: PAK, features a modification of the amino acid from V to L at position 269.
+The protein's natural variant, known as in strain: PAK, features a modification of the amino acid from R to G at position 353.
+The protein's natural variant, known as in strain: NVIII-41, features a modification of the amino acid from S to T at position 12.
+The protein's natural variant, known as in strain: NVIII-9, features a modification of the amino acid from G to C at position 47.
+The protein's natural variant, known as in strain: NVIII-m11, features a modification of the amino acid from T to TQQQQ at position 65.
+The protein's natural variant, known as in strain: NVIII-m13, features a modification of the amino acid from Q to E at position 212.
+The protein's natural variant, known as in strain: NVIII-m11, features a modification of the amino acid from L to M at position 213.
+The protein's natural variant, known as in strain: s81 and s196, features a modification of the amino acid from N to K at position 57.
+The protein's natural variant, known as in strain: s82 and s84, features a modification of the amino acid from Q to L at position 86.
+The protein's natural variant, known as in strain: s82, features a modification of the amino acid from P to L at position 127.
+The protein's natural variant, known as in strain: s131, features a modification of the amino acid from A to S at position 137.
+The protein's natural variant, known as in strain: s95, features a modification of the amino acid from T to A at position 165.
+The protein's natural variant, known as in strain: s95, features a modification of the amino acid from K to Q at position 202.
+The protein's natural variant, known as in strain: s81, s95, s125, s131 and s196, features a modification of the amino acid from S to A at position 204.
+The protein's natural variant, known as in strain: s81 and s196, features a modification of the amino acid from T to A at position 281.
+The protein's natural variant, known as in strain: s189, features a modification of the amino acid from T to I at position 730.
+The protein's natural variant, known as in strain: s191, features a modification of the amino acid from Q to E at position 1408.
+The protein's natural variant, known as rare variant found in a patient with mitochondrial complex I deficiency; unknown pathological significance; found in association with a nucleotide transition causing exon skipping; does not affect protein stability, processing and import in the mitochondrion; can restore complex I activity when overexpressed in patient fibroblasts;, features a modification of the amino acid from G to R at position 56.
+The protein's natural variant, known as in MC1DN21;, features a modification of the amino acid from D to Y at position 105.
+The protein's natural variant, known as in MC1DN21;, features a modification of the amino acid from L to F at position 193.
+The protein's natural variant, known as in GA1;, features a modification of the amino acid from E to D at position 64.
+The protein's natural variant, known as in GA1;, features a modification of the amino acid from R to C at position 88.
+The protein's natural variant, known as in GA1;, features a modification of the amino acid from R to L at position 94.
+The protein's natural variant, known as in GA1;, features a modification of the amino acid from G to R at position 101.
+The protein's natural variant, known as in GA1;, features a modification of the amino acid from C to Y at position 115.
+The protein's natural variant, known as in GA1;, features a modification of the amino acid from A to V at position 122.
+The protein's natural variant, known as in GA1, features a modification of the amino acid from R to G at position 128.
+The protein's natural variant, known as in GA1; impaired protein stability; loss of activity;, features a modification of the amino acid from R to G at position 138.
+The protein's natural variant, known as in GA1;, features a modification of the amino acid from S to L at position 139.
+The protein's natural variant, known as in GA1;, features a modification of the amino acid from V to I at position 148.
+The protein's natural variant, known as in GA1;, features a modification of the amino acid from R to Q at position 161.
+The protein's natural variant, known as in GA1;, features a modification of the amino acid from G to R at position 178.
+The protein's natural variant, known as in GA1;, features a modification of the amino acid from L to R at position 179.
+The protein's natural variant, known as in GA1;, features a modification of the amino acid from M to T at position 191.
+The protein's natural variant, known as in GA1, features a modification of the amino acid from A to T at position 195.
+The protein's natural variant, known as in GA1;, features a modification of the amino acid from R to P at position 227.
+The protein's natural variant, known as in GA1;, features a modification of the amino acid from F to L at position 236.
+The protein's natural variant, known as in GA1;, features a modification of the amino acid from R to Q at position 257.
+The protein's natural variant, known as in GA1;, features a modification of the amino acid from R to W at position 257.
+The protein's natural variant, known as in GA1; severe phenotype; residual activity of 30% as measured in patient fibroblasts, features a modification of the amino acid from M to V at position 263.
+The protein's natural variant, known as in GA1;, features a modification of the amino acid from M to V at position 266.
+The protein's natural variant, known as in GA1;, features a modification of the amino acid from G to V at position 268.
+The protein's natural variant, known as in GA1;, features a modification of the amino acid from P to S at position 278.
+The protein's natural variant, known as in GA1, features a modification of the amino acid from L to P at position 283.
+The protein's natural variant, known as in GA1;, features a modification of the amino acid from A to T at position 293.
+The protein's natural variant, known as in GA1, features a modification of the amino acid from R to W at position 294.
+The protein's natural variant, known as in GA1;, features a modification of the amino acid from Y to H at position 295.
+The protein's natural variant, known as in GA1;, features a modification of the amino acid from S to L at position 305.
+The protein's natural variant, known as in GA1;, features a modification of the amino acid from C to S at position 308.
+The protein's natural variant, known as in GA1;, features a modification of the amino acid from L to W at position 309.
+The protein's natural variant, known as in GA1;, features a modification of the amino acid from R to W at position 313.
+The protein's natural variant, known as in GA1;, features a modification of the amino acid from Q to E at position 333.
+The protein's natural variant, known as in GA1;, features a modification of the amino acid from A to T at position 349.
+The protein's natural variant, known as in GA1, features a modification of the amino acid from G to R at position 354.
+The protein's natural variant, known as in GA1;, features a modification of the amino acid from G to S at position 354.
+The protein's natural variant, known as in GA1;, features a modification of the amino acid from R to C at position 355.
+The protein's natural variant, known as in GA1;, features a modification of the amino acid from R to H at position 355.
+The protein's natural variant, known as in GA1;, features a modification of the amino acid from E to K at position 365.
+The protein's natural variant, known as in GA1;, features a modification of the amino acid from C to R at position 375.
+The protein's natural variant, known as in GA1;, features a modification of the amino acid from A to T at position 382.
+The protein's natural variant, known as in GA1;, features a modification of the amino acid from R to C at position 383.
+The protein's natural variant, known as in GA1;, features a modification of the amino acid from R to H at position 383.
+The protein's natural variant, known as in GA1;, features a modification of the amino acid from R to Q at position 386.
+The protein's natural variant, known as in GA1;, features a modification of the amino acid from G to A at position 390.
+The protein's natural variant, known as in GA1;, features a modification of the amino acid from G to R at position 390.
+The protein's natural variant, known as in GA1;, features a modification of the amino acid from N to D at position 392.
+The protein's natural variant, known as in GA1;, features a modification of the amino acid from V to M at position 400.
+The protein's natural variant, known as in GA1;, features a modification of the amino acid from R to Q at position 402.
+The protein's natural variant, known as in GA1; most common mutation identified; loss of tetramerization; loss enzyme activity;, features a modification of the amino acid from R to W at position 402.
+The protein's natural variant, known as in GA1, features a modification of the amino acid from H to R at position 403.
+The protein's natural variant, known as in GA1, features a modification of the amino acid from N to K at position 406.
+The protein's natural variant, known as in GA1;, features a modification of the amino acid from L to P at position 407.
+The protein's natural variant, known as in GA1; loss of enzyme activity;, features a modification of the amino acid from E to K at position 414.
+The protein's natural variant, known as in GA1;, features a modification of the amino acid from T to I at position 416.
+The protein's natural variant, known as in GA1;, features a modification of the amino acid from A to T at position 421.
+The protein's natural variant, known as in GA1; impaired association of subunits;, features a modification of the amino acid from A to V at position 421.
+The protein's natural variant, known as in GA1;, features a modification of the amino acid from T to M at position 429.
+The protein's natural variant, known as in GA1;, features a modification of the amino acid from A to E at position 433.
+The protein's natural variant, known as in strain: IAM 1208, features a modification of the amino acid from E to D at position 212.
+The protein's natural variant, known as in strain: IAM 1208, features a modification of the amino acid from S to A at position 226.
+The protein's natural variant, known as in strain: IAM 1208, features a modification of the amino acid from K to R at position 239.
+The protein's natural variant, known as in strain: IAM 1208, features a modification of the amino acid from D to N at position 282.
+The natural variant of this protein is characterized by an amino acid alteration from K to R at position 494.
+The natural variant of this protein is characterized by an amino acid alteration from Q to H at position 51.
+The protein's natural variant, known as in allele APOA5*3; associated with high plasma triglyceride levels;, features a modification of the amino acid from S to W at position 19.
+The protein's natural variant, known as associated with high plasma triglyceride levels;, features a modification of the amino acid from G to C at position 185.
+The protein's natural variant, known as in BMFS4;, features a modification of the amino acid from H to R at position 656.
+The protein's natural variant, known as in HHC3; there is a rightward shift in Ca(2+)concentration-response curves with the mutant compared to wild-type, indicating a decrease in the sensitivity of cells expressing CASR to extracellular calcium;, features a modification of the amino acid from R to C at position 15.
+The protein's natural variant, known as in HHC3; there is a rightward shift in Ca(2+)concentration-response curves with the mutant compared to wild-type, indicating a decrease in the sensitivity of cells expressing CASR to extracellular calcium;, features a modification of the amino acid from R to H at position 15.
+The protein's natural variant, known as in HHC3; there is a rightward shift in Ca(2+)concentration-response curves with the mutant compared to wild-type, indicating a decrease in the sensitivity of cells expressing CASR to extracellular calcium;, features a modification of the amino acid from R to L at position 15.
+The protein's natural variant, known as in CDG2L;, features a modification of the amino acid from G to V at position 549.
+The protein's natural variant, known as in XP-G; patient cells show a strong DNA repair defect in response to UV light but not in response to oxidative stress; decreased nucleotide-excision repair activity;, features a modification of the amino acid from A to D at position 28.
+The protein's natural variant, known as in XP-G; combined with features of Cockayne syndrome;, features a modification of the amino acid from P to H at position 72.
+The protein's natural variant, known as in XP-G; mild form;, features a modification of the amino acid from A to V at position 792.
+The protein's natural variant, known as in XP-G; reduced stability and greatly impaired endonuclease activity;, features a modification of the amino acid from L to P at position 858.
+The protein's natural variant, known as in XP-G; mild form; residual activity;, features a modification of the amino acid from A to T at position 874.
+The protein's natural variant, known as in XP-G; patient cells show a strong DNA repair defect in response to UV light but not in response to oxidative stress; decreased nucleotide-excision repair activity;, features a modification of the amino acid from W to C at position 968.
+The protein's natural variant, known as found in a patient diagnosed with multiple sclerosis; unknown pathological significance;, features a modification of the amino acid from S to A at position 1078.
+The protein's natural variant, known as requires 2 nucleotide substitutions;, features a modification of the amino acid from G to Q at position 1080.
+The protein's natural variant, known as in MGCA9; unknown pathological significance;, features a modification of the amino acid from R to W at position 114.
+The protein's natural variant, known as in MGCA9; unknown pathological significance;, features a modification of the amino acid from T to M at position 149.
+The natural variant of this protein is characterized by an amino acid alteration from T to A at position 29.
+The natural variant of this protein is characterized by an amino acid alteration from F to L at position 40.
+The natural variant of this protein is characterized by an amino acid alteration from N to S at position 425.
+The natural variant of this protein is characterized by an amino acid alteration from A to V at position 83.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 100.
+The natural variant of this protein is characterized by an amino acid alteration from R to W at position 154.
+The natural variant of this protein is characterized by an amino acid alteration from QK to LN at position 240.
+The natural variant of this protein is characterized by an amino acid alteration from S to N at position 686.
+The protein's natural variant, known as in MC1DN30;, features a modification of the amino acid from E to K at position 121.
+The protein's natural variant, known as in CLS;, features a modification of the amino acid from G to V at position 75.
+The protein's natural variant, known as in CLS;, features a modification of the amino acid from V to F at position 82.
+The protein's natural variant, known as in CLS;, features a modification of the amino acid from R to W at position 114.
+The protein's natural variant, known as in XLID19;, features a modification of the amino acid from T to S at position 115.
+The protein's natural variant, known as in CLS, features a modification of the amino acid from H to Q at position 127.
+The protein's natural variant, known as in CLS, features a modification of the amino acid from D to Y at position 154.
+The protein's natural variant, known as in CLS;, features a modification of the amino acid from I to K at position 189.
+The protein's natural variant, known as in CLS;, features a modification of the amino acid from A to V at position 225.
+The protein's natural variant, known as in CLS;, features a modification of the amino acid from S to A at position 227.
+The protein's natural variant, known as in CLS;, features a modification of the amino acid from F to S at position 268.
+The protein's natural variant, known as in XLID19; kinase activity is decreased but not abolished;, features a modification of the amino acid from R to W at position 383.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from I to V at position 416.
+The protein's natural variant, known as in CLS, features a modification of the amino acid from G to D at position 431.
+The protein's natural variant, known as in a gastric adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from Y to C at position 483.
+The protein's natural variant, known as in a glioblastoma multiforme sample; somatic mutation, features a modification of the amino acid from L to F at position 608.
+The protein's natural variant, known as in CLS;, features a modification of the amino acid from R to Q at position 729.
+The natural variant of this protein is characterized by an amino acid alteration from A to L at position 218.
+The protein's natural variant, known as in EPM7; causes a dominant-negative loss of current upon membrane depolarization;, features a modification of the amino acid from R to H at position 320.
+The protein's natural variant, known as in MEGDEL, features a modification of the amino acid from G to D at position 401.
+The protein's natural variant, known as in MEGDEL, features a modification of the amino acid from G to E at position 404.
+The protein's natural variant, known as in MEGDEL;, features a modification of the amino acid from S to T at position 498.
+The protein's natural variant, known as in MEGDEL; unknown pathological significance;, features a modification of the amino acid from G to E at position 526.
+The natural variant of this protein is characterized by an amino acid alteration from C to CEMSPL at position 178.
+The protein's natural variant, known as in strain: MD-8, features a modification of the amino acid from M to V at position 282.
+The protein's natural variant, known as in strain: MD-8, features a modification of the amino acid from I to V at position 313.
+The protein's natural variant, known as in strain: MD-8, features a modification of the amino acid from P to L at position 640.
+The protein's natural variant, known as in strain: MD-8, features a modification of the amino acid from S to P at position 747.
+The protein's natural variant, known as in strain: MD-8, features a modification of the amino acid from S to N at position 897.
+The protein's natural variant, known as in strain: MD-8, features a modification of the amino acid from H to Y at position 1122.
+The protein's natural variant, known as in strain: Chinese, features a modification of the amino acid from G to S at position 3.
+The protein's natural variant, known as in strain: Chinese, features a modification of the amino acid from E to G at position 120.
+The protein's natural variant, known as in HSN1E; unstable protein with decreased enzymatic activity and impaired heterochromatin binding ability after the S phase;, features a modification of the amino acid from DP to EY at position 491.
+The protein's natural variant, known as in HSN1E; unstable protein with decreased enzymatic activity and impaired heterochromatin binding ability after the S phase;, features a modification of the amino acid from Y to C at position 495.
+The protein's natural variant, known as in ADCADN;, features a modification of the amino acid from A to V at position 554.
+The protein's natural variant, known as in ADCADN;, features a modification of the amino acid from G to A at position 589.
+The protein's natural variant, known as in ADCADN;, features a modification of the amino acid from V to F at position 590.
+The natural variant of this protein is characterized by an amino acid alteration from A to T at position 85.
+The protein's natural variant, known as in SPAI-3, features a modification of the amino acid from R to G at position 148.
+The protein's natural variant, known as in SPAI-3, features a modification of the amino acid from S to G at position 156.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from IDGQL to VDEQI at position 31.
+The protein's natural variant, known as in strain: cv. Di-17, features a modification of the amino acid from G to E at position 29.
+The protein's natural variant, known as in strain: cv. Di-17 and cv. Landsberg erecta, features a modification of the amino acid from SGK to RGE at position 87.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from GKGV to EKGI at position 91.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from C to R at position 100.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from E to D at position 121.
+The protein's natural variant, known as in strain: cv. Di-17, features a modification of the amino acid from F to L at position 129.
+The protein's natural variant, known as in strain: cv. Di-17, features a modification of the amino acid from Q to QQ at position 133.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from G to V at position 138.
+The protein's natural variant, known as in strain: cv. Di-17, features a modification of the amino acid from K to T at position 173.
+The protein's natural variant, known as in strain: cv. Di-17, features a modification of the amino acid from G to C at position 177.
+The protein's natural variant, known as in strain: cv. Di-17, features a modification of the amino acid from Y to S at position 253.
+The protein's natural variant, known as in strain: cv. Di-17, features a modification of the amino acid from R to P at position 257.
+The protein's natural variant, known as in strain: cv. Di-17, features a modification of the amino acid from A to T at position 265.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from R to K at position 267.
+The protein's natural variant, known as in strain: cv. Di-17, features a modification of the amino acid from V to L at position 270.
+The protein's natural variant, known as in strain: cv. Di-17, features a modification of the amino acid from V to R at position 283.
+The protein's natural variant, known as in strain: cv. Di-17 and cv. Landsberg erecta, features a modification of the amino acid from A to V at position 369.
+The protein's natural variant, known as in strain: cv. Di-17 and cv. Landsberg erecta, features a modification of the amino acid from F to S at position 387.
+The protein's natural variant, known as in strain: cv. Di-17 and cv. Landsberg erecta, features a modification of the amino acid from W to C at position 399.
+The protein's natural variant, known as in strain: cv. Di-17 and cv. Landsberg erecta, features a modification of the amino acid from C to R at position 426.
+The protein's natural variant, known as in strain: cv. Di-17 and cv. Landsberg erecta, features a modification of the amino acid from N to F at position 429.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from DSEISTYSLFY to YSKISAYDLFN at position 446.
+The protein's natural variant, known as in strain: cv. Di-17, features a modification of the amino acid from EISTYS to KITTQE at position 443.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from A to V at position 450.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from E to Q at position 460.
+The protein's natural variant, known as in strain: cv. Di-17, features a modification of the amino acid from DNYLSWQ to NKYLRVH at position 486.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from DN to NR at position 481.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from WQ to SH at position 486.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from Y to N at position 489.
+The protein's natural variant, known as in strain: cv. Di-17 and cv. Landsberg erecta, features a modification of the amino acid from I to K at position 514.
+The protein's natural variant, known as in strain: cv. Di-17 and cv. Landsberg erecta, features a modification of the amino acid from C to S at position 518.
+The protein's natural variant, known as in strain: cv. Di-17, features a modification of the amino acid from T to I at position 519.
+The protein's natural variant, known as in strain: cv. Di-17, features a modification of the amino acid from S to R at position 528.
+The protein's natural variant, known as in strain: cv. Di-17, features a modification of the amino acid from S to R at position 537.
+The protein's natural variant, known as in strain: cv. Di-17, features a modification of the amino acid from H to Q at position 542.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from I to L at position 543.
+The protein's natural variant, known as in strain: cv. Di-17, features a modification of the amino acid from KNKT to RNNA at position 550.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from K to N at position 549.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from PRFEEDYW to WDEDFG at position 565.
+The protein's natural variant, known as in strain: cv. Di-17, features a modification of the amino acid from PRF to SRFK at position 560.
+The protein's natural variant, known as in strain: cv. Di-17, features a modification of the amino acid from Y to F at position 564.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from S to Y at position 584.
+The protein's natural variant, known as in strain: cv. Di-17 and cv. Landsberg erecta, features a modification of the amino acid from C to S at position 595.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from YEAK to FLAG at position 612.
+The protein's natural variant, known as in strain: cv. Di-17, features a modification of the amino acid from NLRVDT to DLSVHE at position 635.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from RVDTE to SVNNK at position 636.
+The protein's natural variant, known as in strain: cv. Di-17, features a modification of the amino acid from Q to E at position 650.
+The protein's natural variant, known as in strain: cv. Di-17, features a modification of the amino acid from YL to HI at position 654.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from M to K at position 660.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from YLY to FLF at position 678.
+The protein's natural variant, known as in strain: cv. Di-17, features a modification of the amino acid from YG to FR at position 679.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from R to H at position 692.
+The protein's natural variant, known as in strain: cv. Di-17, features a modification of the amino acid from R to Q at position 697.
+The protein's natural variant, known as in strain: cv. Di-17, features a modification of the amino acid from A to G at position 700.
+The protein's natural variant, known as in strain: cv. Di-17, features a modification of the amino acid from T to S at position 724.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from NF to YV at position 727.
+The protein's natural variant, known as in strain: cv. Di-17, features a modification of the amino acid from SL to TP at position 731.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from LETY to PEIF at position 734.
+The protein's natural variant, known as in strain: cv. Di-17 and cv. Landsberg erecta, features a modification of the amino acid from Q to E at position 752.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from F to L at position 768.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from VHLFLIYCG to AQIYICNCR at position 781.
+The protein's natural variant, known as in strain: cv. Di-17, features a modification of the amino acid from VHLFLIYCG to THIHLLFCR at position 781.
+The protein's natural variant, known as in strain: cv. Di-17, features a modification of the amino acid from RLARKAFL to QLTDEAFV at position 807.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from RLAR to KLTF at position 803.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from LGS to AGR at position 809.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from P to T at position 819.
+The protein's natural variant, known as in strain: cv. Di-17 and cv. Landsberg erecta, features a modification of the amino acid from VI to AL at position 824.
+The protein's natural variant, known as in strain: cv. Di-17, features a modification of the amino acid from E to D at position 825.
+The protein's natural variant, known as in strain: cv. Landsberg erecta, features a modification of the amino acid from KE to EQ at position 829.
+The protein's natural variant, known as in strain: cv. Di-17 and cv. Landsberg erecta, features a modification of the amino acid from D to H at position 851.
+The protein's natural variant, known as in strain: cv. Di-17 and cv. Landsberg erecta, features a modification of the amino acid from K to E at position 854.
+The protein's natural variant, known as in bladder carcinoma cell line Hu549; requires 2 nucleotide substitutions, features a modification of the amino acid from C to Q at position 26.
+The protein's natural variant, known as in bladder carcinoma cell line Hu549;, features a modification of the amino acid from S to G at position 35.
+The protein's natural variant, known as in HIGM3, features a modification of the amino acid from C to G at position 37.
+The protein's natural variant, known as in bladder carcinoma cell line Hu549, features a modification of the amino acid from S to T at position 39.
+The protein's natural variant, known as in HIGM3;, features a modification of the amino acid from C to R at position 83.
+The protein's natural variant, known as in a breast pleomorphic lobular carcinoma sample; somatic mutation, features a modification of the amino acid from D to H at position 297.
+The protein's natural variant, known as in ACY1D; loss of activity;, features a modification of the amino acid from R to W at position 197.
+The protein's natural variant, known as in ACY1D; loss of activity;, features a modification of the amino acid from E to D at position 233.
+The protein's natural variant, known as in ACY1D; loss of activity;, features a modification of the amino acid from R to C at position 353.
+The protein's natural variant, known as in ACY1D;, features a modification of the amino acid from R to Q at position 378.
+The protein's natural variant, known as in ACY1D; slightly reduced activity;, features a modification of the amino acid from R to W at position 378.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from E to D at position 381.
+The protein's natural variant, known as in ACY1D; loss of activity;, features a modification of the amino acid from R to C at position 386.
+The protein's natural variant, known as in ACY1D;, features a modification of the amino acid from R to H at position 393.
+The protein's natural variant, known as in CPT2D; muscular type;, features a modification of the amino acid from P to H at position 50.
+The protein's natural variant, known as in CPT2D; muscular form; frequent mutation;, features a modification of the amino acid from S to L at position 113.
+The protein's natural variant, known as in CPT2D;, features a modification of the amino acid from R to Q at position 151.
+The protein's natural variant, known as in CPT2D; muscular type;, features a modification of the amino acid from E to K at position 174.
+The protein's natural variant, known as in CPT2D, features a modification of the amino acid from Y to D at position 210.
+The protein's natural variant, known as in CPT2D;, features a modification of the amino acid from D to G at position 213.
+The protein's natural variant, known as in CPT2D;, features a modification of the amino acid from M to T at position 214.
+The protein's natural variant, known as in CPT2D;, features a modification of the amino acid from P to L at position 227.
+The protein's natural variant, known as in CPT2D;, features a modification of the amino acid from R to Q at position 296.
+The protein's natural variant, known as associated with susceptibility to IIAE4; 3-fold decrease of affinity for L-carnitine; lower thermal stability compared to wild-type;, features a modification of the amino acid from F to C at position 352.
+The protein's natural variant, known as associated with susceptibility to IIAE4; no effect on activity; does not affect affinity for L-carnitine; lower thermal stability compared to wild-type;, features a modification of the amino acid from V to I at position 368.
+The protein's natural variant, known as in CPT2D; hepatocardiomuscular form;, features a modification of the amino acid from F to Y at position 383.
+The protein's natural variant, known as in CPT2D;, features a modification of the amino acid from F to L at position 448.
+The protein's natural variant, known as in CPT2D;, features a modification of the amino acid from Y to F at position 479.
+The protein's natural variant, known as in CPT2D;, features a modification of the amino acid from R to C at position 503.
+The protein's natural variant, known as in a patient with IIAE4;, features a modification of the amino acid from P to L at position 504.
+The protein's natural variant, known as in CPT2D;, features a modification of the amino acid from G to D at position 549.
+The protein's natural variant, known as in CPT2D, features a modification of the amino acid from Q to R at position 550.
+The protein's natural variant, known as in CPT2D;, features a modification of the amino acid from D to N at position 553.
+The protein's natural variant, known as in CPT2D, features a modification of the amino acid from G to R at position 600.
+The protein's natural variant, known as in CPT2D, features a modification of the amino acid from P to S at position 604.
+The protein's natural variant, known as in a patient with IIAE4;, features a modification of the amino acid from V to L at position 605.
+The protein's natural variant, known as in CPT2DI; hepatocardiomuscular form;, features a modification of the amino acid from Y to S at position 628.
+The protein's natural variant, known as in CPT2DI and CPT2D; early-onset hepatocardiomuscular form;, features a modification of the amino acid from R to C at position 631.
+The protein's natural variant, known as confirmed at protein level;, features a modification of the amino acid from M to V at position 647.
+The protein's natural variant, known as in strain: KIM5, features a modification of the amino acid from LTGKHWQLKLT to FVNDG at position 140.
+The protein's natural variant, known as in one patient with acute myeloid leukemya; somatic mutation, features a modification of the amino acid from V to E at position 685.
+The protein's natural variant, known as in NDNC3, features a modification of the amino acid from T to R at position 209.
+The protein's natural variant, known as in NDNC3, features a modification of the amino acid from I to T at position 574.
+The natural variant of this protein is characterized by an amino acid alteration from H to Q at position 27.
+The protein's natural variant, known as in RP17;, features a modification of the amino acid from A to T at position 12.
+The protein's natural variant, known as in RP17; abolishes interaction with SLC4A4; impaired SLC4A4 cotransporter activity stimulation;, features a modification of the amino acid from R to W at position 14.
+The protein's natural variant, known as in RP17; has no effect on carbonate dehydratase activity; loss of interaction with SLC4A4;, features a modification of the amino acid from R to H at position 69.
+The protein's natural variant, known as in RP17; abolishes carbonate dehydratase activity; impaired SLC4A4 cotransporter activity stimulation;, features a modification of the amino acid from R to S at position 219.
+The protein's natural variant, known as in MTDPS11; impaired exonuclease activity;, features a modification of the amino acid from Y to C at position 233.
+The protein's natural variant, known as in allele POLB100, features a modification of the amino acid from G to D at position 401.
+The natural variant of this protein is characterized by an amino acid alteration from A to P at position 25.
+The natural variant of this protein is characterized by an amino acid alteration from I to L at position 46.
+The natural variant of this protein is characterized by an amino acid alteration from V to A at position 116.
+The natural variant of this protein is characterized by an amino acid alteration from T to I at position 142.
+The natural variant of this protein is characterized by an amino acid alteration from L to A at position 188.
+The natural variant of this protein is characterized by an amino acid alteration from P to T at position 200.
+The natural variant of this protein is characterized by an amino acid alteration from S to T at position 267.
+The natural variant of this protein is characterized by an amino acid alteration from S to A at position 284.
+The natural variant of this protein is characterized by an amino acid alteration from S to G at position 301.
+The natural variant of this protein is characterized by an amino acid alteration from D to G at position 324.
+The natural variant of this protein is characterized by an amino acid alteration from D to E at position 72.
+The protein's natural variant, known as associated with susceptibility to myocardial infarction type 1; increases activation of MAPK14 by oxidized low density lipoprotein;, features a modification of the amino acid from R to Q at position 952.
+The protein's natural variant, known as in strain: 129/SvJ, features a modification of the amino acid from I to V at position 46.
+The protein's natural variant, known as in strain: 129/SvJ, features a modification of the amino acid from D to G at position 66.
+The protein's natural variant, known as in strain: 129/SvJ, features a modification of the amino acid from T to P at position 137.
+The protein's natural variant, known as in strain: 129/SvJ, features a modification of the amino acid from S to T at position 159.
+The protein's natural variant, known as in strain: 129/SvJ, features a modification of the amino acid from D to E at position 243.
+The protein's natural variant, known as in strain: 129/SvJ, features a modification of the amino acid from S to P at position 526.
+The protein's natural variant, known as in strain: 129/SvJ, features a modification of the amino acid from A to V at position 536.
+The protein's natural variant, known as in cell line V79-4, features a modification of the amino acid from L to Q at position 133.
+The protein's natural variant, known as in cell line V79-4, features a modification of the amino acid from C to W at position 135.
+The natural variant of this protein is characterized by an amino acid alteration from H to N at position 88.
+The natural variant of this protein is characterized by an amino acid alteration from S to T at position 90.
+The natural variant of this protein is characterized by an amino acid alteration from T to S at position 124.
+The natural variant of this protein is characterized by an amino acid alteration from G to C at position 91.
+The protein's natural variant, known as rare variant found in patients with X-linked intellectual disability; unknown pathological significance;, features a modification of the amino acid from V to G at position 311.
+The protein's natural variant, known as in CDG1CC; no effect on protein expression; decreased protein N-linked glycosylation of STT3B-specific substrates;, features a modification of the amino acid from K to N at position 324.
+The protein's natural variant, known as in variant C, features a modification of the amino acid from H to I at position 23.
+The protein's natural variant, known as in variant A, features a modification of the amino acid from P to L at position 31.
+The protein's natural variant, known as in variant A, features a modification of the amino acid from E to Q at position 92.
+The protein's natural variant, known as in variants E and C, features a modification of the amino acid from R to K at position 115.
+The protein's natural variant, known as in variant E, features a modification of the amino acid from T to A at position 209.
+The protein's natural variant, known as in variants E and C, features a modification of the amino acid from T to A at position 210.
+The protein's natural variant, known as rare variant found in patients with X-linked intellectual disability; unknown pathological significance;, features a modification of the amino acid from P to L at position 153.
+The protein's natural variant, known as in CLN7;, features a modification of the amino acid from G to R at position 52.
+The protein's natural variant, known as in CLN7;, features a modification of the amino acid from Y to C at position 121.
+The protein's natural variant, known as in CLN7;, features a modification of the amino acid from R to H at position 139.
+The protein's natural variant, known as in CLN7; due to a deletion-insertion mutation at nucleotide level, features a modification of the amino acid from A to P at position 157.
+The protein's natural variant, known as in CLN7;, features a modification of the amino acid from T to I at position 160.
+The protein's natural variant, known as in CLN7, features a modification of the amino acid from T to N at position 160.
+The protein's natural variant, known as in CLN7;, features a modification of the amino acid from T to K at position 294.
+The protein's natural variant, known as in CLN7; lysosomal localization;, features a modification of the amino acid from G to D at position 310.
+The protein's natural variant, known as in CCMD;, features a modification of the amino acid from E to Q at position 336.
+The protein's natural variant, known as in CLN7;, features a modification of the amino acid from P to L at position 412.
+The protein's natural variant, known as in CLN7; lysosomal localization;, features a modification of the amino acid from G to D at position 429.
+The protein's natural variant, known as in CLN7, features a modification of the amino acid from P to L at position 447.
+The protein's natural variant, known as in CLN7, features a modification of the amino acid from T to K at position 458.
+The protein's natural variant, known as in CLN7;, features a modification of the amino acid from R to Q at position 465.
+The protein's natural variant, known as in CLN7;, features a modification of the amino acid from R to W at position 465.
+The protein's natural variant, known as in CLN7;, features a modification of the amino acid from M to V at position 470.
+The protein's natural variant, known as in an ovarian mucinous carcinoma sample; somatic mutation;, features a modification of the amino acid from N to K at position 525.
+The protein's natural variant, known as in an ovarian serous carcinoma sample; somatic mutation, features a modification of the amino acid from S to R at position 956.
+The protein's natural variant, known as in a renal clear cell carcinoma sample; somatic mutation, features a modification of the amino acid from D to H at position 1347.
+The natural variant of this protein is characterized by an amino acid alteration from S to R at position 244.
+The natural variant of this protein is characterized by an amino acid alteration from L to S at position 258.
+The protein's natural variant, known as in plasmid pWR100, features a modification of the amino acid from V to A at position 58.
+The protein's natural variant, known as in AADCD;, features a modification of the amino acid from P to H at position 47.
+The protein's natural variant, known as in AADCD;, features a modification of the amino acid from A to V at position 91.
+The protein's natural variant, known as in AADCD;, features a modification of the amino acid from G to S at position 102.
+The protein's natural variant, known as in AADCD;, features a modification of the amino acid from S to R at position 147.
+The protein's natural variant, known as in AADCD;, features a modification of the amino acid from S to F at position 250.
+The protein's natural variant, known as in AADCD;, features a modification of the amino acid from A to T at position 275.
+The protein's natural variant, known as in AADCD;, features a modification of the amino acid from F to L at position 309.
+The protein's natural variant, known as in AADCD;, features a modification of the amino acid from R to Q at position 347.
+The protein's natural variant, known as in AADCD, features a modification of the amino acid from L to I at position 408.
+The natural variant of this protein is characterized by an amino acid alteration from ST to AK at position 26.
+The natural variant of this protein is characterized by an amino acid alteration from P to S at position 70.
+The natural variant of this protein is characterized by an amino acid alteration from V to M at position 61.
+The natural variant of this protein is characterized by an amino acid alteration from N to S at position 197.
+The natural variant of this protein is characterized by an amino acid alteration from W to R at position 205.
+The protein's natural variant, known as in strain: R-26.1, features a modification of the amino acid from V to F at position 24.
+The protein's natural variant, known as in MT58 cell line, features a modification of the amino acid from R to H at position 140.
+The natural variant of this protein is characterized by an amino acid alteration from K to N at position 5.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from R to T at position 6.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from L to P at position 17.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from P to L at position 26.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from G to A at position 27.
+The protein's natural variant, known as in HPE3; the same mutation in the mouse sequence introduces a cleavage site for a furin-like protease resulting in abnormal protein processing; cleavage at this site removes 11 amino acids from the N-terminal domain and reduces affinity of Shh for Ptch1 and signaling potency in assays using chicken embryo neural plate explants and mouse C3H10T1/2 stem cells;, features a modification of the amino acid from G to R at position 31.
+The protein's natural variant, known as in HPE3;, features a modification of the amino acid from L to P at position 39.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from E to K at position 53.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from D to V at position 83.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from I to F at position 84.
+The protein's natural variant, known as in HPE3; familial; the same mutation in the mouse sequence moderately reduces Ptch1 binding in vitro and signaling potency in chicken embryo neural plate explant assays compared with wild-type sequence;, features a modification of the amino acid from D to V at position 88.
+The protein's natural variant, known as in HPE3; sporadic; in the mouse sequence does not affect signaling activity in any of Shh signaling assays and causes no apparent defects in cholesterol-mediated autoprocessing reactions;, features a modification of the amino acid from Q to H at position 100.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from C to R at position 102.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from C to Y at position 102.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from L to F at position 109.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from A to D at position 110.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from A to T at position 110.
+The protein's natural variant, known as in SMMCI;, features a modification of the amino acid from I to F at position 111.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from I to N at position 111.
+The protein's natural variant, known as in HPE3; familial; in the mouse sequence shows no change in activities at different temperatures;, features a modification of the amino acid from N to K at position 115.
+The protein's natural variant, known as in HPE3; the same mutation in the mouse sequence causes a failure of Shh processing leading to retention of the immature glycosylated protein within the endoplasmic reticulum of transfected cells; causes a temperature-dependent conformational change that allows Shh to bind Ptch1 at 4 or 32 degrees Celsius but not at 37 degrees Celsius; the mutation drastically reduces signaling potency in chicken embryo neural plate explant assays;, features a modification of the amino acid from W to G at position 117.
+The protein's natural variant, known as in HPE3; the same mutation in the mouse sequence causes a failure of Shh processing leading to retention of the immature glycosylated protein within the endoplasmic reticulum of transfected cells; causes a temperature-dependent conformational change that allows Shh to bind Ptch1 at 4 or 32 degrees Celsius but not at 37 degrees Celsius; drastically reduces signaling potency in chicken embryo neural plate explant assays;, features a modification of the amino acid from W to R at position 117.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from V to M at position 124.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from E to K at position 136.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from H to P at position 140.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from H to Q at position 140.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from G to D at position 143.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from R to P at position 144.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from D to N at position 147.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from T to K at position 150.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from T to R at position 150.
+The protein's natural variant, known as in HPE3;, features a modification of the amino acid from S to R at position 156.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from F to C at position 170.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from D to H at position 171.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from C to F at position 183.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from C to R at position 183.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from C to Y at position 183.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from S to L at position 184.
+The protein's natural variant, known as in HPE3; familial;, features a modification of the amino acid from E to Q at position 188.
+The protein's natural variant, known as in HPE3;, features a modification of the amino acid from G to E at position 196.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from G to V at position 197.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from C to F at position 198.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from C to S at position 198.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from L to P at position 218.
+The protein's natural variant, known as in HPE3; familial;, features a modification of the amino acid from D to N at position 222.
+The protein's natural variant, known as in HPE3;, features a modification of the amino acid from V to E at position 224.
+The protein's natural variant, known as in HPE3; familial;, features a modification of the amino acid from A to T at position 226.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from G to V at position 231.
+The protein's natural variant, known as in HPE3;, features a modification of the amino acid from R to G at position 232.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from L to P at position 234.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from S to N at position 236.
+The protein's natural variant, known as in HPE3; familial;, features a modification of the amino acid from S to R at position 236.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from F to L at position 241.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from F to V at position 241.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from I to N at position 255.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from T to I at position 267.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from L to P at position 271.
+The protein's natural variant, known as in HPE3;, features a modification of the amino acid from A to E at position 275.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from S to W at position 280.
+The protein's natural variant, known as in HPE3; sporadic;, features a modification of the amino acid from G to D at position 290.
+The protein's natural variant, known as in HPE3; unknown pathological significance;, features a modification of the amino acid from G to A at position 296.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from R to C at position 310.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from R to S at position 321.
+The protein's natural variant, known as in HPE3 and SMMCI;, features a modification of the amino acid from V to A at position 332.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from A to V at position 346.
+The protein's natural variant, known as in HPE3;, features a modification of the amino acid from P to L at position 347.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from P to Q at position 347.
+The protein's natural variant, known as in HPE3;, features a modification of the amino acid from P to R at position 347.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from I to T at position 354.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from S to L at position 362.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from C to Y at position 363.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from Y to C at position 364.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from A to T at position 373.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from H to R at position 374.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from A to D at position 376.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from F to S at position 377.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from R to P at position 381.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from L to P at position 382.
+The protein's natural variant, known as in HPE3; sporadic;, features a modification of the amino acid from A to T at position 383.
+The protein's natural variant, known as in HPE3; unknown pathological significance;, features a modification of the amino acid from A to T at position 391.
+The protein's natural variant, known as in HPE3; unknown pathological significance, features a modification of the amino acid from G to GG at position 411.
+The protein's natural variant, known as in HPE3; unknown pathological significance;, features a modification of the amino acid from T to A at position 416.
+The protein's natural variant, known as in HPE3; familial;, features a modification of the amino acid from P to A at position 424.
+The protein's natural variant, known as in HPE3, features a modification of the amino acid from Y to N at position 435.
+The protein's natural variant, known as in HPE3; sporadic, features a modification of the amino acid from S to L at position 436.
+The protein's natural variant, known as in HPE3; unknown pathological significance, features a modification of the amino acid from G to R at position 456.
+The protein's natural variant, known as found in a family with prostate cancer;, features a modification of the amino acid from P to A at position 36.
+The protein's natural variant, known as found in patients with prostate cancer;, features a modification of the amino acid from S to Y at position 41.
+The protein's natural variant, known as found in patients with prostate cancer;, features a modification of the amino acid from V to A at position 113.
+The protein's natural variant, known as found in patients with prostate cancer;, features a modification of the amino acid from D to Y at position 174.
+The protein's natural variant, known as found in patients with Barrett esophagus;, features a modification of the amino acid from L to V at position 254.
+The protein's natural variant, known as found in a family with prostate cancer;, features a modification of the amino acid from G to S at position 369.
+The protein's natural variant, known as found in patients with prostate cancer;, features a modification of the amino acid from H to R at position 441.
+The natural variant of this protein is characterized by an amino acid alteration from S to T at position 712.
+The protein's natural variant, known as in allele ADH1-Cm, features a modification of the amino acid from Y to D at position 52.
+The protein's natural variant, known as in allele ADH1-S, features a modification of the amino acid from A to G at position 127.
+The protein's natural variant, known as in allele ADH1-Cm and allele ADH1-S, features a modification of the amino acid from Y to I at position 179.
+The protein's natural variant, known as in allele ADH1-S, features a modification of the amino acid from D to N at position 363.
+The protein's natural variant, known as in COXPD34; results in decreased mitochondrial protein synthesis and reduced levels of respiratory complexes; MRPS7 mRNA and protein levels are reduced;, features a modification of the amino acid from M to V at position 184.
+The protein's natural variant, known as in LIS1;, features a modification of the amino acid from F to S at position 31.
+The protein's natural variant, known as in LIS1; abrogates interaction with NDE1 and reduces neuronal migration in vitro;, features a modification of the amino acid from H to R at position 149.
+The protein's natural variant, known as in LIS1;, features a modification of the amino acid from G to S at position 162.
+The protein's natural variant, known as in SBH; abrogates interaction with NDE1 and reduces neuronal migration in vitro;, features a modification of the amino acid from S to P at position 169.
+The protein's natural variant, known as in SBH; somatic mosaicism in 18% of lymphocytes and 21% of hair root cells;, features a modification of the amino acid from R to P at position 241.
+The protein's natural variant, known as in LIS1;, features a modification of the amino acid from H to P at position 277.
+The protein's natural variant, known as in LIS1; reduces neuronal migration in vitro;, features a modification of the amino acid from D to H at position 317.
+The protein's natural variant, known as in strain: GS77; resistant to cerulenin, features a modification of the amino acid from I to F at position 109.
+The protein's natural variant, known as in strain: Isolate SO-03/2/17-2, features a modification of the amino acid from K to T at position 6.
+The protein's natural variant, known as in strain: Isolate SO-03/2/17-2, features a modification of the amino acid from I to T at position 39.
+The protein's natural variant, known as in strain: Isolate SO-03/2/17-2, features a modification of the amino acid from S to L at position 213.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from E to K at position 278.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from E to Q at position 640.
+The protein's natural variant, known as in CVID13; abolishes binding to DNA; has diffuse nuclear localization;, features a modification of the amino acid from R to L at position 162.
+The protein's natural variant, known as in CVID13; abolishes binding to DNA; has diffuse nuclear localization;, features a modification of the amino acid from R to Q at position 162.
+The protein's natural variant, known as in CVID13; abolishes binding to DNA; has diffuse nuclear localization;, features a modification of the amino acid from H to R at position 167.
+The protein's natural variant, known as in CVID13; abolishes binding to DNA; has diffuse nuclear localization;, features a modification of the amino acid from R to Q at position 184.
+The protein's natural variant, known as in CVID13; decreases binding to pericentromeric heterochromatin DNA; has diffuse nuclear localization;, features a modification of the amino acid from Y to C at position 210.
+The natural variant of this protein is characterized by an amino acid alteration from R to K at position 54.
+The natural variant of this protein is characterized by an amino acid alteration from A to S at position 97.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 125.
+The protein's natural variant, known as in TDH6, features a modification of the amino acid from Q to H at position 36.
+The protein's natural variant, known as in TDH6;, features a modification of the amino acid from R to W at position 376.
+The protein's natural variant, known as found in a patient with very early onset inflammatory bowel disease; unknown pathological significance; no effect on subcellular location; significantly reduced ROS generation, which may decrease resistance to infection by enteric pathogens, such as Escherichia coli;, features a modification of the amino acid from R to C at position 1211.
+The protein's natural variant, known as found in a patient with very early onset inflammatory bowel disease; unknown pathological significance; no effect on subcellular location; significantly reduced ROS generation, which may decrease resistance to infection by enteric pathogens, such as Escherichia coli;, features a modification of the amino acid from R to C at position 1492.
+The protein's natural variant, known as in TDH6; the enzyme is non-functional; expressed at the cell surface of cells albeit at low level;, features a modification of the amino acid from G to S at position 1518.
+The natural variant of this protein is characterized by an amino acid alteration from T to R at position 60.
+The protein's natural variant, known as in WMS1; shows consistent and significantly diminished protein secretion, features a modification of the amino acid from A to T at position 25.
+The protein's natural variant, known as in MLS, features a modification of the amino acid from R to G at position 222.
+The protein's natural variant, known as in MLS;, features a modification of the amino acid from C to R at position 294.
+The protein's natural variant, known as in MLS; atypical without hematologic, neuromuscular, or cerebral involvement, features a modification of the amino acid from E to K at position 327.
+The protein's natural variant, known as in APMR4; unknown pathological significance, features a modification of the amino acid from G to D at position 12.
+The protein's natural variant, known as in APMR4; unknown pathological significance, features a modification of the amino acid from Y to C at position 14.
+The protein's natural variant, known as in HYPT14; the protein is present in the ER but also mislocalized to the cytoplasm, features a modification of the amino acid from L to V at position 102.
+The protein's natural variant, known as in APMR4; changed localization; the protein is present in the ER but is also mislocalized to the cytoplasm;, features a modification of the amino acid from N to Y at position 209.
+The protein's natural variant, known as in HYPT14; changed localization; the protein is present in the ER but is also mislocalized to the cytoplasm;, features a modification of the amino acid from L to P at position 248.
+The protein's natural variant, known as in APMR4; unknown pathological significance, features a modification of the amino acid from R to P at position 260.
+The protein's natural variant, known as in APMR4; unknown pathological significance, features a modification of the amino acid from Y to C at position 286.
+The protein's natural variant, known as in CTRCT44; associated with hypotrichosis; unknown pathological significance, features a modification of the amino acid from I to S at position 342.
+The protein's natural variant, known as in HYPT14; changed localization; the protein is present in the ER but is also mislocalized to the cytoplasm;, features a modification of the amino acid from F to S at position 391.
+The protein's natural variant, known as in APMR4; unknown pathological significance, features a modification of the amino acid from N to S at position 516.
+The protein's natural variant, known as in CTRCT44; loss of lanosterol synthase activity;, features a modification of the amino acid from W to R at position 581.
+The protein's natural variant, known as in CTRCT44; loss of lanosterol synthase activity;, features a modification of the amino acid from G to S at position 588.
+The protein's natural variant, known as in CTRCT44; associated with hypotrichosis; unknown pathological significance, features a modification of the amino acid from W to C at position 629.
+The protein's natural variant, known as in APMR4; unknown pathological significance, features a modification of the amino acid from T to I at position 652.
+The protein's natural variant, known as in APMR4; unknown pathological significance, features a modification of the amino acid from T to K at position 705.
+The protein's natural variant, known as in a lung large cell carcinoma sample; somatic mutation, features a modification of the amino acid from E to K at position 25.
+The protein's natural variant, known as in SRTD6;, features a modification of the amino acid from G to R at position 145.
+The protein's natural variant, known as in SRTD6, features a modification of the amino acid from L to S at position 253.
+The protein's natural variant, known as in ALS24; associated with disease susceptibility;, features a modification of the amino acid from R to H at position 261.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation, features a modification of the amino acid from A to P at position 294.
+The natural variant of this protein is characterized by an amino acid alteration from K to N at position 745.
+The natural variant of this protein is characterized by an amino acid alteration from F to V at position 80.
+The natural variant of this protein is characterized by an amino acid alteration from S to P at position 2.
+The natural variant of this protein is characterized by an amino acid alteration from L to M at position 8.
+The natural variant of this protein is characterized by an amino acid alteration from W to G at position 23.
+The natural variant of this protein is characterized by an amino acid alteration from M to T at position 38.
+The natural variant of this protein is characterized by an amino acid alteration from N to S at position 103.
+The natural variant of this protein is characterized by an amino acid alteration from I to M at position 148.
+The natural variant of this protein is characterized by an amino acid alteration from H to Y at position 218.
+The natural variant of this protein is characterized by an amino acid alteration from I to M at position 226.
+The natural variant of this protein is characterized by an amino acid alteration from I to T at position 226.
+The natural variant of this protein is characterized by an amino acid alteration from A to T at position 230.
+The natural variant of this protein is characterized by an amino acid alteration from S to F at position 236.
+The natural variant of this protein is characterized by an amino acid alteration from P to S at position 245.
+The natural variant of this protein is characterized by an amino acid alteration from F to Y at position 298.
+The natural variant of this protein is characterized by an amino acid alteration from F to M at position 304.
+The natural variant of this protein is characterized by an amino acid alteration from T to M at position 308.
+The natural variant of this protein is characterized by an amino acid alteration from T to A at position 319.
+The natural variant of this protein is characterized by an amino acid alteration from L to M at position 320.
+The natural variant of this protein is characterized by an amino acid alteration from F to L at position 324.
+The natural variant of this protein is characterized by an amino acid alteration from V to M at position 335.
+The natural variant of this protein is characterized by an amino acid alteration from A to V at position 345.
+The natural variant of this protein is characterized by an amino acid alteration from I to S at position 348.
+The natural variant of this protein is characterized by an amino acid alteration from T to M at position 352.
+The natural variant of this protein is characterized by an amino acid alteration from D to T at position 186.
+The natural variant of this protein is characterized by an amino acid alteration from S to T at position 317.
+The protein's natural variant, known as in NEM6;, features a modification of the amino acid from R to S at position 248.
+The protein's natural variant, known as in NEM6;, features a modification of the amino acid from K to N at position 390.
+The protein's natural variant, known as in NEM6;, features a modification of the amino acid from R to C at position 408.
+The protein's natural variant, known as in CTX;, features a modification of the amino acid from G to E at position 145.
+The protein's natural variant, known as in CTX; impairs sterol 26-hydroxylase activity;, features a modification of the amino acid from R to C at position 395.
+The protein's natural variant, known as in CTX; impairs sterol 26-hydroxylase activity;, features a modification of the amino acid from R to S at position 395.
+The protein's natural variant, known as in CTX; impairs sterol 26-hydroxylase activity;, features a modification of the amino acid from R to Q at position 405.
+The protein's natural variant, known as in CTX; impairs sterol 26-hydroxylase activity;, features a modification of the amino acid from R to Q at position 474.
+The protein's natural variant, known as in CTX; impairs sterol 26-hydroxylase activity;, features a modification of the amino acid from R to W at position 474.
+The protein's natural variant, known as in CTX; impairs sterol 26-hydroxylase activity;, features a modification of the amino acid from R to C at position 479.
+The protein's natural variant, known as in SCAR29; unknown pathological significance; no effect on protein expression, features a modification of the amino acid from E to G at position 13.
+The protein's natural variant, known as disrupts interaction with ARL8B; impairs lysosomal localization and degradation of endocytosed cargo;, features a modification of the amino acid from T to P at position 146.
+The protein's natural variant, known as in SCAR29; decreased protein abundance; cannot form a functional HOPS complex; causes a kinetic defect in the endosome-lysosome fusion process;, features a modification of the amino acid from S to P at position 285.
+The protein's natural variant, known as in SCAR29; unknown pathological significance; decreased protein abundance, features a modification of the amino acid from R to P at position 633.
+The protein's natural variant, known as in SCAR29; decreased protein abundance, features a modification of the amino acid from C to F at position 791.
+The natural variant of this protein is characterized by an amino acid alteration from Y to F at position 72.
+The protein's natural variant, known as in ECA6;, features a modification of the amino acid from F to L at position 161.
+The protein's natural variant, known as in HALD4; changed calcium channel activity; increased aldosterone production in response to potassium ion stimulation; increased expression of genes involved in aldosterone biosynthesis, with the strongest effect observed on CYP11B2 expression in response to potassium ion stimulation;, features a modification of the amino acid from S to L at position 196.
+The protein's natural variant, known as in ECA6;, features a modification of the amino acid from E to K at position 282.
+The protein's natural variant, known as in ECA6; results in increased T-current amplitude and lower threshold for spikes generation; results in increased neuronal excitability, features a modification of the amino acid from C to S at position 456.
+The protein's natural variant, known as in ECA6;, features a modification of the amino acid from G to S at position 499.
+The protein's natural variant, known as found in a patient with drug-resistant focal epilepsy; unknown pathological significance;, features a modification of the amino acid from H to Y at position 516.
+The protein's natural variant, known as in EIG6;, features a modification of the amino acid from P to L at position 618.
+The protein's natural variant, known as in ECA6; creates a dileucine internalization motif that promotes recruitment of clathrin;, features a modification of the amino acid from P to L at position 648.
+The protein's natural variant, known as in ECA6;, features a modification of the amino acid from R to Q at position 744.
+The protein's natural variant, known as in ECA6;, features a modification of the amino acid from A to V at position 748.
+The protein's natural variant, known as in EIG6;, features a modification of the amino acid from G to D at position 755.
+The protein's natural variant, known as in ECA6;, features a modification of the amino acid from G to D at position 773.
+The protein's natural variant, known as in ECA6;, features a modification of the amino acid from G to S at position 784.
+The protein's natural variant, known as in ECA6;, features a modification of the amino acid from V to M at position 831.
+The protein's natural variant, known as in ECA6;, features a modification of the amino acid from G to S at position 848.
+The protein's natural variant, known as in ECA6;, features a modification of the amino acid from D to N at position 1463.
+The protein's natural variant, known as in HALD4; changed calcium channel activity; increased aldosterone production in response to potassium ion stimulation; increased expression of genes involved in aldosterone biosynthesis, with the strongest effect observed on CYP11B2 expression in response to potassium ion stimulation, features a modification of the amino acid from M to I at position 1549.
+The protein's natural variant, known as in HALD4; changed calcium channel activity;, features a modification of the amino acid from M to V at position 1549.
+The protein's natural variant, known as probable disease-associated variant responsible for primary aldosteronism found in a patient with aldosterone-producing adenoma; changed Ca(2+) channel activity;, features a modification of the amino acid from V to E at position 1951.
+The protein's natural variant, known as found in a patient with autism; unknown pathological significance;, features a modification of the amino acid from S to C at position 1970.
+The protein's natural variant, known as in HALD4; changed calcium channel activity;, features a modification of the amino acid from P to L at position 2083.
+The protein's natural variant, known as in inactive enzyme, features a modification of the amino acid from G to W at position 187.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from V to E at position 392.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from V to L at position 392.
+The protein's natural variant, known as in NEDIES; unknown pathological significance; in the neuroblastoma cell line SH-SY5Y, in which NCDN has been knocked out, does not rescue impaired neurite formation following retinoic acid treatment, contrary to wild-type; no effect on phosphorylation of ERK1/ERK2, features a modification of the amino acid from E to Q at position 433.
+The protein's natural variant, known as in NEDIES; in the neuroblastoma cell line SH-SY5Y, in which NCDN has been knocked out, does not rescue impaired neurite formation following retinoic acid treatment, contrary to wild-type; no effect on phosphorylation of ERK1/ERK2, features a modification of the amino acid from R to Q at position 478.
+The protein's natural variant, known as in NEDIES; in the neuroblastoma cell line SH-SY5Y, in which NCDN has been knocked out, does not rescue impaired neurite formation following retinoic acid treatment, contrary to wild-type; in these cells, associated with markedly decreased phosphorylation of ERK1/ERK2, compared to wild-type, suggesting impaired GRM5 activation, features a modification of the amino acid from W to R at position 498.
+The protein's natural variant, known as in NEDIES; in the neuroblastoma cell line SH-SY5Y, in which NCDN has been knocked out, does not rescue impaired neurite formation following retinoic acid treatment, contrary to wild-type; in these cells, associated with markedly decreased phosphorylation of ERK1/ERK2, compared to wild-type, suggesting impaired GRM5 activation, features a modification of the amino acid from P to L at position 652.
+The protein's natural variant, known as in ZTTKS; unknown pathological significance; de novo mutation associated in cis with Y-1843, features a modification of the amino acid from T to S at position 1637.
+The protein's natural variant, known as in ZTTKS; unknown pathological significance; de novo mutation associated in cis with S-1637, features a modification of the amino acid from S to Y at position 1843.
+The protein's natural variant, known as in EDSMC1; associated in a complex allele with Q-137; results in altered intracellular processing;, features a modification of the amino acid from R to G at position 135.
+The protein's natural variant, known as in EDSMC1; associated in a complex allele with G-135; results in altered intracellular processing;, features a modification of the amino acid from L to Q at position 137.
+The protein's natural variant, known as in EDSMC1; results in altered intracellular processing;, features a modification of the amino acid from R to P at position 213.
+The protein's natural variant, known as in EDSMC1; loss of activity;, features a modification of the amino acid from P to L at position 281.
+The protein's natural variant, known as in EDSMC1; loss of activity;, features a modification of the amino acid from C to S at position 289.
+The protein's natural variant, known as in EDSMC1; results in altered intracellular processing; loss of activity;, features a modification of the amino acid from Y to C at position 293.
+The protein's natural variant, known as in sedc mice, features a modification of the amino acid from R to C at position 989.
+The protein's natural variant, known as in HTX2; complete loss of activity; abnormal cell surface localization;, features a modification of the amino acid from R to C at position 112.
+The protein's natural variant, known as found in a patient with lymphoma; inhibits interaction with SKP1;, features a modification of the amino acid from R to H at position 44.
+The protein's natural variant, known as found in a patient with lymphoma;, features a modification of the amino acid from H to N at position 212.
+The protein's natural variant, known as requires 2 nucleotide substitutions; found in a patient with lymphoma; partial loss of function in controlling the stability of BCL2, features a modification of the amino acid from V to C at position 762.
+The protein's natural variant, known as found in a patient with lymphoma; partial loss of function in controlling the stability of BCL2;, features a modification of the amino acid from R to W at position 825.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from V to G at position 385.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from V to I at position 385.
+The protein's natural variant, known as in a melanoma patient, features a modification of the amino acid from E to K at position 969.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from P to Q at position 82.
+The protein's natural variant, known as in MSSGM1; results in loss of activity; does not affect affinity for Gly-tRNA;, features a modification of the amino acid from G to R at position 206.
+The protein's natural variant, known as in strain: JU726, features a modification of the amino acid from V to I at position 62.
+The protein's natural variant, known as found in a renal cell carcinoma sample; somatic mutation, features a modification of the amino acid from G to W at position 441.
+The protein's natural variant, known as in HJDD; due to a nucleotide substitution that affects a canonical splice site; patient cells contain normally spliced transcripts corresponding to protein variant T-355 but also transcripts lacking exon 5 and corresponding to protein variant 271-L--A-355 del;, features a modification of the amino acid from A to T at position 355.
+The protein's natural variant, known as in HJDD; loss of ferroxidase activity;, features a modification of the amino acid from M to T at position 1059.
+The natural variant of this protein is characterized by an amino acid alteration from K to R at position 144.
+The protein's natural variant, known as in strain: IFO 3455, features a modification of the amino acid from D to H at position 127.
+The protein's natural variant, known as in strain: IFO 3455, features a modification of the amino acid from G to A at position 176.
+The protein's natural variant, known as in strain: IFO 3455, features a modification of the amino acid from HPG to T at position 197.
+The protein's natural variant, known as in strain: IFO 3455, features a modification of the amino acid from I to Y at position 350.
+The protein's natural variant, known as in strain: IFO 3455, features a modification of the amino acid from GD to A at position 389.
+The protein's natural variant, known as in strain: IFO 3455, features a modification of the amino acid from AE to SP at position 392.
+The protein's natural variant, known as in strain: IFO 3455, features a modification of the amino acid from SAA to PPR at position 396.
+The protein's natural variant, known as in strain: IFO 3455, features a modification of the amino acid from KAGQA to NAQG at position 439.
+The protein's natural variant, known as in strain: IFO 3455, features a modification of the amino acid from I to V at position 454.
+The protein's natural variant, known as in strain: IFO 3455, features a modification of the amino acid from A to R at position 460.
+The protein's natural variant, known as in strain: IFO 3455, features a modification of the amino acid from V to L at position 479.
+The protein's natural variant, known as in strain: Berkeley, features a modification of the amino acid from G to E at position 165.
+The protein's natural variant, known as in a patient with Noonan syndrome;, features a modification of the amino acid from T to A at position 37.
+The protein's natural variant, known as in NS4;, features a modification of the amino acid from P to R at position 102.
+The protein's natural variant, known as in NS4;, features a modification of the amino acid from E to K at position 108.
+The protein's natural variant, known as in NS4;, features a modification of the amino acid from P to R at position 112.
+The protein's natural variant, known as in NS4;, features a modification of the amino acid from K to E at position 170.
+The protein's natural variant, known as in NS4;, features a modification of the amino acid from I to T at position 252.
+The protein's natural variant, known as in NS4;, features a modification of the amino acid from T to K at position 266.
+The protein's natural variant, known as in NS4;, features a modification of the amino acid from M to R at position 269.
+The protein's natural variant, known as in NS4;, features a modification of the amino acid from M to T at position 269.
+The protein's natural variant, known as in NS4;, features a modification of the amino acid from D to Y at position 309.
+The protein's natural variant, known as in NS4;, features a modification of the amino acid from Y to C at position 337.
+The protein's natural variant, known as in NS4;, features a modification of the amino acid from T to A at position 378.
+The protein's natural variant, known as in NS4, features a modification of the amino acid from M to V at position 422.
+The protein's natural variant, known as in NS4;, features a modification of the amino acid from E to K at position 424.
+The protein's natural variant, known as in NS4, features a modification of the amino acid from KNID to N at position 430.
+The protein's natural variant, known as in NS4;, features a modification of the amino acid from W to R at position 432.
+The protein's natural variant, known as in NS4;, features a modification of the amino acid from E to K at position 433.
+The protein's natural variant, known as in NS4; requires 2 nucleotide substitutions;, features a modification of the amino acid from G to K at position 434.
+The protein's natural variant, known as in NS4;, features a modification of the amino acid from G to R at position 434.
+The protein's natural variant, known as in NS4;, features a modification of the amino acid from I to T at position 437.
+The protein's natural variant, known as in NS4;, features a modification of the amino acid from C to Y at position 441.
+The protein's natural variant, known as in NS4;, features a modification of the amino acid from Q to R at position 477.
+The protein's natural variant, known as found in patients with Noonan syndrome;, features a modification of the amino acid from P to L at position 478.
+The protein's natural variant, known as in NS4;, features a modification of the amino acid from P to R at position 478.
+The protein's natural variant, known as in NS4;, features a modification of the amino acid from G to R at position 482.
+The protein's natural variant, known as in NS4, features a modification of the amino acid from L to R at position 490.
+The protein's natural variant, known as in NS4; one patient with Noonan syndrome also carries a likely pathogenic mutation Ser-261 in RAF1; the mutant protein cannot induce ERK1 phosphorylation;, features a modification of the amino acid from R to Q at position 497.
+The protein's natural variant, known as in NS4;, features a modification of the amino acid from S to R at position 548.
+The protein's natural variant, known as in NS4;, features a modification of the amino acid from T to K at position 549.
+The protein's natural variant, known as in NS4;, features a modification of the amino acid from L to P at position 550.
+The protein's natural variant, known as in NS4; increases the basal level of active RAS; prolonges RAS activation after EGF stimulation and enhances ERK activation;, features a modification of the amino acid from R to G at position 552.
+The protein's natural variant, known as in NS4;, features a modification of the amino acid from R to K at position 552.
+The protein's natural variant, known as in NS4;, features a modification of the amino acid from R to M at position 552.
+The protein's natural variant, known as in NS4;, features a modification of the amino acid from R to S at position 552.
+The protein's natural variant, known as in NS4;, features a modification of the amino acid from R to T at position 552.
+The protein's natural variant, known as in NS4, features a modification of the amino acid from LDVTM to K at position 558.
+The protein's natural variant, known as in NS4;, features a modification of the amino acid from F to I at position 623.
+The protein's natural variant, known as in NS4;, features a modification of the amino acid from Y to H at position 702.
+The protein's natural variant, known as in NS4; promotes constitutive RAS activation and enhances ERK activation, features a modification of the amino acid from W to L at position 729.
+The protein's natural variant, known as in NS4;, features a modification of the amino acid from I to F at position 733.
+The protein's natural variant, known as in a patient with Noonan syndrome;, features a modification of the amino acid from I to T at position 784.
+The protein's natural variant, known as in NS4;, features a modification of the amino acid from E to K at position 846.
+The protein's natural variant, known as in NS4;, features a modification of the amino acid from P to R at position 894.
+The natural variant of this protein is characterized by an amino acid alteration from Q to R at position 977.
+The protein's natural variant, known as in a patient with Noonan syndrome;, features a modification of the amino acid from R to K at position 1131.
+The protein's natural variant, known as in a patient with Noonan syndrome;, features a modification of the amino acid from L to I at position 1140.
+The protein's natural variant, known as in a patient with Noonan syndrome;, features a modification of the amino acid from T to A at position 1257.
+The natural variant of this protein is characterized by an amino acid alteration from H to R at position 1320.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from F to L at position 136.
+The protein's natural variant, known as could be associated with cerebellar ataxia and hypogonadotropic hypogonadism;, features a modification of the amino acid from G to V at position 398.
+The protein's natural variant, known as in LGMDR18; unknown pathological significance, features a modification of the amino acid from Q to P at position 284.
+The protein's natural variant, known as found in a patient with congenital disorder of glycosylation; unknown pathological significance, features a modification of the amino acid from P to A at position 381.
+The protein's natural variant, known as in LGMDR18;, features a modification of the amino acid from G to R at position 980.
+The protein's natural variant, known as found in a patient with congenital disorder of glycosylation; unknown pathological significance;, features a modification of the amino acid from T to A at position 1104.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from P to R at position 226.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from T to P at position 1316.
+The protein's natural variant, known as in a chronic myelomonocytic leukemia sample; somatic mutation;, features a modification of the amino acid from S to N at position 145.
+The protein's natural variant, known as in chronic myelomonocytic leukemia and acute myeloid leukemia samples;, features a modification of the amino acid from A to T at position 308.
+The protein's natural variant, known as in an acute myeloid leukemia sample; somatic mutation, features a modification of the amino acid from N to S at position 312.
+The protein's natural variant, known as in myelodysplastic/myeloproliferative disorders; a patient positive for mutation F-617 in JAK2, features a modification of the amino acid from P to L at position 399.
+The protein's natural variant, known as in a chronic myelomonocytic leukemia sample; somatic mutation;, features a modification of the amino acid from S to F at position 460.
+The protein's natural variant, known as in a chronic myelomonocytic leukemia sample; somatic mutation, features a modification of the amino acid from D to G at position 666.
+The protein's natural variant, known as in myelodysplastic/myeloproliferative disorders;, features a modification of the amino acid from S to T at position 817.
+The protein's natural variant, known as in a chronic myelomonocytic leukemia sample; somatic mutation;, features a modification of the amino acid from P to S at position 941.
+The natural variant of this protein is characterized by an amino acid alteration from E to V at position 1073.
+The protein's natural variant, known as in a myeloproliferative disorder; somatic mutation;, features a modification of the amino acid from C to Y at position 1135.
+The protein's natural variant, known as in a myelodysplatic/myeloproliferative disorder and a chronic myelomonocytic leukemia sample, features a modification of the amino acid from R to T at position 1167.
+The protein's natural variant, known as in a refractory anemia with ringed sideroblasts sample, features a modification of the amino acid from I to V at position 1175.
+The protein's natural variant, known as in a myeloproliferative disorder; somatic mutation, features a modification of the amino acid from S to C at position 1204.
+The protein's natural variant, known as in a myelodysplastic syndrome; somatic mutation in a chronic myelomonocytic leukemia sample;, features a modification of the amino acid from R to W at position 1214.
+The protein's natural variant, known as requires 2 nucleotide substitutions, features a modification of the amino acid from D to R at position 1242.
+The protein's natural variant, known as in myeloproliferative disorders, features a modification of the amino acid from D to V at position 1242.
+The protein's natural variant, known as in a myeloproliferative disorder; somatic mutation, features a modification of the amino acid from Y to S at position 1245.
+The protein's natural variant, known as in a myeloproliferative disorder; somatic mutation;, features a modification of the amino acid from R to C at position 1261.
+The protein's natural variant, known as in a chronic myelomonocytic leukemia sample; somatic mutation;, features a modification of the amino acid from R to H at position 1261.
+The protein's natural variant, known as in a myelodysplastic syndrome, features a modification of the amino acid from R to L at position 1261.
+The protein's natural variant, known as in myelodysplastic/myeloproliferative disorders; no effect on interaction with DCAF1, monoubiquitination, nor on 5-methylcytosine demethylase activity in vivo, when tested in a heterologous system, features a modification of the amino acid from F to L at position 1287.
+The protein's natural variant, known as in a myelodysplastic syndrome; somatic mutation; loss of 5-methylcytosine demethylase activity in vivo; no effect on interaction with DCAF1, nor on monoubiquitination, when tested in a heterologous system, features a modification of the amino acid from W to R at position 1291.
+The protein's natural variant, known as in a refractory anemia sample; loss of monoubiquitination, chromatin binding and 5-methylcytosine demethylase activity in vivo, when tested in a heterologous system, features a modification of the amino acid from K to E at position 1299.
+The protein's natural variant, known as in chronic myelomonocytic leukemia samples; loss of monoubiquitination, chromatin binding and 5-methylcytosine demethylase activity in vivo, when tested in a heterologous system, features a modification of the amino acid from K to N at position 1299.
+The protein's natural variant, known as in primary myelofibrosis and chronic myelomonocytic leukemia samples; loss of interaction with DCAF1, monoubiquitination and of 5-methylcytosine demethylase activity in vivo, when tested in a heterologous system, features a modification of the amino acid from R to G at position 1302.
+The protein's natural variant, known as in chronic myelomonocytic leukemia samples; no effect on interaction with DCAF1, monoubiquitination, nor on 5-methylcytosine demethylase activity in vivo, when tested in a heterologous system, features a modification of the amino acid from E to G at position 1318.
+The protein's natural variant, known as in a chronic myelomonocytic leukemia sample, features a modification of the amino acid from P to S at position 1367.
+The protein's natural variant, known as in IMD75; loss of methylcytosine dioxygenase activity, features a modification of the amino acid from H to R at position 1382.
+The protein's natural variant, known as in a myelodysplastic syndrome, features a modification of the amino acid from C to W at position 1396.
+The protein's natural variant, known as in a myelodysplastic syndrome; somatic mutation, features a modification of the amino acid from L to R at position 1398.
+The protein's natural variant, known as in a chronic myelomonocytic leukemia sample; somatic mutation;, features a modification of the amino acid from V to F at position 1417.
+The protein's natural variant, known as in refractory anemia with ringed sideroblasts; somatic mutation in an acute myeloid leukemia sample;, features a modification of the amino acid from V to L at position 1718.
+The protein's natural variant, known as in a chronic myelomonocytic leukemia sample; somatic mutation, features a modification of the amino acid from H to D at position 1757.
+The protein's natural variant, known as in a chronic myelomonocytic leukemia sample; somatic mutation, features a modification of the amino acid from C to R at position 1811.
+The protein's natural variant, known as in a myeloproliferative disorder; somatic mutation, features a modification of the amino acid from Q to L at position 1828.
+The protein's natural variant, known as in an essential thrombocythemia sample;, features a modification of the amino acid from G to W at position 1869.
+The protein's natural variant, known as in a refractory anemia with excess blasts sample, features a modification of the amino acid from L to P at position 1872.
+The protein's natural variant, known as in myelodysplastic syndromes, myeloproliferative disorders and chronic myelomonocytic leukemia; somatic mutation in acute myeloid leukemia and chronic myelomonocytic leukemia samples;, features a modification of the amino acid from I to T at position 1873.
+The protein's natural variant, known as in a myelodysplastic syndrome; somatic mutation, features a modification of the amino acid from C to R at position 1875.
+The protein's natural variant, known as in a myelodysplastic syndrome; somatic mutation, features a modification of the amino acid from H to Q at position 1881.
+The protein's natural variant, known as in a myeloproliferative disorder; somatic mutation; also in a patient with systemic mastocytosis associated with chronic myelomonocytic leukemia;, features a modification of the amino acid from H to R at position 1881.
+The protein's natural variant, known as in a primary acute myeloid leukemia sample; somatic mutation; reduces enzyme activity, features a modification of the amino acid from R to M at position 1896.
+The protein's natural variant, known as in a myeloproliferative disorder; somatic mutation, features a modification of the amino acid from R to S at position 1896.
+The protein's natural variant, known as in a secondary acute myeloid leukemia sample; somatic mutation; loss of enzyme activity;, features a modification of the amino acid from S to F at position 1898.
+The natural variant of this protein is characterized by an amino acid alteration from V to A at position 1900.
+The protein's natural variant, known as in myelodysplastic syndromes; refractory cytopenia with multilineage dysplasia and ringed sideroblasts; somatic mutation in a patient, features a modification of the amino acid from G to D at position 1913.
+The protein's natural variant, known as in a myeloproliferative disorder; somatic mutation;, features a modification of the amino acid from A to V at position 1919.
+The protein's natural variant, known as in a chronic myelomonocytic leukemia sample; somatic mutation;, features a modification of the amino acid from R to H at position 1926.
+The protein's natural variant, known as in a chronic myelomonocytic leukemia sample; somatic mutation;, features a modification of the amino acid from P to S at position 1941.
+The protein's natural variant, known as in a myelodysplastic syndrome;, features a modification of the amino acid from P to L at position 1962.
+The protein's natural variant, known as in a chronic myelomonocytic leukemia sample; somatic mutation;, features a modification of the amino acid from R to H at position 1966.
+The protein's natural variant, known as in a chronic myelomonocytic leukemia sample; somatic mutation;, features a modification of the amino acid from R to M at position 1974.
+The natural variant of this protein is characterized by an amino acid alteration from R to K at position 2000.
+The protein's natural variant, known as in strain: HV109/R; optochin-resistant, features a modification of the amino acid from W to S at position 206.
+The protein's natural variant, known as in temperature-sensitive mutants parE206 and parE374, features a modification of the amino acid from V to M at position 67.
+The protein's natural variant, known as in temperature-sensitive mutant parE377, features a modification of the amino acid from G to S at position 399.
+The protein's natural variant, known as in temperature-sensitive mutant parE493, features a modification of the amino acid from T to P at position 583.
+The protein's natural variant, known as in strain: Isolate LHS 541, features a modification of the amino acid from V to A at position 232.
+The protein's natural variant, known as in strain: Isolate LHS 541, features a modification of the amino acid from I to T at position 348.
+The protein's natural variant, known as in strain: Isolate LHS 541, features a modification of the amino acid from V to I at position 363.
+The protein's natural variant, known as in strain: Isolate LHS 541, features a modification of the amino acid from M to I at position 368.
+The protein's natural variant, known as in strain: 689426 and LO4035, features a modification of the amino acid from E to D at position 63.
+The protein's natural variant, known as in strain: 689426 and LO4035, features a modification of the amino acid from D to E at position 102.
+The protein's natural variant, known as in DSD;, features a modification of the amino acid from P to L at position 370.
+The protein's natural variant, known as in RTSC3; does not interact with VPS29;, features a modification of the amino acid from A to T at position 830.
+The protein's natural variant, known as in strain: Isolate PK 4847, features a modification of the amino acid from M to V at position 108.
+The protein's natural variant, known as in strain: Isolate PK 4847, features a modification of the amino acid from I to V at position 238.
+The protein's natural variant, known as in strain: Berkeley, M2, M26, M36, M40, M55 and SFS 3.4, features a modification of the amino acid from S to A at position 19.
+The protein's natural variant, known as in strain: SFS 3.4, features a modification of the amino acid from N to I at position 46.
+The protein's natural variant, known as in IGS2; reduced presence at the cell membrane; loss of interaction with CUBN; reduced CUBN expression at the cell surface;, features a modification of the amino acid from T to I at position 41.
+The protein's natural variant, known as in IGS2; loss of interaction with CUBN; strongly reduced CUBN expression at the cell surface;, features a modification of the amino acid from M to K at position 69.
+The protein's natural variant, known as in IGS2; loss of interaction with CUBN; strongly reduced CUBN expression at the cell surface;, features a modification of the amino acid from C to F at position 234.
+The protein's natural variant, known as in strain: B, features a modification of the amino acid from L to V at position 8.
+The protein's natural variant, known as in clone 1, features a modification of the amino acid from M to V at position 93.
+The protein's natural variant, known as in clone 11, features a modification of the amino acid from I to A at position 105.
+The protein's natural variant, known as in clone 11, features a modification of the amino acid from I to V at position 128.
+The protein's natural variant, known as in clone 11, features a modification of the amino acid from G to A at position 142.
+The protein's natural variant, known as in strain: 297, LP7 and Sh-2-82, features a modification of the amino acid from R to K at position 34.
+The protein's natural variant, known as in strain: 297, LP7 and Sh-2-82, features a modification of the amino acid from R to S at position 37.
+The protein's natural variant, known as in strain: 297, LP7 and Sh-2-82, features a modification of the amino acid from DIT to AIV at position 43.
+The protein's natural variant, known as in strain: 297, LP7 and Sh-2-82, features a modification of the amino acid from D to K at position 52.
+The protein's natural variant, known as in strain: 297, LP7 and Sh-2-82, features a modification of the amino acid from LK to SM at position 56.
+The protein's natural variant, known as in strain: 297, LP7 and Sh-2-82, features a modification of the amino acid from K to E at position 128.
+The protein's natural variant, known as in strain: 297, LP7 and Sh-2-82, features a modification of the amino acid from D to M at position 140.
+The protein's natural variant, known as in strain: 297, LP7 and Sh-2-82, features a modification of the amino acid from T to K at position 169.
+The protein's natural variant, known as in strain: 297, LP7 and Sh-2-82, features a modification of the amino acid from YC to QD at position 173.
+The protein's natural variant, known as in strain: 297, LP7 and Sh-2-82, features a modification of the amino acid from ENSTFTDEKCKNN to NTEDSTAKS at position 191.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from G to A at position 270.
+The protein's natural variant, known as in LQT3;, features a modification of the amino acid from G to V at position 9.
+The protein's natural variant, known as in BRGDA1 and LQT3; unknown pathological significance;, features a modification of the amino acid from R to Q at position 18.
+The protein's natural variant, known as rare variant; found in a patient with long QT syndrome; unknown pathological significance;, features a modification of the amino acid from R to W at position 18.
+The protein's natural variant, known as in BRGDA1 and LQT3;, features a modification of the amino acid from R to H at position 27.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from E to G at position 30.
+The protein's natural variant, known as in LQT3; does not affect baseline kinetics of sodium currents; causes an unusual hyperpolarizing shift of the activation kinetics after lidocaine treatment;, features a modification of the amino acid from R to Q at position 43.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from E to K at position 48.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from P to S at position 52.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from R to Q at position 53.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from N to K at position 70.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from D to N at position 84.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from F to S at position 93.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from I to S at position 94.
+The protein's natural variant, known as in BRGDA1;, features a modification of the amino acid from V to I at position 95.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from R to G at position 104.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from R to Q at position 104.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from R to W at position 104.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from N to K at position 109.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from S to G at position 115.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from R to Q at position 121.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from R to W at position 121.
+The protein's natural variant, known as in LQT3;, features a modification of the amino acid from V to L at position 125.
+The protein's natural variant, known as in BRGDA1;, features a modification of the amino acid from K to E at position 126.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from L to P at position 136.
+The protein's natural variant, known as in ATFB10;, features a modification of the amino acid from M to I at position 138.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from V to M at position 146.
+The protein's natural variant, known as in BRGDA1 and PFHB1A;, features a modification of the amino acid from E to K at position 161.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from E to Q at position 161.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from K to N at position 175.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from A to G at position 178.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from C to R at position 182.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from A to V at position 185.
+The protein's natural variant, known as in BRGDA1; loss of function;, features a modification of the amino acid from T to I at position 187.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from A to V at position 204.
+The protein's natural variant, known as in LQT3;, features a modification of the amino acid from L to P at position 212.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from L to Q at position 212.
+The protein's natural variant, known as rare variant found in patients with atrial fibrillation; unknown pathological significance;, features a modification of the amino acid from S to L at position 216.
+The protein's natural variant, known as in SSS1 and BRGDA1;, features a modification of the amino acid from T to I at position 220.
+The protein's natural variant, known as in BRGDA1 and LQT3;, features a modification of the amino acid from R to Q at position 222.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from V to L at position 223.
+The protein's natural variant, known as in LQT3;, features a modification of the amino acid from R to Q at position 225.
+The protein's natural variant, known as in PFHB1A, BRGDA1 and LQT3;, features a modification of the amino acid from R to W at position 225.
+The protein's natural variant, known as in BRGDA1;, features a modification of the amino acid from A to V at position 226.
+The protein's natural variant, known as in BRGDA1;, features a modification of the amino acid from I to V at position 230.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from V to I at position 232.
+The protein's natural variant, known as in BRGDA1 and LQT3;, features a modification of the amino acid from V to M at position 240.
+The protein's natural variant, known as in LQT3;, features a modification of the amino acid from Q to K at position 245.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from V to L at position 247.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from Q to K at position 270.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from N to K at position 275.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from L to Q at position 276.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from H to D at position 278.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from R to C at position 282.
+The protein's natural variant, known as in BRGDA1;, features a modification of the amino acid from R to H at position 282.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from G to S at position 289.
+The protein's natural variant, known as in BRGDA1;, features a modification of the amino acid from V to M at position 294.
+The protein's natural variant, known as in PFHB1A; also in irritable bowel syndrome; results in reduction of whole cell current density and a delay in channel activation kinetics without a change in single-channel conductance;, features a modification of the amino acid from G to S at position 298.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from V to I at position 300.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from L to P at position 315.
+The protein's natural variant, known as in BRGDA1;, features a modification of the amino acid from G to S at position 319.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from T to N at position 320.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from L to R at position 325.
+The protein's natural variant, known as in BRGDA1; severe reduction of sodium currents;, features a modification of the amino acid from P to L at position 336.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from R to W at position 340.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from G to D at position 351.
+The protein's natural variant, known as in BRGDA1; 7-fold current reduction;, features a modification of the amino acid from G to V at position 351.
+The protein's natural variant, known as in BRGDA1;, features a modification of the amino acid from T to I at position 353.
+The protein's natural variant, known as in BRGDA1; loss of function;, features a modification of the amino acid from D to N at position 356.
+The protein's natural variant, known as in BRGDA1 and LQT3; express no current;, features a modification of the amino acid from R to C at position 367.
+The protein's natural variant, known as in BRGDA1; express no current;, features a modification of the amino acid from R to H at position 367.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from R to L at position 367.
+The protein's natural variant, known as in BRGDA1;, features a modification of the amino acid from M to K at position 369.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from T to M at position 370.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from W to G at position 374.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance; also found in patients with atrial fibrillation;, features a modification of the amino acid from R to H at position 376.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from G to E at position 386.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from G to R at position 386.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from V to A at position 396.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from V to L at position 396.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from I to T at position 397.
+The protein's natural variant, known as in LQT3;, features a modification of the amino acid from L to Q at position 404.
+The protein's natural variant, known as in LQT3;, features a modification of the amino acid from N to K at position 406.
+The protein's natural variant, known as in BRGDA1;, features a modification of the amino acid from N to S at position 406.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from L to V at position 409.
+The protein's natural variant, known as in LQT3;, features a modification of the amino acid from V to M at position 411.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from A to E at position 413.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from A to T at position 413.
+The protein's natural variant, known as in ATFB10;, features a modification of the amino acid from E to K at position 428.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from E to K at position 439.
+The protein's natural variant, known as in ATFB10;, features a modification of the amino acid from H to D at position 445.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from E to A at position 462.
+The protein's natural variant, known as in LQT3;, features a modification of the amino acid from E to K at position 462.
+The protein's natural variant, known as in ATFB10;, features a modification of the amino acid from N to K at position 470.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from D to G at position 501.
+The protein's natural variant, known as in PFHB1A; voltage-dependent activation and inactivation of the I-512 channel is shifted negatively by 8 to 9 mV and had enhanced slow activation and slower recovery from inactivation commpared to the wild-type channel; the double mutant R-558/I-512 channel shows that R-558 eliminates the negative shift induced by I-512 but only partially restores the kinetic abnormalities;, features a modification of the amino acid from T to I at position 512.
+The protein's natural variant, known as in BRGDA1 and PFHB1A;, features a modification of the amino acid from G to C at position 514.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from R to H at position 526.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from F to V at position 530.
+The protein's natural variant, known as in SIDS and BRGDA1;, features a modification of the amino acid from F to C at position 532.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from R to Q at position 535.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from F to L at position 543.
+The protein's natural variant, known as in BRGDA1;, features a modification of the amino acid from G to R at position 552.
+The protein's natural variant, known as channels properties are similar to wild-type; the double mutant R-558/I-512 channel shows that R-558 eliminates the negative shift induced by Ile-512 but only partially restores the kinetic abnormalities; can modulate the gating defects caused by Ala-2006 and other mutations;, features a modification of the amino acid from H to R at position 558.
+The protein's natural variant, known as in BRGDA1;, features a modification of the amino acid from L to Q at position 567.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from R to W at position 569.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from S to I at position 571.
+The protein's natural variant, known as in LQT3 and ATFB10; likely benign variant;, features a modification of the amino acid from A to D at position 572.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from A to S at position 572.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from A to V at position 572.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from Q to E at position 573.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from G to R at position 579.
+The protein's natural variant, known as in LQT3 and BRGDA1; drug-induced LQT syndrome;, features a modification of the amino acid from G to E at position 615.
+The protein's natural variant, known as in LQT3 and BRGDA1;, features a modification of the amino acid from L to F at position 619.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from R to C at position 620.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from T to M at position 632.
+The protein's natural variant, known as in LQT3;, features a modification of the amino acid from P to L at position 637.
+The protein's natural variant, known as in LQT3;, features a modification of the amino acid from G to R at position 639.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from P to A at position 640.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from A to D at position 647.
+The protein's natural variant, known as in LQT3 and BRGDA1;, features a modification of the amino acid from P to L at position 648.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from E to K at position 654.
+The protein's natural variant, known as in ATFB10;, features a modification of the amino acid from E to K at position 655.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from R to W at position 661.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from L to P at position 673.
+The protein's natural variant, known as in LQT3;, features a modification of the amino acid from R to H at position 680.
+The protein's natural variant, known as in BRGDA1;, features a modification of the amino acid from H to P at position 681.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from C to G at position 683.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from R to C at position 689.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from R to H at position 689.
+The protein's natural variant, known as in BRGDA1 and LQT3;, features a modification of the amino acid from P to L at position 701.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from P to L at position 717.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from T to I at position 731.
+The protein's natural variant, known as in BRGDA1;, features a modification of the amino acid from A to E at position 735.
+The protein's natural variant, known as in BRGDA1 and SSS1; expresses currents with steady state activation voltage shifted to more positive potentials and exhibit reduced sodium channel current at the end of phase I of the action potential;, features a modification of the amino acid from A to V at position 735.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from E to K at position 746.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from Q to R at position 750.
+The protein's natural variant, known as in BRGDA1 and PFHB1A;, features a modification of the amino acid from G to R at position 752.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from G to E at position 758.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from M to R at position 764.
+The protein's natural variant, known as in BRGDA1 and LQT3;, features a modification of the amino acid from D to N at position 772.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from P to S at position 773.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from V to I at position 789.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from R to P at position 808.
+The protein's natural variant, known as in BRGDA1; decreased protein abundance; retained intracellularly; decreased voltage-gated sodium channel activity; hyperpolarizing shift of the voltage dependence of inactivation leading to reduced sodium window current; no dominant negative effect, features a modification of the amino acid from L to Q at position 812.
+The protein's natural variant, known as in BRGDA1;, features a modification of the amino acid from R to Q at position 814.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from F to Y at position 816.
+The protein's natural variant, known as in BRGDA1; no effect on localization to the plasma membrane; decreased voltage-gated sodium channel activity; shift in the voltage dependence of activation and changed recovery from inactivation, features a modification of the amino acid from K to E at position 817.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from L to P at position 839.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from I to F at position 848.
+The protein's natural variant, known as in BRGDA1;, features a modification of the amino acid from F to L at position 851.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from E to Q at position 867.
+The protein's natural variant, known as in BRGDA1;, features a modification of the amino acid from R to C at position 878.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from R to H at position 878.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from H to P at position 886.
+The protein's natural variant, known as in BRGDA1;, features a modification of the amino acid from F to I at position 892.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from R to C at position 893.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from R to H at position 893.
+The protein's natural variant, known as in BRGDA1;, features a modification of the amino acid from C to S at position 896.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from E to K at position 901.
+The protein's natural variant, known as in BRGDA1;, features a modification of the amino acid from S to L at position 910.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from C to R at position 915.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from L to R at position 917.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from N to S at position 927.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from L to P at position 928.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from L to P at position 935.
+The protein's natural variant, known as in LQT3; also in SIDS;, features a modification of the amino acid from S to N at position 941.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from Q to K at position 960.
+The protein's natural variant, known as in BRGDA1; steady state inactivation shifted to a more negative potential; slower recovery from inactivation;, features a modification of the amino acid from R to C at position 965.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from R to H at position 965.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from R to L at position 965.
+The protein's natural variant, known as in LQT3;, features a modification of the amino acid from R to C at position 971.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from C to F at position 981.
+The protein's natural variant, known as in LQT3; also found in patients with atrial fibrillation; sodium current characterized by slower decay and a 2- to 3-fold increase in late sodium current;, features a modification of the amino acid from A to S at position 997.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from A to T at position 997.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from C to R at position 1004.
+The protein's natural variant, known as in BRGDA1;, features a modification of the amino acid from R to H at position 1023.
+The protein's natural variant, known as in BRGDA1, ATFB10 and LQT3; abolishes binding to ANK3 and also prevents accumulation of SCN5A at cell surface sites in ventricular cardiomyocytes;, features a modification of the amino acid from E to K at position 1053.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from D to G at position 1055.
+The protein's natural variant, known as in LQT3;, features a modification of the amino acid from T to M at position 1069.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from S to Y at position 1079.
+The protein's natural variant, known as in SIDS; unknown pathological significance;, features a modification of the amino acid from G to S at position 1084.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from A to V at position 1100.
+The protein's natural variant, known as may confer susceptibility to acquired arrhythmia;, features a modification of the amino acid from S to Y at position 1103.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from A to V at position 1113.
+The protein's natural variant, known as in LQT3;, features a modification of the amino acid from D to N at position 1114.
+The protein's natural variant, known as in ATFB10;, features a modification of the amino acid from T to I at position 1131.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from S to T at position 1140.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from D to N at position 1166.
+The protein's natural variant, known as in BRGDA1 and LQT3; also found in patients with atrial fibrillation; accelerates the inactivation of the sodium channel current and exhibit reduced sodium channel current at the end of phase I of the action potential;, features a modification of the amino acid from R to Q at position 1193.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from Y to S at position 1199.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from S to N at position 1219.
+The protein's natural variant, known as in BRGDA1 and LQT3;, features a modification of the amino acid from E to K at position 1225.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from Y to H at position 1228.
+The protein's natural variant, known as in LQT3;, features a modification of the amino acid from E to K at position 1231.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from R to Q at position 1232.
+The protein's natural variant, known as in BRGDA1 and PFHB1A;, features a modification of the amino acid from R to W at position 1232.
+The protein's natural variant, known as in BRGDA1;, features a modification of the amino acid from K to N at position 1236.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from L to P at position 1239.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from D to N at position 1243.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from V to D at position 1249.
+The protein's natural variant, known as in LQT3; drug-induced LQT syndrome;, features a modification of the amino acid from F to L at position 1250.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from E to G at position 1253.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from G to S at position 1262.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from W to C at position 1271.
+The protein's natural variant, known as in CMD1E, BRGDA1, PFHB1A and ATRST1; in familial atrial standstill is found in association with variants in the regulatory region of GJA5; decreases expression at the cell membrane; alters channel kinetics; shifts activation and inactivation to more positive membrane potentials;, features a modification of the amino acid from D to N at position 1275.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from L to M at position 1283.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from A to G at position 1288.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from F to S at position 1293.
+The protein's natural variant, known as in LQT3; causes significant positive shifts in the half-maximal voltage of steady-state inactivation and activation;, features a modification of the amino acid from E to K at position 1295.
+The protein's natural variant, known as in SSS1;, features a modification of the amino acid from P to L at position 1298.
+The protein's natural variant, known as in LQT3;, features a modification of the amino acid from T to M at position 1304.
+The protein's natural variant, known as associated with I-232 in a case of lidocaine-induced Brugada syndrome;, features a modification of the amino acid from L to F at position 1308.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from L to P at position 1311.
+The protein's natural variant, known as in BRGDA1;, features a modification of the amino acid from G to V at position 1319.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from V to G at position 1323.
+The protein's natural variant, known as in LQT3;, features a modification of the amino acid from N to S at position 1325.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from A to S at position 1326.
+The protein's natural variant, known as in LQT3;, features a modification of the amino acid from A to P at position 1330.
+The protein's natural variant, known as in LQT3;, features a modification of the amino acid from A to T at position 1330.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from P to L at position 1332.
+The protein's natural variant, known as in LQT3 and SIDS;, features a modification of the amino acid from S to Y at position 1333.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from I to V at position 1334.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from L to V at position 1338.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from F to L at position 1344.
+The protein's natural variant, known as in BRGDA1;, features a modification of the amino acid from F to S at position 1344.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from L to I at position 1346.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from L to P at position 1346.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from M to R at position 1351.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from V to M at position 1353.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from G to W at position 1358.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from K to N at position 1359.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from F to C at position 1360.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from C to Y at position 1363.
+The protein's natural variant, known as in BRGDA1;, features a modification of the amino acid from S to I at position 1382.
+The protein's natural variant, known as in BRGDA1;, features a modification of the amino acid from V to L at position 1405.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from V to M at position 1405.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from G to E at position 1406.
+The protein's natural variant, known as in BRGDA1;, features a modification of the amino acid from G to R at position 1406.
+The protein's natural variant, known as in SSS1 and BRGDA1;, features a modification of the amino acid from G to R at position 1408.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from Y to C at position 1409.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from L to F at position 1412.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from K to E at position 1419.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from G to R at position 1420.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from A to S at position 1427.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from A to V at position 1428.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from R to G at position 1432.
+The protein's natural variant, known as in BRGDA1 and LQT3;, features a modification of the amino acid from R to S at position 1432.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from G to V at position 1433.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from P to L at position 1438.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from E to Q at position 1441.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from I to L at position 1448.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from I to T at position 1448.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from Y to C at position 1449.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from V to D at position 1451.
+The protein's natural variant, known as in LQT3;, features a modification of the amino acid from S to Y at position 1458.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from N to Y at position 1463.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from V to F at position 1468.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from N to S at position 1472.
+The protein's natural variant, known as in LQT3;, features a modification of the amino acid from F to C at position 1473.
+The protein's natural variant, known as in LQT3;, features a modification of the amino acid from G to E at position 1481.
+The protein's natural variant, known as in LQT3;, features a modification of the amino acid from F to L at position 1486.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from M to L at position 1487.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from T to R at position 1488.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from E to D at position 1489.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from K to R at position 1493.
+The protein's natural variant, known as in BRGDA1;, features a modification of the amino acid from Y to N at position 1494.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from Y to S at position 1495.
+The protein's natural variant, known as found in a patient with long QT syndrome; unknown pathological significance;, features a modification of the amino acid from M to T at position 1498.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from M to V at position 1498.
+The protein's natural variant, known as in LQT3 and BRGDA1;, features a modification of the amino acid from L to V at position 1501.
+The protein's natural variant, known as in BRGDA1;, features a modification of the amino acid from G to S at position 1502.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from K to N at position 1505.
+The protein's natural variant, known as in BRGDA1; significantly affects cardiac sodium channel characteristics; associated with an increase in inward sodium current during the action potential upstroke;, features a modification of the amino acid from R to W at position 1512.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from I to K at position 1521.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from V to M at position 1525.
+The protein's natural variant, known as in BRGDA1; asymptomatic patient; associated with P-1569;, features a modification of the amino acid from K to R at position 1527.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from V to I at position 1532.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from E to K at position 1548.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from L to F at position 1560.
+The protein's natural variant, known as in BRGDA1; asymptomatic patient; associated with R-1527;, features a modification of the amino acid from A to P at position 1569.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from F to C at position 1571.
+The protein's natural variant, known as in BRGDA1; affects channel activity; the mutant displays a hyperpolarizing shift in the voltage dependence of inactivation causing slower inactivation compared to the wild type, slower recovery and a reduced availability of channels at rest;, features a modification of the amino acid from F to L at position 1571.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from E to K at position 1574.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from L to P at position 1582.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from R to C at position 1583.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from R to H at position 1583.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from I to M at position 1593.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from F to S at position 1594.
+The protein's natural variant, known as in PFHB1A; significant defect in the kinetics of fast-channel inactivation distinct from mutations reported in LQT3;, features a modification of the amino acid from D to N at position 1595.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from F to I at position 1596.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from V to M at position 1604.
+The protein's natural variant, known as in LQT3;, features a modification of the amino acid from S to W at position 1609.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from Q to L at position 1613.
+The protein's natural variant, known as in LQT3 and PFHB1A;, features a modification of the amino acid from T to K at position 1620.
+The protein's natural variant, known as in BRGDA1; arrhythmogenicity revealed only at temperatures approaching the physiologic range;, features a modification of the amino acid from T to M at position 1620.
+The protein's natural variant, known as in LQT3;, features a modification of the amino acid from R to L at position 1623.
+The protein's natural variant, known as in LQT3 and BRGDA1;, features a modification of the amino acid from R to Q at position 1623.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from R to H at position 1626.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from R to P at position 1626.
+The protein's natural variant, known as in BRGDA1; changed voltage-gated sodium channel activity; no difference in current density but changed inactivation kinetics and prolonged recovery from inactivation;, features a modification of the amino acid from R to Q at position 1629.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from G to E at position 1642.
+The protein's natural variant, known as in LQT3;, features a modification of the amino acid from R to C at position 1644.
+The protein's natural variant, known as in LQT3;, features a modification of the amino acid from R to H at position 1644.
+The protein's natural variant, known as in LQT3;, features a modification of the amino acid from T to M at position 1645.
+The protein's natural variant, known as in BRGDA1;, features a modification of the amino acid from A to V at position 1649.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from L to F at position 1650.
+The protein's natural variant, known as in LQT3;, features a modification of the amino acid from M to R at position 1652.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from M to T at position 1652.
+The protein's natural variant, known as in BRGDA1 and LQT3; complete loss of sodium currents due to defective channel trafficking to the plasma membrane;, features a modification of the amino acid from I to V at position 1660.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from G to R at position 1661.
+The protein's natural variant, known as in LQT3 and BRGDA1;, features a modification of the amino acid from V to I at position 1667.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from S to Y at position 1672.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from A to T at position 1680.
+The protein's natural variant, known as in BRGDA1; decreased localization to the plasma membrane; decreased voltage-gated sodium channel activity; dominant negative effect; no effect on voltage dependence for activation and inactivation;, features a modification of the amino acid from D to N at position 1690.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from A to T at position 1698.
+The protein's natural variant, known as in SIDS; causes a hyperpolarizing shift of steady-state inactivation and delayed recovery from inactivation;, features a modification of the amino acid from F to S at position 1705.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from T to M at position 1709.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from T to R at position 1709.
+The protein's natural variant, known as in VF1;, features a modification of the amino acid from S to L at position 1710.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from G to S at position 1712.
+The protein's natural variant, known as in BRGDA1; strong decrease of current density; does not affect ion selectivity properties;, features a modification of the amino acid from D to G at position 1714.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from N to D at position 1722.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from T to N at position 1723.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from C to R at position 1728.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from C to W at position 1728.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from R to W at position 1739.
+The protein's natural variant, known as in BRGDA1;, features a modification of the amino acid from G to R at position 1740.
+The protein's natural variant, known as in BRGDA1;, features a modification of the amino acid from G to E at position 1743.
+The protein's natural variant, known as in BRGDA1; decreases expression at the cell membrane; yields nearly undetectable currents in transfected cells;, features a modification of the amino acid from G to R at position 1743.
+The protein's natural variant, known as in BRGDA1; decreased localization to the plasma membrane; decreased voltage-gated sodium channel activity; dominant negative effect; changed voltage dependence for activation and inactivation, features a modification of the amino acid from G to D at position 1748.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from L to F at position 1761.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from L to H at position 1761.
+The protein's natural variant, known as in LQT3;, features a modification of the amino acid from V to M at position 1763.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from V to F at position 1764.
+The protein's natural variant, known as in LQT3; affects protein trafficking;, features a modification of the amino acid from M to L at position 1766.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from Y to C at position 1767.
+The protein's natural variant, known as in LQT3; increases the rate of recovery from inactivation and the channel availability, observed as a positive shift of the steady-state inactivation curve;, features a modification of the amino acid from I to V at position 1768.
+The protein's natural variant, known as in LQT3;, features a modification of the amino acid from V to M at position 1777.
+The protein's natural variant, known as in LQT3 and BRGDA1;, features a modification of the amino acid from T to M at position 1779.
+The protein's natural variant, known as in LQT3 and BRGDA1;, features a modification of the amino acid from E to K at position 1784.
+The protein's natural variant, known as in LQT3;, features a modification of the amino acid from D to G at position 1790.
+The protein's natural variant, known as in SSS1;, features a modification of the amino acid from D to N at position 1792.
+The protein's natural variant, known as in LQT3; also in a family associating LQT syndrome and atrial fibrillation; slows the onset of activation, but does not cause a marked negative shift in the voltage dependence of inactivation or affect the kinetics of the recovery from inactivation; increases the expression of sustained Na(+) channel activity and promotes entrance into an intermediate or slowly developing inactivated state;, features a modification of the amino acid from Y to C at position 1795.
+The protein's natural variant, known as in BRGDA1; accelerates the onset of activation and causes a marked negative shift in the voltage dependence of inactivation; does not affect the kinetics of the recovery from inactivation; increases the expression of sustained Na(+) channel activity and promotes entrance into an intermediate or slowly developing inactivated state;, features a modification of the amino acid from Y to H at position 1795.
+The protein's natural variant, known as in LQT3 and BRGDA1; 7.3-mV negative shift of the steady-state inactivation curve and 8.1-mV positive shift of the steady-state activation curve; may reduce sodium current during the upstroke of the action potential, features a modification of the amino acid from Y to YD at position 1795.
+The protein's natural variant, known as in LQT3; digenic; the patient also carries mutation G-100 on KCNH2;, features a modification of the amino acid from D to N at position 1819.
+The protein's natural variant, known as in LQT3; drug-induced LQT syndrome;, features a modification of the amino acid from L to P at position 1825.
+The protein's natural variant, known as in ATFB10;, features a modification of the amino acid from R to C at position 1826.
+The protein's natural variant, known as in LQT3; sodium current characterized by slower decay and a 2- to 3-fold increase in late sodium current;, features a modification of the amino acid from R to H at position 1826.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from Q to E at position 1832.
+The protein's natural variant, known as in LQT3;, features a modification of the amino acid from D to G at position 1839.
+The protein's natural variant, known as in LQT3; decreased interaction with FGF12, FGF13 and FGF14; increased voltage-gated sodium channel activity; altered inactivation;, features a modification of the amino acid from H to R at position 1849.
+The protein's natural variant, known as in BRGDA1; decreased I(Na) density; shift of the steady-state inactivation towards negative potentials;, features a modification of the amino acid from C to S at position 1850.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from V to I at position 1861.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from K to N at position 1872.
+The protein's natural variant, known as in atrial fibrillation; pronounced depolarized shift of the voltage dependence of steady-state inactivation; no persistent sodium current;, features a modification of the amino acid from M to T at position 1875.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from R to W at position 1897.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from E to Q at position 1901.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from V to L at position 1903.
+The protein's natural variant, known as in LQT3; promotes late sodium currents by increasing the propensity of the channel to reopen during prolonged depolarization;, features a modification of the amino acid from S to L at position 1904.
+The protein's natural variant, known as in LQT3;, features a modification of the amino acid from Q to R at position 1909.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from R to H at position 1913.
+The protein's natural variant, known as in BRGDA1; significantly affect cardiac sodium channel characteristics; associated with an increase in inward sodium current during the action potential upstroke;, features a modification of the amino acid from A to T at position 1924.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from G to S at position 1935.
+The protein's natural variant, known as in BRGDA1; unknown pathological significance;, features a modification of the amino acid from E to K at position 1938.
+The protein's natural variant, known as in LQT3;, features a modification of the amino acid from A to S at position 1949.
+The protein's natural variant, known as in BRGDA1 and LQT3; also found in patients with atrial fibrillation; unknown pathological significance;, features a modification of the amino acid from V to L at position 1951.
+The protein's natural variant, known as in ATFB10;, features a modification of the amino acid from V to M at position 1951.
+The protein's natural variant, known as found in a patient with long QT syndrome; unknown pathological significance;, features a modification of the amino acid from R to Q at position 1958.
+The protein's natural variant, known as in BRGDA1;, features a modification of the amino acid from I to S at position 1968.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from Y to N at position 1977.
+The protein's natural variant, known as in ATFB10;, features a modification of the amino acid from N to K at position 1987.
+The protein's natural variant, known as in LQT3 and BRGDA1; also found in patients with atrial fibrillation; results in channels with decreased peak and persistent current amplitudes; increased closed-state and slow inactivation; decelerated recovery from inactivation;, features a modification of the amino acid from F to L at position 2004.
+The protein's natural variant, known as in BRGDA1 and LQT3;, features a modification of the amino acid from F to V at position 2004.
+The protein's natural variant, known as found in a patient with long QT syndrome; unknown pathological significance; causes an increase of persistent sodium current and produces a depolarizing shift in voltage dependence of inactivation;, features a modification of the amino acid from P to A at position 2006.
+The protein's natural variant, known as in LQT3; unknown pathological significance;, features a modification of the amino acid from R to C at position 2012.
+The protein's natural variant, known as in CRMCC1;, features a modification of the amino acid from A to V at position 227.
+The protein's natural variant, known as in CRMCC1;, features a modification of the amino acid from V to M at position 259.
+The protein's natural variant, known as in CRMCC1;, features a modification of the amino acid from G to R at position 503.
+The protein's natural variant, known as in CRMCC1;, features a modification of the amino acid from V to G at position 665.
+The protein's natural variant, known as in CRMCC1;, features a modification of the amino acid from R to W at position 840.
+The protein's natural variant, known as in CRMCC1;, features a modification of the amino acid from V to M at position 871.
+The protein's natural variant, known as in CRMCC1;, features a modification of the amino acid from R to G at position 975.
+The protein's natural variant, known as in CRMCC1;, features a modification of the amino acid from R to W at position 987.
+The protein's natural variant, known as in CRMCC1;, features a modification of the amino acid from L to H at position 1142.
+The protein's natural variant, known as in recC-1004; holoenzyme prefers an altered Chi over wild-type Chi sequence. Pseudorevertant of a frameshift mutation at aa 647, features a modification of the amino acid from QERISQRFL to KNVSASVF at position 655.
+The protein's natural variant, known as in RP88; unknown pathological significance;, features a modification of the amino acid from P to H at position 19.
+The protein's natural variant, known as in OCMD;, features a modification of the amino acid from R to W at position 45.
+The protein's natural variant, known as in RP88; unknown pathological significance;, features a modification of the amino acid from R to Q at position 152.
+The protein's natural variant, known as in OCMD; unknown pathological significance;, features a modification of the amino acid from R to H at position 950.
+The protein's natural variant, known as in OCMD;, features a modification of the amino acid from W to R at position 960.
+The protein's natural variant, known as in OCMD; unknown pathological significance;, features a modification of the amino acid from S to C at position 1199.
+The protein's natural variant, known as in OCMD; unknown pathological significance;, features a modification of the amino acid from G to D at position 1200.
+The protein's natural variant, known as in allele RP1L1-3, features a modification of the amino acid from A to S at position 1285.
+The protein's natural variant, known as in allele RP1L1-2, features a modification of the amino acid from E to EGVQLEETKTEEGLQEE at position 1313.
+The protein's natural variant, known as in allele RP1L1-3, features a modification of the amino acid from E to EGVQLEETKTEEGLQEEGVQLEETKTEEGLQEE at position 1313.
+The protein's natural variant, known as in allele RP1L1-4, features a modification of the amino acid from E to EGVQLEETKTEEGLQEEGVQLEETKTEEGLQEEGVQLEETKTEEGLQEE at position 1313.
+The protein's natural variant, known as in allele RP1L1-5, features a modification of the amino acid from E to EGVQLEETKTEEGLQEEGVQLEETKTEEGLQEEGVQLEETKTEEGLQEEGVQLEETKTEEGLQEE at position 1313.
+The protein's natural variant, known as in allele RP1L1-6, features a modification of the amino acid from E to EGVQLEETKTEEGLQEEGVQLEETKTEEGLQEEGVQLEETKTEEGLQEEGVQLEETKTEEGLQEEGVQLEETKTEEGLQEE at position 1313.
+The protein's natural variant, known as in allele RP1L1-3;, features a modification of the amino acid from E to G at position 1324.
+The protein's natural variant, known as in allele RP1L1-3;, features a modification of the amino acid from TE to VI at position 1328.
+The protein's natural variant, known as in allele RP1L1-2 and allele RP1L1-3;, features a modification of the amino acid from G to R at position 1335.
+The natural variant of this protein is characterized by an amino acid alteration from K to KK at position 1578.
+The natural variant of this protein is characterized by an amino acid alteration from G to V at position 2069.
+The natural variant of this protein is characterized by an amino acid alteration from E to G at position 2242.
+The protein's natural variant, known as associated with increased glycogen content and metabolism in skeletal muscle; results in increased basal and AMP-activated AMPK activity;, features a modification of the amino acid from R to W at position 225.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from I to N at position 87.
+The protein's natural variant, known as in allele 6M1-15*03;, features a modification of the amino acid from M to V at position 81.
+The protein's natural variant, known as in allele 6M1-15*02;, features a modification of the amino acid from D to N at position 296.
+The protein's natural variant, known as in PCH2D; abrogates enzyme activity;, features a modification of the amino acid from A to T at position 239.
+The protein's natural variant, known as in PCH2D;, features a modification of the amino acid from T to S at position 325.
+The protein's natural variant, known as in PCH2D; abrogates enzyme activity;, features a modification of the amino acid from Y to C at position 334.
+The protein's natural variant, known as in strain: F, features a modification of the amino acid from I to T at position 90.
+The protein's natural variant, known as in CMD1P; impairs phosphorylation by PKA and inhibition of ATP2A1-mediated calcium uptake;, features a modification of the amino acid from R to C at position 9.
+The protein's natural variant, known as in CMD1P; impairs phosphorylation by PKA and inhibition of ATP2A1-mediated calcium uptake;, features a modification of the amino acid from R to H at position 9.
+The protein's natural variant, known as in CMD1P; impairs phosphorylation by PKA and inhibition of ATP2A1-mediated calcium uptake, features a modification of the amino acid from R to L at position 9.
+The protein's natural variant, known as in strain: BNCV / Serogroup B, features a modification of the amino acid from G to S at position 3.
+The protein's natural variant, known as in strain: BNCV / Serogroup B, features a modification of the amino acid from G to S at position 12.
+The protein's natural variant, known as in strain: BNCV / Serogroup B, features a modification of the amino acid from N to D at position 33.
+The protein's natural variant, known as confirmed at protein level;, features a modification of the amino acid from V to I at position 62.
+The protein's natural variant, known as in AHUS1, features a modification of the amino acid from R to G at position 78.
+The protein's natural variant, known as in CFHD; with membranoproliferative glomerulonephritis;, features a modification of the amino acid from R to L at position 127.
+The protein's natural variant, known as in AHUS1, features a modification of the amino acid from C to Y at position 325.
+The protein's natural variant, known as in AHUS1;, features a modification of the amino acid from Q to K at position 400.
+The protein's natural variant, known as associated with ARMD4;, features a modification of the amino acid from Y to H at position 402.
+The protein's natural variant, known as in CFHD; with membranoproliferative glomerulonephritis;, features a modification of the amino acid from C to S at position 431.
+The protein's natural variant, known as in CFHD;, features a modification of the amino acid from C to R at position 536.
+The protein's natural variant, known as associated with basal laminar drusen;, features a modification of the amino acid from R to G at position 567.
+The protein's natural variant, known as in AHUS1;, features a modification of the amino acid from V to I at position 609.
+The protein's natural variant, known as in AHUS1, features a modification of the amino acid from C to W at position 630.
+The protein's natural variant, known as in CFHD; with membranoproliferative glomerulonephritis, features a modification of the amino acid from C to S at position 673.
+The protein's natural variant, known as in AHUS1;, features a modification of the amino acid from C to Y at position 673.
+The protein's natural variant, known as in AHUS1; variant confirmed at protein level;, features a modification of the amino acid from E to K at position 850.
+The protein's natural variant, known as in AHUS1;, features a modification of the amino acid from H to R at position 893.
+The protein's natural variant, known as in AHUS1, features a modification of the amino acid from C to S at position 915.
+The protein's natural variant, known as associated with hemolytic uremic syndrome and basal laminar drusen;, features a modification of the amino acid from E to D at position 936.
+The protein's natural variant, known as in AHUS1;, features a modification of the amino acid from Q to H at position 950.
+The protein's natural variant, known as in AHUS1;, features a modification of the amino acid from Y to H at position 951.
+The protein's natural variant, known as in AHUS1;, features a modification of the amino acid from T to M at position 956.
+The protein's natural variant, known as in CFHD; variant confirmed at protein level;, features a modification of the amino acid from C to Y at position 959.
+The protein's natural variant, known as in AHUS1, features a modification of the amino acid from W to C at position 978.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 1007.
+The protein's natural variant, known as in AHUS1, features a modification of the amino acid from Y to F at position 1021.
+The protein's natural variant, known as in AHUS1, features a modification of the amino acid from C to R at position 1043.
+The protein's natural variant, known as associated with basal laminar drusen;, features a modification of the amino acid from N to Y at position 1050.
+The protein's natural variant, known as in CFHD;, features a modification of the amino acid from Q to E at position 1076.
+The protein's natural variant, known as associated with basal laminar drusen;, features a modification of the amino acid from R to S at position 1078.
+The protein's natural variant, known as in CFHD;, features a modification of the amino acid from D to G at position 1119.
+The protein's natural variant, known as in AHUS1, features a modification of the amino acid from V to G at position 1134.
+The protein's natural variant, known as in AHUS1, features a modification of the amino acid from Y to D at position 1142.
+The protein's natural variant, known as confirmed at protein level;, features a modification of the amino acid from Q to E at position 1143.
+The protein's natural variant, known as in AHUS1, features a modification of the amino acid from W to R at position 1157.
+The protein's natural variant, known as in AHUS1, features a modification of the amino acid from C to W at position 1163.
+The protein's natural variant, known as in AHUS1, features a modification of the amino acid from I to L at position 1169.
+The protein's natural variant, known as in AHUS1, features a modification of the amino acid from W to C at position 1183.
+The protein's natural variant, known as in AHUS1, features a modification of the amino acid from W to L at position 1183.
+The protein's natural variant, known as in AHUS1, features a modification of the amino acid from W to R at position 1183.
+The protein's natural variant, known as in CFHD, features a modification of the amino acid from T to R at position 1184.
+The protein's natural variant, known as in AHUS1;, features a modification of the amino acid from L to R at position 1189.
+The protein's natural variant, known as in AHUS1;, features a modification of the amino acid from S to L at position 1191.
+The protein's natural variant, known as in AHUS1;, features a modification of the amino acid from G to D at position 1194.
+The protein's natural variant, known as in AHUS1;, features a modification of the amino acid from V to A at position 1197.
+The protein's natural variant, known as in AHUS1, features a modification of the amino acid from E to A at position 1198.
+The protein's natural variant, known as in AHUS1, features a modification of the amino acid from F to S at position 1199.
+The protein's natural variant, known as in CFHD and ARMD4; rare penetrant mutation that confers high risk of age-related macular degeneration;, features a modification of the amino acid from R to C at position 1210.
+The protein's natural variant, known as in AHUS1;, features a modification of the amino acid from R to G at position 1215.
+The protein's natural variant, known as in CFHD, features a modification of the amino acid from R to Q at position 1215.
+The protein's natural variant, known as in AHUS1, features a modification of the amino acid from YPTCAKR to FQS at position 1231.
+The protein's natural variant, known as in AHUS1; atypical, features a modification of the amino acid from P to S at position 1226.
+The natural variant of this protein is characterized by an amino acid alteration from A to M at position 97.
+The natural variant of this protein is characterized by an amino acid alteration from I to P at position 191.
+The natural variant of this protein is characterized by an amino acid alteration from I to L at position 202.
+The protein's natural variant, known as in strain: cv. RTCS 2, features a modification of the amino acid from G to R at position 5.
+The protein's natural variant, known as in HFE4;, features a modification of the amino acid from Y to N at position 64.
+The protein's natural variant, known as in HFE4;, features a modification of the amino acid from A to D at position 77.
+The protein's natural variant, known as in HFE4; Reduces protein stability. Loss of cell surface localization. Loss of iron export function. Increases intracellular manganese;, features a modification of the amino acid from G to S at position 80.
+The protein's natural variant, known as in HFE4;, features a modification of the amino acid from G to V at position 80.
+The protein's natural variant, known as in HFE4;, features a modification of the amino acid from N to D at position 144.
+The protein's natural variant, known as in HFE4; Does not affect protein stability. Does not affect cell surface localization. Increases iron export activity;, features a modification of the amino acid from N to H at position 144.
+The protein's natural variant, known as in HFE4; Does not affect protein stability. Does not affect cell surface localization. Increases iron export activity;, features a modification of the amino acid from N to T at position 144.
+The protein's natural variant, known as in HFE4; Reduces protein stability. Loss of cell surface localization. Loss of iron export activity. Increases intracellular manganese;, features a modification of the amino acid from D to G at position 157.
+The protein's natural variant, known as in iron overload;, features a modification of the amino acid from N to I at position 174.
+The protein's natural variant, known as in HFE4;, features a modification of the amino acid from D to V at position 181.
+The protein's natural variant, known as in HFE4;, features a modification of the amino acid from Q to H at position 182.
+The protein's natural variant, known as associated with mild anemia and a tendency to iron loading. Prevents hepcidin/HAMP-induced degradation. Protects against severe malaria disease;, features a modification of the amino acid from Q to H at position 248.
+The protein's natural variant, known as in HFE4;, features a modification of the amino acid from G to D at position 267.
+The protein's natural variant, known as in HFE4;, features a modification of the amino acid from D to V at position 270.
+The protein's natural variant, known as in HFE4;, features a modification of the amino acid from G to V at position 323.
+The protein's natural variant, known as in iron overload, features a modification of the amino acid from C to Y at position 326.
+The protein's natural variant, known as in HFE4; Loss of iron export activity;, features a modification of the amino acid from G to D at position 490.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from S to C at position 129.
+The protein's natural variant, known as in JBS; decreased, but detectable activity in a yeast-based assay, features a modification of the amino acid from V to L at position 122.
+The protein's natural variant, known as in JBS, features a modification of the amino acid from C to F at position 127.
+The protein's natural variant, known as in JBS; prevents proper folding of the UBR-type zinc finger; may decrease protein stability; loss of activity in a yeast-based assay;, features a modification of the amino acid from H to R at position 136.
+The protein's natural variant, known as in JBS, features a modification of the amino acid from H to R at position 166.
+The protein's natural variant, known as in JBS, features a modification of the amino acid from L to R at position 217.
+The protein's natural variant, known as in JBS, features a modification of the amino acid from I to R at position 286.
+The protein's natural variant, known as in JBS, features a modification of the amino acid from L to P at position 317.
+The protein's natural variant, known as in JBS; unknown pathological significance;, features a modification of the amino acid from L to R at position 427.
+The protein's natural variant, known as in JBS;, features a modification of the amino acid from A to D at position 563.
+The protein's natural variant, known as in JBS, features a modification of the amino acid from S to P at position 700.
+The protein's natural variant, known as in JBS;, features a modification of the amino acid from R to C at position 754.
+The protein's natural variant, known as in JBS;, features a modification of the amino acid from R to H at position 754.
+The protein's natural variant, known as in JBS; strong decrease in activity in a yeast-based assay, features a modification of the amino acid from Q to E at position 1102.
+The protein's natural variant, known as in JBS;, features a modification of the amino acid from R to G at position 1242.
+The protein's natural variant, known as in JBS, features a modification of the amino acid from G to S at position 1279.
+The protein's natural variant, known as in JBS, features a modification of the amino acid from P to L at position 1426.
+The protein's natural variant, known as in JBS;, features a modification of the amino acid from S to F at position 1427.
+The protein's natural variant, known as in JBS;, features a modification of the amino acid from S to P at position 1431.
+The protein's natural variant, known as in JBS, features a modification of the amino acid from G to R at position 1661.
+The protein's natural variant, known as in DEE13; unknown pathological significance; no effect on channel activity, features a modification of the amino acid from D to N at position 58.
+The protein's natural variant, known as in DEE13, features a modification of the amino acid from F to L at position 210.
+The protein's natural variant, known as in DEE13; unknown pathological significance; requires 2 nucleotide substitutions, features a modification of the amino acid from N to R at position 215.
+The protein's natural variant, known as in DEE13;, features a modification of the amino acid from V to D at position 216.
+The protein's natural variant, known as in DEE13; loss of function mutation; reduces channel activity;, features a modification of the amino acid from R to G at position 223.
+The protein's natural variant, known as in DEE13, features a modification of the amino acid from S to P at position 232.
+The protein's natural variant, known as in DEE13; unknown pathological significance;, features a modification of the amino acid from F to S at position 260.
+The protein's natural variant, known as in DEE13; unknown pathological significance;, features a modification of the amino acid from N to S at position 307.
+The protein's natural variant, known as in DEE13; unknown pathological significance;, features a modification of the amino acid from L to F at position 407.
+The protein's natural variant, known as in DEE13; unknown pathological significance, features a modification of the amino acid from A to T at position 408.
+The protein's natural variant, known as in DEE13; unknown pathological significance;, features a modification of the amino acid from V to L at position 410.
+The protein's natural variant, known as in DEE13; unknown pathological significance, features a modification of the amino acid from E to V at position 479.
+The protein's natural variant, known as in DEE13; unknown pathological significance;, features a modification of the amino acid from R to C at position 662.
+The protein's natural variant, known as in DEE13; gain-of-function mutation; increases channel activity;, features a modification of the amino acid from T to I at position 767.
+The protein's natural variant, known as in DEE13;, features a modification of the amino acid from F to S at position 846.
+The protein's natural variant, known as in DEE13; requires 2 nucleotide substitutions, features a modification of the amino acid from R to E at position 850.
+The protein's natural variant, known as in DEE13; unknown pathological significance;, features a modification of the amino acid from R to Q at position 850.
+The protein's natural variant, known as in DEE13;, features a modification of the amino acid from A to T at position 890.
+The protein's natural variant, known as in DEE13;, features a modification of the amino acid from V to M at position 891.
+The protein's natural variant, known as in DEE13; unknown pathological significance;, features a modification of the amino acid from V to D at position 960.
+The protein's natural variant, known as in DEE13;, features a modification of the amino acid from S to G at position 978.
+The protein's natural variant, known as in DEE13; gain-of-function mutation; increased channel activity;, features a modification of the amino acid from N to K at position 984.
+The protein's natural variant, known as in DEE13, features a modification of the amino acid from L to V at position 1279.
+The protein's natural variant, known as in DEE13; unknown pathological significance, features a modification of the amino acid from A to S at position 1323.
+The protein's natural variant, known as in DEE13;, features a modification of the amino acid from I to V at position 1327.
+The protein's natural variant, known as in DEE13; unknown pathological significance;, features a modification of the amino acid from L to V at position 1331.
+The protein's natural variant, known as in DEE13; loss of channel activity;, features a modification of the amino acid from G to S at position 1451.
+The protein's natural variant, known as in DEE13;, features a modification of the amino acid from N to K at position 1466.
+The protein's natural variant, known as in DEE13;, features a modification of the amino acid from N to T at position 1466.
+The protein's natural variant, known as in DEE13;, features a modification of the amino acid from G to R at position 1475.
+The protein's natural variant, known as in DEE13; unknown pathological significance;, features a modification of the amino acid from I to V at position 1479.
+The protein's natural variant, known as in BFIS5;, features a modification of the amino acid from E to K at position 1483.
+The protein's natural variant, known as in DEE13; unknown pathological significance;, features a modification of the amino acid from V to L at position 1592.
+The protein's natural variant, known as in DEE13; unknown pathological significance;, features a modification of the amino acid from S to C at position 1596.
+The protein's natural variant, known as in DEE13, features a modification of the amino acid from V to A at position 1598.
+The protein's natural variant, known as in DEE13; unknown pathological significance, features a modification of the amino acid from I to R at position 1605.
+The protein's natural variant, known as in DEE13; gain-of-function mutation; increased channel activity; impaired channel inactivation;, features a modification of the amino acid from R to Q at position 1617.
+The protein's natural variant, known as in DEE13;, features a modification of the amino acid from A to T at position 1650.
+The protein's natural variant, known as in MYOCL2; decreased channel activity; results in significantly reduced inward sodium current without changes of voltage-dependent channel activation and inactivation;, features a modification of the amino acid from P to R at position 1719.
+The protein's natural variant, known as in DEE13; unknown pathological significance, features a modification of the amino acid from F to S at position 1754.
+The protein's natural variant, known as in DEE13; gain-of-function mutation; results in increased persistent sodium currents and incomplete channel inactivation;, features a modification of the amino acid from N to D at position 1768.
+The protein's natural variant, known as in DEE13; unknown pathological significance;, features a modification of the amino acid from Q to E at position 1801.
+The protein's natural variant, known as in DEE13; unknown pathological significance, features a modification of the amino acid from L to P at position 1865.
+The protein's natural variant, known as in DEE13; gain-of-function mutation; increased channel activity; impaired channel inactivation;, features a modification of the amino acid from R to L at position 1872.
+The protein's natural variant, known as in DEE13; gain-of-function mutation; increased channel activity; impaired channel inactivation;, features a modification of the amino acid from R to Q at position 1872.
+The protein's natural variant, known as in DEE13; gain-of-function mutation; increased channel activity; impaired channel inactivation; no effect on interactions with FGF14, SCN1B, GNB2 and GNG3;, features a modification of the amino acid from R to W at position 1872.
+The protein's natural variant, known as in DEE13 and BFIS5; also found in a patient with drug-resistant focal epilepsy and mild intellectual disability;, features a modification of the amino acid from N to S at position 1877.
+The protein's natural variant, known as in strain: MGAS 1896, features a modification of the amino acid from G to S at position 17.
+The protein's natural variant, known as in strain: MGAS 168, features a modification of the amino acid from V to I at position 80.
+The protein's natural variant, known as in strain: MGAS 165, 168, 429, 659, 660, 796, 800, 1719, 1838, 1882, 2017 and 2018, features a modification of the amino acid from A to V at position 111.
+The protein's natural variant, known as in strain: MGAS 650, features a modification of the amino acid from T to I at position 137.
+The protein's natural variant, known as in strain: MGAS 684, features a modification of the amino acid from D to N at position 154.
+The protein's natural variant, known as in strain: MGAS 366, 427, 758, 1294, 1911, 1914A and 1991, features a modification of the amino acid from L to V at position 211.
+The protein's natural variant, known as in strain: MGAS 1901 and Sv, features a modification of the amino acid from I to V at position 305.
+The protein's natural variant, known as in strain: MGAS 429, 659, 807, 1226, 1719, 1832, 1842, 1871, 1872, 2017 and 2018, features a modification of the amino acid from S to G at position 308.
+The protein's natural variant, known as in strain: MGAS 165, 168, 289, 302, 1233 and 1898, features a modification of the amino acid from A to S at position 317.
+The protein's natural variant, known as in strain: MGAS 1871, features a modification of the amino acid from G to D at position 384.
+The protein's natural variant, known as in strain: MGAS 366 and 1294, features a modification of the amino acid from V to I at position 394.
+The protein's natural variant, known as in RP83; unknown pathological significance;, features a modification of the amino acid from Y to C at position 90.
+The protein's natural variant, known as in JBTS35;, features a modification of the amino acid from R to C at position 149.
+The protein's natural variant, known as in JBTS35; decreased release of NPHP3 and INPP5E cargos to the cilium;, features a modification of the amino acid from R to H at position 149.
+The protein's natural variant, known as rare variant found in patients with X-linked intellectual disability; unknown pathological significance;, features a modification of the amino acid from P to L at position 412.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from V to I at position 220.
+The protein's natural variant, known as in CILD29; decreases formation of basal bodies in multiciliated cells;, features a modification of the amino acid from L to P at position 213.
+The protein's natural variant, known as in CILD29;, features a modification of the amino acid from H to R at position 239.
+The protein's natural variant, known as found in a patient with a form of spinal muscular atrophy; unknown pathological significance, features a modification of the amino acid from P to R at position 79.
+The protein's natural variant, known as in HK; decreases TSPO2 expression levels. Abnormal chromosome condensation and chromosome segregation in differentiating erythrocytes, resulting in abnormal cytokinesis and differentiation, features a modification of the amino acid from C to Y at position 40.
+The protein's natural variant, known as in HK; associated in cis with F-98 DEL and I-120; decreases TSPO2 expression levels, features a modification of the amino acid from V to F at position 89.
+The protein's natural variant, known as in HK; associated in cis with F-89 and F-98 DEL; decreases TSPO2 expression levels, features a modification of the amino acid from T to I at position 120.
+The protein's natural variant, known as in IPEX; mild phenotype; no loss of protein expression, features a modification of the amino acid from L to P at position 242.
+The protein's natural variant, known as in IPEX; mild phenotype; no loss of protein expression;, features a modification of the amino acid from F to L at position 324.
+The protein's natural variant, known as in IPEX; no loss of protein expression;, features a modification of the amino acid from P to A at position 339.
+The protein's natural variant, known as in IPEX; mild phenotype; no loss of protein expression; impairs its ability to confer inhibitory function to regulatory T-cells; no loss of DNA-binding when associated with A-373;, features a modification of the amino acid from R to H at position 347.
+The protein's natural variant, known as in IPEX, features a modification of the amino acid from I to V at position 363.
+The protein's natural variant, known as in IPEX; no effect on dimerization;, features a modification of the amino acid from F to C at position 371.
+The protein's natural variant, known as in IPEX; requires 2 nucleotide substitutions; no loss of protein expression; disrupts dimerization; impairs its ability to confer inhibitory function to regulatory T-cells; no loss of DNA-binding when associated with H-347;, features a modification of the amino acid from F to A at position 373.
+The protein's natural variant, known as in IPEX; no loss of protein expression, features a modification of the amino acid from F to C at position 374.
+The protein's natural variant, known as in IPEX; no loss of protein expression;, features a modification of the amino acid from A to T at position 384.
+The protein's natural variant, known as in IPEX;, features a modification of the amino acid from R to W at position 397.
+The protein's natural variant, known as in strain: cv. P-10 Inbred, features a modification of the amino acid from L to V at position 18.
+The protein's natural variant, known as in strain: cv. P-10 Inbred, features a modification of the amino acid from I to M at position 370.
+The protein's natural variant, known as in strain: cv. P-10 Inbred, features a modification of the amino acid from N to D at position 376.
+The natural variant of this protein is characterized by an amino acid alteration from H to R at position 64.
+The protein's natural variant, known as in RHFCA;, features a modification of the amino acid from S to P at position 146.
+The protein's natural variant, known as in RHFCA;, features a modification of the amino acid from R to L at position 363.
+The protein's natural variant, known as increased antiprotease activity and increased MAPK8 inhibition activity;, features a modification of the amino acid from G to A at position 351.
+The protein's natural variant, known as in HYPT5; unknown pathological significance, features a modification of the amino acid from A to T at position 8.
+The protein's natural variant, known as in DEE40;, features a modification of the amino acid from A to S at position 609.
+The natural variant of this protein is characterized by an amino acid alteration from S to SPESPDTTSQEPPDTTSQEPPDTTS at position 253.
+The protein's natural variant, known as in Spd, features a modification of the amino acid from G to R at position 42.
+The protein's natural variant, known as in BAMS; no change in protein abundance;, features a modification of the amino acid from L to P at position 107.
+The protein's natural variant, known as in FSHD2, features a modification of the amino acid from A to T at position 110.
+The protein's natural variant, known as in BAMS; no change in protein abundance;, features a modification of the amino acid from M to K at position 129.
+The protein's natural variant, known as in BAMS; has an increased ATPase activity, features a modification of the amino acid from A to S at position 134.
+The protein's natural variant, known as in BAMS; has an increased ATPase activity; no change in protein abundance;, features a modification of the amino acid from S to C at position 135.
+The protein's natural variant, known as in BAMS; no change in protein abundance;, features a modification of the amino acid from S to I at position 135.
+The protein's natural variant, known as in BAMS; no change in protein abundance; does not affect ATPase activity;, features a modification of the amino acid from S to N at position 135.
+The protein's natural variant, known as in BAMS; no change in protein abundance;, features a modification of the amino acid from E to D at position 136.
+The protein's natural variant, known as in BAMS; has an increased ATPase activity, features a modification of the amino acid from E to G at position 136.
+The protein's natural variant, known as in BAMS and FSHD2; no change in protein abundance; strongly increased ATPase activity;, features a modification of the amino acid from G to E at position 137.
+The protein's natural variant, known as in BAMS; no change in protein abundance;, features a modification of the amino acid from N to H at position 139.
+The protein's natural variant, known as in BAMS; no change in protein abundance;, features a modification of the amino acid from L to F at position 141.
+The protein's natural variant, known as in BAMS; no change in protein abundance;, features a modification of the amino acid from F to V at position 171.
+The protein's natural variant, known as in FSHD2; decreased ATPase activity, features a modification of the amino acid from L to F at position 194.
+The protein's natural variant, known as in BAMS; no change in protein abundance;, features a modification of the amino acid from A to G at position 242.
+The protein's natural variant, known as in FSHD2; decreased ATPase activity, features a modification of the amino acid from H to D at position 263.
+The protein's natural variant, known as in FSHD2; does not affect ATPase activity;, features a modification of the amino acid from Y to C at position 283.
+The protein's natural variant, known as in BAMS; slightly decreased ATPase activity, features a modification of the amino acid from W to S at position 342.
+The protein's natural variant, known as in BAMS; no change in protein abundance;, features a modification of the amino acid from Q to R at position 345.
+The protein's natural variant, known as in BAMS; no change in protein abundance; does not affect ATPase activity;, features a modification of the amino acid from H to R at position 348.
+The protein's natural variant, known as in FSHD2; decreased protein level in fibroblasts as compared to wild-type protein; abolished ATPase activity, features a modification of the amino acid from Y to C at position 353.
+The protein's natural variant, known as in BAMS; no change in protein abundance;, features a modification of the amino acid from Q to L at position 400.
+The protein's natural variant, known as in BAMS; no change in protein abundance; slightly decreased ATPase activity;, features a modification of the amino acid from D to V at position 420.
+The protein's natural variant, known as in FSHD2, features a modification of the amino acid from G to R at position 425.
+The protein's natural variant, known as in BAMS; no change in protein abundance; slightly decreased ATPase activity;, features a modification of the amino acid from E to Q at position 473.
+The protein's natural variant, known as in FSHD2; abolished ATPase activity, features a modification of the amino acid from G to E at position 478.
+The protein's natural variant, known as in FSHD2; decreased protein level in fibroblasts as compared to wild-type protein, features a modification of the amino acid from R to P at position 479.
+The protein's natural variant, known as in FSHD2; decreased protein level in fibroblasts as compared to wild-type protein, features a modification of the amino acid from C to R at position 492.
+The protein's natural variant, known as in BAMS; increased ATPase activity, features a modification of the amino acid from K to E at position 518.
+The protein's natural variant, known as in BAMS; no change in protein abundance; slightly decreased ATPase activity;, features a modification of the amino acid from T to K at position 523.
+The protein's natural variant, known as in BAMS; no change in protein abundance;, features a modification of the amino acid from N to S at position 524.
+The protein's natural variant, known as in FSHD2; decreased ATPase activity;, features a modification of the amino acid from T to M at position 527.
+The protein's natural variant, known as in BAMS; no change in protein abundance; does not affect ATPase activity;, features a modification of the amino acid from R to Q at position 552.
+The protein's natural variant, known as in FSHD2, features a modification of the amino acid from V to D at position 615.
+The protein's natural variant, known as in FSHD2; decreased protein level in fibroblasts as compared to wild-type protein; decreased ATPase activity;, features a modification of the amino acid from P to S at position 690.
+The protein's natural variant, known as in FSHD2, features a modification of the amino acid from G to S at position 716.
+The protein's natural variant, known as in FSHD2, features a modification of the amino acid from L to P at position 748.
+The protein's natural variant, known as in FSHD2, features a modification of the amino acid from D to N at position 849.
+The protein's natural variant, known as in FSHD2; decreased protein level in fibroblasts as compared to wild-type protein, features a modification of the amino acid from S to N at position 868.
+The protein's natural variant, known as in FSHD2, features a modification of the amino acid from TD to MH at position 1177.
+The protein's natural variant, known as in FSHD2, features a modification of the amino acid from R to K at position 1449.
+The protein's natural variant, known as in FSHD2, features a modification of the amino acid from Q to P at position 1463.
+The protein's natural variant, known as in FSHD2, features a modification of the amino acid from M to I at position 1468.
+The protein's natural variant, known as in FSHD2, features a modification of the amino acid from P to L at position 1485.
+The protein's natural variant, known as in FSHD2, features a modification of the amino acid from QP to HQ at position 1488.
+The protein's natural variant, known as in FSHD2; decreased protein level in fibroblasts as compared to wild-type protein, features a modification of the amino acid from F to S at position 1554.
+The protein's natural variant, known as in plasmid IncFIIR1, features a modification of the amino acid from H to R at position 14.
+The protein's natural variant, known as in plasmid IncFIIR1, features a modification of the amino acid from W to R at position 210.
+The protein's natural variant, known as in MPPH1;, features a modification of the amino acid from G to R at position 373.
+The protein's natural variant, known as in MPPH1; unknown pathological significance;, features a modification of the amino acid from K to E at position 376.
+The protein's natural variant, known as in MPPH1;, features a modification of the amino acid from L to P at position 401.
+The protein's natural variant, known as in MPPH1;, features a modification of the amino acid from D to H at position 557.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from I to M at position 229.
+The protein's natural variant, known as in OI13; the mutation leads to severely reduced post-translational N-glycosylation of the protein and impairs protein secretion; leads to both reduced secretion and subsequent reduced processing of the substrates CHRD and COL1A1;, features a modification of the amino acid from G to R at position 12.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from D to H at position 45.
+The protein's natural variant, known as in OI13; leads to a protein with deficient procollagen IC-terminal propeptide proteolytic activity;, features a modification of the amino acid from F to L at position 249.
+The protein's natural variant, known as in OI13; partial loss of activity;, features a modification of the amino acid from M to V at position 270.
+The protein's natural variant, known as in strain: 14021-0251.0, features a modification of the amino acid from D to A at position 25.
+The protein's natural variant, known as in strain: HW00, HW09, NC37, NC48, TT00 and TT01, features a modification of the amino acid from N to S at position 115.
+The protein's natural variant, known as in strain: MD106, MD225 and RU35, features a modification of the amino acid from F to Y at position 118.
+The protein's natural variant, known as in strain: 14021-0251.0, C167, AU023, DSR, DSW, KY007, KY045, KY201, KY215, MD106, MD111, MD112, MD199, MD221, MD225, MDW86, RU00, RU01, RU07, RU35, RU259 and Sc00, features a modification of the amino acid from T to S at position 129.
+The protein's natural variant, known as in strain: 14021-0251.0, C167, AU023, DSR, DSW, KY007, KY045, KY201, KY215, MD106, MD111, MD112, MD199, MD221, MD225, MDW86, RU00, RU01, RU07, RU35, RU259 and Sc00, features a modification of the amino acid from T to I at position 130.
+The protein's natural variant, known as in strain: AU023, C167, DSR, DSW, KY007, KY045, KY201, KY215, MD106, MD111, MD112, MD199, MD221, MD225, MDW86, RU00, RU01, RU07, RU35, RU259 and Sc00, features a modification of the amino acid from V to I at position 165.
+The protein's natural variant, known as in strain: 14021-0251.0, features a modification of the amino acid from H to N at position 218.
+The protein's natural variant, known as in RP48;, features a modification of the amino acid from G to R at position 157.
+The protein's natural variant, known as in strain: ATCC 43504, features a modification of the amino acid from E to Q at position 19.
+The protein's natural variant, known as in strain: ATCC 43504, features a modification of the amino acid from K to R at position 37.
+The protein's natural variant, known as in strain: ATCC 43504, features a modification of the amino acid from N to D at position 74.
+The protein's natural variant, known as in rc, features a modification of the amino acid from R to Q at position 100.
+The protein's natural variant, known as in strain: cv. C24, features a modification of the amino acid from W to R at position 183.
+The protein's natural variant, known as in strain: cv. C24, features a modification of the amino acid from S to T at position 344.
+The natural variant of this protein is characterized by an amino acid alteration from G to E at position 462.
+The protein's natural variant, known as in FPDMM;, features a modification of the amino acid from R to Q at position 139.
+The protein's natural variant, known as in FPDMM; impaired phosphorylation;, features a modification of the amino acid from R to Q at position 174.
+The protein's natural variant, known as in strain: cv. Ak-1, features a modification of the amino acid from G to D at position 114.
+The protein's natural variant, known as in strain: cv. Ak-1; cv. Bay-0 and cv. Landsberg erecta, features a modification of the amino acid from M to T at position 188.
+The protein's natural variant, known as in strain: cv. Bay-0, features a modification of the amino acid from T to A at position 196.
+The protein's natural variant, known as in KIDAD;, features a modification of the amino acid from G to R at position 12.
+The protein's natural variant, known as in KIDAD;, features a modification of the amino acid from S to F at position 17.
+The protein's natural variant, known as in DFNB1A;, features a modification of the amino acid from R to H at position 32.
+The protein's natural variant, known as in DFNB1A; it is correctly synthesized and targeted to the plasma membrane; it inefficiently forms intercellular channels that display an abnormal electrical behavior;, features a modification of the amino acid from M to T at position 34.
+The protein's natural variant, known as in DFNB1A;, features a modification of the amino acid from V to I at position 37.
+The protein's natural variant, known as in DFNA3A;, features a modification of the amino acid from W to C at position 44.
+The protein's natural variant, known as in DFNA3A; does not affect protein trafficking; affects the ability to form functional channels; dominant negative effect;, features a modification of the amino acid from W to S at position 44.
+The protein's natural variant, known as in deafness;, features a modification of the amino acid from G to E at position 45.
+The protein's natural variant, known as may contribute to deafness, features a modification of the amino acid from DEQ to E at position 48.
+The protein's natural variant, known as in DFNA3A; the mutant is targeted to the plasma membrane but fails to transfer ionic calcium or propidium iodide intercellularly suggesting disruption of both ionic and biochemical coupling; heterozygous gap junctions also show dysfunctional intercellular couplings and hemichannel opening confirming the dominant-negative nature of the mutation, features a modification of the amino acid from D to E at position 46.
+The protein's natural variant, known as in KIDAD and HID syndrome;, features a modification of the amino acid from D to N at position 50.
+The protein's natural variant, known as in KIDAD;, features a modification of the amino acid from D to Y at position 50.
+The protein's natural variant, known as in BAPS;, features a modification of the amino acid from N to K at position 54.
+The protein's natural variant, known as in PPKDFN; impairs trafficking; localizes intracellularly closed to the nucleus; affects the ability to form functional channels; phenotype can be rescued by coexpression with wild-type protein;, features a modification of the amino acid from G to A at position 59.
+The protein's natural variant, known as in BAPS;, features a modification of the amino acid from G to S at position 59.
+The protein's natural variant, known as in VOWNKL and PPKDFN; impairs trafficking; localizes intracellularly closed to the nucleus; affects the ability to form functional channels; phenotype can be rescued by coexpression with wild-type protein;, features a modification of the amino acid from D to H at position 66.
+The protein's natural variant, known as in deafness;, features a modification of the amino acid from I to T at position 71.
+The protein's natural variant, known as in PPKDFN; the mutant has a dominant-negative effect on connexin trafficking;, features a modification of the amino acid from H to R at position 73.
+The protein's natural variant, known as in PPKDFN; the mutant protein completely prevents the formation of functional channels;, features a modification of the amino acid from R to Q at position 75.
+The protein's natural variant, known as in PPKDFN and DFNA3A; does not affect protein trafficking; affects the ability to form functional channels; dominant negative effect;, features a modification of the amino acid from R to W at position 75.
+The protein's natural variant, known as in DFNB1A;, features a modification of the amino acid from W to R at position 77.
+The protein's natural variant, known as in DFNB1A;, features a modification of the amino acid from L to P at position 79.
+The protein's natural variant, known as in DFNB1A, features a modification of the amino acid from Q to K at position 80.
+The protein's natural variant, known as in DFNB1A; sorted to the plasma membrane normally and forms gap junctions that were morphologically and electrically indistinguishable from those of control; the mutation reduces the permeability of GJB2 gap junction channels to inositol 1,4,5-trisphosphate (Ins(1,4,5)P3), resulting in blockade of the Ins(1,4,5)P3-induced inward calcium current in neighboring cells;, features a modification of the amino acid from V to L at position 84.
+The protein's natural variant, known as in DFNB1A; the mutant disrupts cellular communication;, features a modification of the amino acid from V to M at position 84.
+The protein's natural variant, known as in DFNB1A; does not form gap junctions since the mutated protein is confined in the cytoplasm and not transported to the cell membrane; when the mutation is coexpressed with the wild-type protein ionic and biochemical coupling is normal consistent with the recessive nature of the mutation;, features a modification of the amino acid from T to R at position 86.
+The protein's natural variant, known as in DFNB1A;, features a modification of the amino acid from L to P at position 90.
+The protein's natural variant, known as in DFNB1A;, features a modification of the amino acid from M to I at position 93.
+The protein's natural variant, known as in DFNB1A;, features a modification of the amino acid from V to M at position 95.
+The protein's natural variant, known as in DFNB1A;, features a modification of the amino acid from S to R at position 113.
+The natural variant of this protein is characterized by an amino acid alteration from D to H at position 117.
+The protein's natural variant, known as in DFNB1A;, features a modification of the amino acid from E to K at position 129.
+The protein's natural variant, known as in DFNB1A;, features a modification of the amino acid from G to A at position 130.
+The protein's natural variant, known as in DFNB1A;, features a modification of the amino acid from G to D at position 130.
+The protein's natural variant, known as in VOWNKL, features a modification of the amino acid from G to V at position 130.
+The protein's natural variant, known as in DFNA3A;, features a modification of the amino acid from R to Q at position 143.
+The protein's natural variant, known as in DFNB1A;, features a modification of the amino acid from R to W at position 143.
+The natural variant of this protein is characterized by an amino acid alteration from A to P at position 148.
+The protein's natural variant, known as may contribute to deafness;, features a modification of the amino acid from V to I at position 153.
+The protein's natural variant, known as in DFNB1A;, features a modification of the amino acid from D to V at position 159.
+The protein's natural variant, known as may contribute to deafness;, features a modification of the amino acid from V to M at position 167.
+The protein's natural variant, known as in a patient with congenital erythrokeratodermia; unknown pathological significance;, features a modification of the amino acid from K to R at position 168.
+The protein's natural variant, known as in DFNB1A;, features a modification of the amino acid from V to A at position 178.
+The protein's natural variant, known as in DFNA3A;, features a modification of the amino acid from D to N at position 179.
+The protein's natural variant, known as in DFNB1A;, features a modification of the amino acid from R to P at position 184.
+The protein's natural variant, known as in DFNA3A;, features a modification of the amino acid from R to Q at position 184.
+The protein's natural variant, known as in DFNB1A;, features a modification of the amino acid from R to W at position 184.
+The protein's natural variant, known as in DFNA3A;, features a modification of the amino acid from A to S at position 197.
+The protein's natural variant, known as in DFNA3A;, features a modification of the amino acid from C to F at position 202.
+The protein's natural variant, known as in DFNB1A, features a modification of the amino acid from I to K at position 203.
+The protein's natural variant, known as in DFNB1A, features a modification of the amino acid from L to P at position 214.
+The protein's natural variant, known as in LCA4; no significant effect on interaction with NUB1;, features a modification of the amino acid from C to R at position 239.
+The protein's natural variant, known as in LCA4, features a modification of the amino acid from R to H at position 270.
+The protein's natural variant, known as found in a patient with LCA4; there is no interaction with NUB1;, features a modification of the amino acid from R to L at position 302.
+The protein's natural variant, known as found in a patient with LCA4, features a modification of the amino acid from E to DLNRREL at position 309.
+The protein's natural variant, known as in alpha-2, features a modification of the amino acid from K to KL at position 11.
+The protein's natural variant, known as in alpha-2, features a modification of the amino acid from K to A at position 27.
+The protein's natural variant, known as in alpha-2, features a modification of the amino acid from L to K at position 31.
+The natural variant of this protein is characterized by an amino acid alteration from G to V at position 580.
+The natural variant of this protein is characterized by an amino acid alteration from R to K at position 588.
+The natural variant of this protein is characterized by an amino acid alteration from R to S at position 725.
+The protein's natural variant, known as in strain: Isolate SAS-5, features a modification of the amino acid from L to F at position 102.
+The protein's natural variant, known as in strain: Isolate SAS-6, features a modification of the amino acid from I to T at position 229.
+The protein's natural variant, known as acts as a disease modifier in patients with aminoglycoside-induced deafness and a mutation in mitochondrial 12S rRNA; affects tRNA processing by decreasing thiolation and increasing aminoacylation of tRNAs; the mutant has lower thermal stability than wild-type; does not affect import in the mitochondria;, features a modification of the amino acid from A to S at position 10.
+The protein's natural variant, known as in LFIT;, features a modification of the amino acid from Y to H at position 77.
+The protein's natural variant, known as in LFIT;, features a modification of the amino acid from G to D at position 272.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from R to C at position 750.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from T to M at position 145.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from S to T at position 239.
+The protein's natural variant, known as in CPPB2, features a modification of the amino acid from C to G at position 340.
+The protein's natural variant, known as in CPPB2;, features a modification of the amino acid from R to S at position 365.
+The protein's natural variant, known as in CPPB2, features a modification of the amino acid from F to I at position 417.
+The protein's natural variant, known as in CPPB2;, features a modification of the amino acid from H to Q at position 420.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from T to P at position 176.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from K to N at position 420.
+The natural variant of this protein is characterized by an amino acid alteration from V to A at position 353.
+The protein's natural variant, known as in IMD88; loss of binding to DNA; loss of transcriptional activity shown in IFNG promoter-driven luciferase assay; unable to activate IFNG production, features a modification of the amino acid from EM to SL at position 157.
+The protein's natural variant, known as in BOMOS; loss of localization at the plasma membrane, features a modification of the amino acid from S to P at position 148.
+The protein's natural variant, known as in BOMOS; loss of localization at the plasma membrane, features a modification of the amino acid from D to V at position 363.
+The protein's natural variant, known as in strain: MS21; loss of lycopene cyclase activity, features a modification of the amino acid from E to K at position 78.
+The protein's natural variant, known as in strain: MS35; loss of lycopene cyclase activity, features a modification of the amino acid from T to I at position 86.
+The protein's natural variant, known as in strain: MS36; loss of phytoene cyclase activity, features a modification of the amino acid from D to G at position 409.
+The protein's natural variant, known as in HTX4;, features a modification of the amino acid from R to H at position 40.
+The protein's natural variant, known as in HTX4;, features a modification of the amino acid from V to I at position 494.
+The protein's natural variant, known as in strain: ZBMEL131, features a modification of the amino acid from H to N at position 49.
+The protein's natural variant, known as in strain: ZBMEL145 and ZBMEL186, features a modification of the amino acid from L to M at position 70.
+The protein's natural variant, known as in strain: ZBMEL84, features a modification of the amino acid from AE to ED at position 100.
+The protein's natural variant, known as in strain: ZBMEL95, features a modification of the amino acid from T to A at position 119.
+The protein's natural variant, known as in strain: ZBMEL229, features a modification of the amino acid from K to T at position 139.
+The protein's natural variant, known as in TRMA, features a modification of the amino acid from D to H at position 93.
+The protein's natural variant, known as in TRMA;, features a modification of the amino acid from S to F at position 143.
+The protein's natural variant, known as in TRMA;, features a modification of the amino acid from G to D at position 172.
+The protein's natural variant, known as in MFDM;, features a modification of the amino acid from R to W at position 262.
+The protein's natural variant, known as in MFDM, features a modification of the amino acid from C to R at position 476.
+The protein's natural variant, known as in MFDM;, features a modification of the amino acid from L to R at position 637.
+The protein's natural variant, known as found in a colorectal sample; somatic mutation, features a modification of the amino acid from A to T at position 189.
+The protein's natural variant, known as found in a colorectal sample; somatic mutation;, features a modification of the amino acid from R to H at position 231.
+The protein's natural variant, known as found in a colorectal sample; somatic mutation;, features a modification of the amino acid from P to H at position 286.
+The protein's natural variant, known as found in a colorectal sample; somatic mutation;, features a modification of the amino acid from P to R at position 286.
+The protein's natural variant, known as found in a colorectal sample; somatic mutation, features a modification of the amino acid from F to S at position 367.
+The protein's natural variant, known as in CRCS12; associated with disease susceptibility;, features a modification of the amino acid from V to L at position 411.
+The protein's natural variant, known as in CRCS12; associated with disease susceptibility;, features a modification of the amino acid from L to V at position 424.
+The protein's natural variant, known as found in a colorectal sample; somatic mutation;, features a modification of the amino acid from P to R at position 436.
+The protein's natural variant, known as in CRCS12, features a modification of the amino acid from Y to F at position 458.
+The protein's natural variant, known as found in a colorectal sample; somatic mutation, features a modification of the amino acid from S to F at position 459.
+The protein's natural variant, known as found in a colorectal sample; somatic mutation;, features a modification of the amino acid from R to W at position 762.
+The protein's natural variant, known as found in a colorectal sample; somatic mutation, features a modification of the amino acid from K to N at position 777.
+The protein's natural variant, known as in IMAGEI; unknown pathological significance;, features a modification of the amino acid from A to P at position 1007.
+The protein's natural variant, known as found in a colorectal sample; somatic mutation, features a modification of the amino acid from K to N at position 1008.
+The protein's natural variant, known as found in a colorectal sample; somatic mutation, features a modification of the amino acid from L to V at position 1255.
+The protein's natural variant, known as found in a colorectal sample; somatic mutation;, features a modification of the amino acid from V to M at position 1368.
+The protein's natural variant, known as found in a colorectal sample; somatic mutation;, features a modification of the amino acid from R to C at position 1382.
+The natural variant of this protein is characterized by an amino acid alteration from P to S at position 1421.
+The protein's natural variant, known as found in a colorectal sample; somatic mutation;, features a modification of the amino acid from D to N at position 1752.
+The protein's natural variant, known as found in a colorectal sample; somatic mutation, features a modification of the amino acid from I to T at position 1925.
+The natural variant of this protein is characterized by an amino acid alteration from D to N at position 2013.
+The protein's natural variant, known as found in a colorectal sample; somatic mutation;, features a modification of the amino acid from A to T at position 2056.
+The protein's natural variant, known as found in a colorectal sample; somatic mutation, features a modification of the amino acid from A to V at position 2213.
+The protein's natural variant, known as in the cold-sensitive allele sen2-3; defective in cleavage only at the 5'-splice site of tRNA precursors, features a modification of the amino acid from G to E at position 292.
+The protein's natural variant, known as in strain: Czech II, features a modification of the amino acid from P to S at position 1384.
+The protein's natural variant, known as in strain: Czech II, features a modification of the amino acid from N to D at position 1658.
+The protein's natural variant, known as in strain: Czech II, features a modification of the amino acid from S to G at position 1682.
+The protein's natural variant, known as in FANCG; associated with a mild clinical phenotype; disruption of HES1-binding; no effect on FANCA-binding, features a modification of the amino acid from L to P at position 71.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from A to T at position 607.
+The protein's natural variant, known as in strain: PAC174, features a modification of the amino acid from DA to ES at position 149.
+The protein's natural variant, known as in strain: PAC174, features a modification of the amino acid from R to A at position 195.
+The natural variant of this protein is characterized by an amino acid alteration from H to W at position 62.
+The protein's natural variant, known as in ENFL1;, features a modification of the amino acid from S to F at position 280.
+The protein's natural variant, known as in ENFL1, features a modification of the amino acid from S to L at position 280.
+The protein's natural variant, known as in DRRS;, features a modification of the amino acid from H to R at position 888.
+The protein's natural variant, known as in LQT12; leads to a gain of function of the voltage dependent sodium channel;, features a modification of the amino acid from A to G at position 257.
+The protein's natural variant, known as in LQT12; results in released inhibition of nNOS, S-nitrosylation of SCN5A and increased late sodium current;, features a modification of the amino acid from A to V at position 390.
+The protein's natural variant, known as in SPG83;, features a modification of the amino acid from G to D at position 50.
+The protein's natural variant, known as in NEDSWMA; unknown pathological significance; decreased protein abundance;, features a modification of the amino acid from W to R at position 157.
+The protein's natural variant, known as in NEDSWMA; unknown pathological significance; decreased protein abundance;, features a modification of the amino acid from C to Y at position 168.
+The protein's natural variant, known as in NEDSWMA;, features a modification of the amino acid from L to P at position 176.
+The protein's natural variant, known as in NEDSWMA; unknown pathological significance; decreased protein abundance;, features a modification of the amino acid from W to C at position 179.
+The protein's natural variant, known as in NEDSWMA; unknown pathological significance, features a modification of the amino acid from L to P at position 217.
+The protein's natural variant, known as in NEDSWMA; unknown pathological significance;, features a modification of the amino acid from L to P at position 234.
+The protein's natural variant, known as in NEDSWMA; unknown pathological significance, features a modification of the amino acid from L to P at position 248.
+The protein's natural variant, known as in NEDSWMA; unknown pathological significance;, features a modification of the amino acid from H to Q at position 251.
+The protein's natural variant, known as in NEDSWMA; unknown pathological significance;, features a modification of the amino acid from G to E at position 260.
+The protein's natural variant, known as in NEDSWMA; unknown pathological significance;, features a modification of the amino acid from I to T at position 266.
+The protein's natural variant, known as in SPG83; unknown pathological significance;, features a modification of the amino acid from Y to H at position 287.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from C to F at position 842.
+The protein's natural variant, known as no changes in receptor binding or functional signaling;, features a modification of the amino acid from R to K at position 63.
+The protein's natural variant, known as no changes in receptor binding or functional signaling;, features a modification of the amino acid from R to Q at position 152.
+The protein's natural variant, known as in CMD1C;, features a modification of the amino acid from S to L at position 189.
+The protein's natural variant, known as in CMD1C;, features a modification of the amino acid from T to I at position 206.
+The protein's natural variant, known as in CMD1C;, features a modification of the amino acid from I to M at position 345.
+The protein's natural variant, known as in CMD1C;, features a modification of the amino acid from D to N at position 673.
+The protein's natural variant, known as in strain: Russet Burbank-0, alleles 1, 2 and 3, features a modification of the amino acid from A to T at position 3.
+The protein's natural variant, known as in strain: Russet Burbank-0, allele 1, features a modification of the amino acid from S to N at position 138.
+The protein's natural variant, known as in strain: Russet Burbank-0, allele 1, features a modification of the amino acid from H to Y at position 206.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from D to G at position 42.
+The protein's natural variant, known as in NPHS23; decreased localization to cell membrane due to intracellular retention; affects integrity of podocyte cell-cell junctions and leads to altered cellular permeability;, features a modification of the amino acid from R to C at position 440.
+The protein's natural variant, known as in NPHS23; unknown pathological significance; affects integrity of podocyte cell-cell junctions and leads to altered cellular permeability;, features a modification of the amino acid from S to L at position 573.
+The protein's natural variant, known as in CILD42; reduced number of cilia and basal bodies;, features a modification of the amino acid from G to D at position 366.
+The protein's natural variant, known as in CILD42; reduced expression; reduced number of cilia and basal bodies;, features a modification of the amino acid from R to H at position 381.
+The protein's natural variant, known as in UMS, features a modification of the amino acid from L to P at position 143.
+The protein's natural variant, known as in UMS, features a modification of the amino acid from Y to S at position 149.
+The natural variant of this protein is characterized by an amino acid alteration from P to S at position 18.
+The natural variant of this protein is characterized by an amino acid alteration from Y to F at position 61.
+The protein's natural variant, known as in CGD3; the protein remains cytosolic, does not localize to phagosomes or endosomes and is unable to bind phosphatidylinositol 3-phosphate (PtdIns(3)P) in a lipid-binding assay; unable to rescue the NADPH-oxidase defect of NCF4 functionally null cells;, features a modification of the amino acid from R to Q at position 105.
+The natural variant of this protein is characterized by an amino acid alteration from L to I at position 147.
+The protein's natural variant, known as found in patients with neuropsychiatric disorders; unknown pathological significance; disrupts synaptic localization;, features a modification of the amino acid from R to C at position 12.
+The protein's natural variant, known as in PHMDS;, features a modification of the amino acid from P to A at position 141.
+The protein's natural variant, known as found in patients with neuropsychiatric disorders; unknown pathological significance; disrupts synaptic localization;, features a modification of the amino acid from R to C at position 300.
+The protein's natural variant, known as found in a patient with neuropsychiatric disorders; unknown pathological significance, features a modification of the amino acid from Q to R at position 321.
+The protein's natural variant, known as found in patient with neuropsychiatric disorders; unknown pathological significance;, features a modification of the amino acid from S to L at position 341.
+The natural variant of this protein is characterized by an amino acid alteration from H to Q at position 493.
+The protein's natural variant, known as in SCZD15;, features a modification of the amino acid from R to W at position 536.
+The natural variant of this protein is characterized by an amino acid alteration from A to T at position 720.
+The natural variant of this protein is characterized by an amino acid alteration from A to G at position 963.
+The protein's natural variant, known as found in a patient with neuropsychiatric disorders; unknown pathological significance;, features a modification of the amino acid from A to S at position 970.
+The natural variant of this protein is characterized by an amino acid alteration from G to V at position 1010.
+The protein's natural variant, known as found in a patient with neuropsychiatric disorders; unknown pathological significance;, features a modification of the amino acid from A to T at position 1173.
+The protein's natural variant, known as found in a patient with neuropsychiatric disorders; unknown pathological significance;, features a modification of the amino acid from P to L at position 1263.
+The protein's natural variant, known as found in a patient with neuropsychiatric disorders; unknown pathological significance;, features a modification of the amino acid from L to V at position 1406.
+The protein's natural variant, known as found in a patient with neuropsychiatric disorders; unknown pathological significance;, features a modification of the amino acid from M to T at position 1443.
+The protein's natural variant, known as in PHMDS, features a modification of the amino acid from A to S at position 1452.
+The protein's natural variant, known as found in a patient with neuropsychiatric disorders; unknown pathological significance;, features a modification of the amino acid from G to S at position 1557.
+The natural variant of this protein is characterized by an amino acid alteration from P to T at position 1645.
+The protein's natural variant, known as found in patients with neuropsychiatric disorders; unknown pathological significance;, features a modification of the amino acid from P to T at position 1654.
+The natural variant of this protein is characterized by an amino acid alteration from S to C at position 97.
+The natural variant of this protein is characterized by an amino acid alteration from I to M at position 113.
+The protein's natural variant, known as in CMT4J;, features a modification of the amino acid from L to P at position 17.
+The protein's natural variant, known as in CMT4J; the mutant protein is unstable; low levels of the protein results from impaired interaction with VAC14;, features a modification of the amino acid from I to T at position 41.
+The protein's natural variant, known as in ALS11;, features a modification of the amino acid from D to Y at position 53.
+The protein's natural variant, known as in YVS; complete loss of function mutation;, features a modification of the amino acid from G to D at position 104.
+The protein's natural variant, known as in YVS; complete loss of function mutation;, features a modification of the amino acid from L to P at position 175.
+The protein's natural variant, known as in CMT4J; loss of function;, features a modification of the amino acid from E to K at position 302.
+The protein's natural variant, known as in BTOP; partial loss of function;, features a modification of the amino acid from D to V at position 783.
+The protein's natural variant, known as in strain: GN346, features a modification of the amino acid from R to A at position 97.
+The protein's natural variant, known as in strain: GN346, features a modification of the amino acid from G to D at position 143.
+The protein's natural variant, known as in strain: GN346, features a modification of the amino acid from V to I at position 145.
+The protein's natural variant, known as in strain: GN346, features a modification of the amino acid from E to A at position 150.
+The protein's natural variant, known as in strain: GN346, features a modification of the amino acid from S to P at position 185.
+The protein's natural variant, known as in strain: GN346, features a modification of the amino acid from L to R at position 224.
+The protein's natural variant, known as in strain: GN346, features a modification of the amino acid from V to L at position 243.
+The protein's natural variant, known as in strain: GN346, features a modification of the amino acid from A to V at position 325.
+The protein's natural variant, known as in strain: GN346, features a modification of the amino acid from A to V at position 368.
+The protein's natural variant, known as in allele Ren-1D, features a modification of the amino acid from W to R at position 58.
+The protein's natural variant, known as in allele Ren-1D, features a modification of the amino acid from T to I at position 68.
+The protein's natural variant, known as in allele Ren-1D; requires 2 nucleotide substitutions, features a modification of the amino acid from S to V at position 160.
+The protein's natural variant, known as in allele Ren-1D, features a modification of the amino acid from E to D at position 315.
+The protein's natural variant, known as in allele Ren-1D, features a modification of the amino acid from N to Y at position 352.
+The protein's natural variant, known as in ASD4; significant gain of function in sequence-specific DNA binding transcription factor activity; gain of function in sequence-specific DNA binding transcription factor activity in the presence of cotranscription factors NKX2-5 and GATA4 or GATA5;, features a modification of the amino acid from I to M at position 121.
+The protein's natural variant, known as in ASD4; gain of function in sequence-specific DNA binding transcription factor activity; gain of function in sequence-specific DNA binding transcription factor activity in the presence of cotranscription factors NKX2-5 and GATA4 or GATA5;, features a modification of the amino acid from I to M at position 152.
+The protein's natural variant, known as in DEAPLE; unknown pathological significance;, features a modification of the amino acid from R to H at position 80.
+The protein's natural variant, known as in CMTRIB; severely affects enzyme activity;, features a modification of the amino acid from L to H at position 105.
+The protein's natural variant, known as in DFNB89;, features a modification of the amino acid from Y to H at position 145.
+The protein's natural variant, known as in LEPID; does not rescue the developmental defects caused by KARS1 depletion in xenopus, features a modification of the amino acid from G to D at position 189.
+The protein's natural variant, known as in DEAPLE and LEPID; reduces interaction with AIMP2. Reduces tRNA-lysine aminoacylation, features a modification of the amino acid from P to L at position 200.
+The protein's natural variant, known as in DEAPLE; reduces interaction with AIMP2. Reduces tRNA-lysine aminoacylation;, features a modification of the amino acid from F to V at position 263.
+The protein's natural variant, known as in CMTRIB;, features a modification of the amino acid from I to M at position 274.
+The protein's natural variant, known as in DFNB89;, features a modification of the amino acid from D to N at position 349.
+The protein's natural variant, known as found in a patient with hypertrophic cardiomyopathy and mild intellectual disability together with proximal muscle weakness; unknown pathological significance, features a modification of the amino acid from L to H at position 350.
+The protein's natural variant, known as found in a patient with hypertrophic cardiomyopathy and mild intellectual disability together with proximal muscle weakness; unknown pathological significance, features a modification of the amino acid from P to R at position 390.
+The protein's natural variant, known as in LEPID; unknown pathological significance;, features a modification of the amino acid from R to W at position 438.
+The protein's natural variant, known as in DEAPLE; unknown pathological significance, features a modification of the amino acid from V to F at position 448.
+The protein's natural variant, known as in DEAPLE and LEPID; decreases tRNA-lysine aminoacylation; induces protein aggregation; releases from the subunit complex; no effect on cytoplasmic location; no effect on oligomerization;, features a modification of the amino acid from R to H at position 477.
+The protein's natural variant, known as in DEAPLE; decreases tRNA-lysine aminoacylation; slightly induces protein aggregation; no effect on cytoplasmic location; no effect on oligomerization;, features a modification of the amino acid from P to S at position 505.
+The protein's natural variant, known as in LEPID; unknown pathological significance;, features a modification of the amino acid from E to K at position 525.
+The protein's natural variant, known as in LEPID; decreases tRNA-lysine aminoacylation activity of both the mitochondrial and cytosolic forms. Does not rescue the developmental defects caused by KARS1 depletion in xenopus, features a modification of the amino acid from L to F at position 568.
+The protein's natural variant, known as in MDDGA8;, features a modification of the amino acid from R to H at position 158.
+The protein's natural variant, known as in MDDGC8; no effect on protein expression; unchanged localization to the endoplasmic reticulum; decreased protein O-GlcNAc transferase catalytic activity, features a modification of the amino acid from M to T at position 165.
+The protein's natural variant, known as in MDDGC8; no effect on protein expression; unchanged localization to the endoplasmic reticulum; decreased protein O-GlcNAc transferase catalytic activity;, features a modification of the amino acid from P to L at position 253.
+The protein's natural variant, known as in GHDP; affects cell-surface expression; impairs constitutive activity; does not affect the ability to respond to ghrelin;, features a modification of the amino acid from A to E at position 204.
+The protein's natural variant, known as in GHDP; results in partial loss of constitutive activity of the receptor; does not affect response to ghrelin; does not affect receptor cell-surface expression;, features a modification of the amino acid from R to W at position 237.
+The natural variant of this protein is characterized by an amino acid alteration from Q to H at position 253.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from I to M at position 175.
+The protein's natural variant, known as in strain: A3969.2, features a modification of the amino acid from V to L at position 153.
+The protein's natural variant, known as in strain: A3969.2, features a modification of the amino acid from S to T at position 274.
+The protein's natural variant, known as in lah, features a modification of the amino acid from Y to S at position 196.
+The protein's natural variant, known as in strain: cv. Triumph, features a modification of the amino acid from C to Y at position 208.
+The protein's natural variant, known as in strain: cv. Triumph, features a modification of the amino acid from H to Q at position 243.
+The protein's natural variant, known as in strain: cv. Triumph, features a modification of the amino acid from R to L at position 378.
+The protein's natural variant, known as associated with low glucose tolerance;, features a modification of the amino acid from P to L at position 387.
+The protein's natural variant, known as in strain: cv. Torsdag, features a modification of the amino acid from S to W at position 360.
+The protein's natural variant, known as in strain: cv. Torsdag, features a modification of the amino acid from S to V at position 411.
+The protein's natural variant, known as in strain: cv. Torsdag, features a modification of the amino acid from I to V at position 417.
+The protein's natural variant, known as in strain: cv. Torsdag, features a modification of the amino acid from P to A at position 560.
+The protein's natural variant, known as in strain: cv. Torsdag, features a modification of the amino acid from P to A at position 566.
+The protein's natural variant, known as in LSDMCA1; loss of function; no effect on localization to mitochondrion;, features a modification of the amino acid from R to C at position 217.
+The protein's natural variant, known as in hcrO221, requires high CO2 levels for growth, features a modification of the amino acid from G to D at position 146.
+The protein's natural variant, known as in PARK8;, features a modification of the amino acid from M to V at position 712.
+The protein's natural variant, known as in PARK8; unknown pathological significance;, features a modification of the amino acid from R to M at position 793.
+The protein's natural variant, known as in PARK8; unknown pathological significance;, features a modification of the amino acid from Q to R at position 930.
+The protein's natural variant, known as in PARK8;, features a modification of the amino acid from R to Q at position 1067.
+The protein's natural variant, known as in PARK8; unknown pathological significance;, features a modification of the amino acid from S to C at position 1096.
+The protein's natural variant, known as in PARK8;, features a modification of the amino acid from I to V at position 1122.
+The protein's natural variant, known as in PARK8;, features a modification of the amino acid from S to T at position 1228.
+The protein's natural variant, known as found in a renal cell carcinoma sample; somatic mutation, features a modification of the amino acid from K to I at position 1359.
+The protein's natural variant, known as in PARK8; unknown pathological significance;, features a modification of the amino acid from I to V at position 1371.
+The protein's natural variant, known as in PARK8; shows an increase in activity in both autophosphorylation and phosphorylation of a generic substrate; loss of interaction with SEC16A; shows an increase in activity in phosphorylation of RAB10; decreases phosphorylation-dependent binding to YWHAG;, features a modification of the amino acid from R to C at position 1441.
+The protein's natural variant, known as in PARK8; shows a progressive reduction in neurite length and branching; shows an increase in activity in phosphorylation of RAB8A and RAB10; decreases phosphorylation-dependent binding to YWHAG;, features a modification of the amino acid from R to G at position 1441.
+The protein's natural variant, known as in PARK8; shows an increase in activity in phosphorylation of RAB8A and RAB10; decreases phosphorylation-dependent binding to YWHAG;, features a modification of the amino acid from R to H at position 1441.
+The protein's natural variant, known as in PARK8; unknown pathological significance;, features a modification of the amino acid from R to Q at position 1514.
+The protein's natural variant, known as in PARK8; unknown pathological significance;, features a modification of the amino acid from P to S at position 1542.
+The protein's natural variant, known as in an ovarian mucinous carcinoma sample; somatic mutation;, features a modification of the amino acid from R to Q at position 1550.
+The protein's natural variant, known as in PARK8; unknown pathological significance;, features a modification of the amino acid from V to E at position 1598.
+The protein's natural variant, known as may be associated with Parkinson disease in some populations;, features a modification of the amino acid from R to P at position 1628.
+The protein's natural variant, known as in PARK8; shows no progressive reduction in neurite length and branching; no loss of interaction with SEC16A; shows an increase in activity in phosphorylation of RAB8A and RAB10;, features a modification of the amino acid from Y to C at position 1699.
+The protein's natural variant, known as in an ovarian serous carcinoma sample; somatic mutation, features a modification of the amino acid from R to P at position 1723.
+The protein's natural variant, known as in PARK8; shows an increase in activity in phosphorylation of RAB8A and RAB10;, features a modification of the amino acid from R to H at position 1728.
+The protein's natural variant, known as in PARK8;, features a modification of the amino acid from R to L at position 1728.
+The protein's natural variant, known as in PARK8; unknown pathological significance;, features a modification of the amino acid from M to T at position 1869.
+The protein's natural variant, known as does not inhibit interaction with RAB29; shows a progressive increase in neurite length and branching, features a modification of the amino acid from K to M at position 1906.
+The protein's natural variant, known as in PARK8;, features a modification of the amino acid from R to H at position 1941.
+The protein's natural variant, known as in PARK8; unknown pathological significance;, features a modification of the amino acid from I to T at position 2012.
+The protein's natural variant, known as in PARK8; shows an increase in activity in both autophosphorylation and phosphorylation of a generic substrate; results in increased PRDX3 phosphorylation promoting dysregulation of mitochondrial function and oxidative damage; results in increased APP phosphorylation on 'T-743' promoting neurotoxicity in dopaminergic neurons; shows increased kinase activity in the phosphorylation of RAB10; does not inhibit interaction with RAB29; shows a progressive reduction in neurite length and branching; shows distinctive spheroid-like inclusions within both neuronal processes and at intracellular membranous structures; shows lysosomal swelling and reduced retrograde transport of selective cargo between lysosomes and the Golgi apparatus; shows apoptotic mechanism of cell death; no loss of interaction with SEC16A;, features a modification of the amino acid from G to S at position 2019.
+The protein's natural variant, known as in PARK8; significant increase in autophosphorylation of about 40% in comparison to wild-type protein in vitro; shows a progressive reduction in neurite length and branching; shows an increase in activity in phosphorylation of RAB8A and RAB10;, features a modification of the amino acid from I to T at position 2020.
+The protein's natural variant, known as in PARK8; shows an increase in activity in phosphorylation of RAB8A and RAB10;, features a modification of the amino acid from T to S at position 2031.
+The protein's natural variant, known as in PARK8;, features a modification of the amino acid from T to M at position 2141.
+The protein's natural variant, known as in PARK8;, features a modification of the amino acid from R to H at position 2143.
+The protein's natural variant, known as in PARK8; shows decreased WD domain homodimerization; no effect on kinase activity;, features a modification of the amino acid from D to H at position 2175.
+The protein's natural variant, known as in PARK8; no effect on WD domain homodimerization; no effect on kinase activity;, features a modification of the amino acid from Y to C at position 2189.
+The protein's natural variant, known as in PARK8; shows decreased WD domain homodimerization; no effect on kinase activity;, features a modification of the amino acid from T to I at position 2356.
+The protein's natural variant, known as in PARK8; under conditions of oxidative stress the variant protein is more toxic and is associated with a higher rate of apoptosis; reduced binding to synaptic vesicles; no loss of interaction with SEC16A; shows an increase in activity in phosphorylation of RAB8A and RAB10; shows decreased WD domain homodimerization; reduced autophosphorylation at Ser-935;, features a modification of the amino acid from G to R at position 2385.
+The protein's natural variant, known as in PARK8; shows decreased WD domain homodimerization; no effect on kinase activity;, features a modification of the amino acid from V to M at position 2390.
+The protein's natural variant, known as in PARK8; shows decreased WD domain homodimerization; no effect on kinase activity;, features a modification of the amino acid from L to I at position 2439.
+The protein's natural variant, known as in PARK8;, features a modification of the amino acid from L to H at position 2466.
+The protein's natural variant, known as in DFNA80; unknown pathological significance, features a modification of the amino acid from T to I at position 116.
+The protein's natural variant, known as in RHDA3, features a modification of the amino acid from R to H at position 128.
+The protein's natural variant, known as in RHDA3, features a modification of the amino acid from R to L at position 192.
+The protein's natural variant, known as able to rescue renal hypoplasia in zebrafish morphants;, features a modification of the amino acid from R to Q at position 241.
+The protein's natural variant, known as in RHDA3, features a modification of the amino acid from G to V at position 273.
+The protein's natural variant, known as in DFNA80; unknown pathological significance, features a modification of the amino acid from N to S at position 283.
+The protein's natural variant, known as in RHDA3;, features a modification of the amino acid from R to Q at position 328.
+The protein's natural variant, known as in RHDA3, features a modification of the amino acid from A to G at position 497.
+The protein's natural variant, known as in RHDA3, features a modification of the amino acid from S to R at position 605.
+The protein's natural variant, known as in RHDA3, features a modification of the amino acid from L to F at position 716.
+The protein's natural variant, known as in RHDA3;, features a modification of the amino acid from R to C at position 751.
+The protein's natural variant, known as in RHDA3;, features a modification of the amino acid from R to H at position 751.
+The protein's natural variant, known as in RHDA3;, features a modification of the amino acid from E to Q at position 761.
+The protein's natural variant, known as able to rescue renal hypoplasia in zebrafish morphants;, features a modification of the amino acid from A to V at position 926.
+The protein's natural variant, known as in RHDA3; probable loss of function; does not rescue renal hypoplasia in zebrafish morphants;, features a modification of the amino acid from R to P at position 1066.
+The protein's natural variant, known as in RHDA3, features a modification of the amino acid from M to T at position 1502.
+The protein's natural variant, known as in RHDA3;, features a modification of the amino acid from D to V at position 1509.
+The protein's natural variant, known as in RHDA3;, features a modification of the amino acid from H to R at position 1536.
+The protein's natural variant, known as in RHDA3, features a modification of the amino acid from V to A at position 1549.
+The protein's natural variant, known as in RHDA3;, features a modification of the amino acid from R to S at position 1558.
+The protein's natural variant, known as in RHDA3; probable loss of function; does not rescue renal hypoplasia in zebrafish morphants;, features a modification of the amino acid from L to P at position 1567.
+The protein's natural variant, known as in RHDA3, features a modification of the amino acid from A to V at position 1576.
+The protein's natural variant, known as in RHDA3;, features a modification of the amino acid from V to I at position 1615.
+The protein's natural variant, known as in RHDA3; probable loss of function; does not rescue renal hypoplasia in zebrafish morphants, features a modification of the amino acid from I to T at position 1655.
+The protein's natural variant, known as in RHDA3, features a modification of the amino acid from Y to C at position 1664.
+The protein's natural variant, known as in RHDA3; probable loss of function; does not rescue renal hypoplasia in zebrafish morphants;, features a modification of the amino acid from V to M at position 1690.
+The protein's natural variant, known as in RHDA3, features a modification of the amino acid from D to N at position 1775.
+The protein's natural variant, known as in RHDA3;, features a modification of the amino acid from L to R at position 1793.
+The protein's natural variant, known as in RHDA3;, features a modification of the amino acid from R to H at position 1884.
+The protein's natural variant, known as in COXPD43; affects assembly or stability of the translocase, features a modification of the amino acid from V to L at position 33.
+The protein's natural variant, known as in allele suppressor SLC1-1, features a modification of the amino acid from Q to L at position 44.
+The protein's natural variant, known as in strain: NSY, features a modification of the amino acid from T to A at position 222.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from G to W at position 52.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from G to W at position 100.
+The protein's natural variant, known as found in a family with atypical autism and severe epilepsy; unknown pathological significance;, features a modification of the amino acid from M to V at position 270.
+The protein's natural variant, known as in CYSRD; may impair splicing; hypomorphic mutation;, features a modification of the amino acid from E to G at position 932.
+The protein's natural variant, known as in 50% of the molecules, features a modification of the amino acid from V to I at position 2.
+The protein's natural variant, known as in CILD19; unknown pathological significance, features a modification of the amino acid from N to K at position 61.
+The protein's natural variant, known as in CILD19; unknown pathological significance;, features a modification of the amino acid from A to P at position 74.
+The protein's natural variant, known as in CILD19; no effect on interaction with ZMYND10, features a modification of the amino acid from C to R at position 87.
+The protein's natural variant, known as in CILD19; no effect on interaction with ZMYND10; reduced expression in cytoplasm; decreased expression of inner and outer dynein proteins; mislocation of inner and outer dynein proteins;, features a modification of the amino acid from D to H at position 146.
+The protein's natural variant, known as in strain: Isolate Deca, features a modification of the amino acid from Q to E at position 537.
+The protein's natural variant, known as in XSCID, features a modification of the amino acid from D to N at position 39.
+The protein's natural variant, known as in XSCID, features a modification of the amino acid from C to G at position 62.
+The protein's natural variant, known as in XSCID, features a modification of the amino acid from E to G at position 68.
+The protein's natural variant, known as in XSCID;, features a modification of the amino acid from E to K at position 68.
+The protein's natural variant, known as in XSCID, features a modification of the amino acid from N to K at position 84.
+The protein's natural variant, known as in XSCID, features a modification of the amino acid from Y to C at position 89.
+The protein's natural variant, known as in XSCID;, features a modification of the amino acid from Y to C at position 105.
+The protein's natural variant, known as in XSCID;, features a modification of the amino acid from G to D at position 114.
+The protein's natural variant, known as in XSCID, features a modification of the amino acid from C to F at position 115.
+The protein's natural variant, known as in XSCID; atypical;, features a modification of the amino acid from C to R at position 115.
+The protein's natural variant, known as in XSCID, features a modification of the amino acid from H to P at position 123.
+The protein's natural variant, known as in XSCID, features a modification of the amino acid from Y to N at position 125.
+The protein's natural variant, known as in XSCID, features a modification of the amino acid from Q to P at position 144.
+The protein's natural variant, known as in XSCID;, features a modification of the amino acid from I to N at position 153.
+The protein's natural variant, known as in XSCID;, features a modification of the amino acid from A to V at position 156.
+The protein's natural variant, known as in XSCID, features a modification of the amino acid from L to H at position 162.
+The protein's natural variant, known as in XSCID, features a modification of the amino acid from L to P at position 172.
+The protein's natural variant, known as in XSCID, features a modification of the amino acid from L to Q at position 172.
+The protein's natural variant, known as in XSCID, features a modification of the amino acid from C to R at position 182.
+The protein's natural variant, known as in XSCID, features a modification of the amino acid from L to S at position 183.
+The protein's natural variant, known as in XCID;, features a modification of the amino acid from R to C at position 222.
+The protein's natural variant, known as in XSCID;, features a modification of the amino acid from R to W at position 224.
+The protein's natural variant, known as in XSCID;, features a modification of the amino acid from R to C at position 226.
+The protein's natural variant, known as in XSCID;, features a modification of the amino acid from R to H at position 226.
+The protein's natural variant, known as in XSCID, features a modification of the amino acid from F to C at position 227.
+The protein's natural variant, known as in XSCID, features a modification of the amino acid from L to P at position 230.
+The protein's natural variant, known as in XSCID, features a modification of the amino acid from C to Y at position 231.
+The protein's natural variant, known as in XSCID;, features a modification of the amino acid from G to R at position 232.
+The protein's natural variant, known as in XSCID, features a modification of the amino acid from W to WQHW at position 237.
+The protein's natural variant, known as in XSCID, features a modification of the amino acid from W to C at position 240.
+The protein's natural variant, known as in XSCID, features a modification of the amino acid from S to I at position 241.
+The protein's natural variant, known as in XSCID, features a modification of the amino acid from M to R at position 270.
+The protein's natural variant, known as in XSCID;, features a modification of the amino acid from R to Q at position 285.
+The protein's natural variant, known as in XCID;, features a modification of the amino acid from L to Q at position 293.
+The protein's natural variant, known as in BRYLIB2; unknown pathological significance; no effect on protein abundance, features a modification of the amino acid from A to V at position 8.
+The protein's natural variant, known as in BRYLIB2, features a modification of the amino acid from R to C at position 9.
+The protein's natural variant, known as in BRYLIB1, features a modification of the amino acid from R to G at position 9.
+The protein's natural variant, known as in BRYLIB1, features a modification of the amino acid from R to S at position 9.
+The protein's natural variant, known as in BRYLIB2; unknown pathological significance; no effect on protein abundance, features a modification of the amino acid from K to E at position 10.
+The protein's natural variant, known as in BRYLIB2; unknown pathological significance, features a modification of the amino acid from S to P at position 11.
+The protein's natural variant, known as in BRYLIB2; unknown pathological significance, features a modification of the amino acid from G to R at position 14.
+The protein's natural variant, known as in BRYLIB1; unknown pathological significance, features a modification of the amino acid from A to G at position 16.
+The protein's natural variant, known as in BRYLIB1, features a modification of the amino acid from R to G at position 18.
+The protein's natural variant, known as in BRYLIB1; unknown pathological significance, features a modification of the amino acid from T to I at position 23.
+The protein's natural variant, known as in BRYLIB2; unknown pathological significance; no effect on protein abundance, features a modification of the amino acid from T to K at position 23.
+The protein's natural variant, known as in GLM; glioblastoma multiforme samples and diffuse intrinsic pontine glioma; somatic mutation; more prevalent in pediatric than adult malignancies; results in reduced allosteric activation of PRC2 causing a global decrease of H3K27me3 levels; has no effect on H3K4me3 or H3K36me3 levels;, features a modification of the amino acid from K to M at position 28.
+The protein's natural variant, known as in BRYLIB2; unknown pathological significance, features a modification of the amino acid from A to P at position 30.
+The protein's natural variant, known as in BRYLIB1; unknown pathological significance, features a modification of the amino acid from A to T at position 30.
+The protein's natural variant, known as in BRYLIB1; unknown pathological significance, features a modification of the amino acid from S to F at position 32.
+The protein's natural variant, known as in GLM; glioblastoma multiforme samples; somatic mutation; also found in osteosarcoma samples; results in global decrease of H3K36me2 and H3K36me3 levels; has no effect on H3K27me3 levels;, features a modification of the amino acid from G to R at position 35.
+The protein's natural variant, known as in GLM and BRYLIB2; glioblastoma multiforme samples; somatic mutation; affects regulation of gene expression and results in up-regulation of MYCN; results in global decrease of H3K36me2 and H3K36me3 levels; has no effect on H3K27me3 levels, features a modification of the amino acid from G to V at position 35.
+The protein's natural variant, known as probable disease-associated variant found in giant cell tumors of bone; somatic mutation, features a modification of the amino acid from G to W at position 35.
+The protein's natural variant, known as in BRYLIB1, features a modification of the amino acid from K to E at position 37.
+The protein's natural variant, known as probable disease-associated variant found in chondroblastoma and clear cell chondrosarcoma; somatic mutation; also found in a subset of human papillomavirus-negative head and neck squamous cell carcinomas; results in global decrease of H3K36me2 and H3K36me3 levels and increased H3K27me3 levels, features a modification of the amino acid from K to M at position 37.
+The protein's natural variant, known as in BRYLIB2; unknown pathological significance, features a modification of the amino acid from H to R at position 40.
+The protein's natural variant, known as in BRYLIB1; unknown pathological significance, features a modification of the amino acid from H to Y at position 40.
+The protein's natural variant, known as in BRYLIB1; unknown pathological significance; increased protein abundance, features a modification of the amino acid from R to C at position 41.
+The protein's natural variant, known as in BRYLIB1, features a modification of the amino acid from T to I at position 46.
+The protein's natural variant, known as in BRYLIB2; unknown pathological significance, features a modification of the amino acid from L to R at position 49.
+The protein's natural variant, known as in BRYLIB2; unknown pathological significance; decreased protein abundance, features a modification of the amino acid from I to N at position 52.
+The protein's natural variant, known as in BRYLIB1; unknown pathological significance; no effect on protein abundance, features a modification of the amino acid from Q to K at position 56.
+The protein's natural variant, known as in BRYLIB1; unknown pathological significance, features a modification of the amino acid from L to R at position 62.
+The protein's natural variant, known as in BRYLIB1; unknown pathological significance, features a modification of the amino acid from D to N at position 78.
+The protein's natural variant, known as in BRYLIB1; unknown pathological significance, features a modification of the amino acid from D to H at position 82.
+The protein's natural variant, known as in BRYLIB1, features a modification of the amino acid from R to C at position 84.
+The protein's natural variant, known as in BRYLIB1, features a modification of the amino acid from G to R at position 91.
+The protein's natural variant, known as in BRYLIB1 and BRYLIB2; unknown pathological significance, features a modification of the amino acid from N to S at position 109.
+The protein's natural variant, known as in BRYLIB1; unknown pathological significance, features a modification of the amino acid from I to L at position 113.
+The protein's natural variant, known as in BRYLIB1; unknown pathological significance, features a modification of the amino acid from I to V at position 113.
+The protein's natural variant, known as in BRYLIB1; unknown pathological significance, features a modification of the amino acid from V to L at position 118.
+The protein's natural variant, known as in BRYLIB1; decreased protein abundance, features a modification of the amino acid from M to I at position 121.
+The protein's natural variant, known as in BRYLIB1, features a modification of the amino acid from M to K at position 121.
+The protein's natural variant, known as in BRYLIB2, features a modification of the amino acid from M to V at position 121.
+The protein's natural variant, known as in BRYLIB1, features a modification of the amino acid from P to L at position 122.
+The protein's natural variant, known as in BRYLIB1 and BRYLIB2, features a modification of the amino acid from P to R at position 122.
+The protein's natural variant, known as in BRYLIB1 and BRYLIB2, features a modification of the amino acid from Q to R at position 126.
+The protein's natural variant, known as in BRYLIB1; unknown pathological significance, features a modification of the amino acid from R to C at position 129.
+The protein's natural variant, known as in BRYLIB1; unknown pathological significance; decreased protein abundance; increased interaction with DAXX; not changed subcellular location, features a modification of the amino acid from R to H at position 129.
+The protein's natural variant, known as in DFNB114;, features a modification of the amino acid from Q to L at position 104.
+The protein's natural variant, known as in strain: NG13, features a modification of the amino acid from M to V at position 250.
+The protein's natural variant, known as in strain: NG13, features a modification of the amino acid from L to F at position 425.
+The protein's natural variant, known as in strain: NG13, features a modification of the amino acid from R to S at position 465.
+The protein's natural variant, known as associated with the impaired acrosomal reaction phenotype, features a modification of the amino acid from H to N at position 174.
+The natural variant of this protein is characterized by an amino acid alteration from C to R at position 229.
+The protein's natural variant, known as in cly5; temperature-sensitive mutation that cause cell lysis at high temperature, features a modification of the amino acid from T to I at position 958.
+The protein's natural variant, known as in cly7; temperature-sensitive mutation that cause cell lysis at high temperature, features a modification of the amino acid from P to S at position 1023.
+The protein's natural variant, known as in DURS2; behaves as a dominant gain-of-function allele that increases CHN1 activity in vitro; appears to enhance membrane translocation and CHN1 activity by destabilizing the closed conformation of CHN1 protein in response to phorbol 12-myristate 13-acetate (PMA);, features a modification of the amino acid from L to F at position 20.
+The protein's natural variant, known as in DURS2; behaves as a dominant gain-of -function allele that increases CHN1 activity in vitro;, features a modification of the amino acid from I to M at position 126.
+The protein's natural variant, known as in DURS2; behaves as a dominant gain-of-function allele that increases CHN1 activity in vitro; appears to enhance membrane translocation and CHN1 activity by destabilizing the closed conformation of CHN1 protein in response to phorbol 12-myristate 13-acetate (PMA);, features a modification of the amino acid from Y to H at position 143.
+The protein's natural variant, known as in DURS2; behaves as a dominant gain-of-function allele that increases CHN1 activity in vitro; appears to enhance membrane translocation and CHN1 activity by destabilizing the closed conformation of CHN1 protein in response to phorbol 12-myristate 13-acetate (PMA);, features a modification of the amino acid from A to V at position 223.
+The protein's natural variant, known as in DURS2; behaves as a dominant gain-of-function allele that increases CHN1 activity in vitro;, features a modification of the amino acid from G to S at position 228.
+The protein's natural variant, known as in DURS2; behaves as a dominant gain-of-function allele that increases CHN1 activity in vitro; appears to enhance membrane translocation and CHN1 activity by destabilizing the closed conformation of CHN1 protein in response to phorbol 12-myristate 13-acetate (PMA);, features a modification of the amino acid from P to Q at position 252.
+The protein's natural variant, known as in DURS2; behaves as a dominant gain-of-function allele that increases CHN1 activity in vitro;, features a modification of the amino acid from E to K at position 313.
+The protein's natural variant, known as in strain: cv. Wassilewskija, features a modification of the amino acid from Q to QQQQQQQQQQ at position 550.
+The protein's natural variant, known as retained in the ER due to impaired N-glycosylation; may present a vulnerability factor for iron induced oxidative stress in Parkinson disease;, features a modification of the amino acid from I to T at position 63.
+The protein's natural variant, known as reduced ferroxidase activity; may present a vulnerability factor for iron induced oxidative stress in Parkinson disease;, features a modification of the amino acid from D to E at position 544.
+The natural variant of this protein is characterized by an amino acid alteration from I to V at position 117.
+The natural variant of this protein is characterized by an amino acid alteration from M to K at position 148.
+The natural variant of this protein is characterized by an amino acid alteration from E to Q at position 168.
+The protein's natural variant, known as in WS2A; unknown pathological significance;, features a modification of the amino acid from A to T at position 294.
+The protein's natural variant, known as in WS2A; unknown pathological significance, features a modification of the amino acid from R to K at position 310.
+The protein's natural variant, known as in COMMAD; has both cytoplasmic and nuclear localization; decreased binding to M-box or E-box DNA sequences;, features a modification of the amino acid from K to N at position 313.
+The protein's natural variant, known as in TADS;, features a modification of the amino acid from N to K at position 317.
+The protein's natural variant, known as in COMMAD;, features a modification of the amino acid from R to G at position 324.
+The protein's natural variant, known as in WS2A;, features a modification of the amino acid from S to P at position 357.
+The protein's natural variant, known as in WS2A, features a modification of the amino acid from N to D at position 385.
+The protein's natural variant, known as in WS2A;, features a modification of the amino acid from S to P at position 405.
+The protein's natural variant, known as in CMM8; associated with disease susceptibility; also associated with pheochromocytomas and paragangliomas susceptibility; results in impaired sumoylation;, features a modification of the amino acid from E to K at position 425.
+The protein's natural variant, known as in strain: XCPA69 and XCPA112, features a modification of the amino acid from S to N at position 105.
+The protein's natural variant, known as in strain: XCPA4, XCPA7, XCPA25, XCPA51, XCPA77, XCPA93, XCPA102, XCPA105, XCPA122 and XCPA125, features a modification of the amino acid from G to A at position 290.
+The protein's natural variant, known as in strain: C3H/HeJ and DBA/2J; does not change transcriptional activity, features a modification of the amino acid from A to S at position 172.
+The protein's natural variant, known as found in a patient with severe delayed speech, autism spectrum and Gilles de la Tourette disorders, features a modification of the amino acid from P to T at position 667.
+The protein's natural variant, known as in strain: 129/Sv, features a modification of the amino acid from H to Q at position 109.
+The protein's natural variant, known as in strain: C57BL/6 XCBA and 129/Sv, features a modification of the amino acid from A to G at position 168.
+The protein's natural variant, known as in strain: C57BL/6 XCBA, features a modification of the amino acid from R to T at position 449.
+The protein's natural variant, known as in strain: C57BL/6 XCBA, requires 2 nucleotide substitutions, features a modification of the amino acid from R to A at position 492.
+The protein's natural variant, known as in strain: 129/Sv, features a modification of the amino acid from KQ to NE at position 687.
+The protein's natural variant, known as in strain: 129/Sv, features a modification of the amino acid from E to D at position 857.
+The protein's natural variant, known as in strain: C57BL/6 XCBA, features a modification of the amino acid from E to D at position 983.
+The protein's natural variant, known as in strain: C57BL/6 XCBA and 129/Sv, features a modification of the amino acid from N to D at position 1169.
+The protein's natural variant, known as in strain: C57BL/6 XCBA and 129/Sv, features a modification of the amino acid from C to W at position 1329.
+The protein's natural variant, known as in WPW and CMH6; impaired AMP- and ATP-binding;, features a modification of the amino acid from R to Q at position 302.
+The protein's natural variant, known as in CMH6; severe, features a modification of the amino acid from R to RL at position 350.
+The protein's natural variant, known as in CMH6; severe; impaired AMP- and ATP-binding;, features a modification of the amino acid from H to R at position 383.
+The protein's natural variant, known as in CMH6; severe; impaired AMP- and ATP-binding;, features a modification of the amino acid from T to N at position 400.
+The protein's natural variant, known as in CMH6; severe;, features a modification of the amino acid from N to I at position 488.
+The protein's natural variant, known as in WPW; absence of cardiac hypertrophy; onset in childhood; impaired AMP- and ATP-binding;, features a modification of the amino acid from R to G at position 531.
+The protein's natural variant, known as in GSDH; reduction of binding affinities for AMP and ATP; loss of cooperative binding; enhanced basal activity; increased phosphorylation of the alpha-subunit;, features a modification of the amino acid from R to Q at position 531.
+The protein's natural variant, known as found in a patient with Leber congenital amaurosis, features a modification of the amino acid from S to G at position 199.
+The protein's natural variant, known as associated with the development of retinal degeneration in individuals with ciliopathies caused by mutations in other genes; found in patients with Leber congenital amaurosis, Senior-Loken syndrome, Joubert syndrome and Bardet-Biedl syndrome; abrogates interaction with RPGR;, features a modification of the amino acid from A to T at position 229.
+The protein's natural variant, known as in JBTS7;, features a modification of the amino acid from E to K at position 393.
+The protein's natural variant, known as found in a patient with Leber congenital amaurosis;, features a modification of the amino acid from L to F at position 546.
+The protein's natural variant, known as in JBTS7;, features a modification of the amino acid from Q to R at position 550.
+The protein's natural variant, known as in JBTS7; affects interaction with NPHP4;, features a modification of the amino acid from T to P at position 615.
+The protein's natural variant, known as in JBTS7;, features a modification of the amino acid from C to R at position 633.
+The protein's natural variant, known as in COACH3;, features a modification of the amino acid from S to P at position 659.
+The protein's natural variant, known as in JBTS7; also in a patient with Leber congenital amaurosis; affects interaction with NPHP4;, features a modification of the amino acid from T to I at position 677.
+The protein's natural variant, known as in JBTS7; seems not to affect interaction with NPHP4;, features a modification of the amino acid from A to P at position 695.
+The protein's natural variant, known as in a patient with Leber congenital amaurosis;, features a modification of the amino acid from R to L at position 937.
+The protein's natural variant, known as in a patient with Meckel-Gruber like syndrome also carrying L-220 and V-280 in TTC21B; also found in patients with Leber congenital amaurosis and a patient with Bardet-Biedl syndrome;, features a modification of the amino acid from A to G at position 1183.
+The protein's natural variant, known as in MKS5;, features a modification of the amino acid from R to C at position 1236.
+The protein's natural variant, known as in patients with Leber congenital amaurosis, features a modification of the amino acid from D to Y at position 1264.
+The protein's natural variant, known as in strain: LW15, features a modification of the amino acid from H to Y at position 184.
+The protein's natural variant, known as in strain: AF-F, F1-F, F1-1S, JA-F, LW8, MW18 and ZW20, features a modification of the amino acid from V to I at position 329.
+The protein's natural variant, known as in strain: JA-S, features a modification of the amino acid from V to A at position 471.
+The protein's natural variant, known as in GAMOS2;, features a modification of the amino acid from V to F at position 106.
+The protein's natural variant, known as in GAMOS2;, features a modification of the amino acid from F to S at position 137.
+The protein's natural variant, known as in an ovarian serous carcinoma sample; somatic mutation, features a modification of the amino acid from E to Q at position 1413.
+The protein's natural variant, known as in WS2F; unknown pathological significance, features a modification of the amino acid from R to C at position 32.
+The protein's natural variant, known as in FPHH; gain-of-function mutation; sKITLG reveales that the mutant Ser-36 sKITLG increases the content of the melanin by 109% compared with the wild-type sKITLG; tyrosinase activity is significantly increased by the mutant sKITLG compared to wild-type control;, features a modification of the amino acid from N to S at position 36.
+The protein's natural variant, known as in DCUA; loss of cell membrane association, features a modification of the amino acid from HC to R at position 68.
+The protein's natural variant, known as in WS2F; unknown pathological significance; reduces secretion;, features a modification of the amino acid from L to V at position 104.
+The protein's natural variant, known as in WS2F; unknown pathological significance, features a modification of the amino acid from I to T at position 148.
+The protein's natural variant, known as in ANXD3; unknown pathological significance;, features a modification of the amino acid from R to C at position 94.
+The protein's natural variant, known as in ANXD3; unknown pathological significance, features a modification of the amino acid from L to F at position 145.
+The natural variant of this protein is characterized by an amino acid alteration from LP to S at position 14.
+The protein's natural variant, known as found in a patient with polycystic ovary syndrome; unknown pathological significance, features a modification of the amino acid from H to Y at position 500.
+The natural variant of this protein is characterized by an amino acid alteration from S to I at position 73.
+The protein's natural variant, known as in allele DRB1*03:01, allele DRB1*03:02, allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:03, allele DRB1*08:04, allele DRB1*10:01, allele DRB1*11:01, allele DRB1*11:04, allele DRB1*11:06, allele DRB1*11:11, allele DRB1*11:19, allele DRB1*12:01, allele DRB1*12:02, allele DRB1*13:01, allele DRB1*13:02, allele DRB1*13:03, allele DRB1*13:05, allele DRB1*13:07, allele DRB1*13:12, allele DRB1*14:01, allele DRB1*14:03, allele DRB1*14:05, allele DRB1*14:06 and allele DRB1*14:07;, features a modification of the amino acid from K to R at position 5.
+The protein's natural variant, known as in allele DRB1*04:01, allele DRB1*04:02, allele DRB1*04:04, allele DRB1*04:05, allele DRB1*04:06, allele DRB1*04:07, allele DRB1*04:08, allele DRB1*04:10 and allele DRB1*04:11;, features a modification of the amino acid from L to F at position 6.
+The protein's natural variant, known as in allele DRB1*03:01, allele DRB1*03:02, allele DRB1*04:01, allele DRB1*04:02, allele DRB1*04:04, allele DRB1*04:05, allele DRB1*04:06, allele DRB1*04:07, allele DRB1*04:08, allele DRB1*04:10, allele DRB1*04:11, allele DRB1*07:01, allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:03, allele DRB1*08:04, allele DRB1*09:01, allele DRB1*10:01, allele DRB1*11:01, allele DRB1*11:04, allele DRB1*11:06, allele DRB1*11:11, allele DRB1*11:19, allele DRB1*12:01, allele DRB1*12:02, allele DRB1*13:01, allele DRB1*13:02, allele DRB1*13:03, allele DRB1*13:05, allele DRB1*13:07, allele DRB1*13:12, allele DRB1*14:01, allele DRB1*14:03, allele DRB1*14:05, allele DRB1*14:06 and allele DRB1*14:07;, features a modification of the amino acid from T to A at position 13.
+The protein's natural variant, known as in allele DRB1*03:01, allele DRB1*03:02, allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:03, allele DRB1*08:04, allele DRB1*10:01, allele DRB1*11:01, allele DRB1*11:04, allele DRB1*11:06, allele DRB1*11:11, allele DRB1*11:19, allele DRB1*12:01, allele DRB1*12:02, allele DRB1*13:01, allele DRB1*13:02, allele DRB1*13:03, allele DRB1*13:05, allele DRB1*13:07, allele DRB1*13:12, allele DRB1*14:01, allele DRB1*14:03, allele DRB1*14:05, allele DRB1*14:06 and allele DRB1*14:07;, features a modification of the amino acid from A to V at position 14.
+The protein's natural variant, known as in allele DRB1*01:01, allele DRB1*01:02, allele DRB1*03:01, allele DRB1*03:02, allele DRB1*04:01, allele DRB1*04:02, allele DRB1*04:04, allele DRB1*04:05, allele DRB1*04:06, allele DRB1*04:07, allele DRB1*04:08, allele DRB1*04:10, allele DRB1*04:11, allele DRB1*07:01, allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:03, allele DRB1*08:04, allele DRB1*09:01, allele DRB1*10:01, allele DRB1*11:01, allele DRB1*11:04, allele DRB1*11:06, allele DRB1*11:11, allele DRB1*11:19, allele DRB1*12:01, allele DRB1*12:02, allele DRB1*13:01, allele DRB1*13:02, allele DRB1*13:03, allele DRB1*13:05, allele DRB1*13:07, allele DRB1*13:12, allele DRB1*14:01, allele DRB1*14:03, allele DRB1*14:05, allele DRB1*14:06, allele DRB1*14:07, allele DRB1*16:01 and allele DRB1*16:02;, features a modification of the amino acid from S to A at position 29.
+The protein's natural variant, known as in allele DRB1*07:01 and allele DRB1*09:01;, features a modification of the amino acid from R to Q at position 33.
+The protein's natural variant, known as in allele DRB1*03:01, allele DRB1*03:02, allele DRB1*04:01, allele DRB1*04:02, allele DRB1*04:04, allele DRB1*04:05, allele DRB1*04:06, allele DRB1*04:07, allele DRB1*04:08, allele DRB1*04:10, allele DRB1*04:11, allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:03, allele DRB1*08:04, allele DRB1*10:01, allele DRB1*11:01, allele DRB1*11:04, allele DRB1*11:06, allele DRB1*11:11, allele DRB1*11:19, allele DRB1*12:01, allele DRB1*12:02, allele DRB1*13:01, allele DRB1*13:02, allele DRB1*13:03, allele DRB1*13:05, allele DRB1*13:07, allele DRB1*13:12, allele DRB1*14:01, allele DRB1*14:03, allele DRB1*14:05, allele DRB1*14:06 and allele DRB1*14:07; requires 2 nucleotide substitutions, features a modification of the amino acid from W to E at position 38.
+The protein's natural variant, known as in allele DRB1*09:01; requires 2 nucleotide substitutions, features a modification of the amino acid from W to K at position 38.
+The protein's natural variant, known as in allele DRB1*10:01;, features a modification of the amino acid from Q to E at position 39.
+The protein's natural variant, known as in allele DRB1*03:01, allele DRB1*03:02, allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:03, allele DRB1*08:04, allele DRB1*11:01, allele DRB1*11:04, allele DRB1*11:06, allele DRB1*11:11, allele DRB1*11:19, allele DRB1*12:01, allele DRB1*12:02, allele DRB1*13:01, allele DRB1*13:02, allele DRB1*13:03, allele DRB1*13:05, allele DRB1*13:07, allele DRB1*13:12, allele DRB1*14:01, allele DRB1*14:03, allele DRB1*14:05, allele DRB1*14:06 and allele DRB1*14:07; requires 2 nucleotide substitutions, features a modification of the amino acid from Q to Y at position 39.
+The protein's natural variant, known as in allele DRB1*09:01; requires 2 nucleotide substitutions, features a modification of the amino acid from P to D at position 40.
+The protein's natural variant, known as in allele DRB1*07:01; requires 2 nucleotide substitutions, features a modification of the amino acid from P to G at position 40.
+The protein's natural variant, known as in allele DRB1*01:01 and allele DRB1*01:02; associated with increased risk for rheumatoid arthritis;, features a modification of the amino acid from P to L at position 40.
+The protein's natural variant, known as in allele DRB1*03:01, allele DRB1*03:02, allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:03, allele DRB1*08:04, allele DRB1*11:01, allele DRB1*11:04, allele DRB1*11:06, allele DRB1*11:11, allele DRB1*11:19, allele DRB1*12:01, allele DRB1*12:02, allele DRB1*13:01, allele DRB1*13:02, allele DRB1*13:03, allele DRB1*13:05, allele DRB1*13:07, allele DRB1*13:12, allele DRB1*14:01, allele DRB1*14:03, allele DRB1*14:05, allele DRB1*14:06 and allele DRB1*14:07;, features a modification of the amino acid from P to S at position 40.
+The protein's natural variant, known as in allele DRB1*04:01, allele DRB1*04:02, allele DRB1*04:04, allele DRB1*04:05, allele DRB1*04:06, allele DRB1*04:07, allele DRB1*04:08, allele DRB1*04:10, allele DRB1*04:11 and allele DRB1*10:01; associated with increased risk for rheumatoid arthritis; requires 2 nucleotide substitutions, features a modification of the amino acid from P to V at position 40.
+The protein's natural variant, known as in allele DRB1*03:01, allele DRB1*03:02, allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:03, allele DRB1*08:04, allele DRB1*11:01, allele DRB1*11:04, allele DRB1*11:06, allele DRB1*11:11, allele DRB1*11:19, allele DRB1*12:01, allele DRB1*12:02, allele DRB1*13:01, allele DRB1*13:02, allele DRB1*13:03, allele DRB1*13:05, allele DRB1*13:07, allele DRB1*13:12, allele DRB1*14:01, allele DRB1*14:03, allele DRB1*14:05, allele DRB1*14:06 and allele DRB1*14:07;, features a modification of the amino acid from K to T at position 41.
+The protein's natural variant, known as in allele DRB1*01:01, allele DRB1*01:02, allele DRB1*09:01 and allele DRB1*10:01; associated with increased risk for rheumatoid arthritis; requires 2 nucleotide substitutions, features a modification of the amino acid from R to F at position 42.
+The protein's natural variant, known as in allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:03, allele DRB1*08:04, allele DRB1*12:01 and allele DRB1*12:02;, features a modification of the amino acid from R to G at position 42.
+The protein's natural variant, known as in allele DRB1*04:01, allele DRB1*04:02, allele DRB1*04:04, allele DRB1*04:05, allele DRB1*04:06, allele DRB1*04:07, allele DRB1*04:08, allele DRB1*04:10 and allele DRB1*04:11; associated with increased risk for rheumatoid arthritis, features a modification of the amino acid from R to H at position 42.
+The protein's natural variant, known as in allele DRB1*03:01, allele DRB1*03:02, allele DRB1*11:01, allele DRB1*11:04, allele DRB1*11:06, allele DRB1*11:11, allele DRB1*11:19, allele DRB1*13:01, allele DRB1*13:02, allele DRB1*13:03, allele DRB1*13:05, allele DRB1*13:07, allele DRB1*13:12, allele DRB1*14:01, allele DRB1*14:03, allele DRB1*14:05, allele DRB1*14:06 and allele DRB1*14:07;, features a modification of the amino acid from R to S at position 42.
+The protein's natural variant, known as in allele DRB1*07:01; requires 2 nucleotide substitutions, features a modification of the amino acid from R to Y at position 42.
+The protein's natural variant, known as in allele DRB1*07:01;, features a modification of the amino acid from E to K at position 43.
+The protein's natural variant, known as in allele DRB1*14:05;, features a modification of the amino acid from H to Q at position 45.
+The protein's natural variant, known as in allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:03, allele DRB1*08:04, allele DRB1*12:01 and allele DRB1*12:02;, features a modification of the amino acid from H to Y at position 45.
+The protein's natural variant, known as in allele DRB1*07:01;, features a modification of the amino acid from R to Q at position 54.
+The protein's natural variant, known as in allele DRB1*01:01, allele DRB1*01:02, allele DRB1*10:01, allele DRB1*12:01 and allele DRB1*12:02;, features a modification of the amino acid from F to L at position 55.
+The protein's natural variant, known as in allele DRB1*03:01, allele DRB1*09:01;, features a modification of the amino acid from F to Y at position 55.
+The protein's natural variant, known as in allele DRB1*01:01, allele DRB1*01:02, allele DRB1*03:02, allele DRB1*07:01, allele DRB1*10:01, allele DRB1*12:01, allele DRB1*12:02, allele DRB1*14:03 and allele DRB1*14:06;, features a modification of the amino acid from D to E at position 57.
+The protein's natural variant, known as in allele DRB1*09:01;, features a modification of the amino acid from D to H at position 57.
+The protein's natural variant, known as in allele DRB1*01:01 and allele DRB1*01:02;, features a modification of the amino acid from Y to C at position 59.
+The protein's natural variant, known as in allele DRB1*09:01; requires 2 nucleotide substitutions, features a modification of the amino acid from Y to G at position 59.
+The protein's natural variant, known as in allele DRB1*12:01, allele DRB1*12:02 and allele DRB1*15:03;, features a modification of the amino acid from Y to H at position 59.
+The protein's natural variant, known as in allele DRB1*07:01; requires 2 nucleotide substitutions, features a modification of the amino acid from Y to L at position 59.
+The protein's natural variant, known as in allele DRB1*10:01; requires 2 nucleotide substitutions, features a modification of the amino acid from Y to R at position 59.
+The protein's natural variant, known as in allele DRB1*01:01, allele DRB1*01:02 and allele DRB1*09:01;, features a modification of the amino acid from F to I at position 60.
+The protein's natural variant, known as in allele DRB1*10:01;, features a modification of the amino acid from F to V at position 60.
+The protein's natural variant, known as in allele DRB1*03:01, allele DRB1*03:02, allele DRB1*10:01, allele DRB1*12:01, allele DRB1*12:02, allele DRB1*13:01, allele DRB1*13:02, allele DRB1*13:05, allele DRB1*14:01, allele DRB1*14:03, allele DRB1*14:05, allele DRB1*14:06 and allele DRB1*14:07;, features a modification of the amino acid from Y to H at position 61.
+The protein's natural variant, known as in allele DRB1*04:01, allele DRB1*04:02, allele DRB1*04:04, allele DRB1*04:05, allele DRB1*04:06, allele DRB1*04:07, allele DRB1*04:08, allele DRB1*04:10 and allele DRB1*04:11;, features a modification of the amino acid from N to H at position 62.
+The protein's natural variant, known as in allele DRB1*07:01, allele DRB1*14:01, allele DRB1*14:05 and allele DRB1*14:07;, features a modification of the amino acid from S to F at position 66.
+The protein's natural variant, known as in allele DRB1*12:01 and allele DRB1*12:02, features a modification of the amino acid from S to L at position 66.
+The protein's natural variant, known as in allele DRB1*03:01, allele DRB1*03:02, allele DRB1*09:01, allele DRB1*13:01, allele DRB1*13:02, allele DRB1*13:05, allele DRB1*14:03 and allele DRB1*14:06;, features a modification of the amino acid from S to N at position 66.
+The protein's natural variant, known as in allele DRB1*04:01, allele DRB1*04:02, allele DRB1*04:04, allele DRB1*04:05, allele DRB1*04:07, allele DRB1*04:08, allele DRB1*04:10, allele DRB1*04:11, allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:03, allele DRB1*08:04, allele DRB1*10:01, allele DRB1*11:01, allele DRB1*11:04, allele DRB1*11:06, allele DRB1*11:11, allele DRB1*11:19, allele DRB1*13:03, allele DRB1*13:07 and allele DRB1*13:12;, features a modification of the amino acid from S to Y at position 66.
+The protein's natural variant, known as in allele DRB1*10:01;, features a modification of the amino acid from V to A at position 67.
+The protein's natural variant, known as in allele DRB1*12:01 and allele DRB1*12:02;, features a modification of the amino acid from V to L at position 67.
+The protein's natural variant, known as in allele DRB1*10:01;, features a modification of the amino acid from F to Y at position 69.
+The protein's natural variant, known as in allele DRB1*01:01, allele DRB1*01:02, allele DRB1*03:02, allele DRB1*04:01, allele DRB1*04:02, allele DRB1*04:04, allele DRB1*04:05, allele DRB1*04:06, allele DRB1*04:07, allele DRB1*04:08, allele DRB1*04:10, allele DRB1*04:11, allele DRB1*07:01, allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:03, allele DRB1*08:04, allele DRB1*09:01, allele DRB1*10:01, allele DRB1*13:03, allele DRB1*13:07, allele DRB1*13:12, allele DRB1*14:01, allele DRB1*14:03, allele DRB1*14:05, allele DRB1*14:06, allele DRB1*14:07, allele DRB1*16:01 and allele DRB1*16:02;, features a modification of the amino acid from F to Y at position 76.
+The protein's natural variant, known as in allele DRB1*14:01, allele DRB1*14:07;, features a modification of the amino acid from D to A at position 86.
+The protein's natural variant, known as in allele DRB1*04:05, allele DRB1*04:10; allele DRB1*04:11, allele DRB1*08:01, allele DRB1*08:03, allele DRB1*13:03 and allele DRB1*13:12; requires 2 nucleotide substitutions, features a modification of the amino acid from D to S at position 86.
+The protein's natural variant, known as in allele DRB1*07:01, allele DRB1*09:01, allele DRB1*12:01 and allele DRB1*12:02;, features a modification of the amino acid from D to V at position 86.
+The protein's natural variant, known as in allele DRB1*11:01, allele DRB1*11:04, allele DRB1*11:06, allele DRB1*11:11 and allele DRB1*11:19, features a modification of the amino acid from A to E at position 87.
+The protein's natural variant, known as in allele DRB1*14:01, allele DRB1*14:07;, features a modification of the amino acid from Y to H at position 89.
+The protein's natural variant, known as in allele DRB1*07:01, allele DRB1*09:01, allele DRB1*12:01 and allele DRB1*12:02;, features a modification of the amino acid from Y to S at position 89.
+The protein's natural variant, known as in allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:04, allele DRB1*09:01, allele DRB1*11:01, allele DRB1*11:04, allele DRB1*11:06, allele DRB1*11:11, allele DRB1*12:02, allele DRB1*13:05, allele DRB1*13:07 and allele DRB1*16:01;, features a modification of the amino acid from I to F at position 96.
+The protein's natural variant, known as in allele DRB1*01:01, allele DRB1*01:02, allele DRB1*03:01, allele DRB1*03:02, allele DRB1*04:01, allele DRB1*04:04, allele DRB1*04:05, allele DRB1*04:06, allele DRB1*04:07, allele DRB1*04:08, allele DRB1*04:10, allele DRB1*04:11, allele DRB1*10:01, allele DRB1*14:01, allele DRB1*14:03, allele DRB1*14:05, allele DRB1*14:06, allele DRB1*14:07 and allele DRB1*16:02;, features a modification of the amino acid from I to L at position 96.
+The protein's natural variant, known as in allele DRB1*04:02, allele DRB1*07:01, allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:03, allele DRB1*08:04, allele DRB1*11:01, allele DRB1*11:04, allele DRB1*11:06, allele DRB1*11:11, allele DRB1*11:19, allele DRB1*12:01, allele DRB1*12:02, allele DRB1*13:01, allele DRB1*13:02, allele DRB1*13:03, allele DRB1*13:05, allele DRB1*13:07, allele DRB1*13:12, allele DRB1*14:03, allele DRB1*16:01 and allele DRB1*16:02; requires 2 nucleotide substitutions, features a modification of the amino acid from Q to D at position 99.
+The protein's natural variant, known as in allele DRB1*09:01, allele DRB1*10:01, allele DRB1*14:01, allele DRB1*14:05 and allele DRB1*14:07;, features a modification of the amino acid from Q to R at position 99.
+The protein's natural variant, known as in allele DRB1*04:02, allele DRB1*11:11, allele DRB1*13:01 and allele DRB1*13:02;, features a modification of the amino acid from A to E at position 100.
+The protein's natural variant, known as in allele DRB1*03:01, allele DRB1*03:02, allele DRB1*04:01 and allele DRB1*13:03; requires 2 nucleotide substitutions;, features a modification of the amino acid from A to K at position 100.
+The protein's natural variant, known as in allele DRB1*01:01, allele DRB1*01:02, allele DRB1*04:04, allele DRB1*04:05, allele DRB1*04:06, allele DRB1*04:07, allele DRB1*04:08, allele DRB1*04:10, allele DRB1*04:11, allele DRB1*07:01, allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:03, allele DRB1*08:04, allele DRB1*09:01, allele DRB1*10:01, allele DRB1*11:01, allele DRB1*11:04, allele DRB1*11:06, allele DRB1*11:19, allele DRB1*12:01, allele DRB1*12:02, allele DRB1*13:05, allele DRB1*13:07, allele DRB1*13:12, allele DRB1*14:01, allele DRB1*14:03, allele DRB1*14:05, allele DRB1*14:06, allele DRB1*14:07, allele DRB1*16:01 and allele DRB1*16:02; requires 2 nucleotide substitutions, features a modification of the amino acid from A to R at position 100.
+The protein's natural variant, known as in allele DRB1*03:01, allele DRB1*03:02 and allele DRB1*07:01;, features a modification of the amino acid from A to G at position 102.
+The protein's natural variant, known as in allele DRB1*04:06, allele DRB1*04:07, allele DRB1*04:11, allele DRB1*09:01, allele DRB1*14:01, allele DRB1*14:05 and allele DRB1*14:07;, features a modification of the amino acid from A to E at position 103.
+The protein's natural variant, known as in allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:03, allele DRB1*08:04 and allele DRB1*14:03; requires 2 nucleotide substitutions, features a modification of the amino acid from A to L at position 103.
+The protein's natural variant, known as in allele DRB1*07:01; requires 2 nucleotide substitutions, features a modification of the amino acid from A to Q at position 103.
+The protein's natural variant, known as in allele DRB1*03:01 and allele DRB1*03:02; requires 2 nucleotide substitutions, features a modification of the amino acid from A to R at position 103.
+The protein's natural variant, known as in allele DRB1*03:01, allele DRB1*03:02;, features a modification of the amino acid from T to N at position 106.
+The protein's natural variant, known as in allele DRB1*07:01 and allele DRB1*09:01; requires 2 nucleotide substitutions, features a modification of the amino acid from Y to V at position 107.
+The protein's natural variant, known as in allele DRB1*01:02, allele DRB1*11:06, allele DRB1*12:01, allele DRB1*12:02;, features a modification of the amino acid from V to A at position 114.
+The protein's natural variant, known as in allele DRB1*01:01, allele DRB1*03:02, allele DRB1*04:01, allele DRB1*04:05, allele DRB1*04:07, allele DRB1*04:08, allele DRB1*07:01, allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:03, allele DRB1*09:01, allele DRB1*10:01, allele DRB1*11:01, allele DRB1*11:11, allele DRB1*11:19, allele DRB1*13:02, allele DRB1*13:03, allele DRB1*13:05, allele DRB1*13:07, allele DRB1*13:12, allele DRB1*14:03, allele DRB1*14:07, allele DRB1*15:02, allele DRB1*16:01 and allele DRB1*16:02;, features a modification of the amino acid from V to G at position 115.
+The protein's natural variant, known as in allele DRB1*01:01 and allele DRB1*01:02;, features a modification of the amino acid from Q to E at position 125.
+The protein's natural variant, known as in allele DRB1*03:01, allele DRB1*03:02, allele DRB1*07:01, allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:03, allele DRB1*08:04, allele DRB1*09:01, allele DRB1*11:01, allele DRB1*11:04, allele DRB1*11:06, allele DRB1*11:11, allele DRB1*11:19, allele DRB1*12:01, allele DRB1*12:02, allele DRB1*13:01, allele DRB1*13:02, allele DRB1*13:03, allele DRB1*13:05, allele DRB1*13:07, allele DRB1*13:12, allele DRB1*14:01, allele DRB1*14:03, allele DRB1*14:05, allele DRB1*14:06 and allele DRB1*14:07;, features a modification of the amino acid from Q to H at position 125.
+The protein's natural variant, known as in allele DRB1*04:01, allele DRB1*04:02, allele DRB1*04:04, allele DRB1*04:05, allele DRB1*04:06, allele DRB1*04:07, allele DRB1*04:08, allele DRB1*04:10 and allele DRB1*04:11; requires 2 nucleotide substitutions, features a modification of the amino acid from Q to Y at position 125.
+The protein's natural variant, known as in allele DRB1*04:01, allele DRB1*04:02, allele DRB1*04:04, allele DRB1*04:05, allele DRB1*04:06, allele DRB1*04:07, allele DRB1*04:08, allele DRB1*04:10, allele DRB1*04:11, allele DRB1*07:01 and allele DRB1*09:01;, features a modification of the amino acid from K to E at position 127.
+The protein's natural variant, known as in allele DRB1*04:01, allele DRB1*04:02, allele DRB1*04:04, allele DRB1*04:05, allele DRB1*04:06, allele DRB1*04:07, allele DRB1*04:08, allele DRB1*04:10, allele DRB1*04:11, allele DRB1*07:01 and allele DRB1*09:01;, features a modification of the amino acid from S to A at position 133.
+The protein's natural variant, known as in allele DRB1*14:01;, features a modification of the amino acid from H to Y at position 141.
+The protein's natural variant, known as in allele DRB1*04:01, allele DRB1*04:02, allele DRB1*04:04, allele DRB1*04:05, allele DRB1*04:06, allele DRB1*04:07, allele DRB1*04:08, allele DRB1*04:10, allele DRB1*04:11 and allele DRB1*10:01;, features a modification of the amino acid from S to N at position 149.
+The protein's natural variant, known as in allele DRB1*01:01, allele DRB1*01:02, allele DRB1*03:01, allele DRB1*03:02,allele DRB1*04:01, allele DRB1*04:02, allele DRB1*04:04, allele DRB1*04:05, allele DRB1*04:06, allele DRB1*04:07, allele DRB1*04:08, allele DRB1*04:10, allele DRB1*04:11, allele DRB1*07:01, allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:03, allele DRB1*08:04, allele DRB1*09:01, allele DRB1*10:01, allele DRB1*11:01, allele DRB1*11:04, allele DRB1*11:06, allele DRB1*11:11, allele DRB1*11:19, allele DRB1*12:01, allele DRB1*12:02, allele DRB1*13:01, allele DRB1*13:02, allele DRB1*13:03, allele DRB1*13:05, allele DRB1*13:07, allele DRB1*13:12, allele DRB1*14:01, allele DRB1*14:03, allele DRB1*14:05, allele DRB1*14:06 and allele DRB1*14:07;, features a modification of the amino acid from L to R at position 162.
+The protein's natural variant, known as in allele DRB1*03:01, allele DRB1*03:02, allele DRB1*04:01, allele DRB1*04:02, allele DRB1*04:04, allele DRB1*04:05, allele DRB1*04:06, allele DRB1*04:07, allele DRB1*04:08, allele DRB1*04:10, allele DRB1*04:11, allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:03, allele DRB1*08:04, allele DRB1*10:01, allele DRB1*11:01, allele DRB1*11:04, allele DRB1*11:06, allele DRB1*11:11, allele DRB1*11:19, allele DRB1*12:01, allele DRB1*12:02, allele DRB1*13:01, allele DRB1*13:02, allele DRB1*13:03, allele DRB1*13:05, allele DRB1*13:07, allele DRB1*13:12, allele DRB1*14:01, allele DRB1*14:03, allele DRB1*14:05, allele DRB1*14:06 and allele DRB1*14:07;, features a modification of the amino acid from A to T at position 169.
+The protein's natural variant, known as in allele DRB1*01:01, allele DRB1*01:02, allele DRB1*03:01, allele DRB1*03:02, allele DRB1*04:01, allele DRB1*04:02, allele DRB1*04:04, allele DRB1*04:05, allele DRB1*04:06, allele DRB1*04:07, allele DRB1*04:08, allele DRB1*04:10, allele DRB1*04:11, allele DRB1*07:01, allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:03, allele DRB1*08:04, allele DRB1*09:01, allele DRB1*10:01, allele DRB1*11:01, allele DRB1*11:04, allele DRB1*11:06, allele DRB1*11:11, allele DRB1*11:19, allele DRB1*12:01, allele DRB1*12:02, allele DRB1*13:01, allele DRB1*13:02, allele DRB1*13:03, allele DRB1*13:05, allele DRB1*13:07, allele DRB1*13:12, allele DRB1*14:01, allele DRB1*14:03, allele DRB1*14:05, allele DRB1*14:06 and allele DRB1*14:07;, features a modification of the amino acid from M to V at position 171.
+The protein's natural variant, known as in allele DRB1*03:01, allele DRB1*03:02, allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:03, allele DRB1*08:04, allele DRB1*11:01, allele DRB1*11:04, allele DRB1*11:06, allele DRB1*11:11, allele DRB1*11:19, allele DRB1*12:01, allele DRB1*12:02, allele DRB1*13:01, allele DRB1*13:02, allele DRB1*13:03, allele DRB1*13:05, allele DRB1*13:07, allele DRB1*13:12, allele DRB1*14:01, allele DRB1*14:03, allele DRB1*14:05, allele DRB1*14:06 and allele DRB1*14:07;, features a modification of the amino acid from Q to H at position 178.
+The protein's natural variant, known as in allele DRB1*10:01;, features a modification of the amino acid from R to Q at position 195.
+The protein's natural variant, known as in allele DRB1*04:01, allele DRB1*04:02, allele DRB1*04:04, allele DRB1*04:05, allele DRB1*04:06, allele DRB1*04:07, allele DRB1*04:08, allele DRB1*04:10 and allele DRB1*04:11;, features a modification of the amino acid from V to L at position 209.
+The protein's natural variant, known as in allele DRB1*07:01, allele DRB1*09:01 and allele DRB1*10:01, features a modification of the amino acid from T to M at position 210.
+The protein's natural variant, known as in allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:03 and allele DRB1*08:04, features a modification of the amino acid from R to S at position 218.
+The protein's natural variant, known as in allele DRB1*10:01;, features a modification of the amino acid from Q to P at position 260.
+The protein's natural variant, known as in allele DRB1*03:01, allele DRB1*03:02, allele DRB1*11:01, allele DRB1*11:04, allele DRB1*11:06, allele DRB1*11:11, allele DRB1*11:19, allele DRB1*12:01, allele DRB1*12:02, allele DRB1*13:01, allele DRB1*13:02, allele DRB1*13:03, allele DRB1*13:05, allele DRB1*13:07, allele DRB1*13:12, allele DRB1*14:01, allele DRB1*14:03, allele DRB1*14:05, allele DRB1*14:06 and allele DRB1*14:07;, features a modification of the amino acid from T to R at position 262.
+The protein's natural variant, known as in HTX7; found associated with K-215;, features a modification of the amino acid from R to W at position 31.
+The protein's natural variant, known as in HTX7; found associated with W-31;, features a modification of the amino acid from E to K at position 215.
+The protein's natural variant, known as in HTX7;, features a modification of the amino acid from I to T at position 226.
+The protein's natural variant, known as in HTX7;, features a modification of the amino acid from H to Y at position 283.
+The protein's natural variant, known as in HTX7;, features a modification of the amino acid from I to T at position 285.
+The protein's natural variant, known as in HTX7;, features a modification of the amino acid from A to P at position 321.
+The protein's natural variant, known as in HTX7;, features a modification of the amino acid from R to C at position 360.
+The protein's natural variant, known as in HTX7, features a modification of the amino acid from R to H at position 375.
+The protein's natural variant, known as in HTX7; unknown pathological significance;, features a modification of the amino acid from R to G at position 408.
+The natural variant of this protein is characterized by an amino acid alteration from F to L at position 103.
+The natural variant of this protein is characterized by an amino acid alteration from E to K at position 108.
+The protein's natural variant, known as in a colchicine-selected multidrug-resistant cell line; confers increased resistance to colchicine;, features a modification of the amino acid from G to V at position 185.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from K to N at position 887.
+The protein's natural variant, known as common allele; associated with susceptibility to IBD13; has decreased enzyme activity;, features a modification of the amino acid from S to A at position 893.
+The protein's natural variant, known as rare allele;, features a modification of the amino acid from S to T at position 893.
+The protein's natural variant, known as in some sporadic lung cancer sample; appears to cause loss of tumor suppressor activity;, features a modification of the amino acid from K to R at position 106.
+The protein's natural variant, known as in BRWS1;, features a modification of the amino acid from N to D at position 12.
+The protein's natural variant, known as in BRWS1;, features a modification of the amino acid from L to V at position 65.
+The protein's natural variant, known as in DJO; modifies cell response to latrunculin A;, features a modification of the amino acid from R to W at position 183.
+The protein's natural variant, known as in BRWS1;, features a modification of the amino acid from R to C at position 196.
+The protein's natural variant, known as in BRWS1;, features a modification of the amino acid from R to H at position 196.
+The protein's natural variant, known as in SPG12;, features a modification of the amino acid from S to F at position 367.
+The natural variant of this protein is characterized by an amino acid alteration from M to I at position 225.
+The natural variant of this protein is characterized by an amino acid alteration from W to C at position 276.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from G to E at position 289.
+The natural variant of this protein is characterized by an amino acid alteration from S to A at position 398.
+The protein's natural variant, known as in JEB5B;, features a modification of the amino acid from C to R at position 38.
+The protein's natural variant, known as in JEB5B;, features a modification of the amino acid from C to Y at position 61.
+The protein's natural variant, known as in JEB5B, features a modification of the amino acid from D to Y at position 131.
+The protein's natural variant, known as in JEB5B;, features a modification of the amino acid from L to P at position 156.
+The protein's natural variant, known as in JEB5B, features a modification of the amino acid from C to G at position 245.
+The protein's natural variant, known as in JEB5B;, features a modification of the amino acid from R to C at position 252.
+The protein's natural variant, known as in JEB5B;, features a modification of the amino acid from G to D at position 273.
+The protein's natural variant, known as in JEB5B;, features a modification of the amino acid from R to C at position 283.
+The protein's natural variant, known as in JEB5B;, features a modification of the amino acid from V to D at position 325.
+The protein's natural variant, known as in JEB5B, features a modification of the amino acid from L to P at position 336.
+The protein's natural variant, known as in JEB5B;, features a modification of the amino acid from C to R at position 562.
+The protein's natural variant, known as in JEB5A;, features a modification of the amino acid from G to D at position 931.
+The protein's natural variant, known as in JEB5B;, features a modification of the amino acid from R to H at position 1225.
+The protein's natural variant, known as in JEB5B; abolishes interaction with PLEC and reduces interaction with COL17A1;, features a modification of the amino acid from R to W at position 1281.
+The protein's natural variant, known as found in a patient with CHARGE syndrome; unknown pathological significance;, features a modification of the amino acid from S to L at position 703.
+The protein's natural variant, known as in strain: IFO 16449, features a modification of the amino acid from T to I at position 57.
+The protein's natural variant, known as in strain: IFO 16449, features a modification of the amino acid from AT to RA at position 139.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from P to S at position 529.
+The protein's natural variant, known as no effect on kinase activity; increased accumulation of lysosomal cholesterol;, features a modification of the amino acid from N to S at position 251.
+The protein's natural variant, known as found in a patient with developmental delay, speech difficulties, attention deficit hyperactivity disorder, behavioral problems and dysmorphic features; unknown pathological significance;, features a modification of the amino acid from E to Q at position 227.
+The protein's natural variant, known as probable disease-associated variant found in a patient with developmental delay, speech and learning difficulties, dysmorphic features and abnormal digits;, features a modification of the amino acid from R to W at position 377.
+The protein's natural variant, known as in LQT8; unknown pathological significance; increased channel activity, features a modification of the amino acid from A to T at position 28.
+The natural variant of this protein is characterized by an amino acid alteration from G to R at position 37.
+The protein's natural variant, known as in BRGDA3; unknown pathological significance; affects channel activity, features a modification of the amino acid from A to V at position 39.
+The protein's natural variant, known as in NEDHLSS, features a modification of the amino acid from F to L at position 166.
+The protein's natural variant, known as in NEDHLSS, features a modification of the amino acid from K to R at position 177.
+The natural variant of this protein is characterized by an amino acid alteration from I to T at position 304.
+The protein's natural variant, known as in NEDHLSS, features a modification of the amino acid from R to W at position 324.
+The protein's natural variant, known as in LQT8; unknown pathological significance; no effect on channel activity, features a modification of the amino acid from P to S at position 381.
+The protein's natural variant, known as in TS, features a modification of the amino acid from G to S at position 402.
+The protein's natural variant, known as in NEDHLSS, features a modification of the amino acid from V to M at position 403.
+The protein's natural variant, known as in TS; causes a nearly complete loss of voltage-dependent channel inactivation, features a modification of the amino acid from G to R at position 406.
+The protein's natural variant, known as in LQT8; unknown pathological significance; no effect on channel activity, features a modification of the amino acid from M to I at position 456.
+The protein's natural variant, known as in LQT8; unknown pathological significance, features a modification of the amino acid from E to K at position 477.
+The protein's natural variant, known as in BRGDA3; unknown pathological significance; affects channel activity, features a modification of the amino acid from G to R at position 490.
+The protein's natural variant, known as in TS; only with cardiac manifestation; decreased current density; associated with slower inactivation; altered localization, features a modification of the amino acid from R to C at position 518.
+The protein's natural variant, known as in TS; only with cardiac manifestation; decreased current density; associated with slower inactivation, features a modification of the amino acid from R to H at position 518.
+The protein's natural variant, known as in LQT8; gain-of-function effect on channel activity; slower inactivation, features a modification of the amino acid from A to D at position 582.
+The protein's natural variant, known as in NEDHLSS, features a modification of the amino acid from L to R at position 601.
+The protein's natural variant, known as in NEDHLSS, features a modification of the amino acid from M to T at position 611.
+The protein's natural variant, known as in NEDHLSS, features a modification of the amino acid from L to P at position 614.
+The protein's natural variant, known as in NEDHLSS, features a modification of the amino acid from L to R at position 614.
+The protein's natural variant, known as in TS; affects voltage-gated calcium channel activity resulting in a marked decrease in peak currents and increased late currents, features a modification of the amino acid from S to F at position 643.
+The protein's natural variant, known as in NEDHLSS, features a modification of the amino acid from L to F at position 657.
+The natural variant of this protein is characterized by an amino acid alteration from A to T at position 752.
+The natural variant of this protein is characterized by an amino acid alteration from P to S at position 817.
+The protein's natural variant, known as in LQT8; unknown pathological significance, features a modification of the amino acid from K to E at position 834.
+The protein's natural variant, known as in LQT8, features a modification of the amino acid from P to L at position 857.
+The protein's natural variant, known as in LQT8; leads to increased calcium currents; increased surface membrane expression of the channel, features a modification of the amino acid from P to R at position 857.
+The protein's natural variant, known as in LQT8; gain-of-function effect on channel activity; slower inactivation, features a modification of the amino acid from R to H at position 858.
+The protein's natural variant, known as in LQT8; gain-of-function effect on channel activity, features a modification of the amino acid from R to G at position 860.
+The protein's natural variant, known as found in a clear cell renal carcinoma case; somatic mutation, features a modification of the amino acid from S to R at position 878.
+The protein's natural variant, known as in TS; affects voltage-gated calcium channel activity resulting in loss of calcium selectivity; mutant channels show a marked increase in sodium-mediated inward currents and potassium-mediated outward currents, features a modification of the amino acid from E to K at position 1135.
+The protein's natural variant, known as found in a patient with autism; unknown pathological significance, features a modification of the amino acid from R to H at position 1159.
+The protein's natural variant, known as in TS and LQT8; electrophysiological phenotype characterized by loss of current density and gain-of-function shift in activation leading to increased steady-state current; gain of function activity, features a modification of the amino acid from I to T at position 1186.
+The protein's natural variant, known as in LQT8; gain of function activity, features a modification of the amino acid from I to V at position 1186.
+The protein's natural variant, known as in NEDHLSS, features a modification of the amino acid from V to A at position 1187.
+The protein's natural variant, known as in LQT8; unknown pathological significance, features a modification of the amino acid from A to T at position 1365.
+The protein's natural variant, known as in NEDHLSS; affects voltage-gated calcium channel activity resulting in decreased current density when expressed in a heterologous system, features a modification of the amino acid from L to V at position 1408.
+The protein's natural variant, known as in NEDHLSS, features a modification of the amino acid from V to L at position 1411.
+The protein's natural variant, known as in NEDHLSS, features a modification of the amino acid from V to M at position 1411.
+The protein's natural variant, known as in LQT8; gain of function activity, features a modification of the amino acid from I to M at position 1523.
+The protein's natural variant, known as in LQT8; gain of function activity, features a modification of the amino acid from E to K at position 1544.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 1755.
+The natural variant of this protein is characterized by an amino acid alteration from A to G at position 1765.
+The protein's natural variant, known as in LQT8; unknown pathological significance, features a modification of the amino acid from D to N at position 1787.
+The protein's natural variant, known as in LQT8; unknown pathological significance, features a modification of the amino acid from T to I at position 1800.
+The protein's natural variant, known as in LQT8; unknown pathological significance; no effect on channel activity, features a modification of the amino acid from G to C at position 1831.
+The natural variant of this protein is characterized by an amino acid alteration from T to M at position 1835.
+The natural variant of this protein is characterized by an amino acid alteration from G to R at position 1843.
+The protein's natural variant, known as in LQT8; unknown pathological significance, features a modification of the amino acid from E to K at position 1948.
+The protein's natural variant, known as in LQT8; unknown pathological significance, features a modification of the amino acid from T to M at position 1953.
+The natural variant of this protein is characterized by an amino acid alteration from R to C at position 1972.
+The protein's natural variant, known as in LQT8; unknown pathological significance, features a modification of the amino acid from R to Q at position 1989.
+The protein's natural variant, known as in LQT8; unknown pathological significance;, features a modification of the amino acid from T to N at position 2081.
+The protein's natural variant, known as rare variant; found in a case of sudden unexplained death in the young; unknown pathological significance; results in increased whole-cell calcium currents, features a modification of the amino acid from A to S at position 2091.
+The protein's natural variant, known as in LQT8; unknown pathological significance, features a modification of the amino acid from V to I at position 2097.
+The protein's natural variant, known as in LQT8; unknown pathological significance;, features a modification of the amino acid from A to G at position 2122.
+The natural variant of this protein is characterized by an amino acid alteration from A to T at position 2169.
+The natural variant of this protein is characterized by an amino acid alteration from N to S at position 2174.
+The protein's natural variant, known as in SRTD2;, features a modification of the amino acid from H to Q at position 105.
+The protein's natural variant, known as in SRTD2;, features a modification of the amino acid from A to P at position 701.
+The protein's natural variant, known as in Lep d 2.0201 and Lep d 2.0203, features a modification of the amino acid from T to S at position 35.
+The protein's natural variant, known as in Lep d 2.0201 and Lep d 2.0203, features a modification of the amino acid from E to Q at position 48.
+The protein's natural variant, known as in Lep d 2.0201 and Lep d 2.0203, features a modification of the amino acid from E to D at position 53.
+The protein's natural variant, known as in Lep d 2.0201 and Lep d 2.0203, features a modification of the amino acid from A to N at position 63.
+The protein's natural variant, known as in Lep d 2.0103, features a modification of the amino acid from A to T at position 71.
+The protein's natural variant, known as in Lep d 2.0201 and Lep d 2.0203, features a modification of the amino acid from F to V at position 90.
+The protein's natural variant, known as in Lep d 2.0201 and Lep d 2.0203, features a modification of the amino acid from I to L at position 91.
+The protein's natural variant, known as in Lep d 2.0201 and Lep d 2.0203, features a modification of the amino acid from V to I at position 95.
+The protein's natural variant, known as in Lep d 2.0201 and Lep d 2.0203, features a modification of the amino acid from I to N at position 104.
+The protein's natural variant, known as in Lep d 2.0201 and Lep d 2.0203, features a modification of the amino acid from S to G at position 106.
+The protein's natural variant, known as in Lep d 2.0201 and Lep d 2.0203, features a modification of the amino acid from G to M at position 107.
+The protein's natural variant, known as in Lep d 2.0201 and Lep d 2.0203, features a modification of the amino acid from V to I at position 116.
+The protein's natural variant, known as in Lep d 2.0203, features a modification of the amino acid from A to V at position 118.
+The protein's natural variant, known as in Lep d 2.0201 and Lep d 2.0203, features a modification of the amino acid from I to V at position 125.
+The protein's natural variant, known as in Lep d 2.0201 and Lep d 2.0203, features a modification of the amino acid from V to I at position 136.
+The protein's natural variant, known as in PEOB1;, features a modification of the amino acid from R to P at position 3.
+The natural variant of this protein is characterized by an amino acid alteration from Q to QQ at position 55.
+The natural variant of this protein is characterized by an amino acid alteration from Q to QQQ at position 55.
+The protein's natural variant, known as in PEOB1 and MTDPS4B;, features a modification of the amino acid from R to W at position 227.
+The protein's natural variant, known as in MTDPS4A, features a modification of the amino acid from R to G at position 232.
+The protein's natural variant, known as in LS;, features a modification of the amino acid from R to H at position 232.
+The protein's natural variant, known as in MTDPS4A, features a modification of the amino acid from L to P at position 244.
+The protein's natural variant, known as in PEOB1, MTDPS4A and MTDPS4B;, features a modification of the amino acid from T to I at position 251.
+The protein's natural variant, known as in PEOB1; sporadic case;, features a modification of the amino acid from G to A at position 268.
+The protein's natural variant, known as in PEOB1; also found in SANDO;, features a modification of the amino acid from L to R at position 304.
+The protein's natural variant, known as in PEOB1, features a modification of the amino acid from L to SANDO at position 304.
+The protein's natural variant, known as in PEOB1; sporadic case;, features a modification of the amino acid from Q to H at position 308.
+The protein's natural variant, known as in PEOB1, features a modification of the amino acid from R to L at position 309.
+The protein's natural variant, known as in PEOB1; sporadic case, features a modification of the amino acid from W to R at position 312.
+The protein's natural variant, known as in PEOB1, features a modification of the amino acid from G to D at position 380.
+The protein's natural variant, known as in PEOB1; sporadic case, features a modification of the amino acid from G to V at position 431.
+The protein's natural variant, known as in PEOB1, SANDO, SCAE and MTDPS4A; results in clearly decreased activity, DNA binding and processivity of the polymerase;, features a modification of the amino acid from A to T at position 467.
+The protein's natural variant, known as in PEOB1;, features a modification of the amino acid from N to D at position 468.
+The protein's natural variant, known as in SANDO and SCAE;, features a modification of the amino acid from Q to H at position 497.
+The protein's natural variant, known as in PEOA1;, features a modification of the amino acid from S to N at position 511.
+The protein's natural variant, known as in SANDO;, features a modification of the amino acid from G to V at position 517.
+The protein's natural variant, known as in PEOB1; sporadic case;, features a modification of the amino acid from R to Q at position 562.
+The protein's natural variant, known as in PEOB1; sporadic case;, features a modification of the amino acid from R to W at position 574.
+The protein's natural variant, known as in PEOB1;, features a modification of the amino acid from R to W at position 579.
+The protein's natural variant, known as in PEOB1, MTDPS4A and MTDPS4B;, features a modification of the amino acid from P to L at position 587.
+The protein's natural variant, known as in PEOB1, features a modification of the amino acid from M to L at position 603.
+The protein's natural variant, known as in SANDO; shows DNA binding affinity and processivities similar to the controls;, features a modification of the amino acid from R to Q at position 627.
+The protein's natural variant, known as in SANDO; sporadic case;, features a modification of the amino acid from R to W at position 627.
+The protein's natural variant, known as in PEOB1; sporadic case; also in SANDO;, features a modification of the amino acid from P to R at position 648.
+The protein's natural variant, known as in PEOB1; with absence of progressive external ophthalmoplegia;, features a modification of the amino acid from G to R at position 737.
+The protein's natural variant, known as in SANDO, SCAE and MTDPS4A; unknown pathological significance;, features a modification of the amino acid from W to S at position 748.
+The protein's natural variant, known as in MTDPS4A, features a modification of the amino acid from A to D at position 767.
+The protein's natural variant, known as in SANDO;, features a modification of the amino acid from R to C at position 807.
+The protein's natural variant, known as in PEOB1; sporadic case, features a modification of the amino acid from R to P at position 807.
+The protein's natural variant, known as in PEOA1 and MTDPS4A; unknown pathological significance;, features a modification of the amino acid from Y to C at position 831.
+The protein's natural variant, known as in PEOB1, MTDPS4A, MTDPS4B and LS;, features a modification of the amino acid from G to S at position 848.
+The protein's natural variant, known as in PEOB1; with absence of progressive external ophthalmoplegia;, features a modification of the amino acid from R to W at position 853.
+The protein's natural variant, known as in MTDPS4B;, features a modification of the amino acid from N to S at position 864.
+The protein's natural variant, known as in MTDPS4A, features a modification of the amino acid from Q to H at position 879.
+The protein's natural variant, known as in MTDPS4A, features a modification of the amino acid from T to S at position 885.
+The protein's natural variant, known as in PEOB1;, features a modification of the amino acid from A to T at position 889.
+The protein's natural variant, known as in MTDPS4A;, features a modification of the amino acid from T to P at position 914.
+The protein's natural variant, known as in PEOA1, features a modification of the amino acid from G to D at position 923.
+The protein's natural variant, known as in SANDO and PEOB1; sporadic case;, features a modification of the amino acid from H to Y at position 932.
+The protein's natural variant, known as in PEOA1, features a modification of the amino acid from R to H at position 943.
+The protein's natural variant, known as in PEOA1;, features a modification of the amino acid from R to C at position 953.
+The protein's natural variant, known as in PEOA1; can underlie parkinsonism; 45-fold decrease in apparent binding affinity for the incoming nucleoside triphosphate; 2-fold less accurate for basepair substitutions than wild-type;, features a modification of the amino acid from Y to C at position 955.
+The protein's natural variant, known as in MTDPS4A, features a modification of the amino acid from A to P at position 957.
+The protein's natural variant, known as in PEOA1;, features a modification of the amino acid from A to S at position 957.
+The protein's natural variant, known as in PEOB1; sporadic case;, features a modification of the amino acid from R to Q at position 1047.
+The protein's natural variant, known as in SANDO;, features a modification of the amino acid from G to R at position 1051.
+The protein's natural variant, known as in PEOB1, features a modification of the amino acid from G to V at position 1076.
+The protein's natural variant, known as in PEOB1 and MTDPS4A;, features a modification of the amino acid from R to C at position 1096.
+The protein's natural variant, known as in MTDPS4A;, features a modification of the amino acid from R to H at position 1096.
+The protein's natural variant, known as in PEOB1; sporadic case;, features a modification of the amino acid from S to C at position 1104.
+The protein's natural variant, known as in PEOB1;, features a modification of the amino acid from A to T at position 1105.
+The protein's natural variant, known as in PEOB1, features a modification of the amino acid from V to I at position 1106.
+The protein's natural variant, known as in MTDPS4A, features a modification of the amino acid from H to Y at position 1110.
+The protein's natural variant, known as in MTDPS4A, features a modification of the amino acid from H to R at position 1134.
+The protein's natural variant, known as in MTDPS4A;, features a modification of the amino acid from E to K at position 1136.
+The protein's natural variant, known as in PEOB1; unknown pathological significance;, features a modification of the amino acid from R to C at position 1146.
+The protein's natural variant, known as in PEOA1;, features a modification of the amino acid from S to L at position 1176.
+The protein's natural variant, known as in PEOB1;, features a modification of the amino acid from D to N at position 1184.
+The protein's natural variant, known as in PEOA1, features a modification of the amino acid from D to H at position 1186.
+The protein's natural variant, known as in MTDPS4A;, features a modification of the amino acid from K to N at position 1191.
+The protein's natural variant, known as in NCL, features a modification of the amino acid from L to P at position 164.
+The protein's natural variant, known as in strain: Tai18, features a modification of the amino acid from F to L at position 10.
+The protein's natural variant, known as in strain: Tai18, features a modification of the amino acid from K to Q at position 175.
+The protein's natural variant, known as in strain: Tai18, features a modification of the amino acid from L to M at position 806.
+The protein's natural variant, known as in strain: Tai18, features a modification of the amino acid from L to V at position 863.
+The protein's natural variant, known as in carboxin-resistant mutant, features a modification of the amino acid from H to L at position 253.
+The protein's natural variant, known as in allele CROC-75-3, features a modification of the amino acid from L to F at position 122.
+The protein's natural variant, known as in allele CROC-75-3, features a modification of the amino acid from A to V at position 453.
+The protein's natural variant, known as in AICAR; loss of transformylase activity;, features a modification of the amino acid from K to R at position 426.
+The protein's natural variant, known as in HLAS; partially retained in the endoplasmic reticulum; results in reduced nucleoside transport;, features a modification of the amino acid from M to R at position 116.
+The protein's natural variant, known as in HLAS;, features a modification of the amino acid from R to C at position 134.
+The protein's natural variant, known as in HLAS;, features a modification of the amino acid from S to R at position 184.
+The protein's natural variant, known as in HLAS;, features a modification of the amino acid from R to Q at position 363.
+The protein's natural variant, known as in HLAS;, features a modification of the amino acid from R to W at position 363.
+The protein's natural variant, known as in HLAS; almost total loss of nucleoside transport;, features a modification of the amino acid from G to S at position 427.
+The protein's natural variant, known as in HLAS; results in reduced nucleoside transport;, features a modification of the amino acid from G to R at position 437.
+The protein's natural variant, known as in HLAS; results in reduced nucleoside transport;, features a modification of the amino acid from T to R at position 449.
+The protein's natural variant, known as in allele HA-2M; the HA-2V allele constitute the HA-2 epitope while HA-2M is not recognized by HA-2 cytotoxic T lymphocytes;, features a modification of the amino acid from V to M at position 49.
+The natural variant of this protein is characterized by an amino acid alteration from V to I at position 6.
+The natural variant of this protein is characterized by an amino acid alteration from T to A at position 141.
+The natural variant of this protein is characterized by an amino acid alteration from E to G at position 276.
+The protein's natural variant, known as in hibernating adult liver isoform, features a modification of the amino acid from N to D at position 7.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from R to G at position 50.
+The protein's natural variant, known as in ARCL2C;, features a modification of the amino acid from L to P at position 128.
+The protein's natural variant, known as in ARCL2C;, features a modification of the amino acid from R to W at position 212.
+The protein's natural variant, known as in CMH20; affects interaction with ACTA1 and F-actin;, features a modification of the amino acid from Q to E at position 131.
+The protein's natural variant, known as in CMH20; the mutant protein accumulates in the cytoplasm but binding to ACTA1 is not altered;, features a modification of the amino acid from R to C at position 279.
+The protein's natural variant, known as in CMD1CC; affects cardiac Z line integrity; no effect on protein expression and stability;, features a modification of the amino acid from P to T at position 611.
+The protein's natural variant, known as in CMD1CC; affects cardiac Z line integrity; no effect on protein expression and stability;, features a modification of the amino acid from Y to C at position 652.
+The protein's natural variant, known as in spontaneously hypertensive rats, features a modification of the amino acid from V to M at position 779.
+The natural variant of this protein is characterized by an amino acid alteration from E to D at position 165.
+The natural variant of this protein is characterized by an amino acid alteration from T to S at position 254.
+The natural variant of this protein is characterized by an amino acid alteration from K to Q at position 472.
+The protein's natural variant, known as in PCARP;, features a modification of the amino acid from N to D at position 121.
+The protein's natural variant, known as in PCARP; also found in a patient with sensory neuropathy and pain insensitivity;, features a modification of the amino acid from C to R at position 192.
+The protein's natural variant, known as probable disease-associated variant found in a patient with sensory neuropathy and pain insensitivity;, features a modification of the amino acid from P to S at position 221.
+The protein's natural variant, known as in PCARP;, features a modification of the amino acid from A to T at position 241.
+The protein's natural variant, known as in PCARP;, features a modification of the amino acid from G to R at position 493.
+The protein's natural variant, known as in a lung adenocarcinoma sample; somatic mutation, features a modification of the amino acid from R to K at position 339.
+The protein's natural variant, known as in MRD61;, features a modification of the amino acid from T to I at position 326.
+The protein's natural variant, known as in MRD61, features a modification of the amino acid from P to Q at position 327.
+The protein's natural variant, known as in MRD61, features a modification of the amino acid from P to S at position 327.
+The protein's natural variant, known as in MRD61; unknown pathological significance, features a modification of the amino acid from P to T at position 540.
+The protein's natural variant, known as in MRD61; unknown pathological significance, features a modification of the amino acid from Q to K at position 2060.
+The protein's natural variant, known as in MRD61; unknown pathological significance, features a modification of the amino acid from A to V at position 2064.
+The protein's natural variant, known as in cauli, features a modification of the amino acid from I to K at position 855.
+The protein's natural variant, known as in MCAR; decreased chloride transport; decreased localization to the plasma membrane; dominant negative effect on chloride transport and localization to the plasma membrane; no significant effect on chloride channel activity; no effect on homodimerization;, features a modification of the amino acid from Q to R at position 43.
+The protein's natural variant, known as in MCAR; unknown pathological significance; no effect on chloride transport;, features a modification of the amino acid from S to L at position 70.
+The protein's natural variant, known as in MCAR; unknown pathological significance; no effect on chloride transport;, features a modification of the amino acid from T to A at position 82.
+The protein's natural variant, known as in MCAR; no effect on chloride transport;, features a modification of the amino acid from R to C at position 105.
+The protein's natural variant, known as in MCAD;, features a modification of the amino acid from M to V at position 128.
+The protein's natural variant, known as in MCAR, features a modification of the amino acid from D to G at position 136.
+The protein's natural variant, known as in MCAR; reduced chloride transport; decreased localization to the plasma membrane; no significant effect on chloride channel activity;, features a modification of the amino acid from Y to D at position 137.
+The protein's natural variant, known as in MCAR, features a modification of the amino acid from Y to C at position 150.
+The protein's natural variant, known as no effect on chloride transport;, features a modification of the amino acid from Q to R at position 154.
+The protein's natural variant, known as in MCAR; reduced chloride transport; decreased localization to the plasma membrane; no significant effect on chloride channel activity;, features a modification of the amino acid from Q to H at position 160.
+The protein's natural variant, known as in MCAD and MCAR, features a modification of the amino acid from F to V at position 161.
+The protein's natural variant, known as in MCAR; altered chloride channel activity, features a modification of the amino acid from W to R at position 164.
+The protein's natural variant, known as in MCAR;, features a modification of the amino acid from V to G at position 165.
+The protein's natural variant, known as in MCAR; no effect on chloride transport;, features a modification of the amino acid from F to L at position 167.
+The protein's natural variant, known as in MCAR; loss of chloride channel activity;, features a modification of the amino acid from G to S at position 190.
+The protein's natural variant, known as in MCAD;, features a modification of the amino acid from E to K at position 193.
+The protein's natural variant, known as in MCAR; changed chloride channel activity, features a modification of the amino acid from I to R at position 197.
+The protein's natural variant, known as in MCAD; reduced chloride transport; changed calcium channel activity; changed gating of the channel;, features a modification of the amino acid from L to P at position 198.
+The protein's natural variant, known as in MCAD and MCAR;, features a modification of the amino acid from G to R at position 200.
+The protein's natural variant, known as in MCAD and MCAR; changed ion selectivity; loss of chloride transport; mild dominant effect;, features a modification of the amino acid from G to E at position 230.
+The protein's natural variant, known as in MCAR; loss of chloride transport; changed calcium channel activity; changed gating of the channel;, features a modification of the amino acid from V to L at position 236.
+The protein's natural variant, known as in MCAR;, features a modification of the amino acid from Y to C at position 261.
+The protein's natural variant, known as in MCAR; decreased chloride channel activity, features a modification of the amino acid from G to V at position 270.
+The protein's natural variant, known as in MCAR; reduced chloride transport; no effect on protein abundance;, features a modification of the amino acid from C to R at position 277.
+The protein's natural variant, known as in MCAR; reduced chloride transport; changed calcium channel activity; changed gating of the channel; no effect on protein abundance, features a modification of the amino acid from C to Y at position 277.
+The protein's natural variant, known as in MCAR; loss of chloride channel activity;, features a modification of the amino acid from G to E at position 285.
+The protein's natural variant, known as in MCAD; reduced chloride transport; changed calcium channel activity; changed gating of the channel; dominant negative effect;, features a modification of the amino acid from V to A at position 286.
+The protein's natural variant, known as in MCAD; reduced chloride transport; changed chloride channel activity; changed gating of the channel; dominant negative effect;, features a modification of the amino acid from I to M at position 290.
+The protein's natural variant, known as in MCAR; loss of calcium channel activity; no dominant negative effect;, features a modification of the amino acid from E to K at position 291.
+The protein's natural variant, known as no effect on chloride transport;, features a modification of the amino acid from R to Q at position 300.
+The protein's natural variant, known as in MCAD; reduced chloride transport; changed chloride channel activity; changed gating of the channel; dominant negative effect;, features a modification of the amino acid from F to S at position 307.
+The protein's natural variant, known as in MCAD and MCAR;, features a modification of the amino acid from A to T at position 313.
+The protein's natural variant, known as in MCAD; reduced chloride transport; changed chloride channel activity; changed gating of the channel;, features a modification of the amino acid from R to Q at position 317.
+The protein's natural variant, known as in MCAR;, features a modification of the amino acid from V to I at position 327.
+The protein's natural variant, known as in MCAR, features a modification of the amino acid from I to T at position 329.
+The protein's natural variant, known as in MCAD and MCAR;, features a modification of the amino acid from R to Q at position 338.
+The protein's natural variant, known as in MCAR; loss of chloride transport; decreased localization to the plasma membrane; loss of homodimerization; might be degraded;, features a modification of the amino acid from Q to P at position 412.
+The protein's natural variant, known as in MCAR;, features a modification of the amino acid from F to C at position 413.
+The protein's natural variant, known as in MCAR, features a modification of the amino acid from A to V at position 415.
+The protein's natural variant, known as in MCAR; unknown pathological significance; no effect on chloride channel activity;, features a modification of the amino acid from R to W at position 453.
+The protein's natural variant, known as in MCAD; decreased protein abundance, features a modification of the amino acid from P to H at position 480.
+The protein's natural variant, known as in MCAD; loss of chloride transport; changed chloride channel activity; changed gating of the channel; dominant effect;, features a modification of the amino acid from P to L at position 480.
+The protein's natural variant, known as in MCAR;, features a modification of the amino acid from G to R at position 482.
+The protein's natural variant, known as in MCAD; reduced chloride transport; changed calcium channel activity; changed channel gating; no dominant negative effect;, features a modification of the amino acid from F to L at position 484.
+The protein's natural variant, known as in MCAR;, features a modification of the amino acid from M to V at position 485.
+The protein's natural variant, known as in MCAR; loss of chloride channel activity; recessive;, features a modification of the amino acid from R to S at position 496.
+The protein's natural variant, known as in MCAR; reduced chloride transport; changed calcium channel activity; changed channel gating;, features a modification of the amino acid from G to R at position 499.
+The protein's natural variant, known as in MCAR; unknown pathological significance, features a modification of the amino acid from I to T at position 527.
+The protein's natural variant, known as in MCAR; unknown pathological significance, features a modification of the amino acid from T to I at position 533.
+The protein's natural variant, known as in MCAR; unknown pathological significance;, features a modification of the amino acid from V to L at position 536.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from E to K at position 548.
+The protein's natural variant, known as in MCAD and MCAR; also found in myotonia levior; reduced chloride transport; changed calcium channel activity; changed channel gating; weak dominant negative effect;, features a modification of the amino acid from Q to R at position 552.
+The protein's natural variant, known as in MCAD and MCAR; mild form; reduced chloride transport; changed chloride channel activity; changed gating of the channel; partial dominant negative effect;, features a modification of the amino acid from I to N at position 556.
+The protein's natural variant, known as in MCAR, features a modification of the amino acid from V to I at position 563.
+The protein's natural variant, known as in MCAR; unknown pathological significance; no effect on calcium channel activity, features a modification of the amino acid from L to P at position 628.
+The protein's natural variant, known as in MCAR; reduced calcium channel activity;, features a modification of the amino acid from V to G at position 640.
+The protein's natural variant, known as in MCAR, features a modification of the amino acid from F to L at position 708.
+The protein's natural variant, known as in MCAR; unknown pathological significance; no effect on chloride channel activity;, features a modification of the amino acid from G to S at position 845.
+The protein's natural variant, known as in MCAR; unknown pathological significance;, features a modification of the amino acid from G to E at position 855.
+The protein's natural variant, known as in MCAR; unknown pathological significance;, features a modification of the amino acid from P to L at position 932.
+The protein's natural variant, known as in MCAR; unknown pathological significance, features a modification of the amino acid from V to E at position 947.
+The protein's natural variant, known as in MCAD; unknown pathological significance;, features a modification of the amino acid from E to K at position 950.
+The protein's natural variant, known as in RNA edited version, features a modification of the amino acid from Y to C at position 429.
+The protein's natural variant, known as in strain: CBS 5512, features a modification of the amino acid from I to M at position 90.
+The protein's natural variant, known as in strain: CBS 5512, features a modification of the amino acid from I to M at position 142.
+The protein's natural variant, known as in strain: CBS 5512, features a modification of the amino acid from M to I at position 169.
+The protein's natural variant, known as in a lung neuroendocrine carcinoma sample; somatic mutation, features a modification of the amino acid from A to V at position 221.
+The protein's natural variant, known as found in a patient with features of Silver-Russell syndrome and multi-locus imprinting disturbance; unknown pathological significance;, features a modification of the amino acid from V to D at position 23.
+The protein's natural variant, known as found in patients with Beckwith-Wiedemann syndrome and multi-locus imprinting disturbance; when associated in cis with Q-76; unknown pathological significance;, features a modification of the amino acid from M to T at position 52.
+The protein's natural variant, known as found in patients with Beckwith-Wiedemann syndrome and multi-locus imprinting disturbance; when associated in cis with T-52; unknown pathological significance;, features a modification of the amino acid from E to Q at position 76.
+The protein's natural variant, known as found in patients with female infertility; when associated in cis with C-462; unknown pathological significance;, features a modification of the amino acid from R to P at position 143.
+The protein's natural variant, known as found in patients with female infertility; unknown pathological significance; reduces protein abundance in oocytes and embryos, features a modification of the amino acid from G to E at position 289.
+The protein's natural variant, known as found in patients with female infertility; unknown pathological significance;, features a modification of the amino acid from P to L at position 354.
+The protein's natural variant, known as found in patients with female infertility; when associated in cis with P-143; unknown pathological significance;, features a modification of the amino acid from R to C at position 462.
+The protein's natural variant, known as found in a patient with mild cognitive retardation and multi-locus imprinting disturbance; unknown pathological significance;, features a modification of the amino acid from R to C at position 533.
+The protein's natural variant, known as found in patients with female infertility; unknown pathological significance;, features a modification of the amino acid from R to P at position 533.
+The protein's natural variant, known as found in a patient with Beckwith-Wiedemann syndrome and multi-locus imprinting disturbance; unknown pathological significance, features a modification of the amino acid from G to V at position 555.
+The protein's natural variant, known as found in patients with female infertility; unknown pathological significance;, features a modification of the amino acid from R to C at position 635.
+The protein's natural variant, known as found in patients with female infertility; unknown pathological significance, features a modification of the amino acid from L to R at position 640.
+The protein's natural variant, known as found in patients with female infertility; unknown pathological significance, features a modification of the amino acid from T to I at position 694.
+The protein's natural variant, known as found in a patient with Silver-Russell syndrome and multi-locus imprinting disturbance; unknown pathological significance;, features a modification of the amino acid from C to R at position 774.
+The protein's natural variant, known as found in patients with female infertility; unknown pathological significance;, features a modification of the amino acid from S to T at position 893.
+The protein's natural variant, known as found in patients with female infertility; unknown pathological significance; reduces protein abundance in oocytes and embryos;, features a modification of the amino acid from T to I at position 1107.
+The protein's natural variant, known as in strain: Isolate 240-3, features a modification of the amino acid from H to R at position 34.
+The protein's natural variant, known as in strain: Isolate 240-3, features a modification of the amino acid from T to A at position 96.
+The protein's natural variant, known as in mnb1; reduced brain volume, features a modification of the amino acid from A to T at position 191.
+The protein's natural variant, known as in allele ENPP1b, features a modification of the amino acid from H to R at position 651.
+The protein's natural variant, known as in allele ENPP1b, features a modification of the amino acid from R to S at position 680.
+The protein's natural variant, known as in strain: G7, features a modification of the amino acid from V to E at position 3.
+The protein's natural variant, known as in strain: G7, features a modification of the amino acid from L to P at position 15.
+The protein's natural variant, known as in strain: G7, features a modification of the amino acid from S to A at position 49.
+The protein's natural variant, known as in strain: G7, features a modification of the amino acid from K to R at position 77.
+The protein's natural variant, known as in strain: G7, features a modification of the amino acid from Q to E at position 85.
+The protein's natural variant, known as in strain: G7, features a modification of the amino acid from P to A at position 91.
+The protein's natural variant, known as in strain: G7, features a modification of the amino acid from S to GEF at position 104.
+The natural variant of this protein is characterized by an amino acid alteration from M to V at position 597.
+The protein's natural variant, known as in CAGSSS; unknown pathological significance;, features a modification of the amino acid from G to R at position 203.
+The protein's natural variant, known as in CAGSSS; unknown pathological significance;, features a modification of the amino acid from F to S at position 227.
+The protein's natural variant, known as found in a patient with Leigh syndrome; unknown pathological significance;, features a modification of the amino acid from E to K at position 708.
+The protein's natural variant, known as in CAGSSS; unknown pathological significance;, features a modification of the amino acid from H to R at position 761.
+The protein's natural variant, known as in CAGSSS; unknown pathological significance;, features a modification of the amino acid from R to H at position 817.
+The protein's natural variant, known as in CAGSSS; unknown pathological significance;, features a modification of the amino acid from F to L at position 859.
+The protein's natural variant, known as in CAGSSS; unknown pathological significance;, features a modification of the amino acid from G to R at position 874.
+The protein's natural variant, known as in CAGSSS; unknown pathological significance;, features a modification of the amino acid from P to L at position 909.
+The protein's natural variant, known as in CAGSSS; unknown pathological significance;, features a modification of the amino acid from P to S at position 909.
+The protein's natural variant, known as in strain: 1299 and 1373, features a modification of the amino acid from R to K at position 37.
+The protein's natural variant, known as in strain: 1373, features a modification of the amino acid from K to S at position 62.
+The protein's natural variant, known as in strain: 1373, features a modification of the amino acid from E to D at position 73.
+The protein's natural variant, known as in strain: 1373, features a modification of the amino acid from D to E at position 78.
+The protein's natural variant, known as in strain: 1373, features a modification of the amino acid from A to G at position 85.
+The protein's natural variant, known as in RHDA1; unknown pathological significance;, features a modification of the amino acid from T to M at position 255.
+The protein's natural variant, known as in RHDA1; the mutant does not localize at the cell membrane;, features a modification of the amino acid from G to R at position 407.
+The natural variant of this protein is characterized by an amino acid alteration from V to L at position 567.
+The protein's natural variant, known as in ACHM3; unknown pathological significance;, features a modification of the amino acid from G to R at position 107.
+The protein's natural variant, known as in ACHM3;, features a modification of the amino acid from K to E at position 148.
+The protein's natural variant, known as in ACHM3;, features a modification of the amino acid from S to F at position 156.
+The protein's natural variant, known as in ACHM3; unknown pathological significance;, features a modification of the amino acid from E to K at position 199.
+The protein's natural variant, known as in ACHM3;, features a modification of the amino acid from P to L at position 309.
+The protein's natural variant, known as found in macular degeneration; unknown pathological significance;, features a modification of the amino acid from R to Q at position 403.
+The protein's natural variant, known as in ACHM3;, features a modification of the amino acid from S to F at position 435.
+The protein's natural variant, known as in ACHM3; unknown pathological significance;, features a modification of the amino acid from M to T at position 466.
+The protein's natural variant, known as in STGD1;, features a modification of the amino acid from Y to D at position 469.
+The protein's natural variant, known as in ACHM3; unknown pathological significance, features a modification of the amino acid from D to N at position 494.
+The protein's natural variant, known as in ACHM3; unknown pathological significance;, features a modification of the amino acid from D to Y at position 513.
+The protein's natural variant, known as in ACHM3; requires 2 nucleotide substitutions, features a modification of the amino acid from F to N at position 525.
+The protein's natural variant, known as in ACHM3;, features a modification of the amino acid from G to C at position 558.
+The protein's natural variant, known as in ACHM3;, features a modification of the amino acid from L to F at position 595.
+The protein's natural variant, known as in ACHM3; unknown pathological significance, features a modification of the amino acid from T to P at position 672.
+The protein's natural variant, known as in OPLL, features a modification of the amino acid from L to P at position 91.
+The protein's natural variant, known as in ARHR2, features a modification of the amino acid from G to D at position 92.
+The protein's natural variant, known as in COLED; impaired homodimerization, features a modification of the amino acid from C to R at position 120.
+The protein's natural variant, known as in GACI1, features a modification of the amino acid from C to R at position 126.
+The protein's natural variant, known as in COLED; impaired homodimerization, features a modification of the amino acid from C to R at position 133.
+The protein's natural variant, known as in COLED;, features a modification of the amino acid from C to S at position 149.
+The protein's natural variant, known as in COLED;, features a modification of the amino acid from C to S at position 164.
+The protein's natural variant, known as associated with T2D; decreased nucleotide phosphodiesterase activity; no effect on localization to plasma membrane;, features a modification of the amino acid from K to Q at position 173.
+The protein's natural variant, known as in COLED, features a modification of the amino acid from C to S at position 177.
+The protein's natural variant, known as in COLED;, features a modification of the amino acid from C to Y at position 177.
+The protein's natural variant, known as in GACI1; loss of nucleotide phosphodiesterase activity; loss of localization to plasma membrane;, features a modification of the amino acid from C to R at position 195.
+The protein's natural variant, known as in GACI1; loss of nucleotide phosphodiesterase activity; loss of localization to plasma membrane, features a modification of the amino acid from C to S at position 195.
+The protein's natural variant, known as in GACI1; unknown pathological significance;, features a modification of the amino acid from S to Y at position 216.
+The protein's natural variant, known as in GACI1;, features a modification of the amino acid from D to V at position 218.
+The protein's natural variant, known as in ARHR2; unknown pathological significance, features a modification of the amino acid from G to R at position 219.
+The protein's natural variant, known as in GACI1; unknown pathological significance, features a modification of the amino acid from G to E at position 242.
+The protein's natural variant, known as in GACI1; unknown pathological significance;, features a modification of the amino acid from P to L at position 250.
+The protein's natural variant, known as in ARHR2;, features a modification of the amino acid from G to V at position 266.
+The protein's natural variant, known as in GACI1; unknown pathological significance;, features a modification of the amino acid from D to N at position 276.
+The protein's natural variant, known as in OPLL;, features a modification of the amino acid from S to F at position 287.
+The protein's natural variant, known as in GACI1; loss of nucleotide phosphodiesterase activity; loss of localization to plasma membrane, features a modification of the amino acid from Y to C at position 301.
+The protein's natural variant, known as in GACI1; loss of nucleotide phosphodiesterase activity; no effect on localization to plasma membrane;, features a modification of the amino acid from P to T at position 305.
+The protein's natural variant, known as in GACI1;, features a modification of the amino acid from G to V at position 342.
+The protein's natural variant, known as in GACI1; unknown pathological significance;, features a modification of the amino acid from R to K at position 349.
+The protein's natural variant, known as in GACI1; unknown pathological significance;, features a modification of the amino acid from Y to F at position 371.
+The protein's natural variant, known as in GACI1;, features a modification of the amino acid from R to Q at position 456.
+The protein's natural variant, known as in GACI1; decreased nucleotide phosphodiesterase activity; no effect on localization to plasma membrane;, features a modification of the amino acid from Y to C at position 471.
+The protein's natural variant, known as in GACI1; unknown pathological significance;, features a modification of the amino acid from R to W at position 481.
+The protein's natural variant, known as in GACI1, features a modification of the amino acid from H to P at position 500.
+The protein's natural variant, known as in GACI1; decreased nucleotide phosphodiesterase activity; no effect on localization to plasma membrane, features a modification of the amino acid from S to R at position 504.
+The protein's natural variant, known as in GACI1; loss of nucleotide phosphodiesterase activity; no effect on localization to plasma membrane;, features a modification of the amino acid from Y to C at position 513.
+The protein's natural variant, known as in GACI1; loss of nucleotide phosphodiesterase activity; no effect on localization to plasma membrane;, features a modification of the amino acid from D to H at position 538.
+The protein's natural variant, known as in GACI1;, features a modification of the amino acid from Y to C at position 570.
+The protein's natural variant, known as in GACI1; unknown pathological significance;, features a modification of the amino acid from L to F at position 579.
+The protein's natural variant, known as in GACI1; loss of nucleotide phosphodiesterase activity; loss of localization to plasma membrane;, features a modification of the amino acid from G to R at position 586.
+The protein's natural variant, known as in GACI1; decreased nucleotide phosphodiesterase activity; no effect on localization to plasma membrane;, features a modification of the amino acid from Y to C at position 659.
+The protein's natural variant, known as no effect on nucleotide phosphodiesterase activity; no effect on localization to plasma membrane;, features a modification of the amino acid from E to K at position 668.
+The protein's natural variant, known as in GACI1, features a modification of the amino acid from C to R at position 726.
+The protein's natural variant, known as decreased nucleotide phosphodiesterase activity; no effect on localization to plasma membrane;, features a modification of the amino acid from R to C at position 774.
+The protein's natural variant, known as in GACI1; decreased nucleotide phosphodiesterase activity; no effect on localization to plasma membrane;, features a modification of the amino acid from H to R at position 777.
+The protein's natural variant, known as in ARHR2 and GACI1;, features a modification of the amino acid from N to S at position 792.
+The protein's natural variant, known as in GACI1, features a modification of the amino acid from D to H at position 804.
+The protein's natural variant, known as decreased nucleotide phosphodiesterase activity; no effect on localization to plasma membrane;, features a modification of the amino acid from R to H at position 821.
+The protein's natural variant, known as in GACI1; loss of nucleotide phosphodiesterase activity; loss of localization to plasma membrane;, features a modification of the amino acid from R to W at position 888.
+The protein's natural variant, known as in ARHR2; loss of activity;, features a modification of the amino acid from Y to S at position 901.
+The protein's natural variant, known as in wr; destabilizes and consequently reduces protein levels, as well as those of the GARP complex, features a modification of the amino acid from L to Q at position 967.
+The protein's natural variant, known as in a breast pleomorphic lobular carcinoma sample; somatic mutation, features a modification of the amino acid from F to C at position 270.
+The protein's natural variant, known as in MD, features a modification of the amino acid from T to P at position 75.
+The protein's natural variant, known as in strain: NCPF7367, features a modification of the amino acid from V to I at position 38.
+The protein's natural variant, known as in strain: NCPF7367, features a modification of the amino acid from W to R at position 213.
+The protein's natural variant, known as in allele GSTP1*B and allele GSTP1*C;, features a modification of the amino acid from I to V at position 105.
+The protein's natural variant, known as in allele GSTP1*C;, features a modification of the amino acid from A to V at position 114.
+The protein's natural variant, known as in strain: cv. Sha, features a modification of the amino acid from K to R at position 130.
+The protein's natural variant, known as in strain: ZBMEL95 and ZBMEL157, features a modification of the amino acid from L to P at position 9.
+The protein's natural variant, known as in strain: MEL11, ZBMEL145, ZBMEL131, ZBMEL229 and ZBMEL384, features a modification of the amino acid from A to V at position 96.
+The protein's natural variant, known as in strain: MEL01, MEL02, MEL12, MEL13, MEL14, MEL15, MEL16, MEL17, MEL18, MEL19, MEL20, ZBMEL84, ZBMEL95, ZBMEL131, ZBMEL157, ZBMEL191, ZBMEL377 and ZBMEL398, features a modification of the amino acid from R to H at position 125.
+The protein's natural variant, known as in strain: ZBMEL186, features a modification of the amino acid from P to R at position 239.
+The natural variant of this protein is characterized by an amino acid alteration from V to A at position 66.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation;, features a modification of the amino acid from P to S at position 1238.
+The protein's natural variant, known as does not affect exonuclease activity;, features a modification of the amino acid from D to N at position 115.
+The protein's natural variant, known as does not affect exonuclease activity;, features a modification of the amino acid from G to V at position 172.
+The natural variant of this protein is characterized by an amino acid alteration from V to L at position 29.
+The natural variant of this protein is characterized by an amino acid alteration from F to P at position 52.
+The protein's natural variant, known as in TufB, features a modification of the amino acid from N to S at position 140.
+The protein's natural variant, known as in TufB, features a modification of the amino acid from K to R at position 294.
+The protein's natural variant, known as in HOKPP1;, features a modification of the amino acid from R to G at position 528.
+The protein's natural variant, known as in HOKPP1;, features a modification of the amino acid from R to H at position 528.
+The protein's natural variant, known as in HOKPP1, features a modification of the amino acid from R to S at position 900.
+The protein's natural variant, known as in MHS5;, features a modification of the amino acid from R to H at position 1086.
+The protein's natural variant, known as in HOKPP1;, features a modification of the amino acid from R to G at position 1239.
+The protein's natural variant, known as in HOKPP1;, features a modification of the amino acid from R to H at position 1239.
+The protein's natural variant, known as in allele C*17:01;, features a modification of the amino acid from R to Q at position 7.
+The protein's natural variant, known as in allele C*01:02, allele C*02:02, allele C*03:02, allele C*03:04, allele C*04:01, allele C*05:01, allele C*06:02, allele C*08:01, allele C*12:02, allele C*14:02, allele C*15:02 and allele C*16:01;, features a modification of the amino acid from A to T at position 8.
+The protein's natural variant, known as in allele C*01:02, allele C*03:02, allele C*03:04, allele C*04:01, allele C*05:01, allele C*06:02, allele C*08:01, allele C*12:02, allele C*14:02 and allele C*16:01;, features a modification of the amino acid from L to I at position 10.
+The protein's natural variant, known as in allele C*01:02, allele C*02:02, allele C*03:02, allele C*03:04, allele C*04:01, allele C*05:01, allele C*06:02, allele C*08:01, allele C*12:02, allele C*14:02, allele C*15:02, allele C*16:01 and allele C*17:01;, features a modification of the amino acid from G to A at position 16.
+The protein's natural variant, known as in allele C*17:01;, features a modification of the amino acid from T to I at position 20.
+The protein's natural variant, known as in allele C*03:02, allele C*03:04, allele C*04:01 and allele C*17:01;, features a modification of the amino acid from C to G at position 25.
+The protein's natural variant, known as in allele C*01:02;, features a modification of the amino acid from R to K at position 30.
+The protein's natural variant, known as in allele C*01:02; requires 2 nucleotide substitutions, features a modification of the amino acid from D to F at position 33.
+The protein's natural variant, known as in allele C*04:01 and allele C*14:02; requires 2 nucleotide substitutions, features a modification of the amino acid from D to S at position 33.
+The protein's natural variant, known as in allele C*02:02, allele C*03:02, allele C*03:04, allele C*05:01, allele C*08:01, allele C*12:02, allele C*15:02, allele C*16:01 and allele C*17:01;, features a modification of the amino acid from D to Y at position 33.
+The protein's natural variant, known as in allele C*01:02, allele C*04:01 and allele C*14:02;, features a modification of the amino acid from A to S at position 35.
+The protein's natural variant, known as in allele C*04:01;, features a modification of the amino acid from R to W at position 38.
+The protein's natural variant, known as in allele C*02:02;, features a modification of the amino acid from G to S at position 40.
+The protein's natural variant, known as in allele C*02:02, allele C*03:02, allele C*03:04 and allele C*15:02;, features a modification of the amino acid from R to H at position 45.
+The protein's natural variant, known as in allele C*02:02, allele C*03:02, allele C*03:04, allele C*04:01, allele C*05:01, allele C*08:01, allele C*12:02, allele C*14:02, allele C*15:02, allele C*16:01 and allele C*17:01;, features a modification of the amino acid from S to A at position 48.
+The protein's natural variant, known as in allele C*05:01 and C*08:01;, features a modification of the amino acid from R to Q at position 59.
+The protein's natural variant, known as in allele C*04:01;, features a modification of the amino acid from A to E at position 73.
+The protein's natural variant, known as in allele C*07:01, C*15:02;, features a modification of the amino acid from K to N at position 90.
+The protein's natural variant, known as in allele C*01:02, allele C*02:02, allele C*03:02, allele C*03:04, allele C*05:01, allele C*08:01, allele C*14:02, allele C*15:02 and allele C*16:01;, features a modification of the amino acid from A to T at position 97.
+The protein's natural variant, known as in allele C*02:02, allele C*04:01, allele C*05:01, allele C*06:02, allele C*15:02, allele C*17:01 and allele C*18:01;, features a modification of the amino acid from S to N at position 101.
+The protein's natural variant, known as in allele C*02:02, allele C*04:01, allele C*05:01, allele C*06:02, allele C*15:02, allele C*17:01 and allele C*18:01;, features a modification of the amino acid from N to K at position 104.
+The protein's natural variant, known as in allele C*01:02, allele C*02:02, allele C*03:02, allele C*03:04, allele C*05:01, allele C*08:01, allele C*12:02, allele C*14:02, allele C*15:02, allele C*16:01 and allele C*17:01;, features a modification of the amino acid from D to A at position 114.
+The protein's natural variant, known as in allele C*03:02, allele C*03:04 and allele C*15:02;, features a modification of the amino acid from T to I at position 118.
+The protein's natural variant, known as in allele C*07:04;, features a modification of the amino acid from L to F at position 119.
+The protein's natural variant, known as in allele C*03:04, allele C*15:02 and allele C*17:01;, features a modification of the amino acid from L to I at position 119.
+The protein's natural variant, known as in allele C*01:02, allele C*06:02, allele C*14:02 and allele C*16:01;, features a modification of the amino acid from R to W at position 121.
+The protein's natural variant, known as in allele C*01:02;, features a modification of the amino acid from S to C at position 123.
+The protein's natural variant, known as in allele C*04:01, allele C*14:02 and allele C*18:01;, features a modification of the amino acid from S to F at position 123.
+The protein's natural variant, known as in allele C*07:01, allele C*02:02, allele C*03:02, allele C*03:04, allele C*05:01, allele C*06:02, allele C*07:04, allele C*08:01, allele C*12:02, allele C*15:02, allele C*16:01 and allele C*17:01;, features a modification of the amino acid from S to Y at position 123.
+The protein's natural variant, known as in allele C*03:02 and allele C*03:04;, features a modification of the amino acid from L to V at position 127.
+The protein's natural variant, known as in allele C*15:02;, features a modification of the amino acid from Y to H at position 137.
+The protein's natural variant, known as in allele C*04:01, allele C*05:01, allele C*08:01, allele C*17:01 and allele C*18:01;, features a modification of the amino acid from D to N at position 138.
+The protein's natural variant, known as in allele C*04:01, allele C*05:01, allele C*07:04, allele C*08:01, allele C*17:01 and allele C*18:01;, features a modification of the amino acid from S to F at position 140.
+The protein's natural variant, known as in allele C*15:02, features a modification of the amino acid from S to L at position 140.
+The protein's natural variant, known as in alleles C*01:02, C*03:04;, features a modification of the amino acid from S to Y at position 140.
+The protein's natural variant, known as in allele C*05:01, features a modification of the amino acid from T to K at position 162.
+The protein's natural variant, known as in allele C*17:01;, features a modification of the amino acid from T to S at position 167.
+The protein's natural variant, known as in allele C*01:02, allele C*02:02, allele C*03:02, allele C*03:04, allele C*04:01, allele C*05:01, allele C*06:02, allele C*08:01, allele C*12:02, allele C*14:02, allele C*15:02, allele C*16:01 and allele C*18:01;, features a modification of the amino acid from L to W at position 171.
+The protein's natural variant, known as in allele C*01:02, allele C*02:02, allele C*03:02, allele C*03:04, allele C*04:01, allele C*05:01, allele C*06:02, allele C*12:02, allele C*14:02, allele C*15:02, allele C*17:01 and allele C*18:01;, features a modification of the amino acid from A to E at position 176.
+The protein's natural variant, known as in allele C*08:01;, features a modification of the amino acid from A to T at position 176.
+The protein's natural variant, known as in allele C*07:04; requires 2 nucleotide substitutions, features a modification of the amino acid from L to D at position 180.
+The protein's natural variant, known as in allele C*16:01;, features a modification of the amino acid from L to Q at position 180.
+The protein's natural variant, known as in allele C*01:02, allele C*04:01, allele C*05:01, allele C*14:02 and allele C*18:01;, features a modification of the amino acid from L to R at position 180.
+The protein's natural variant, known as in allele C*02:02, allele C*06:02 and allele C*12:02;, features a modification of the amino acid from L to W at position 180.
+The protein's natural variant, known as in alleles C*02:02 and allele C*17:01; requires 2 nucleotide substitutions, features a modification of the amino acid from T to E at position 187.
+The protein's natural variant, known as in allele C*03:02 and allele C*03:04; requires 2 nucleotide substitutions, features a modification of the amino acid from T to L at position 187.
+The protein's natural variant, known as in allele C*17:01;, features a modification of the amino acid from R to G at position 194.
+The protein's natural variant, known as in allele C*03:02 and allele C*03:04;, features a modification of the amino acid from E to K at position 197.
+The protein's natural variant, known as in allele C*05:01, allele C*07:04 and allele C*08:01;, features a modification of the amino acid from E to K at position 201.
+The protein's natural variant, known as in allele C*01:02, allele C*02:02, allele C*03:02, allele C*03:04, allele C*04:01, allele C*05:01, allele C*06:02, allele C*08:01, allele C*12:02, allele C*14:02, allele C*15:02, allele C*16:01 and allele C*18:01;, features a modification of the amino acid from P to H at position 208.
+The protein's natural variant, known as in allele C*17:01;, features a modification of the amino acid from P to R at position 208.
+The protein's natural variant, known as in allele C*16:01;, features a modification of the amino acid from P to L at position 217.
+The protein's natural variant, known as in allele C*01:02, allele C*02:02, allele C*03:02, allele C*03:04, allele C*04:01, allele C*05:01, allele C*06:02, allele C*08:01, allele C*12:02, allele C*14:02, allele C*15:02, allele C*16:01, allele C*17:01 and allele C*18:01;, features a modification of the amino acid from L to V at position 218.
+The protein's natural variant, known as in allele C*02:02;, features a modification of the amino acid from A to T at position 235.
+The protein's natural variant, known as in alleles C*01:02, allele C*03:02, allele C*03:04, allele C*04:01, allele C*14:02 and allele C*18:01;, features a modification of the amino acid from R to W at position 243.
+The protein's natural variant, known as in allele C*01:02;, features a modification of the amino acid from V to M at position 272.
+The protein's natural variant, known as in allele C*01:02, allele C*02:02, allele C*03:02, allele C*03:04, allele C*04:01, allele C*05:01, allele C*06:02, allele C*08:01, allele C*12:02, allele C*14:02, allele C*15:02, allele C*16:01 and allele C*18:01;, features a modification of the amino acid from Q to E at position 277.
+The protein's natural variant, known as in allele C*01:02, allele C*02:02, allele C*03:02, allele C*03:04, allele C*04:01, allele C*05:01, allele C*06:02, allele C*08:01, allele C*12:02, allele C*14:02, allele C*15:02, allele C*16:01, allele C*17:01 and allele C*18:01;, features a modification of the amino acid from M to V at position 285.
+The protein's natural variant, known as in allele C*01:02, allele C*02:02, allele C*03:02, allele C*03:04, allele C*04:01, allele C*05:01, allele C*06:02, allele C*08:01, allele C*12:02, allele C*14:02, allele C*15:02, allele C*16:01 and allele C*18:01;, features a modification of the amino acid from Q to P at position 291.
+The protein's natural variant, known as in allele C*17:01; requires 2 nucleotide substitutions;, features a modification of the amino acid from L to C at position 294.
+The protein's natural variant, known as in allele C*01:02, allele C*02:02, allele C*03:02, allele C*03:04, allele C*04:01, allele C*05:01, allele C*06:02, allele C*08:01, allele C*12:02, allele C*14:02, allele C*15:02, allele C*16:01, allele C*17:01 and allele C*18:01;, features a modification of the amino acid from S to R at position 297.
+The protein's natural variant, known as in alleles C*05:01 and allele C*08:01, features a modification of the amino acid from E to G at position 299.
+The protein's natural variant, known as in allele C*04:01, allele C*17:01 and allele C*18:01;, features a modification of the amino acid from E to K at position 299.
+The protein's natural variant, known as in allele C*17:01, features a modification of the amino acid from IMGIVAGLAVLV to NLGIVSGPAVLAVLAVLA at position 319.
+The protein's natural variant, known as in allele C*01:02, allele C*02:02, allele C*03:02, allele C*03:04, allele C*04:01, allele C*05:01, allele C*06:02, allele C*08:01, allele C*12:02, allele C*14:02, allele C*15:02, allele C*16:01 and allele C*18:01;, features a modification of the amino acid from M to V at position 309.
+The protein's natural variant, known as in allele C*01:02, allele C*02:02, allele C*03:02, allele C*03:04, allele C*04:01, allele C*05:01, allele C*06:02, allele C*08:01, allele C*12:02, allele C*14:02, allele C*15:02 and allele C*16:01;, features a modification of the amino acid from V to A at position 319.
+The protein's natural variant, known as in allele C*04:01;, features a modification of the amino acid from V to M at position 327.
+The protein's natural variant, known as in allele C*05:01, allele C*06:02, allele C*08:01, allele C*12:02 and allele C*15:02, features a modification of the amino acid from V to M at position 328.
+The protein's natural variant, known as in allele C*01:02, allele C*02:02, allele C*03:02, allele C*03:04, allele C*04:01, allele C*05:01, allele C*06:02, allele C*08:01, allele C*12:02, allele C*14:02, allele C*15:02, allele C*16:01, allele C*17:01 and allele C*18:01;, features a modification of the amino acid from T to A at position 329.
+The protein's natural variant, known as in allele C*02:02, allele C*04:01, allele C*05:01, allele C*06:02, allele C*08:01, allele C*12:02, allele C*14:02, allele C*15:02, allele C*16:01 and allele C*18:01;, features a modification of the amino acid from A to V at position 330.
+The protein's natural variant, known as in allele C*01:02, allele C*02:02, allele C*03:02, allele C*03:04, allele C*04:01, allele C*05:01, allele C*06:02, allele C*08:01, allele C*12:02, allele C*14:02, allele C*15:02, allele C*16:01, allele C*17:01 and allele C*18:01;, features a modification of the amino acid from M to V at position 331.
+The protein's natural variant, known as in allele C*17:01;, features a modification of the amino acid from M to I at position 332.
+The protein's natural variant, known as in allele C*17:01; requires 2 nucleotide substitutions, features a modification of the amino acid from C to H at position 333.
+The protein's natural variant, known as in allele C*01:02, allele C*02:02, allele C*03:02, allele C*03:04, allele C*04:01, allele C*05:01, allele C*06:02, allele C*08:01, allele C*12:02, allele C*14:02, allele C*15:02, allele C*16:01, allele C*17:01 and allele C*18:01;, features a modification of the amino acid from C to S at position 350.
+The protein's natural variant, known as in allele C*01:02, allele C*02:02, allele C*03:02, allele C*03:04, allele C*04:01, allele C*05:01, allele C*06:02, allele C*08:01, allele C*12:02, allele C*14:02, allele C*15:02, allele C*16:01, allele C*17:01 and allele C*18:01;, features a modification of the amino acid from T to A at position 363.
+The protein's natural variant, known as in CILD34; loss of expression in patient cells; increased proteasome-mediated degradation; no effect on homodimerization;, features a modification of the amino acid from M to R at position 278.
+The protein's natural variant, known as in NEDISHM;, features a modification of the amino acid from C to F at position 1233.
+The protein's natural variant, known as in NEDISHM, features a modification of the amino acid from R to T at position 1500.
+The protein's natural variant, known as in MRT27; unknown pathological significance;, features a modification of the amino acid from E to K at position 313.
+The natural variant of this protein is characterized by an amino acid alteration from E to L at position 56.
+The natural variant of this protein is characterized by an amino acid alteration from L to G at position 63.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from S to F at position 474.
+The protein's natural variant, known as in strain: DM4593, features a modification of the amino acid from A to T at position 121.
+The protein's natural variant, known as in MCPH22; impairs mitotic chromosome compaction;, features a modification of the amino acid from E to A at position 1153.
+The protein's natural variant, known as in L2HGA;, features a modification of the amino acid from G to D at position 55.
+The protein's natural variant, known as in L2HGA;, features a modification of the amino acid from G to R at position 57.
+The protein's natural variant, known as in L2HGA; alters protein processing and abolishes catalytic activity;, features a modification of the amino acid from K to E at position 81.
+The protein's natural variant, known as in L2HGA;, features a modification of the amino acid from H to R at position 98.
+The protein's natural variant, known as in L2HGA, features a modification of the amino acid from H to Y at position 98.
+The protein's natural variant, known as in L2HGA; alters protein processing and abolishes catalytic activity, features a modification of the amino acid from E to D at position 176.
+The protein's natural variant, known as in L2HGA;, features a modification of the amino acid from P to L at position 302.
+The protein's natural variant, known as in L2HGA;, features a modification of the amino acid from H to P at position 434.
+The protein's natural variant, known as in DIAR2, features a modification of the amino acid from H to R at position 81.
+The protein's natural variant, known as in DIAR2, features a modification of the amino acid from E to K at position 82.
+The protein's natural variant, known as in PFIC10, features a modification of the amino acid from R to C at position 92.
+The protein's natural variant, known as in DIAR2;, features a modification of the amino acid from V to G at position 108.
+The protein's natural variant, known as in PFIC10; unknown pathological significance, features a modification of the amino acid from Y to C at position 119.
+The protein's natural variant, known as in DIAR2, features a modification of the amino acid from A to E at position 143.
+The protein's natural variant, known as in PFIC10; unknown pathological significance, features a modification of the amino acid from S to F at position 158.
+The protein's natural variant, known as in DIAR2;, features a modification of the amino acid from G to R at position 168.
+The protein's natural variant, known as in DIAR2;, features a modification of the amino acid from R to H at position 219.
+The protein's natural variant, known as in PFIC10; decreased ABCB11 targeting to the apical/canalicular plasma membrane in hepatocytes from a homozygous patient, features a modification of the amino acid from C to R at position 266.
+The protein's natural variant, known as in DIAR2;, features a modification of the amino acid from G to R at position 316.
+The protein's natural variant, known as in DIAR2; unknown pathological significance, features a modification of the amino acid from G to V at position 316.
+The protein's natural variant, known as in DIAR2; unknown pathological significance, features a modification of the amino acid from G to R at position 336.
+The protein's natural variant, known as in PFIC10 and DIAR2, features a modification of the amino acid from M to T at position 392.
+The protein's natural variant, known as in PFIC10, features a modification of the amino acid from R to C at position 401.
+The protein's natural variant, known as in DIAR2;, features a modification of the amino acid from R to H at position 401.
+The protein's natural variant, known as in DIAR2; unknown pathological significance, features a modification of the amino acid from I to N at position 416.
+The protein's natural variant, known as in DIAR2;, features a modification of the amino acid from G to R at position 435.
+The protein's natural variant, known as in DIAR2, features a modification of the amino acid from N to S at position 456.
+The protein's natural variant, known as in PFIC10; unknown pathological significance, features a modification of the amino acid from I to T at position 488.
+The protein's natural variant, known as in DIAR2; unknown pathological significance, features a modification of the amino acid from D to G at position 492.
+The protein's natural variant, known as in DIAR2; unknown pathological significance, features a modification of the amino acid from I to F at position 497.
+The protein's natural variant, known as in PFIC10; unknown pathological significance, features a modification of the amino acid from I to T at position 500.
+The protein's natural variant, known as in DIAR2, features a modification of the amino acid from C to R at position 514.
+The protein's natural variant, known as in PFIC10; unknown pathological significance, features a modification of the amino acid from P to L at position 517.
+The protein's natural variant, known as in PFIC10; unknown pathological significance, features a modification of the amino acid from S to N at position 535.
+The protein's natural variant, known as in DIAR2; found in a compound heterozygote also carrying F-550; enterocytes carrying S-538 and F-550 display disruption of cell polarity, mislocalized apical and basolateral transporter proteins and altered distribution of endosomal/lysosomal constituents including Rab GTPases, features a modification of the amino acid from F to S at position 538.
+The protein's natural variant, known as in DIAR2; found in a compound heterozygote also carrying S-538; enterocytes carrying S-538 and F-550 display disruption of cell polarity, mislocalized apical and basolateral transporter proteins and altered distribution of endosomal/lysosomal constituents including Rab GTPases, features a modification of the amino acid from I to F at position 550.
+The protein's natural variant, known as in PFIC10; unknown pathological significance, features a modification of the amino acid from V to L at position 557.
+The protein's natural variant, known as in DIAR2; unknown pathological significance, features a modification of the amino acid from L to P at position 580.
+The protein's natural variant, known as in PFIC10; unknown pathological significance, features a modification of the amino acid from S to N at position 583.
+The protein's natural variant, known as in PFIC10; unknown pathological significance, features a modification of the amino acid from L to P at position 642.
+The protein's natural variant, known as in PFIC10, features a modification of the amino acid from Y to C at position 654.
+The protein's natural variant, known as in DIAR2;, features a modification of the amino acid from R to C at position 656.
+The protein's natural variant, known as in DIAR2; patient enterocytes show alterations in junctional composition, loss of polarity in basolateral and apical compartments, loss of apical brush border and formation of microvillus inclusions in cells at the villus tips; the mutation causes the motor to move slowly along F-actin;, features a modification of the amino acid from P to L at position 660.
+The protein's natural variant, known as in DIAR2; unknown pathological significance, features a modification of the amino acid from T to M at position 686.
+The protein's natural variant, known as in PFIC10; unknown pathological significance, features a modification of the amino acid from R to W at position 799.
+The protein's natural variant, known as in PFIC10, features a modification of the amino acid from R to C at position 824.
+The protein's natural variant, known as in PFIC10; unknown pathological significance, features a modification of the amino acid from I to S at position 934.
+The protein's natural variant, known as in PFIC10; unknown pathological significance, features a modification of the amino acid from Q to H at position 1079.
+The protein's natural variant, known as in DIAR2; unknown pathological significance, features a modification of the amino acid from L to P at position 1361.
+The protein's natural variant, known as in DIAR2, features a modification of the amino acid from L to R at position 1556.
+The protein's natural variant, known as in isozyme 2, features a modification of the amino acid from G to S at position 18.
+The protein's natural variant, known as in isozyme 2, features a modification of the amino acid from E to D at position 104.
+The protein's natural variant, known as in isozyme 2, features a modification of the amino acid from G to V at position 221.
+The protein's natural variant, known as in isozyme 2, features a modification of the amino acid from S to T at position 227.
+The protein's natural variant, known as in isozyme 2, features a modification of the amino acid from E to K at position 245.
+The protein's natural variant, known as in isozyme 2, features a modification of the amino acid from L to P at position 270.
+The protein's natural variant, known as in isozyme 2, features a modification of the amino acid from E to D at position 375.
+The protein's natural variant, known as in isozyme 2, features a modification of the amino acid from L to F at position 411.
+The protein's natural variant, known as in isozyme 2, features a modification of the amino acid from A to V at position 413.
+The protein's natural variant, known as in isozyme 2, features a modification of the amino acid from K to R at position 466.
+The protein's natural variant, known as in an ovarian papillary serous adenocarcinoma sample; somatic mutation, features a modification of the amino acid from L to I at position 98.
+The protein's natural variant, known as in an ovarian mucinous carcinoma sample; somatic mutation;, features a modification of the amino acid from R to Q at position 149.
+The protein's natural variant, known as in CSYN;, features a modification of the amino acid from T to M at position 280.
+The protein's natural variant, known as in alpha-A', features a modification of the amino acid from T to I at position 34.
+The protein's natural variant, known as in haplotype K1, allele pvr6(8), features a modification of the amino acid from P to T at position 15.
+The protein's natural variant, known as in haplotype F1, allele pvr6(6), features a modification of the amino acid from P to T at position 16.
+The protein's natural variant, known as in haplotypes G1 and G2, allele pvr6(9). In haplotype E1, allele pvr6(5). In haplotype H1, allele pvr6(7). In haplotype Ih1, features a modification of the amino acid from A to E at position 20.
+The protein's natural variant, known as in haplotype A1, allele pvr6(2), features a modification of the amino acid from A to T at position 20.
+The protein's natural variant, known as in haplotypes G1 and G2, allele pvr6(9). In haplotype H1, allele pvr6(7), features a modification of the amino acid from V to A at position 24.
+The protein's natural variant, known as in haplotype K1, allele pvr6(8), features a modification of the amino acid from V to E at position 24.
+The protein's natural variant, known as in haplotype Ih1, features a modification of the amino acid from V to S at position 24.
+The protein's natural variant, known as in haplotype B1, allele pvr6(3), features a modification of the amino acid from P to S at position 27.
+The protein's natural variant, known as in haplotype K1, allele pvr6(8), features a modification of the amino acid from K to N at position 56.
+The protein's natural variant, known as in haplotype H1, allele pvr6(7). In haplotype Ih1, features a modification of the amino acid from V to I at position 63.
+The protein's natural variant, known as in strain: cv. CDP01246; haplotype D1, allele pvr6(4). In haplotype B1, allele pvr6(3), features a modification of the amino acid from A to T at position 90.
+The protein's natural variant, known as in haplotype K1, allele pvr6(8), features a modification of the amino acid from A to P at position 115.
+The protein's natural variant, known as in haplotype E1, allele pvr6(5), features a modification of the amino acid from T to I at position 119.
+The protein's natural variant, known as in allele Sej; non-secretor phenotype;, features a modification of the amino acid from I to F at position 140.
+The protein's natural variant, known as in COXPD47; strong decrease in mitochondrial translation and in oxidative phosphorylation biogenesis; this phenotype could be reversed in patient's fibroblasts by transfection with the wild-type protein;, features a modification of the amino acid from K to R at position 119.
+The protein's natural variant, known as in strain: Zimbabwe 53, features a modification of the amino acid from L to M at position 170.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation;, features a modification of the amino acid from R to Q at position 191.
+The protein's natural variant, known as in LCCS6; loss of function mutation;, features a modification of the amino acid from R to H at position 397.
+The protein's natural variant, known as frequent in Golden retrievers and Labrador retrievers, features a modification of the amino acid from N to K at position 263.
+The protein's natural variant, known as in strain: Shiba, features a modification of the amino acid from S to G at position 607.
+The protein's natural variant, known as in strain: Isolate 13, features a modification of the amino acid from Q to K at position 137.
+The protein's natural variant, known as in strain: Isolate 13, features a modification of the amino acid from A to P at position 197.
+The protein's natural variant, known as in strain: Isolate 13, features a modification of the amino acid from D to N at position 419.
+The protein's natural variant, known as in strain: Isolate 13, features a modification of the amino acid from CLN to SLY at position 450.
+The protein's natural variant, known as in strain: Isolate 13, features a modification of the amino acid from T to A at position 482.
+The protein's natural variant, known as in strain: Isolate 13, features a modification of the amino acid from M to I at position 529.
+The protein's natural variant, known as in strain: Isolate 13, features a modification of the amino acid from L to F at position 573.
+The protein's natural variant, known as in strain: Isolate 13, features a modification of the amino acid from P to A at position 578.
+The protein's natural variant, known as in a patient with non small cell lung carcinomas; homozygous;, features a modification of the amino acid from P to L at position 166.
+The protein's natural variant, known as in a patient with non small cell lung carcinomas, features a modification of the amino acid from R to P at position 202.
+The protein's natural variant, known as in a patient with non small cell lung carcinomas, features a modification of the amino acid from F to S at position 536.
+The protein's natural variant, known as in OAZON; unknown pathological significance, features a modification of the amino acid from G to R at position 161.
+The protein's natural variant, known as associated with increased risk for thiopurines toxicity; decreased thermostability; decreased diphosphatase activity towards 6-thio-dGTP and 6-thio-GTP;, features a modification of the amino acid from V to I at position 18.
+The protein's natural variant, known as associated with increased risk for thiopurines toxicity; decreased thermostability; decreased diphosphatase activity towards 6-thio-dGTP and 6-thio-GTP, features a modification of the amino acid from V to VGV at position 18.
+The protein's natural variant, known as associated with increased risk for thiopurines toxicity; decreased thermostability; loss of diphosphatase activity towards 6-thio-dGTP and 6-thio-GTP;, features a modification of the amino acid from R to C at position 139.
+The protein's natural variant, known as associated with increased risk for thiopurines toxicity; decreased thermostability; decreased diphosphatase activity towards 6-thio-dGTP and 6-thio-GTP;, features a modification of the amino acid from R to H at position 139.
+The protein's natural variant, known as in NIDDM; abolishes transport activity of the transporter expressed in Xenopus oocytes;, features a modification of the amino acid from V to I at position 197.
+The protein's natural variant, known as in FBS;, features a modification of the amino acid from L to P at position 389.
+The protein's natural variant, known as in FBS;, features a modification of the amino acid from P to L at position 417.
+The protein's natural variant, known as in FBS;, features a modification of the amino acid from V to E at position 423.
+The protein's natural variant, known as in 50% of the molecules, features a modification of the amino acid from T to A at position 55.
+The protein's natural variant, known as in HYXKY; reduced 3-hydroxykynureninase activity;, features a modification of the amino acid from T to A at position 198.
+The protein's natural variant, known as in MLIIIA; also found in patients with intermediate phenotype between MLII and MLIIIA; no effect on protein abundance; decreased retention in the Golgi; mistargeted to lysosomes and plasma membrane; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity;, features a modification of the amino acid from K to Q at position 4.
+The protein's natural variant, known as in MLIIIA; unknown pathological significance; no effect on protein abundance; decreased protein cleavage into alpha and beta subunits; decreased retention in the Golgi; mistargeted to lysosomes and plasma membrane; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity;, features a modification of the amino acid from S to Y at position 15.
+The protein's natural variant, known as in MLII; loss of Golgi localization; defects in protein cleavage into alpha and beta subunits; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity, features a modification of the amino acid from D to G at position 76.
+The protein's natural variant, known as in MLII and MLIIIA; no effect on protein abundance; decreased localization to the Golgi; defects in protein cleavage into alpha and beta subunits; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity;, features a modification of the amino acid from W to L at position 81.
+The protein's natural variant, known as in MLII; unknown pathological significance; decreased localization to the Golgi; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity;, features a modification of the amino acid from V to D at position 182.
+The protein's natural variant, known as in MLIIIA; also found in patients with intermediate phenotype between MLII and MLIIIA; unknown pathological significance; no effect on protein abundance; no effect on localization to the Golgi; no effect on protein cleavage into alpha and beta subunits; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity;, features a modification of the amino acid from D to V at position 190.
+The protein's natural variant, known as in MLII; unknown pathological significance;, features a modification of the amino acid from Q to P at position 205.
+The protein's natural variant, known as in MLII; no effect on protein abundance; loss of localization to the Golgi; loss of protein cleavage into alpha and beta subunits; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity;, features a modification of the amino acid from R to L at position 334.
+The protein's natural variant, known as in MLIIIA; no effect on protein abundance; loss of localization to the Golgi; loss of protein cleavage into alpha and beta subunits; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity;, features a modification of the amino acid from R to Q at position 334.
+The protein's natural variant, known as in MLII; unknown pathological significance; no effect on protein abundance; no effect on localization to the Golgi; no effect on protein cleavage into alpha and beta subunits; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity;, features a modification of the amino acid from I to L at position 348.
+The protein's natural variant, known as in MLII and MLIIIA; no effect on protein abundance; no effect on localization to the Golgi; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity;, features a modification of the amino acid from F to L at position 374.
+The protein's natural variant, known as in MLII; no loss of Golgi localization; no defects in protein cleavage into alpha and beta subunits; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity, features a modification of the amino acid from S to L at position 385.
+The protein's natural variant, known as in MLIIIA; no effect on protein abundance; loss of localization to the Golgi; defects in protein cleavage into alpha and beta subunits; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity;, features a modification of the amino acid from S to F at position 399.
+The protein's natural variant, known as in MLIIIA; loss of localization to the Golgi; loss of protein cleavage into alpha and beta subunits; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity;, features a modification of the amino acid from I to T at position 403.
+The protein's natural variant, known as in MLIIIA; no effect on protein abundance; no effect on localization to the Golgi; no effect on protein cleavage into alpha and beta subunits; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity;, features a modification of the amino acid from D to A at position 407.
+The protein's natural variant, known as in MLIIIA; no effect on localization to the Golgi; no effect on protein cleavage into alpha and beta subunits; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity toward some substrates;, features a modification of the amino acid from C to Y at position 442.
+The protein's natural variant, known as rare variant; found in individuals suffering from stuttering; unknown pathological significance;, features a modification of the amino acid from A to S at position 455.
+The protein's natural variant, known as in MLIIIA; no effect on protein abundance; no effect on localization to the Golgi; no effect on protein cleavage into alpha and beta subunits; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity toward some substrates;, features a modification of the amino acid from C to G at position 461.
+The protein's natural variant, known as in MLIIIA; patients with intermediate phenotype between MLII and MLIIIA; no effect on protein abundance; no effect on localization to the Golgi; no effect on protein cleavage into alpha and beta subunits; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity toward some substrates;, features a modification of the amino acid from C to S at position 468.
+The protein's natural variant, known as in MLIIIA; unknown pathological significance; decreased localization to the Golgi; decreased protein cleavage into alpha and beta subunits; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity; reduces protein abundance;, features a modification of the amino acid from C to Y at position 505.
+The protein's natural variant, known as found in a patient with mucolipidosis type II or III; unknown pathological significance; decreased localization to the Golgi; decreased protein cleavage into alpha and beta subunits; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity, features a modification of the amino acid from C to R at position 523.
+The protein's natural variant, known as in MLIIIA; significantly reduces protein cleavage into alpha and beta subunits; reduces protein abundance; significantly decreased localization to the Golgi; significantly reduces UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase, features a modification of the amino acid from G to R at position 575.
+The protein's natural variant, known as in MLIIIA; decreased localization to the Golgi; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity;, features a modification of the amino acid from R to P at position 587.
+The protein's natural variant, known as found in a patient with mucolipidosis type II or III; unknown pathological significance; decreased localization to the Golgi; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity;, features a modification of the amino acid from A to T at position 592.
+The protein's natural variant, known as rare variant; found in individuals suffering from stuttering; unknown pathological significance;, features a modification of the amino acid from F to L at position 625.
+The protein's natural variant, known as in MLIIIA; reduces protein cleavage into alpha and beta subunits; reduces protein abundance; no effect on subcellular location in Golgi apparatus; mildly affects UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase;, features a modification of the amino acid from T to M at position 644.
+The protein's natural variant, known as in MLII; no effect on localization to the Golgi; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity toward some substrates;, features a modification of the amino acid from K to N at position 732.
+The protein's natural variant, known as found in a patient with mucolipidosis type II or III; unknown pathological significance; no effect on localization to the Golgi; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity toward some substrates;, features a modification of the amino acid from L to W at position 785.
+The protein's natural variant, known as in MLIIIA; no effect on localization to the Golgi; loss of protein cleavage into alpha and beta subunits; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity;, features a modification of the amino acid from Q to P at position 926.
+The protein's natural variant, known as in MLII; unknown pathological significance;, features a modification of the amino acid from K to R at position 928.
+The protein's natural variant, known as in MLII; unknown pathological significance; no effect on protein abundance; no effect on localization to the Golgi; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity;, features a modification of the amino acid from A to V at position 955.
+The protein's natural variant, known as in MLIIIA; unknown pathological significance;, features a modification of the amino acid from H to R at position 956.
+The protein's natural variant, known as in MLIIIA; no effect on protein abundance; no effect on localization to the Golgi;, features a modification of the amino acid from H to Y at position 956.
+The protein's natural variant, known as in MLII; decreased protein abundance; no effect on localization to the Golgi; no effect on protein cleavage into alpha and beta subunits; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity;, features a modification of the amino acid from R to C at position 986.
+The protein's natural variant, known as in MLII; no effect on protein abundance; decreased localization to the Golgi; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity;, features a modification of the amino acid from L to P at position 1001.
+The protein's natural variant, known as in MLIIIA; patients with intermediate phenotype between MLII and MLIIIA; unknown pathological significance; no effect on protein abundance; decreased localization to the Golgi; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity;, features a modification of the amino acid from D to G at position 1018.
+The protein's natural variant, known as in MLII; unknown pathological significance; no effect on localization to the Golgi; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity;, features a modification of the amino acid from L to V at position 1054.
+The protein's natural variant, known as in MLIIIA; no effect on protein abundance; no effect on localization to the Golgi; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity;, features a modification of the amino acid from N to S at position 1153.
+The protein's natural variant, known as may be a risk factor for stuttering;, features a modification of the amino acid from E to K at position 1200.
+The protein's natural variant, known as in MLII; decreased protein abundance; no effect on localization to the Golgi; does not suppress protein cleavage into alpha and beta subunits; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity, features a modification of the amino acid from K to M at position 1236.
+The protein's natural variant, known as in NEDAUS; decreases interaction with KEAP1;, features a modification of the amino acid from V to A at position 285.
+The protein's natural variant, known as in PHA2E;, features a modification of the amino acid from D to G at position 413.
+The protein's natural variant, known as in PHA2E;, features a modification of the amino acid from K to R at position 459.
+The protein's natural variant, known as found in a patient with autism spectrum disorder; unknown pathological significance;, features a modification of the amino acid from H to R at position 719.
+The protein's natural variant, known as in a breast infiltrating ductal carcinoma sample; somatic mutation, features a modification of the amino acid from P to L at position 108.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation;, features a modification of the amino acid from E to K at position 422.
+The protein's natural variant, known as in a lung large cell carcinoma sample; somatic mutation, features a modification of the amino acid from S to N at position 472.
+The protein's natural variant, known as in a lung squamous cell carcinoma sample; somatic mutation;, features a modification of the amino acid from R to C at position 554.
+The protein's natural variant, known as in a renal clear cell carcinoma sample; somatic mutation, features a modification of the amino acid from G to R at position 570.
+The protein's natural variant, known as in a colorectal adenocarcinoma sample; somatic mutation, features a modification of the amino acid from V to A at position 596.
+The protein's natural variant, known as in SRTD11, features a modification of the amino acid from C to F at position 148.
+The protein's natural variant, known as in SRTD11, features a modification of the amino acid from R to W at position 182.
+The protein's natural variant, known as in SRTD11;, features a modification of the amino acid from A to V at position 341.
+The protein's natural variant, known as in SRTD11;, features a modification of the amino acid from T to M at position 354.
+The protein's natural variant, known as in SRTD11, features a modification of the amino acid from P to L at position 390.
+The protein's natural variant, known as in SRTD11;, features a modification of the amino acid from G to S at position 393.
+The protein's natural variant, known as in SRTD11, features a modification of the amino acid from S to I at position 410.
+The protein's natural variant, known as in SRTD11;, features a modification of the amino acid from K to R at position 436.
+The protein's natural variant, known as in SRTD11;, features a modification of the amino acid from R to Q at position 447.
+The protein's natural variant, known as in SRTD11;, features a modification of the amino acid from R to W at position 447.
+The protein's natural variant, known as in WVS; decreased histone methyltransferase activity;, features a modification of the amino acid from P to S at position 132.
+The protein's natural variant, known as in WVS; decreased histone methyltransferase activity, features a modification of the amino acid from Y to C at position 133.
+The protein's natural variant, known as in WVS, features a modification of the amino acid from M to T at position 134.
+The protein's natural variant, known as in WVS, features a modification of the amino acid from K to E at position 156.
+The protein's natural variant, known as decreased histone methyltransferase activity;, features a modification of the amino acid from D to H at position 185.
+The protein's natural variant, known as in WVS, features a modification of the amino acid from H to R at position 279.
+The protein's natural variant, known as found in a patient with myelodysplastic syndrome and myelodysplastic-myeloproliferative neoplasms; somatic mutation; loss of histone methyltransferase activity, features a modification of the amino acid from C to W at position 571.
+The protein's natural variant, known as in WVS; unknown pathological significance;, features a modification of the amino acid from V to M at position 621.
+The protein's natural variant, known as in a patient with diffuse large B-cell lymphoma; somatic mutation; changed substrate preferences; prefers substrates with greater methylation H3K27me0<me1<me2, features a modification of the amino acid from Y to C at position 641.
+The protein's natural variant, known as found in a patient with follicular lymphoma; also in diffuse large B-cell lymphoma; somatic mutation; changed substrate preferences; prefers substrates with greater methylation H3K27me0<me1<me2;, features a modification of the amino acid from Y to F at position 641.
+The protein's natural variant, known as found in patients with follicular lymphoma; also in diffuse large B-cell lymphoma; somatic mutation; changed substrate preferences; prefers substrates with greater methylation H3K27me0<me1<me2;, features a modification of the amino acid from Y to H at position 641.
+The protein's natural variant, known as found in patients with follicular lymphoma; also in diffuse large B-cell lymphoma; somatic mutation; changed substrate preferences; prefers substrates with greater methylation H3K27me0<me1<me2;, features a modification of the amino acid from Y to N at position 641.
+The protein's natural variant, known as found in patients with follicular lymphoma; also in diffuse large B-cell lymphoma; somatic mutation;, features a modification of the amino acid from Y to S at position 641.
+The protein's natural variant, known as in WVS, features a modification of the amino acid from Y to N at position 658.
+The protein's natural variant, known as found in a patient with B-cell lymphoma; increased hypertrimethylation of H3K27; changed substrate preferences; confers biochemical activity independent of H3K27 methylation state;, features a modification of the amino acid from A to G at position 677.
+The protein's natural variant, known as in WVS;, features a modification of the amino acid from A to T at position 677.
+The protein's natural variant, known as in WVS; decreased histone methyltransferase activity;, features a modification of the amino acid from R to C at position 679.
+The protein's natural variant, known as found in a patient with myeloid disorders; somatic mutation; loss of histone methyltransferase activity, features a modification of the amino acid from R to C at position 685.
+The protein's natural variant, known as in a patient with chronic myelomonocytic leukemia;, features a modification of the amino acid from R to H at position 685.
+The protein's natural variant, known as in WVS; decreased histone methyltransferase activity;, features a modification of the amino acid from H to Y at position 689.
+The protein's natural variant, known as in WVS, features a modification of the amino acid from S to L at position 690.
+The protein's natural variant, known as found in a patient with chronic myelomonocytic leukemia; somatic mutation; loss of histone methyltransferase activity, features a modification of the amino acid from Y to D at position 726.
+The protein's natural variant, known as in WVS, features a modification of the amino acid from Y to C at position 736.
+The protein's natural variant, known as in WVS; unknown pathological significance;, features a modification of the amino acid from E to K at position 740.
+The protein's natural variant, known as in strain: XH1549, features a modification of the amino acid from I to V at position 3.
+The protein's natural variant, known as in strain: AS2.101, AS2.1406, AS2.179, AS2.7, AS2.724, AS2.771, AS2.820 and AS2.93, features a modification of the amino acid from R to Q at position 6.
+The protein's natural variant, known as in strain: XH1549, features a modification of the amino acid from NK to T at position 10.
+The protein's natural variant, known as in strain: XH1549, features a modification of the amino acid from I to L at position 16.
+The protein's natural variant, known as in strain: XH1549, features a modification of the amino acid from K to Q at position 19.
+The protein's natural variant, known as in strain: XH1549, features a modification of the amino acid from T to S at position 22.
+The protein's natural variant, known as in strain: XH1549, features a modification of the amino acid from V to G at position 32.
+The protein's natural variant, known as in strain: AS2.101, AS2.1406, AS2.179, AS2.7, AS2.724, AS2.771, AS2.820, AS2.93 and XH1549, features a modification of the amino acid from S to N at position 42.
+The protein's natural variant, known as in strain: AS2.724 and AS2.820, features a modification of the amino acid from R to H at position 92.
+The protein's natural variant, known as in MECD1;, features a modification of the amino acid from M to T at position 129.
+The protein's natural variant, known as in MECD1;, features a modification of the amino acid from M to V at position 129.
+The protein's natural variant, known as in MECD1;, features a modification of the amino acid from Q to P at position 130.
+The protein's natural variant, known as in MECD1; increased expression of keratins KRT5, KRT6, KRT14 and KRT16 and decreased expression of KRT12 in the corneal epithelium; increased expression of DDIT3/CHOP and CASP12 in the corneal epithelium indicative of up-regulation of the unfolded protein response.;, features a modification of the amino acid from L to P at position 132.
+The protein's natural variant, known as in MECD1, features a modification of the amino acid from L to V at position 132.
+The protein's natural variant, known as in MECD1;, features a modification of the amino acid from R to G at position 135.
+The protein's natural variant, known as in MECD1;, features a modification of the amino acid from R to I at position 135.
+The protein's natural variant, known as in MECD1;, features a modification of the amino acid from R to S at position 135.
+The protein's natural variant, known as in MECD1;, features a modification of the amino acid from R to T at position 135.
+The protein's natural variant, known as in MECD1;, features a modification of the amino acid from A to P at position 137.
+The protein's natural variant, known as in MECD1, features a modification of the amino acid from L to Q at position 140.
+The protein's natural variant, known as in MECD1;, features a modification of the amino acid from L to R at position 140.
+The protein's natural variant, known as in MECD1;, features a modification of the amino acid from V to L at position 143.
+The protein's natural variant, known as in MECD1; unknown pathological significance;, features a modification of the amino acid from D to N at position 248.
+The protein's natural variant, known as in MECD1, features a modification of the amino acid from L to LISNLEAQLL at position 399.
+The protein's natural variant, known as in MECD1;, features a modification of the amino acid from I to S at position 426.
+The protein's natural variant, known as in MECD1; unknown pathological significance;, features a modification of the amino acid from I to V at position 426.
+The protein's natural variant, known as in MECD1;, features a modification of the amino acid from Y to C at position 429.
+The protein's natural variant, known as in MECD1;, features a modification of the amino acid from Y to D at position 429.
+The protein's natural variant, known as in MECD1;, features a modification of the amino acid from R to P at position 430.
+The protein's natural variant, known as in MECD1;, features a modification of the amino acid from L to R at position 433.
+The protein's natural variant, known as in HPMRS2; decrease in mannose-ethanolamine phosphotransferase activity;, features a modification of the amino acid from R to W at position 119.
+The protein's natural variant, known as probable disease-associated variant found in a patient with epileptic encephalopathy; decrease in mannose-ethanolamine phosphotransferase activity; decreased protein expression, features a modification of the amino acid from T to N at position 130.
+The protein's natural variant, known as found in patients with severe infantile epileptic encephalopathy; unknown pathological significance;, features a modification of the amino acid from M to I at position 255.
+The protein's natural variant, known as in HPMRS2; decrease in mannose-ethanolamine phosphotransferase activity; decreased protein expression; unknown pathological significance;, features a modification of the amino acid from M to K at position 344.
+The protein's natural variant, known as in HPMRS2; decrease in mannose-ethanolamine phosphotransferase activity; decreased protein expression;, features a modification of the amino acid from N to S at position 370.
+The protein's natural variant, known as in a colorectal cancer sample; somatic mutation, features a modification of the amino acid from L to M at position 686.
+The protein's natural variant, known as in HPMRS2; unknown pathological significance;, features a modification of the amino acid from H to P at position 871.
+The protein's natural variant, known as in HPMRS2;, features a modification of the amino acid from L to F at position 957.
+The protein's natural variant, known as in HPMRS2; decrease in mannose-ethanolamine phosphotransferase activity; increased protein expression, features a modification of the amino acid from K to E at position 1047.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from P to A at position 210.
+The protein's natural variant, known as in PPD1; unknown pathological significance;, features a modification of the amino acid from L to Q at position 506.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from T to I at position 514.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from E to Q at position 817.
+The natural variant of this protein is characterized by an amino acid alteration from D to A at position 884.
+The protein's natural variant, known as in primary osteoporosis, features a modification of the amino acid from A to T at position 29.
+The protein's natural variant, known as in OPPG; unknown pathological significance;, features a modification of the amino acid from W to R at position 79.
+The protein's natural variant, known as in OPTA1, features a modification of the amino acid from D to Y at position 111.
+The protein's natural variant, known as in OPPG; unknown pathological significance;, features a modification of the amino acid from R to Q at position 142.
+The protein's natural variant, known as in EVR4;, features a modification of the amino acid from L to F at position 145.
+The protein's natural variant, known as in HBM, features a modification of the amino acid from R to M at position 154.
+The protein's natural variant, known as in OPTA1;, features a modification of the amino acid from G to R at position 171.
+The protein's natural variant, known as in HBM; also in HBM individuals with enlarged mandible and torus palatinus; abolishes interaction with MESD; impairs transport to cell surface; no enhancement of DKK1 binding by MESD resulting in impaired inhibition of Wnt signaling by DKK1;, features a modification of the amino acid from G to V at position 171.
+The protein's natural variant, known as in EVR4; an individual with abnormal retinal vasculature and retinal folds;, features a modification of the amino acid from T to M at position 173.
+The protein's natural variant, known as in OPPG;, features a modification of the amino acid from D to N at position 203.
+The protein's natural variant, known as in WENHY;, features a modification of the amino acid from A to T at position 214.
+The protein's natural variant, known as in WENHY;, features a modification of the amino acid from A to V at position 214.
+The protein's natural variant, known as in OPTA1, VBCH2 and WENHY;, features a modification of the amino acid from A to T at position 242.
+The protein's natural variant, known as in OPPG; appears to traffic less well than does the wild-type protein; appears to be post-translationally modified similar to wild-type protein; is unable to transduce Wnt signal; has a significantly reduced ability to transduce Norrin signal;, features a modification of the amino acid from T to M at position 244.
+The protein's natural variant, known as in OPTA1;, features a modification of the amino acid from T to I at position 253.
+The protein's natural variant, known as in HBM; unknown pathological significance; lowered LRP5-mediated Wnt signaling; no effect on DKK1 binding, features a modification of the amino acid from M to V at position 282.
+The protein's natural variant, known as in OPPG;, features a modification of the amino acid from S to F at position 307.
+The protein's natural variant, known as in OPPG and EVR1; reduces Norrin signal transduction;, features a modification of the amino acid from R to W at position 348.
+The protein's natural variant, known as in OPPG, features a modification of the amino acid from R to Q at position 353.
+The protein's natural variant, known as in idiopathic osteoporosis and OPPG; appears to traffic comparably than does the wild-type protein; appears to be post-translationally modified similar to wild-type protein; is unable to transduce Wnt signal; has a significantly reduced ability to transduce Norrin signal;, features a modification of the amino acid from S to L at position 356.
+The protein's natural variant, known as in EVR1; reduces Norrin signal transduction;, features a modification of the amino acid from D to N at position 381.
+The protein's natural variant, known as in OPPG; is unable to traffic normally; appears to be post-translationally modified similar to wild-type protein; is unable to transduce Wnt signal; has a significantly reduced ability to transduce Norrin signal, features a modification of the amino acid from T to K at position 390.
+The protein's natural variant, known as in OPPG;, features a modification of the amino acid from A to E at position 400.
+The protein's natural variant, known as in OPPG; appears to traffic less well than does the wild-type protein; appears to be post-translationally modified similar to wild-type protein; has 50% of wild-type activity to transduce Wnt signal; has a significantly reduced ability to transduce Norrin signal;, features a modification of the amino acid from G to R at position 404.
+The protein's natural variant, known as in OPPG;, features a modification of the amino acid from T to A at position 409.
+The protein's natural variant, known as in EVR4; the mutation results in significantly reduced Norrin signal transduction;, features a modification of the amino acid from A to T at position 422.
+The protein's natural variant, known as in OPPG; unknown pathological significance; appears to traffic less well than does the wild-type protein; appears to be post-translationally modified similar to wild-type protein; has 50% of wild-type activity to transduce Wnt signal; has a significantly reduced ability to transduce Norrin signal;, features a modification of the amino acid from D to N at position 434.
+The protein's natural variant, known as in EVR4;, features a modification of the amino acid from E to K at position 441.
+The protein's natural variant, known as in EVR4; associated in a EVR1 patient with mutation Gln-417 in FZD4;, features a modification of the amino acid from R to C at position 444.
+The protein's natural variant, known as in PCLD4; unknown pathological significance;, features a modification of the amino acid from V to M at position 454.
+The protein's natural variant, known as in idiopathic osteoporosis; shows an inhibitory effect on Wnt signal transduction;, features a modification of the amino acid from S to L at position 455.
+The protein's natural variant, known as in OPPG;, features a modification of the amino acid from E to K at position 460.
+The protein's natural variant, known as in OPPG;, features a modification of the amino acid from W to R at position 478.
+The protein's natural variant, known as in OPPG;, features a modification of the amino acid from R to Q at position 494.
+The protein's natural variant, known as in OPPG;, features a modification of the amino acid from W to C at position 504.
+The protein's natural variant, known as in EVR4;, features a modification of the amino acid from D to A at position 511.
+The protein's natural variant, known as in OPPG; appears to traffic comparably than does the wild-type protein; appears to be post-translationally modified similar to wild-type protein; is unable to transduce Wnt signal; has a significantly reduced ability to transduce Norrin signal, features a modification of the amino acid from G to V at position 520.
+The protein's natural variant, known as in EVR4;, features a modification of the amino acid from A to T at position 522.
+The protein's natural variant, known as in OPPG, features a modification of the amino acid from N to I at position 531.
+The protein's natural variant, known as in EVR4; autosomal recessive;, features a modification of the amino acid from T to M at position 535.
+The protein's natural variant, known as in EVR4; the mutation results in significantly reduced Norrin signal transduction, features a modification of the amino acid from L to P at position 540.
+The protein's natural variant, known as in OPPG; unknown pathological significance, features a modification of the amino acid from L to P at position 541.
+The protein's natural variant, known as in EVR4; autosomal recessive;, features a modification of the amino acid from G to R at position 550.
+The protein's natural variant, known as found in a family affected by polycystic kidney and liver disease; unknown pathological significance; the patients carried additional PKD1 variants; the mutation results in significantly reduced WNT3A-induced signaling pathway;, features a modification of the amino acid from W to C at position 560.
+The protein's natural variant, known as in EVR4; autosomal recessive; has significantly reduced Wnt or Norrin signal transduction;, features a modification of the amino acid from R to Q at position 570.
+The protein's natural variant, known as in OPPG;, features a modification of the amino acid from R to W at position 570.
+The protein's natural variant, known as in EVR4 and OPPG; unknown pathological significance; appears to traffic less well than does the wild-type protein; appears to be post-translationally modified similar to wild-type protein; has 60% of wild-type activity to transduce Wnt signal; has a significantly reduced ability to transduce Norrin signal;, features a modification of the amino acid from G to R at position 610.
+The protein's natural variant, known as in EVR4; autosomal recessive;, features a modification of the amino acid from F to C at position 617.
+The protein's natural variant, known as in EVR1; reduces Norrin signal transduction;, features a modification of the amino acid from R to W at position 624.
+The protein's natural variant, known as in PCLD4; unknown pathological significance; the patient carried additional PKHD1 variant;, features a modification of the amino acid from K to E at position 638.
+The protein's natural variant, known as in OPPG;, features a modification of the amino acid from D to N at position 683.
+The protein's natural variant, known as in PCLD4; unknown pathological significance; the patient carried additional PKHD1 variant;, features a modification of the amino acid from V to A at position 684.
+The protein's natural variant, known as in OPPG;, features a modification of the amino acid from Y to H at position 733.
+The protein's natural variant, known as in EVR4; autosomal recessive;, features a modification of the amino acid from R to G at position 752.
+The protein's natural variant, known as in EVR4;, features a modification of the amino acid from T to A at position 798.
+The protein's natural variant, known as in EVR4;, features a modification of the amino acid from R to W at position 805.
+The protein's natural variant, known as likely benign variant; no effect on Norrin signal transduction, features a modification of the amino acid from Q to P at position 816.
+The protein's natural variant, known as in EVR4; de novo mutation found in a patient also carrying mutation P-540; unknown pathological significance; the mutation results in significantly reduced Norrin signal transduction;, features a modification of the amino acid from T to M at position 852.
+The protein's natural variant, known as in PCLD4; unknown pathological significance; the patient carried additional PKHD1 variant;, features a modification of the amino acid from R to C at position 925.
+The protein's natural variant, known as in primary osteoporosis; unknown pathological significance; found in a patient affected by polycystic kidney disease; unknown pathological significance;, features a modification of the amino acid from R to Q at position 1036.
+The protein's natural variant, known as in OPPG, features a modification of the amino acid from D to Y at position 1099.
+The protein's natural variant, known as in OPPG;, features a modification of the amino acid from R to C at position 1113.
+The protein's natural variant, known as in EVR4; unknown pathological significance;, features a modification of the amino acid from N to D at position 1121.
+The protein's natural variant, known as found in a patient affected by polycystic kidney disease; unknown pathological significance; the patient carried pathogenic PKD1 variant; the mutation results in significantly reduced WNT3A-induced signaling pathway;, features a modification of the amino acid from Q to H at position 1156.
+The protein's natural variant, known as in EVR4; an individual with total retinal detachment and retinoschisis; is unable to transduce Wnt or Norrin signal transduction;, features a modification of the amino acid from Y to H at position 1168.
+The protein's natural variant, known as in PCLD4; the mutation results in significantly reduced WNT3A-induced signaling pathway;, features a modification of the amino acid from R to W at position 1188.
+The protein's natural variant, known as in EVR4;, features a modification of the amino acid from C to F at position 1253.
+The protein's natural variant, known as in EVR4; autosomal dominant; has mildly reduced Wnt or Norrin signal transduction;, features a modification of the amino acid from C to G at position 1361.
+The protein's natural variant, known as in EVR4; autosomal recessive;, features a modification of the amino acid from E to K at position 1367.
+The protein's natural variant, known as in OPPG; unknown pathological significance, features a modification of the amino acid from G to D at position 1401.
+The protein's natural variant, known as in EVR1; decreases protein abundance;, features a modification of the amino acid from Y to C at position 1517.
+The protein's natural variant, known as in PCLD4; found in a family affected by polycystic liver disease; unknown pathological significance, features a modification of the amino acid from R to S at position 1529.
+The protein's natural variant, known as could be associated with idiopathic osteoporosis; does not result in a significant alteration of Wnt signal transduction;, features a modification of the amino acid from A to T at position 1537.
+The protein's natural variant, known as in PCLD4; unknown pathological significance; the patient carried additional PKHD1 variant;, features a modification of the amino acid from T to M at position 1541.
+The protein's natural variant, known as in PCLD4; unknown pathological significance; the mutation results in significantly reduced WNT3A-induced signaling pathway;, features a modification of the amino acid from D to N at position 1551.
+The protein's natural variant, known as in BURHAS; loss of function in Wnt signaling pathway, features a modification of the amino acid from C to G at position 41.
+The protein's natural variant, known as in BURHAS, features a modification of the amino acid from P to L at position 50.
+The protein's natural variant, known as in BURHAS; loss of function in Wnt signaling pathway, features a modification of the amino acid from C to F at position 128.
+The protein's natural variant, known as in BURHAS; loss of function in Wnt signaling pathway, features a modification of the amino acid from T to A at position 168.
+The protein's natural variant, known as in BURHAS; loss of function in Wnt signaling pathway, features a modification of the amino acid from G to R at position 174.
+The protein's natural variant, known as in RNS, features a modification of the amino acid from I to N at position 258.
+The protein's natural variant, known as in RNS; mild non-lethal form; decreased protein kinase activity;, features a modification of the amino acid from T to M at position 268.
+The protein's natural variant, known as in RNS;, features a modification of the amino acid from G to R at position 280.
+The protein's natural variant, known as in RNS; mild non-lethal form; decreased protein kinase activity; FAM20A is still able to increase remaining protein kinase activity;, features a modification of the amino acid from P to S at position 328.
+The protein's natural variant, known as in RNS;, features a modification of the amino acid from G to E at position 379.
+The protein's natural variant, known as in RNS, features a modification of the amino acid from G to R at position 379.
+The protein's natural variant, known as in RNS;, features a modification of the amino acid from L to R at position 388.
+The protein's natural variant, known as in RNS; mild non-lethal form; decreased protein kinase activity, features a modification of the amino acid from D to N at position 451.
+The protein's natural variant, known as in RNS;, features a modification of the amino acid from R to W at position 549.
+The natural variant of this protein is characterized by an amino acid alteration from K to T at position 3.
+The protein's natural variant, known as in THC1, features a modification of the amino acid from L to F at position 27.
+The protein's natural variant, known as in WAS;, features a modification of the amino acid from E to K at position 31.
+The protein's natural variant, known as in WAS; moderate form, features a modification of the amino acid from C to W at position 43.
+The protein's natural variant, known as in WAS and THC1;, features a modification of the amino acid from T to M at position 45.
+The protein's natural variant, known as in THC1, features a modification of the amino acid from T to I at position 48.
+The protein's natural variant, known as in WAS, features a modification of the amino acid from Q to H at position 52.
+The protein's natural variant, known as found in a patient with THC1; unknown pathological significance, features a modification of the amino acid from A to T at position 56.
+The protein's natural variant, known as in THC1;, features a modification of the amino acid from A to V at position 56.
+The protein's natural variant, known as in WAS, features a modification of the amino acid from P to L at position 58.
+The protein's natural variant, known as in THC1;, features a modification of the amino acid from P to R at position 58.
+The protein's natural variant, known as in WAS, features a modification of the amino acid from G to W at position 70.
+The protein's natural variant, known as in WAS; severe form, features a modification of the amino acid from C to R at position 73.
+The protein's natural variant, known as in THC1;, features a modification of the amino acid from V to M at position 75.
+The protein's natural variant, known as in WAS; attenuated form;, features a modification of the amino acid from S to P at position 82.
+The protein's natural variant, known as in THC1, features a modification of the amino acid from Y to C at position 83.
+The protein's natural variant, known as in WAS; severe form, features a modification of the amino acid from F to L at position 84.
+The protein's natural variant, known as in WAS, features a modification of the amino acid from R to C at position 86.
+The protein's natural variant, known as in WAS;, features a modification of the amino acid from R to H at position 86.
+The protein's natural variant, known as in WAS;, features a modification of the amino acid from R to L at position 86.
+The protein's natural variant, known as in WAS; mild form;, features a modification of the amino acid from G to D at position 89.
+The protein's natural variant, known as in WAS; attenuated form, features a modification of the amino acid from W to C at position 97.
+The protein's natural variant, known as in WAS; found in a patient with MRT52;, features a modification of the amino acid from E to K at position 131.
+The protein's natural variant, known as in WAS; severe form, features a modification of the amino acid from E to K at position 133.
+The protein's natural variant, known as in WAS, features a modification of the amino acid from A to T at position 134.
+The protein's natural variant, known as in WAS, features a modification of the amino acid from G to C at position 187.
+The protein's natural variant, known as in THC1, features a modification of the amino acid from A to E at position 236.
+The protein's natural variant, known as in XLN; a constitutively activating mutation;, features a modification of the amino acid from L to P at position 270.
+The protein's natural variant, known as in WAS, features a modification of the amino acid from K to E at position 476.
+The protein's natural variant, known as in THC1, features a modification of the amino acid from R to K at position 477.
+The protein's natural variant, known as in THC1;, features a modification of the amino acid from I to N at position 481.
+The protein's natural variant, known as in GCCD1; complete loss of activity;, features a modification of the amino acid from S to I at position 74.
+The protein's natural variant, known as in GCCD1;, features a modification of the amino acid from D to N at position 103.
+The protein's natural variant, known as in GCCD1;, features a modification of the amino acid from D to N at position 107.
+The protein's natural variant, known as in GCCD1;, features a modification of the amino acid from S to R at position 120.
+The protein's natural variant, known as in GCCD1;, features a modification of the amino acid from R to C at position 128.
+The protein's natural variant, known as found in a glucocorticoid deficiency patient carrying also mutation I-74;, features a modification of the amino acid from R to P at position 137.
+The protein's natural variant, known as in GCCD1; partial loss of ACTIVITY;, features a modification of the amino acid from R to W at position 137.
+The protein's natural variant, known as in GCCD1;, features a modification of the amino acid from R to H at position 146.
+The protein's natural variant, known as in GCCD1;, features a modification of the amino acid from C to F at position 251.
+The protein's natural variant, known as in GCCD1; complete loss of activity;, features a modification of the amino acid from Y to C at position 254.
+The protein's natural variant, known as in LAD1;, features a modification of the amino acid from D to N at position 128.
+The protein's natural variant, known as in LAD1;, features a modification of the amino acid from D to Y at position 128.
+The protein's natural variant, known as in LAD1;, features a modification of the amino acid from S to P at position 138.
+The protein's natural variant, known as in LAD1;, features a modification of the amino acid from L to P at position 149.
+The protein's natural variant, known as in LAD1;, features a modification of the amino acid from G to R at position 169.
+The protein's natural variant, known as in LAD1;, features a modification of the amino acid from P to L at position 178.
+The protein's natural variant, known as in LAD1;, features a modification of the amino acid from K to T at position 196.
+The protein's natural variant, known as in LAD1;, features a modification of the amino acid from A to T at position 239.
+The protein's natural variant, known as in LAD1;, features a modification of the amino acid from G to R at position 273.
+The protein's natural variant, known as in LAD1;, features a modification of the amino acid from G to S at position 284.
+The protein's natural variant, known as in LAD1;, features a modification of the amino acid from D to V at position 300.
+The protein's natural variant, known as in LAD1;, features a modification of the amino acid from N to S at position 351.
+The protein's natural variant, known as in LAD1;, features a modification of the amino acid from R to W at position 586.
+The protein's natural variant, known as in LAD1;, features a modification of the amino acid from R to C at position 593.
+The protein's natural variant, known as in LAD1;, features a modification of the amino acid from G to A at position 716.
+The protein's natural variant, known as in F5F8D1; loss of interaction with MCFD2 and ability to bind D-mannose, features a modification of the amino acid from W to S at position 67.
+The protein's natural variant, known as in RP84;, features a modification of the amino acid from R to Q at position 324.
+The protein's natural variant, known as in RP84; unknown pathological significance;, features a modification of the amino acid from G to D at position 332.
+The natural variant of this protein is characterized by an amino acid alteration from T to A at position 1217.
+The protein's natural variant, known as in DYT8;, features a modification of the amino acid from A to V at position 7.
+The protein's natural variant, known as in DYT8;, features a modification of the amino acid from A to V at position 9.
+The protein's natural variant, known as in CFZS1; unknown pathological significance, features a modification of the amino acid from W to R at position 79.
+The protein's natural variant, known as in CFZS1; unknown pathological significance; supports cell fusion in a heterologous cell fusion assay in vitro; decreased localization at the plasma membrane; partially rescues of mymk knockout fish; primary myoblasts from a compound heterozygote associating T-91 and R-185 exhibit no difference in their capability to differentiate compared to control myoblasts, but show a significant difference in the fusion index, with a higher percentage of singly-nucleated relative to multinucleated cells in compound heterozygous compared to control myoblasts;, features a modification of the amino acid from P to T at position 91.
+The protein's natural variant, known as in CFZS1; loss of localization at the plasma membrane; loss of cell fusion in a heterologous cell fusion assay in vitro; no rescue of mymk knockout fish;, features a modification of the amino acid from G to S at position 100.
+The protein's natural variant, known as in CFZS1; decreased localization at the plasma membrane; reduced cell fusion in a heterologous cell fusion assay in vitro compared to wild-type; partially rescues of mymk knockout fish;, features a modification of the amino acid from I to T at position 154.
+The protein's natural variant, known as in CFZS1; loss of localization at the plasma membrane; loss of cell fusion in a heterologous cell fusion assay in vitro; no rescue of mymk knockout fish; primary myoblasts from a compound heterozygote associating T-91 and R-185 exhibit no difference in their capability to differentiate compared to control myoblasts, but show a significant difference in the fusion index, with a higher percentage of singly-nucleated relative to multinucleated cells in compound heterozygous compared to control myoblasts;, features a modification of the amino acid from C to R at position 185.
+The protein's natural variant, known as in a renal clear cell carcinoma sample; somatic mutation;, features a modification of the amino acid from R to C at position 378.
+The protein's natural variant, known as in LMPHM1; recessive form; results in reduced autophosphorylation; results in impaired ligand-induced receptor internalization and downstream signaling;, features a modification of the amino acid from A to T at position 855.
+The protein's natural variant, known as in LMPHM1; loss of kinase activity;, features a modification of the amino acid from G to R at position 857.
+The protein's natural variant, known as in LMPHM1;, features a modification of the amino acid from V to M at position 878.
+The protein's natural variant, known as in HCI;, features a modification of the amino acid from P to S at position 954.
+The protein's natural variant, known as in a metastatic melanoma sample; somatic mutation, features a modification of the amino acid from T to I at position 1010.
+The protein's natural variant, known as in LMPHM1, features a modification of the amino acid from Q to L at position 1020.
+The protein's natural variant, known as probable disease-associated variant found in sporadic congenital lymphedema; de novo mutation, features a modification of the amino acid from H to Q at position 1035.
+The protein's natural variant, known as in LMPHM1; loss of kinase activity;, features a modification of the amino acid from H to R at position 1035.
+The protein's natural variant, known as in LMPHM1; loss of kinase activity;, features a modification of the amino acid from R to P at position 1041.
+The protein's natural variant, known as in LMPHM1; loss of kinase activity;, features a modification of the amino acid from L to P at position 1044.
+The protein's natural variant, known as in LMPHM1;, features a modification of the amino acid from I to T at position 1086.
+The protein's natural variant, known as in LMPHM1;, features a modification of the amino acid from E to K at position 1106.
+The protein's natural variant, known as in LMPHM1; loss of kinase activity;, features a modification of the amino acid from P to L at position 1114.
+The protein's natural variant, known as in HCI, features a modification of the amino acid from P to S at position 1137.
+The protein's natural variant, known as in CHTD7; unknown pathological significance, features a modification of the amino acid from L to V at position 1173.
+The protein's natural variant, known as in LMPHM1; recessive form, features a modification of the amino acid from S to C at position 1235.
+The protein's natural variant, known as in PHGDHD; results in a 2-fold decrease in enzyme activity with 3-phosphohydroxypyruvate, but no change in substrate affinity;, features a modification of the amino acid from R to W at position 135.
+The protein's natural variant, known as in NLS1;, features a modification of the amino acid from G to R at position 140.
+The protein's natural variant, known as in NLS1;, features a modification of the amino acid from R to Q at position 163.
+The protein's natural variant, known as in PHGDHD; results in a four-fold decrease in substrate affinity and a slight increase in maximal enzyme activity with 3-phosphohydroxypyruvate;, features a modification of the amino acid from V to M at position 261.
+The protein's natural variant, known as in PHGDHD; results in almost undetectable enzyme activity with 3-phosphohydroxypyruvate;, features a modification of the amino acid from A to T at position 373.
+The protein's natural variant, known as in PHGDHD; results in a 2-fold decrease in enzyme activity with 3-phosphohydroxypyruvate, but no change in substrate affinity;, features a modification of the amino acid from G to S at position 377.
+The protein's natural variant, known as in PHGDHD; results in almost undetectable enzyme activity with 3-phosphohydroxypyruvate;, features a modification of the amino acid from V to M at position 425.
+The protein's natural variant, known as in PHGDHD; results in almost undetectable enzyme activity with 3-phosphohydroxypyruvate;, features a modification of the amino acid from V to M at position 490.
+The protein's natural variant, known as found in a patient with isolated coloboma; unknown pathological significance, features a modification of the amino acid from P to Q at position 20.
+The protein's natural variant, known as in strain: Zimbabwe, features a modification of the amino acid from Y to F at position 127.
+The protein's natural variant, known as in strain: NC335, NC390, NC397 and NC774, features a modification of the amino acid from Q to QQ at position 89.
+The protein's natural variant, known as in strain: NC336 and MW6, features a modification of the amino acid from Q to QQQ at position 89.
+The protein's natural variant, known as in strain: MW11, features a modification of the amino acid from I to M at position 113.
+The protein's natural variant, known as in strain: NC303 and NC399, features a modification of the amino acid from S to T at position 190.
+The protein's natural variant, known as in IDDECA; unknown pathological significance, features a modification of the amino acid from C to S at position 90.
+The protein's natural variant, known as in IDDECA; deleterious effect on embryonic development, when assayed in a heterologous system;, features a modification of the amino acid from G to A at position 92.
+The protein's natural variant, known as in IDDECA; deleterious effect on embryonic development, when assayed in a heterologous system;, features a modification of the amino acid from K to R at position 94.
+The protein's natural variant, known as in IDDECA, features a modification of the amino acid from S to R at position 409.
+The protein's natural variant, known as in IDDECA; loss of function in cerebellar development, when assayed in a heterologous system;, features a modification of the amino acid from R to Q at position 462.
+The protein's natural variant, known as no effect on cerebellar development, when assayed in a heterologous system;, features a modification of the amino acid from T to A at position 476.
+The natural variant of this protein is characterized by an amino acid alteration from D to Q at position 2.
+The protein's natural variant, known as in ALS9, features a modification of the amino acid from F to S at position 12.
+The protein's natural variant, known as in ALS9, features a modification of the amino acid from P to S at position 20.
+The protein's natural variant, known as in ALS9; reduced ribonucleolytic activity; low angiogenic activity; reduced mitogenic activity; wild type far-UVCD spectra;, features a modification of the amino acid from Q to L at position 36.
+The protein's natural variant, known as in ALS9;, features a modification of the amino acid from Y to H at position 38.
+The protein's natural variant, known as in ALS9; reduced ribonucleolytic activity;, features a modification of the amino acid from K to E at position 41.
+The protein's natural variant, known as in ALS9; loss of angiogenic activity; reduced ribonucleolytic activity; retains nuclear translocation;, features a modification of the amino acid from K to I at position 41.
+The protein's natural variant, known as in ALS9; homodimerization is similar to wild-type; localization in the nucleus is similar to the wild-type; strongly reduces ribonucleolytic activity;, features a modification of the amino acid from D to G at position 46.
+The protein's natural variant, known as in ALS9; loss of angiogenic activity; reduced ribonucleolytic activity; unable to translocate to the nucleus;, features a modification of the amino acid from S to N at position 52.
+The protein's natural variant, known as in ALS9; marginally reduced ribonucleolytic activity; wild type far-UVCD spectra;, features a modification of the amino acid from R to K at position 55.
+The protein's natural variant, known as in ALS9; reduced ribonucleolytic activity; low angiogenic activity; reduced mitogenic activity; reduced thermal stability;, features a modification of the amino acid from C to W at position 63.
+The protein's natural variant, known as in ALS9; reduced ribonucleolytic activity; low angiogenic activity; reduced mitogenic activity; moderate reduction of thermal stability;, features a modification of the amino acid from K to I at position 64.
+The protein's natural variant, known as in some ALS9 patients; pathogenicity uncertain; reduced ribonucleolytic activity; moderate reduction of thermal stability;, features a modification of the amino acid from I to V at position 70.
+The protein's natural variant, known as in ALS9; loss of angiogenic activity; reduced ribonucleolytic activity; unable to translocate to the nucleus;, features a modification of the amino acid from P to L at position 136.
+The protein's natural variant, known as in ALS9;, features a modification of the amino acid from V to I at position 137.
+The protein's natural variant, known as in ALS9, features a modification of the amino acid from H to R at position 138.
+The protein's natural variant, known as in ASD6;, features a modification of the amino acid from M to L at position 182.
+The protein's natural variant, known as in ASD6;, features a modification of the amino acid from V to A at position 238.
+The protein's natural variant, known as in ASD6;, features a modification of the amino acid from I to V at position 629.
+The protein's natural variant, known as in a breast cancer sample; somatic mutation, features a modification of the amino acid from L to V at position 688.
+The protein's natural variant, known as in strain: ZBMEL131, features a modification of the amino acid from C to S at position 14.
+The protein's natural variant, known as in strain: MEL18 and MEL20, features a modification of the amino acid from I to V at position 60.
+The protein's natural variant, known as in strain: ZBMEL82, features a modification of the amino acid from I to T at position 95.
+The protein's natural variant, known as in strain: MEL11, MEL12, ZBMEL82, ZBMEL131, ZBMEL186, ZBMEL191 and ZBMEL229, features a modification of the amino acid from I to V at position 106.